doc_id	sent_index	relation_id	relation	trigger	trigger_offset	arg_num	arg_base_np	arg_protein	arg_domain	arg_site	arg_sugar	PSource	SiteSource	NProtein	NID	SiteName	sent_text
24125761	11	67	gly	glycosylation	1573:1585	arg1	N282	protein		N282		Fterm		protein		N282	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	11	67	gly	glycosylation	1573:1585	arg2	N282	protein		N282		Fterm		protein		N282	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	11	67	gly	glycosylation	1573:1585	arg1	AADAC	AADAC		N282		PUBTATOR		AADAC	13	N282	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	11	67	gly	glycosylation	1573:1585	arg2	N282			N282						N282	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	11	67	gly	glycosylation	1573:1585	arg2	N282	AADAC		N282		PUBTATOR		AADAC	13	N282	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
1512232	7	18	gly	serine	1421:1426	arg1	O-GlcNAc attachment			serine residues	O-GlcNAc attachment					serine residues	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
8286855	4	7	part_of	Ser23	661:665	arg1	GpA	GpA		Ser23		PUBTATOR	AminoAcid	GpA	2993	Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58	Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA.
8286855	4	13	part_of	Ser15	654:658	arg1	GpA	GpA		Ser15		PUBTATOR	AminoAcid	GpA	2993	Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58	Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA.
8286855	4	18	part_of	Ser14	647:651	arg1	GpA	GpA		Ser14		PUBTATOR	AminoAcid	GpA	2993	Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58	Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA.
8286855	4	25	part_of	Ser1	641:644	arg1	GpA	GpA		Ser1		PUBTATOR	AminoAcid	GpA	2993	Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58	Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA.
8286855	4	63	part_of	Thr58	678:682	arg1	GpA	GpA		Thr58		PUBTATOR	AminoAcid	GpA	2993	Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58	Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA.
8286855	4	69	part_of	Thr28	668:672	arg1	GpA	GpA		Thr28		PUBTATOR	AminoAcid	GpA	2993	Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58	Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA.
11710528	1	23	gly	cells--A431	309:319	arg1	hTR	hTR			cells--A431	PUBTATOR		hTR	P25116		The structural analysis of high mannose-type Asn-linked (N-linked) oligosaccharides of the human transferrin receptor (hTR) from D-[2-3H]mannose metabolic-radiolabeled human cells--A431, K562, BeWo, and HL60--was investigated.
11710528	1	23	gly	cells--A431	309:319	arg1	the human transferrin receptor	transferrin receptor			cells--A431	PUBTATOR		transferrin receptor	7037		The structural analysis of high mannose-type Asn-linked (N-linked) oligosaccharides of the human transferrin receptor (hTR) from D-[2-3H]mannose metabolic-radiolabeled human cells--A431, K562, BeWo, and HL60--was investigated.
11710528	1	41	gly	receptor	244:251	arg1	high mannose-type Asn-linked (N-linked) oligosaccharides	transferrin receptor			high mannose-type Asn-linked (N-linked) oligosaccharides	PUBTATOR		transferrin receptor	7037		The structural analysis of high mannose-type Asn-linked (N-linked) oligosaccharides of the human transferrin receptor (hTR) from D-[2-3H]mannose metabolic-radiolabeled human cells--A431, K562, BeWo, and HL60--was investigated.
11710528	1	65	gly	Asn-linked	180:189	arg1	high mannose-type Asn-linked (N-linked) oligosaccharides			Asn	high mannose-type Asn-linked (N-linked) oligosaccharides					Asn	The structural analysis of high mannose-type Asn-linked (N-linked) oligosaccharides of the human transferrin receptor (hTR) from D-[2-3H]mannose metabolic-radiolabeled human cells--A431, K562, BeWo, and HL60--was investigated.
16342937	7	38	part_of	proteins	1018:1025	arg1	The primary sequences	proteins		The primary sequences		Fterm	Site	proteins		sequences	The primary sequences of the rat zonae proteins have been deduced from cDNA.
2498325	0	83	gly	Glycosylation	0:12	arg1	human apolipoprotein E	human apolipoprotein E				PUBTATOR		apolipoprotein E	348		Glycosylation of human apolipoprotein E.
10889209	5	29	gly	glycosylation	787:799	arg1	Asn			Asn(119)						Asn(119)	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	5	29	gly	glycosylation	787:799	arg2	Asn			Asn(119)						Asn(119)	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	5	29	gly	glycosylation	787:799	arg1	119			Asn(119)						Asn(119)	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	5	29	gly	glycosylation	787:799	arg2	Asn			Asn(119)						Asn(119)	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	5	29	gly	glycosylation	787:799	arg1	119			Asn(119)						Asn(119)	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	5	29	gly	glycosylation	787:799	arg1	119			Asn(119)						Asn(119)	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
19202066	3	38	gly	modified	530:537	arg3	IKKbeta AND O-linked beta-N-acetyl glucosamine	IKKbeta			O-linked beta-N-acetyl glucosamine	PUBTATOR		IKKbeta	16150		Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	38	gly	modified	530:537	arg3	IKKbeta AND O-GlcNAc	IKKbeta			O-GlcNAc	PUBTATOR		IKKbeta	16150		Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
15458386	2	46	gly	N-glycosylation	247:261	arg2	five potential N-glycosylation sites			five potential N-glycosylation sites						sites	It has five potential N-glycosylation sites and predicated transmembrane domains at both the N- and C-termini.
16638743	4	40	gly	O-glycosylation	663:677	arg1	a subtilisin-like proprotein convertase recognition sequence motif			motif						motif	Here, we demonstrate that the secretion of the phosphaturic factor fibroblast growth factor 23 (FGF23) requires O-glycosylation, and that GalNAc-T3 selectively directs O-glycosylation in a subtilisin-like proprotein convertase recognition sequence motif, which blocks processing of FGF23.
479158	11	42	part_of	Glu-plasminogen	1050:1064	arg1	the Glu-plasminogen sequence	plasminogen		the Glu-plasminogen sequence		OGER	Site	plasminogen	P00747	sequence	The threonine was found to be residue 345 in the Glu-plasminogen sequence.
16768443	2	32	part_of	contain	453:459	arg1	GLP-1 AND a proline or alanine residue	GLP-1		alanine residue		OGER	AminoAcid	GLP-1	Q9H9B1	alanine residue	DPP-IV inactivates the glucagon-like peptide (GLP-1) and several other naturally produced bioactive peptides that contain preferentially a proline or alanine residue in the second amino acid sequence position by cleaving the N-terminal dipeptide.
16768443	2	32	part_of	contain	453:459	arg1	several other naturally produced bioactive peptides AND a proline or alanine residue	GLP-1		alanine residue		OGER	AminoAcid	GLP-1	Q9H9B1	alanine residue	DPP-IV inactivates the glucagon-like peptide (GLP-1) and several other naturally produced bioactive peptides that contain preferentially a proline or alanine residue in the second amino acid sequence position by cleaving the N-terminal dipeptide.
16768443	2	32	part_of	contain	453:459	arg1	several other naturally produced bioactive peptides AND a proline or alanine residue	GLP-1		alanine residue		OGER	AminoAcid	GLP-1	Q9H9B1	alanine residue	DPP-IV inactivates the glucagon-like peptide (GLP-1) and several other naturally produced bioactive peptides that contain preferentially a proline or alanine residue in the second amino acid sequence position by cleaving the N-terminal dipeptide.
18729387	7	92	gly	glycopeptide	1201:1212	arg2	glycopeptide MS data			glycopeptide MS data						glycopeptide	A set of glycopeptide MS data, including the mass spectrum, the mass spectrum in the selected ion monitoring mode, and the product ion spectra, was selected from all data based on carbohydrate-related ions in the MS/MS spectrum.
20505120	5	33	part_of	Eph	677:679	arg1	the Eph ligand-binding domain	Eph		the Eph ligand-binding domain		OGER	Site	Eph	P21709	domain	The structures reveal an elongated architecture with novel Eph/Eph interactions, both within and outside of the Eph ligand-binding domain, that suggest the molecular mechanism underlying Eph/ephrin clustering.
32155444	4	31	gly	glycoprotein	519:530	arg1	the SARS-CoV-2 S glycoprotein	the SARS-CoV-2 S glycoprotein				Cterm		S glycoprotein	43740568		We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs.
18061361	9	6	gly	unglycosylated	1642:1655	arg1	the unglycosylated protein	the unglycosylated protein				Fterm		protein			PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
17015441	0	2	part_of	contains	36:43	arg1	The cold and menthol receptor TRPM8 AND a functionally important double cysteine motif	The cold and menthol receptor TRPM8		a functionally important double cysteine motif		PUBTATOR	AminoAcid	TRPM8	Q7Z2W7	cysteine motif	The cold and menthol receptor TRPM8 contains a functionally important double cysteine motif.
24090084	3	61	gly	glycopeptides	516:528	arg2	tryptic glycopeptides			tryptic glycopeptides						glycopeptides	In the next step, tryptic glycopeptides were enriched using zwitterionic hydrophilic interaction liquid chromatography (Zic-HILIC) and fractionated by reversed-phase liquid chromatography (RPLC; pH 7.9).
24308486	2	47	gly	glycosylation	364:376	arg1	IgE	IgE				PUBTATOR		IgE	P01854		Here, we present site-specific glycosylation analysis of IgE from three different sources: IgE from the serum of a hyperimmune donor, from the pooled serum of multiple nondiseased donors, and from the pooled serum of 2 patients with IgE myeloma.
1512232	6	16	gly	presence	962:969	arg1	four peptides AND a single substoichiometric O-GlcNAc residue			four peptides	a single substoichiometric O-GlcNAc residue					peptides	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
23319596	9	8	part_of	hLOX	1454:1457	arg1	The catalytic domain	hLOX		The catalytic domain		PUBTATOR	Site	hLOX	4015	domain	The catalytic domain of hLOX was not secreted from S2 cells using the same expression system.
2387072	1	59	gly	glycoproteins	167:179	arg1	peripheral membrane glycoproteins	peripheral membrane glycoproteins				Fterm		glycoproteins			Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
19167329	4	41	gly	glycosylation	621:633	arg1	the nascent polypeptide			the nascent polypeptide						polypeptide	The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum.
20133774	4	50	gly	CNTN4	826:830	arg1	the four N-terminal immunoglobulin repeats	CNTN4			the four N-terminal immunoglobulin repeats	PUBTATOR		CNTN4	269784		Furthermore, we present crystal structures of the four N-terminal immunoglobulin repeats of mouse CNTN4 both alone and in complex with the carbonic anhydrase-like domain of mouse PTPRG.
25092234	3	78	gly	glycosylation	462:474	arg1	hFXI	hFXI				PUBTATOR		hFXI	2160		This study reports the first in-depth glycosylation analysis of hFXI based on advanced MS approaches.
7107587	13	31	gly	contains	1613:1620	arg1	fibrinogen AND four oligosaccharide chains	fibrinogen			four oligosaccharide chains	PUBTATOR		fibrinogen	2244		Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
15728350	0	6	part_of	ICAM-3	90:95	arg1	the binding domains	ICAM-3		the binding domains		PUBTATOR	Site	ICAM-3	3385	domains	An atomic resolution view of ICAM recognition in a complex between the binding domains of ICAM-3 and integrin alphaLbeta2.
19038967	4	63	gly	glycosylated	872:883	arg1	fully glycosylated TPP1	fully glycosylated TPP1				Cterm		TPP1			In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	37	gly	H-deglycosylated	757:772	arg1	an endoglycosidase H-deglycosylated form	H-deglycosylated form of TPP1				Cterm		H-deglycosylated form of TPP1			In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
1482348	5	40	gly	O-glycosylated	633:646	arg1	the O-glycosylated oligosaccharide				the O-glycosylated oligosaccharide						From these studies, the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF was concluded as [formula: see text].
12122212	3	10	part_of	CD21	410:413	arg1	the CD21 SCR1-SCR2 fragment	structure of the CD21		the CD21 SCR1-SCR2 fragment		PUBTATOR	Site	structure of the CD21	1380	fragment	Here we present the crystal structure of the CD21 SCR1-SCR2 fragment in the absence of ligand and demonstrate that it is able to bind EBV.
12122212	3	55	part_of	SCR1-SCR2	415:423	arg1	the CD21 SCR1-SCR2 fragment	SCR2		the CD21 SCR1-SCR2 fragment		PUBTATOR	Site	SCR2	5937	fragment	Here we present the crystal structure of the CD21 SCR1-SCR2 fragment in the absence of ligand and demonstrate that it is able to bind EBV.
21573946	6	62	gly	core-fucosylated	981:996	arg1	The EC-SOD N-glycans				The EC-SOD N-glycans						The EC-SOD N-glycans were basically core-fucosylated (98.3% of the total N-glycan content), and were high mannose sugar chain, and mono-, bi-, tri-, and tetra-antennary complex sugar chains exhibiting varying degrees of sialylation.
21573946	6	62	gly	core-fucosylated	981:996	arg1	the total N-glycan content				the total N-glycan content						The EC-SOD N-glycans were basically core-fucosylated (98.3% of the total N-glycan content), and were high mannose sugar chain, and mono-, bi-, tri-, and tetra-antennary complex sugar chains exhibiting varying degrees of sialylation.
7514386	4	95	gly	form	511:514	arg1	the asparagine-linked sugar chain	form of CD59			the asparagine-linked sugar chain	PUBTATOR		form of CD59	966		The structures of the GPI anchor and the asparagine-linked sugar chain of a soluble form of CD59 in urine, U-CD59, were determined.
7514386	4	97	gly	asparagine-linked	468:484	arg1	the asparagine-linked sugar chain			asparagine	the asparagine-linked sugar chain					asparagine	The structures of the GPI anchor and the asparagine-linked sugar chain of a soluble form of CD59 in urine, U-CD59, were determined.
3427055	0	19	part_of	SPARC/BM-40/osteonectin	73:95	arg1	Calcium binding domains	BM-40		Calcium binding domains		PUBTATOR	Site	BM-40	6678	domains	Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues.
2511201	4	105	part_of	found	899:903	arg2	bovine factors VII AND the same position	bovine factors VII		the same position		Cterm	Site	VII		position	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
3514617	10	70	gly	Asn-linked	1672:1681	arg1	the Asn-linked unit			Asn	the Asn-linked unit					Asn	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
16770729	0	31	gly	Glycosylation	0:12	arg1	Kv1.2 potassium channel	Kv1.2 potassium channel				OGER		potassium channel			Glycosylation and cell surface expression of Kv1.2 potassium channel are regulated by determinants in the pore region.
16770729	0	48	gly	determinants	86:97	arg1	the pore region			the pore region	the pore region		Site			region	Glycosylation and cell surface expression of Kv1.2 potassium channel are regulated by determinants in the pore region.
11706042	10	59	part_of	TLR4	1789:1792	arg1	N-linked sites	TLR4		N-linked sites		PUBTATOR	Site	TLR4	7099	sites	This suggests that the functional integrity of the LPS receptor depends both on the surface expression of at least three proteins, CD14, MD-2, and TLR4, and that N-linked sites of both MD-2 and TLR4 are essential in maintaining the functional integrity of this receptor.
11706042	10	62	part_of	MD-2	1780:1783	arg1	N-linked sites	MD-2		N-linked sites		OGER	Site	MD-2	Q9Y6Y9	sites	This suggests that the functional integrity of the LPS receptor depends both on the surface expression of at least three proteins, CD14, MD-2, and TLR4, and that N-linked sites of both MD-2 and TLR4 are essential in maintaining the functional integrity of this receptor.
11326277	9	26	part_of	Tas1r3	1150:1155	arg1	the sequence	Tas1r3		the sequence		PUBTATOR	Site	Tas1r3	83771	sequence	By comparing the sequence of Tas1r3 from several independently derived strains of mice, we identified a specific polymorphism that assorts between taster and non-taster strains.
8407981	9	11	gly	glycosylated	1408:1419	arg1	the N terminus			the N terminus						terminus	We conclude that the N terminus of P-450(arom) is translocated across the endoplasmic reticulum membrane to be glycosylated at the luminal side.
3980466	2	18	gly	sialylation	285:295	arg1	their asparagine-linked oligosaccharides				their asparagine-linked oligosaccharides						The influence of peptide structure of endogenous cell-surface glycoproteins on the branching and sialylation of their asparagine-linked oligosaccharides was evaluated in a murine B cell lymphoma, AKTB-1b.
3980466	2	26	gly	asparagine-linked	306:322	arg1	their asparagine-linked oligosaccharides			asparagine	their asparagine-linked oligosaccharides					asparagine	The influence of peptide structure of endogenous cell-surface glycoproteins on the branching and sialylation of their asparagine-linked oligosaccharides was evaluated in a murine B cell lymphoma, AKTB-1b.
3980466	2	89	gly	glycoproteins	250:262	arg1	endogenous cell-surface glycoproteins	endogenous cell-surface glycoproteins				Fterm		glycoproteins			The influence of peptide structure of endogenous cell-surface glycoproteins on the branching and sialylation of their asparagine-linked oligosaccharides was evaluated in a murine B cell lymphoma, AKTB-1b.
2943741	1	55	gly	leukosialin	178:188	arg1	O-linked oligosaccharides	leukosialin			O-linked oligosaccharides	PUBTATOR		leukosialin	P16150		Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
10024660	3	49	gly	monosialylated	632:645	arg1	monosialylated structures				monosialylated structures						Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
2013294	4	10	part_of	SABP	311:314	arg1	The complete amino acid sequence	SABP		The complete amino acid sequence		PUBTATOR	Site	SABP	5304	sequence	The complete amino acid sequence of SABP was determined with the aid of fragments generated by trypsin, Staphylococcus aureus V8 protease and pepsin.
1885588	2	46	gly	contains	293:300	arg1	The enzyme AND a high mannose type sugar chain	The enzyme			a high mannose type sugar chain	Fterm		enzyme			The enzyme contains a high mannose type sugar chain that can be cleaved by endo-beta-N-acetyl-D-glucosaminidase H without significantly affecting the catalytic activity.
16877748	8	47	gly	N-glycosylation	1406:1420	arg1	mouse sICAM-1	sICAM-1		sites		Cterm		sICAM-1	3383	sites	The N-glycosylation sites of mouse sICAM-1 were analyzed by MALDI-Fourier transform ion cyclotron resonance (FTICR)-MS and nanoLC-ESI-FTICR-MS of tryptic digests of mouse sICAM-1 expressed in the Lec1 mutant of CHO cells.
2129367	8	14	gly	Glc-Ser	1082:1088	arg1	a (Xyl2)Glc-Ser structure			Ser	a (Xyl2)Glc-Ser structure					Ser	These results indicate the existence of a (Xyl2)Glc-Ser structure in factors VII, IX and protein Z. Similar results were obtained for human factors VII, IX and protein Z.
11493670	2	13	part_of	NG2	389:391	arg1	the cytoplasmic domain	NG2		the cytoplasmic domain		PUBTATOR	Site	NG2	1464	domain	Both the cytoplasmic domain and the chondroitin sulfate chain of NG2 appear to have roles in sorting NG2 to subcellular microdomains destined to become retraction fibers.
1820200	3	22	part_of	hCG	1841:1843	arg1	individual N-glycosylation sites	hCG		individual N-glycosylation sites		PUBTATOR	Site	hCG	93659	sites	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
8344280	2	0	part_of	proteins	229:236	arg1	artificially introduced N-glycosylation or O-glycosylation sites	proteins		artificially introduced N-glycosylation or O-glycosylation sites		Fterm	Site	proteins		sites	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
10024660	1	17	gly	derived	165:171	arg2	bile salt-stimulated lipase AND N- glycans	bile salt-stimulated lipase			N- glycans	PUBTATOR		bile salt-stimulated lipase	P19835		The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	1	17	gly	derived	165:171	arg1	BSSL AND N- glycans	BSSL			N- glycans	PUBTATOR		BSSL	P19835		The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
19358553	1	19	gly	glycopeptides	185:197	arg2	N-linked glycopeptides			N-linked glycopeptides						glycopeptides	Site-specific glycoprofiling of N-linked glycopeptides using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) is an emerging technique, but its quantitative accuracy lacks documentation.
8687384	3	30	gly	sialylated	794:803	arg1	related and previously unidentified sialylated glycans				related and previously unidentified sialylated glycans						We also report the characterization of a series of related and previously unidentified sialylated glycans.
22121020	0	23	gly	H2B	25:27	arg1	GlcNAcylation	histone H2B			GlcNAcylation	PUBTATOR		histone H2B	3772104		GlcNAcylation of histone H2B facilitates its monoubiquitination.
18795891	2	32	gly	glycoproteins	349:361	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Normal platelet activation is dependent on tetraspanins, a superfamily of glycoproteins that function as 'organisers' of cell membranes by recruiting other receptors and signalling proteins into tetraspanin-enriched microdomains.
17005555	4	47	part_of	Lingo-1	712:718	arg1	the ligand-binding ectodomain	Lingo-1		the ligand-binding ectodomain		PUBTATOR	Site	Lingo-1	84894	ectodomain	Here we report on the crystal structure of the ligand-binding ectodomain of human Lingo-1 and show it has a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules.
2209609	0	44	gly	glycoprotein	117:128	arg1	a recombinant soluble CD4 glycoprotein	a recombinant soluble CD4 glycoprotein				PUBTATOR		CD4 glycoprotein	P01730		The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
19951703	9	12	gly	glycosylation	1240:1252	arg1	UGT1A9	UGT1A9				PUBTATOR		UGT1A9	54600		These results suggest that the glycosylation that occurs during translation is important for the folding of UGT1A9.
2511201	5	46	gly	glycopeptide	937:948	arg2	A glycopeptide			A glycopeptide						glycopeptide	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
25053408	5	26	part_of	PCFT	781:784	arg1	the seven cysteine (Cys) residues	PCFT		the seven cysteine (Cys) residues		PUBTATOR	Site	PCFT	113235	residues	In this study we mutated the seven cysteine (Cys) residues of human PCFT to serine, creating Cys-less PCFT.
24967714	0	4	gly	gp120	61:65	arg1	the highly conserved N-glycan at Asn260	gp120			the highly conserved N-glycan at Asn260	PUBTATOR		gp120	155971		Deletion of the highly conserved N-glycan at Asn260 of HIV-1 gp120 affects folding and lysosomal degradation of gp120, and results in loss of viral infectivity.
24967714	0	13	gly	Asn260	45:50	arg1	the highly conserved N-glycan at Asn260			Asn260	the highly conserved N-glycan at Asn260					Asn260	Deletion of the highly conserved N-glycan at Asn260 of HIV-1 gp120 affects folding and lysosomal degradation of gp120, and results in loss of viral infectivity.
32363391	7	61	gly	glycosylation	1372:1384	arg1	the spike protein	the spike protein				Fterm		protein			Our data on the N- and O- glycosylation is strengthened by extensive manual interpretation of each glycopeptide spectra in addition to using bioinformatics tools to confirm the complexity of glycosylation in the spike protein.
32363391	7	76	gly	glycopeptide	1280:1291	arg2	each glycopeptide spectra			each glycopeptide spectra						glycopeptide	Our data on the N- and O- glycosylation is strengthened by extensive manual interpretation of each glycopeptide spectra in addition to using bioinformatics tools to confirm the complexity of glycosylation in the spike protein.
11439087	6	43	part_of	contains	904:911	arg1	BST-1 AND four putative N-glycosylation sites	BST-1		four putative N-glycosylation sites		PUBTATOR	Site	BST-1	683	sites	BST-1 contains four putative N-glycosylation sites.
3200844	2	49	part_of	protein	333:339	arg1	the primary sequence	protein		the primary sequence		Fterm	Site	protein		sequence	We sought to determine the primary sequence of a nuclear pore protein modified by O-linked GlcNAc.
7620335	6	61	gly	Asn49	1079:1083	arg1	the neutral oligosaccharides			Asn39 and Asn49 residues	the neutral oligosaccharides					Asn39 and Asn49 residues	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	6	79	gly	Asn39	1069:1073	arg1	the neutral oligosaccharides			Asn39 and Asn49 residues	the neutral oligosaccharides					Asn39 and Asn49 residues	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
9539702	0	13	part_of	molecule-1	85:94	arg1	the N-terminal two domains	intercellular adhesion molecule-1		the N-terminal two domains		OGER	Site	intercellular adhesion molecule-1	P05362	domains	A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1.
19690161	6	23	gly	glycosylation	736:748	arg1	the Asn-89 site	vIL		Asn-89 site		OGER		vIL	P09327	Asn-89 site	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	6	23	gly	glycosylation	736:748	arg2	the Asn-89 site	vIL		Asn-89 site		OGER		vIL	P09327	Asn-89 site	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	6	23	gly	glycosylation	736:748	arg2	the Asn-89 site			Asn-89 site						Asn-89 site	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
21241660	6	28	gly	structures	711:720	arg1	PANP	PANP			structures	PUBTATOR		PANP	319352		Specific O-glycan structures on PANP were found to be required for PILR recognition of this ligand.
27462106	5	54	gly	presence	1104:1111	arg1	the +1 subsite AND d-mannose			the +1 subsite	d-mannose					subsite	The X-ray structures with key catalytic cycle intermediates highlight that an insertion between the +1 and +2 subsites contributes to the enzyme's activity and substrate specificity, and reveal that the presence of d-mannose at the +1 subsite renders the acid catalyst less efficient during the cleavage of the monoglucosylated substrate.
9597769	5	48	gly	glycosylated	1160:1171	arg1	The higher glycosylated GalNAc2-substituted fragments			The higher glycosylated GalNAc2-substituted fragments							The higher glycosylated GalNAc2-substituted fragments were mainly observed as multiply ionized species.
2059624	4	21	gly	released	889:896	arg1	N289 AND the oligosaccharides			N289	the oligosaccharides					N289	At the earliest postinfection (p.i.) time period studied, i.e., 0-20 h, virtually all (96%) of the oligosaccharides released with glycopeptidase F from N289 of the expressed r-HPg were of the high-mannose type and comprised nearly the full range of such structures, containing 3-9 mannose units.
22601780	3	6	part_of	contains	344:351	arg1	Del-1 AND 2 discoidin-like domains	Del-1		2 discoidin-like domains	3 epidermal growth factor (EGF)-like repeats	PUBTATOR	Site	Del-1	10085	domains	Del-1 contains 3 epidermal growth factor (EGF)-like repeats and 2 discoidin-like domains.
20622017	4	62	gly	released	711:718	arg2	isolated GGT AND glycans	isolated GGT			glycans	OGER		GGT			Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	4	70	gly	microheterogeneity	543:560	arg1	glycans				glycans						Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	4	85	gly	glycans	588:594	arg1	specific glycopeptides			specific glycopeptides	specific glycopeptides		Site			glycopeptides	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	4	90	gly	glycopeptides	608:620	arg2	specific glycopeptides			specific glycopeptides						glycopeptides	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
15152093	5	51	gly	glycosylated	869:880	arg1	GCPII	GCPII				PUBTATOR		GCPII	2346		As a type II membrane protein, GCPII is heavily glycosylated.
15152093	5	51	gly	glycosylated	869:880	arg1	a type II membrane protein	a type II membrane protein				PUBTATOR		type II membrane protein	10329		As a type II membrane protein, GCPII is heavily glycosylated.
23661698	6	44	gly	deglycosylated	911:924	arg1	deglycosylated ephrin-A1	deglycosylated ephrin-A1				PUBTATOR		ephrin-A1	1942		Data obtained by surface plasmon resonance confirms that deglycosylated ephrin-A1 does not bind EphA2 with high affinity.
12527193	8	52	gly	N-glycosylation	1258:1272	arg2	a conserved N-glycosylation site			a conserved N-glycosylation site						site	Mouse and human CRB3 have identical intracellular domains but divergent extracellular domains except for a conserved N-glycosylation site.
23010571	1	50	part_of	ADAMTS	311:316	arg1	ADAMTS ancillary domains	ADAMTS		ADAMTS ancillary domains		PUBTATOR	Site	ADAMTS	11504	domains	ADAMTS-like proteins are related to ADAMTS metalloproteases by their similarity to ADAMTS ancillary domains.
16407218	3	47	gly	glycosylation	628:640	arg2	eight N-linked glycosylation sites			eight N-linked glycosylation sites						sites	We isolated the serum protease inhibitor alpha(2) macroglobulin (alpha2M), a heavily glycosylated thiol ester protein (TEP) composed of four identical 180-kDa subunits, each of which has eight N-linked glycosylation sites.
16407218	3	74	gly	glycosylated	511:522	arg1	a heavily glycosylated thiol ester protein	a heavily glycosylated thiol ester protein				Fterm		protein			We isolated the serum protease inhibitor alpha(2) macroglobulin (alpha2M), a heavily glycosylated thiol ester protein (TEP) composed of four identical 180-kDa subunits, each of which has eight N-linked glycosylation sites.
16407218	3	74	gly	glycosylated	511:522	arg1	the serum protease inhibitor alpha(2) macroglobulin	the serum protease inhibitor alpha(2) macroglobulin				PUBTATOR		alpha(2) macroglobulin	2		We isolated the serum protease inhibitor alpha(2) macroglobulin (alpha2M), a heavily glycosylated thiol ester protein (TEP) composed of four identical 180-kDa subunits, each of which has eight N-linked glycosylation sites.
23527852	0	86	gly	glycoforms	42:51	arg1	new apolipoprotein-CIII glycoforms	new apolipoprotein-CIII glycoforms				PUBTATOR		apolipoprotein-CIII	345		Identification of new apolipoprotein-CIII glycoforms with ultrahigh resolution MALDI-FTICR mass spectrometry of human sera.
18340083	3	14	gly	N-glycosylated	505:518	arg2	Asn-76	GPIHBP1		Asn-76		PUBTATOR		GPIHBP1	68453	Asn-76	Here, we show that mouse GPIHBP1 is N-glycosylated at Asn-76 within the Ly-6 domain.
8286855	0	39	part_of	motifs	88:93	arg1	human glycophorin A	glycophorin A		motifs		PUBTATOR	Site	glycophorin A	2993	motifs	Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.
28514451	2	48	part_of	extracellular	337:349	arg1	the extracellular domain	r		the extracellular domain		PUBTATOR	Site	r	10663	domain	Here we report the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation.
28514451	2	6	part_of	containing	317:326	arg1	full-length GCGR AND transmembrane domain	GCGR		domain		PUBTATOR	Site	GCGR	2642	domain	Here we report the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation.
26791533	9	17	gly	sialylated	1206:1215	arg1	the glycoproteins	the glycoproteins				Fterm		glycoproteins			Most of the glycoproteins were either sialylated, fucosylated, or both.
26791533	9	19	gly	glycoproteins	1180:1192	arg1	the glycoproteins	the glycoproteins				Fterm		glycoproteins			Most of the glycoproteins were either sialylated, fucosylated, or both.
26791533	9	59	gly	fucosylated	1218:1228	arg1	the glycoproteins	the glycoproteins				Fterm		glycoproteins			Most of the glycoproteins were either sialylated, fucosylated, or both.
1740433	6	83	part_of	A-SAA	941:945	arg1	the corresponding region	SAA		the corresponding region		PUBTATOR	Site	SAA	6288	region	The 112-residue mature molecule is 8 residues longer than human A-SAA; the size difference is due to the presence of an octapeptide between positions 70 and 77 that is not found in the corresponding region of human A-SAA.
20622017	12	91	part_of	glycoprotein	1657:1668	arg1	individual glycopeptides	glycoprotein		individual glycopeptides		Fterm	Site	glycoprotein		glycopeptides	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
21467029	8	44	part_of	COX	985:987	arg1	the COX site	COX		the COX site		OGER	Site	COX		site	Substrate and nonsubstrate fatty acids (FAs) and some COX inhibitors (e.g. naproxen) preferentially bind to the COX site of E(allo).
24509848	0	50	gly	Glycosylation	0:12	arg2	Asn211			Asn211						Asn211	Glycosylation at Asn211 regulates the activation state of the discoidin domain receptor 1 (DDR1).
19467646	1	55	part_of	Growth	96:101	arg1	polypeptides	Growth		polypeptides		Cterm	Site	Growth		polypeptides	OBJECTIVE: Growth factors, including brain-derived neurotrophic factor (BDNF), are polypeptides that are involved in the maintenance, survival, and death of central and peripheral cells.
24279413	0	92	gly	glycopeptides	53:65	arg2	intact glycopeptides			intact glycopeptides						glycopeptides	Computational framework for identification of intact glycopeptides in complex samples.
20507882	5	4	gly	glycosylation	994:1006	arg2	glycosylation site occupancy			glycosylation site occupancy						site	The HexNAc-O-Ser/Thr, but not Hex-O-Thr glycopeptides, displayed heterogeneity regarding glycan core structures and level of glycosylation site occupancy.
20507882	5	60	gly	glycopeptides	909:921	arg2	Hex-O-Thr glycopeptides			Hex-O-Thr glycopeptides						Thr glycopeptides	The HexNAc-O-Ser/Thr, but not Hex-O-Thr glycopeptides, displayed heterogeneity regarding glycan core structures and level of glycosylation site occupancy.
1374031	9	105	gly	found	1631:1635	arg2	normal urinary hCG AND The major O-linked carbohydrate chains	normal urinary hCG			The major O-linked carbohydrate chains	OGER		hCG			The major O-linked carbohydrate chains identified are the tetrasaccharide Neu5Ac alpha 2-3Gal beta 1-3(Neu5Ac alpha 2-6)GalNAc-ol and the hexasaccharide Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6(Neu5Ac alpha 2-3Gal beta 1-3)GalNAc-ol, both also found in normal urinary hCG.
2393398	8	11	gly	pro-urokinase	1194:1206	arg1	the carbohydrate composition			pro	the carbohydrate composition					pro	Also, the carbohydrate composition of recombinant pro-urokinase is reported.
11546839	4	10	part_of	region	479:484	arg1	its tails	region		its tails						tails	In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation.
19088065	10	62	gly	modified	1329:1336	arg3	ovarian cancer-derived KLK6 AND alpha2-6-linked sialic acid	ovarian cancer-derived KLK6			alpha2-6-linked sialic acid	Cterm		KLK6			Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
20624874	0	47	gly	ADAMTS13	53:60	arg1	sugar chains	ADAMTS13			sugar chains	PUBTATOR		ADAMTS13	11093		Proteolytic fragmentation and sugar chains of plasma ADAMTS13 purified by a conformation-dependent monoclonal antibody.
8344278	0	59	gly	proteins	75:82	arg1	the oligosaccharide moieties	proteins			the oligosaccharide moieties	Fterm		proteins			Structural study of the oligosaccharide moieties of sphingolipid activator proteins, saposins A, C and D obtained from the spleen of a Gaucher patient.
2550193	4	27	gly	EPO	528:530	arg1	almost all N-linked oligosaccharide chains	Namalwa EPO			almost all N-linked oligosaccharide chains	PUBTATOR		Namalwa EPO	2056		Oligosaccharide structure analyses suggested that almost all N-linked oligosaccharide chains of Namalwa EPO are shared by urinary EPO.
3356193	4	1	gly	plasminogen	475:485	arg1	the N-glycan	plasminogen			the N-glycan	OGER		plasminogen	P00747		In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	4	77	gly	sialylated	508:517	arg1	the two antennae				the two antennae						In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
22226965	4	7	gly	PPARγ	641:645	arg1	the major O-GlcNAc site	PPARγ 			the major O-GlcNAc site	PUBTATOR		PPARγ 	19016		Mass spectrometric analysis and mutant studies revealed that the threonine 54 of the N-terminal AF-1 domain of PPARγ is the major O-GlcNAc site.
22226965	4	47	gly	threonine	595:603	arg1	the major O-GlcNAc site			threonine 54	the major O-GlcNAc site					threonine 54	Mass spectrometric analysis and mutant studies revealed that the threonine 54 of the N-terminal AF-1 domain of PPARγ is the major O-GlcNAc site.
22226965	4	50	gly	AF-1	626:629	arg1	the major O-GlcNAc site	AF-1			the major O-GlcNAc site	OGER		AF-1	P38484		Mass spectrometric analysis and mutant studies revealed that the threonine 54 of the N-terminal AF-1 domain of PPARγ is the major O-GlcNAc site.
18586680	6	10	part_of	O-GlcNAcase	1019:1029	arg1	C-terminal O-GlcNAcase fragments	O-GlcNAcase		C-terminal O-GlcNAcase fragments		PUBTATOR	Site	O-GlcNAcase	10724	fragments	Finally, we show that O-GlcNAcase activity is not affected by caspase-3 cleavage because the N- and C-terminal O-GlcNAcase fragments remain associated after the cleavage.
20879038	6	74	part_of	PRP-modified	1334:1345	arg1	45 new PRP-modified residues	PRP		45 new PRP-modified residues		OGER	Site	PRP	Q9NP58	residues	In summary, salivary peptidome data analysis allowed the identification of 45 new PRP-modified residues, mainly due to glycosylation, phosphorylation and conversion of Gln to pyro-Glu.
9023546	4	72	part_of	peptides	468:475	arg1	sequences	peptides		sequences						sequences	Synthetic peptides with sequences taken from five proteins previously shown to contain O-linked fucose (Harris and Spellman, 1993; Glycobiology, 3, 219-224) did not serve as efficient acceptor substrates.
16477002	2	43	part_of	IL-2	405:408	arg1	the human IL-2 receptor ectodomains	IL-2 receptor		the human IL-2 receptor ectodomains		PUBTATOR	Site	IL-2 receptor	3560	ectodomains	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	2	97	part_of	receptor	410:417	arg1	the human IL-2 receptor ectodomains	IL-2 receptor		the human IL-2 receptor ectodomains		PUBTATOR	Site	IL-2 receptor	3560	ectodomains	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
24509848	5	63	gly	N-glycosylation	648:662	arg1	the Asn(211) residue			Asn(211) residue						Asn(211) residue	Here, we report that N-glycosylation at the Asn(211) residue plays a unique role in the control of DDR1 dimerization and autophosphorylation.
10413465	5	42	gly	O-glycosylation	1142:1156	arg2	the O-glycosylation site	Thr194-Ala		site		Cterm		Thr194-Ala	348	site	This analysis showed that a mutation in the O-glycosylation site of apoE2 (Thr194-Ala) did not affect the SDS-stable binding of apoE to Abeta.
10413465	5	42	gly	O-glycosylation	1142:1156	arg2	the O-glycosylation site	apoE2		site		PUBTATOR		apoE2	348	site	This analysis showed that a mutation in the O-glycosylation site of apoE2 (Thr194-Ala) did not affect the SDS-stable binding of apoE to Abeta.
3934016	5	26	gly	utilized	932:939	arg2	only 2 of 3 potential sites			only 2 of 3 potential sites						sites	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	5	38	gly	utilized	1026:1033	arg2	all 4 potential sites			all 4 potential sites						sites	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	5	43	gly	N-glycosylation	911:925	arg2	only 2 of 3 potential sites			only 2 of 3 potential sites						sites	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	5	13	gly	N-glycosylation	980:994	arg2	all 4 potential sites	angiotensinogen		sites		PUBTATOR		angiotensinogen	183	sites	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
22171320	11	108	gly	glycoproteins	1846:1858	arg1	53 glycoproteins	53 glycoproteins				Fterm		glycoproteins			In total, 58 N- and 63 O-linked glycopeptides from 53 glycoproteins were characterized with respect to glycan- and peptide sequences.
22171320	11	20	gly	glycopeptides	1824:1836	arg1	53 glycoproteins	glycoproteins		glycopeptides		Fterm		glycoproteins		glycopeptides	In total, 58 N- and 63 O-linked glycopeptides from 53 glycoproteins were characterized with respect to glycan- and peptide sequences.
6776528	7	1	part_of	chain	984:988	arg1	the COOH terminus	47A chain		the COOH terminus		OGER	Site	47A chain		terminus	Comparison of the 511 alppha chain with the 47A alpha chain reveals two noncconservative amino acid changes at the COOH terminus of the 47A chain, Ser-Gln for VAl-Thr in the 511 chain.
6526384	2	34	gly	glycoprotein	311:322	arg1	a monomeric glycoprotein	a monomeric glycoprotein				Fterm		glycoprotein			The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
2808371	0	1	gly	moiety	25:30	arg1	discrete peptide			discrete peptide	discrete peptide		Site			peptide	O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.
1904059	2	89	gly	glycoprotein	229:240	arg1	a multidomain	glycoprotein		multidomain		Fterm		glycoprotein		multidomain	Factor VII is a multidomain, vitamin K-dependent plasma glycoprotein that participates in the extrinsic pathway of blood coagulation.
2040275	11	1	gly	glycoforms	1633:1642	arg1	the tail peptide			the tail peptide						peptide	Various roles for the different glycoforms of the tail peptide are discussed.
14754895	1	61	part_of	contains	239:246	arg1	a type I integral membrane protein AND one HEXXH + E zinc-binding consensus sequence	a type I integral membrane protein		one HEXXH + E zinc-binding consensus sequence		Fterm	Site	protein		sequence	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	61	part_of	contains	239:246	arg1	The angiotensin-converting enzyme AND one HEXXH + E zinc-binding consensus sequence	The angiotensin-converting enzyme		one HEXXH + E zinc-binding consensus sequence		OGER	Site	angiotensin-converting enzyme	P12821	sequence	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
21606496	5	39	gly	2B4	641:643	arg1	sialylation	2B4			sialylation	PUBTATOR		2B4	51744		In contrast, sialylation of 2B4 has a negative impact on ligand binding, as the interaction between 2B4 and CD48 is increased after the removal of sialic acids.
21606496	5	54	gly	sialylation	626:636	arg1	2B4	2B4				PUBTATOR		2B4	51744		In contrast, sialylation of 2B4 has a negative impact on ligand binding, as the interaction between 2B4 and CD48 is increased after the removal of sialic acids.
10413465	0	91	gly	glycosylation	34:46	arg2	the glycosylation site threonine 194			site threonine 194						site threonine 194	Contribution of cysteine 158, the glycosylation site threonine 194, the amino- and carboxy-terminal domains of apolipoprotein E in the binding to amyloid peptide beta (1-40).
27384988	4	10	gly	glycosylated	383:394	arg2	the Asn165 residue			the Asn165 residue						Asn165 residue	Presently, mass spectrometry analysis revealed rpS3 to be glycosylated at the Asn165 residue.
11602603	1	78	gly	sequence	176:183	arg1	sequence tag				sequence tag						Probing of the GenBank expressed sequence tag (EST) data base with varied human tryptase cDNAs identified two truncated ESTs that subsequently were found to encode overlapping portions of a novel human serine protease (designated tryptase epsilon or protease, serine S1 family member 22 (PRSS22)).
2393398	2	49	gly	glycopeptide	234:245	arg2	A glycopeptide			A glycopeptide						glycopeptide	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	2	65	gly	containing	247:256	arg1	A glycopeptide AND the monosaccharide, fucose,			A glycopeptide	the monosaccharide, fucose,					glycopeptide	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
12901863	0	26	gly	N-glycosylation	29:43	arg1	human ABCC6	human ABCC6				PUBTATOR		ABCC6	368		Subcellular localization and N-glycosylation of human ABCC6, expressed in MDCKII cells.
2513186	6	27	gly	glycosylated	993:1004	arg1	Asn184			Asn184						Asn184	Asn184 is only partially glycosylated and substituted by fucosylated triantennary and small amounts of diantennary N-acetyllactosaminic glycans.
2513186	6	59	gly	fucosylated	1025:1035	arg1	diantennary N-acetyllactosaminic glycans				diantennary N-acetyllactosaminic glycans						Asn184 is only partially glycosylated and substituted by fucosylated triantennary and small amounts of diantennary N-acetyllactosaminic glycans.
8223648	12	20	gly	glycosylated	1359:1370	arg1	glycosylated and nonglycosylated IFN-omega 1	glycosylated and nonglycosylated IFN-omega 1				PUBTATOR		IFN-omega 1	3467		Circular dichroism and fluorescence spectroscopy did not reveal any structural differences between glycosylated and nonglycosylated IFN-omega 1.
8223648	12	63	gly	nonglycosylated	1376:1390	arg1	glycosylated and nonglycosylated IFN-omega 1	glycosylated and nonglycosylated IFN-omega 1				PUBTATOR		IFN-omega 1	3467		Circular dichroism and fluorescence spectroscopy did not reveal any structural differences between glycosylated and nonglycosylated IFN-omega 1.
11326277	10	7	gly	interfere	1444:1452	arg1	an extra amino-terminal glycosylation site			an extra amino-terminal glycosylation site						site	According to models of its structure, T1r3 from non-tasters is predicted to have an extra amino-terminal glycosylation site that, if used, would interfere with dimerization.
11326277	10	56	gly	glycosylation	1404:1416	arg2	an extra amino-terminal glycosylation site			an extra amino-terminal glycosylation site						site	According to models of its structure, T1r3 from non-tasters is predicted to have an extra amino-terminal glycosylation site that, if used, would interfere with dimerization.
8344280	9	75	gly	glycopeptide	1169:1180	arg2	the tryptic glycopeptide APTPPPK			the tryptic glycopeptide APTPPPK						glycopeptide	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	9	110	gly	attached	1308:1315	arg2	Thr AND the only carbohydrate constituents			Thr	the only carbohydrate constituents					Thr	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8615697	8	24	gly	glycosylation	1085:1097	arg2	these confirmed glycosylation sites			these confirmed glycosylation sites						sites	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
26859261	2	40	gly	glycoprotein	375:386	arg1	the glycosylphosphatidylinositol (GPI)-anchored glycoprotein Juno	the glycosylphosphatidylinositol (GPI)-anchored glycoprotein Juno				Fterm		glycoprotein Juno	390243		A decade-long search for a protein pair mediating this event in mammals culminated in the identification of the glycosylphosphatidylinositol (GPI)-anchored glycoprotein Juno as the egg plasma membrane receptor of sperm Izumo1 [1,2].
7607222	2	19	gly	glycoprotein	237:248	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Lithostathine, also known as pancreatic stone protein, pancreatic thread protein or regenerating protein, is a glycoprotein which is normally found in the exocrine pancreas, whereas in other tissues it appears either only under pathological conditions, such as Alzheimer's disease (brain), cancer (colon) or during regeneration (endocrine pancreas).
22967898	3	26	gly	N-glycosylation	385:399	arg1	cathepsin V	cathepsin V				PUBTATOR		cathepsin V	1515		In this study, we clarified the role of N-glycosylation of cathepsin V for its functions.
7514386	6	17	part_of	U-CD59	832:837	arg1	the carboxy terminus	CD59		the carboxy terminus		PUBTATOR	Site	CD59	966	terminus	This indicates that a GPI anchor, which ended with inositol, is linked at the carboxy terminus of U-CD59.
1567356	3	79	part_of	site	444:447	arg1	its molecular variants	variants		site		Fterm	Site	variants		site	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	3	79	part_of	site	444:447	arg1	OMD	OMD		site		OGER	Site	OMD	Q99983	site	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1904059	12	55	gly	presence	1734:1741	arg2	serine 60 AND O-linked fucose			serine 60	O-linked fucose					serine 60	Metabolic labeling studies using [14C]fucose confirmed the presence of O-linked fucose at serine 60.
14760718	9	16	part_of	sites	1307:1311	arg1	77 proteins	proteins		sites		Fterm	Site	proteins		sites	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
8344946	4	80	gly	NF-L	830:833	arg1	GlcNAc/mol	NF-L			GlcNAc/mol	PUBTATOR		NF-L	4747		In purified neurofilament proteins, the O-GlcNAc modifications occur at a stoichiometry of approximately 0.1 and 0.15 mol of GlcNAc/mol of NF-L and NF-M, respectively.
8344946	4	84	gly	NF-M	839:842	arg1	GlcNAc/mol	NF-M			GlcNAc/mol	PUBTATOR		NF-M	4741		In purified neurofilament proteins, the O-GlcNAc modifications occur at a stoichiometry of approximately 0.1 and 0.15 mol of GlcNAc/mol of NF-L and NF-M, respectively.
11080501	6	2	gly	glycosylation	1275:1287	arg2	glycosylation sites			glycosylation sites						sites	Analysis of glycosylation sites showed that GA733-2 antigen contained N-linked carbohydrate but that no O-linked carbohydrate groups were detected.
10944330	1	33	part_of	Fab	134:136	arg1	the Fab fragment	structure of the Fab		the Fab fragment		PUBTATOR	Site	structure of the Fab	2187	fragment	The crystal structure of the Fab fragment from the monoclonal anti-preS2 antibody F124 (IgG1,kappa) has been solved by molecular replacement and refined at 3.0 A resolution.
22412906	9	12	gly	N-glycosylation	1400:1414	arg1	the GIP receptor	the GIP receptor				PUBTATOR		GIP receptor	2695		N-glycosylation is also required for expression of the GIP receptor at the plasma membrane and efficient GIP potentiation of glucose-induced insulin secretion from the INS-1 pancreatic beta cell line.
24342833	3	35	gly	β-catenin	489:497	arg1	the putative O-GlcNAc sites	-catenin			the putative O-GlcNAc sites	PUBTATOR		-catenin	1499		OBJECTIVE: The objectives of this investigation were to identify the putative O-GlcNAc sites of β-catenin and the relevance of identified sites in the regulation of β-catenin's localization and transcriptional activity.
24342833	3	42	gly	sites	531:535	arg1	the putative O-GlcNAc sites			sites	the putative O-GlcNAc sites					sites	OBJECTIVE: The objectives of this investigation were to identify the putative O-GlcNAc sites of β-catenin and the relevance of identified sites in the regulation of β-catenin's localization and transcriptional activity.
18420935	5	25	part_of	receptor	880:887	arg1	the cytoplasmic Toll interleukin-1 receptor (TIR) domains	receptor		the cytoplasmic Toll interleukin-1 receptor (TIR) domains		Fterm	Site	receptor		domains	This juxtaposition could mediate downstream signaling by dimerizing the cytoplasmic Toll interleukin-1 receptor (TIR) domains.
11069170	7	6	part_of	possess	1117:1123	arg1	G-protein-coupled neurotransmitter receptors AND extracellular ligand-binding sites	G-protein-coupled neurotransmitter receptors		extracellular ligand-binding sites		Fterm	Site	receptors		sites	This scheme in the initial receptor activation could be applied generally to G-protein-coupled neurotransmitter receptors that possess extracellular ligand-binding sites.
18703501	3	16	part_of	IX	548:549	arg1	the CA IX catalytic domain	CA IX		the CA IX catalytic domain		PUBTATOR	Site	CA IX	768	domain	The recombinant proteins consisted of either the CA IX catalytic domain only (CA form) or the extracellular domain, which included both the proteoglycan and catalytic domains (PG + CA form).
18703501	3	66	part_of	CA	545:546	arg1	the CA IX catalytic domain	CA IX		the CA IX catalytic domain		PUBTATOR	Site	CA IX	768	domain	The recombinant proteins consisted of either the CA IX catalytic domain only (CA form) or the extracellular domain, which included both the proteoglycan and catalytic domains (PG + CA form).
21573946	3	3	gly	EC-SOD	483:488	arg1	a precise N-glycan profile	EC-SOD			a precise N-glycan profile	PUBTATOR		EC-SOD	20657		Thus, a precise N-glycan profile of the recombinant EC-SOD is not available.
3521732	3	52	gly	containing	391:400	arg1	Cyanogen bromide peptides AND carbohydrate			Cyanogen bromide peptides	carbohydrate					peptides	Cyanogen bromide peptides containing carbohydrate were further digested with trypsin, and the peptides containing carbohydrate were isolated and sequenced.
3521732	3	15	gly	containing	468:477	arg1	the peptides AND carbohydrate			the peptides	carbohydrate					peptides	Cyanogen bromide peptides containing carbohydrate were further digested with trypsin, and the peptides containing carbohydrate were isolated and sequenced.
29932112	9	12	gly	N-glycosylation	1264:1278	arg1	Panx2	Panx2				PUBTATOR		Panx2	56666		Our study indicates that N-glycosylation may be important for folding and trafficking of Panx2.
8910321	5	73	gly	glycosylated	834:845	arg1	Asn-408			Asn-408 and -488	the N-linked structures					Asn-408 and -488	Mass spectral analysis showed that Asn-408 and -488 are the glycosylated sites, the N-linked structures identified belonging to both high-mannose and complex type glycans.
8910321	5	73	gly	glycosylated	834:845	arg1	-488			Asn-408 and -488	the N-linked structures					Asn-408 and -488	Mass spectral analysis showed that Asn-408 and -488 are the glycosylated sites, the N-linked structures identified belonging to both high-mannose and complex type glycans.
8910321	5	73	gly	glycosylated	834:845	arg1	the glycosylated sites			sites	the N-linked structures					sites	Mass spectral analysis showed that Asn-408 and -488 are the glycosylated sites, the N-linked structures identified belonging to both high-mannose and complex type glycans.
8910321	5	73	gly	glycosylated	834:845	arg1	-488			Asn-408 and -488						Asn-408 and -488	Mass spectral analysis showed that Asn-408 and -488 are the glycosylated sites, the N-linked structures identified belonging to both high-mannose and complex type glycans.
21148085	8	5	part_of	VEGF-D	1091:1096	arg1	N-terminally truncated VEGF-D polypeptides	VEGF-D		N-terminally truncated VEGF-D polypeptides		PUBTATOR	Site	VEGF-D	2277	polypeptides	Both receptor binding and functional assays of N-terminally truncated VEGF-D polypeptides indicated that the residues between the reported proteolytic cleavage sites are important for VEGF-D binding and activation of VEGFR-3, but not of VEGFR-2.
25458834	8	7	part_of	subunit	990:996	arg1	the C terminus	subunit		the C terminus		Fterm	Site	subunit		terminus	Carboxyl groups from the sialic acid residue on podoplanin and from the C terminus of the rhodocytin α subunit interact differently at this "second" binding site on CLEC-2.
25458834	8	32	part_of	site	1044:1047	arg1	CLEC-2	CLEC-2		site		PUBTATOR	Site	CLEC-2	51266	site	Carboxyl groups from the sialic acid residue on podoplanin and from the C terminus of the rhodocytin α subunit interact differently at this "second" binding site on CLEC-2.
1374031	3	71	gly	sialylated	646:655	arg1	their intact sialylated forms				their intact sialylated forms						The carbohydrate chains were purified in their intact sialylated forms by FPLC anion-exchange chromatography on Mono Q, HPLC on Lichrosorb-NH2, and high-pH anion-exchange chromatography on CarboPac PA1.
1899031	2	8	gly	glycosylation	871:883	arg2	this sole potential N-linked glycosylation site			this sole potential N-linked glycosylation site						site	Employing high-performance anion-exchange liquid chromatography mapping of the oligosaccharide units cleaved from the protein by glycopeptidase F, compared with elution positions of standard oligosaccharides, coupled with monosaccharide compositional determinations and analyses of sequential exoglycosidase digestions and specific lectin binding, we find that considerable microheterogeneity in oligosaccharide structure exists at this sole potential N-linked glycosylation site on HPg.
18780401	6	65	gly	N-glycosylated	1035:1048	arg1	N-glycosylated sites			N-glycosylated sites						sites	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
12171601	0	100	gly	Glycosylation	0:12	arg1	hPAR2	hPAR2				PUBTATOR		hPAR2	2150		Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	0	100	gly	Glycosylation	0:12	arg1	human proteinase-activated receptor-2	human proteinase-activated receptor-2				PUBTATOR		proteinase-activated receptor-2	2150		Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
11320094	6	49	part_of	multi-spanning	1280:1293	arg1	a multi-spanning membrane domain	multi		a multi-spanning membrane domain		OGER	Site	multi		domain	This leads to a model in which each half has a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain.
21733844	4	20	gly	glycosylation	563:575	arg2	three predicted glycosylation sites			three predicted glycosylation sites						sites	This finding confirms one of three predicted glycosylation sites for hAQP10, and its glycosylation is unique for the human aquaporins overproduced in this host.
16601115	5	60	part_of	F	1046:1046	arg1	the two N-linked glycosylation sites	cystatin F		the two N-linked glycosylation sites		PUBTATOR	Site	cystatin F	8530	sites	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
17548821	5	60	part_of	site	1129:1132	arg1	the receptor	receptor		site		Fterm	Site	receptor		site	Structure-guided alanine mutagenesis of R5-6 revealed that two Lys residues (Lys-2360 and Lys-2467) constitute a central binding site for the low-density lipoprotein receptor class A module in the receptor, indicating a strong similarity to the ligand recognition mode shared among the endocytic lipoprotein receptors.
22412906	6	49	gly	glycosylated	1060:1071	arg1	these Asn residues			these Asn residues						Asn residues	Here, we show that each of these Asn residues is glycosylated when either human receptor is expressed in Chinese hamster ovary cells.
22351761	0	43	gly	N-glycosylated	21:34	arg1	N-glycosylated human glypican-1 core protein	N-glycosylated human glypican-1 core protein				Fterm		protein			Crystal structure of N-glycosylated human glypican-1 core protein: structure of two loops evolutionarily conserved in vertebrate glypican-1.
17040911	6	78	part_of	protease	1036:1043	arg1	the protease domain	protease		the protease domain		Fterm	Site	protease		domain	The removal of two glycans in the protease domain at Asn-234 and Asn-270, as well as one in the tumor necrosis factor receptor-associated factor domain at Asn-452, by a deglycosidase under nondenaturing conditions decreased the chemical and thermal stability of the homo-oligomer without affecting quaternary structure.
25456591	10	89	gly	O-glycosylation	1678:1692	arg1	the same site			site						site	Moreover, the phosphorylation and O-glycosylation on the same site such as T159 of Factor IX and T170 of kappa-casein were able to be unambiguously differentiated.
3202829	8	27	gly	glycosylation	1074:1086	arg1	human seminal RNase	human seminal RNase				OGER		RNase	P07998		The glycosylation pattern of human seminal RNase is very similar to that of the pancreatic enzyme.
23980170	3	55	part_of	ST2	530:532	arg1	the ectodomain	ST2		the ectodomain		PUBTATOR	Site	ST2	Q06520	ectodomain	To clarify the interaction of IL-33 with its receptors, we determined the crystal structure of IL-33 in complex with the ectodomain of ST2 at a resolution of 3.27 Å.
17956937	6	70	gly	predominant	1207:1217	arg2	the seminal plasma PSA AND high-mannose and hybrid types	the seminal plasma PSA			high-mannose and hybrid types	PUBTATOR		PSA	354		In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17548821	4	51	part_of	R5-6	816:819	arg1	the R5-6 fragment	R5-6		the R5-6 fragment		Cterm	Site	R5-6		fragment	A 2.0-A crystal structure from the R5-6 fragment revealed not only a unique domain arrangement wherein two repeats were aligned side by side with the same orientation, but also the unexpected presence of bound Zn ions.
23319596	8	42	part_of	LOX	1277:1279	arg1	the LOX catalytic domain	LOX		the LOX catalytic domain		PUBTATOR	Site	LOX	4015	domain	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	8	58	part_of	LOX	1349:1351	arg1	the LOX catalytic domain	LOX		the LOX catalytic domain		PUBTATOR	Site	LOX	4015	domain	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	8	73	part_of	hLOX	1373:1376	arg1	the LOX catalytic domain	hLOX		the LOX catalytic domain		PUBTATOR	Site	hLOX	4015	domain	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
29019981	4	69	part_of	channel-distal	634:647	arg1	the N terminus	channel		the N terminus		Fterm	Site	channel		terminus	Combined with mutagenesis analysis, the TRPML1 structure reveals that phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) binds to the N terminus of the channel-distal from the pore-and the helix-turn-helix extension between segments S2 and S3 probably couples ligand binding to pore opening.
8631363	9	10	part_of	factor-alpha	1590:1601	arg1	Ser 4	tumor necrosis factor-alpha		Ser 4		PUBTATOR	SpecificSite	tumor necrosis factor-alpha	7124	Ser 4	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	9	10	part_of	factor-alpha	1590:1601	arg1	the 0-glycosylation site	tumor necrosis factor-alpha		the 0-glycosylation site		PUBTATOR	Site	tumor necrosis factor-alpha	7124	site	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
1657953	3	16	part_of	insulin	335:341	arg1	His209	insulin receptor		His209		PUBTATOR	AminoAcid	insulin receptor	3630	His209	His209 (insulin receptor numbering system) is 1 of 2 amino acid residues that are identically conserved in the cysteine-rich domains of insulin receptors, epidermal growth factor receptors, and other homologous receptors.
1657953	3	27	part_of	receptors	506:514	arg1	the cysteine-rich domains	receptors		the cysteine-rich domains		Fterm	Site	receptors		domains	His209 (insulin receptor numbering system) is 1 of 2 amino acid residues that are identically conserved in the cysteine-rich domains of insulin receptors, epidermal growth factor receptors, and other homologous receptors.
1657953	3	38	part_of	receptors	538:546	arg1	the cysteine-rich domains	receptors		the cysteine-rich domains		Fterm	Site	receptors		domains	His209 (insulin receptor numbering system) is 1 of 2 amino acid residues that are identically conserved in the cysteine-rich domains of insulin receptors, epidermal growth factor receptors, and other homologous receptors.
1657953	3	51	part_of	receptor	343:350	arg1	His209	insulin receptor		His209		PUBTATOR	AminoAcid	insulin receptor	3630	His209	His209 (insulin receptor numbering system) is 1 of 2 amino acid residues that are identically conserved in the cysteine-rich domains of insulin receptors, epidermal growth factor receptors, and other homologous receptors.
1657953	3	56	part_of	receptors	471:479	arg1	the cysteine-rich domains	insulin receptors		the cysteine-rich domains		PUBTATOR	Site	insulin receptors	3630	domains	His209 (insulin receptor numbering system) is 1 of 2 amino acid residues that are identically conserved in the cysteine-rich domains of insulin receptors, epidermal growth factor receptors, and other homologous receptors.
14718370	11	81	gly	C-mannosylation	1711:1725	arg1	the Cys subdomains			the Cys subdomains						Cys subdomains	C-mannosylation is likely required for proper folding of the Cys subdomains and/or for some aspect of ER export during mucin biosynthesis.
8670172	0	111	part_of	CD59	66:69	arg1	Structural composition	CD59		Structural composition		PUBTATOR	Site	CD59	966	position	Structural composition and functional characterization of soluble CD59: heterogeneity of the oligosaccharide and glycophosphoinositol (GPI) anchor revealed by laser-desorption mass spectrometric analysis.
15044018	0	10	gly	glycoprotein	87:98	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			The islet-specific glucose-6-phosphatase-related protein, implicated in diabetes, is a glycoprotein embedded in the endoplasmic reticulum membrane.
11375981	5	102	gly	N-glycosylation	1080:1094	arg2	potential N-glycosylation sites			potential N-glycosylation sites						sites	In contrast, potential N-glycosylation sites introduced near the N terminus, or between putative transmembrane (TM) helices 4 and 5, were not glycosylated.
11375981	5	26	gly	glycosylated	1199:1210	arg1	potential N-glycosylation sites			sites						sites	In contrast, potential N-glycosylation sites introduced near the N terminus, or between putative transmembrane (TM) helices 4 and 5, were not glycosylated.
25081999	5	12	gly	Ser41	997:1001	arg1	the O-GlcNAc modification site			Ser41 residue	the O-GlcNAc modification site					Ser41 residue	To gain insight into the PTM of hSCP1, we used the Western blot, immunoprecipitation, succinylayed wheat germ agglutininprecipitation, liquid chromatography-mass spectrometry analyses, and site-directed mutagenesis and identified the Ser41 residue of hSCP1 as the O-GlcNAc modification site.
25081999	5	50	gly	hSCP1	1014:1018	arg1	the O-GlcNAc modification site	hSCP1			the O-GlcNAc modification site	PUBTATOR		hSCP1	58190		To gain insight into the PTM of hSCP1, we used the Western blot, immunoprecipitation, succinylayed wheat germ agglutininprecipitation, liquid chromatography-mass spectrometry analyses, and site-directed mutagenesis and identified the Ser41 residue of hSCP1 as the O-GlcNAc modification site.
7781780	1	4	part_of	erythropoietin	285:298	arg1	glycosylation site I	erythropoietin		glycosylation site I		PUBTATOR	Site	erythropoietin	2056	site	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	4	part_of	erythropoietin	285:298	arg1	Asn-24	erythropoietin		Asn-24		PUBTATOR	SpecificSite	erythropoietin	2056	Asn-24	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
10383441	0	0	gly	I	83:83	arg1	mannose phosphorylation	DNase I			mannose phosphorylation	PUBTATOR		DNase I	13419		Identification of amino acids that modulate mannose phosphorylation of mouse DNase I, a secretory glycoprotein.
10383441	0	36	gly	glycoprotein	98:109	arg1	mouse DNase I	mouse DNase I				PUBTATOR		DNase I	13419		Identification of amino acids that modulate mannose phosphorylation of mouse DNase I, a secretory glycoprotein.
10383441	0	36	gly	glycoprotein	98:109	arg1	a secretory glycoprotein	a secretory glycoprotein				Fterm		glycoprotein			Identification of amino acids that modulate mannose phosphorylation of mouse DNase I, a secretory glycoprotein.
14711516	1	24	gly	glycosylation	234:246	arg2	individual glycosylation sites			individual glycosylation sites						sites	Structural studies of asparagine-linked glycoproteins are complicated by the oligosaccharide heterogeneity inherent to individual glycosylation sites.
14711516	1	54	gly	glycoproteins	144:156	arg1	asparagine-linked glycoproteins	asparagine-linked glycoproteins				Fterm		glycoproteins			Structural studies of asparagine-linked glycoproteins are complicated by the oligosaccharide heterogeneity inherent to individual glycosylation sites.
21402931	1	5	part_of	ZP-C	228:231	arg1	ZP-N and ZP-C regions	ZP		ZP-N and ZP-C regions		Cterm	Site	ZP		regions	The zona pellucida (ZP) domain is a bipartite protein structural element comprised of ZP-N and ZP-C regions.
21402931	1	72	part_of	ZP-N	219:222	arg1	ZP-N and ZP-C regions	ZP		ZP-N and ZP-C regions		Cterm	Site	ZP		regions	The zona pellucida (ZP) domain is a bipartite protein structural element comprised of ZP-N and ZP-C regions.
2403553	11	0	gly	contain	1642:1648	arg1	the receptors AND both complex-type and high mannose-type N-linked oligosaccharides	the receptors			both complex-type and high mannose-type N-linked oligosaccharides	Fterm		receptors			In addition, the receptors from all three cell lines contain both complex-type and high mannose-type N-linked oligosaccharides.
8636209	3	99	part_of	gamma	390:394	arg1	the extracellular (EC), transmembrane (TM), and cytoplasmic (CY) domain	CD3 gamma		the extracellular (EC), transmembrane (TM), and cytoplasmic (CY) domain		PUBTATOR	Site	CD3 gamma	917	domain	In this study we examined the role of the extracellular (EC), transmembrane (TM), and cytoplasmic (CY) domain of CD3 gamma in assembly and cell surface expression of the complete TCR in human T cells.
28327546	0	84	gly	N-glycosylation	28:42	arg2	the N-glycosylation site			the N-glycosylation site						site	Missense mutations near the N-glycosylation site of the A2 domain lead to various intracellular trafficking defects in coagulation factor VIII.
28327546	0	84	gly	N-glycosylation	28:42	arg2	the A2 domain			domain						domain	Missense mutations near the N-glycosylation site of the A2 domain lead to various intracellular trafficking defects in coagulation factor VIII.
1533657	7	9	part_of	SCR2	1083:1086	arg1	identical sequences	SCR2		sequences		PUBTATOR	Site	SCR2	5937	sequences	Amino acid comparison of these factor H-related proteins showed identical leader sequences, an exchange of three amino acids in SCR1, identical sequences of SCR2, and a lower degree of homology between SCR3-4 (h24 and h29) and SCR4-5 (h37 and h42).
6587378	1	25	gly	2-glycoprotein	128:141	arg1	a human plasma protein	a human plasma protein				Fterm		protein			We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	1	25	gly	2-glycoprotein	128:141	arg1	beta 2-glycoprotein I	beta 2-glycoprotein I				OGER		beta 2-glycoprotein I	P02749		We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
11588155	5	12	gly	apoB100	982:988	arg1	The N-glycan composition	apoB100			The N-glycan composition	PUBTATOR		apoB100	338		The N-glycan composition of apoB100 derived from five LDL subpopulations (LDL1, d = 1.018-1.023; LDL2, d = 1.023-1.030; LDL3, d = 1.030-1.040; LDL4, d = 1.040-1.051; LDL5, d = 1.051-1.065 g/ml) did not vary in normolipidemic or hypercholesterolemic subjects.
20427285	6	1	part_of	ZPI	826:828	arg1	Glu-383	ZPI		residues Glu-313 and Glu-383		PUBTATOR	SpecificSite	ZPI	51156	residues Glu-313 and Glu-383	Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Glu-383 in fXa binding.
20427285	6	1	part_of	ZPI	826:828	arg1	Glu-313	ZPI		residues Glu-313 and Glu-383		PUBTATOR	SpecificSite	ZPI	51156	residues Glu-313 and Glu-383	Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Glu-383 in fXa binding.
20427285	6	1	part_of	ZPI	826:828	arg1	Glu-313	ZPI		residues Glu-313 and Glu-383		PUBTATOR	SpecificSite	ZPI	51156	residues Glu-313 and Glu-383	Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Glu-383 in fXa binding.
9572875	9	51	gly	O-glycosylated	1730:1743	arg1	a central region			a central region						region	A model of IGFBP-6 is developed in which these distinct domains are separated by a central region which is O-glycosylated.
9136890	7	67	gly	Asn	882:884	arg1	The oligosaccharides			Asn 251	The oligosaccharides					Asn 251	The oligosaccharides at Asn 251 are of the complex type.
2363690	0	10	gly	proteins	85:92	arg1	the N-linked oligosaccharide structures	proteins			the N-linked oligosaccharide structures	Fterm		proteins			A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins.
8069634	0	24	part_of	N2	72:73	arg1	the human lactotransferrin N2 fragment	lactotransferrin N2		the human lactotransferrin N2 fragment		PUBTATOR	Site	lactotransferrin N2	4057	fragment	Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety.
8069634	0	32	part_of	lactotransferrin	55:70	arg1	the human lactotransferrin N2 fragment	lactotransferrin N2		the human lactotransferrin N2 fragment		PUBTATOR	Site	lactotransferrin N2	4057	fragment	Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety.
1326557	8	62	part_of	protein	1855:1861	arg1	other reported protein sequences	protein		other reported protein sequences		Fterm	Site	protein		sequences	The central 595-amino acid portion of neurocan has no homology with other reported protein sequences.
20068230	3	54	gly	sites	580:584	arg1	proteins	proteins			sites	Fterm		proteins			Here, we identify 141 previously unknown O-GlcNAc sites on proteins that function in spindle assembly and cytokinesis.
22766194	7	81	part_of	CD10	1329:1332	arg1	the three consensus sites	CD10		the three consensus sites		PUBTATOR	Site	CD10	4311	sites	All of the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10 were confirmed to be N-glycosylated.
3353370	1	80	gly	glycoprotein	188:199	arg1	human glycoprotein Ib	human glycoprotein Ib				Fterm		glycoprotein			The primary structure of the beta chain of human glycoprotein Ib (GPIb), the platelet receptor for von Willebrand factor, has been established by a combination of cDNA cloning and amino acid sequence analysis.
26598643	5	3	gly	O-glycans	1059:1067	arg1	human blood plasma proteins	proteins			O-glycans	Fterm		proteins			To this end pooled human blood plasma of healthy donors was proteolytically digested using a broad-specific enzyme (Proteinase K), followed by a precipitation step, as well as a glycopeptide enrichment and fractionation step via hydrophilic interaction liquid chromatography, the latter being optimized for intact O-glycopeptides carrying short mucin-type core-1 and -2 O-glycans, which represent the vast majority of O-glycans on human blood plasma proteins.
26598643	5	19	gly	O-glycopeptides	955:969	arg2	intact O-glycopeptides			intact O-glycopeptides						O-glycopeptides	To this end pooled human blood plasma of healthy donors was proteolytically digested using a broad-specific enzyme (Proteinase K), followed by a precipitation step, as well as a glycopeptide enrichment and fractionation step via hydrophilic interaction liquid chromatography, the latter being optimized for intact O-glycopeptides carrying short mucin-type core-1 and -2 O-glycans, which represent the vast majority of O-glycans on human blood plasma proteins.
26598643	5	115	gly	glycopeptide	819:830	arg2	a glycopeptide enrichment			a glycopeptide enrichment						glycopeptide	To this end pooled human blood plasma of healthy donors was proteolytically digested using a broad-specific enzyme (Proteinase K), followed by a precipitation step, as well as a glycopeptide enrichment and fractionation step via hydrophilic interaction liquid chromatography, the latter being optimized for intact O-glycopeptides carrying short mucin-type core-1 and -2 O-glycans, which represent the vast majority of O-glycans on human blood plasma proteins.
26598643	5	20	gly	carrying	971:978	arg1	intact O-glycopeptides AND -2 O-glycans			intact O-glycopeptides	-2 O-glycans					O-glycopeptides	To this end pooled human blood plasma of healthy donors was proteolytically digested using a broad-specific enzyme (Proteinase K), followed by a precipitation step, as well as a glycopeptide enrichment and fractionation step via hydrophilic interaction liquid chromatography, the latter being optimized for intact O-glycopeptides carrying short mucin-type core-1 and -2 O-glycans, which represent the vast majority of O-glycans on human blood plasma proteins.
19838169	0	27	gly	glycopeptides	14:26	arg2	glycopeptides			glycopeptides						glycopeptides	Enrichment of glycopeptides for glycan structure and attachment site identification.
9822688	6	50	part_of	has	780:782	arg1	The 1.8 A structure AND a beta-sandwich C-terminal domain	structure of rPLRP2		domain		PUBTATOR	Site	structure of rPLRP2	117554	domain	The 1.8 A structure of rPLRP2, like the tertiary structure of human PTL, has a globular N-terminal domain and a beta-sandwich C-terminal domain.
12944413	2	58	gly	glycoprotein	189:200	arg1	an oligomeric glycoprotein	glycoprotein			two sialic acid residues	Fterm		glycoprotein			The serotonin transporter (SERT) is an oligomeric glycoprotein with two sialic acid residues on each of two complex oligosaccharide molecules.
15173186	8	3	gly	glycoprotein	1284:1295	arg1	glycoprotein Ib	glycoprotein Ib				Fterm		glycoprotein			Using circular dichroism spectroscopy, we show here that purified human Toll-like receptor 2 and 4 proteins have secondary structure contents similar to glycoprotein Ib.
20378933	2	0	gly	glycosylation	252:264	arg2	six potential N-linked glycosylation sites			six potential N-linked glycosylation sites						sites	It is a heavily glycosylated protein with six potential N-linked glycosylation sites.
20378933	2	25	gly	glycosylated	203:214	arg1	a heavily glycosylated protein	a heavily glycosylated protein				Fterm		protein			It is a heavily glycosylated protein with six potential N-linked glycosylation sites.
10200178	9	48	gly	Asn-180	1699:1705	arg1	The Lewisx trisaccharide			Asn-180	The Lewisx trisaccharide					Asn-180	The Lewisx trisaccharide is the major nonreducing structure at Asn-180, and significant amounts of both Lewisx and sialyl Lewisx epitopes are observed at Asn-196.
10200178	9	73	gly	epitopes	1765:1772	arg1	both Lewisx and sialyl Lewisx epitopes				both Lewisx and sialyl Lewisx epitopes						The Lewisx trisaccharide is the major nonreducing structure at Asn-180, and significant amounts of both Lewisx and sialyl Lewisx epitopes are observed at Asn-196.
10200178	9	98	gly	observed	1778:1785	arg1	Asn-196 AND both Lewisx and sialyl Lewisx epitopes			Asn-196	both Lewisx and sialyl Lewisx epitopes					Asn-196	The Lewisx trisaccharide is the major nonreducing structure at Asn-180, and significant amounts of both Lewisx and sialyl Lewisx epitopes are observed at Asn-196.
23662732	1	39	gly	glycosylation	138:150	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
23662732	1	68	gly	glycoproteins	161:173	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
7505568	3	17	part_of	MAG	290:292	arg1	human MAG glycopeptides	MAG		human MAG glycopeptides		PUBTATOR	Site	MAG	4099	glycopeptides	In this study, human MAG glycopeptides were isolated and sequenced.
25374123	9	23	gly	N-glycopeptides	1264:1278	arg2	17 site-specific N-glycopeptides			17 site-specific N-glycopeptides						N-glycopeptides	As a result, a total of 17 site-specific N-glycopeptides were completely identified in all of the three N-glycosylation sites of vitronectin in human plasma, including 12 N-glycopeptides first reported.
25374123	9	38	gly	N-glycopeptides	1394:1408	arg2	12 N-glycopeptides			12 N-glycopeptides						N-glycopeptides	As a result, a total of 17 site-specific N-glycopeptides were completely identified in all of the three N-glycosylation sites of vitronectin in human plasma, including 12 N-glycopeptides first reported.
25374123	9	73	gly	N-glycosylation	1327:1341	arg1	vitronectin	vitronectin		sites		PUBTATOR		vitronectin	7448	sites	As a result, a total of 17 site-specific N-glycopeptides were completely identified in all of the three N-glycosylation sites of vitronectin in human plasma, including 12 N-glycopeptides first reported.
25374123	9	73	gly	N-glycosylation	1327:1341	arg1	vitronectin	vitronectin		N-glycopeptides		PUBTATOR		vitronectin	7448	N-glycopeptides	As a result, a total of 17 site-specific N-glycopeptides were completely identified in all of the three N-glycosylation sites of vitronectin in human plasma, including 12 N-glycopeptides first reported.
23302862	5	12	gly	receptor	1013:1020	arg1	the first leucine-rich-repeat domain	insulin receptor			the first leucine-rich-repeat domain	PUBTATOR		insulin receptor	P01308		The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	38	gly	leucine-rich-repeat	970:988	arg1	the first leucine-rich-repeat domain			leucine	the first leucine-rich-repeat domain					leucine	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
8068684	3	17	gly	N-glycosylation	569:583	arg2	the individual potential N-glycosylation sites			the individual potential N-glycosylation sites						sites	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	17	gly	N-glycosylation	569:583	arg2	Asn to Asp			Asn to Asp						Asp	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	43	gly	glycosylation	448:460	arg2	the sites			the sites						sites	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
2511201	11	1	part_of	Z	1968:1968	arg1	the first epidermal growth factor-like domains	protein Z		the first epidermal growth factor-like domains		Cterm	Site	protein Z		domains	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	49	part_of	VII	1945:1947	arg1	the first epidermal growth factor-like domains	VII		the first epidermal growth factor-like domains		Cterm	Site	VII		domains	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
12421832	14	88	part_of	PAPP-A	1935:1940	arg1	individual, putative PAPP-A domains	PAPP-A		individual, putative PAPP-A domains		PUBTATOR	Site	PAPP-A	5069	domains	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
8639592	4	49	gly	N-glycosylation	763:777	arg2	three potential N-glycosylation sites			three potential N-glycosylation sites						sites	Among three potential N-glycosylation sites, both Asn117 and Asn167 were fully N-glycosylated but Asn228 was not.
8639592	4	78	gly	N-glycosylated	820:833	arg1	Asn167			Asn117 and Asn167						Asn117 and Asn167	Among three potential N-glycosylation sites, both Asn117 and Asn167 were fully N-glycosylated but Asn228 was not.
2642896	10	7	part_of	enzyme	1551:1556	arg1	The amino acid composition	enzyme		The amino acid composition		Fterm	Site	enzyme		position	The amino acid composition of the purified enzyme indicated that about 20 residues of hydrophobic amino acids of the N terminus are post-translationally deleted, probably as a signal peptide.
17222411	1	36	gly	sialoglycoprotein	140:156	arg1	Podoplanin	Podoplanin				OGER		Podoplanin	Q86YL7		Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation.
17222411	1	36	gly	sialoglycoprotein	140:156	arg1	a mucin-type sialoglycoprotein	a mucin-type sialoglycoprotein				Fterm		sialoglycoprotein			Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation.
9530955	11	95	gly	presence	1763:1770	arg2	epitectin AND N-linked saccharides	epitectin			N-linked saccharides	Fterm		epitectin			Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
8416919	3	38	gly	released	457:464	arg1	pepsin-digested protein AND The oligosaccharides	pepsin-digested protein			The oligosaccharides	Fterm		protein			The oligosaccharides were released from pepsin-digested protein by glycoamidase A (from almond) digestion.
19478079	0	1	gly	modification	29:40	arg1	CCAAT enhancer-binding protein beta	CCAAT enhancer-binding protein beta			modification	PUBTATOR		CCAAT enhancer-binding protein beta	1051		O-linked N-acetylglucosamine modification on CCAAT enhancer-binding protein beta: role during adipocyte differentiation.
8636209	7	36	gly	glycosylation	832:844	arg2	N-linked glycosylation sites			N-linked glycosylation sites						sites	Mutagenesis of N-linked glycosylation sites showed that glycosylation of CD3 gamma is not required for TCR assembly and expression.
8636209	7	68	gly	glycosylation	864:876	arg1	TCR assembly	TCR assembly				PUBTATOR		TCR	6962		Mutagenesis of N-linked glycosylation sites showed that glycosylation of CD3 gamma is not required for TCR assembly and expression.
8636209	7	68	gly	glycosylation	864:876	arg1	CD3 gamma	CD3 gamma				PUBTATOR		CD3 gamma	917		Mutagenesis of N-linked glycosylation sites showed that glycosylation of CD3 gamma is not required for TCR assembly and expression.
3550808	2	27	gly	asparagine-linked	193:209	arg1	two asparagine-linked carbohydrate side chains			asparagine	two asparagine-linked carbohydrate side chains					asparagine	The protein consists of 218 amino acid residues, contains two asparagine-linked carbohydrate side chains, and is joined together by four disulfide bonds.
3550808	2	19	gly	contains	180:187	arg1	The protein AND two asparagine-linked carbohydrate side chains	The protein			two asparagine-linked carbohydrate side chains	Fterm		protein			The protein consists of 218 amino acid residues, contains two asparagine-linked carbohydrate side chains, and is joined together by four disulfide bonds.
26563299	9	10	gly	sialylated	1414:1423	arg1	core 1				core 1						IL-15 contained no O-glycans, whereas sIL-15Rα was heavily O-glycosylated with partially sialylated core 1 and 2-type mono- to hexasaccharides on Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160.
26563299	9	15	gly	hexasaccharides	1452:1466	arg1	Thr81			Thr81	Thr81		AminoAcid			Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160	IL-15 contained no O-glycans, whereas sIL-15Rα was heavily O-glycosylated with partially sialylated core 1 and 2-type mono- to hexasaccharides on Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160.
26563299	9	15	gly	hexasaccharides	1452:1466	arg1	Ser158			Ser158	Ser158		AminoAcid			Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160	IL-15 contained no O-glycans, whereas sIL-15Rα was heavily O-glycosylated with partially sialylated core 1 and 2-type mono- to hexasaccharides on Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160.
26563299	9	15	gly	hexasaccharides	1452:1466	arg1	Ser160			Ser160	Ser160		AminoAcid			Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160	IL-15 contained no O-glycans, whereas sIL-15Rα was heavily O-glycosylated with partially sialylated core 1 and 2-type mono- to hexasaccharides on Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160.
26563299	9	15	gly	hexasaccharides	1452:1466	arg1	Thr86			Thr86	Thr86		AminoAcid			Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160	IL-15 contained no O-glycans, whereas sIL-15Rα was heavily O-glycosylated with partially sialylated core 1 and 2-type mono- to hexasaccharides on Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160.
26563299	9	15	gly	hexasaccharides	1452:1466	arg1	Thr156			Thr156	Thr156		AminoAcid			Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160	IL-15 contained no O-glycans, whereas sIL-15Rα was heavily O-glycosylated with partially sialylated core 1 and 2-type mono- to hexasaccharides on Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160.
26563299	9	15	gly	hexasaccharides	1452:1466	arg1	Thr2			Thr2	Thr2		AminoAcid			Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160	IL-15 contained no O-glycans, whereas sIL-15Rα was heavily O-glycosylated with partially sialylated core 1 and 2-type mono- to hexasaccharides on Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160.
26563299	9	58	gly	O-glycosylated	1384:1397	arg1	sIL-15Rα	sIL-15Rα				OGER		sIL	Q15468		IL-15 contained no O-glycans, whereas sIL-15Rα was heavily O-glycosylated with partially sialylated core 1 and 2-type mono- to hexasaccharides on Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160.
26563299	9	97	gly	contained	1331:1339	arg1	IL-15 AND no O-glycans	IL-15			no O-glycans	PUBTATOR		IL-15	3600		IL-15 contained no O-glycans, whereas sIL-15Rα was heavily O-glycosylated with partially sialylated core 1 and 2-type mono- to hexasaccharides on Thr2, Thr81, Thr86, Thr156, Ser158, and Ser160.
15536627	4	43	gly	glycopeptides	780:792	arg2	the glycopeptides			the glycopeptides						glycopeptides	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
9757569	2	26	gly	glycosylated	391:402	arg1	S14N angiotensinogen	S14N angiotensinogen		Asn14		PUBTATOR		S14N angiotensinogen	P01019	Asn14	The molecular weight was about 3,000 larger than that of wild-type ovine angiotensinogen, indicating that S14N angiotensinogen was glycosylated at Asn14.
15616124	3	7	part_of	has	416:418	arg1	Human FVII AND two N-glycosylation sites	Human FVII		two N-glycosylation sites		Cterm	Site	Human FVII	2155	sites	Human FVII has two N-glycosylation sites (N145 and N322).
15616124	3	7	part_of	has	416:418	arg1	Human FVII AND N145	Human FVII		N145 and N322		Cterm	SpecificSite	Human FVII	2155	N145 and N322	Human FVII has two N-glycosylation sites (N145 and N322).
20622017	7	37	gly	released	972:979	arg1	liver membrane glycoproteins AND N-Glycans	liver membrane glycoproteins			N-Glycans	Fterm		glycoproteins			N-Glycans released from liver membrane glycoproteins included many glycans also identified in the kidney.
20622017	7	95	gly	glycoproteins	1001:1013	arg1	liver membrane glycoproteins	liver membrane glycoproteins				Fterm		glycoproteins			N-Glycans released from liver membrane glycoproteins included many glycans also identified in the kidney.
21264968	2	33	gly	O-glycosylation	689:703	arg2	O-glycosylation site(s)			O-glycosylation site(s)						site	Here we report an efficient approach by combining MS and NMR spectroscopy that allows for the identification of O-glycosylation site(s) and the effect of O-glycosylation on the peptide backbone structures during enzymatic mucin domain assembly by using an isoform UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T2 (ppGalNAcT2) in vitro.
21264968	2	124	gly	O-glycosylation	731:745	arg1	the peptide backbone structures			the peptide backbone structures						peptide	Here we report an efficient approach by combining MS and NMR spectroscopy that allows for the identification of O-glycosylation site(s) and the effect of O-glycosylation on the peptide backbone structures during enzymatic mucin domain assembly by using an isoform UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T2 (ppGalNAcT2) in vitro.
7929098	4	61	gly	glycosylated	659:670	arg1	a glycosylated protein	a glycosylated protein				Fterm		protein			This generated a glycosylated protein of 93 kDa.
11371615	0	42	part_of	Sp1	36:38	arg1	Sp1 activation domain	Sp1		Sp1 activation domain		OGER	Site	Sp1	Q8N907	domain	O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability.
7654718	7	8	part_of	C-tail	1093:1098	arg1	C-tail fragment	C-tail		C-tail fragment		Cterm	Site	C-tail		fragment	Edman degradation of C-tail fragment and its pronase subfragment suggest a number of glycosylation sites which are flanked by a consensus motif of PVPP.
15677325	3	61	part_of	GluR6	534:538	arg1	the GluR6 S1S2 domain	GluR6		the GluR6 S1S2 domain		PUBTATOR	Site	GluR6	2898	domain	In common with the AMPA receptor subunit GluR2, the GluR6 S1S2 domain associates as a dimer, with many of the interdimer contacts being conserved.
23010571	5	10	gly	glycoprotein	762:773	arg1	a secreted, N-glycosylated 60kDa glycoprotein	a secreted, N-glycosylated 60kDa glycoprotein				Fterm		glycoprotein			Recombinant ADAMTSL5 is a secreted, N-glycosylated 60kDa glycoprotein located in the subcellular matrix, on the cell-surface, and in the medium of transfected cells.
23010571	5	10	gly	glycoprotein	762:773	arg1	Recombinant ADAMTSL5	Recombinant ADAMTSL5				PUBTATOR		Recombinant ADAMTSL5	339366		Recombinant ADAMTSL5 is a secreted, N-glycosylated 60kDa glycoprotein located in the subcellular matrix, on the cell-surface, and in the medium of transfected cells.
23661698	2	23	part_of	ephrin-A1	368:376	arg1	the Asn-26	ephrin-A1		the Asn-26		PUBTATOR	SpecificSite	ephrin-A1	1942	Asn-26	The crystal structure of the ligand-receptor complex revealed a glycosylation on the Asn-26 of ephrin-A1.
8617200	7	48	gly	8-Cys	1149:1153	arg1	an 8-Cys repeat			Cys	an 8-Cys repeat					Cys	The data indicate that an 8-Cys repeat of LTBP is capable of covalent and specific protein-protein interactions.
27313224	4	81	gly	N-glycosylation	774:788	arg2	five putative N-glycosylation sites			sites						sites	SV2C-LD4 exhibits the strongest protein-protein interaction and comprises five putative N-glycosylation sites (PNG sites).
3497398	4	48	part_of	Additional	592:601	arg1	Additional fragments	Additional		Additional fragments		Cterm	Site	Additional		fragments	Additional fragments were obtained by treatment of native glycocalicin with trypsin, Staphylococcus aureus V8 protease, and Serratia marcescens protease.
7944531	1	33	gly	glycoprotein	150:161	arg1	carbohydrate deficient glycoprotein				carbohydrate deficient glycoprotein						The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	1	33	gly	glycoprotein	150:161	arg1	CDG				CDG						The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
30459171	3	1	gly	glycopeptides	428:440	arg2	O-linked glycopeptides			O-linked glycopeptides						glycopeptides	Here, a chemoenzymatic method is introduced for the site-specific extraction of O-linked glycopeptides (EXoO), which enabled the mapping of over 3,000 O-linked glycosylation sites and definition of their glycans on over 1,000 proteins in human kidney tissues, T cells, and serum.
30459171	3	21	gly	glycosylation	499:511	arg2	over 3,000 O-linked glycosylation sites			over 3,000 O-linked glycosylation sites						sites	Here, a chemoenzymatic method is introduced for the site-specific extraction of O-linked glycopeptides (EXoO), which enabled the mapping of over 3,000 O-linked glycosylation sites and definition of their glycans on over 1,000 proteins in human kidney tissues, T cells, and serum.
17563389	2	34	gly	glycosylation	324:336	arg1	the NK1R	the NK1R				PUBTATOR		NK1R	6869		We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	2	73	gly	glycosylation	498:510	arg2	both glycosylation sites			both glycosylation sites						sites	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	2	82	gly	mutants	420:426	arg1	Asn --> Gln-18			Asn --> Gln-18						Gln-18	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	2	82	gly	mutants	420:426	arg1	Asn --> Gln-14			Asn --> Gln-14						Gln-14 and Asn	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
27314333	7	22	gly	N-glycosylation	1287:1301	arg2	Rspo2 N-glycosylation site			Rspo2 N-glycosylation site						site	Similar effect can be observed in the N137 Rspo1 or Rspo3 mutant engineered with Rspo2 N-glycosylation site.
21959264	2	54	gly	leucine-rich	309:320	arg1	the extracellular leucine-rich repeats			leucine	the extracellular leucine-rich repeats					leucine	RP105 (radioprotective 105 kDa), a TLR-related molecule, is similar to TLR4 in that the extracellular leucine-rich repeats associate with MD-1, the MD-2-like molecule.
11285216	1	1	part_of	region	183:188	arg1	the (6)F1(1)F2(2)F2 fragment	region		the (6)F1(1)F2(2)F2 fragment						fragment	The solution structure of the (6)F1(1)F2(2)F2 fragment from the gelatin-binding region of fibronectin has been determined (Protein Data Bank entry codes 1e88 and 1e8b).
11285216	1	54	part_of	fibronectin	193:203	arg1	the gelatin-binding region	fibronectin		the gelatin-binding region		PUBTATOR	Site	fibronectin	2335	region	The solution structure of the (6)F1(1)F2(2)F2 fragment from the gelatin-binding region of fibronectin has been determined (Protein Data Bank entry codes 1e88 and 1e8b).
19692335	1	65	gly	glycoproteins	269:281	arg1	multidomain transmembrane glycoproteins	multidomain transmembrane glycoproteins				Fterm		glycoproteins			ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
22226965	7	14	gly	PPARγ	1063:1067	arg1	the O-GlcNAc state	PPARγ 			the O-GlcNAc state	PUBTATOR		PPARγ 	19016		Our results suggest that the O-GlcNAc state of PPARγ influences its transcriptional activity and is involved in adipocyte differentiation.
27991905	5	4	part_of	channel-like	908:919	arg1	the homologous channel-like region	channel		the homologous channel-like region		Fterm	Site	channel		region	The TOP-domain fold is conserved among the polycystins, including the homologous channel-like region of PC1, and is the site of a cluster of ADPKD-associated missense variants.
27991905	5	16	part_of	PC1	931:933	arg1	the homologous channel-like region	PC1		the homologous channel-like region		PUBTATOR	Site	PC1	5310	region	The TOP-domain fold is conserved among the polycystins, including the homologous channel-like region of PC1, and is the site of a cluster of ADPKD-associated missense variants.
17525160	11	51	part_of	hCTR1	1334:1338	arg1	The 17-kDa hCTR1 polypeptide	hCTR1		The 17-kDa hCTR1 polypeptide		PUBTATOR	Site	hCTR1	1317	polypeptide	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
10899108	4	0	part_of	p40	570:572	arg1	Several charged residues	p40		Several charged residues		PUBTATOR	Site	p40	3578	residues	Several charged residues from p35 and p40 intercalate to form a unique interlocking topography, shown by mutagenesis to be critical for p70 formation.
10899108	4	6	part_of	p35	562:564	arg1	Several charged residues	p35		Several charged residues		PUBTATOR	Site	p35	3592	residues	Several charged residues from p35 and p40 intercalate to form a unique interlocking topography, shown by mutagenesis to be critical for p70 formation.
11320094	4	31	gly	glycosylation	833:845	arg2	eight glycosylation sites			eight glycosylation sites						sites	Using trypsin digestion, site-directed mutagenesis, concanavalin A binding, and endoglycosidase digestion, we show that ABCR contains eight glycosylation sites.
29992770	9	56	gly	N-glycopeptides	1236:1250	arg1	haptoglobin	haptoglobin		N-glycopeptides		Fterm		haptoglobin	3240	N-glycopeptides	N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls.
29992770	9	56	gly	N-glycopeptides	1236:1250	arg1	transferrin	transferrin		N-glycopeptides		Fterm		transferrin	7018	N-glycopeptides	N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls.
21932778	4	81	gly	N-glycosylation	622:636	arg2	the potential N-glycosylation sites			the potential N-glycosylation sites						sites	Mutagenesis and enzymatic cleavage indicated that the potential N-glycosylation sites are invariably occupied.
21932778	4	89	gly	occupied	659:666	arg2	the potential N-glycosylation sites			the potential N-glycosylation sites						sites	Mutagenesis and enzymatic cleavage indicated that the potential N-glycosylation sites are invariably occupied.
1904059	2	137	part_of	Factor	173:178	arg1	a multidomain	Factor VII		a multidomain		OGER	Site	Factor VII	P08709	multidomain	Factor VII is a multidomain, vitamin K-dependent plasma glycoprotein that participates in the extrinsic pathway of blood coagulation.
2275556	8	45	gly	glycosylation	1529:1541	arg2	the two potential N-linked glycosylation sites			the two potential N-linked glycosylation sites						sites	The results indicated that only one of the two potential N-linked glycosylation sites (the one at Asn221) is glycosylated.
2275556	8	127	gly	glycosylated	1572:1583	arg1	the two potential N-linked glycosylation sites			the two potential N-linked glycosylation sites						sites	The results indicated that only one of the two potential N-linked glycosylation sites (the one at Asn221) is glycosylated.
11439087	13	30	gly	N-glycosylation	1726:1740	arg2	N-glycosylation sites			N-glycosylation sites						sites	Thus the artificial engineering of N-glycosylation sites could be an effective method to generate homogeneous material for structural studies.
7947762	3	63	part_of	containing	447:456	arg1	peptides AND this residue	peptides		this residue						residue	Mass spectrometric analysis of peptides containing this residue showed a molecular mass 162 Da higher than that expected for tryptophan.
27314333	0	47	gly	N-Glycosylation	0:14	arg1	Human R-Spondin 1	Human R-Spondin 1				PUBTATOR		Human R-Spondin 1	284654		N-Glycosylation of Human R-Spondin 1 Is Required for Efficient Secretion and Stability but Not for Its Heparin Binding Ability.
8435067	4	51	gly	glycosylated	629:640	arg1	all seven sites			all seven sites						sites	We have eliminated these sites individually by site-directed mutagenesis and thereby demonstrated that all seven sites are glycosylated.
2141278	7	16	part_of	alpha	1604:1608	arg1	the N-terminal alpha 1 fragment	N-terminal alpha 1		the N-terminal alpha 1 fragment		PUBTATOR	Site	N-terminal alpha 1	146	fragment	In contrast, both alpha 2 and the N-terminal alpha 1 fragment, starting at serine 24 of the A chain, were able to compete significantly with intact C1s for the formation of the Ca2(+)-dependent C1-s-C1r-C1-r-C1-s tetramer.
2141278	7	54	part_of	N-terminal	1593:1602	arg1	the N-terminal alpha 1 fragment	N-terminal alpha 1		the N-terminal alpha 1 fragment		PUBTATOR	Site	N-terminal alpha 1	146	fragment	In contrast, both alpha 2 and the N-terminal alpha 1 fragment, starting at serine 24 of the A chain, were able to compete significantly with intact C1s for the formation of the Ca2(+)-dependent C1-s-C1r-C1-r-C1-s tetramer.
12421832	12	7	gly	subunit	1655:1661	arg1	N-linked carbohydrate substitution	PAPP-A subunit			N-linked carbohydrate substitution	PUBTATOR		PAPP-A subunit	5069		We also show that of 13 potential sites for N-linked carbohydrate substitution of the PAPP-A subunit, 11 are occupied.
1872845	6	33	gly	Asn-linked	977:986	arg1	its Asn-linked oligosaccharides			Asn	its Asn-linked oligosaccharides					Asn	Our results indicate that vWF itself contains UEA-I reactive sugar chains in its Asn-linked oligosaccharides.
1872845	6	42	gly	contains	933:940	arg1	vWF itself AND UEA-I reactive sugar chains	vWF itself			UEA-I reactive sugar chains	PUBTATOR		vWF	7450		Our results indicate that vWF itself contains UEA-I reactive sugar chains in its Asn-linked oligosaccharides.
22159084	8	17	gly	glycosylation	1071:1083	arg2	glycosylation sites			glycosylation sites						sites	To localize glycosylation sites, we mutated the five consensus sites by replacing asparagine (N) with glutamine.
21757702	7	44	gly	modified	1033:1040	arg3	serine AND O-glucose			serine	O-glucose					serine	We also show through biochemical and mass spectral analyses that serine is the only hydroxyamino acid that is modified with O-glucose on EGF repeats.
18250328	4	42	part_of	NL2	588:590	arg1	the ectodomain	NL2		the ectodomain		PUBTATOR	Site	NL2	79258	ectodomain	Here, we present the 3.3-A crystal structure of the ectodomain from NL2 containing splice insertion A (NL2A).
22000856	4	28	part_of	Dkk1	442:445	arg1	the Dkk1 C-terminal domain	structure of the Dkk1		the Dkk1 C-terminal domain		PUBTATOR	Site	structure of the Dkk1	22943	domain	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	4	30	part_of	Dkk1	503:506	arg1	the Dkk1 N-terminal domain	Dkk1		the Dkk1 N-terminal domain		PUBTATOR	Site	Dkk1	22943	domain	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
3667593	1	24	gly	interferon-beta	186:200	arg1	the major oligosaccharide	interferon-beta			the major oligosaccharide	PUBTATOR		interferon-beta	3456		The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line has been determined.
11746818	6	4	gly	N-glycosylation	1253:1267	arg2	an N-glycosylation site			an N-glycosylation site						site	Multiple peptide alignment showed several sequence motifs corresponding to putative catalytic domains that are conserved throughout all members of the beta 3-galactosyltransferase family, namely, a type II transmembrane domain, a conserved DxD motif, an N-glycosylation site, and five conserved cysteins.
11733580	5	49	part_of	CCR5	680:683	arg1	the CCR5 NH2 terminus	CCR5		the CCR5 NH2 terminus		PUBTATOR	Site	CCR5	1234	terminus	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus was important for efficient beta-chemokine binding.
8142896	5	26	gly	glycosylated	886:897	arg1	Asn223			Asn223						Asn223	Asn223 was never found to be glycosylated.
30899004	5	11	gly	N-glycosite	967:977	arg2	N-glycosite heterogeneity			N-glycosite heterogeneity						N-glycosite	Our data reveal that N-glycosylation profiles can differ between subcellular regions and structural domains and that N-glycosite heterogeneity manifests in several different forms, including dramatic differences in glycosites on the same protein.
30899004	5	24	gly	glycosites	1065:1074	arg2	glycosites			glycosites						glycosites	Our data reveal that N-glycosylation profiles can differ between subcellular regions and structural domains and that N-glycosite heterogeneity manifests in several different forms, including dramatic differences in glycosites on the same protein.
12731887	0	37	part_of	p67	35:37	arg1	A glycosylation site	p67		A glycosylation site		PUBTATOR	Site	p67	64370	site	A glycosylation site, 60SGTS63, of p67 is required for its ability to regulate the phosphorylation and activity of eukaryotic initiation factor 2alpha.
16422668	5	33	part_of	CH1	848:850	arg1	the CH1 domain	CH1		the CH1 domain		OGER	Site	CH1	Q9UBS9	domain	The carbohydrate may act to shield part of the lateral surface of the CH1 domain and crowd the junction between the CH1 and CH2 domains, thereby limiting the segmental flexibility of the Fab arms in intact Yvo IgM, especially at low temperatures.
16422668	5	35	part_of	CH1	894:896	arg1	the CH1 and CH2 domains	CH1		the CH1 and CH2 domains		OGER	Site	CH1	Q9UBS9	domains	The carbohydrate may act to shield part of the lateral surface of the CH1 domain and crowd the junction between the CH1 and CH2 domains, thereby limiting the segmental flexibility of the Fab arms in intact Yvo IgM, especially at low temperatures.
16422668	5	81	part_of	arms	969:972	arg1	intact Yvo IgM	Yvo IgM		arms		Cterm	Site	Yvo IgM	P01871	arms	The carbohydrate may act to shield part of the lateral surface of the CH1 domain and crowd the junction between the CH1 and CH2 domains, thereby limiting the segmental flexibility of the Fab arms in intact Yvo IgM, especially at low temperatures.
7654718	8	19	part_of	C-tail	1301:1306	arg1	the C-tail region	C-tail		the C-tail region		Cterm	Site	C-tail		region	We suggest that this motif may serve as a signal for O-glycosylation in the C-tail region of BAL.
7654718	8	74	part_of	BAL	1318:1320	arg1	the C-tail region	BAL		the C-tail region		OGER	Site	BAL	P19835	region	We suggest that this motif may serve as a signal for O-glycosylation in the C-tail region of BAL.
7514386	1	51	gly	glycoprotein	159:170	arg1	CD59	CD59				PUBTATOR		CD59	966		CD59 is an 18-kDa glycoprotein widely expressed on human cells.
7514386	1	51	gly	glycoprotein	159:170	arg1	an 18-kDa glycoprotein	an 18-kDa glycoprotein				Fterm		glycoprotein			CD59 is an 18-kDa glycoprotein widely expressed on human cells.
2514791	7	53	gly	glycoproteins	2062:2074	arg1	mammalian glycoproteins	mammalian glycoproteins				Fterm		glycoproteins			The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
24509848	10	57	gly	N-glycosylation	1482:1496	arg1	the highly conserved (211)NDS motif			motif						motif	Taken together, these data suggest that N-glycosylation at the highly conserved (211)NDS motif evolved to act as a negative repressor of DDR1 phosphorylation in the absence of ligand.
9705299	1	3	gly	glycoprotein	196:207	arg1	an endoplasmic reticulum transmembrane glycoprotein	an endoplasmic reticulum transmembrane glycoprotein				Fterm		glycoprotein			Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
9705299	1	3	gly	glycoprotein	196:207	arg1	glucose-6-phosphatase	glucose-6-phosphatase				OGER		glucose-6-phosphatase	P35575		Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
16342937	6	68	gly	glycoproteins	805:817	arg1	the zonae glycoproteins	the zonae glycoproteins				Fterm		glycoproteins			These data are consistent with our mass spectrometric analysis of the native rat zona pellucida proteome (defined as the fraction of the total rat proteome to which the zonae glycoproteins contribute) demonstrating that the rat zonae glycoproteins share a high degree of conservation of structural features with respect to their mouse counterparts.
16342937	6	133	gly	glycoproteins	864:876	arg1	the rat zonae glycoproteins	the rat zonae glycoproteins				Fterm		glycoproteins			These data are consistent with our mass spectrometric analysis of the native rat zona pellucida proteome (defined as the fraction of the total rat proteome to which the zonae glycoproteins contribute) demonstrating that the rat zonae glycoproteins share a high degree of conservation of structural features with respect to their mouse counterparts.
7994575	4	12	gly	glycosylation	615:627	arg2	each glycosylation site			each glycosylation site						site	RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%.
3163150	1	38	part_of	kallikrein	122:131	arg1	The amino acid sequence	kallikrein		The amino acid sequence		PUBTATOR	Site	kallikrein	9622	sequence	The amino acid sequence of human urinary kallikrein was determined by protein-chemical methods.
16170054	10	35	gly	N-glycosylation	1821:1835	arg1	tissue-specific glycoproteins	tissue-specific glycoproteins				Fterm		glycoproteins			Lamellar granules are organelles found in the terminally differentiating cells of keratinizing epithelia, and desmosomes are intercellular junctions in vertebrate epithelial cells, thus indicating that N-glycosylation of tissue-specific glycoproteins may contribute to increase the relative proportion of high mannose glycans.
16170054	10	91	gly	glycoproteins	1856:1868	arg1	tissue-specific glycoproteins	tissue-specific glycoproteins				Fterm		glycoproteins			Lamellar granules are organelles found in the terminally differentiating cells of keratinizing epithelia, and desmosomes are intercellular junctions in vertebrate epithelial cells, thus indicating that N-glycosylation of tissue-specific glycoproteins may contribute to increase the relative proportion of high mannose glycans.
12878160	0	33	gly	glycoproteins	78:90	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			VIPL, a VIP36-like membrane protein with a putative function in the export of glycoproteins from the endoplasmic reticulum.
9884403	1	57	part_of	glycoprotein	138:149	arg1	The N-glycosylation sites	Tamm-Horsfall glycoprotein		The N-glycosylation sites		OGER	Site	Tamm-Horsfall glycoprotein	P07911	sites	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
23167757	4	78	gly	glycosylation	723:735	arg2	three predicted N-linked glycosylation sites			three predicted N-linked glycosylation sites						sites	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
16870210	0	41	gly	peptide	39:45	arg1	Structural determinants			peptide	Structural determinants					peptide	Structural determinants of natriuretic peptide receptor specificity and degeneracy.
8702538	4	34	gly	glycosylation	660:672	arg2	N-linked glycosylation sites			N-linked glycosylation sites						sites	These observations suggest that N-linked glycosylation sites on the CD22 molecule may play a role in the regulation of CD22-mediated adhesion.
7774715	4	3	gly	alpha-2,3-monosialylated	599:622	arg1	alpha-2,3-monosialylated (20%) forms				alpha-2,3-monosialylated (20%) forms						The identified structures corresponded to N-acetyllactosaminic biantennary glycans and were alpha-2,3-disialylated forms (80%) or alpha-2,3-monosialylated (20%) forms.
7774715	4	34	gly	alpha-2,3-disialylated	561:582	arg1	alpha-2,3-disialylated forms				alpha-2,3-disialylated forms						The identified structures corresponded to N-acetyllactosaminic biantennary glycans and were alpha-2,3-disialylated forms (80%) or alpha-2,3-monosialylated (20%) forms.
19671700	5	64	gly	containing	908:917	arg1	TSR1 AND a Glc-Fuc disaccharide	TSR1			a Glc-Fuc disaccharide	PUBTATOR		TSR1	55720		Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	5	64	gly	containing	908:917	arg1	TSR1 AND O-fucosylation	TSR1			O-fucosylation	PUBTATOR		TSR1	55720		Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
26536155	4	9	gly	glycopeptides	762:774	arg2	the resulting glycopeptides			the resulting glycopeptides						glycopeptides	While the resulting glycopeptides are very useful for tandem mass spectrometric investigation, the analysis with conventional 1D-LC-ESI-MS/MS approaches can lead to incomplete glycosylation coverage because of the very heterogeneous physicochemical properties of the glycopeptides depending on the peptide sequence as well as the size and charges of the glycan moiety.
26536155	4	63	gly	glycopeptides	1009:1021	arg2	the glycopeptides			the glycopeptides						glycopeptides	While the resulting glycopeptides are very useful for tandem mass spectrometric investigation, the analysis with conventional 1D-LC-ESI-MS/MS approaches can lead to incomplete glycosylation coverage because of the very heterogeneous physicochemical properties of the glycopeptides depending on the peptide sequence as well as the size and charges of the glycan moiety.
28973932	5	22	gly	domains	1215:1221	arg1	O-Man glycosylation			domains	O-Man glycosylation					domains	In addition, O-Man glycosylation of IPT/TIG domains of plexins and hepatocyte growth factor receptor was not affected in TMTC KO cells, suggesting the existence of yet another O-Man glycosylation machinery.
28973932	5	12	gly	glycosylation	1190:1202	arg1	hepatocyte growth factor receptor	hepatocyte growth factor receptor		domains		PUBTATOR		hepatocyte growth factor receptor	4233	domains	In addition, O-Man glycosylation of IPT/TIG domains of plexins and hepatocyte growth factor receptor was not affected in TMTC KO cells, suggesting the existence of yet another O-Man glycosylation machinery.
9884403	2	24	gly	glycosylation	594:606	arg2	the potential glycosylation site			the potential glycosylation site						site	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	24	gly	glycosylation	594:606	arg2	Asn14			Asn14						Asn14	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	80	gly	N-glycosylation	456:470	arg2	the eight potential N-glycosylation sites			the eight potential N-glycosylation sites						sites	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	82	gly	used	661:664	arg2	the potential glycosylation site			the potential glycosylation site						site	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	82	gly	used	661:664	arg2	Asn14			Asn14						Asn14	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn56			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn208			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn372			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn489			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn52			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn251			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn208			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn372			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn489			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn52			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn251			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn372			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn489			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn52			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn251			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn489			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn52			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn251			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn52			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn251			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn251			Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489						Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
8130392	0	109	gly	Asn-linked	6:15	arg1	Novel Asn-linked oligosaccharides			Asn	Novel Asn-linked oligosaccharides					Asn	Novel Asn-linked oligosaccharides terminating in GalNAc beta (1-->4)[Fuc alpha (1-->3)]GlcNAc beta (1-->.)
1991473	5	13	gly	sites	748:752	arg1	N-acetyllactosamine-type structures			sites	N-acetyllactosamine-type structures					sites	N-acetyllactosamine-type structures at all three glycosylation sites.
1991473	5	20	gly	glycosylation	734:746	arg2	all three glycosylation sites			all three glycosylation sites						sites	N-acetyllactosamine-type structures at all three glycosylation sites.
21676880	3	13	gly	N-glycosylation	565:579	arg2	two distinct N-glycosylation sites			two distinct N-glycosylation sites						sites	We show that KCNE1 has two distinct N-glycosylation sites: a typical co-translational site and a consensus site ∼20 residues away that unexpectedly acquires N-glycans after protein synthesis (post-translational).
21676880	3	15	gly	site	615:618	arg1	∼20 residues			∼20 residues						residues	We show that KCNE1 has two distinct N-glycosylation sites: a typical co-translational site and a consensus site ∼20 residues away that unexpectedly acquires N-glycans after protein synthesis (post-translational).
21676880	3	32	gly	sites	581:585	arg1	two distinct N-glycosylation sites			two distinct N-glycosylation sites						sites	We show that KCNE1 has two distinct N-glycosylation sites: a typical co-translational site and a consensus site ∼20 residues away that unexpectedly acquires N-glycans after protein synthesis (post-translational).
21676880	3	13	gly	N-glycosylation	565:579	arg2	a consensus site			site						site	We show that KCNE1 has two distinct N-glycosylation sites: a typical co-translational site and a consensus site ∼20 residues away that unexpectedly acquires N-glycans after protein synthesis (post-translational).
21676880	3	32	gly	sites	581:585	arg1	a consensus site			site						site	We show that KCNE1 has two distinct N-glycosylation sites: a typical co-translational site and a consensus site ∼20 residues away that unexpectedly acquires N-glycans after protein synthesis (post-translational).
2737288	2	13	part_of	containing	176:185	arg1	Two peptides AND the potential N-glycosylation sites	Two peptides		the potential N-glycosylation sites						sites	Two peptides, containing the potential N-glycosylation sites at Asn-86 and Asn-125, were isolated and analyzed by amino acid analysis, sequencing and carbohydrate component analysis.
18533687	8	89	part_of	RXFP1	1330:1334	arg1	the potential N-glycosylation sites	RXFP1		the potential N-glycosylation sites		PUBTATOR	Site	RXFP1	59350	sites	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
16763549	5	25	part_of	NRP1	795:798	arg1	the differential GAG composition	NRP1		the differential GAG composition		OGER	Site	NRP1	O14786	position	Glycosylation increased VEGF binding in both cell types, but the differential GAG composition of NRP1 mediates opposite responsiveness to VEGF in ECs and SMCs.
21327254	0	60	part_of	protein	60:66	arg1	peptides	protein		peptides		Fterm	Site	protein		peptides	Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.
19343721	2	17	gly	hPC	505:507	arg1	complex di- and tri-sialylated structures	hPC			complex di- and tri-sialylated structures	OGER		hPC	P11498		The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	2	17	gly	hPC	505:507	arg1	The N-glycans	hPC			The N-glycans	OGER		hPC	P11498		The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	2	67	gly	tri-sialylated	529:542	arg1	The N-glycans				The N-glycans						The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	2	67	gly	tri-sialylated	529:542	arg1	complex di- and tri-sialylated structures				complex di- and tri-sialylated structures						The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
23001782	4	28	gly	glycans	814:820	arg1	intact hSHBG	hSHBG			glycans	PUBTATOR		hSHBG	6462		MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	91	gly	hSHBG	832:836	arg1	detailed glycan structures	hSHBG			detailed glycan structures	PUBTATOR		hSHBG	6462		MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	91	gly	hSHBG	832:836	arg1	glycans	hSHBG			glycans	PUBTATOR		hSHBG	6462		MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	91	gly	hSHBG	832:836	arg1	monosaccharide compositions	hSHBG			monosaccharide compositions	PUBTATOR		hSHBG	6462		MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	117	gly	structures	766:775	arg1	intact hSHBG	hSHBG			structures	PUBTATOR		hSHBG	6462		MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	124	gly	compositions	736:747	arg1	intact hSHBG	hSHBG			compositions	PUBTATOR		hSHBG	6462		MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	61	gly	glycosylation	670:682	arg1	glycans			sites	glycans					sites	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
19561611	4	3	part_of	HHIP	500:503	arg1	the human HHIP ectodomain	HHIP		the human HHIP ectodomain		PUBTATOR	Site	HHIP	Q96QV1	ectodomain	We have solved a series of crystal structures for the human HHIP ectodomain and Desert hedgehog (DHH) in isolation, as well as HHIP in complex with DHH (HHIP-DHH) and Sonic hedgehog (Shh) (HHIP-Shh), with and without Ca2+.
6546754	4	12	part_of	Bb	546:547	arg1	the Bb fragment	Bb		the Bb fragment		Cterm	Site	Bb		fragment	It is proposed that this region of the Bb fragment functions as a cofactor-binding domain for C3b.
30237853	0	51	gly	glycoprotein	17:28	arg1	Distinct urinary glycoprotein signatures	Distinct urinary glycoprotein signatures				Fterm		glycoprotein			Distinct urinary glycoprotein signatures in prostate cancer patients.
8344278	3	31	gly	A	587:587	arg1	the oligosaccharide moieties	saposin A			the oligosaccharide moieties	Cterm		saposin A			The characteristic features of the oligosaccharide moieties of saposin A are (a) the predominance of a fucosylated trimannosyl core structure and (b) the occurrence of several different oligomannose-type and N-acetyllactosamine-type oligosaccharides.
8344278	3	38	gly	fucosylated	619:629	arg1	a fucosylated trimannosyl core structure				a fucosylated trimannosyl core structure						The characteristic features of the oligosaccharide moieties of saposin A are (a) the predominance of a fucosylated trimannosyl core structure and (b) the occurrence of several different oligomannose-type and N-acetyllactosamine-type oligosaccharides.
8507662	3	15	part_of	cDNA	526:529	arg1	the pro-major basic protein cDNA sequence	cDNA		the pro-major basic protein cDNA sequence		Cterm	Site	cDNA		sequence	We could identify all the peptides which were expected from the pro-major basic protein cDNA sequence.
8507662	3	19	part_of	protein	518:524	arg1	the pro-major basic protein cDNA sequence	protein		the pro-major basic protein cDNA sequence		Fterm	Site	protein		sequence	We could identify all the peptides which were expected from the pro-major basic protein cDNA sequence.
22363519	4	22	gly	Toll-like	582:590	arg1	a model repeat protein	Toll-like receptor4			a model repeat protein	PUBTATOR		Toll-like receptor4	7099		As a model repeat protein, a Toll-like receptor4 (TLR4) decoy receptor composed of leucine-rich repeat (LRR) modules was used, and its interaction interface was rationally engineered to increase the binding affinity for myeloid differentiation protein 2 (MD2).
22363519	4	35	gly	leucine-rich	636:647	arg1	LRR			leucine	LRR					leucine	As a model repeat protein, a Toll-like receptor4 (TLR4) decoy receptor composed of leucine-rich repeat (LRR) modules was used, and its interaction interface was rationally engineered to increase the binding affinity for myeloid differentiation protein 2 (MD2).
22363519	4	35	gly	leucine-rich	636:647	arg1	leucine-rich repeat			leucine	leucine-rich repeat					leucine	As a model repeat protein, a Toll-like receptor4 (TLR4) decoy receptor composed of leucine-rich repeat (LRR) modules was used, and its interaction interface was rationally engineered to increase the binding affinity for myeloid differentiation protein 2 (MD2).
22363519	4	71	gly	TLR4	603:606	arg1	a model repeat protein	TLR4			a model repeat protein	PUBTATOR		TLR4	7099		As a model repeat protein, a Toll-like receptor4 (TLR4) decoy receptor composed of leucine-rich repeat (LRR) modules was used, and its interaction interface was rationally engineered to increase the binding affinity for myeloid differentiation protein 2 (MD2).
22363519	4	80	gly	receptor4	592:600	arg1	a model repeat protein	Toll-like receptor4			a model repeat protein	PUBTATOR		Toll-like receptor4	7099		As a model repeat protein, a Toll-like receptor4 (TLR4) decoy receptor composed of leucine-rich repeat (LRR) modules was used, and its interaction interface was rationally engineered to increase the binding affinity for myeloid differentiation protein 2 (MD2).
18340083	5	15	gly	released	619:626	arg1	mouse GPIHBP1 AND The N-linked glycan	mouse GPIHBP1			The N-linked glycan	PUBTATOR		GPIHBP1	68453		The N-linked glycan could be released from mouse GPIHBP1 with N-glycosidase F, endoglycosidase H, or endoglycosidase F1.
21949356	9	74	part_of	motif	1285:1289	arg1	the consensus sequence	motif		the consensus sequence						sequence	EGF16 of mouse Notch2, which has a diserine motif in the consensus sequence ( ), is also modified with either O-Xyl or O-glucose glycans in cells.
18061361	8	7	gly	N-glycosylated	1452:1465	arg1	nearly all NCBE	nearly all NCBE				PUBTATOR		NCBE	94229		By Western blot, nearly all NCBE in mouse and rat brain is highly N-glycosylated (approximately 150 kDa).
8349699	8	88	gly	N-glycosylated	1120:1133	arg1	This site			site						site	This site is N-glycosylated in about 50% of PGH synthase-2 molecules, resulting in two peptide bands on SDS-polyacrylamide gel electrophoresis (72 and 74 kDa).
9153399	8	45	part_of	ICAM-2	1268:1273	arg1	domains 1 and 2	ICAM-2		domains 1 and 2		PUBTATOR	Site	ICAM-2	3384	domains	A bend between domains 1 and 2 of ICAM-2 and a tripod-like arrangement of N-linked glycans in the membrane-proximal region of domain 2 may be important for presenting the recognition surface to LFA-1.
9153399	8	57	part_of	domains	1249:1255	arg1	the membrane-proximal region	domains		the membrane-proximal region						region	A bend between domains 1 and 2 of ICAM-2 and a tripod-like arrangement of N-linked glycans in the membrane-proximal region of domain 2 may be important for presenting the recognition surface to LFA-1.
19671700	5	47	part_of	punctin-1	838:846	arg1	tryptic fragments	punctin-1		tryptic fragments		PUBTATOR	Site	punctin-1	92949	fragments	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	5	64	part_of	containing	908:917	arg1	TSR1 AND the (36)WDAWGPWSECSRTC(49) sequence	TSR1		the (36)WDAWGPWSECSRTC(49) sequence	O-fucosylation	PUBTATOR	Site	TSR1	55720	sequence	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
17293352	9	37	gly	glycoprotein	1523:1534	arg1	The recombinant rabbit glycoprotein	The recombinant rabbit glycoprotein				Fterm		glycoprotein			The recombinant rabbit glycoprotein contained a broad array of different N-glycans, comprising oligomannose-, hybrid-, and complex-type structures.
6177036	0	18	gly	glycoprotein	20:31	arg1	Neuronal cell Thy-1 glycoprotein	Neuronal cell Thy-1 glycoprotein				PUBTATOR		Thy-1 glycoprotein	21838		Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin.
7688323	4	42	gly	O-glycosylation	747:761	arg2	Ser847			Ser847						Ser847	Ser847 was identified as the O-glycosylation site.
7688323	4	42	gly	O-glycosylation	747:761	arg2	the O-glycosylation site			the O-glycosylation site						site	Ser847 was identified as the O-glycosylation site.
21712440	2	28	gly	glycopeptides	513:525	arg2	released APP/Aβ glycopeptides			released APP/Aβ glycopeptides						glycopeptides	Although APP is a well-known membrane glycoprotein carrying both N- and O-glycans, nothing is known about the occurrence of released APP/Aβ glycopeptides in cerebrospinal fluid (CSF).
21712440	2	49	gly	glycoprotein	411:422	arg1	a well-known membrane glycoprotein	a well-known membrane glycoprotein				Fterm		glycoprotein			Although APP is a well-known membrane glycoprotein carrying both N- and O-glycans, nothing is known about the occurrence of released APP/Aβ glycopeptides in cerebrospinal fluid (CSF).
21712440	2	49	gly	glycoprotein	411:422	arg1	APP	APP				OGER		APP	P05067		Although APP is a well-known membrane glycoprotein carrying both N- and O-glycans, nothing is known about the occurrence of released APP/Aβ glycopeptides in cerebrospinal fluid (CSF).
21712440	2	6	gly	carrying	424:431	arg1	a well-known membrane glycoprotein AND O-glycans	a well-known membrane glycoprotein			O-glycans	Fterm		glycoprotein			Although APP is a well-known membrane glycoprotein carrying both N- and O-glycans, nothing is known about the occurrence of released APP/Aβ glycopeptides in cerebrospinal fluid (CSF).
21712440	2	6	gly	carrying	424:431	arg1	a well-known membrane glycoprotein AND N-	a well-known membrane glycoprotein			N-	Fterm		glycoprotein			Although APP is a well-known membrane glycoprotein carrying both N- and O-glycans, nothing is known about the occurrence of released APP/Aβ glycopeptides in cerebrospinal fluid (CSF).
21712440	2	6	gly	carrying	424:431	arg1	APP AND O-glycans	APP			O-glycans	OGER		APP	P05067		Although APP is a well-known membrane glycoprotein carrying both N- and O-glycans, nothing is known about the occurrence of released APP/Aβ glycopeptides in cerebrospinal fluid (CSF).
21712440	2	6	gly	carrying	424:431	arg1	APP AND N-	APP			N-	OGER		APP	P05067		Although APP is a well-known membrane glycoprotein carrying both N- and O-glycans, nothing is known about the occurrence of released APP/Aβ glycopeptides in cerebrospinal fluid (CSF).
18467335	0	14	gly	inhibitor	42:50	arg1	N-glycans	protein C inhibitor			N-glycans	OGER		protein C inhibitor	P05154		N-glycans and the N terminus of protein C inhibitor affect the cofactor-enhanced rates of thrombin inhibition.
17015441	5	9	gly	glycosylation	717:729	arg2	two potential N-linked glycosylation sites			two potential N-linked glycosylation sites						sites	We identified two potential N-linked glycosylation sites in TRPM8 (Asn-821 and Asn-934) and mutated them to show that only the site in the putative pore region at position 934 is modified and that glycosylation of this site is not absolutely necessary for cell surface expression or responsiveness to icilin, menthol, and cool temperatures.
17015441	5	43	gly	glycosylation	877:889	arg1	this site			this site						site	We identified two potential N-linked glycosylation sites in TRPM8 (Asn-821 and Asn-934) and mutated them to show that only the site in the putative pore region at position 934 is modified and that glycosylation of this site is not absolutely necessary for cell surface expression or responsiveness to icilin, menthol, and cool temperatures.
17015441	5	24	gly	identified	683:692	arg1	Asn-821			Asn-821 and Asn-934						Asn-821 and Asn-934	We identified two potential N-linked glycosylation sites in TRPM8 (Asn-821 and Asn-934) and mutated them to show that only the site in the putative pore region at position 934 is modified and that glycosylation of this site is not absolutely necessary for cell surface expression or responsiveness to icilin, menthol, and cool temperatures.
3886654	4	24	part_of	XII	554:556	arg1	the complete amino acid sequence	factor XII		the complete amino acid sequence		OGER	Site	factor XII	P00748	sequence	258, 10924-10933), the complete amino acid sequence of human factor XII has been established.
8053566	5	12	part_of	proteins	1026:1033	arg1	Glycopeptides	proteins		Glycopeptides		Fterm	Site	proteins		Glycopeptides	Glycopeptides from well-characterized proteins, fetuin, alpha 1-acid glycoprotein, and tissue plasminogen activator were also analyzed to confirm exoglycosidase specificity for glycopeptides and establish the quantitative significance of the relative intensities of peaks in the mass spectra.
20507882	2	27	gly	glycopeptides	453:465	arg2	tryptic glycopeptides			glycopeptides	alpha-dystroglycan					glycopeptides	By immunoprecipitation and sialic acid capture-and-release enrichment strategies, we isolated tryptic glycopeptides of alpha-dystroglycan from human skeletal muscle.
17711303	6	85	gly	glycosylated	1035:1046	arg1	both residues			both residues						residues	Mutation of Asn25 or Asn39 to Gln in the N-terminal domain reduced the Mr by approximately 5 kDa, indicating that both residues were glycosylated.
26013384	7	35	gly	O-glycopeptides	836:850	arg2	The O-glycopeptides			The O-glycopeptides						O-glycopeptides	The O-glycopeptides were not detected in the fraction of the variant.
22967898	2	4	part_of	contains	226:233	arg1	Cathepsin V AND two predicted N-glycosylation sites	Cathepsin V		two predicted N-glycosylation sites		PUBTATOR	Site	Cathepsin V	1515	sites	Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not.
3497398	6	70	gly	glycoprotein	929:940	arg1	glycoprotein Ib	glycoprotein Ib				Fterm		glycoprotein			This region of glycoprotein Ib is largely hydrophobic and contains only two N-linked and one O-linked carbohydrate chains.
3497398	6	9	gly	contains	972:979	arg1	This region AND only two N-linked and one O-linked carbohydrate chains			This region	only two N-linked and one O-linked carbohydrate chains					region	This region of glycoprotein Ib is largely hydrophobic and contains only two N-linked and one O-linked carbohydrate chains.
15498570	6	60	gly	N-glycosylation	1144:1158	arg1	Asn171			Asn171						Asn171	Furthermore, N-glycosylation of Asn171 was confirmed as potential crucial process for the secretory protein via site-directed mutagenesis assay.
25153361	3	25	part_of	glycoproteins	587:599	arg1	glycopeptides	glycoproteins		glycopeptides		Fterm	Site	glycoproteins		glycopeptides	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
19690161	0	0	gly	glycans	17:23	arg1	Asn-89			Asn-89	Asn-89		SpecificSite			Asn-89	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
24509848	10	68	part_of	motif	1531:1535	arg1	N-glycosylation	t N-glycosylation		motif		PUBTATOR	Site	t N-glycosylation	780	motif	Taken together, these data suggest that N-glycosylation at the highly conserved (211)NDS motif evolved to act as a negative repressor of DDR1 phosphorylation in the absence of ligand.
16679516	10	90	gly	hTg-CS	1570:1575	arg1	the chondroitin 6-sulfate oligosaccharide unit	hTg			the chondroitin 6-sulfate oligosaccharide unit	OGER		hTg	P01266		Furthermore, the chondroitin 6-sulfate oligosaccharide unit of hTg-CS protected peptide bond Lys2714-Gly2715 from proteolysis, during the limited digestion of hTg-CS with trypsin.
24884609	10	23	gly	O-glycoforms	1413:1424	arg1	isoform-specific ITIH4 O-glycoforms	isoform-specific ITIH4 O-glycoforms				PUBTATOR		ITIH4	3700		We also identified isoform-specific ITIH4 O-glycoforms and documented that utilization of O-glycosylation sites on ITIH4 differed between the cell line and serum.
24884609	10	51	gly	O-glycosylation	1461:1475	arg2	O-glycosylation sites			O-glycosylation sites						sites	We also identified isoform-specific ITIH4 O-glycoforms and documented that utilization of O-glycosylation sites on ITIH4 differed between the cell line and serum.
11706042	1	24	gly	multi-protein	141:153	arg1	The lipopolysaccharide (LPS) receptor	multi			The lipopolysaccharide (LPS) receptor	OGER		multi			The lipopolysaccharide (LPS) receptor is a multi-protein complex that consists of at least three proteins, CD14, TLR4, and MD-2.
2049076	10	16	gly	glycopeptides	1515:1527	arg2	glycopeptides			glycopeptides						glycopeptides	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
25765764	5	0	part_of	LRIG1	739:743	arg1	the LRIG1 domains	LRIG1		the LRIG1 domains		PUBTATOR	Site	LRIG1	26018	domains	We could not detect any binding of the LRIG1 domains or the LRIG1-LRR-1Ig fragment to the EGF receptor (EGFR), either in solution using biosensor analysis or when the EGFR was expressed on the cell surface.
25765764	5	44	part_of	LRIG1-LRR-1Ig	760:772	arg1	the LRIG1-LRR-1Ig fragment	LRIG1		the LRIG1-LRR-1Ig fragment		PUBTATOR	Site	LRIG1	26018	fragment	We could not detect any binding of the LRIG1 domains or the LRIG1-LRR-1Ig fragment to the EGF receptor (EGFR), either in solution using biosensor analysis or when the EGFR was expressed on the cell surface.
21241660	0	27	gly	O-glycosylated	16:29	arg1	PANP	PANP				PUBTATOR		PANP	319352		PANP is a novel O-glycosylated PILRα ligand expressed in neural tissues.
8636209	10	29	part_of	gamma	1284:1288	arg1	the entire CY domain	CD3 gamma		the entire CY domain		PUBTATOR	Site	CD3 gamma	917	domain	Deletion of the entire CY domain of CD3 gamma did not prevent assembly and expression of the TCR.
16335952	5	48	gly	deglycosylated	1052:1065	arg1	the deglycosylated peptides			the deglycosylated peptides						peptides	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
4603214	0	1	gly	glycoprotein	35:46	arg1	alpha1-acid glycoprotein	alpha1-acid glycoprotein				Fterm		glycoprotein			The disulfide bonds of alpha1-acid glycoprotein.
19038966	3	66	gly	glycosylated	449:460	arg1	the fully glycosylated TPP1 precursor	the fully glycosylated TPP1 precursor				PUBTATOR		TPP1 precursor	1200		We crystallized the fully glycosylated TPP1 precursor under conditions that implied partial autocatalytic cleavage between the prosegment and the catalytic domain.
21805521	6	61	gly	attached	1142:1149	arg2	two O-linked glycans AND Ser³⁰			Ser³⁰	two O-linked glycans					Ser³⁰	HuDKK1 contains two O-linked glycans, GalNAc (sialic acid)-Gal-sialic acid (65%) and GalNAc-Gal[sialic acid] (30%), attached at Ser³⁰ as confirmed by β-elimination and targeted LC-MS/MS.
21805521	6	61	gly	attached	1142:1149	arg2	GalNAc-Gal[sialic acid] AND Ser³⁰			Ser³⁰	GalNAc-Gal[sialic acid]					Ser³⁰	HuDKK1 contains two O-linked glycans, GalNAc (sialic acid)-Gal-sialic acid (65%) and GalNAc-Gal[sialic acid] (30%), attached at Ser³⁰ as confirmed by β-elimination and targeted LC-MS/MS.
21805521	6	61	gly	attached	1142:1149	arg2	GalNAc (sialic acid)-Gal-sialic acid AND Ser³⁰			Ser³⁰	GalNAc (sialic acid)-Gal-sialic acid					Ser³⁰	HuDKK1 contains two O-linked glycans, GalNAc (sialic acid)-Gal-sialic acid (65%) and GalNAc-Gal[sialic acid] (30%), attached at Ser³⁰ as confirmed by β-elimination and targeted LC-MS/MS.
9334252	0	40	gly	RNase	25:29	arg1	C-Mannosylation	RNase 2			C-Mannosylation	PUBTATOR		RNase 2	6036		C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells.
16201406	1	18	gly	glycoprotein	203:214	arg1	Human lactoferrin	Human lactoferrin				OGER		Human lactoferrin	P02788		Human lactoferrin (hLF) is an iron-binding glycoprotein involved in the host defence against infection and excessive inflammation.
16201406	1	18	gly	glycoprotein	203:214	arg1	an iron-binding glycoprotein	an iron-binding glycoprotein				Fterm		glycoprotein			Human lactoferrin (hLF) is an iron-binding glycoprotein involved in the host defence against infection and excessive inflammation.
7944531	0	37	gly	glycoprotein	23:34	arg1	Carbohydrate deficient glycoprotein syndrome type II				Carbohydrate deficient glycoprotein syndrome type II						Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.
1445902	4	18	part_of	IL-3	732:735	arg1	the reduced tryptic and endopeptidase lysyl-C peptides	IL-3		the reduced tryptic and endopeptidase lysyl-C peptides		PUBTATOR	Site	IL-3	16187	peptides	Liquid secondary ion mass spectrometric analysis was carried out on the reduced tryptic and endopeptidase lysyl-C peptides of glycosylated and deglycosylated IL-3.
16650853	5	6	gly	peptide	1141:1147	arg1	GalNAc-glycosylated peptide substrates				GalNAc-glycosylated peptide substrates						The distance between the catalytic center and the carbohydrate-binding site on the lectin beta sub-domain influences the position of GalNAc glycosylation on GalNAc-glycosylated peptide substrates.
16650853	5	14	gly	GalNAc-glycosylated	1121:1139	arg1	GalNAc-glycosylated peptide substrates				GalNAc-glycosylated peptide substrates						The distance between the catalytic center and the carbohydrate-binding site on the lectin beta sub-domain influences the position of GalNAc glycosylation on GalNAc-glycosylated peptide substrates.
16650853	5	47	gly	site	1035:1038	arg1	the lectin beta sub-domain			the lectin beta sub-domain	the lectin beta sub-domain		Site			sub-domain	The distance between the catalytic center and the carbohydrate-binding site on the lectin beta sub-domain influences the position of GalNAc glycosylation on GalNAc-glycosylated peptide substrates.
16650853	5	49	gly	position	1085:1092	arg1	GalNAc-glycosylated peptide substrates			position	GalNAc-glycosylated peptide substrates					position	The distance between the catalytic center and the carbohydrate-binding site on the lectin beta sub-domain influences the position of GalNAc glycosylation on GalNAc-glycosylated peptide substrates.
18340083	4	33	gly	glycosylated	576:587	arg1	Human GPIHBP1	Human GPIHBP1				PUBTATOR		Human GPIHBP1	338328		Human GPIHBP1 is also glycosylated.
7107587	12	15	gly	fibrinogen	1334:1343	arg1	greater than 95% biantennary oligosaccharide chains	fibrinogen			greater than 95% biantennary oligosaccharide chains	PUBTATOR		fibrinogen	2244		Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	12	40	gly	glycopeptides	1252:1264	arg2	the glycopeptides			the glycopeptides						glycopeptides	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	12	67	gly	glycopeptides	1315:1327	arg2	the glycopeptides	fibrinogen		glycopeptides		PUBTATOR		fibrinogen	2244	glycopeptides	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
8670172	3	11	part_of	CD59	578:581	arg1	the detailed structural composition	CD59		the detailed structural composition		PUBTATOR	Site	CD59	966	position	We have investigated the detailed structural composition of the naturally occurring soluble urinary CD59 (CD59u) using peptide mapping, anion-exchange chromatography, sequential exoglycosidase digestion and matrix-assisted laser-desorption mass spectrometry (MALDI-MS).
12603841	1	46	gly	N-glycosylation	174:188	arg2	two conserved N-glycosylation sites			two conserved N-glycosylation sites						sites	The ligand-binding domains of AMPA receptor subunits carry two conserved N-glycosylation sites.
2498325	1	25	gly	threonine	77:85	arg1	The carbohydrate attachment site			threonine 194	The carbohydrate attachment site					threonine 194	The carbohydrate attachment site is threonine 194.
8702840	7	36	part_of	NF-M	1099:1102	arg1	Ser48	NF-M		Ser48		PUBTATOR	AminoAcid	NF-M	4741	Ser34 and Ser48	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	47	part_of	NF-L	1127:1130	arg1	Ser48	NF-L		Ser48		PUBTATOR	AminoAcid	NF-L	4747	Ser34 and Ser48	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	53	part_of	sites	1038:1042	arg1	NF-L	NF-L		sites		PUBTATOR	Site	NF-L	4747	sites	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	53	part_of	sites	1038:1042	arg1	NF-M	NF-M		sites		PUBTATOR	Site	NF-M	4741	sites	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	36	part_of	NF-M	1099:1102	arg1	Thr19	NF-M		Thr19 and Ser34		PUBTATOR	AminoAcid	NF-M	4741	Thr19 and Ser34	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	47	part_of	NF-L	1127:1130	arg1	Thr19	NF-L		Thr19 and Ser34		PUBTATOR	AminoAcid	NF-L	4747	Thr19 and Ser34	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
17956937	8	8	gly	site	1856:1859	arg1	a complexed form			site	a complexed form					site	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	8	37	gly	attached	1824:1831	arg1	the N-glycosylation site AND oligosaccharides	PSA		site	oligosaccharides	PUBTATOR		PSA	354	site	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	8	104	gly	N-glycosylation	1840:1854	arg1	PSA	PSA		site		PUBTATOR		PSA	354	site	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
3934016	4	16	gly	N-Glycosylation	778:792	arg1	secreted angiotensinogen	secreted angiotensinogen				PUBTATOR		angiotensinogen	183		N-Glycosylation of secreted angiotensinogen was inhibited using tunicamycin.
24509848	5	54	part_of	residue	680:686	arg1	N-glycosylation	t N-glycosylation		residue		PUBTATOR	SpecificSite	t N-glycosylation	780	Asn(211) residue	Here, we report that N-glycosylation at the Asn(211) residue plays a unique role in the control of DDR1 dimerization and autophosphorylation.
25419660	5	39	part_of	LH3	968:970	arg1	the amino-terminal fragment	LH3		the amino-terminal fragment		PUBTATOR	Site	LH3	26433	fragment	The oligomerization could be completely restored with the full length LH3 or the amino-terminal fragment of LH3 that possesses the glycosyltransferase activities.
27161523	2	58	part_of	cadherin	403:410	arg1	their extracellular cadherin (EC) domains	cadherin		their extracellular cadherin (EC) domains		Fterm	Site	cadherin		domains	How Pcdhs bind homophilically through their extracellular cadherin (EC) domains among dozens of highly similar isoforms has not been determined.
1991473	8	21	gly	sialylated	1270:1279	arg1	The oligosaccharides				The oligosaccharides						The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	8	70	gly	Asn78	1248:1252	arg1	The oligosaccharides			Asn78	The oligosaccharides					Asn78	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	8	75	gly	sequence	1326:1333	arg1	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta				the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta						The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
19159218	2	39	gly	N-glycopeptides	363:377	arg2	tryptic N-glycopeptides			tryptic N-glycopeptides						N-glycopeptides	Solid phase extraction of tryptic N-glycopeptides by hydrazide chemistry is becoming a popular protocol for the analysis of N-glycoproteome.
1457969	7	34	gly	glycosylation	1298:1310	arg2	glycosylation site			glycosylation site						site	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	81	gly	sulphated/sialylated	1322:1341	arg1	the sulphated/sialylated diantennary oligosaccharide				the sulphated/sialylated diantennary oligosaccharide						The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
16698036	1	70	gly	Lysosomal	137:145	arg1	Hex A	Lysosomal beta-hexosaminidase A			Hex A	PUBTATOR		Lysosomal beta-hexosaminidase A	3073		Lysosomal beta-hexosaminidase A (Hex A) is essential for the degradation of GM2 gangliosides in the central and peripheral nervous system.
16698036	1	75	gly	beta-hexosaminidase	147:165	arg1	Hex A	Lysosomal beta-hexosaminidase A			Hex A	PUBTATOR		Lysosomal beta-hexosaminidase A	3073		Lysosomal beta-hexosaminidase A (Hex A) is essential for the degradation of GM2 gangliosides in the central and peripheral nervous system.
8687384	0	45	gly	glycosylation	4:16	arg1	Bowes melanoma tissue plasminogen activator	Bowes melanoma tissue plasminogen activator				PUBTATOR		tissue plasminogen activator	P00750		The glycosylation of Bowes melanoma tissue plasminogen activator: lectin mapping, reaction with anti-L2/HNK-1 antibodies and the presence of sulphated/glucuronic acid containing glycans.
18250328	0	44	part_of	cholinesterase-like	39:57	arg1	the extracellular cholinesterase-like domain	cholinesterase		the extracellular cholinesterase-like domain		OGER	Site	cholinesterase	P06276	domain	Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2.
24393138	2	29	gly	glycoproteins	445:457	arg1	intact glycoproteins	intact glycoproteins				Fterm		glycoproteins			We demonstrate that glycan compositions can easily be determined directly by LC-ESI/TOF-MS from intact glycoproteins even with a very complex glycosylation pattern.
16452088	6	56	gly	peptides	933:940	arg1	these O-GlcNAc-modified peptides				these O-GlcNAc-modified peptides						65 of these O-GlcNAc-modified peptides were sequenced and belonged to proteins with diverse functions in synaptic transmission.
11676606	8	46	part_of	CD154	1220:1224	arg1	asparagine 240	CD154		asparagine 240		PUBTATOR	SpecificSite	CD154	959	asparagine 240	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
7620335	2	21	part_of	factor	471:476	arg1	the XAP region	factor X		the XAP region		OGER	Site	factor X	P00742	region	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	2	85	part_of	X.	478:479	arg1	X. Four glycopeptides	factor X		X. Four glycopeptides		OGER	Site	factor X	P00742	glycopeptides	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7505568	3	2	gly	glycopeptides	294:306	arg2	human MAG glycopeptides			human MAG glycopeptides						glycopeptides	In this study, human MAG glycopeptides were isolated and sequenced.
2110822	4	114	gly	SAP-1	878:882	arg1	Sugar chains	SAP-1			Sugar chains	PUBTATOR		SAP-1	5660		Sugar chains of SAP-1 purified from normal human liver and from GM1 gangliosidosis (type 1) liver were different from each other, although both of them were derived from complex-type sugar chains.
24161696	1	60	gly	glycoproteins	195:207	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			BACKGROUND: Vacancy of occupied N-glycosylation sites of glycoproteins is quite disruptive to a multicellular organism, as underlined by congenital disorders of glycosylation.
24161696	1	3	gly	N-glycosylation	170:184	arg2	occupied N-glycosylation sites	glycoproteins		sites		Fterm		glycoproteins		sites	BACKGROUND: Vacancy of occupied N-glycosylation sites of glycoproteins is quite disruptive to a multicellular organism, as underlined by congenital disorders of glycosylation.
22660477	0	14	part_of	GBR2	91:94	arg1	the extracellular domain	GBR2		the extracellular domain		Cterm	Site	GBR2		domain	Structure and functional interaction of the extracellular domain of human GABA(B) receptor GBR2.
7613477	7	58	gly	glycosylation	1594:1606	arg2	potential N-linked glycosylation sites			potential N-linked glycosylation sites						sites	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	7	98	gly	glycopeptides	1478:1490	arg2	The three additional glycopeptides			The three additional glycopeptides						glycopeptides	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
16474139	10	96	gly	O-glycosylation	1655:1669	arg1	the 3a protein	the 3a protein				Fterm		protein			O-glycosylation of the 3a protein was indeed confirmed using an in situ O-glycosylation assay of endoplasmic reticulum-retained mutants.
26271046	9	24	gly	epitope	1638:1644	arg1	the HNK-1 epitope				the HNK-1 epitope						Moreover, we found that N413 was the main potential site of the HNK-1 epitope that promoted the interaction of GluA2 with N-cadherin, resulting in enhanced cell surface expression of GluA2.
16766521	3	70	part_of	receptor	557:564	arg1	the putative signal peptide	receptor		the putative signal peptide		Fterm	Site	receptor		peptide	Here, we have assessed the functional significance of the putative signal peptide of the CRF(2(a)) receptor and show that it is surprisingly completely incapable of mediating endoplasmic reticulum targeting, despite meeting all sequence criteria for a functional signal by prediction algorithms.
1445902	4	42	gly	deglycosylated	717:730	arg1	glycosylated and deglycosylated IL-3	glycosylated and deglycosylated IL-3				PUBTATOR		IL-3	16187		Liquid secondary ion mass spectrometric analysis was carried out on the reduced tryptic and endopeptidase lysyl-C peptides of glycosylated and deglycosylated IL-3.
1445902	4	66	gly	glycosylated	700:711	arg1	glycosylated and deglycosylated IL-3	glycosylated and deglycosylated IL-3				PUBTATOR		IL-3	16187		Liquid secondary ion mass spectrometric analysis was carried out on the reduced tryptic and endopeptidase lysyl-C peptides of glycosylated and deglycosylated IL-3.
16046623	6	0	gly	glycosylated	1020:1031	arg1	the predicted sites	protein		sites		Fterm		protein		sites	Moreover, mutagenesis analysis showed that all of the predicted sites were glycosylated in the protein used for crystallization.
16046623	6	0	gly	glycosylated	1020:1031	arg2	the predicted sites	protein		sites		Fterm		protein		sites	Moreover, mutagenesis analysis showed that all of the predicted sites were glycosylated in the protein used for crystallization.
16046623	6	0	gly	glycosylated	1020:1031	arg2	the predicted sites			sites						sites	Moreover, mutagenesis analysis showed that all of the predicted sites were glycosylated in the protein used for crystallization.
10441114	14	48	part_of	collagen	1976:1983	arg1	collagen XVIII- and XV-related fragments	collagen XVIII		collagen XVIII- and XV-related fragments		PUBTATOR	Site	collagen XVIII	80781	fragments	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	14	91	part_of	XV-related	1996:2005	arg1	collagen XVIII- and XV-related fragments	XV-related		collagen XVIII- and XV-related fragments		Cterm	Site	XV-related		fragments	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	14	94	part_of	XVIII-	1985:1990	arg1	collagen XVIII- and XV-related fragments	collagen XVIII		collagen XVIII- and XV-related fragments		PUBTATOR	Site	collagen XVIII	80781	fragments	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
1374031	7	10	gly	1-6-fucosylation	1178:1193	arg1	the asparagine-bound GlcNAc				the asparagine-bound GlcNAc						The same holds for the alpha 1-6-fucosylation of the asparagine-bound GlcNAc (95% vs 42%).
1374031	7	103	gly	asparagine-bound	1202:1217	arg1	the asparagine-bound GlcNAc			asparagine	the asparagine-bound GlcNAc					asparagine	The same holds for the alpha 1-6-fucosylation of the asparagine-bound GlcNAc (95% vs 42%).
11904304	0	64	gly	O-glycosylation	26:40	arg1	nucleocytoplasmic proteins	nucleocytoplasmic proteins				Fterm		proteins			Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: alternative glycosylation/phosphorylation of THR-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens.
11150294	1	41	part_of	containing	262:271	arg1	MUPP1 AND 13 PDZ domains	MUPP1		13 PDZ domains		OGER	Site	MUPP1	O55164	domains	By using the yeast two-hybrid system, we previously isolated a cDNA clone encoding a novel member of the multivalent PDZ protein family called MUPP1 containing 13 PDZ domains.
1709161	11	9	part_of	IGFBPs	1334:1339	arg1	10 repetitive domains	IGFBPs		10 repetitive domains		PUBTATOR	Site	IGFBPs	3487	domains	A most intriguing homology exists between the COOH-terminal quarter of the five IGFBPs, 10 repetitive domains of human thyroglobulin, a gastrointestinal tumor-associated antigen, and the invariant chain of the class II histocompatibility antigen.
1709161	11	50	part_of	thyroglobulin	1373:1385	arg1	10 repetitive domains	thyroglobulin, a gastrointestinal tumor-associated antigen		10 repetitive domains		PUBTATOR	Site	thyroglobulin, a gastrointestinal tumor-associated antigen	7038	domains	A most intriguing homology exists between the COOH-terminal quarter of the five IGFBPs, 10 repetitive domains of human thyroglobulin, a gastrointestinal tumor-associated antigen, and the invariant chain of the class II histocompatibility antigen.
21569239	7	19	part_of	F-spondin	939:947	arg1	F-spondin FS domain	F-spondin		F-spondin FS domain		PUBTATOR	Site	F-spondin	10418	domain	The unique feature of F-spondin FS domain is the presence of three disulfide bonds associated with the N- and C-termini of the domain and a highly conserved N-linked glycosylation site.
3264725	1	7	gly	glycoprotein	186:197	arg1	Blood coagulation factor VII	Blood coagulation factor VII				OGER		coagulation factor VII	P08709		Blood coagulation factor VII is a vitamin K dependent glycoprotein which in its activated form, factor VIIa, participates in the coagulation process by activating factor X and/or factor IX in the presence of Ca2+ and tissue factor.
3264725	1	7	gly	glycoprotein	186:197	arg1	a vitamin K dependent glycoprotein	a vitamin K dependent glycoprotein				Fterm		glycoprotein			Blood coagulation factor VII is a vitamin K dependent glycoprotein which in its activated form, factor VIIa, participates in the coagulation process by activating factor X and/or factor IX in the presence of Ca2+ and tissue factor.
17591618	2	16	part_of	containing	340:349	arg1	CFH AND nine potential N-glycosylation sites	CFH		nine potential N-glycosylation sites		PUBTATOR	Site	CFH	P08603	sites	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	2	16	part_of	containing	340:349	arg1	a 155-kDa glycoprotein AND nine potential N-glycosylation sites	a 155-kDa glycoprotein		nine potential N-glycosylation sites		Fterm	Site	glycoprotein		sites	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
20356926	4	36	gly	glycosylation	392:404	arg1	the luminal domain			domain						domain	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	4	36	gly	glycosylation	392:404	arg1	CREB-H	CREB-H		domain		PUBTATOR		CREB-H	84699	domain	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	4	36	gly	glycosylation	392:404	arg1	CREB-H	CREB-H		domain		PUBTATOR		CREB-H	84699	domain	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
8068684	1	99	part_of	contains	181:188	arg1	NHE-1 AND three consensus sites	NHE-1		three consensus sites		PUBTATOR	Site	NHE-1	6548	sites	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
7535613	4	2	part_of	proteins	564:571	arg1	The structurally conserved regions	proteins		The structurally conserved regions		Fterm	Site	proteins		regions	The structurally conserved regions of the 4 reference X-ray proteins provided the core structure of PSA, whereas the loop structures were modeled on the loops of tonin and kallikrein.
10397151	10	55	gly	RIIa	1294:1297	arg1	core mannose oligosaccharide side chains	Fc gamma RIIa			core mannose oligosaccharide side chains	PUBTATOR		Fc gamma RIIa	2212		Electrospray ionisation mass spectrometry (ESMS) indicate that the N-glycans of baculovirus derived Fc gamma RIIa are core mannose oligosaccharide side chains.
10397151	10	55	gly	RIIa	1294:1297	arg1	the N-glycans	Fc gamma RIIa			the N-glycans	PUBTATOR		Fc gamma RIIa	2212		Electrospray ionisation mass spectrometry (ESMS) indicate that the N-glycans of baculovirus derived Fc gamma RIIa are core mannose oligosaccharide side chains.
1885588	7	26	part_of	protein	1306:1312	arg1	a luminally oriented catalytic domain	protein		a luminally oriented catalytic domain		Fterm	Site	protein		domain	These results indicate that glucosidase I is a transmembrane protein with a luminally oriented catalytic domain.
12775711	1	37	gly	glycoprotein	140:151	arg1	The 39-kDa human cartilage glycoprotein	The 39-kDa human cartilage glycoprotein				Fterm		glycoprotein			The 39-kDa human cartilage glycoprotein (HCGP39), a member of a novel family of chitinase-like lectins (Chilectins), is overexpressed in articular chondrocytes and certain cancers.
12775711	1	37	gly	glycoprotein	140:151	arg1	HCGP39	HCGP39				PUBTATOR		HCGP39	1116		The 39-kDa human cartilage glycoprotein (HCGP39), a member of a novel family of chitinase-like lectins (Chilectins), is overexpressed in articular chondrocytes and certain cancers.
2498325	2	37	gly	glycosylation	96:108	arg1	human apolipoprotein (apo) E	human apolipoprotein (apo) E				PUBTATOR		apolipoprotein (apo) E	348		The glycosylation of human apolipoprotein (apo) E was examined with purified plasma apoE and apoE produced by transfected cell lines.
12603841	2	33	gly	sites	337:341	arg1	these sites			these sites						sites	In order to gain insight into the functional role of the corresponding N-glycans, we examined how the elimination of glycosylation at these sites (N407 and N414) affects the ligand-binding characteristics, structural stability, cell-surface expression, and channel properties of homomeric GluR-D (GluR4) receptor and its soluble ligand-binding domain (S1S2).
12603841	2	33	gly	sites	337:341	arg1	N414			N407 and N414						N407 and N414	In order to gain insight into the functional role of the corresponding N-glycans, we examined how the elimination of glycosylation at these sites (N407 and N414) affects the ligand-binding characteristics, structural stability, cell-surface expression, and channel properties of homomeric GluR-D (GluR4) receptor and its soluble ligand-binding domain (S1S2).
23236605	1	10	gly	N-glycosylation	330:344	arg2	three potential N-glycosylation sites			three potential N-glycosylation sites						sites	The mouse macrophage-derived apoptosis inhibitor of macrophage (AIM), which is incorporated into adipocytes and induces lipolysis by suppressing fatty acid synthase (FAS) activity, possesses three potential N-glycosylation sites.
16040958	0	54	gly	glycosylation	9:21	arg2	Asn3			Asn3						Asn3	N-linked glycosylation at Asn3 and the positively charged residues within the amino-terminal domain of the c1 inhibitor are required for interaction of the C1 Inhibitor with Salmonella enterica serovar typhimurium lipopolysaccharide and lipid A.
16740002	7	5	part_of	sites	1067:1071	arg1	the proteins	proteins		sites		Fterm	Site	proteins		sites	In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
17117926	9	29	gly	glycosylation	1189:1201	arg1	Wnt-5a	Wnt-5a				PUBTATOR		Wnt-5a	7474		In contrast, glycosylation was necessary for the secretion of Wnt-5a, but not essential for the actions of Wnt-5a.
6267033	0	10	gly	glycopeptide	81:92	arg2	pro-opiomelanocortin NH2-terminal glycopeptide			pro-opiomelanocortin NH2-terminal glycopeptide						glycopeptide	Primary structure of the major human pituitary pro-opiomelanocortin NH2-terminal glycopeptide.
10731668	3	60	gly	Asn	525:527	arg1	The oligosaccharide structure			Asn(32 )	The oligosaccharide structure					Asn(32 )	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	3	66	gly	fucosylated	591:601	arg1	a core fucosylated biantennary complex-type oligosaccharide				a core fucosylated biantennary complex-type oligosaccharide						The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
24721674	2	48	gly	glycopeptides	395:407	arg2	glycopeptides			glycopeptides						glycopeptides	However, the effective extraction of membrane proteins, the selective isolation of glycopeptides and the mass spectrometric characterization of glycosylation are challenging with current analytical techniques.
25458834	8	59	gly	residue	924:930	arg1	podoplanin	podoplanin			residue	OGER		podoplanin	Q86YL7		Carboxyl groups from the sialic acid residue on podoplanin and from the C terminus of the rhodocytin α subunit interact differently at this "second" binding site on CLEC-2.
9376680	3	45	gly	sequence	600:607	arg1	the new carbohydrate sequence Gal(alpha1-3)GalNAc(alpha1-3)[Fuc(alpha1-2)]Gal				the new carbohydrate sequence Gal(alpha1-3)GalNAc(alpha1-3)[Fuc(alpha1-2)]Gal						The main characteristics of the species Bufo bufo consists in the presence of the new carbohydrate sequence Gal(alpha1-3)GalNAc(alpha1-3)[Fuc(alpha1-2)]Gal, in which a blood group A determinant is substituted with an external alpha1-3 linked galactose unit.
20507882	3	24	gly	glycopeptides	595:607	arg2	glycopeptides			glycopeptides						glycopeptides	Nano-liquid chromatography tandem mass spectrometry was used to identify both glycopeptides and peptides corresponding to the mucin-like and C-terminal domain of alpha-dystroglycan.
21983541	1	45	gly	leucine-rich	184:195	arg1	three cell surface leucine-rich repeat (LRR) proteins			leucine	three cell surface leucine-rich repeat (LRR) proteins					leucine	AMIGO-1 is the parent member of a novel family of three cell surface leucine-rich repeat (LRR) proteins.
12604466	8	42	gly	glycosylated	1195:1206	arg1	N592			N592						N592	However, N592 (on the same loop) is glycosylated when the other two sites are mutated.
19951703	6	9	gly	unglycosylated	826:839	arg1	unglycosylated UGT1A9	unglycosylated UGT1A9				PUBTATOR		UGT1A9	54600		To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin.
19951703	6	42	gly	glycosylation	776:788	arg1	the enzyme activity	the enzyme activity				Fterm		enzyme			To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin.
16170054	7	110	part_of	glycoproteins	1122:1134	arg1	19 N-glycosylation sites	glycoproteins		19 N-glycosylation sites		Fterm	Site	glycoproteins		sites	We identified 15 glycoproteins with 19 N-glycosylation sites that carry high mannose type glycans by off-line LC-MALDI-TOF/TOF mass spectrometry.
20813955	3	12	part_of	JAML	488:491	arg1	JAML ectodomain	JAML		JAML ectodomain		PUBTATOR	Site	JAML	120425	ectodomain	Crystal structures of JAML ectodomain (2.2 angstroms) and its complex with CAR (2.8 angstroms) reveal an unusual immunoglobulin-domain assembly for JAML and a charged interface that confers high specificity.
27966990	0	44	gly	N-Glycosylation	14:28	arg1	Endothelial Cell Receptor Tyrosine Kinase VEGFR-2	Endothelial Cell Receptor Tyrosine Kinase VEGFR-2				OGER		VEGFR-2	P35968		Site-Specific N-Glycosylation of Endothelial Cell Receptor Tyrosine Kinase VEGFR-2.
6118137	13	35	gly	glycoprotein	1324:1335	arg1	the Thy-1 glycoprotein	the Thy-1 glycoprotein				PUBTATOR		Thy-1 glycoprotein	24832		The sequence of the Thy-1 glycoprotein showed homologies with immunoglobulin domains.
12063277	5	10	gly	glycosylation	746:758	arg1	functional HERG channels	functional HERG channels				PUBTATOR		HERG channels	3757		Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
22451694	6	46	part_of	fibronectin	1084:1094	arg1	the auxiliary synergy site	fibronectin		the auxiliary synergy site		PUBTATOR	Site	fibronectin	2335	site	The structure also enabled the precise prediction of the acceptor residue for the auxiliary synergy site of fibronectin on the α5 subunit, which was experimentally confirmed by mutagenesis and kinetic binding assays.
26563299	5	78	gly	glycopeptides	806:818	arg2	glycopeptides			glycopeptides						glycopeptides	Intact IL-15 and sIL-15Rα and derived glycans and glycopeptides were separately profiled using multiple LC-MS/MS strategies.
7679920	8	52	gly	AFP	1730:1732	arg1	the carbohydrate chains	AFP			the carbohydrate chains	PUBTATOR		AFP	174		These results indicate that the increment in fucosylation and branching to form new antennae is a characteristic feature of the carbohydrate chains of AFP from patients with neoplastic diseases of the liver.
9013598	3	3	gly	glycopeptides	674:686	arg2	the glycopeptides			the glycopeptides						glycopeptides	The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type.
14693913	5	54	gly	O-glycosylation	958:972	arg2	potential O-glycosylation sites			potential O-glycosylation sites						sites	The C-terminal 192 residues of hBSSL contain 16 Pro-rich 11-amino-acid repeats, which include 32 Ser/Thr residues as potential O-glycosylation sites.
14693913	5	54	gly	O-glycosylation	958:972	arg2	32 Ser/Thr residues			32 Ser/Thr residues						residues	The C-terminal 192 residues of hBSSL contain 16 Pro-rich 11-amino-acid repeats, which include 32 Ser/Thr residues as potential O-glycosylation sites.
14693913	5	108	gly	Pro-rich	879:886	arg1	16 Pro-rich 11-amino-acid repeats			Pro	16 Pro-rich 11-amino-acid repeats					Pro	The C-terminal 192 residues of hBSSL contain 16 Pro-rich 11-amino-acid repeats, which include 32 Ser/Thr residues as potential O-glycosylation sites.
14693913	5	2	gly	contain	868:874	arg1	hBSSL AND 16 Pro-rich 11-amino-acid repeats	hBSSL		residues	16 Pro-rich 11-amino-acid repeats	PUBTATOR		hBSSL	1056	residues	The C-terminal 192 residues of hBSSL contain 16 Pro-rich 11-amino-acid repeats, which include 32 Ser/Thr residues as potential O-glycosylation sites.
18930737	1	26	gly	alpha2-glycoprotein	218:236	arg1	zinc alpha2-glycoprotein	zinc alpha2-glycoprotein				PUBTATOR		zinc alpha2-glycoprotein	563		This is the first report on the formation of a complex between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP).
18930737	1	26	gly	alpha2-glycoprotein	218:236	arg1	ZAG	ZAG				PUBTATOR		ZAG	563		This is the first report on the formation of a complex between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP).
6327299	1	62	gly	glycoprotein	141:152	arg1	glycoprotein Ib	glycoprotein Ib				Fterm		glycoprotein			Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
19139490	1	18	gly	fucosylation	94:105	arg1	some glycoproteins	some glycoproteins				Fterm		glycoproteins			Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	1	71	gly	glycoproteins	129:141	arg1	Core fucosylation (CF) patterns	glycoproteins			Core fucosylation (CF) patterns	Fterm		glycoproteins			Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
12171601	1	4	gly	glycosylation	150:162	arg1	human proteinase-activated receptor-2	human proteinase-activated receptor-2				PUBTATOR		proteinase-activated receptor-2	2150		We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
12171601	1	4	gly	glycosylation	150:162	arg1	hPAR(2)	hPAR(2)				PUBTATOR		hPAR(2)	2150		We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
17715132	0	15	part_of	contain	19:25	arg1	Pannexin1 channels AND a glycosylation site	Pannexin1 channels		a glycosylation site		PUBTATOR	Site	Pannexin1 channels	24145	site	Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane.
19413349	3	43	gly	glycosylated	421:432	arg1	melanopsin	melanopsin				PUBTATOR		melanopsin	192223		To investigate if melanopsin is N-linked glycosylated and whether N-bound glycans influence the response of melanopsin to light as evidenced by Fos mRNA induction, we transfected PC12 cells to stably express rat wild-type melanopsin or mutant melanopsin lacking both N-linked glycosylation sites.
19413349	3	47	gly	glycosylation	656:668	arg2	both N-linked glycosylation sites			both N-linked glycosylation sites						sites	To investigate if melanopsin is N-linked glycosylated and whether N-bound glycans influence the response of melanopsin to light as evidenced by Fos mRNA induction, we transfected PC12 cells to stably express rat wild-type melanopsin or mutant melanopsin lacking both N-linked glycosylation sites.
11180632	6	25	gly	protein	1164:1170	arg1	The pentasaccharides	protein			The pentasaccharides	Fterm		protein			The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	6	27	gly	asparagine-linked	1196:1212	arg1	the asparagine-linked complex type			asparagine	the asparagine-linked complex type					asparagine	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
3356193	10	6	gly	plasminogens	1372:1383	arg1	the carbohydrate moiety	plasminogens			the carbohydrate moiety	Fterm		plasminogens			This study on the carbohydrate moiety of these three plasminogens reveals species specificity in terms of various types of microheterogeneities.
16467855	6	31	gly	enzyme	1005:1010	arg1	the carbohydrate moieties	enzyme			the carbohydrate moieties	Fterm		enzyme			One of the carbohydrate moieties of the enzyme is essential for homodimer formation of GCPII.
30659065	10	66	part_of	containing	1731:1740	arg1	an unmodified peptide AND a proline residue	an unmodified peptide		a proline residue						proline residue at position 93	In digests of the sera from a subset of donors, we detected an unmodified peptide containing a proline residue at position 93; this substitution would strongly disfavor N-glycosylation at N92.
20837471	6	39	gly	glycosylated	1054:1065	arg1	potential sites			potential sites						sites	Screening of a panel of proteins known to affect lipid metabolism for potential sites glycosylated by GalNAc-T2 led to identification of Thr(226) adjacent to the proprotein convertase processing site in ANGPTL3.
20837471	6	43	gly	Thr	1105:1107	arg1	adjacent to the proprotein convertase processing site			adjacent to the proprotein convertase processing site						site	Screening of a panel of proteins known to affect lipid metabolism for potential sites glycosylated by GalNAc-T2 led to identification of Thr(226) adjacent to the proprotein convertase processing site in ANGPTL3.
21550978	7	37	gly	glycosylation	1357:1369	arg2	these N-linked glycosylation sequons			these N-linked glycosylation sequons							Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg2	Asn(250)	receptor		Asn(250)		Fterm		receptor		Asn(250)	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg1	receptor stability	receptor				Fterm		receptor			Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg1	Asn(250)	receptor		Asn(250)		Fterm		receptor		Asn(250)	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg1	receptor stability	receptor		Asn(250)		Fterm		receptor		Asn(250)	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg1	Asn(250)			Asn(250)						Asn(250)	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg1	Asn(250)	receptor		Asn(250)		Fterm		receptor		Asn(250)	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
6619128	6	83	part_of	proteins	767:774	arg1	the hinge region	proteins		the hinge region		Fterm	Site	proteins		region	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
15809306	7	59	part_of	Ala	1037:1039	arg1	FAPalpha	FAPalpha		Ala		PUBTATOR	SpecificSite	FAPalpha	2191	Ala(657)	Ala(657) in FAPalpha, instead of Asp(663) as in DP-PIV, reduces the acidity in this pocket, and this change could explain the lower affinity for N-terminal amines by FAPalpha.
22547800	4	20	gly	channel	791:797	arg1	a leucine-rich repeat (LRR)-containing membrane protein	BK channel			a leucine-rich repeat (LRR)-containing membrane protein	OGER		BK channel			We recently identified a leucine-rich repeat (LRR)-containing membrane protein, LRRC26, as a BK channel auxiliary subunit, which causes an unprecedented large negative shift (∼140 mV) in voltage dependence of channel activation.
22547800	4	23	gly	BK	788:789	arg1	a leucine-rich repeat (LRR)-containing membrane protein	BK channel			a leucine-rich repeat (LRR)-containing membrane protein	OGER		BK channel			We recently identified a leucine-rich repeat (LRR)-containing membrane protein, LRRC26, as a BK channel auxiliary subunit, which causes an unprecedented large negative shift (∼140 mV) in voltage dependence of channel activation.
22547800	4	55	gly	leucine-rich	720:731	arg1	LRR			leucine	LRR					leucine	We recently identified a leucine-rich repeat (LRR)-containing membrane protein, LRRC26, as a BK channel auxiliary subunit, which causes an unprecedented large negative shift (∼140 mV) in voltage dependence of channel activation.
22547800	4	55	gly	leucine-rich	720:731	arg1	a leucine-rich repeat			leucine	a leucine-rich repeat					leucine	We recently identified a leucine-rich repeat (LRR)-containing membrane protein, LRRC26, as a BK channel auxiliary subunit, which causes an unprecedented large negative shift (∼140 mV) in voltage dependence of channel activation.
11502179	0	19	part_of	receptor	118:125	arg1	a soluble bioactive amino-terminal extracellular domain	thyrotropin receptor		a soluble bioactive amino-terminal extracellular domain		PUBTATOR	Site	thyrotropin receptor	7253	domain	Purification and characterization of a soluble bioactive amino-terminal extracellular domain of the human thyrotropin receptor.
17704566	4	28	part_of	NEP	819:821	arg1	the soluble extracellular domain	NEP		the soluble extracellular domain		PUBTATOR	Site	NEP	4311	domain	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
16740002	5	10	gly	N-glycoproteins	944:958	arg1	45 unique N-glycoproteins	45 unique N-glycoproteins				Fterm		N-glycoproteins			Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
16740002	5	42	gly	N-glycosylated	905:918	arg1	84 formerly N-glycosylated peptides			84 formerly N-glycosylated peptides						peptides	Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
18491227	7	44	part_of	E-cadherin	1216:1225	arg1	cytoplasmic domain	E-cadherin		cytoplasmic domain		PUBTATOR	Site	E-cadherin	999	domain	It was observed that the ration of M4 E-cadherin binding to calnexin was significantly increased compared with that of other variants, suggesting that it was a misfolded protein, though cytoplasmic domain of M4 E-cadherin could associate with beta-catenin.
15677325	1	39	gly	glycosylated	138:149	arg1	the kainate receptor subunit GluR6	subunit GluR6		domain		OGER		subunit GluR6	2898	domain	We report the crystal structure of the glycosylated ligand-binding (S1S2) domain of the kainate receptor subunit GluR6, in complex with the agonist domoate.
22613618	9	80	gly	containing	1376:1385	arg1	membrane proteins AND complex type N-glycans	membrane proteins			complex type N-glycans	Fterm		proteins			The GlcNAc effect appears to apply mainly to membrane proteins containing complex type N-glycans.
21402931	6	28	part_of	ZP	1001:1002	arg1	the ZP region	ZP		the ZP region		Cterm	Site	ZP		region	The EHP region, which was previously thought to be external to the ZP region, is integral to the ZP-C domain and corresponds to the ZP-C G strand.
21402931	6	61	part_of	ZP-C	1031:1034	arg1	the ZP-C domain	ZP		the ZP-C domain		Cterm	Site	ZP		domain	The EHP region, which was previously thought to be external to the ZP region, is integral to the ZP-C domain and corresponds to the ZP-C G strand.
3123586	5	9	part_of	apoC-III	726:733	arg1	the mutant apoC-III polypeptide	apoC-III		the mutant apoC-III polypeptide		PUBTATOR	Site	apoC-III	345	polypeptide	As a result of this amino acid replacement, the mutant apoC-III polypeptide is not glycosylated.
15901639	0	62	gly	glycoprotein	19:30	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Demonstration of a glycoprotein derived from the Ceacam10 gene in mouse seminal vesicle secretions.
24393138	1	2	gly	glycopeptides	227:239	arg2	proteolytic glycopeptides			proteolytic glycopeptides						glycopeptides	Glycans are important modulators of the biological function of proteins and are normally characterized from proteolytic glycopeptides or from (N-)glycans released enzymatically by glycosidase treatment or chemically by hydrazinolysis.
7240157	1	33	gly	monofucosylated	138:152	arg1	a monofucosylated tetra-antennary glycopeptide fraction				a monofucosylated tetra-antennary glycopeptide fraction						Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
7240157	1	60	gly	glycoprotein	223:234	arg1	a monofucosylated tetra-antennary glycopeptide fraction	glycoprotein			a monofucosylated tetra-antennary glycopeptide fraction	Fterm		glycoprotein			Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
3181129	1	3	gly	glycoprotein	192:203	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			The MRC OX-45 cell surface antigen is a glycoprotein of 45,000 apparent mol.
2215480	5	50	part_of	B151-TRF	1080:1087	arg1	secreted B151-TRF polypeptide	TRF		secreted B151-TRF polypeptide		PUBTATOR	Site	TRF	16191	polypeptide	This finding supports the notion that secreted B151-TRF polypeptide consists of 113 amino acids.
8089145	2	34	part_of	contains	408:415	arg1	The larger subunit AND Gly-X-Ser-X-Gly	The larger subunit		Gly-X-Ser-X-Gly		OGER	Site	subunit	313	Gly-X-Ser-X-Gly	The larger subunit contains an amino acid sequence (Gly-X-Ser-X-Gly) that is found at the active sites of many lipases, while the smaller subunit has amino acid sequence similarity to saposins (sphingolipid activator proteins), cofactors for sphingolipid glycohydrolases.
8089145	2	34	part_of	contains	408:415	arg1	The larger subunit AND an amino acid sequence	The larger subunit		an amino acid sequence		OGER	Site	subunit	313	sequence	The larger subunit contains an amino acid sequence (Gly-X-Ser-X-Gly) that is found at the active sites of many lipases, while the smaller subunit has amino acid sequence similarity to saposins (sphingolipid activator proteins), cofactors for sphingolipid glycohydrolases.
17924658	10	80	gly	glycosylation	1926:1938	arg2	the seven N-linked glycosylation sites			the seven N-linked glycosylation sites						sites	Incubation of the enzyme with a mechanism-based inhibitor, enzymatic digest, and mass spectrometric analysis provided the first unambiguous identification of Thr381 as the active site nucleophile of human gamma-glutamyltranspeptidase, and confirmed four of the seven N-linked glycosylation sites.
18642129	6	7	gly	non-fucosylated	976:990	arg1	diantennary, disialylated non-fucosylated (A2S2) glycans				diantennary, disialylated non-fucosylated (A2S2) glycans						A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	6	30	gly	glycoprotein	912:923	arg1	a 50.1 kDa glycoprotein	a 50.1 kDa glycoprotein				Fterm		glycoprotein			A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	6	30	gly	glycoprotein	912:923	arg1	FVII	FVII				OGER		FVII	P08709		A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	6	62	gly	disialylated	963:974	arg1	diantennary, disialylated non-fucosylated (A2S2) glycans				diantennary, disialylated non-fucosylated (A2S2) glycans						A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
2015821	6	13	gly	carries	1264:1270	arg1	alpha 1-antichymotrypsin AND four oligosaccharide side chains	alpha 1-antichymotrypsin			four oligosaccharide side chains	PUBTATOR		alpha 1-antichymotrypsin	12		From these experiments it is concluded that alpha 1-antichymotrypsin carries four oligosaccharide side chains.
14747736	3	23	part_of	NEP	578:580	arg1	the soluble extracellular domain	NEP		the soluble extracellular domain		PUBTATOR	Site	NEP	4311	domain	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
2113054	0	28	gly	glycoprotein	90:101	arg1	CD4 T lymphocyte glycoprotein	CD4 T lymphocyte glycoprotein				Fterm		glycoprotein			High level expression in Chinese hamster ovary cells of soluble forms of CD4 T lymphocyte glycoprotein including glycosylation variants.
25568315	3	64	gly	N-glycosylation	498:512	arg2	the N-glycosylation sites			the N-glycosylation sites						sites	To determine the structural-functional importance of the conserved cysteines and the N-glycosylation sites in NBCe1-A EL-3, we analyzed the potential interplay between EL-3 disulfide bonding and N-glycosylation and their roles in EL-3 topological folding.
16274239	9	6	gly	glycosylation	1753:1765	arg1	N			N(579)						N(579)	Moreover, although WT-EGFRs confer cell survival in 32D cells in the absence of interleukin-3 and EGF, we found that receptors lacking glycosylation at N(579) do not.
15702487	3	26	gly	glycans	544:550	arg1	proteins	proteins			glycans	Fterm		proteins			The subdiscipline of glycomics (or glycoproteomics) is rapidly growing in importance as glycans in proteins have shown to be involved in protein-protein or protein-(drug, virus, antibody) interactions.
1517205	1	28	gly	linked	196:201	arg2	a serine residue AND (Xyl)2-Glc			a serine residue	(Xyl)2-Glc					serine residue	We have recently discovered unusual sugar chains (xylose (Xyl)-glucose (Glc) and (Xyl)2-Glc) linked to a serine residue in the epidermal growth factor (EGF)-like domains of human and bovine clotting factors VII (Ser-52), IX (Ser-53), and protein Z (Ser-53), in addition to bovine platelet glycoprotein thrombospondin.
1517205	1	53	gly	glycoprotein	392:403	arg1	bovine platelet glycoprotein thrombospondin	bovine platelet glycoprotein thrombospondin				Fterm		glycoprotein			We have recently discovered unusual sugar chains (xylose (Xyl)-glucose (Glc) and (Xyl)2-Glc) linked to a serine residue in the epidermal growth factor (EGF)-like domains of human and bovine clotting factors VII (Ser-52), IX (Ser-53), and protein Z (Ser-53), in addition to bovine platelet glycoprotein thrombospondin.
25187573	4	30	gly	O-glycopeptides	818:832	arg2	185 O-glycopeptides			185 O-glycopeptides						O-glycopeptides	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
20450227	5	41	gly	glycosylated	893:904	arg2	N187			N187, N202, N213, N241, and N284						N187, N202, N213, N241, and N284	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N284			N187, N202, N213, N241, and N284						N187, N202, N213, N241, and N284	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N241			N187, N202, N213, N241, and N284						N187, N202, N213, N241, and N284	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N213			N187, N202, N213, N241, and N284						N187, N202, N213, N241, and N284	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N284			N187, N202, N213, N241, and N284						N187, N202, N213, N241, and N284	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N241			N187, N202, N213, N241, and N284						N187, N202, N213, N241, and N284	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N213			N187, N202, N213, N241, and N284						N187, N202, N213, N241, and N284	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N241			N187, N202, N213, N241, and N284						N187, N202, N213, N241, and N284	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N213			N187, N202, N213, N241, and N284						N187, N202, N213, N241, and N284	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N213			N187, N202, N213, N241, and N284						N187, N202, N213, N241, and N284	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
8435067	8	19	gly	glycosylation	1016:1028	arg2	the second glycosylation site			the second glycosylation site						site	However, removal of the second glycosylation site at Asn-233 interferes dramatically with the formation of mature enzyme.
2056274	6	12	gly	glycosylation	1068:1080	arg2	sites			sites						sites	This inserted region is rich in serine and threonine residues that may serve as sites of O-linked glycosylation, and contains a potential site of N-linked glycosylation and a potential site of chondroitin sulphate attachment.
2056274	6	12	gly	glycosylation	1068:1080	arg2	threonine			serine and threonine residues						serine and threonine residues	This inserted region is rich in serine and threonine residues that may serve as sites of O-linked glycosylation, and contains a potential site of N-linked glycosylation and a potential site of chondroitin sulphate attachment.
2056274	6	51	gly	glycosylation	1125:1137	arg2	a potential site			site						site	This inserted region is rich in serine and threonine residues that may serve as sites of O-linked glycosylation, and contains a potential site of N-linked glycosylation and a potential site of chondroitin sulphate attachment.
16847056	1	61	gly	glycoproteins	134:146	arg1	Voltage-gated sodium channels	Voltage-gated sodium channels				Fterm		channels			Voltage-gated sodium channels (Nav) are complex glycoproteins comprised of an alpha subunit and often one to several beta subunits.
16847056	1	61	gly	glycoproteins	134:146	arg1	complex glycoproteins	complex glycoproteins				Fterm		glycoproteins			Voltage-gated sodium channels (Nav) are complex glycoproteins comprised of an alpha subunit and often one to several beta subunits.
27384988	7	41	gly	glycosylation	672:684	arg1	rpS3	rpS3				PUBTATOR		rpS3	6188		N-linked glycosylation of rpS3 was confirmed as necessary for rpS3 secretion into culture media via the ER-Golgi dependent pathway.
24841998	6	77	gly	N-glycopeptides	988:1002	arg2	intact N-glycopeptides			intact N-glycopeptides						N-glycopeptides	Identification was performed on the web-based tool GlycopeptideID, developed for in silico analysis of intact N-glycopeptides.
10029548	0	0	part_of	transferrin	76:86	arg1	the N-lobe	transferrin		the N-lobe		PUBTATOR	Site	transferrin	7018	N-lobe	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
27238017	3	56	gly	glycoprotein	499:510	arg1	the cleaved glycoprotein	the cleaved glycoprotein				Fterm		glycoprotein			Here, we present a 4.4 Å structure of full-length human NPC1 and a low-resolution reconstruction of NPC1 in complex with the cleaved glycoprotein (GPcl) of EBOV, both determined by single-particle electron cryomicroscopy.
11459848	7	13	gly	N-glycans	821:829	arg1	both proteins	proteins			N-glycans	Fterm		proteins			Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	7	13	gly	N-glycans	821:829	arg1	recombinant BSP	BSP			N-glycans	PUBTATOR		BSP	3381		Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	7	60	gly	O-glycans	868:876	arg1	both proteins	proteins			O-glycans	Fterm		proteins			Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	7	60	gly	O-glycans	868:876	arg1	recombinant BSP	BSP			O-glycans	PUBTATOR		BSP	3381		Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
9884403	4	29	gly	contains	876:883	arg1	Glycosylation site Asn489 AND tri-charged oligosaccharides			Glycosylation site Asn489	tri-charged oligosaccharides					Asn489	Glycosylation site Asn489 contains mainly di- and tri-charged oligosaccharides which comprise, among others, the GalNAc4 S (beta1-4)GlcNAc terminal sequence.
9884403	4	29	gly	contains	876:883	arg1	Glycosylation site Asn489 AND di-			Glycosylation site Asn489	di-					Asn489	Glycosylation site Asn489 contains mainly di- and tri-charged oligosaccharides which comprise, among others, the GalNAc4 S (beta1-4)GlcNAc terminal sequence.
11371615	4	2	gly	modified	644:651	arg3	transcription factors AND O-GlcNAc	transcription factors			O-GlcNAc	Fterm		factors			Meanwhile, transcription factors and RNA polymerase II can be modified by O-GlcNAc.
11371615	4	2	gly	modified	644:651	arg3	RNA polymerase II AND O-GlcNAc	RNA polymerase II			O-GlcNAc	OGER		RNA polymerase II			Meanwhile, transcription factors and RNA polymerase II can be modified by O-GlcNAc.
3877053	10	16	part_of	XII	1477:1479	arg1	The carboxyl-terminal region	factor XII		The carboxyl-terminal region		OGER	Site	factor XII	P00748	region	The carboxyl-terminal region of factor XII shares considerable amino acid sequence homology with other serine proteases including trypsin and many clotting factors.
28450392	4	7	part_of	histone	874:880	arg1	histone H4 residues Lys-16, Lys-5, and Lys-8	histone H4		residues Lys-16, Lys-5, and Lys-8		OGER	SpecificSite	histone H4	P62805	residues Lys-16, Lys-5, and Lys-8	Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8.
28450392	4	7	part_of	histone	874:880	arg1	Lys-5	histone H4		residues Lys-16, Lys-5, and Lys-8		OGER	SpecificSite	histone H4	P62805	residues Lys-16, Lys-5, and Lys-8	Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8.
28450392	4	7	part_of	histone	874:880	arg1	Lys-8	histone H4		residues Lys-16, Lys-5, and Lys-8		OGER	SpecificSite	histone H4	P62805	residues Lys-16, Lys-5, and Lys-8	Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8.
28450392	4	7	part_of	histone	874:880	arg1	Lys-5	histone H4		residues Lys-16, Lys-5, and Lys-8		OGER	SpecificSite	histone H4	P62805	residues Lys-16, Lys-5, and Lys-8	Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8.
28450392	4	7	part_of	histone	874:880	arg1	Lys-8	histone H4		residues Lys-16, Lys-5, and Lys-8		OGER	SpecificSite	histone H4	P62805	residues Lys-16, Lys-5, and Lys-8	Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8.
28450392	4	7	part_of	histone	874:880	arg1	Lys-8	histone H4		residues Lys-16, Lys-5, and Lys-8		OGER	SpecificSite	histone H4	P62805	residues Lys-16, Lys-5, and Lys-8	Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8.
28450392	4	57	part_of	H4	882:883	arg1	histone H4 residues Lys-16, Lys-5, and Lys-8	histone H4		residues Lys-16, Lys-5, and Lys-8		OGER	SpecificSite	histone H4	P62805	residues Lys-16, Lys-5, and Lys-8	Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8.
28450392	4	57	part_of	H4	882:883	arg1	Lys-5	histone H4		residues Lys-16, Lys-5, and Lys-8		OGER	SpecificSite	histone H4	P62805	residues Lys-16, Lys-5, and Lys-8	Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8.
28450392	4	57	part_of	H4	882:883	arg1	Lys-8	histone H4		residues Lys-16, Lys-5, and Lys-8		OGER	SpecificSite	histone H4	P62805	residues Lys-16, Lys-5, and Lys-8	Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8.
28450392	4	57	part_of	H4	882:883	arg1	Lys-5	histone H4		residues Lys-16, Lys-5, and Lys-8		OGER	SpecificSite	histone H4	P62805	residues Lys-16, Lys-5, and Lys-8	Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8.
28450392	4	57	part_of	H4	882:883	arg1	Lys-8	histone H4		residues Lys-16, Lys-5, and Lys-8		OGER	SpecificSite	histone H4	P62805	residues Lys-16, Lys-5, and Lys-8	Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8.
28450392	4	57	part_of	H4	882:883	arg1	Lys-8	histone H4		residues Lys-16, Lys-5, and Lys-8		OGER	SpecificSite	histone H4	P62805	residues Lys-16, Lys-5, and Lys-8	Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8.
29741879	8	29	part_of	glycoproteins	1778:1790	arg1	1 731 N-linked glycosites	glycoproteins		1 731 N-linked glycosites		Fterm	Site	glycoproteins		glycosites	Together, 11 292 N-linked glycopeptides corresponding to 1 731 N-linked glycosites from 883 human glycoproteins were identified from the two data sets.
22826440	8	45	gly	Zinc	1653:1656	arg1	the first human O-GlcNAc-6-phosphate modified protein	Zinc finger protein 462			the first human O-GlcNAc-6-phosphate modified protein	PUBTATOR		Zinc finger protein 462	58499		By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	8	85	gly	finger	1658:1663	arg1	the first human O-GlcNAc-6-phosphate modified protein	Zinc finger protein 462			the first human O-GlcNAc-6-phosphate modified protein	PUBTATOR		Zinc finger protein 462	58499		By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
20147294	5	46	part_of	ADGF/ADA2-specific	680:697	arg1	two ADGF/ADA2-specific domains	ADA2		two ADGF/ADA2-specific domains		PUBTATOR	Site	ADA2	51816	domains	In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors.
24417605	10	50	gly	sialylated	1518:1527	arg1	HDL	HDL				OGER		HDL	Q9UNE0		This report describes for the first time a glycomic approach for analyzing HDL, highlighting that HDL are highly sialylated particles.
18308854	8	67	gly	glycosylation	1534:1546	arg2	more than one glycosylation site			more than one glycosylation site						site	Constructs in which more than one glycosylation site were eliminated had reduced transport activity but not necessarily reduced transporter expression.
9933650	11	16	gly	residue	1638:1644	arg1	the N-acetylgalactosamine residue			residue in	the N-acetylgalactosamine residue					residue in	Since IL-1beta did not bind to thyroid-stimulating hormone, which has the sulfate group at C-4 of the N-acetylgalactosamine residue in its N-linked sugar chains, the binding of IL-1beta toward oligosaccharides in fraction AR was considered to be highly specific.
9933650	11	21	gly	residue	1638:1644	arg1	its N-linked sugar chains			residue in	its N-linked sugar chains					residue in	Since IL-1beta did not bind to thyroid-stimulating hormone, which has the sulfate group at C-4 of the N-acetylgalactosamine residue in its N-linked sugar chains, the binding of IL-1beta toward oligosaccharides in fraction AR was considered to be highly specific.
9933650	11	59	gly	chains	1668:1673	arg1	the N-acetylgalactosamine residue			the N-acetylgalactosamine residue	the N-acetylgalactosamine residue		AminoAcid			residue in	Since IL-1beta did not bind to thyroid-stimulating hormone, which has the sulfate group at C-4 of the N-acetylgalactosamine residue in its N-linked sugar chains, the binding of IL-1beta toward oligosaccharides in fraction AR was considered to be highly specific.
9933650	11	2	gly	has	1580:1582	arg1	thyroid-stimulating hormone AND the N-acetylgalactosamine residue	thyroid-stimulating hormone			the N-acetylgalactosamine residue	OGER		thyroid-stimulating hormone			Since IL-1beta did not bind to thyroid-stimulating hormone, which has the sulfate group at C-4 of the N-acetylgalactosamine residue in its N-linked sugar chains, the binding of IL-1beta toward oligosaccharides in fraction AR was considered to be highly specific.
16732286	2	10	part_of	Tie2	273:276	arg1	the Tie2 ligand-binding region	Tie2		the Tie2 ligand-binding region		PUBTATOR	Site	Tie2	7010	region	Here we present the crystal structures of the Tie2 ligand-binding region alone and in complex with Ang2.
18952059	6	29	gly	glycosylation	755:767	arg1	IZUMO	IZUMO				PUBTATOR		IZUMO	73456		These data suggest that glycosylation is not essential for the function of IZUMO, but has a role in protecting it from fragmentation in cauda epididymis.
19656770	3	89	gly	glycoprotein	684:695	arg1	the cell surface N-linked glycoprotein subproteome	the cell surface N-linked glycoprotein subproteome				Fterm		glycoprotein			The cell surface capturing technology was used here to uncover the cell surface N-linked glycoprotein subproteome of myoblasts and to identify potential markers of myoblast differentiation.
10551839	7	22	gly	C-mannosylated	1138:1151	arg1	Trp residues			Trp residues						Trp residues	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
16014566	1	4	gly	glycosylation	169:181	arg1	this platelet-specific receptor	this platelet-specific receptor				Fterm		receptor			Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	11	gly	glycoprotein	109:120	arg1	human glycoprotein VI (GPVI)	human glycoprotein VI (GPVI)				PUBTATOR		glycoprotein VI	51206		Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
3542030	0	75	part_of	protein	47:53	arg1	Amino acid sequence	sex steroid binding protein		Amino acid sequence		PUBTATOR	Site	sex steroid binding protein	6462	sequence	Amino acid sequence of the sex steroid binding protein of human blood plasma.
26859261	5	5	part_of	receptors	1159:1167	arg1	the rigid ligand-binding site	receptors		the rigid ligand-binding site		Fterm	Site	receptors	390243	site	Here, we report the crystal structure of Juno and find that the overall fold is similar to that of FRα and FRβ but with significant flexibility within the area that corresponds to the rigid ligand-binding site of these bona fide folate receptors.
10988252	3	72	gly	glycoprotein	433:444	arg1	a soluble 105 kDa glycoprotein	a soluble 105 kDa glycoprotein				Fterm		glycoprotein			The human epidermoid carcinoma A431 cell line secretes a soluble 105 kDa glycoprotein (sEGFR) that represents the extracellular domain of the membrane-bound form, and its glycosylation pattern has been investigated.
10988252	3	72	gly	glycoprotein	433:444	arg1	sEGFR	sEGFR				PUBTATOR		EGFR	1956		The human epidermoid carcinoma A431 cell line secretes a soluble 105 kDa glycoprotein (sEGFR) that represents the extracellular domain of the membrane-bound form, and its glycosylation pattern has been investigated.
9530955	7	40	gly	epitectin	1191:1199	arg1	The O-linked saccharides	epitectin			The O-linked saccharides	Fterm		epitectin			The O-linked saccharides of epitectin were fractionated by HPLC and analyzed by permethylation and FAB-MS.
18984734	9	61	gly	GlcNAcylation	1261:1273	arg1	individual sites			individual sites						sites	CONCLUSIONS: GlcNAcylation is differentially regulated at individual sites on erythrocyte proteins in response to glycemic status.
17222411	0	0	gly	factor	96:101	arg1	glycan structure	factor			glycan structure	Fterm		factor			Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.
17222411	0	29	gly	glycosylation	11:23	arg1	human podoplanin	human podoplanin				OGER		podoplanin	Q86YL7		Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.
11683872	4	81	gly	N-glycosylation	583:597	arg2	the five potential N-glycosylation sites			the five potential N-glycosylation sites						sites	Of the five potential N-glycosylation sites, the predicted transient receptor potential channel-like transmembrane folding proposes N604 is localized extracellularly.
16274239	0	63	part_of	receptor	78:85	arg1	Asn-579	epidermal growth factor receptor		Asn-579		PUBTATOR	SpecificSite	epidermal growth factor receptor	13649	Asn-579	Functional effects of glycosylation at Asn-579 of the epidermal growth factor receptor.
9136890	9	29	gly	glycopeptide	1024:1035	arg2	The glycopeptide			The glycopeptide						glycopeptide	The glycopeptide containing the site at Asn 317 was obtained after limited tryptic digestion and RP-HPLC.
24884609	9	6	part_of	contained	1294:1302	arg1	recombinant ITIH4 AND Site N274	recombinant ITIH4		Site N274	high-mannose N-linked glycans	PUBTATOR	SpecificSite	ITIH4	3700	N274	Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4.
1421757	0	1	part_of	receptor	75:82	arg1	the O-linked glycosylation site	transferrin receptor		the O-linked glycosylation site		PUBTATOR	Site	transferrin receptor	7037	site	Identification of the O-linked glycosylation site of the human transferrin receptor.
24036510	5	18	gly	analogs	869:875	arg1	the active site			the active site	the active site		Site			site	Unexpectedly, the N-glycan attached to Asn372 interacts with iduronate analogs in the active site and is required for enzymatic activity.
24036510	5	19	gly	attached	825:832	arg1	Asn372 AND the N-glycan			Asn372	the N-glycan					Asn372	Unexpectedly, the N-glycan attached to Asn372 interacts with iduronate analogs in the active site and is required for enzymatic activity.
9677334	12	5	part_of	TPO	1654:1656	arg1	position 110	TPO		position 110		PUBTATOR	Site	TPO	7066	position 110	We also demonstrate that the O-glycosylation site located at position 110 of TPO is not necessary for the bioactivity of the cytokine.
20856818	7	50	gly	glycosylated	1290:1301	arg1	glycosylated lysines			glycosylated lysines						lysines	Otolin is a secreted glycoprotein of ∼70 kDa, with a C-terminal globular domain that is homologous to the immune complement C1q, and contains extensive posttranslational modifications including hydroxylated prolines and glycosylated lysines.
20856818	7	70	gly	glycoprotein	1091:1102	arg1	a secreted glycoprotein	a secreted glycoprotein				Fterm		glycoprotein			Otolin is a secreted glycoprotein of ∼70 kDa, with a C-terminal globular domain that is homologous to the immune complement C1q, and contains extensive posttranslational modifications including hydroxylated prolines and glycosylated lysines.
20856818	7	70	gly	glycoprotein	1091:1102	arg1	Otolin	Otolin				Fterm		Otolin			Otolin is a secreted glycoprotein of ∼70 kDa, with a C-terminal globular domain that is homologous to the immune complement C1q, and contains extensive posttranslational modifications including hydroxylated prolines and glycosylated lysines.
19167329	1	6	gly	glycosylation	124:136	arg1	polypeptides			polypeptides						polypeptides	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST).
1900431	2	49	gly	linked	252:257	arg2	threonine-61 AND The monosaccharide fucose			threonine-61	The monosaccharide fucose					threonine-61	The monosaccharide fucose is glycosidically linked to threonine-61 in the epidermal growth factor region of t-PA.
27599734	3	9	part_of	fibronectin	542:552	arg1	two fibronectin type III domains	fibronectin		two fibronectin type III domains		OGER	Site	fibronectin	P02751	domains	Similar to other class 2 receptors, IFNγR2 has two fibronectin type III domains.
27599734	3	44	part_of	has	534:536	arg1	IFNγR2 AND two fibronectin type III domains	IFNγR2		two fibronectin type III domains		Cterm	Site	2		domains	Similar to other class 2 receptors, IFNγR2 has two fibronectin type III domains.
9405696	0	40	part_of	N-src	43:47	arg1	the SH3 domain	N-src		the SH3 domain		PUBTATOR	Site	N-src	20779	domain	Interactive cloning with the SH3 domain of N-src identifies a new brain specific ion channel protein, with homology to eag and cyclic nucleotide-gated channels.
2513186	5	43	gly	Asn117	862:867	arg1	Asn117 oligomannosidic glycans			Asn117	Asn117 oligomannosidic glycans					Asn117	The results demonstrate that recombinant tPA from C127 cells carries at Asn117 oligomannosidic glycans with 5-8 mannose residues as well as small amounts of hybrid-type species.
12901863	3	10	gly	glycosylated	455:466	arg1	The human ABCC6	The human ABCC6				PUBTATOR		ABCC6	368		The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells.
12901863	3	52	gly	underglycosylated	488:504	arg1	the protein	form of the protein				Fterm		form of the protein			The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells.
7538124	1	2	gly	phosphoglycoproteins	151:170	arg1	Keratin polypeptides 8 and 18 (K8/18)	phosphoglycoproteins		polypeptides		Fterm		phosphoglycoproteins		polypeptides	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
11080501	0	30	part_of	GA733-2	118:124	arg1	N-glycosylation sites	GA733-2		N-glycosylation sites		OGER	Site	GA733-2	P16422	sites	Determination of disulfide bond assignments and N-glycosylation sites of the human gastrointestinal carcinoma antigen GA733-2 (CO17-1A, EGP, KS1-4, KSA, and Ep-CAM).
2015821	4	16	gly	disialylated	904:915	arg1	disialylated triantennary oligosaccharide				disialylated triantennary oligosaccharide						The results indicated the presence of disialyl diantennary and of trisialyl triantennary type glycanic structures, the latter being accompanied by traces of disialylated triantennary oligosaccharide.
15152093	7	57	gly	N-glycosylation	1021:1035	arg2	the predicted N-glycosylation sites			the predicted N-glycosylation sites						sites	Analysis of the predicted N-glycosylation sites also provides evidence that these sites are critical for GCPII carboxypeptidase activity.
2387072	4	27	gly	glycopeptides	966:978	arg2	The glycopeptides			The glycopeptides						glycopeptides	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
4835136	0	8	part_of	subunit	109:115	arg1	the amino acid sequence	subunit		the amino acid sequence		Fterm	Site	subunit		sequence	Human follicle stimulating hormone: first proposal for the amino acid sequence of the hormone-specific, beta subunit (hFSHb).
11439087	8	0	gly	N-glycosylation	1182:1196	arg2	a single N-glycosylation site			a single N-glycosylation site						site	Site-directed mutagenesis was performed to generate sBST-1 mutants (N1-N4), each preserving a single N-glycosylation site.
18585350	3	38	gly	glycoprotein	484:495	arg1	CALHM1	CALHM1				PUBTATOR		CALHM1	255022		We show that CALHM1 encodes a multipass transmembrane glycoprotein that controls cytosolic Ca(2+) concentrations and Abeta levels.
18585350	3	38	gly	glycoprotein	484:495	arg1	a multipass transmembrane glycoprotein	a multipass transmembrane glycoprotein				Fterm		glycoprotein			We show that CALHM1 encodes a multipass transmembrane glycoprotein that controls cytosolic Ca(2+) concentrations and Abeta levels.
16622833	2	52	gly	N-glycosylation	245:259	arg2	The three N-glycosylation sites	A1PI		sites		PUBTATOR		A1PI	5265	sites	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	2	16	gly	contain	275:281	arg1	The three N-glycosylation sites AND diantennary N-glycans but also triantennary and even traces	A1PI		sites	diantennary N-glycans but also triantennary and even traces	PUBTATOR		A1PI	5265	sites	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
25153361	7	24	gly	glycopeptides	1235:1247	arg2	the glycopeptides			the glycopeptides						glycopeptides	The tandem mass spectra exhibited product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation.
12654314	10	69	gly	attached	1652:1659	arg2	individual IgM glycosylation sites AND oligosaccharides			individual IgM glycosylation sites	oligosaccharides					sites	These results indicated great complexity in the structure and composition of oligosaccharides attached to individual IgM glycosylation sites.
12654314	10	72	gly	glycosylation	1679:1691	arg2	individual IgM glycosylation sites			individual IgM glycosylation sites						sites	These results indicated great complexity in the structure and composition of oligosaccharides attached to individual IgM glycosylation sites.
18533687	2	52	gly	leucine-rich	332:343	arg1	leucine-rich repeats			leucine	leucine-rich repeats					leucine	These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site.
18533687	2	27	gly	containing	321:330	arg1	a large extracellular ectodomain AND leucine-rich repeats			a large extracellular ectodomain	leucine-rich repeats					ectodomain	These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site.
26791533	7	4	gly	glycopeptides	971:983	arg2	243 glycopeptides			243 glycopeptides						glycopeptides	We have elucidated glycan compositions and proposed structures for 243 glycopeptides belonging to 73 N-glycosylation sites on 50 glycoproteins.
26791533	7	32	gly	N-glycosylation	1001:1015	arg2	73 N-glycosylation sites			73 N-glycosylation sites						sites	We have elucidated glycan compositions and proposed structures for 243 glycopeptides belonging to 73 N-glycosylation sites on 50 glycoproteins.
26791533	7	56	gly	glycoproteins	1029:1041	arg1	50 glycoproteins	50 glycoproteins				Fterm		glycoproteins			We have elucidated glycan compositions and proposed structures for 243 glycopeptides belonging to 73 N-glycosylation sites on 50 glycoproteins.
3342889	2	23	part_of	contains	211:218	arg1	Cathepsin H AND 230 residues	Cathepsin H		230 residues		PUBTATOR	Site	Cathepsin H	1512	residues	Cathepsin H contains 230 residues and has an Mr of 25116.
1900431	3	34	part_of	contain	460:466	arg1	tryptic and chymotryptic peptides AND this site	tryptic and chymotryptic peptides		this site						site	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
12901863	4	5	gly	glycosylation	585:597	arg2	the major glycosylation site			the major glycosylation site						site	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
2513186	2	34	gly	glycopeptides	363:375	arg2	tryptic glycopeptides			tryptic glycopeptides						glycopeptides	Oligosaccharides present were liberated by treatment of tryptic glycopeptides with endo-beta-N-acetylglucosaminidase H or peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F and fractionated by high-performance liquid chromatography.
3980466	1	20	gly	asparagine-linked	152:168	arg1	asparagine-linked oligosaccharides			asparagine	asparagine-linked oligosaccharides					asparagine	Reproducible site-specific patterns of sialylation and branching in asparagine-linked oligosaccharides.
15173186	6	20	part_of	contain	889:895	arg1	all Toll-like receptors AND N-linked glycosylation consensus sites	all Toll-like receptors		N-linked glycosylation consensus sites		Fterm	Site	receptors		sites	Additionally, all Toll-like receptors contain N-linked glycosylation consensus sites, and Toll-like receptor 4 requires glycosylation for function.
12527193	7	65	part_of	has	992:994	arg1	CRB3 AND a very short extracellular domain	CRB3		a very short extracellular domain		PUBTATOR	Site	CRB3	92359	domain	In contrast to Drosophila Crumbs and CRB1, CRB3 has a very short extracellular domain but like these proteins it has a conserved intracellular domain that allows it to complex with Pals1 and PATJ.
10441114	5	19	gly	O-glycosylated	730:743	arg2	residue 9			residue 9						residue 9	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	5	100	gly	galactose	823:831	arg1	residues			residues						residues	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	5	19	gly	O-glycosylated	730:743	arg2	125			T(125)						T(125)	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
12063277	3	14	gly	glycosylation	408:420	arg1	N598			N598, N629						N598, N629	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
11180632	3	31	gly	released	621:628	arg1	the proteins AND The oligosaccharides	the proteins			The oligosaccharides	Fterm		proteins			The oligosaccharides were enzymatically released from the proteins by treatment with peptidyl-N-glycosidase F and separated from the proteins by reversed-phase high-performance liquid chromatography (HPLC).
1544894	5	18	gly	fucosylated	943:953	arg2	Thr-90	factor XII		Thr-90		OGER		factor XII	P00748	Thr-90	We found that factor XII is fully fucosylated at Thr-90.
7477400	3	24	part_of	CLIP	477:480	arg1	the CLIP fragment	CLIP		the CLIP fragment		PUBTATOR	Site	CLIP	6249	fragment	The structure shows that the CLIP fragment binds to DR3 in a way almost identical to that in which antigenic peptides bind class II histocompatibility glycoproteins.
10537111	3	34	part_of	receptor	614:621	arg1	the principal ligand-binding region	GCSF receptor		the principal ligand-binding region		PUBTATOR	Site	GCSF receptor	1441	region	Here we have determined the crystal structure of GCSF complexed to the BN-BC domains, the principal ligand-binding region of the GCSF receptor (GCSFR).
10537111	3	34	part_of	receptor	614:621	arg1	the BN-BC domains	GCSF receptor		the BN-BC domains		PUBTATOR	Site	GCSF receptor	1441	domains	Here we have determined the crystal structure of GCSF complexed to the BN-BC domains, the principal ligand-binding region of the GCSF receptor (GCSFR).
30659065	11	16	part_of	IgM	1842:1844	arg1	N272	IgM		sites N46, N209, and N272		OGER	SpecificSite	IgM	P01871	sites N46, N209, and N272	IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms.
30659065	11	16	part_of	IgM	1842:1844	arg1	N46	IgM		sites N46, N209, and N272		OGER	SpecificSite	IgM	P01871	sites N46, N209, and N272	IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms.
30659065	11	16	part_of	IgM	1842:1844	arg1	IgM sites	IgM		sites N46, N209, and N272		OGER	SpecificSite	IgM	P01871	sites N46, N209, and N272	IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms.
30659065	11	16	part_of	IgM	1842:1844	arg1	N46	IgM		sites N46, N209, and N272		OGER	SpecificSite	IgM	P01871	sites N46, N209, and N272	IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms.
30659065	11	16	part_of	IgM	1842:1844	arg1	IgM sites	IgM		sites N46, N209, and N272		OGER	SpecificSite	IgM	P01871	sites N46, N209, and N272	IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms.
30659065	11	16	part_of	IgM	1842:1844	arg1	IgM sites	IgM		sites N46, N209, and N272		OGER	SpecificSite	IgM	P01871	sites N46, N209, and N272	IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms.
7841792	6	2	gly	glycopeptide	1089:1100	arg2	a tryptic glycopeptide			a tryptic glycopeptide						glycopeptide	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
7841792	6	62	gly	glycopeptide	1062:1073	arg2	glycopeptide			glycopeptide						glycopeptide	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
7841792	6	68	gly	attached	1134:1141	arg2	Asn494 AND the oligosaccharide			Asn494	the oligosaccharide					Asn494	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
17372356	4	14	part_of	enzyme	882:887	arg1	the S1' site	enzyme		the S1' site		Fterm	Site	enzyme		site	In addition, models were constructed for binding of the inhibitors willardiine, homoibotenate, L-2-amino-4-phosphonobutanoic acid and L-serine-O-sulfate to the S1' site of the enzyme.
20729549	4	65	gly	K8/18	643:647	arg1	O-GlcNAcylation	K8/18			O-GlcNAcylation	PUBTATOR		K8/18	3856		Here, by comparing immortalized (Chang) and transformed hepatocyte (HepG2) cell lines, we have demonstrated that O-GlcNAcylation of K8/18 exhibits a positive correlation with their solubility (Nonidet P-40 extractability).
15476821	2	5	part_of	DPPX	529:532	arg1	the extracellular domain	DPPX		the extracellular domain		PUBTATOR	Site	DPPX	1804	domain	Here we report the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution.
10092871	0	54	gly	metalloproteinase-1	30:48	arg1	N-glycan structures	matrix metalloproteinase-1			N-glycan structures	PUBTATOR		matrix metalloproteinase-1	4312		N-glycan structures of matrix metalloproteinase-1 derived from human fibroblasts and from HT-1080 fibrosarcoma cells.
6776528	9	74	part_of	serine-126	1355:1364	arg1	the 511 alpha chain	chain		serine-126		OGER	SpecificSite	chain		serine-126	The remainder of the 47A constant region, including the hinge region, is identical to the 511 alpha chain, except for two conservative changes in the CH1 domain: serine-126 and theonine-197 in the 511 alpha chain are both replaced by alanine in the 47A chain.
6776528	9	75	part_of	CH1	1343:1345	arg1	the CH1 domain	CH1		the CH1 domain		OGER	Site	CH1	Q9UBS9	domain	The remainder of the 47A constant region, including the hinge region, is identical to the 511 alpha chain, except for two conservative changes in the CH1 domain: serine-126 and theonine-197 in the 511 alpha chain are both replaced by alanine in the 47A chain.
6776528	9	78	part_of	alanine	1427:1433	arg1	the 47A chain	47A chain		alanine		OGER	AminoAcid	47A chain		alanine	The remainder of the 47A constant region, including the hinge region, is identical to the 511 alpha chain, except for two conservative changes in the CH1 domain: serine-126 and theonine-197 in the 511 alpha chain are both replaced by alanine in the 47A chain.
25759508	3	42	part_of	IgG3	425:428	arg1	the IgG3 hinge region	IgG3		the IgG3 hinge region		PUBTATOR	Site	IgG3	P01860	region	This study reports partial O-glycosylation of the IgG3 hinge region, observed with nanoLC-ESI-IT-MS(/MS) analysis after proteolytic digestion.
2136357	3	26	gly	glycoprotein	1033:1044	arg1	Tamm-Horsfall glycoprotein	Tamm-Horsfall glycoprotein				OGER		Tamm-Horsfall glycoprotein	P07911		In this work, we have extended the observation of pregnancy-associated inhibitory activity to a second species, and have compared the oligomannose profile of Tamm-Horsfall glycoprotein (nonpregnant) with that of uromodulin (pregnant) derived from both human and bovine sources.
3356193	8	31	gly	disialylated	1043:1054	arg1	The disialylated form				The disialylated form						The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
20696930	4	48	part_of	HER2	528:531	arg1	the HER2 extracellular domain	HER2		the HER2 extracellular domain		PUBTATOR	Site	HER2	2064	domain	Here we determined the structure of Zher2 in solution and the crystal structure of Zher2 in complex with the HER2 extracellular domain.
12768205	4	11	gly	has	556:558	arg1	Fcalpha AND interdomain N-linked carbohydrates	Fcalpha			interdomain N-linked carbohydrates	Cterm		Fcalpha	P01876		Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
27294781	1	1	part_of	BoNT/A1	305:311	arg1	the BoNT/A1 receptor-binding domain	BoNT/A1		the BoNT/A1 receptor-binding domain		Cterm	Site	BoNT/A1		domain	Here we report a 2.0-Å-resolution crystal structure of the BoNT/A1 receptor-binding domain in complex with its neuronal receptor, glycosylated human SV2C.
27294781	1	3	part_of	receptor-binding	313:328	arg1	the BoNT/A1 receptor-binding domain	receptor		the BoNT/A1 receptor-binding domain		Fterm	Site	receptor		domain	Here we report a 2.0-Å-resolution crystal structure of the BoNT/A1 receptor-binding domain in complex with its neuronal receptor, glycosylated human SV2C.
2110822	1	79	gly	Asparagine-linked	158:174	arg1	Asparagine-linked sugar chains			Asparagine	Asparagine-linked sugar chains					Asparagine	Asparagine-linked sugar chains of sphingolipid activator protein 1 (SAP-1) purified from normal human liver and GM1 gangliosidosis (type 1) liver were comparatively investigated.
2110822	1	89	gly	protein	215:221	arg1	Asparagine-linked sugar chains	activator protein 1			Asparagine-linked sugar chains	PUBTATOR		activator protein 1	5660		Asparagine-linked sugar chains of sphingolipid activator protein 1 (SAP-1) purified from normal human liver and GM1 gangliosidosis (type 1) liver were comparatively investigated.
26791533	10	76	gly	glycoproteins	1365:1377	arg1	multiple seminal plasma glycoproteins	multiple seminal plasma glycoproteins				Fterm		glycoproteins			Many Lewis x/a and y/b epitopes bearing glycans were found, suggesting immune-modulating epitopes on multiple seminal plasma glycoproteins.
18930737	6	45	part_of	PIP	831:833	arg1	The amino acid sequence	PIP		The amino acid sequence		PUBTATOR	Site	PIP	5304	sequence	The amino acid sequence of PIP contains one potential N-glycosylation site at Asn77, and the same is found glycosylated with four sugar residues.
18930737	6	66	part_of	contains	835:842	arg1	The amino acid sequence AND one potential N-glycosylation site	The amino acid sequence		one potential N-glycosylation site						site	The amino acid sequence of PIP contains one potential N-glycosylation site at Asn77, and the same is found glycosylated with four sugar residues.
15536627	6	77	gly	glycopeptides	1621:1633	arg2	the glycopeptides			the glycopeptides						glycopeptides	Moreover, fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc) specifically occurred at Asn630, as demonstrated by treatment of the glycopeptides with alpha1-3/4-L-fucosidase.
15536627	6	22	gly	fucosylation	1487:1498	arg1	Fucalpha1-6GlcNAc			Asn630	Fucalpha1-6GlcNAc					Asn630	Moreover, fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc) specifically occurred at Asn630, as demonstrated by treatment of the glycopeptides with alpha1-3/4-L-fucosidase.
15536627	6	22	gly	fucosylation	1487:1498	arg1	the reducing-terminal GlcNAc			Asn630	the reducing-terminal GlcNAc					Asn630	Moreover, fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc) specifically occurred at Asn630, as demonstrated by treatment of the glycopeptides with alpha1-3/4-L-fucosidase.
21609021	4	66	gly	glycopeptides	820:832	arg2	the IgG glycopeptides			the IgG glycopeptides						glycopeptides	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
24334224	4	49	part_of	found	917:921	arg2	endogenous human G-CSF AND the equivalent O-linked glycosylation site	endogenous human G-CSF		the equivalent O-linked glycosylation site		PUBTATOR	Site	G-CSF	1440	site	Our results demonstrated that Thr134, the equivalent O-linked glycosylation site found on endogenous human G-CSF, is the only site modified with a single mannose, allowing glycoengineered P. pastoris to be used as a viable production platform for therapeutic rhG-CSF.
24334224	4	49	part_of	found	917:921	arg2	endogenous human G-CSF AND Thr134	endogenous human G-CSF		Thr134		PUBTATOR	AminoAcid	G-CSF	1440	Thr134	Our results demonstrated that Thr134, the equivalent O-linked glycosylation site found on endogenous human G-CSF, is the only site modified with a single mannose, allowing glycoengineered P. pastoris to be used as a viable production platform for therapeutic rhG-CSF.
3038148	3	61	part_of	tonin	550:554	arg1	the tonin sequence	tonin		the tonin sequence		PUBTATOR	Site	tonin	24841	sequence	The important Asp residue has now been localized in a 16 amino acid peptide previously reported as missing in the tonin sequence.
26283364	8	10	part_of	SSL3	1084:1087	arg1	The binding site	SSL3		The binding site		Cterm	Site	SSL3	Q12988	site	The binding site of SSL3 overlaps those of TLR2 dimerization partners TLR1 and TLR6 extensively.
8670172	14	8	gly	CD59	1926:1929	arg1	N-linked oligosaccharide	CD59			N-linked oligosaccharide	PUBTATOR		CD59	966		These results document the structural heterogeneity of both the GPI anchor and N-linked oligosaccharide of CD59 and demonstrate that the phospholipid tail is needed for the full functional activity of CD59.
8670172	14	23	gly	heterogeneity	1857:1869	arg1	N-linked oligosaccharide				N-linked oligosaccharide						These results document the structural heterogeneity of both the GPI anchor and N-linked oligosaccharide of CD59 and demonstrate that the phospholipid tail is needed for the full functional activity of CD59.
12218058	6	62	gly	glycosylation	1076:1088	arg2	individual glycosylation sites			individual glycosylation sites						sites	BMP-1 molecules lacking individual glycosylation sites were efficiently secreted and exhibited full procollagen C-proteinase activity, but N332Q and N599Q exhibited a slower rate of cleavage.
23431362	10	69	part_of	gp120	1875:1879	arg1	the N332-region	HIV-1 gp120		the N332-region		PUBTATOR	SpecificSite	HIV-1 gp120	155971	N332	Overall, our results add to the growing body of evidence that the human immune system is capable of recognizing the N332-region of HIV-1 gp120 in diverse ways.
2113054	1	81	part_of	receptor	287:294	arg1	four Ig-like domains	receptor		four Ig-like domains		Fterm	Site	receptor		domains	The CD4 cell surface antigen is of interest as a marker of T lymphocytes that recognize foreign antigens in the context of MHC Class II antigen, as a receptor for the human immunodeficiency virus (HIV) and as a member of the immunoglobulin superfamily (IgSF) with four Ig-like domains present in the extracellular domain.
8323299	3	41	gly	glycoproteins	500:512	arg1	both glycoproteins	both glycoproteins				Fterm		glycoproteins			In both glycoproteins, the O-glycans appear in clusters.
12421832	6	93	part_of	PAPP-A	1034:1039	arg1	cysteine residues	PAPP-A		cysteine residues		PUBTATOR	AminoAcid	PAPP-A	5069	cysteine residues	To establish the connectivities of cysteine residues of the PAPP-A.
16332679	10	28	gly	hyperglycosylation	1617:1634	arg1	Sp1	Sp1				OGER		Sp1	P08047		Treatment of cells with streptozotocin (a potent inhibitor of O-GlcNAcase) led to hyperglycosylation of Sp1 that failed to be significantly phosphorylated.
9265423	0	3	gly	glycoproteins	51:63	arg1	high-mannose-containing glycoproteins				high-mannose-containing glycoproteins						Direct isoform analysis of high-mannose-containing glycoproteins by on-line capillary electrophoresis electrospray mass spectrometry.
2393398	3	47	gly	glycopeptide	455:466	arg2	The glycopeptide			The glycopeptide						glycopeptide	The glycopeptide was isolated by semi-preparative reversed phase high performance liquid chromatography.
20837471	3	25	gly	O-glycosylation	605:619	arg1	the processing site			site						site	We developed an in vivo model system in CHO ldlD cells that was used to show that O-glycosylation in the processing site blocked processing of ANGPTL3.
16362042	5	42	part_of	Gas6	782:785	arg1	the major and minor Gas6 binding sites	Gas6		the major and minor Gas6 binding sites		PUBTATOR	Site	Gas6	2621	sites	Structure-based mutagenesis, protein binding assays and receptor activation experiments demonstrate that both the major and minor Gas6 binding sites are required for productive transmembrane signalling.
20356926	5	17	gly	glycosylation	508:520	arg2	three N-linked glycosylation sites			three N-linked glycosylation sites						sites	We found that CREB-H is modified at three N-linked glycosylation sites in this region.
10091666	5	1	gly	deglycosylated	998:1011	arg1	the glycosylated and deglycosylated wild-type proteins	the glycosylated and deglycosylated wild-type proteins				Fterm		proteins			The kinetic parameters of the glycosylated and deglycosylated wild-type proteins were the same while the k(cat)/Km values for D197A and D197N were 10(6)-10(7) times lower than the wild-type enzyme.
10091666	5	28	gly	glycosylated	981:992	arg1	the glycosylated and deglycosylated wild-type proteins	the glycosylated and deglycosylated wild-type proteins				Fterm		proteins			The kinetic parameters of the glycosylated and deglycosylated wild-type proteins were the same while the k(cat)/Km values for D197A and D197N were 10(6)-10(7) times lower than the wild-type enzyme.
23187000	4	31	part_of	TIMP-1	683:688	arg1	the catalytic domain	TIMP-1		the catalytic domain		PUBTATOR	Site	TIMP-1	7076	domain	The structural analysis of the catalytic domain of human stromelysin-1 (MMP-3) and human TIMP-1 suggests new possibilities of the role of TIMP-1 glycan moieties as a tuner for the proteolytic activities by MMPs.
23187000	4	65	part_of	stromelysin-1	651:663	arg1	the catalytic domain	stromelysin-1		the catalytic domain		PUBTATOR	Site	stromelysin-1	4314	domain	The structural analysis of the catalytic domain of human stromelysin-1 (MMP-3) and human TIMP-1 suggests new possibilities of the role of TIMP-1 glycan moieties as a tuner for the proteolytic activities by MMPs.
20406422	4	66	part_of	CLN7	657:660	arg1	C-terminal domains	CLN7		C-terminal domains		PUBTATOR	Site	CLN7	256471	domains	To identify lysosomal targeting motifs, we generated CD4-chimera fused to the N- and C-terminal domains of CLN7.
27152332	5	12	gly	structure	997:1005	arg1	the two copper-binding sites			the two copper-binding sites						sites	The catalytic core structure shows two different conformations: an open active site, as also seen in another member of this enzyme family [the peptidylglycine α-hydroxylating (and α-amidating) monooxygenase], and a closed active site structure, in which the two copper-binding sites are only 4 to 5 Å apart, in what might be a coupled binuclear copper site.
27152332	5	12	gly	structure	997:1005	arg1	a coupled binuclear copper site			a coupled binuclear copper site						site	The catalytic core structure shows two different conformations: an open active site, as also seen in another member of this enzyme family [the peptidylglycine α-hydroxylating (and α-amidating) monooxygenase], and a closed active site structure, in which the two copper-binding sites are only 4 to 5 Å apart, in what might be a coupled binuclear copper site.
25517345	5	9	part_of	N241	579:582	arg1	gp120	gp120		N241		PUBTATOR	SpecificSite	gp120	3700	N241, N262 and N356	However, interestingly, N241, N262 and N356 on gp120 have never been found to be affected after prolonged CBA exposure.
25517345	5	29	part_of	N262	585:588	arg1	gp120	gp120		N262		PUBTATOR	SpecificSite	gp120	3700	N241, N262 and N356	However, interestingly, N241, N262 and N356 on gp120 have never been found to be affected after prolonged CBA exposure.
25517345	5	35	part_of	N356	594:597	arg1	gp120	gp120		N356		PUBTATOR	SpecificSite	gp120	3700	N241, N262 and N356	However, interestingly, N241, N262 and N356 on gp120 have never been found to be affected after prolonged CBA exposure.
23756651	1	11	gly	leucine-rich	142:153	arg1	leucine-rich repeat-containing G-protein-coupled receptors 4-6			leucine	leucine-rich repeat-containing G-protein-coupled receptors 4-6					leucine	R-spondins (RSPOs) enhance Wnt signaling, affect stem cell behavior, bind to leucine-rich repeat-containing G-protein-coupled receptors 4-6, (LGR4-6) and the transmembrane E3 ubiquitin ligases RING finger 43/zinc and RING finger 3 (RNF43/ZNRF3).
19952283	4	18	part_of	Np55	657:660	arg1	the ectodomain	Np55		the ectodomain		Cterm	Site	Np55		ectodomain	The present study reports for the first time the crystal structure of the ectodomain of Np55 at 1.95-A resolution and demonstrates that Np55 binds to and activates the fibroblast growth factor receptor 1 (FGFR1).
29391424	0	9	gly	glycopeptide	19:30	arg2	Large-scale intact glycopeptide identification			Large-scale intact glycopeptide identification						glycopeptide	Large-scale intact glycopeptide identification by Mascot database search.
19855092	7	18	gly	desialylated	1146:1157	arg1	desialylated adiponectin	desialylated adiponectin				PUBTATOR		adiponectin	11450		Activity of desialylated adiponectin was comparable to control adiponectin in L6 myotubes and acute assays in adiponectin(-/-) mice.
28489325	0	42	part_of	L-Selectin	126:135	arg1	the Lectin and EGF-Like Domains	Human L-Selectin		the Lectin and EGF-Like Domains		PUBTATOR		Human L-Selectin	6402		Reducing Macro- and Microheterogeneity of N-Glycans Enables the Crystal Structure of the Lectin and EGF-Like Domains of Human L-Selectin To Be Solved at 1.9 Å Resolution.
7525874	12	76	gly	glycosylated	1650:1661	arg1	this protein	this protein				OGER		protein can	P35658		According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
6619126	3	156	gly	released	622:629	arg2	the polypeptide AND These saccharides			the polypeptide	These saccharides					polypeptide	These saccharides were released from the polypeptide by beta-elimination in the presence of sodium borohydride, and aspects of their structure were investigated by glycosidase digestion and periodate oxidation.
16456079	3	6	part_of	receptor	497:504	arg1	The three domains	receptor		The three domains		Fterm	Site	receptor		domains	The three domains of urokinase receptor form a concave shape with a central cone-shaped cavity where the urokinase fragment inserts.
1326557	7	123	part_of	protein-like	1749:1760	arg1	a complement regulatory protein-like sequence	protein		a complement regulatory protein-like sequence		Fterm	Site	protein		sequence	The C-terminal portion (amino acids 951-1215) has approximately 60% identity to regions in the C termini of the fibroblast and cartilage proteoglycans, versican and aggrecan, including two epidermal growth factor-like domains, a lectin-like domain, and a complement regulatory protein-like sequence.
1326557	7	158	part_of	regions	1552:1558	arg1	the C termini	regions		the C termini						termini	The C-terminal portion (amino acids 951-1215) has approximately 60% identity to regions in the C termini of the fibroblast and cartilage proteoglycans, versican and aggrecan, including two epidermal growth factor-like domains, a lectin-like domain, and a complement regulatory protein-like sequence.
10022822	6	54	part_of	p41	924:926	arg1	the p41 fragment	p41		the p41 fragment		PUBTATOR	Site	p41	2035	fragment	The wedge shape and three-loop arrangement of the p41 fragment bound to the active site cleft of cathepsin L are reminiscent of the inhibitory edge of cystatins, thus demonstrating the first example of convergent evolution observed in cysteine protease inhibitors.
8286855	1	46	gly	sialoglycoprotein	144:160	arg1	The human red blood cell sialoglycoprotein	The human red blood cell sialoglycoprotein				Fterm		sialoglycoprotein			The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	1	46	gly	sialoglycoprotein	144:160	arg1	glycophorin A	glycophorin A				PUBTATOR		glycophorin A	2993		The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
1997323	0	31	gly	serotransferrin	39:53	arg1	Carbohydrate microheterogeneity	serotransferrin			Carbohydrate microheterogeneity	PUBTATOR		serotransferrin	24825		Carbohydrate microheterogeneity of rat serotransferrin.
1997323	0	33	gly	microheterogeneity	13:30	arg1	rat serotransferrin	rat serotransferrin				PUBTATOR		serotransferrin	24825		Carbohydrate microheterogeneity of rat serotransferrin.
26791533	2	26	gly	glycoproteins	346:358	arg1	seminal plasma glycoproteins	seminal plasma glycoproteins				Fterm		glycoproteins			Epitopes such as Lewis x and y are known to be present on seminal plasma glycoproteins, which can modulate the maternal immune response.
26791533	2	31	gly	present	320:326	arg2	seminal plasma glycoproteins AND Lewis x	glycoproteins			Lewis x	Fterm		glycoproteins			Epitopes such as Lewis x and y are known to be present on seminal plasma glycoproteins, which can modulate the maternal immune response.
4373463	0	4	gly	immunoglobulin	44:57	arg1	the carbohydrate units	IgA1 immunoglobulin			the carbohydrate units	PUBTATOR		IgA1 immunoglobulin	P01876		Structure of the carbohydrate units of IgA1 immunoglobulin.
10207176	2	39	part_of	motif	228:232	arg1	human RNase 2	RNase 2		motif		PUBTATOR	Site	RNase 2	6036	motif	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
19951703	2	38	part_of	proteins	189:196	arg1	a glycosylated luminal domain	proteins		a glycosylated luminal domain		Fterm	Site	proteins		domain	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
22451694	5	51	part_of	α5β1	940:943	arg1	the top face	α5		the top face		Cterm	Site	α5		face	The RGD-binding pocket is situated at the center of a trenchlike exposed surface on the top face of α5β1 devoid of glycosylation sites.
8435067	6	32	gly	alpha-glucosidase	862:878	arg1	the oligosaccharide side chains	lysosomal alpha-glucosidase			the oligosaccharide side chains	PUBTATOR		lysosomal alpha-glucosidase	2548		Evidence is presented that at least two of the oligosaccharide side chains of human lysosomal alpha-glucosidase are phosphorylated.
20571061	4	4	gly	glycopeptides	811:823	arg2	sialylated glycopeptides			sialylated glycopeptides						glycopeptides	LC-MS/MS analysis of de-glycosylated peptides identified 270 mouse serum peptides (95 glycoproteins) as sialylated glycopeptides, of which 67 glycopeptides were fully characterized by MS/MS analyses in a straightforward manner.
20571061	4	4	gly	glycopeptides	811:823	arg2	270 mouse serum peptides			270 mouse serum peptides						peptides	LC-MS/MS analysis of de-glycosylated peptides identified 270 mouse serum peptides (95 glycoproteins) as sialylated glycopeptides, of which 67 glycopeptides were fully characterized by MS/MS analyses in a straightforward manner.
20571061	4	22	gly	de-glycosylated	717:731	arg1	de-glycosylated peptides			de-glycosylated peptides						peptides	LC-MS/MS analysis of de-glycosylated peptides identified 270 mouse serum peptides (95 glycoproteins) as sialylated glycopeptides, of which 67 glycopeptides were fully characterized by MS/MS analyses in a straightforward manner.
20571061	4	44	gly	glycopeptides	838:850	arg2	67 glycopeptides			67 glycopeptides						glycopeptides	LC-MS/MS analysis of de-glycosylated peptides identified 270 mouse serum peptides (95 glycoproteins) as sialylated glycopeptides, of which 67 glycopeptides were fully characterized by MS/MS analyses in a straightforward manner.
20571061	4	48	gly	sialylated	800:809	arg1	sialylated glycopeptides			sialylated glycopeptides						glycopeptides	LC-MS/MS analysis of de-glycosylated peptides identified 270 mouse serum peptides (95 glycoproteins) as sialylated glycopeptides, of which 67 glycopeptides were fully characterized by MS/MS analyses in a straightforward manner.
20571061	4	48	gly	sialylated	800:809	arg1	270 mouse serum peptides			270 mouse serum peptides						peptides	LC-MS/MS analysis of de-glycosylated peptides identified 270 mouse serum peptides (95 glycoproteins) as sialylated glycopeptides, of which 67 glycopeptides were fully characterized by MS/MS analyses in a straightforward manner.
20571061	4	26	gly	glycoproteins	782:794	arg1	95 glycoproteins	glycoproteins		peptides		Fterm		glycoproteins		peptides	LC-MS/MS analysis of de-glycosylated peptides identified 270 mouse serum peptides (95 glycoproteins) as sialylated glycopeptides, of which 67 glycopeptides were fully characterized by MS/MS analyses in a straightforward manner.
2015821	7	53	gly	contains	1348:1355	arg1	1 AND one diantennary glycans	1			one diantennary glycans	PUBTATOR		peak 1	79834		Moreover our results show that the peak 1 contains four triantennary glycans, the peak 2 three triantennary and one diantennary glycans while the bound peaks 3 + 4 possess, on average, about one triantennary and three diantennary glycans per molecule.
2015821	7	53	gly	contains	1348:1355	arg1	1 AND four triantennary glycans	1			four triantennary glycans	PUBTATOR		peak 1	79834		Moreover our results show that the peak 1 contains four triantennary glycans, the peak 2 three triantennary and one diantennary glycans while the bound peaks 3 + 4 possess, on average, about one triantennary and three diantennary glycans per molecule.
2243102	6	15	part_of	Asn-34	953:958	arg1	lamp-1	lamp-1		Asn-34		PUBTATOR	SpecificSite	lamp-1	3916	Asn-34, Asn-93	Amino acid analysis and sequencing demonstrated that polylactosaminoglycans were located at Asn-34, Asn-93 and/or Asn-102, and Asn-195 and/or Asn-200 in lamp-1, and at Asn-4 and/or Asn-10, and Asn-279 in lamp-2.
18490449	7	80	gly	Thr-14	1265:1270	arg1	an O-glycan site			Thr-14	an O-glycan site					Thr-14	We identified two N-glycan sites at Asn-6 and Asn-12 and an O-glycan site at Thr-14 in the extracellular domain.
18490449	7	80	gly	Thr-14	1265:1270	arg1	two N-glycan sites			Thr-14	two N-glycan sites					Thr-14	We identified two N-glycan sites at Asn-6 and Asn-12 and an O-glycan site at Thr-14 in the extracellular domain.
18490449	7	96	gly	Asn-6	1224:1228	arg1	an O-glycan site			Asn-6 and Asn-12	an O-glycan site					Asn-6 and Asn-12	We identified two N-glycan sites at Asn-6 and Asn-12 and an O-glycan site at Thr-14 in the extracellular domain.
18490449	7	96	gly	Asn-6	1224:1228	arg1	two N-glycan sites			Asn-6 and Asn-12	two N-glycan sites					Asn-6 and Asn-12	We identified two N-glycan sites at Asn-6 and Asn-12 and an O-glycan site at Thr-14 in the extracellular domain.
18490449	7	101	gly	Asn-12	1234:1239	arg1	an O-glycan site			Asn-6 and Asn-12	an O-glycan site					Asn-6 and Asn-12	We identified two N-glycan sites at Asn-6 and Asn-12 and an O-glycan site at Thr-14 in the extracellular domain.
18490449	7	101	gly	Asn-12	1234:1239	arg1	two N-glycan sites			Asn-6 and Asn-12	two N-glycan sites					Asn-6 and Asn-12	We identified two N-glycan sites at Asn-6 and Asn-12 and an O-glycan site at Thr-14 in the extracellular domain.
2775174	7	13	gly	contained	855:863	arg1	The 20 kDa subunit AND one high-mannose-type oligosaccharide chain	The 20 kDa subunit			one high-mannose-type oligosaccharide chain	OGER		subunit	P20933		The 20 kDa subunit contained one high-mannose-type oligosaccharide chain, and the 24 kDa subunit had one high-mannose-type and one complex-type oligosaccharide chain.
2775174	7	1	gly	had	933:935	arg1	the 24 kDa subunit AND complex-type	the 24 kDa subunit			complex-type	OGER		subunit	P20933		The 20 kDa subunit contained one high-mannose-type oligosaccharide chain, and the 24 kDa subunit had one high-mannose-type and one complex-type oligosaccharide chain.
2775174	7	1	gly	had	933:935	arg1	the 24 kDa subunit AND high-mannose-type	the 24 kDa subunit			high-mannose-type	OGER		subunit	P20933		The 20 kDa subunit contained one high-mannose-type oligosaccharide chain, and the 24 kDa subunit had one high-mannose-type and one complex-type oligosaccharide chain.
1731338	3	29	gly	glycosylated	754:765	arg1	25 sites			25 sites						sites	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	29	gly	glycosylated	754:765	arg1	three serine sites			three serine sites						serine sites	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	42	gly	O-glycosylation	702:716	arg2	25 sites			25 sites						sites	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	42	gly	O-glycosylation	702:716	arg2	three serine sites			three serine sites						serine sites	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	58	gly	galactoglycoprotein	606:624	arg1	the native galactoglycoprotein	the native galactoglycoprotein				PUBTATOR		galactoglycoprotein	6693		Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
3497198	7	29	gly	glycosylation	972:984	arg1	H-2Kk	H-2Kk				PUBTATOR		H-2Kk	14972		The glycosylation of H-2Kk did not vary between B10.A and C3H mice.
11805077	3	19	gly	oligosaccharides	499:514	arg1	the EPO	EPO			oligosaccharides	OGER		EPO	P01588		Sulfation occurs in a part of the N-linked oligosaccharides in the EPO.
11912203	0	10	gly	glycosylation	18:30	arg1	adiponectin	adiponectin		domain		PUBTATOR		adiponectin	9370	domain	Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin.
11912203	0	10	gly	glycosylation	18:30	arg1	the collagenous domain			domain						domain	Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin.
11912203	0	10	gly	glycosylation	18:30	arg1	adiponectin	adiponectin		lysine residues		PUBTATOR		adiponectin	9370	lysine residues	Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin.
11912203	0	10	gly	glycosylation	18:30	arg1	the collagenous domain	adiponectin		domain		PUBTATOR		adiponectin	9370	domain	Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin.
1820200	0	9	gly	glycopeptides	87:99	arg2	glycopeptides			glycopeptides						glycopeptides	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
2775232	0	20	gly	glycoprotein	127:138	arg1	human platelet glycoprotein IIb	human platelet glycoprotein IIb				Fterm		glycoprotein			Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human platelet glycoprotein IIb.
17960739	6	41	gly	N-glycosylation	809:823	arg2	all nine potential N-glycosylation sites			all nine potential N-glycosylation sites						sites	This has demonstrated that all nine potential N-glycosylation sites were actually engaged.
28165004	3	24	gly	pembrolizumab/PD-1	418:435	arg1	the complex structure	PD-1			the complex structure	PUBTATOR		PD-1	5133		However, the binding mechanism of nivolumab to PD-1 has not yet been shown, despite a recent report describing the complex structure of pembrolizumab/PD-1.
3422739	4	52	part_of	alanine	758:764	arg1	the murine Ii protein	protein		alanine		Fterm	SpecificSite	protein		alanine at position 201	Ii does not have multiple candidate glycosaminoglycan-attachment sites, and we used site-directed mutagenesis to replace a candidate serine glycosaminoglycan-acceptor site with alanine at position 201 in the murine Ii protein.
20581009	0	43	gly	Endocan	85:91	arg1	a soluble endothelial proteoglycan	Endocan			a soluble endothelial proteoglycan	PUBTATOR		Endocan	11082		Characterization and binding activity of the chondroitin/dermatan sulfate chain from Endocan, a soluble endothelial proteoglycan.
16476442	3	41	part_of	angiotensin	484:494	arg1	the two hemoregulatory peptides	angiotensin I		the two hemoregulatory peptides		PUBTATOR	Site	angiotensin I	183	peptides	Both domains are capable of cleaving the two hemoregulatory peptides angiotensin I and bradykinin, but differ in their affinities for a range of other substrates and inhibitors.
17222411	2	38	part_of	podoplanin	333:342	arg1	the PLAG domain	podoplanin		the PLAG domain		OGER	Site	podoplanin	Q86YL7	domain	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	2	47	part_of	Thr52	299:303	arg1	human podoplanin	podoplanin		Thr52		OGER	AminoAcid	podoplanin	Q86YL7	domain, and Thr52	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	2	48	part_of	possesses	235:243	arg1	Podoplanin AND a platelet aggregation-stimulating (PLAG) domain	Podoplanin		a platelet aggregation-stimulating (PLAG) domain		OGER	AminoAcid	Podoplanin	Q86YL7	domain, and Thr52	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
11447134	10	58	gly	carried	1380:1386	arg1	the recombinant protein AND only three glycans	the recombinant protein			only three glycans	Fterm		protein			For beta-hexosaminidase B from human placenta, four N-glycans were identified and analyzed, whereas the recombinant protein expressed in SF21 cells carried only three glycans.
17525160	12	30	part_of	hCTR1	1605:1609	arg1	the extracellular amino terminus	hCTR1		the extracellular amino terminus		PUBTATOR	Site	hCTR1	1317	terminus	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
28531887	11	45	part_of	MT4-MMP	1449:1455	arg1	the single N-glycosylation site	MT4-MMP		the single N-glycosylation site		PUBTATOR	Site	MT4-MMP	4326	site	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	11	45	part_of	MT4-MMP	1449:1455	arg1	Asn318	MT4-MMP		Asn318		PUBTATOR	AminoAcid	MT4-MMP	4326	Asn318	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
8323280	8	28	gly	desialylated	1691:1702	arg1	desialylated rhLT	desialylated rhLT				Cterm		rhLT			The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
6177036	2	0	part_of	immunoglobulin	345:358	arg1	the primordial immunoglobulin domain	immunoglobulin		the primordial immunoglobulin domain		Fterm	Site	immunoglobulin		domain	There is also good homology with constant domains and beta 2-microglobulin; overall the results suggest that Thy-1 may be like the primordial immunoglobulin domain.
6371807	6	61	gly	present	958:964	arg1	a histidine-rich sequence AND the five glucosamine oligosaccharides			sequence	the five glucosamine oligosaccharides					sequence	Two of the five glucosamine oligosaccharides are present in a histidine-rich sequence of the middle region of the protein, in which the histidines flank beta-turns presumably at the surface of hemopexin.
22106953	3	26	part_of	enzyme	537:542	arg1	the active site	enzyme		the active site		Fterm	Site	enzyme		site	On the basis of residual electron density, a lysine residue has been modeled in the active site of the enzyme; thus, the structure corresponds to an enzyme-product complex.
7916636	6	24	gly	N-glycosylation	765:779	arg2	a N-glycosylation site			a N-glycosylation site						site	Only human kallikrein evolves with an additional Thr-108 and with a N-glycosylation site at aa-141.
8477709	0	52	gly	erythropoietin	51:64	arg1	sialylated oligosaccharides	erythropoietin			sialylated oligosaccharides	PUBTATOR		erythropoietin	2056		Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells.
8477709	0	87	gly	sialylated	14:23	arg1	sialylated oligosaccharides				sialylated oligosaccharides						Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells.
15454184	6	4	gly	fucosylated	787:797	arg1	fucosylated bi- and triantennary complex-type oligosaccharides				fucosylated bi- and triantennary complex-type oligosaccharides						Monosaccharide composition analyses suggested the linkages of fucosylated bi- and triantennary complex-type oligosaccharides on rhFS.
12218058	3	28	gly	N-glycosylated	659:672	arg1	all these sites			all these sites						sites	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
12218058	3	17	gly	occurs	776:781	arg1	726			Asn(726)						Asn(726)	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
1900431	0	30	gly	attached	52:59	arg1	threonine-61 AND an O-linked fucose			threonine-61	an O-linked fucose					threonine-61	Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
1900431	0	23	gly	has	29:31	arg1	Tissue plasminogen activator AND an O-linked fucose	Tissue plasminogen activator			an O-linked fucose	PUBTATOR		Tissue plasminogen activator	P00750		Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
9530955	9	86	gly	epitectin	1476:1484	arg1	The sialic acid	epitectin			The sialic acid	Fterm		epitectin			The sialic acid of urine epitectin consisted entirely of N-acetylneuraminic acid.
22171320	4	19	gly	glycopeptide	768:779	arg2	glycopeptide analysis			glycopeptide analysis						glycopeptide	We have developed a glycoproteomic approach that combines efficient purification of urinary glycoproteins/glycopeptides with complementary MS-fragmentation techniques for glycopeptide analysis.
22171320	4	63	gly	glycoproteins/glycopeptides	689:715	arg2	urinary glycoproteins/glycopeptides			urinary glycoproteins/glycopeptides						glycoproteins/glycopeptides	We have developed a glycoproteomic approach that combines efficient purification of urinary glycoproteins/glycopeptides with complementary MS-fragmentation techniques for glycopeptide analysis.
10419520	10	53	part_of	S2P	1308:1310	arg1	The HEIGH sequence	S2P		The HEIGH sequence		PUBTATOR	Site	S2P	51360	sequence	The HEIGH sequence of S2P, which contains two potential zinc-coordinating residues, is contained within a long hydrophobic segment.
10419520	10	27	part_of	contains	1319:1326	arg1	The HEIGH sequence AND two potential zinc-coordinating residues	The HEIGH sequence		two potential zinc-coordinating residues						residues	The HEIGH sequence of S2P, which contains two potential zinc-coordinating residues, is contained within a long hydrophobic segment.
21757827	5	11	gly	O-glycosylated	776:789	arg1	YIPF3	YIPF3				PUBTATOR		YIPF3	25844		Biochemical and immunofluorescence experiments strongly indicated that YIPF3 is synthesized in the ER as a N-glycosylated form (40 kDa), is then O-glycosylated in the Golgi apparatus to become a lower mobility form (46 kDa) and finally becomes a higher mobility form cleaved at its C-terminal luminal domain (36 kDa).
21757827	5	41	gly	N-glycosylated	738:751	arg1	YIPF3	YIPF3				PUBTATOR		YIPF3	25844		Biochemical and immunofluorescence experiments strongly indicated that YIPF3 is synthesized in the ER as a N-glycosylated form (40 kDa), is then O-glycosylated in the Golgi apparatus to become a lower mobility form (46 kDa) and finally becomes a higher mobility form cleaved at its C-terminal luminal domain (36 kDa).
1577715	6	66	gly	asparagine-linked	945:961	arg1	asparagine-linked oligosaccharide chains			asparagine	asparagine-linked oligosaccharide chains					asparagine	Another noteworthy finding which had not been reported previously was the occurrence of asparagine-linked oligosaccharide chains with blood group A, B, and H(O) structures.
24334224	3	61	gly	glycosylation	785:797	arg2	the specific O-linked glycosylation site			the specific O-linked glycosylation site						site	Peptide mappings using protease and chemical cleavages were performed to determine the specific O-linked glycosylation site used by Pichia-derived rhG-CSF.
18586680	3	16	part_of	N-terminal	492:501	arg1	two fragments	N-terminal		two fragments		Cterm	Site	N-terminal		fragments	Here we show that O-GlcNAcase is cleaved by caspase-3 into two fragments during apoptosis, an N-terminal fragment containing the O-GlcNAcase active site and a C-terminal fragment containing a region with homology to GCN5 histone acetyl-transferases.
18586680	3	16	part_of	N-terminal	492:501	arg1	an N-terminal fragment	N-terminal		an N-terminal fragment		Cterm	Site	N-terminal		fragment	Here we show that O-GlcNAcase is cleaved by caspase-3 into two fragments during apoptosis, an N-terminal fragment containing the O-GlcNAcase active site and a C-terminal fragment containing a region with homology to GCN5 histone acetyl-transferases.
18586680	3	32	part_of	O-GlcNAcase	527:537	arg1	the O-GlcNAcase active site	O-GlcNAcase		the O-GlcNAcase active site		PUBTATOR	Site	O-GlcNAcase	10724	site	Here we show that O-GlcNAcase is cleaved by caspase-3 into two fragments during apoptosis, an N-terminal fragment containing the O-GlcNAcase active site and a C-terminal fragment containing a region with homology to GCN5 histone acetyl-transferases.
18586680	3	30	part_of	containing	512:521	arg1	an N-terminal fragment AND the O-GlcNAcase active site			site						site	Here we show that O-GlcNAcase is cleaved by caspase-3 into two fragments during apoptosis, an N-terminal fragment containing the O-GlcNAcase active site and a C-terminal fragment containing a region with homology to GCN5 histone acetyl-transferases.
18586680	3	7	part_of	containing	577:586	arg1	two fragments AND a region			region						region	Here we show that O-GlcNAcase is cleaved by caspase-3 into two fragments during apoptosis, an N-terminal fragment containing the O-GlcNAcase active site and a C-terminal fragment containing a region with homology to GCN5 histone acetyl-transferases.
7679920	3	96	gly	residue	835:841	arg1	a fucose residue			a fucose residue	a fucose residue		AminoAcid			residue at	The Con A-reactive and LCA-nonreactive species of AFP from patients with hepatocellular carcinoma contained a biantennary sugar chain, and the Con A-reactive and LCA-reactive species had a biantennary one with a fucose residue at the innermost N-acetylglucosamine residue.
1991473	3	74	gly	glycopeptides	374:386	arg2	glycopeptides			glycopeptides						glycopeptides	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	3	27	gly	liberated	316:324	arg1	glycopeptides AND The sugar chains	hLH beta		glycopeptides	The sugar chains	PUBTATOR		hLH beta	3972	glycopeptides	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
8687384	5	49	gly	presence	984:991	arg1	Bowes t-PA AND glycans	Bowes t-PA			glycans	PUBTATOR		t-PA	P00750		The presence on Bowes t-PA of glycans associated primarily with the nervous system is consistent with its expression in a cell line of neuroectodermal origin.
16169851	6	14	gly	glycoprotein	767:778	arg1	herpes virus glycoprotein	herpes virus glycoprotein				PUBTATOR		glycoprotein D	2532		Moreover, the structure shows that BTLA recognizes the same surface on HVEM as gD (herpes virus glycoprotein D) and utilizes a similar binding motif.
23851396	1	5	gly	glycoproteins	145:157	arg1	Folate receptors	Folate receptors				PUBTATOR		Folate receptors (FRα, FRβ and FRγ)	2348		Folate receptors (FRα, FRβ and FRγ) are cysteine-rich cell-surface glycoproteins that bind folate with high affinity to mediate cellular uptake of folate.
23851396	1	5	gly	glycoproteins	145:157	arg1	cysteine-rich cell-surface glycoproteins	cysteine-rich cell-surface glycoproteins				Fterm		glycoproteins			Folate receptors (FRα, FRβ and FRγ) are cysteine-rich cell-surface glycoproteins that bind folate with high affinity to mediate cellular uptake of folate.
8172892	1	105	part_of	IX	234:235	arg1	the activation peptide	coagulation factor IX		the activation peptide		OGER	Site	coagulation factor IX	P00740	peptide	O-Linked oligosaccharide chains were identified in the activation peptide (AP) of human blood coagulation factor IX.
3514617	15	118	gly	glycopeptide	2390:2401	arg2	the tryptic glycopeptide pattern			the tryptic glycopeptide pattern						glycopeptide	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	15	160	gly	residues	2537:2544	arg1	40-61			40-61						residues 40-61	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
19299457	11	71	part_of	TSHR	1461:1464	arg1	TSHR residues N198 and T200	TSHR		residues N198		PUBTATOR	SpecificSite	TSHR	25360	residues N198	TSHR residues N198 and T200, like Y195, are on the convex facet of the leucine-rich domain.
9690478	5	37	part_of	IGF-IR	694:699	arg1	the first three domains	IGF-IR		the first three domains		PUBTATOR	Site	IGF-IR	3480	domains	We now present the structure of the first three domains of IGF-IR (L1-Cys-rich-L2) determined to 2.6 A resolution.
18250328	3	39	part_of	NL	494:495	arg1	the NL cholinesterase domain	NL		the NL cholinesterase domain		Cterm	Site	NL		domain	These interactions may be regulated by two short splice insertions (termed A and B) in the NL cholinesterase domain.
18250328	3	43	part_of	cholinesterase	497:510	arg1	the NL cholinesterase domain	cholinesterase		the NL cholinesterase domain		OGER	Site	cholinesterase	P06276	domain	These interactions may be regulated by two short splice insertions (termed A and B) in the NL cholinesterase domain.
21264968	0	47	gly	O-glycosylation	90:104	arg1	synthetic mucin peptides			synthetic mucin peptides						peptides	An efficient approach for the characterization of mucin-type glycopeptides: the effect of O-glycosylation on the conformation of synthetic mucin peptides.
21264968	0	103	gly	glycopeptides	61:73	arg2	mucin-type glycopeptides			mucin-type glycopeptides						glycopeptides	An efficient approach for the characterization of mucin-type glycopeptides: the effect of O-glycosylation on the conformation of synthetic mucin peptides.
17005555	0	42	part_of	Lingo-1	21:27	arg1	the Lingo-1 ectodomain	structure of the Lingo-1		the Lingo-1 ectodomain		PUBTATOR	Site	structure of the Lingo-1	84894	ectodomain	The structure of the Lingo-1 ectodomain, a module implicated in central nervous system repair inhibition.
10899108	5	40	part_of	p35	715:717	arg1	A central arginine residue	p35		A central arginine residue		PUBTATOR	AminoAcid	p35	3592	arginine residue	A central arginine residue from p35 projects into a deep pocket on p40, which may be an ideal target for a small molecule antagonist of IL-12 formation.
3542989	0	24	part_of	cholinesterase	44:57	arg1	Complete amino acid sequence	cholinesterase		Complete amino acid sequence		PUBTATOR	Site	cholinesterase	534616	sequence	Complete amino acid sequence of human serum cholinesterase.
17704566	1	5	part_of	incretin	303:310	arg1	the incretin hormone glucagon-like peptide 1	incretin hormone		the incretin hormone glucagon-like peptide 1		OGER	Site	incretin hormone	P09681	peptide	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	8	part_of	hormone	312:318	arg1	the incretin hormone glucagon-like peptide 1	incretin hormone		the incretin hormone glucagon-like peptide 1		OGER	Site	incretin hormone	P09681	peptide	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
10756055	5	67	part_of	Env-coreceptor	1132:1145	arg1	the Env-coreceptor contact sites	Env		the Env-coreceptor contact sites		PUBTATOR	Site	Env	100616444	sites	They also suggest a possible explanation for the various observations of restricted virus entry in some cell types and further our understanding of the framework of elements that represent the Env-coreceptor contact sites.
7679920	0	29	gly	non-fucosylated	122:136	arg1	fucosylated and non-fucosylated triantennary glycans				fucosylated and non-fucosylated triantennary glycans						Carbohydrate structures of human alpha-fetoprotein of patients with hepatocellular carcinoma: presence of fucosylated and non-fucosylated triantennary glycans.
7679920	0	37	gly	fucosylated	106:116	arg1	fucosylated and non-fucosylated triantennary glycans				fucosylated and non-fucosylated triantennary glycans						Carbohydrate structures of human alpha-fetoprotein of patients with hepatocellular carcinoma: presence of fucosylated and non-fucosylated triantennary glycans.
7679920	0	45	gly	alpha-fetoprotein	33:49	arg1	Carbohydrate structures	alpha-fetoprotein			Carbohydrate structures	PUBTATOR		alpha-fetoprotein	174		Carbohydrate structures of human alpha-fetoprotein of patients with hepatocellular carcinoma: presence of fucosylated and non-fucosylated triantennary glycans.
7451505	0	14	gly	asparagine-linked	22:38	arg1	asparagine-linked sugar chains			asparagine	asparagine-linked sugar chains					asparagine	Structural studies of asparagine-linked sugar chains of human ceruloplasmin.
7451505	0	31	gly	ceruloplasmin	62:74	arg1	asparagine-linked sugar chains	ceruloplasmin			asparagine-linked sugar chains	PUBTATOR		ceruloplasmin	1356		Structural studies of asparagine-linked sugar chains of human ceruloplasmin.
12408961	0	29	gly	glycoproteins	91:103	arg1	putative secreted glycoproteins	putative secreted glycoproteins				Fterm		glycoproteins			Identification and characterization of novel members of the CREG family, putative secreted glycoproteins expressed specifically in brain.
22023369	2	6	gly	N-glycosylation	484:498	arg2	two N-glycosylation sites			two N-glycosylation sites						sites	Here, we present the 2.2-Å structure of the complex formed between nonfucosylated IgG1-Fc and a soluble form of FcγRIIIa (sFcγRIIIa) with two N-glycosylation sites.
22023369	2	33	gly	nonfucosylated	409:422	arg1	nonfucosylated IgG1-Fc	nonfucosylated IgG1-Fc				OGER		IgG1	P01857		Here, we present the 2.2-Å structure of the complex formed between nonfucosylated IgG1-Fc and a soluble form of FcγRIIIa (sFcγRIIIa) with two N-glycosylation sites.
3756141	5	4	gly	located	585:591	arg2	residues 1-120 AND the carbohydrate prosthetic groups			residues 1-120	the carbohydrate prosthetic groups					residues 1-120	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
6234164	4	9	part_of	protein	814:820	arg1	the four constant region domains	protein		the four constant region domains		Fterm	Site	protein		domains	The complete sequence of the constant region gene segment shows that this segment is split by intervening sequences into four coding segments corresponding to the four constant region domains of the protein.
17956937	5	6	gly	glycopeptides	1110:1122	arg2	the glycopeptides			the glycopeptides						glycopeptides	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
9524075	0	57	gly	non-glycosylated	11:26	arg1	non-glycosylated human procathepsin	non-glycosylated human procathepsin				Fterm		procathepsin S	1520		Sorting of non-glycosylated human procathepsin S in mammalian cells.
12171601	5	36	gly	glycosylated	1067:1078	arg1	both N-linked sites			both N-linked sites						sites	Western blot analysis indicated that both N-linked sites are glycosylated.
15750791	5	23	gly	N-glycan	769:776	arg1	Edg-1/S1P1	Edg-1			N-glycan	PUBTATOR		Edg-1	1901		These studies revealed a possible regulatory role for the N-glycan on Edg-1/S1P1 in the dynamics of the receptor, such as its lateral and internal movements within the membrane, in ligand-stimulated mammalian cells.
2592374	5	49	part_of	sites	956:960	arg1	sCD4	sCD4		sites		PUBTATOR	Site	sCD4	329065	sites	Carbohydrate mapping by mass spectrometry was used to establish that both potential Asn-linked glycosylation sites in sCD4 (Asn271 and Asn300) have oligosaccharides attached.
7514386	8	73	gly	isolated	1088:1095	arg1	these peptides AND the glycan portion			these peptides	the glycan portion					peptides	The asparagine-linked sugar chains and the glycan portion of the GPI anchor were isolated from these peptides following hydrazinolysis or deamination and dephosphorylation, respectively.
7514386	8	73	gly	isolated	1088:1095	arg2	these peptides AND The asparagine-linked sugar chains			these peptides	The asparagine-linked sugar chains					peptides	The asparagine-linked sugar chains and the glycan portion of the GPI anchor were isolated from these peptides following hydrazinolysis or deamination and dephosphorylation, respectively.
7514386	8	102	gly	asparagine-linked	1011:1027	arg1	The asparagine-linked sugar chains			asparagine	The asparagine-linked sugar chains					asparagine	The asparagine-linked sugar chains and the glycan portion of the GPI anchor were isolated from these peptides following hydrazinolysis or deamination and dephosphorylation, respectively.
16186819	1	14	gly	glycoproteins	111:123	arg1	Thrombospondins	Thrombospondins				PUBTATOR		Thrombospondins	7058		Thrombospondins (THBSs) are secreted glycoproteins that have key roles in interactions between cells and the extracellular matrix.
16186819	1	14	gly	glycoproteins	111:123	arg1	secreted glycoproteins	secreted glycoproteins				Fterm		glycoproteins			Thrombospondins (THBSs) are secreted glycoproteins that have key roles in interactions between cells and the extracellular matrix.
19196183	0	55	gly	N-glycosylation	18:32	arg2	N-glycosylation sites			N-glycosylation sites						sites	Identification of N-glycosylation sites on secreted proteins of human hepatocellular carcinoma cells with a complementary proteomics approach.
23269669	0	80	gly	glycosylation	23:35	arg1	receptor guanylyl cyclase C	receptor guanylyl cyclase C				PUBTATOR		guanylyl cyclase C	2984		Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
3665914	4	48	gly	glycoprotein	872:883	arg1	glycoprotein	glycoprotein				Fterm		glycoprotein			The occurrence of a 6-deoxyhexose other than L-fucose in glycoprotein has not been previously reported.
7776966	9	87	gly	glycosylated	1436:1447	arg1	276			Asn's 174 and 276						Asn's 174 and 276	Western blot analyses of the wild type vs. mutant receptors demonstrate that, of the three potential sites for N-linked glycosylation, Asn's 174 and 276 are actually glycosylated.
2971663	2	13	gly	sialoglycoprotein	283:299	arg1	the sialoglycoprotein	the sialoglycoprotein				Fterm		sialoglycoprotein			Both forms of the sialoglycoprotein were identified as leukosialin by a monospecific antiserum, and the differences in molecular weight were found to be due to changes in the carbohydrate structures.
8357534	2	39	part_of	has	374:376	arg1	cathepsin G AND Asn-64	cathepsin G		Asn-64		PUBTATOR	SpecificSite	cathepsin G	1511	Asn-64	Elastase has two N-glycosylation sites occupied (Asn-45 and Asn-144), whereas cathepsin G has only one (Asn-64).
8357534	2	38	part_of	has	293:295	arg1	Elastase AND two N-glycosylation sites	Elastase		two N-glycosylation sites		Fterm	Site	Elastase		sites	Elastase has two N-glycosylation sites occupied (Asn-45 and Asn-144), whereas cathepsin G has only one (Asn-64).
8357534	2	38	part_of	has	293:295	arg1	Elastase AND Asn-45	Elastase		Asn-45 and Asn-144		Fterm	SpecificSite	Elastase		Asn-45 and Asn-144	Elastase has two N-glycosylation sites occupied (Asn-45 and Asn-144), whereas cathepsin G has only one (Asn-64).
19159218	11	82	gly	N-glycosites	1854:1865	arg2	939 N-glycosites			939 N-glycosites						N-glycosites	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	11	95	gly	glycoproteins	1921:1933	arg1	523 noredundant glycoproteins	523 noredundant glycoproteins				Fterm		glycoproteins			A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
21676880	2	3	gly	N-glycosylation	421:435	arg1	one consensus site			one consensus site						site	Here, we examine the kinetics of N-glycan addition to type I transmembrane KCNE1 K(+) channel β-subunits, where point mutations that prevent N-glycosylation at one consensus site give rise to disorders of the cardiac rhythm and congenital deafness.
20188224	1	56	gly	domain	168:173	arg1	7 1/2 repeats			domain	7 1/2 repeats					domain	PGRN is a modular protein with 7 1/2 repeats of the granulin domain separated by short spacer sequences.
20188224	1	72	gly	protein	125:131	arg1	7 1/2 repeats	protein			7 1/2 repeats	Fterm		protein			PGRN is a modular protein with 7 1/2 repeats of the granulin domain separated by short spacer sequences.
14660577	0	70	part_of	anhydrase	80:88	arg1	the extracellular domain	carbonic anhydrase XIV		the extracellular domain		OGER	Site	carbonic anhydrase XIV	Q9WVT6	domain	Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: implications for selective inhibition of membrane-associated isozymes.
7240157	0	20	gly	glycopeptide	94:105	arg2	glycopeptide preparations			glycopeptide preparations						glycopeptide	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.
7240157	0	59	gly	glycoproteins	46:58	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.
12603841	3	32	gly	glycosylated	640:651	arg1	GluR-D S1S2 protein	protein		N407 and N414		Fterm		protein		N407 and N414	GluR-D S1S2 protein expressed as a secreted protein in insect cells was found to be glycosylated at N407 and N414.
12603841	3	32	gly	glycosylated	640:651	arg2	N414			N407 and N414						N407 and N414	GluR-D S1S2 protein expressed as a secreted protein in insect cells was found to be glycosylated at N407 and N414.
12603841	3	32	gly	glycosylated	640:651	arg2	N414	protein		N407 and N414		Fterm		protein		N407 and N414	GluR-D S1S2 protein expressed as a secreted protein in insect cells was found to be glycosylated at N407 and N414.
2498325	3	57	gly	apoE	269:272	arg1	The carbohydrate attachment site	apoE			The carbohydrate attachment site	PUBTATOR		apoE	348		The carbohydrate attachment site of plasma apoE was localized to a single tryptic peptide (residues 192-206).
20188224	12	79	gly	glycosylation	1726:1738	arg2	the observed glycosylation sites			the observed glycosylation sites						sites	Two of the observed glycosylation sites occur within granulin domains, which may have important implications for understanding the structural basis of PGRN action.
20484118	3	0	part_of	residues	354:361	arg1	cytoplasmic and nuclear proteins	proteins		residues		Fterm	Site	proteins		residues	Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes.
29741879	4	81	gly	sialoglycopeptides	892:909	arg2	sialoglycopeptides			sialoglycopeptides						sialoglycopeptides	More importantly, we found that using immobilized metal affinity chromatography (IMAC) technology for the enrichment of phosphopeptides had coenriched a substantial number of sialoglycopeptides, allowing for a large-scale analysis of sialoglycopeptides in conjunction with the analysis of phosphopeptides.
29741879	4	94	gly	sialoglycopeptides	951:968	arg2	sialoglycopeptides			sialoglycopeptides						sialoglycopeptides	More importantly, we found that using immobilized metal affinity chromatography (IMAC) technology for the enrichment of phosphopeptides had coenriched a substantial number of sialoglycopeptides, allowing for a large-scale analysis of sialoglycopeptides in conjunction with the analysis of phosphopeptides.
23187000	7	23	gly	glycosylation	1330:1342	arg1	TIMP-1	TIMP-1				PUBTATOR		TIMP-1	7076		Cancer cells appear to utilize these bilateral aspects of TIMP-1 for cancer progression; an elevated TIMP-1 level exerts to cancer development via MMP-independent pathway during the early phase of tumor formation, whereas it is the aberrant glycosylation of TIMP-1 that overcome the high anti-proteolytic burden.
10861210	0	67	gly	glycoprotein	101:112	arg1	membrane glycoprotein	membrane glycoprotein				Fterm		glycoprotein			Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
2136357	2	20	gly	derived	543:549	arg1	uromodulin AND the Man6(7)GlcNAc2-R glycopeptides	uromodulin			the Man6(7)GlcNAc2-R glycopeptides	PUBTATOR		uromodulin	7369		We report here that the Man6(7)GlcNAc2-R glycopeptides derived from uromodulin inhibit antigen-specific T cell proliferation by 50% at 0.2-2 microM, and further studies, reported elsewhere, confirm that oligomannose glycopeptides from other sources are also inhibitory, with Man9GlcNAc2-R the most inhibitory of those tested [Muchmore et al., J Leukocyte Biol (in press)].
2136357	2	22	gly	glycopeptides	704:716	arg2	oligomannose glycopeptides			oligomannose glycopeptides						glycopeptides	We report here that the Man6(7)GlcNAc2-R glycopeptides derived from uromodulin inhibit antigen-specific T cell proliferation by 50% at 0.2-2 microM, and further studies, reported elsewhere, confirm that oligomannose glycopeptides from other sources are also inhibitory, with Man9GlcNAc2-R the most inhibitory of those tested [Muchmore et al., J Leukocyte Biol (in press)].
25081999	0	45	gly	SCP1	42:45	arg1	In vivo putative O-GlcNAcylation	SCP1			In vivo putative O-GlcNAcylation	PUBTATOR		SCP1	58190		In vivo putative O-GlcNAcylation of human SCP1 and evidence for possible role of its N-terminal disordered structure.
27313224	3	65	part_of	isoforms	607:614	arg1	luminal domain 4	isoforms		luminal domain 4		Fterm	Site	isoforms		domain	The luminal domain 4 (LD4) of the three synaptic vesicle glycoprotein 2 (SV2) isoforms A-C mediates uptake of the clinically most relevant serotype BoNT/A1.
19141282	2	23	part_of	IL-7Ralpha	257:266	arg1	the IL-7Ralpha ectodomain	IL-7Ralpha		the IL-7Ralpha ectodomain		PUBTATOR	Site	IL-7Ralpha	3575	ectodomain	We report that the IL-7Ralpha ectodomain uses glycosylation to modulate its binding constants to IL-7, unlike the other receptors in the gamma(c) family.
15486088	6	70	gly	glycopeptide	1141:1152	arg2	a mucin 1 glycopeptide substrate			a mucin 1 glycopeptide substrate						glycopeptide	A model of a mucin 1 glycopeptide substrate bound to the enzyme shows that the spatial separation between the lectin alpha site and a modeled active site UDP-GalNAc is consistent with the in vitro pattern of glycosylation observed for this peptide catalyzed by ppGaNTase-T1.
10200178	4	42	gly	glycopeptides	927:939	arg2	glycopeptides			glycopeptides						glycopeptides	Recent technical advances in electrospray mass spectrometry now provide the sensitivity to detect low femtomole quantities of glycopeptides with >5000 mass resolution and 30 ppm mass measurement [Medzihradszky, K. F., Besman, M. J., and Burlingame, A. L. (1998) Rapid Commun.
21205830	3	45	part_of	Nixin	672:676	arg1	the Nixin RING domain	Nixin		the Nixin RING domain		PUBTATOR	Site	Nixin	148066	domain	Ectopic expression of wild type Nixin induced a dramatic down-regulation of the ER-localized chaperone calnexin that was prevented by inactivation of the Nixin RING domain.
10731668	5	44	gly	glycosylation	815:827	arg2	32			Asn(32 )						Asn(32 )	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg1	Asn			Asn(32 )						Asn(32 )	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg2	Asn			Asn(32 )						Asn(32 )	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg1	CHO sEGFR	CHO sEGFR		Asn(32 )		PUBTATOR		CHO sEGFR	P00533	Asn(32 )	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg1	Asn			Asn(32 )						Asn(32 )	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg2	Asn			Asn(32 )						Asn(32 )	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg1	CHO sEGFR	CHO sEGFR		Asn(32 )		PUBTATOR		CHO sEGFR	P00533	Asn(32 )	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg2	Asn			Asn(32 )						Asn(32 )	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg1	CHO sEGFR	CHO sEGFR		Asn(32 )		PUBTATOR		CHO sEGFR	P00533	Asn(32 )	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg1	CHO sEGFR	CHO sEGFR		Asn(32 )		PUBTATOR		CHO sEGFR	P00533	Asn(32 )	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
8615697	11	45	gly	glycosylated	1856:1867	arg1	the glycosylated asparagine residue			the glycosylated asparagine residue						asparagine residue	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
7574684	2	54	gly	contains	508:515	arg1	the extracellular domain AND 33.3% carbohydrate moieties	trkB		domain	33.3% carbohydrate moieties	PUBTATOR		trkB	4915	domain	The extracellular domain contains 398 amino acids and has a molecular weight of 60.6 kDa according to laser desorption mass spectrometry, indicating that the extracellular domain of trkB contains 33.3% carbohydrate moieties.
11152692	11	24	gly	O-glycosylation	1339:1353	arg2	a potential O-glycosylation site			a potential O-glycosylation site						site	The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54).
11152692	11	33	gly	N-glycosylation	1243:1257	arg2	an N-glycosylation site			an N-glycosylation site						site	The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54).
11152692	11	38	gly	site	1259:1262	arg1	a heterogeneous oligosaccharide structure			site	a heterogeneous oligosaccharide structure					site	The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54).
11152692	11	61	gly	site	1355:1358	arg1	a heterogeneous oligosaccharide structure			site	a heterogeneous oligosaccharide structure					site	The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54).
11152692	11	24	gly	O-glycosylation	1339:1353	arg2	Asn			Asn(281)						Asn(281)	The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54).
11152692	11	24	gly	O-glycosylation	1339:1353	arg2	Ser			Ser(54)						Ser(54)	The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54).
11152692	11	33	gly	N-glycosylation	1243:1257	arg2	Asn			Asn(281)						Asn(281)	The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54).
11152692	11	33	gly	N-glycosylation	1243:1257	arg2	Ser			Ser(54)						Ser(54)	The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54).
21752865	7	28	gly	N-glycosylated	1245:1258	arg2	Asn170	BRI2		Asn170		PUBTATOR		BRI2	9445	Asn170	These data indicate that BRI2 is N-glycosylated at Asn170.
18729387	4	63	gly	glycosylation	835:847	arg1	rat brain IgLON proteins	rat brain IgLON proteins				Fterm		proteins			In this study, we conducted simultaneous site-specific glycosylation analysis of rat brain IgLON proteins by liquid chromatography and multiple-stage mass spectrometry (LC-MS ( n )).
15807535	3	65	gly	glycosylation	570:582	arg2	three potential N-linked glycosylation sites			three potential N-linked glycosylation sites						sites	Sequence analysis revealed three potential N-linked glycosylation sites in human ABCG2 at amino acids 418, 557, and 596.
17591618	8	3	gly	non-fucosylated	1289:1303	arg1	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides				Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides						Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified.
17591618	8	57	gly	fucosylated	1258:1268	arg1	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides				Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides						Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified.
17591618	8	59	gly	monosialylated	1274:1287	arg1	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides				Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides						Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified.
17591618	8	116	gly	Disialylated	1245:1256	arg1	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides				Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides						Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified.
8672508	6	30	part_of	gp210	1109:1113	arg1	Ser1880	gp210		Ser1880		PUBTATOR	AminoAcid	gp210	23225	Ser1880	This analysis showed that Ser1880 of gp210 was phosphorylated in mitosis, possibly by cyclin B-p34cdc2 or a related kinase.
3980466	4	77	gly	glycosylation	712:724	arg2	11 purified glycosylation sites			11 purified glycosylation sites						sites	[3H]Mannose-labeled oligosaccharides were released from each of 11 purified glycosylation sites by the almond peptide:N-glycosidase and analyzed by a variety of chromatographic procedures and glycosidase treatments.
3980466	4	90	gly	released	678:685	arg1	11 purified glycosylation sites AND [3H]Mannose-labeled oligosaccharides			11 purified glycosylation sites	[3H]Mannose-labeled oligosaccharides					sites	[3H]Mannose-labeled oligosaccharides were released from each of 11 purified glycosylation sites by the almond peptide:N-glycosidase and analyzed by a variety of chromatographic procedures and glycosidase treatments.
18203274	1	34	gly	glycosylated	124:135	arg1	a highly glycosylated protein	a highly glycosylated protein				Fterm		protein			Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	1	34	gly	glycosylated	124:135	arg1	Human butyrylcholinesterase	Human butyrylcholinesterase				PUBTATOR		Human butyrylcholinesterase	590		Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
1569071	11	10	gly	asialoglycopeptide	2342:2359	arg2	the Ser66-Lys88 asialoglycopeptide			the Ser66-Lys88 asialoglycopeptide						asialoglycopeptide	Finally, the association of O-linked oligosaccharide with the E domain peptide of IGF-II was confirmed by demonstrating the specificity of binding of the Ser66-Lys88 asialoglycopeptide to jackfruit lectin.
1997323	11	48	gly	sequence	1264:1271	arg1	the sequence: Neu5Ac(alpha 2-3)Gal(beta 1-3)[Neu5Ac(alpha 2-6)]GlcNAc(beta 1-2)Man				the sequence: Neu5Ac(alpha 2-3)Gal(beta 1-3)[Neu5Ac(alpha 2-6)]GlcNAc(beta 1-2)Man						However, the alpha-1,3-Man-linked antenna in rTf-1 as well as rTf-2 had the sequence: Neu5Ac(alpha 2-3)Gal(beta 1-3)[Neu5Ac(alpha 2-6)]GlcNAc(beta 1-2)Man.
1997323	11	88	gly	antenna	1222:1228	arg1	rTf-1	rTf-1			antenna	PUBTATOR		rTf-1	Q92541		However, the alpha-1,3-Man-linked antenna in rTf-1 as well as rTf-2 had the sequence: Neu5Ac(alpha 2-3)Gal(beta 1-3)[Neu5Ac(alpha 2-6)]GlcNAc(beta 1-2)Man.
1997323	11	88	gly	antenna	1222:1228	arg1	rTf-2	rTf-2			antenna	OGER		rTf-2	Q3T1J8		However, the alpha-1,3-Man-linked antenna in rTf-1 as well as rTf-2 had the sequence: Neu5Ac(alpha 2-3)Gal(beta 1-3)[Neu5Ac(alpha 2-6)]GlcNAc(beta 1-2)Man.
9572875	5	23	part_of	IGFBP-6	884:890	arg1	Glycosylation sites	IGFBP-6		Glycosylation sites		PUBTATOR	Site	IGFBP-6	3489	sites	Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography.
9572875	5	23	part_of	IGFBP-6	884:890	arg1	Thr146	IGFBP-6		Thr126, Ser144, Thr145, Thr146, and Ser152		PUBTATOR	AminoAcid	IGFBP-6	3489	Thr126, Ser144, Thr145, Thr146, and Ser152	Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography.
9572875	5	23	part_of	IGFBP-6	884:890	arg1	Thr126	IGFBP-6		Thr126, Ser144, Thr145, Thr146, and Ser152		PUBTATOR	AminoAcid	IGFBP-6	3489	Thr126, Ser144, Thr145, Thr146, and Ser152	Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography.
9572875	5	23	part_of	IGFBP-6	884:890	arg1	Ser144	IGFBP-6		Thr126, Ser144, Thr145, Thr146, and Ser152		PUBTATOR	AminoAcid	IGFBP-6	3489	Thr126, Ser144, Thr145, Thr146, and Ser152	Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography.
9572875	5	23	part_of	IGFBP-6	884:890	arg1	Ser152	IGFBP-6		Thr126, Ser144, Thr145, Thr146, and Ser152		PUBTATOR	AminoAcid	IGFBP-6	3489	Thr126, Ser144, Thr145, Thr146, and Ser152	Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography.
9572875	5	23	part_of	IGFBP-6	884:890	arg1	Thr126	IGFBP-6		Thr126, Ser144, Thr145, Thr146, and Ser152		PUBTATOR	AminoAcid	IGFBP-6	3489	Thr126, Ser144, Thr145, Thr146, and Ser152	Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography.
9572875	5	23	part_of	IGFBP-6	884:890	arg1	Ser144	IGFBP-6		Thr126, Ser144, Thr145, Thr146, and Ser152		PUBTATOR	AminoAcid	IGFBP-6	3489	Thr126, Ser144, Thr145, Thr146, and Ser152	Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography.
9572875	5	23	part_of	IGFBP-6	884:890	arg1	Ser152	IGFBP-6		Thr126, Ser144, Thr145, Thr146, and Ser152		PUBTATOR	AminoAcid	IGFBP-6	3489	Thr126, Ser144, Thr145, Thr146, and Ser152	Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography.
9572875	5	23	part_of	IGFBP-6	884:890	arg1	Ser144	IGFBP-6		Thr126, Ser144, Thr145, Thr146, and Ser152		PUBTATOR	AminoAcid	IGFBP-6	3489	Thr126, Ser144, Thr145, Thr146, and Ser152	Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography.
9572875	5	23	part_of	IGFBP-6	884:890	arg1	Ser152	IGFBP-6		Thr126, Ser144, Thr145, Thr146, and Ser152		PUBTATOR	AminoAcid	IGFBP-6	3489	Thr126, Ser144, Thr145, Thr146, and Ser152	Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography.
9572875	5	23	part_of	IGFBP-6	884:890	arg1	Ser152	IGFBP-6		Thr126, Ser144, Thr145, Thr146, and Ser152		PUBTATOR	AminoAcid	IGFBP-6	3489	Thr126, Ser144, Thr145, Thr146, and Ser152	Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography.
32363391	3	5	gly	N-glycosylation	571:585	arg2	22 potential N-glycosylation sites			22 potential N-glycosylation sites						sites	The spike protein is comprised of two protein subunits (S1 and S2), which together possess 22 potential N-glycosylation sites.
24927598	7	26	gly	glycosylation	953:965	arg1	ZIP14	ZIP14				PUBTATOR		ZIP14	23516		Asparagine-linked (N-linked) glycosylation of ZIP14, particularly the glycosylation at N102, was required for efficient membrane extraction of ZIP14 and therefore is necessary for its iron sensitivity.
24927598	7	49	gly	glycosylation	994:1006	arg2	N102			N102						N102	Asparagine-linked (N-linked) glycosylation of ZIP14, particularly the glycosylation at N102, was required for efficient membrane extraction of ZIP14 and therefore is necessary for its iron sensitivity.
18065761	6	52	part_of	TSPN-1	1152:1157	arg1	several TSPN-1 domains	TSPN-1		several TSPN-1 domains		Cterm	Site	TSPN-1		domains	The ability of several TSPN-1 domains to bind to glycosaminoglycans simultaneously probably increases the affinity of binding through multivalent interactions.
12604466	6	52	gly	N-glycosylation	861:875	arg2	the seven consensus N-glycosylation sites			the seven consensus N-glycosylation sites						sites	To localize glycosylation sites, we individually mutated the seven consensus N-glycosylation sites by replacing asparagine (N) with glutamine (Q) and assessing mutant transporters in Xenopus laevis oocytes.
12604466	6	65	gly	glycosylation	796:808	arg2	glycosylation sites			glycosylation sites						sites	To localize glycosylation sites, we individually mutated the seven consensus N-glycosylation sites by replacing asparagine (N) with glutamine (Q) and assessing mutant transporters in Xenopus laevis oocytes.
21639859	0	39	part_of	GluA1	44:48	arg1	the glutamate receptor GluA1 N-terminal domain	GluA1		the glutamate receptor GluA1 N-terminal domain		PUBTATOR	Site	GluA1	2890	domain	Crystal structure of the glutamate receptor GluA1 N-terminal domain.
7694285	4	56	gly	glycoprotein	812:823	arg1	a 64-kDa high-mannose glycoprotein	enzyme			a 64-kDa high-mannose glycoprotein	Fterm		enzyme			The enzyme was identified as a 64-kDa high-mannose glycoprotein.
6684483	2	0	gly	glycopeptides	432:444	arg2	its glycopeptides			its glycopeptides						glycopeptides	These conclusions have been based on the results of methylation analysis of the whole glycoprotein and investigation of the structures of its glycopeptides prepared using pronase digestion.
6684483	2	26	gly	glycoprotein	376:387	arg1	whole glycoprotein	whole glycoprotein				Fterm		glycoprotein			These conclusions have been based on the results of methylation analysis of the whole glycoprotein and investigation of the structures of its glycopeptides prepared using pronase digestion.
10756055	4	49	gly	glycosylated	873:884	arg1	cell type-dependent glycosylated CXCR4	cell type-dependent glycosylated CXCR4				PUBTATOR		CXCR4	7852		These results may have far-reaching implications for the differential recognition of cell type-dependent glycosylated CXCR4 by HIV-1 isolates and their evolution in vivo.
7514386	10	58	gly	asparagine-linked	1312:1328	arg1	the asparagine-linked sugar chains			asparagine	the asparagine-linked sugar chains					asparagine	The structures of the asparagine-linked sugar chains of U-CD59 were biantennary complex type, only 4.2% of which are monosialylated.
7514386	10	67	gly	U-CD59	1346:1351	arg1	the asparagine-linked sugar chains	CD59			the asparagine-linked sugar chains	PUBTATOR		CD59	966		The structures of the asparagine-linked sugar chains of U-CD59 were biantennary complex type, only 4.2% of which are monosialylated.
12754519	5	42	gly	contain	882:888	arg1	peptides AND N-linked carbohydrates			peptides	N-linked carbohydrates					peptides	Here we describe a method for the selective isolation, identification and quantification of peptides that contain N-linked carbohydrates.
18780401	0	37	gly	glycoproteins	27:39	arg1	N-linked glycoproteins	N-linked glycoproteins				Fterm		glycoproteins			Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
17222411	6	16	gly	sialylated	872:881	arg1	the sialylated Corel at Thr52			the sialylated Corel at Thr52						Thr52	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
18203274	4	28	gly	glycoprotein	562:573	arg1	this glycoprotein	this glycoprotein				Fterm		glycoprotein			A prerequisite for the therapeutic use of hBChE is a detailed characterization of this glycoprotein purified from human plasma.
21886772	8	18	gly	N-glycosylation	1415:1429	arg1	FKRP homodimer	FKRP homodimer				PUBTATOR		FKRP homodimer	79147		FKRP contains N-glycan of high mannose and/or hybrid type; however, FKRP N-glycosylation is not required for FKRP homodimer or multimer formation.
21886772	8	22	gly	contains	1347:1354	arg1	FKRP AND N-glycan	FKRP			N-glycan	PUBTATOR		FKRP	79147		FKRP contains N-glycan of high mannose and/or hybrid type; however, FKRP N-glycosylation is not required for FKRP homodimer or multimer formation.
6966283	7	47	gly	glycoprotein	661:672	arg1	the glycoprotein	the glycoprotein				Fterm		glycoprotein			The structures of A- and B-chains of the glycoprotein were examined by periodate oxidation, sequential glycosidase digestion, and permethylation.
17322565	8	62	gly	glycosylation	1340:1352	arg2	Asn-116			Asn-116						Asn-116	These data suggest that N-linked glycosylation at Asn-116 reduces the ability of EL to hydrolyze lipids in LDL and HDL2.
8089145	1	44	part_of	Acyloxyacyl	131:141	arg1	a precursor polypeptide	Acyloxyacyl hydrolase		a precursor polypeptide		PUBTATOR	Site	Acyloxyacyl hydrolase	313	polypeptide	Acyloxyacyl hydrolase, a leukocyte enzyme that acts on bacterial lipopolysaccharides (LPSs) and many glycerolipids, is synthesized as a precursor polypeptide that undergoes internal disulfide linkage before being proteolytically processed into two subunits.
18065761	0	47	part_of	thrombospondin-1	57:72	arg1	the thrombospondin-1 N-terminal domain	thrombospondin-1		the thrombospondin-1 N-terminal domain		PUBTATOR	Site	thrombospondin-1	7057	domain	Heparin-induced cis- and trans-dimerization modes of the thrombospondin-1 N-terminal domain.
25802287	9	34	gly	glycosylation	1442:1454	arg1	human serum IgM	human serum IgM				OGER		IgM	P01871		We applied the microarray approach to a detailed site-specific glycosylation analysis of human serum IgM.
8942648	8	5	part_of	TPO	1098:1100	arg1	the cytokine domain	TPO		the cytokine domain		PUBTATOR	Site	TPO	7066	domain	Two unique disulfides are formed between the four cysteines in the cytokine domain of TPO: Cys7-Cys151 and Cys29-Cys85.
8942648	8	39	part_of	cysteines	1062:1070	arg1	TPO	TPO		cysteines		PUBTATOR	AminoAcid	TPO	7066	cysteines	Two unique disulfides are formed between the four cysteines in the cytokine domain of TPO: Cys7-Cys151 and Cys29-Cys85.
7620335	0	1	gly	structures	38:47	arg1	each glycosylation site			each glycosylation site	each glycosylation site		Site			site	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	0	67	gly	site	120:123	arg1	the oligosaccharide structures			site	the oligosaccharide structures					site	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	0	75	gly	peptide	90:96	arg1	the oligosaccharide structures			peptide	the oligosaccharide structures					peptide	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	0	89	gly	glycosylation	106:118	arg2	each glycosylation site			each glycosylation site						site	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
1567356	3	74	gly	glycosylation	430:442	arg2	each glycosylation site			each glycosylation site						site	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
18214858	5	77	gly	Asn211	1019:1024	arg1	haptoglobin N-glycans			Asn211 site	haptoglobin N-glycans					Asn211 site	Tri-antennary N-glycans containing a Lewis X-type fucose markedly increased at the Asn211 site of haptoglobin N-glycans.
9136890	12	42	gly	found	1490:1494	arg1	each position AND oligosaccharides			each position	oligosaccharides					position	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	12	49	gly	glycosylation	1537:1549	arg1	one site			one site						site	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	12	49	gly	glycosylation	1537:1549	arg1	other sites			other sites						sites	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	12	79	gly	glycosylation	1592:1604	arg1	other sites			other sites						sites	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
15253437	0	27	gly	glycosylation	97:109	arg2	their glycosylation sites			their glycosylation sites						sites	A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
15253437	0	65	gly	N-glycosylated	37:50	arg1	N-glycosylated proteins	N-glycosylated proteins				Fterm		proteins			A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
18250328	2	13	part_of	cholinesterase	346:359	arg1	their extracellular cholinesterase domain	cholinesterase		their extracellular cholinesterase domain		OGER	Site	cholinesterase	P06276	domain	Postsynaptic neuroligins engage in Ca2+-dependent transsynaptic interactions via their extracellular cholinesterase domain with presynaptic neurexins (NRXs).
2393398	0	5	gly	composition	13:23	arg1	pro-urokinase			pro-urokinase	pro-urokinase		AminoAcid			pro	Carbohydrate composition and presence of a fucose-protein linkage in recombinant human pro-urokinase.
2393398	0	13	gly	presence	29:36	arg1	pro-urokinase AND a fucose-protein linkage			pro-urokinase	a fucose-protein linkage					pro	Carbohydrate composition and presence of a fucose-protein linkage in recombinant human pro-urokinase.
1468573	0	13	gly	contains	16:23	arg1	Human urokinase AND GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	Human urokinase			GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	Fterm		urokinase			Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
10766826	0	6	part_of	myeloperoxidase	78:92	arg1	halide-binding sites	myeloperoxidase		halide-binding sites		PUBTATOR	Site	myeloperoxidase	4353	sites	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
3038148	1	14	part_of	contain	248:254	arg1	The revised amino acid sequence AND the active site Asp residue	The revised amino acid sequence		the active site Asp residue						Asp residue	The revised amino acid sequence of rat submaxillary gland tonin, a serine protease, does contain the active site Asp residue.
9705299	4	16	gly	utilized	793:800	arg2	Asn203			Asn203 and Asn276						Asn203 and Asn276	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
12799386	8	18	part_of	ZP2	1049:1051	arg1	The N termini	ZP2		The N termini		PUBTATOR	Site	ZP2	22787	termini	The N termini of ZP1 and ZP3, but not ZP2, were blocked by cyclization of glutamine to pyroglutamate.
12799386	8	25	part_of	ZP1	1028:1030	arg1	The N termini	ZP1		The N termini		PUBTATOR	Site	ZP1	22786	termini	The N termini of ZP1 and ZP3, but not ZP2, were blocked by cyclization of glutamine to pyroglutamate.
12799386	8	57	part_of	ZP3	1036:1038	arg1	The N termini	ZP3		The N termini		PUBTATOR	Site	ZP3	22788	termini	The N termini of ZP1 and ZP3, but not ZP2, were blocked by cyclization of glutamine to pyroglutamate.
11067851	5	34	gly	C-mannosylated	665:678	arg1	-423			Trp-368, -420, -423, and -480						Trp-368, -420, -423, and -480	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
11067851	5	34	gly	C-mannosylated	665:678	arg1	-480			Trp-368, -420, -423, and -480						Trp-368, -420, -423, and -480	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
11067851	5	34	gly	C-mannosylated	665:678	arg1	-420			Trp-368, -420, -423, and -480						Trp-368, -420, -423, and -480	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
11067851	5	34	gly	C-mannosylated	665:678	arg1	-480			Trp-368, -420, -423, and -480						Trp-368, -420, -423, and -480	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
11067851	5	34	gly	C-mannosylated	665:678	arg1	-420			Trp-368, -420, -423, and -480						Trp-368, -420, -423, and -480	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
11067851	5	34	gly	C-mannosylated	665:678	arg1	-420			Trp-368, -420, -423, and -480						Trp-368, -420, -423, and -480	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
18340083	7	55	gly	N-glycosylation	906:920	arg2	the N-glycosylation site			the N-glycosylation site						site	Mutating the N-glycosylation site in mouse GPIHBP1 results in an accumulation of GPIHBP1 in the endoplasmic reticulum and a markedly reduced amount of the protein on the cell surface.
15807535	5	19	part_of	residue	857:863	arg1	ABCG2	ABCG2		residue		PUBTATOR	AminoAcid	ABCG2	9429	residue in	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
22932899	4	21	part_of	hAPN	601:604	arg1	the dimeric ectodomain	hAPN		the dimeric ectodomain		PUBTATOR	Site	hAPN	290	ectodomain	Reported here are the high resolution x-ray crystal structures of the dimeric ectodomain of hAPN and its complexes with angiotensin IV and the peptidomimetic inhibitors, amastatin and bestatin.
8477709	1	17	gly	Asn-linked	134:143	arg1	the Asn-linked oligosaccharides			Asn	the Asn-linked oligosaccharides					Asn	The native structures of the Asn-linked oligosaccharides and the O-glycans at Ser126 of human erythropoietin expressed from recombinant BHK cells have been elucidated.
8477709	1	19	gly	Ser126	183:188	arg1	the O-glycans			Ser126	the O-glycans					Ser126	The native structures of the Asn-linked oligosaccharides and the O-glycans at Ser126 of human erythropoietin expressed from recombinant BHK cells have been elucidated.
8172892	9	63	gly	linked	1618:1623	arg2	the threonine residues AND tri-			the threonine residues	tri-					threonine residues	From these results, it was concluded that a part of the activation peptide of human factor IX in circulating blood has tri- and tetrasaccharides O-glycosidically linked to the threonine residues at 159 and 169.
11081633	4	0	part_of	PSGL-1	761:766	arg1	the N-terminal domain	PSGL-1		the N-terminal domain		PUBTATOR	Site	PSGL-1	6404	domain	We also present the crystal structure of P-selectin LE co-complexed with the N-terminal domain of human PSGL-1 modified by both tyrosine sulfation and SLe(X).
12022871	0	60	gly	glycosylation	137:149	arg2	a glycosylation site			a glycosylation site						site	Structure-function analysis of human triacylglycerol hydrolase by site-directed mutagenesis: identification of the catalytic triad and a glycosylation site.
12022871	0	70	gly	analysis	19:26	arg1	a glycosylation site			a glycosylation site						site	Structure-function analysis of human triacylglycerol hydrolase by site-directed mutagenesis: identification of the catalytic triad and a glycosylation site.
23269669	2	70	part_of	enterotoxin	534:544	arg1	the heat-stable enterotoxin peptide	enterotoxin		the heat-stable enterotoxin peptide		Fterm	Site	enterotoxin		peptide	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
10704524	0	83	gly	occupancy	44:52	arg1	N-linked oligosaccharides			site	N-linked oligosaccharides					site	Human alpha-N-acetylgalactosaminidase: site occupancy and structure of N-linked oligosaccharides.
1380064	2	14	part_of	Eo-chemotactic	319:332	arg1	two Eo-chemotactic polypeptides	Eo-chemotactic		two Eo-chemotactic polypeptides		Cterm	Site	Eo-chemotactic		polypeptides	By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity.
8617200	0	0	gly	cysteine	78:85	arg1	an eight cysteine repeat			cysteine	an eight cysteine repeat					cysteine	Association of the small latent transforming growth factor-beta with an eight cysteine repeat of its binding protein LTBP-1.
8617200	0	29	gly	LTBP-1	117:122	arg1	an eight cysteine repeat	LTBP-1			an eight cysteine repeat	PUBTATOR		LTBP-1	4052		Association of the small latent transforming growth factor-beta with an eight cysteine repeat of its binding protein LTBP-1.
23050552	5	38	gly	glycopeptides	562:574	arg2	proteinase K-generated fibrinogen glycopeptides			proteinase K-generated fibrinogen glycopeptides						glycopeptides	Here, we make use of tryptic- and proteinase K-generated fibrinogen glycopeptides for the detailed analysis of the protein's O-glycosylation by combining information obtained from both one- and two-dimensional nanoLC-ESI-ion trap (IT)-MS approaches.
22766194	3	1	gly	N-glycosylation	486:500	arg2	6 consensus N-glycosylation sites			6 consensus N-glycosylation sites						sites	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
25561468	7	66	part_of	N-terminal	1002:1011	arg1	the N-terminal fragment	N-terminal		the N-terminal fragment		Cterm	Site	N-terminal		fragment	Removal of the N-terminal fragment (ICA512-NTF) preceding ME ICA512 allows an ICA512-ΔNTF G553D mutant to exit the endoplasmic reticulum, and ICA512-ΔNTF is constitutively delivered to the cell surface.
22451694	2	15	part_of	α5β1	269:272	arg1	the α5β1 integrin headpiece fragment	structure of the α5		the α5β1 integrin headpiece fragment		Cterm	Site	structure of the α5		fragment	A crystal structure of the α5β1 integrin headpiece fragment bound by an allosteric inhibitory antibody was determined at a 2.9-Å resolution both in the absence and presence of a ligand peptide containing the Arg-Gly-Asp (RGD) sequence.
22451694	2	14	part_of	containing	435:444	arg1	a ligand peptide AND the Arg-Gly-Asp (RGD) sequence	a ligand peptide		the Arg-Gly-Asp (RGD) sequence						sequence	A crystal structure of the α5β1 integrin headpiece fragment bound by an allosteric inhibitory antibody was determined at a 2.9-Å resolution both in the absence and presence of a ligand peptide containing the Arg-Gly-Asp (RGD) sequence.
17310251	3	21	part_of	factor	382:387	arg1	the Von Willebrand factor A (VWA) domain	Von Willebrand factor A		the Von Willebrand factor A (VWA) domain		OGER	Site	Von Willebrand factor A	P04275	domain	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
17310251	3	30	part_of	A	389:389	arg1	the Von Willebrand factor A (VWA) domain	Von Willebrand factor A		the Von Willebrand factor A (VWA) domain		OGER	Site	Von Willebrand factor A	P04275	domain	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
8617200	8	25	gly	8-Cys	1324:1328	arg1	the core 8-Cys repeat			Cys	the core 8-Cys repeat					Cys	These interactions are mediated by exchanging cysteine disulfide bonds between the core 8-Cys repeat and an optionally associated protein during the secretion.
7744025	6	24	gly	glycosylated	1297:1308	arg1	the glycosylated peptides			the glycosylated peptides						peptides	In addition, evidence was obtained that at least 20% of the glycosylated peptides exhibited GalNAc incorporation at Ser20.
29632068	4	11	part_of	domain	664:669	arg1	a region	domain		a region						region	We previously demonstrated that substrate specificity resides in a region of ∼150 residues in the Tram-Lag-CLN8 domain.
29632068	4	27	part_of	Tram-Lag-CLN8	650:662	arg1	the Tram-Lag-CLN8 domain	Tram		the Tram-Lag-CLN8 domain		OGER	Site	Tram	Q86XR7	domain	We previously demonstrated that substrate specificity resides in a region of ∼150 residues in the Tram-Lag-CLN8 domain.
29632068	4	39	part_of	region	619:624	arg1	the Tram-Lag-CLN8 domain	region		the Tram-Lag-CLN8 domain						domain	We previously demonstrated that substrate specificity resides in a region of ∼150 residues in the Tram-Lag-CLN8 domain.
11320094	3	46	part_of	sites	678:682	arg1	ABCR	ABCR		sites		PUBTATOR	Site	ABCR	24	sites	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
10878002	3	22	gly	residues	395:402	arg1	C-Mannosylation			tryptophan residues	C-Mannosylation					tryptophan residues	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
9786864	4	18	part_of	receptor	498:505	arg1	The extracellular domain	leptin receptor		The extracellular domain		PUBTATOR	Site	leptin receptor	3953	domain	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
18514042	1	32	gly	glycosylation	148:160	arg1	some serum proteins	some serum proteins				Fterm		proteins			Changes in the glycosylation of some serum proteins are associated with certain diseases.
21327254	6	9	part_of	Tau	1162:1164	arg1	the carboxy-terminal domains	Tau		the carboxy-terminal domains		Cterm	Site	Tau		domains	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
8193552	0	22	gly	gonadotropin	131:142	arg1	the disialylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chains	chorionic gonadotropin			the disialylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chains	OGER		chorionic gonadotropin			Structure determination of the disialylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chains of equine chorionic gonadotropin.
8193552	0	31	gly	disialylated	31:42	arg1	the disialylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chains				the disialylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chains						Structure determination of the disialylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chains of equine chorionic gonadotropin.
17542669	2	68	part_of	TSHR	300:303	arg1	the TSHR extracellular domain	TSHR		the TSHR extracellular domain		PUBTATOR	Site	TSHR	7253	domain	DESIGN: A complex of part of the TSHR extracellular domain (amino acids 1-260; TSHR260) bound to M22 Fab was prepared and purified.
7106126	3	58	gly	asparagine-linked	564:580	arg1	one asparagine-linked carbohydrate chain			asparagine	one asparagine-linked carbohydrate chain					asparagine	The fragment, comprising 47 residues, was found to contain an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain.
17330941	2	31	gly	glycopeptide	391:402	arg2	a cysteine-containing glycopeptide strategy			a cysteine-containing glycopeptide strategy						glycopeptide	To enhance our analysis of the mouse plasma proteome, we have developed a method for isolating low-abundance proteins using a cysteine-containing glycopeptide strategy.
19855092	5	49	part_of	adiponectin	851:861	arg1	adiponectin multimer composition	adiponectin		adiponectin multimer composition		PUBTATOR	Site	adiponectin	11450	position	Enzymatic removal of sialic acid or its underlying O-linked sugars did not affect adiponectin multimer composition.
21712440	8	21	part_of	peptides	1610:1617	arg1	CSF	CSF		peptides		OGER	Site	CSF		peptides	We observed an increase of up to 2.5 times of Tyr10 glycosylated Aβ peptides in CSF in six AD patients compared to seven non-AD patients.
2209609	2	79	part_of	has	339:341	arg1	The glycoprotein AND Asn271	glycoprotein		sites, Asn271 and Asn300		Fterm	AminoAcid	glycoprotein		sites, Asn271 and Asn300	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	2	79	part_of	has	339:341	arg1	The glycoprotein AND two N-glycosylation sites	glycoprotein		sites, Asn271 and Asn300		Fterm	AminoAcid	glycoprotein		sites, Asn271 and Asn300	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	2	79	part_of	has	339:341	arg1	The glycoprotein AND two N-glycosylation sites	glycoprotein		sites, Asn271 and Asn300		Fterm	AminoAcid	glycoprotein		sites, Asn271 and Asn300	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
20622017	8	41	part_of	GGT	1097:1099	arg1	hepatic GGT glycopeptides	GGT		hepatic GGT glycopeptides		OGER	Site	GGT		glycopeptides	However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT.
2243102	7	36	gly	glycosylation	1115:1127	arg2	only certain glycosylation sites			only certain glycosylation sites						sites	These results indicated that only certain glycosylation sites can be selectively modified by poly-N-acetyllactosamine, and those sites may confer the requirement by beta 1----3-N-acetylglucosaminyl transferase.
2243102	7	45	gly	modified	1154:1161	arg3	only certain glycosylation sites AND poly-N-acetyllactosamine			only certain glycosylation sites	poly-N-acetyllactosamine					sites	These results indicated that only certain glycosylation sites can be selectively modified by poly-N-acetyllactosamine, and those sites may confer the requirement by beta 1----3-N-acetylglucosaminyl transferase.
3651384	6	11	gly	N-glycosylation	897:911	arg2	six potential N-glycosylation sites			six potential N-glycosylation sites						sites	The derived SGP-2 sequence has a molecular weight of 51,379 and contains six potential N-glycosylation sites.
22556278	3	84	gly	O-Glycosylation	387:401	arg1	the 26 S proteasome ATPase subunit Rpt2	the 26 S proteasome ATPase subunit Rpt2				OGER		26 S proteasome			O-Glycosylation of the 26 S proteasome ATPase subunit Rpt2 is known to influence the stability of proteins by reducing their proteasome-dependent degradation.
2226832	3	19	gly	N-glycosylation	397:411	arg2	three N-glycosylation sites			three N-glycosylation sites						sites	It has three N-glycosylation sites, at Asn residues 100, 114 and 145.
8174273	4	32	gly	glycoprotein	1234:1245	arg1	alpha 1-antitrypsin	alpha 1-antitrypsin				PUBTATOR		alpha 1-antitrypsin	5265		Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	32	gly	glycoprotein	1234:1245	arg1	alpha 1-acid glycoprotein	alpha 1-acid glycoprotein				Fterm		glycoprotein			Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	56	gly	glycoprotein	1262:1273	arg1	alpha 2-HS glycoprotein	alpha 2-HS glycoprotein				PUBTATOR		alpha 2-HS glycoprotein	197		Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	56	gly	glycoprotein	1262:1273	arg1	alpha 1-antitrypsin	alpha 1-antitrypsin				PUBTATOR		alpha 1-antitrypsin	5265		Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	72	gly	fucosylated	1315:1325	arg1	increased fucosylated transferrin	increased fucosylated transferrin				PUBTATOR		transferrin	7018		Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
9572875	3	14	gly	glycosylated	659:670	arg1	glycosylated IGFBP-6	glycosylated IGFBP-6				PUBTATOR		IGFBP-6	3489		Electrospray ionization mass spectrometry (ESMS) of glycosylated IGFBP-6 revealed considerable heterogeneity of carbohydrate composition.
9572875	3	28	gly	heterogeneity	702:714	arg1	carbohydrate composition				carbohydrate composition						Electrospray ionization mass spectrometry (ESMS) of glycosylated IGFBP-6 revealed considerable heterogeneity of carbohydrate composition.
11081633	2	41	gly	glycoprotein	466:477	arg1	high-affinity to specific glycoprotein counterreceptors	high-affinity to specific glycoprotein counterreceptors				Fterm		glycoprotein			The selectins bind weakly to sialyl Lewisx (SLe(X))-like glycans, but with high-affinity to specific glycoprotein counterreceptors, including PSGL-1.
9530955	12	22	gly	glycoproteins	2078:2090	arg1	MUC1 glycoproteins	MUC1 glycoproteins				PUBTATOR		MUC1 glycoproteins	4582		The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	12	69	gly	underglycosylated	2112:2128	arg1	MUC1 glycoproteins	MUC1 glycoproteins				PUBTATOR		MUC1 glycoproteins	4582		The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
2040275	10	41	gly	oligosaccharide	1463:1477	arg1	a glycoprotein	glycoprotein			oligosaccharide	Fterm		glycoprotein			Thus, the conformational space available to an N-linked oligosaccharide in a glycoprotein relative to the protein may depend to a large extent upon the flexibility of the asparagine side chain.
2040275	10	56	gly	glycoprotein	1484:1495	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Thus, the conformational space available to an N-linked oligosaccharide in a glycoprotein relative to the protein may depend to a large extent upon the flexibility of the asparagine side chain.
21148085	0	52	gly	factor-D	55:62	arg1	Structural determinants	vascular endothelial growth factor-D			Structural determinants	PUBTATOR		vascular endothelial growth factor-D	2277		Structural determinants of vascular endothelial growth factor-D receptor binding and specificity.
19838169	1	23	gly	glycoproteins	119:131	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			We present a method to enrich for glycoproteins from proteomic samples.
20406422	2	27	part_of	N371	453:456	arg1	CLN7	CLN7		N371		PUBTATOR	SpecificSite	CLN7	256471	N371 and N376	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	30	part_of	N376	462:465	arg1	CLN7	CLN7		N376		PUBTATOR	SpecificSite	CLN7	256471	N371 and N376	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	33	part_of	CLN7	400:403	arg1	two N-glycosylation sites	CLN7		two N-glycosylation sites		PUBTATOR	Site	CLN7	256471	sites	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	33	part_of	CLN7	400:403	arg1	C-terminal tails	CLN7		C-terminal tails		PUBTATOR	Site	CLN7	256471	tails	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
17563389	1	65	part_of	has	226:228	arg1	neurokinin 1 receptor AND Asn-14	neurokinin 1 receptor		sites, Asn-14 and Asn-18		PUBTATOR	SpecificSite	neurokinin 1 receptor	6869	sites, Asn-14 and Asn-18	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	part_of	has	226:228	arg1	neurokinin 1 receptor AND Asn-18	neurokinin 1 receptor		sites, Asn-14 and Asn-18		PUBTATOR	SpecificSite	neurokinin 1 receptor	6869	sites, Asn-14 and Asn-18	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	part_of	has	226:228	arg1	neurokinin 1 receptor AND Asn-18	neurokinin 1 receptor		sites, Asn-14 and Asn-18		PUBTATOR	SpecificSite	neurokinin 1 receptor	6869	sites, Asn-14 and Asn-18	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	part_of	has	226:228	arg1	NK1R AND Asn-14	NK1R		sites, Asn-14 and Asn-18		PUBTATOR	SpecificSite	NK1R	6869	sites, Asn-14 and Asn-18	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	part_of	has	226:228	arg1	NK1R AND Asn-18	NK1R		sites, Asn-14 and Asn-18		PUBTATOR	SpecificSite	NK1R	6869	sites, Asn-14 and Asn-18	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	part_of	has	226:228	arg1	NK1R AND Asn-18	NK1R		sites, Asn-14 and Asn-18		PUBTATOR	SpecificSite	NK1R	6869	sites, Asn-14 and Asn-18	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	part_of	has	226:228	arg1	a G protein-coupled receptor AND Asn-14	receptor		sites, Asn-14 and Asn-18		Fterm	SpecificSite	receptor		sites, Asn-14 and Asn-18	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	part_of	has	226:228	arg1	a G protein-coupled receptor AND Asn-18	receptor		sites, Asn-14 and Asn-18		Fterm	SpecificSite	receptor		sites, Asn-14 and Asn-18	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	part_of	has	226:228	arg1	a G protein-coupled receptor AND Asn-18	receptor		sites, Asn-14 and Asn-18		Fterm	SpecificSite	receptor		sites, Asn-14 and Asn-18	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
18930737	0	14	gly	alpha2-glycoprotein	59:77	arg1	ZAG	ZAG				PUBTATOR		ZAG	563		Crystal structure of the novel complex formed between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human seminal plasma.
18930737	0	14	gly	alpha2-glycoprotein	59:77	arg1	zinc alpha2-glycoprotein	zinc alpha2-glycoprotein				PUBTATOR		zinc alpha2-glycoprotein	563		Crystal structure of the novel complex formed between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human seminal plasma.
18065761	0	66	gly	domain	85:90	arg1	Heparin-induced cis- and trans-dimerization modes			domain	Heparin-induced cis- and trans-dimerization modes					domain	Heparin-induced cis- and trans-dimerization modes of the thrombospondin-1 N-terminal domain.
11152678	1	1	part_of	neurotrophic	186:197	arg1	pro-BDNF	brain-derived neurotrophic factor precursor		pro-BDNF		PUBTATOR	AminoAcid	brain-derived neurotrophic factor precursor	627	pro	We examined the biosynthesis and post-translational processing of the brain-derived neurotrophic factor precursor (pro-BDNF) in cells infected with a pro-BDNF-encoding vaccinia virus.
11152678	1	3	part_of	factor	199:204	arg1	pro-BDNF	brain-derived neurotrophic factor precursor		pro-BDNF		PUBTATOR	AminoAcid	brain-derived neurotrophic factor precursor	627	pro	We examined the biosynthesis and post-translational processing of the brain-derived neurotrophic factor precursor (pro-BDNF) in cells infected with a pro-BDNF-encoding vaccinia virus.
11152678	1	51	part_of	brain-derived	172:184	arg1	pro-BDNF	brain-derived neurotrophic factor precursor		pro-BDNF		PUBTATOR	AminoAcid	brain-derived neurotrophic factor precursor	627	pro	We examined the biosynthesis and post-translational processing of the brain-derived neurotrophic factor precursor (pro-BDNF) in cells infected with a pro-BDNF-encoding vaccinia virus.
23234360	1	67	part_of	proteins	181:188	arg1	Ser/Thr residues	proteins		Ser/Thr residues		Fterm	Site	proteins		residues	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
8702538	9	35	part_of	CD33	1546:1549	arg1	the first Ig domain	CD33		the first Ig domain		PUBTATOR	Site	CD33	945	domain	In contrast, mutation of a NCS motif in the first Ig domain of the I-type lectin CD33 unmasked its sialic acid binding activity.
8702538	9	73	part_of	NCS	1492:1494	arg1	a NCS motif	NCS		a NCS motif		OGER	Site	NCS		motif	In contrast, mutation of a NCS motif in the first Ig domain of the I-type lectin CD33 unmasked its sialic acid binding activity.
24721674	11	25	part_of	proteins	2162:2169	arg1	811 N-glycosylation sites	proteins		811 N-glycosylation sites		Fterm	Site	proteins		sites	Totally 811 N-glycosylation sites from 567 proteins were identified and 177 intact glycopeptides with both glycan composition and peptides sequence were characterized, which provided a solution for site-specific N-glycosylation characterization of membrane.
10644446	4	28	part_of	460-amino-acid	444:457	arg1	a 460-amino-acid polypeptide	460-amino-acid		a 460-amino-acid polypeptide		Cterm	Site	460-amino-acid		polypeptide	Human ANGPTL3 is a 460-amino-acid polypeptide with the characteristic structure of angiopoietins: a signal peptide, an extended helical domain predicted to form dimeric or trimeric coiled-coils, a short linker peptide, and a globular fibrinogen homology domain (FHD).
10644446	4	43	part_of	Human	425:429	arg1	a 460-amino-acid polypeptide	Human ANGPTL3		a 460-amino-acid polypeptide		PUBTATOR	Site	Human ANGPTL3	27329	polypeptide	Human ANGPTL3 is a 460-amino-acid polypeptide with the characteristic structure of angiopoietins: a signal peptide, an extended helical domain predicted to form dimeric or trimeric coiled-coils, a short linker peptide, and a globular fibrinogen homology domain (FHD).
19683538	6	24	gly	glycoprotein	1071:1082	arg1	the alpha-NAGAL glycoprotein	the alpha-NAGAL glycoprotein				Cterm		alpha-NAGAL glycoprotein	4668		To better understand how individual defects in the alpha-NAGAL glycoprotein lead to Schindler disease, we analyzed the effect of disease-causing mutations on the three-dimensional structure.
29741879	2	108	gly	glycoproteins	413:425	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Despite the vital role of glycosylation for proper protein function, the analysis of glycoproteins has been lagged behind to other protein modifications.
8407880	6	51	gly	HGF	1030:1032	arg1	the N-linked oligosaccharides	HGF			the N-linked oligosaccharides	PUBTATOR		HGF	24446		The structures of the N-linked oligosaccharides from rat HGF were also studied.
9295302	6	39	gly	deglycosylation	887:901	arg1	intact MRP	intact MRP				PUBTATOR		MRP	4363		Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
8172892	7	61	gly	NeuNAc-Gal-GalNAc-Thr	1276:1296	arg1	NeuNAc-Gal-GalNAc-Thr structures			Thr	NeuNAc-Gal-GalNAc-Thr structures					Thr	Fast atom bombardment tandem mass spectrometric analysis of AP alpha-D4 suggested the existence of Gal-GalNAc-Thr, NeuNAc-(Gal-)GalNAc-Thr, and NeuNAc-Gal-GalNAc-Thr structures.
23242014	9	68	gly	glycopeptides	1347:1359	arg1	Thr396			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	68	gly	glycopeptides	1347:1359	arg1	Thr473			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	68	gly	glycopeptides	1347:1359	arg1	Thr518			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	68	gly	glycopeptides	1347:1359	arg1	Ser401			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr518			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser401			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser404			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr396			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr473			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	68	gly	glycopeptides	1347:1359	arg1	Thr473			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	68	gly	glycopeptides	1347:1359	arg1	Thr518			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	68	gly	glycopeptides	1347:1359	arg1	Ser401			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr518			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser401			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser404			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr396			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr473			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	68	gly	glycopeptides	1347:1359	arg1	Thr518			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	68	gly	glycopeptides	1347:1359	arg1	Ser401			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr518			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser401			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser404			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr396			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr473			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	68	gly	glycopeptides	1347:1359	arg1	Ser401			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr518			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser401			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser404			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr396			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr473			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	isolated glycopeptides			glycopeptides						glycopeptides	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr518			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser401			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser404			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr396			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr473			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser401			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser404			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr396			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr473			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Ser404			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr396			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr473			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr396			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr473			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
23242014	9	74	gly	glycopeptides	1347:1359	arg2	Thr473			Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518						Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518	Using nano-liquid chromatography and tandem mass spectrometry approaches, we clearly have identified six residues for O-linked glycosylation within isolated glycopeptides (Ser393, Thr396, Ser401, Ser404, Thr473 and Thr518), carrying mainly Core 1 and Core 2 mucin-type structures.
18676855	5	16	part_of	NGEP	1014:1017	arg1	COOH termini	NGEP		COOH termini		PUBTATOR	Site	NGEP	Q6IWH7	termini	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	5	53	part_of	domains	966:972	arg1	COOH termini	domains		COOH termini						termini	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	5	3	part_of	contains	937:944	arg1	NGEP AND eight transmembrane domains	NGEP		eight transmembrane domains		PUBTATOR	Site	NGEP	Q6IWH7	domains	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
16740002	7	15	gly	glycosylation	1085:1097	arg2	44 new sites			44 new sites						sites	In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
14699159	8	16	gly	N-glycosylation	1559:1573	arg2	single or multiple N-glycosylation sites			single or multiple N-glycosylation sites						sites	Additional analysis of p90ATF6 mutants targeting single or multiple N-glycosylation sites also showed higher constitutive transactivating activity than wild type ATF6.
22159084	12	65	gly	deglycosylated	1521:1534	arg1	deglycosylated SLC26A3	deglycosylated SLC26A3				PUBTATOR		SLC26A3	1811		While the mature glycosylated SLC26A3 showed little breakdown after treatment with trypsin, deglycosylated SLC26A3 exhibited increased susceptibility to trypsin, suggesting that the oligosaccharides protect SLC26A3 from tryptic digestion.
22159084	12	68	gly	glycosylated	1446:1457	arg1	the mature glycosylated SLC26A3	the mature glycosylated SLC26A3				PUBTATOR		SLC26A3	1811		While the mature glycosylated SLC26A3 showed little breakdown after treatment with trypsin, deglycosylated SLC26A3 exhibited increased susceptibility to trypsin, suggesting that the oligosaccharides protect SLC26A3 from tryptic digestion.
17027507	3	30	part_of	factor	461:466	arg1	the von Willebrand factor A-type domains	von Willebrand factor A-type		the von Willebrand factor A-type domains		OGER	Site	von Willebrand factor A-type	P04275	domains	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	3	33	part_of	A-type	468:473	arg1	the von Willebrand factor A-type domains	von Willebrand factor A-type		the von Willebrand factor A-type domains		OGER	Site	von Willebrand factor A-type	P04275	domains	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
1998667	1	47	gly	glycoprotein	124:135	arg1	Factor XI	Factor XI				OGER		Factor XI	P03951		Factor XI is a plasma glycoprotein that participates in the blood coagulation cascade.
1998667	1	47	gly	glycoprotein	124:135	arg1	a plasma glycoprotein	a plasma glycoprotein				Fterm		glycoprotein			Factor XI is a plasma glycoprotein that participates in the blood coagulation cascade.
20356926	6	29	gly	glycosylation	633:645	arg1	CREB-H	CREB-H				PUBTATOR		CREB-H	84699		Disruption of all three sites by site-directed mutagenesis completely abrogated N-linked glycosylation of CREB-H.
17082223	2	16	gly	glycosylation	458:470	arg2	putative glycosylation sites			putative glycosylation sites						sites	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	36	gly	sites	472:476	arg1	putative glycosylation sites			putative glycosylation sites						sites	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	16	gly	glycosylation	458:470	arg2	Asn(109)			Asn(109), Asn(116), Asn(122), and Asn(125)						Asn(109), Asn(116), Asn(122), and Asn(125)	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	16	gly	glycosylation	458:470	arg2	Asn(116)			Asn(109), Asn(116), Asn(122), and Asn(125)						Asn(109), Asn(116), Asn(122), and Asn(125)	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	16	gly	glycosylation	458:470	arg2	Asn(125)			Asn(109), Asn(116), Asn(122), and Asn(125)						Asn(109), Asn(116), Asn(122), and Asn(125)	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	16	gly	glycosylation	458:470	arg2	Asn(116)			Asn(109), Asn(116), Asn(122), and Asn(125)						Asn(109), Asn(116), Asn(122), and Asn(125)	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	16	gly	glycosylation	458:470	arg2	Asn(125)			Asn(109), Asn(116), Asn(122), and Asn(125)						Asn(109), Asn(116), Asn(122), and Asn(125)	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	16	gly	glycosylation	458:470	arg2	Asn(125)			Asn(109), Asn(116), Asn(122), and Asn(125)						Asn(109), Asn(116), Asn(122), and Asn(125)	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	36	gly	sites	472:476	arg1	Asn(122)			Asn(109), Asn(116), Asn(122), and Asn(125)						Asn(109), Asn(116), Asn(122), and Asn(125)	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	36	gly	sites	472:476	arg1	Asn(116)			Asn(109), Asn(116), Asn(122), and Asn(125)						Asn(109), Asn(116), Asn(122), and Asn(125)	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	36	gly	sites	472:476	arg1	Asn(109)			Asn(109), Asn(116), Asn(122), and Asn(125)						Asn(109), Asn(116), Asn(122), and Asn(125)	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	36	gly	sites	472:476	arg1	Asn(116)			Asn(109), Asn(116), Asn(122), and Asn(125)						Asn(109), Asn(116), Asn(122), and Asn(125)	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	36	gly	sites	472:476	arg1	Asn(109)			Asn(109), Asn(116), Asn(122), and Asn(125)						Asn(109), Asn(116), Asn(122), and Asn(125)	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	36	gly	sites	472:476	arg1	Asn(109)			Asn(109), Asn(116), Asn(122), and Asn(125)						Asn(109), Asn(116), Asn(122), and Asn(125)	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
15102839	6	23	part_of	enzyme	1443:1448	arg1	the active site	enzyme		the active site		Fterm	Site	enzyme		site	In contrast to an analogous complex previously isolated for Saccharomyces cerevisiae ER mannosidase I, the oligosaccharide in the active site of the murine Golgi enzyme assumes a different conformation to present an alternate oligosaccharide branch into the active site pocket.
10677208	0	7	gly	linked	31:36	arg2	the conserved N-glycosylation site AND Hybrid and complex glycans			the conserved N-glycosylation site	Hybrid and complex glycans					site	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	7	gly	linked	31:36	arg1	the third eight-cysteine domain AND Hybrid and complex glycans			the third eight-cysteine domain	Hybrid and complex glycans					cysteine domain	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	30	gly	N-glycosylation	55:69	arg1	the third eight-cysteine domain			cysteine domain						cysteine domain	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	30	gly	N-glycosylation	55:69	arg1	LTBP-1	LTBP-1		cysteine domain		OGER		LTBP-1	Q14766	cysteine domain	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	30	gly	N-glycosylation	55:69	arg1	LTBP-1	LTBP-1		cysteine domain		OGER		LTBP-1	Q14766	cysteine domain	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	30	gly	N-glycosylation	55:69	arg2	the conserved N-glycosylation site	LTBP-1		site		OGER		LTBP-1	Q14766	site	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
6619128	6	72	gly	oligosaccharide	709:723	arg1	the hinge region			the hinge region	the hinge region		Site			region	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
29490423	6	40	part_of	CD19	996:999	arg1	the extracellular domain	CD19		the extracellular domain		PUBTATOR	Site	CD19	930	domain	Rather than a tandem of c-type immunoglobulin folds predicted from the amino acid sequence, the extracellular domain of CD19 exhibits an elongated β-sandwich formed by two immunoglobulin folds by swapping their C-terminal halves.
7642555	9	10	part_of	c-Myc	1120:1124	arg1	threonine 58	c-Myc		threonine 58		PUBTATOR	SpecificSite	c-Myc	4609	threonine 58	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
25517345	2	22	gly	present	284:290	arg1	viral glycoproteins AND specific glycans	viral glycoproteins			specific glycans	Fterm		glycoproteins			Different carbohydrate-binding agents (CBAs) target specific glycans present on viral glycoproteins of enveloped viruses.
25517345	2	56	gly	glycoproteins	301:313	arg1	viral glycoproteins	viral glycoproteins				Fterm		glycoproteins			Different carbohydrate-binding agents (CBAs) target specific glycans present on viral glycoproteins of enveloped viruses.
16043704	2	16	gly	leucine-rich	352:363	arg1	leucine-rich repeats			leucine	leucine-rich repeats					leucine	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
11676606	2	26	part_of	CD40	321:324	arg1	the CD40 binding site	CD40		the CD40 binding site		PUBTATOR	Site	CD40	P25942	site	Previous studies have described the CD40 binding site as a shallow groove formed between two monomers of CD154.
1445902	5	11	gly	nonglycosylated	877:891	arg1	(2) Asn-86				(2) Asn-86						These studies provided evidence that (1) Asn-16 is heterogeneously glycosylated with four different oligosaccharides, (2) Asn-86 is either nonglycosylated or has attached to it one oligosaccharide, (3) the N-glycosylation sites Asn-44 and Asn-51 are not glycosylated, and (4) there is no O-glycosylation.
1445902	5	74	gly	glycosylated	805:816	arg1	(1) Asn-16				(1) Asn-16						These studies provided evidence that (1) Asn-16 is heterogeneously glycosylated with four different oligosaccharides, (2) Asn-86 is either nonglycosylated or has attached to it one oligosaccharide, (3) the N-glycosylation sites Asn-44 and Asn-51 are not glycosylated, and (4) there is no O-glycosylation.
1445902	5	78	gly	glycosylated	992:1003	arg1	the N-glycosylation sites Asn-44 and Asn-51				the N-glycosylation sites Asn-44 and Asn-51						These studies provided evidence that (1) Asn-16 is heterogeneously glycosylated with four different oligosaccharides, (2) Asn-86 is either nonglycosylated or has attached to it one oligosaccharide, (3) the N-glycosylation sites Asn-44 and Asn-51 are not glycosylated, and (4) there is no O-glycosylation.
1445902	5	78	gly	glycosylated	992:1003	arg1	Asn-51				Asn-51						These studies provided evidence that (1) Asn-16 is heterogeneously glycosylated with four different oligosaccharides, (2) Asn-86 is either nonglycosylated or has attached to it one oligosaccharide, (3) the N-glycosylation sites Asn-44 and Asn-51 are not glycosylated, and (4) there is no O-glycosylation.
1445902	5	78	gly	glycosylated	992:1003	arg1	Asn-44				Asn-44						These studies provided evidence that (1) Asn-16 is heterogeneously glycosylated with four different oligosaccharides, (2) Asn-86 is either nonglycosylated or has attached to it one oligosaccharide, (3) the N-glycosylation sites Asn-44 and Asn-51 are not glycosylated, and (4) there is no O-glycosylation.
17286803	0	72	gly	glycoprotein	44:55	arg1	the CLN3 membrane glycoprotein	the CLN3 membrane glycoprotein				Fterm		glycoprotein			C-terminal prenylation of the CLN3 membrane glycoprotein is required for efficient endosomal sorting to lysosomes.
27922006	0	49	gly	glycoprotein	38:49	arg1	myelin-associated glycoprotein adhesion	myelin-associated glycoprotein adhesion				PUBTATOR		myelin-associated glycoprotein	4099		Structural basis of myelin-associated glycoprotein adhesion and signalling.
8636209	12	50	gly	glycosylation	1531:1543	arg1	CD3 delta	CD3 delta				PUBTATOR		CD3 delta	915		Furthermore, the study indicated that, in contrast to CD3 gamma, glycosylation of CD3 delta is required for TCR assembly and expression.
8636209	12	50	gly	glycosylation	1531:1543	arg1	TCR assembly	TCR assembly				PUBTATOR		TCR	6962		Furthermore, the study indicated that, in contrast to CD3 gamma, glycosylation of CD3 delta is required for TCR assembly and expression.
14660577	6	53	part_of	XIV	1001:1003	arg1	the extracellular domain	CA XIV		the extracellular domain		PUBTATOR	Site	CA XIV	23831	domain	We also report the crystal structure of the extracellular domain of murine CA XIV at 2.8 A resolution and of an enzyme-acetazolamide complex at 2.9 A resolution.
9013598	7	21	gly	glycosylation	1222:1234	arg2	these glycosylation sites			these glycosylation sites						sites	Only one of these glycosylation sites had a counterpart in tACE.
1512232	12	22	part_of	region	2133:2138	arg1	All the glycosylation sites	region		All the glycosylation sites						sites	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
9786864	8	57	gly	glycosylated	1256:1267	arg1	the N-terminal WSXWS motif			motif						motif	On the other hand, the N-terminal WSXWS motif was not glycosylated.
17576745	5	11	part_of	N-terminal	837:846	arg1	the N-terminal fragment	N-terminal		the N-terminal fragment		Cterm	Site	N-terminal		fragment	We demonstrate that GPR56 protein undergoes two major modifications, GPS domain-mediated protein cleavage and N-glycosylation, and that the N-terminal fragment can be released from the cell surface.
22688517	5	67	part_of	LOX-1	995:999	arg1	their corresponding attached site	LOX-1		their corresponding attached site		PUBTATOR	Site	LOX-1	4973	site	Here, an approach using nonspecific protease (Pronase E) digestion followed by MALDI-QIT-TOF MS and multistage MS (MS(3)) analysis is explored to obtain site-specific N-glycosylation information of recombinant human LOX-1, in combination with glycan structure confirmation through characterizing released glycans using tandem MS. The results reveal that N-glycans structures as well as their corresponding attached site of LOX-1 can be identified simultaneously by direct MS analysis of glycopeptides from non-specific protease digestion.
20729549	2	59	gly	phosphoglycoproteins	245:264	arg1	an important determinant	phosphoglycoproteins			an important determinant	Fterm		phosphoglycoproteins			Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
1991473	7	62	gly	N-glycans	1040:1048	arg1	the beta subunit	subunit			N-glycans	Fterm		subunit			However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
21676880	1	31	gly	N-Glycosylation	133:147	arg1	membrane proteins	membrane proteins				Fterm		proteins			N-Glycosylation of membrane proteins is critical for their proper folding, co-assembly and subsequent matriculation through the secretory pathway.
16263699	7	80	gly	deglycosylated	1046:1059	arg1	deglycosylated peptides			deglycosylated peptides						peptides	Derivatization by peptide:N-glycosidase F yielded deglycosylated peptides, which provided the basis for the elucidation of proteins and their sites of modification.
15454184	0	57	gly	glycosylation	26:38	arg1	recombinant human follistatin	recombinant human follistatin				PUBTATOR		follistatin	10468		Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
1457969	0	25	part_of	sites	67:71	arg1	human thyrotrophin	thyrotrophin		sites		Fterm	Site	thyrotrophin		sites	The asparagine-linked oligosaccharides at individual glycosylation sites in human thyrotrophin.
2547792	2	63	part_of	alpha-MSH	263:271	arg1	D-phenylalanine7	MSH		D-phenylalanine7		PUBTATOR	AminoAcid	MSH	17701	phenylalanine7	The melanotropin (MSH) receptor of mouse B16-F1 melanoma cells was characterized by photoaffinity cross-linking, using a potent alpha-MSH photolabel, [norleucine4, D-phenylalanine7, 1'-(2-nitro-4-azidophenylsulfenyl)-tryptophan9]-alpha-melanotropin (Naps-MSH).
3497198	9	34	gly	monosialylated	1267:1280	arg1	the monosialylated structures				the monosialylated structures						For H-2Kk, it had no effect on sialylation, but resulted in a slight under galactosylation of the monosialylated structures at both sites.
3840370	13	44	gly	2-glycoprotein	1955:1968	arg1	the non-complement beta 2-glycoprotein I	the non-complement beta 2-glycoprotein I				OGER		beta 2-glycoprotein I	P02749		These regions in C4b-binding protein are homologous with the three internal-homology regions that have been reported to be present within the Ba region of the complement enzyme factor B and also to the internal-homology regions found in the non-complement beta 2-glycoprotein I.
26902720	0	22	gly	glycoprotein	80:91	arg1	a serum glycoprotein afamin/α-albumin	a serum glycoprotein afamin/α-albumin				Fterm		glycoprotein			Active and water-soluble form of lipidated Wnt protein is maintained by a serum glycoprotein afamin/α-albumin.
1544894	7	2	part_of	VII	1141:1143	arg1	the first EGF domain	factor VII		the first EGF domain		OGER	Site	factor VII	P08709	domain	It has been recently reported that the first EGF domain of human factor VII has O-linked fucose at the equivalent position (Ser-60) (Bjoern, S., Foster, D. C., Thim, L., Wiberg, F. C., Christensen, M., Komiyama, Y., Pedersen, A. H., and Kisiel, W. (1991) J. Biol.
1544894	7	27	part_of	EGF	1114:1116	arg1	the first EGF domain	EGF		the first EGF domain		OGER	Site	EGF	P01133	domain	It has been recently reported that the first EGF domain of human factor VII has O-linked fucose at the equivalent position (Ser-60) (Bjoern, S., Foster, D. C., Thim, L., Wiberg, F. C., Christensen, M., Komiyama, Y., Pedersen, A. H., and Kisiel, W. (1991) J. Biol.
16422668	4	32	part_of	CH1	715:717	arg1	the CH1 domain	CH1		the CH1 domain		OGER	Site	CH1	Q9UBS9	domain	The three-dimensional structure of the branched N-linked oligosaccharide associated with the CH1 domain (first constant domain of heavy chain) is reported.
8404899	0	37	gly	glycosylation	17:29	arg1	human pancreatic bile-salt-dependent lipase	human pancreatic bile-salt-dependent lipase				Fterm		lipase			Variation of the glycosylation of human pancreatic bile-salt-dependent lipase.
3934016	1	9	gly	N-glycosylation	336:350	arg2	potential sites			potential sites						sites	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	1	45	gly	asparagine-linked	219:235	arg1	asparagine-linked oligosaccharide units			asparagine	asparagine-linked oligosaccharide units					asparagine	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
479158	12	35	gly	glycopeptide	1084:1095	arg2	Another glycopeptide unit			Another glycopeptide unit						glycopeptide	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
20332087	4	38	gly	presence	619:626	arg2	positions 323, 355, 391, 483, 729 AND five N-glycans			positions 323, 355, 391, 483, 729	five N-glycans					positions 323, 355, 391, 483, 729	Analyses showed the presence of five N-glycans at positions 323, 355, 391, 483, 729 in both proteins.
10861210	12	9	part_of	site	1608:1611	arg1	human AE1	AE1		site		PUBTATOR	Site	AE1	6521	site	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
14658030	2	42	gly	presence	609:616	arg1	specific sites AND glycans			specific sites	glycans					sites	For glycosylation, it has been increasingly recognized to be of pivotal importance to identify whether potential glycosylation sites are actually modified by glycans, because functions of proteins may be modulated or depend on the presence of glycans at specific sites.
14658030	2	63	gly	modified	524:531	arg3	potential glycosylation sites AND glycans			potential glycosylation sites	glycans					sites	For glycosylation, it has been increasingly recognized to be of pivotal importance to identify whether potential glycosylation sites are actually modified by glycans, because functions of proteins may be modulated or depend on the presence of glycans at specific sites.
14658030	2	75	gly	glycosylation	491:503	arg2	potential glycosylation sites			potential glycosylation sites						sites	For glycosylation, it has been increasingly recognized to be of pivotal importance to identify whether potential glycosylation sites are actually modified by glycans, because functions of proteins may be modulated or depend on the presence of glycans at specific sites.
1997323	12	61	gly	sequence	1450:1457	arg1	the sequence: Neu5Ac(alpha 2-3)Gal(beta 1-3)GlcNAc(beta 1-2)Man				the sequence: Neu5Ac(alpha 2-3)Gal(beta 1-3)GlcNAc(beta 1-2)Man						In addition, the alpha-1,6-Man-linked antenna deviated in rTf-2 from the standard structure by having the sequence: Neu5Ac(alpha 2-3)Gal(beta 1-3)GlcNAc(beta 1-2)Man.
1281977	3	37	gly	glycopeptides	369:381	arg2	these glycopeptides			these glycopeptides						glycopeptides	A lesser accumulation of these glycopeptides is seen in the kidney and brain, and they are also excreted in the urine.
3427055	0	84	gly	glycoprotein	115:126	arg1	SPARC/BM-40/osteonectin	SPARC/BM-40/osteonectin				PUBTATOR		BM-40	6678		Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues.
3427055	0	84	gly	glycoprotein	115:126	arg1	an extracellular glycoprotein	an extracellular glycoprotein				Fterm		glycoprotein			Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues.
25419660	2	55	part_of	residues	282:289	arg1	some collagenous proteins	proteins		residues		Fterm	AminoAcid	proteins		lysine residues	The LH3 has been shown to modify the lysine residues both in collagens and also in some collagenous proteins.
16877748	1	4	gly	N-glycosylated	204:217	arg1	Intercellular adhesion molecule-1	Intercellular adhesion molecule-1				PUBTATOR		Intercellular adhesion molecule-1	15894		Intercellular adhesion molecule-1 (ICAM-1) is a heavily N-glycosylated transmembrane protein comprising five extracellular Ig-like domains.
16877748	1	4	gly	N-glycosylated	204:217	arg1	a heavily N-glycosylated transmembrane protein	a heavily N-glycosylated transmembrane protein				Fterm		protein			Intercellular adhesion molecule-1 (ICAM-1) is a heavily N-glycosylated transmembrane protein comprising five extracellular Ig-like domains.
7925474	3	78	gly	glycoprotein	402:413	arg1	FA1	FA1				PUBTATOR		FA1	8788		FA1 is a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues.
7925474	3	78	gly	glycoprotein	402:413	arg1	a single-chained, heterogeneous glycoprotein	a single-chained, heterogeneous glycoprotein				Fterm		glycoprotein			FA1 is a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues.
17293352	0	105	gly	alpha-glucosidase	36:52	arg1	N-glycans	alpha-glucosidase			N-glycans	Fterm		alpha-glucosidase			N-glycans of recombinant human acid alpha-glucosidase expressed in the milk of transgenic rabbits.
8407880	4	41	part_of	Asn535	811:816	arg1	the alpha-chain	alpha-chain		Asn535		Fterm	AminoAcid	alpha-chain		Asn535 and Asn622	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	4	41	part_of	Asn535	811:816	arg1	the beta-chain	beta-chain		Asn535		Fterm	AminoAcid	beta-chain		Asn535 and Asn622	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	4	45	part_of	Asn622	822:827	arg1	the alpha-chain	alpha-chain		Asn622		Fterm	AminoAcid	alpha-chain		Asn535 and Asn622	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	4	45	part_of	Asn622	822:827	arg1	the beta-chain	beta-chain		Asn622		Fterm	AminoAcid	beta-chain		Asn535 and Asn622	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
18420026	5	14	gly	O-glycosylation	1240:1254	arg2	no O-glycosylation site			no O-glycosylation site						site	There was no O-glycosylation site in either human NECL1 or mouse Necl1.
18586680	7	15	part_of	N-terminal	1147:1156	arg1	the N-terminal and C-terminal caspase fragments	N-terminal		the N-terminal and C-terminal caspase fragments		Cterm	Site	N-terminal		fragments	Furthermore, when co-expressed simultaneously in the same cell, the N-terminal and C-terminal caspase fragments associate to reconstitute O-GlcNAcase enzymatic activity.
24308486	3	10	gly	N-glycosylation	723:737	arg2	all seven potential N-glycosylation sites			all seven potential N-glycosylation sites						sites	The heavy chains were isolated and digested with either trypsin, proteinase K, or chymotrypsin, which permitted coverage of all seven potential N-glycosylation sites.
15809306	6	22	part_of	enzyme	1029:1034	arg1	the active site	enzyme		the active site		Fterm	Site	enzyme		site	Comparison of the crystal structures of FAPalpha and DPPIV revealed one major difference in the vicinity of the Glu motif (Glu(203)-Glu(204) for FAPalpha; Glu(205)-Glu(206) for DPPIV) within the active site of the enzyme.
16497731	3	34	part_of	adiponectin	489:499	arg1	Multimer composition	adiponectin		Multimer composition		PUBTATOR	Site	adiponectin	9370	position	Multimer composition of adiponectin appears to be regulated; however, the molecular mechanisms involved are unknown.
23319596	10	28	part_of	LOX	1630:1632	arg1	the LOX catalytic domain	LOX		the LOX catalytic domain		PUBTATOR	Site	LOX	4015	domain	These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.
8326911	5	70	gly	sialylated	677:686	arg1	di-				di-						O-linked structures included a di- and tetrasaccharide core structure that were in addition sialylated and may be similar to structures found in fetuin.
8326911	5	70	gly	sialylated	677:686	arg1	tetrasaccharide core structure				tetrasaccharide core structure						O-linked structures included a di- and tetrasaccharide core structure that were in addition sialylated and may be similar to structures found in fetuin.
32363391	2	29	gly	glycosylated	380:391	arg1	The coronavirus spike (S) protein	The coronavirus spike (S) protein				OGER		S) protein	P04004		The coronavirus spike (S) protein, which facilitates viral attachment, entry and membrane fusion is heavily glycosylated and plays a critical role in the elicitation of the host immune response.
8702538	5	108	gly	glycosylation	841:853	arg2	potential N-linked glycosylation sites			potential N-linked glycosylation sites						sites	In this work we have performed site-specific mutagenesis of potential N-linked glycosylation sites on CD22 in an effort to determine whether they might be involved in ligand recognition.
25456591	9	44	gly	glycosylation	1623:1635	arg2	the same glycosylation sites			the same glycosylation sites						sites	The FDR decreased from 33% to 3.3% by ΔRt filtering and exclusion of repeated peptide tags that covered the same glycosylation sites.
27462106	1	21	gly	glycoprotein	209:220	arg1	the host cell endoplasmic reticulum (ER) glycoprotein quality control (QC) machinery	the host cell endoplasmic reticulum (ER) glycoprotein quality control (QC) machinery				Fterm		glycoprotein			The biosynthesis of enveloped viruses depends heavily on the host cell endoplasmic reticulum (ER) glycoprotein quality control (QC) machinery.
21500857	8	14	gly	AP180	988:992	arg1	GlcNAc-P	AP180			GlcNAc-P	PUBTATOR		AP180	65178		Analysis of synthetic GlcNAc-6-P produced identical fragmentation products to GlcNAc-P from AP180.
24334224	2	54	gly	glycosylation	489:501	arg1	rhG-CSF	rhG-CSF				OGER		CSF			Using liquid chromatography and tandem mass spectrometry techniques, we analyzed the O-linked glycosylation of recombinant human granulocyte colony-stimulating factor (rhG-CSF) derived from glycoengineered Pichia pastoris with regard to its nature, structure, occupancy, and location.
24334224	2	54	gly	glycosylation	489:501	arg1	recombinant human granulocyte colony-stimulating factor	recombinant human granulocyte colony-stimulating factor				PUBTATOR		granulocyte colony-stimulating factor	1440		Using liquid chromatography and tandem mass spectrometry techniques, we analyzed the O-linked glycosylation of recombinant human granulocyte colony-stimulating factor (rhG-CSF) derived from glycoengineered Pichia pastoris with regard to its nature, structure, occupancy, and location.
1577715	7	83	gly	glycoprotein	1057:1068	arg1	this glycoprotein	this glycoprotein				Fterm		glycoprotein			In the present study, this glycoprotein was shown to contain mono- (0.4% of the total oligosaccharides), bi-(78.2%), tri- (12.3%), and tetraantennary (2.3%) complex type oligosaccharides in addition to a series of high mannose type oligosaccharides, Man6-9GlcNAc2 (0.8%).
18703501	7	48	gly	glycosylation	1295:1307	arg2	Asn(309)			Asn(309)						Asn(309)	Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures.
18703501	7	48	gly	glycosylation	1295:1307	arg2	a unique N-linked glycosylation site			a unique N-linked glycosylation site						site	Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures.
18703501	7	69	gly	bears	1330:1334	arg1	Asn(309) AND high mannose-type glycan structures			Asn(309)	high mannose-type glycan structures					Asn(309)	Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures.
18703501	7	69	gly	bears	1330:1334	arg1	a unique N-linked glycosylation site AND high mannose-type glycan structures			a unique N-linked glycosylation site	high mannose-type glycan structures					site	Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures.
7263706	3	5	part_of	contains	591:598	arg1	The gamma-subunit AND 233 amino acid residues	The gamma-subunit		233 amino acid residues		Fterm	Site	gamma-subunit		residues	The gamma-subunit, a serine protease with arginine specificity, contains 233 amino acid residues and shares sequence homology with other proteases of this family.
7263706	3	5	part_of	contains	591:598	arg1	a serine protease AND 233 amino acid residues	a serine protease		233 amino acid residues		Fterm	Site	protease		residues	The gamma-subunit, a serine protease with arginine specificity, contains 233 amino acid residues and shares sequence homology with other proteases of this family.
18775496	1	45	gly	contain	215:221	arg1	Notch receptors AND EGF repeats	Notch receptors			EGF repeats	Fterm		receptors			Protein O-fucosyltransferase 1 (Pofut1) transfers fucose to serine or threonine on proteins, including Notch receptors, that contain EGF repeats with a particular consensus sequence.
18775496	1	45	gly	contain	215:221	arg1	proteins AND EGF repeats	proteins			EGF repeats	Fterm		proteins			Protein O-fucosyltransferase 1 (Pofut1) transfers fucose to serine or threonine on proteins, including Notch receptors, that contain EGF repeats with a particular consensus sequence.
22159084	9	53	gly	glycosylated	1211:1222	arg2	N165	SLC26A3		N161, and N165		PUBTATOR		SLC26A3	1811	N161, and N165	Immnoblotting suggests that SLC26A3 is glycosylated at N153, N161, and N165.
22159084	9	53	gly	glycosylated	1211:1222	arg2	N161	SLC26A3		N161, and N165		PUBTATOR		SLC26A3	1811	N161, and N165	Immnoblotting suggests that SLC26A3 is glycosylated at N153, N161, and N165.
22159084	9	53	gly	glycosylated	1211:1222	arg2	N161			N161, and N165						N161, and N165	Immnoblotting suggests that SLC26A3 is glycosylated at N153, N161, and N165.
16107205	2	62	part_of	have	465:468	arg1	all the mammalian DNase X proteins AND an N-terminal signal peptide	all the mammalian DNase X proteins		an N-terminal signal peptide		PUBTATOR	Site	DNase X proteins	1774	peptide	A sequence comparison reveals some conserved characteristics: all the mammalian DNase X proteins have an N-terminal signal peptide, a potential N-linked glycosylation site and a C-terminal hydrophobic domain.
16107205	2	62	part_of	have	465:468	arg1	all the mammalian DNase X proteins AND a C-terminal hydrophobic domain	all the mammalian DNase X proteins		a C-terminal hydrophobic domain		PUBTATOR	Site	DNase X proteins	1774	domain	A sequence comparison reveals some conserved characteristics: all the mammalian DNase X proteins have an N-terminal signal peptide, a potential N-linked glycosylation site and a C-terminal hydrophobic domain.
16107205	2	62	part_of	have	465:468	arg1	all the mammalian DNase X proteins AND a potential N-linked glycosylation site	all the mammalian DNase X proteins		a potential N-linked glycosylation site		PUBTATOR	Site	DNase X proteins	1774	site	A sequence comparison reveals some conserved characteristics: all the mammalian DNase X proteins have an N-terminal signal peptide, a potential N-linked glycosylation site and a C-terminal hydrophobic domain.
9578468	0	41	gly	O-glycosylated	42:55	arg1	human eotaxin	human eotaxin				PUBTATOR		eotaxin	6356		Delayed production of biologically active O-glycosylated forms of human eotaxin by tumor-necrosis-factor-alpha-stimulated dermal fibroblasts.
16274239	1	56	gly	glycosylation	131:143	arg1	N			N(579)						N(579)	We have investigated functional effects of glycosylation at N(579) of the epidermal growth factor receptor (EGFR).
16274239	1	56	gly	glycosylation	131:143	arg2	N			N(579)						N(579)	We have investigated functional effects of glycosylation at N(579) of the epidermal growth factor receptor (EGFR).
16274239	1	56	gly	glycosylation	131:143	arg1	579			N(579)						N(579)	We have investigated functional effects of glycosylation at N(579) of the epidermal growth factor receptor (EGFR).
16274239	1	56	gly	glycosylation	131:143	arg2	N			N(579)						N(579)	We have investigated functional effects of glycosylation at N(579) of the epidermal growth factor receptor (EGFR).
16274239	1	56	gly	glycosylation	131:143	arg1	579			N(579)						N(579)	We have investigated functional effects of glycosylation at N(579) of the epidermal growth factor receptor (EGFR).
16274239	1	56	gly	glycosylation	131:143	arg1	579			N(579)						N(579)	We have investigated functional effects of glycosylation at N(579) of the epidermal growth factor receptor (EGFR).
12603841	5	66	gly	glycosylated	936:947	arg1	Purified glycosylated and non-glycosylated S1S2 proteins	Purified glycosylated and non-glycosylated S1S2 proteins				Fterm		proteins			Purified glycosylated and non-glycosylated S1S2 proteins also showed similar thermostabilities as determined by CD spectroscopy.
12603841	5	74	gly	non-glycosylated	953:968	arg1	Purified glycosylated and non-glycosylated S1S2 proteins	Purified glycosylated and non-glycosylated S1S2 proteins				Fterm		proteins			Purified glycosylated and non-glycosylated S1S2 proteins also showed similar thermostabilities as determined by CD spectroscopy.
2668275	11	75	part_of	STS	1416:1418	arg1	the two luminal domains	STS		the two luminal domains		Cterm	Site	STS	412	domains	The stability of STS in lysosomes may be related to the high homology of the two luminal domains of STS with the lysosomal sulfatases, arylsulfatase A, and arylsulfatase B.
15102839	6	19	gly	oligosaccharide	1388:1402	arg1	the active site			the active site	the active site		Site			site	In contrast to an analogous complex previously isolated for Saccharomyces cerevisiae ER mannosidase I, the oligosaccharide in the active site of the murine Golgi enzyme assumes a different conformation to present an alternate oligosaccharide branch into the active site pocket.
15102839	6	19	gly	oligosaccharide	1388:1402	arg1	the murine Golgi enzyme	enzyme			oligosaccharide	Fterm		enzyme			In contrast to an analogous complex previously isolated for Saccharomyces cerevisiae ER mannosidase I, the oligosaccharide in the active site of the murine Golgi enzyme assumes a different conformation to present an alternate oligosaccharide branch into the active site pocket.
15628971	5	16	part_of	C4ST-1	827:832	arg1	the C-terminal region	C4ST-1		the C-terminal region		PUBTATOR	Site	C4ST-1	314694	region	We found that (i) treatment of recombinant C4ST-1 with peptide N-glycosidase F caused a marked decrease in activity, (ii) production of the active form of C4ST-1 by COS-7 cells transfected with cDNA of C4ST-1 was inhibited by tunicamycin, (iii) deletion of the N-glycosylation site located at the C-terminal region of C4ST-1 abolished activity, (iv) attachment of a single N-glycan at the C-terminal region supported production of the active form of C4ST-1, but the resulting recombinant enzyme was much more unstable at 37 degrees C than the control recombinant protein, and (v) truncation of C-terminal region up to the N-glycosylation site at the C-terminal region resulted in total loss of activity.
15628971	5	18	part_of	region	1170:1175	arg1	the N-glycosylation site	region		the N-glycosylation site						site	We found that (i) treatment of recombinant C4ST-1 with peptide N-glycosidase F caused a marked decrease in activity, (ii) production of the active form of C4ST-1 by COS-7 cells transfected with cDNA of C4ST-1 was inhibited by tunicamycin, (iii) deletion of the N-glycosylation site located at the C-terminal region of C4ST-1 abolished activity, (iv) attachment of a single N-glycan at the C-terminal region supported production of the active form of C4ST-1, but the resulting recombinant enzyme was much more unstable at 37 degrees C than the control recombinant protein, and (v) truncation of C-terminal region up to the N-glycosylation site at the C-terminal region resulted in total loss of activity.
11683872	6	31	gly	glycosylated	829:840	arg1	This mutated VR1	This mutated VR1				PUBTATOR		VR1	7442		This mutated VR1 was not glycosylated, confirming the extracellular location of N604 and its role as the exclusive site of glycosylation of the VR1 protein.
11683872	6	49	gly	glycosylation	927:939	arg1	the VR1 protein	VR1 protein		site		PUBTATOR		VR1 protein	7442	site	This mutated VR1 was not glycosylated, confirming the extracellular location of N604 and its role as the exclusive site of glycosylation of the VR1 protein.
20739279	6	23	gly	glycosylation	851:863	arg2	its glycosylation sites			its glycosylation sites						sites Asn(70)	Structural modeling of the corresponding SynCAM 1 Ig1 domain indicates that its glycosylation sites Asn(70)/Asn(104) flank the binding interface of this domain.
20739279	6	29	gly	sites	865:869	arg1	Asn(70)/Asn			Asn(70)/Asn						sites Asn(70)	Structural modeling of the corresponding SynCAM 1 Ig1 domain indicates that its glycosylation sites Asn(70)/Asn(104) flank the binding interface of this domain.
23742080	10	47	gly	N-glycosylation	1467:1481	arg1	residue N183			residue N183						residue N183	Cycloheximide treatment experiments revealed that S185 degrades faster than T185 TMEM106B, potentially due to differences in N-glycosylation at residue N183.
25903135	1	8	gly	glycoprotein	222:233	arg1	a highly expressed neuronal glycoprotein	a highly expressed neuronal glycoprotein				Fterm		glycoprotein			Olfactomedin-1 (Olfm1; also known as noelin and pancortin) is a member of the olfactomedin domain-containing superfamily and a highly expressed neuronal glycoprotein important for nervous system development.
22187327	0	28	gly	Asn54-linked	0:11	arg1	Asn54-linked glycan			Asn54	Asn54-linked glycan					Asn54	Asn54-linked glycan is critical for functional folding of intercellular adhesion molecule-5.
1482348	1	18	gly	HGF	185:187	arg1	O-glycosylated oligosaccharide	HGF			O-glycosylated oligosaccharide	PUBTATOR		HGF	3082		The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	1	37	gly	O-glycosylated	133:146	arg1	O-glycosylated oligosaccharide				O-glycosylated oligosaccharide						The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	1	15	gly	glycosylation	93:105	arg1	O-glycosylated oligosaccharide			site	O-glycosylated oligosaccharide					site	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
22285761	9	63	part_of	uPAR	1437:1440	arg1	uPAR DI-DII domains	uPAR		uPAR DI-DII domains		PUBTATOR	Site	uPAR	5329	domains	The domain boundary between uPAR DI-DII domains is more flexible than the DII-DIII domain boundary.
11567096	1	21	gly	glycosylated	245:256	arg1	a complex glycosylated protein	a complex glycosylated protein				Fterm		protein			Rat corticotropin-releasing factor receptor 1 (rCRFR1) was produced either in transfected HEK 293 cells as a complex glycosylated protein or in the presence of the mannosidase I inhibitor kifunensine as a high mannose glycosylated protein.
11567096	1	64	gly	corticotropin-releasing	132:154	arg1	a high mannose glycosylated protein	corticotropin-releasing factor receptor 1			a high mannose glycosylated protein	PUBTATOR		corticotropin-releasing factor receptor 1	81648		Rat corticotropin-releasing factor receptor 1 (rCRFR1) was produced either in transfected HEK 293 cells as a complex glycosylated protein or in the presence of the mannosidase I inhibitor kifunensine as a high mannose glycosylated protein.
11567096	1	67	gly	factor	156:161	arg1	a high mannose glycosylated protein	corticotropin-releasing factor receptor 1			a high mannose glycosylated protein	PUBTATOR		corticotropin-releasing factor receptor 1	81648		Rat corticotropin-releasing factor receptor 1 (rCRFR1) was produced either in transfected HEK 293 cells as a complex glycosylated protein or in the presence of the mannosidase I inhibitor kifunensine as a high mannose glycosylated protein.
11567096	1	33	gly	glycosylated	346:357	arg1	Rat corticotropin-releasing factor receptor 1	corticotropin-releasing factor receptor 1			a high mannose glycosylated protein	PUBTATOR		corticotropin-releasing factor receptor 1	81648		Rat corticotropin-releasing factor receptor 1 (rCRFR1) was produced either in transfected HEK 293 cells as a complex glycosylated protein or in the presence of the mannosidase I inhibitor kifunensine as a high mannose glycosylated protein.
2403553	7	95	gly	glycopeptides	847:859	arg2	glycopeptides			glycopeptides						glycopeptides	The released radiolabeled glycopeptides and oligosaccharides were separated by a variety of chromatographic techniques, and their structures were analyzed.
23187000	3	19	gly	glycosylation	558:570	arg2	glycosylation sites			glycosylation sites						sites	Among TIMPs, TIMP-1, a 184-residue protein, is the only N-linked glycoprotein with glycosylation sites at N30 and N78.
23187000	3	27	gly	glycoprotein	540:551	arg1	the only N-linked glycoprotein	the only N-linked glycoprotein				Fterm		glycoprotein			Among TIMPs, TIMP-1, a 184-residue protein, is the only N-linked glycoprotein with glycosylation sites at N30 and N78.
23187000	3	27	gly	glycoprotein	540:551	arg1	TIMP-1	TIMP-1				PUBTATOR		TIMP-1	7076		Among TIMPs, TIMP-1, a 184-residue protein, is the only N-linked glycoprotein with glycosylation sites at N30 and N78.
20044576	3	18	gly	glycan	562:567	arg1	the mucin-like domain			the mucin-like domain	the mucin-like domain		Site			domain	Using mass spectrometry- and nuclear magnetic resonance (NMR)-based structural analyses, we identified a phosphorylated O-mannosyl glycan on the mucin-like domain of recombinant alpha-DG, which was required for laminin binding.
20044576	3	18	gly	glycan	562:567	arg1	recombinant alpha-DG	DG,			glycan	PUBTATOR		DG,	1605		Using mass spectrometry- and nuclear magnetic resonance (NMR)-based structural analyses, we identified a phosphorylated O-mannosyl glycan on the mucin-like domain of recombinant alpha-DG, which was required for laminin binding.
8702538	5	83	part_of	sites	855:859	arg1	CD22	CD22		sites		PUBTATOR	Site	CD22	933	sites	In this work we have performed site-specific mutagenesis of potential N-linked glycosylation sites on CD22 in an effort to determine whether they might be involved in ligand recognition.
25760607	6	38	gly	glycosylated	750:761	arg1	glycosylated LLT1	glycosylated LLT1				PUBTATOR		LLT1	29121		The hexamer of glycosylated LLT1 consists of three classical dimers.
26811476	7	0	gly	glycoprotein	1322:1333	arg1	deafness/Crohn's disease-associated homopolymeric glycoproteins	deafness/Crohn's disease-associated homopolymeric glycoproteins				Fterm		glycoproteins			This arrangement is required for filament formation and is directed by an ordered ZP-N/ZP-C linker that is not observed in ZP2 but is conserved in the sequence of deafness/Crohn's disease-associated homopolymeric glycoproteins α-tectorin (TECTA) and glycoprotein 2 (GP2).
26811476	7	0	gly	glycoprotein	1322:1333	arg1	glycoprotein 2	glycoprotein 2				PUBTATOR		glycoprotein 2	2813		This arrangement is required for filament formation and is directed by an ordered ZP-N/ZP-C linker that is not observed in ZP2 but is conserved in the sequence of deafness/Crohn's disease-associated homopolymeric glycoproteins α-tectorin (TECTA) and glycoprotein 2 (GP2).
26811476	7	0	gly	glycoprotein	1322:1333	arg1	GP2	GP2				PUBTATOR		GP2	2813		This arrangement is required for filament formation and is directed by an ordered ZP-N/ZP-C linker that is not observed in ZP2 but is conserved in the sequence of deafness/Crohn's disease-associated homopolymeric glycoproteins α-tectorin (TECTA) and glycoprotein 2 (GP2).
26811476	7	52	gly	glycoproteins	1285:1297	arg1	deafness/Crohn's disease-associated homopolymeric glycoproteins	deafness/Crohn's disease-associated homopolymeric glycoproteins				Fterm		glycoproteins			This arrangement is required for filament formation and is directed by an ordered ZP-N/ZP-C linker that is not observed in ZP2 but is conserved in the sequence of deafness/Crohn's disease-associated homopolymeric glycoproteins α-tectorin (TECTA) and glycoprotein 2 (GP2).
26811476	7	52	gly	glycoproteins	1285:1297	arg1	glycoprotein 2	glycoprotein 2				PUBTATOR		glycoprotein 2	2813		This arrangement is required for filament formation and is directed by an ordered ZP-N/ZP-C linker that is not observed in ZP2 but is conserved in the sequence of deafness/Crohn's disease-associated homopolymeric glycoproteins α-tectorin (TECTA) and glycoprotein 2 (GP2).
26811476	7	52	gly	glycoproteins	1285:1297	arg1	α-tectorin	α-tectorin				PUBTATOR		-tectorin	7007		This arrangement is required for filament formation and is directed by an ordered ZP-N/ZP-C linker that is not observed in ZP2 but is conserved in the sequence of deafness/Crohn's disease-associated homopolymeric glycoproteins α-tectorin (TECTA) and glycoprotein 2 (GP2).
19276170	1	25	gly	glycoprotein	240:251	arg1	thrombospondin-5	thrombospondin-5				PUBTATOR		thrombospondin-5	1311		Cartilage oligomeric matrix protein (COMP), or thrombospondin-5 (TSP-5), is a secreted glycoprotein that is important for growth plate organization and function.
19276170	1	25	gly	glycoprotein	240:251	arg1	Cartilage oligomeric matrix protein	Cartilage oligomeric matrix protein				OGER		Cartilage oligomeric matrix protein	P49747		Cartilage oligomeric matrix protein (COMP), or thrombospondin-5 (TSP-5), is a secreted glycoprotein that is important for growth plate organization and function.
19276170	1	25	gly	glycoprotein	240:251	arg1	a secreted glycoprotein	a secreted glycoprotein				Fterm		glycoprotein			Cartilage oligomeric matrix protein (COMP), or thrombospondin-5 (TSP-5), is a secreted glycoprotein that is important for growth plate organization and function.
2226797	2	3	gly	glycopeptide	319:330	arg2	the tryptic glycopeptide			the tryptic glycopeptide						glycopeptide	After isolation of the tryptic glycopeptide and liberation of the N-linked carbohydrates by polypeptide:N-glycosidase F, 6 major oligosaccharide fractions were separated by HPLC on NH2-bonded phase.
18533687	10	28	gly	N-glycosylation	1631:1645	arg1	optimal intracellular cAMP signaling	cAMP		Asn-303		OGER		cAMP	Q96JM3	Asn-303	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
18533687	10	28	gly	N-glycosylation	1631:1645	arg2	Asn-303			Asn-303						Asn-303	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
18533687	10	28	gly	N-glycosylation	1631:1645	arg2	Asn-303	cAMP		Asn-303		OGER		cAMP	Q96JM3	Asn-303	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
8962717	7	72	part_of	proteins	1225:1232	arg1	consensus glycosylation sites	proteins		consensus glycosylation sites		Fterm	Site	proteins		sites	The large hydrodynamic mass of these oligosaccharides could influence ligand binding, an effect which is likely to vary with the difference in consensus glycosylation sites of proteins related to p170 i.e. p185erbB2/neu, p180erbB3 and p180erbB4.
1899031	2	35	part_of	site	885:888	arg1	HPg	HPg		site		Cterm	Site	HPg	5340	site	Employing high-performance anion-exchange liquid chromatography mapping of the oligosaccharide units cleaved from the protein by glycopeptidase F, compared with elution positions of standard oligosaccharides, coupled with monosaccharide compositional determinations and analyses of sequential exoglycosidase digestions and specific lectin binding, we find that considerable microheterogeneity in oligosaccharide structure exists at this sole potential N-linked glycosylation site on HPg.
2113054	5	83	gly	glycosylation	1109:1121	arg2	a N-linked glycosylation site			a N-linked glycosylation site						site	Domain 1 alone was not expressed and introduction of a N-linked glycosylation site did not facilitate expression.
8576151	5	63	gly	glycosylated	636:647	arg1	The purified procollagenase-3	The purified procollagenase-3				PUBTATOR		collagenase-3	4322		The purified procollagenase-3 was shown to be glycosylated and displayed a M(r) of 60,000, the N-terminal sequence being LPLPSGGD, which is consistent with the cDNA-predicted sequence.
20879038	6	35	gly	glycosylation	1371:1383	arg1	Gln			Gln						Gln	In summary, salivary peptidome data analysis allowed the identification of 45 new PRP-modified residues, mainly due to glycosylation, phosphorylation and conversion of Gln to pyro-Glu.
15253437	2	31	gly	N-glycosylation	409:423	arg2	N-glycosylation sites			N-glycosylation sites						sites	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	2	57	gly	glycosylated	492:503	arg1	glycosylated peptides			glycosylated peptides						peptides	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
10988252	1	3	gly	N-glycosylation	214:228	arg2	11 potential N-glycosylation sites			11 potential N-glycosylation sites						sites	The human epidermal growth factor receptor (EGFR) is a transmembrane glycoprotein having 11 potential N-glycosylation sites in its extracellular domain.
10988252	1	16	gly	glycoprotein	181:192	arg1	a transmembrane glycoprotein	a transmembrane glycoprotein				Fterm		glycoprotein			The human epidermal growth factor receptor (EGFR) is a transmembrane glycoprotein having 11 potential N-glycosylation sites in its extracellular domain.
10988252	1	16	gly	glycoprotein	181:192	arg1	The human epidermal growth factor receptor	The human epidermal growth factor receptor				PUBTATOR		epidermal growth factor receptor	1956		The human epidermal growth factor receptor (EGFR) is a transmembrane glycoprotein having 11 potential N-glycosylation sites in its extracellular domain.
12659834	9	40	gly	N-glycosylation	1833:1847	arg2	N-glycosylation sites			N-glycosylation sites						sites	Further systematic approaches including modulation of degree of N-glycosylation or relocation of N-glycosylation sites in the recombinant pre-S1S2 may make it possible to achieve both enhanced immunogenicity and resistance towards proteolytic degradation of the secreted pre-S antigen.
12659834	9	54	gly	N-glycosylation	1800:1814	arg1	N-glycosylation sites			N-glycosylation sites						sites	Further systematic approaches including modulation of degree of N-glycosylation or relocation of N-glycosylation sites in the recombinant pre-S1S2 may make it possible to achieve both enhanced immunogenicity and resistance towards proteolytic degradation of the secreted pre-S antigen.
20856818	0	51	gly	glycoprotein	31:42	arg1	a multimeric glycoprotein	a multimeric glycoprotein				Fterm		glycoprotein			Mammalian Otolin: a multimeric glycoprotein specific to the inner ear that interacts with otoconial matrix protein Otoconin-90 and Cerebellin-1.
15014436	9	43	gly	TSP-5/COMP	1091:1100	arg1	the T3 repeats	TSP			the T3 repeats	PUBTATOR		TSP	P07996		Mutations in the T3 repeats of TSP-5/COMP, which cause two human skeletal disorders, are predicted to disrupt the tertiary structure of the T3-CTD assembly.
15014436	2	55	gly	TSPs	242:245	arg1	the calcium-binding type 3 (T3) repeats	TSPs			the calcium-binding type 3 (T3) repeats	Cterm		TSPs	7057		The most highly conserved region of all TSPs are the calcium-binding type 3 (T3) repeats and the C-terminal globular domain (CTD).
7592613	4	95	gly	occupied	706:713	arg2	the second site			the second site						site	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
7592613	4	8	gly	carries	609:615	arg1	The Asn-28 site AND complex-type structures			The Asn-28 site	complex-type structures					Asn-28 site	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
7592613	4	8	gly	carries	609:615	arg1	The Asn-28 site AND high mannose			The Asn-28 site	high mannose					Asn-28 site	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
25187573	3	73	part_of	contains	493:500	arg1	Lubricin AND an serine/threonine/proline (STP)-rich domain	Lubricin		an serine/threonine/proline (STP)-rich domain		PUBTATOR	Site	Lubricin	10216	domain	Lubricin contains an serine/threonine/proline (STP)-rich domain composed of imperfect tandem repeats (EPAPTTPK), the target for O-glycosylation.
19196183	5	15	gly	glycosylation	710:722	arg2	300 different glycosylation sites			300 different glycosylation sites						sites	With the use of both methods in combination with nano-LC-ESI-MS/MS analysis, 300 different glycosylation sites within 194 unique glycoproteins were identified, and 172 glycosites have not been determined experimentally previously.
19196183	5	29	gly	glycosites	787:796	arg2	172 glycosites			172 glycosites						glycosites	With the use of both methods in combination with nano-LC-ESI-MS/MS analysis, 300 different glycosylation sites within 194 unique glycoproteins were identified, and 172 glycosites have not been determined experimentally previously.
19196183	5	36	gly	glycoproteins	748:760	arg1	194 unique glycoproteins	194 unique glycoproteins				Fterm		glycoproteins			With the use of both methods in combination with nano-LC-ESI-MS/MS analysis, 300 different glycosylation sites within 194 unique glycoproteins were identified, and 172 glycosites have not been determined experimentally previously.
6510521	2	9	part_of	hemopexin	365:373	arg1	the N-terminal region	hemopexin		the N-terminal region		PUBTATOR	Site	hemopexin	3263	region	By sequence studies of fragments CB1-CB4 and peptides prepared by their enzyme cleavage, a continuous amino acid sequence of the N-terminal region of human hemopexin, comprising 220 amino acid residues, was determined.
12754519	6	2	gly	glycosylated	1095:1106	arg1	formerly N-linked glycosylated peptides			formerly N-linked glycosylated peptides						peptides	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	52	gly	glycopeptides	1035:1047	arg2	glycopeptides			glycopeptides						glycopeptides	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	57	gly	glycoproteins	948:960	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
27294781	4	4	gly	interface	695:703	arg1	SV2	SV2			interface	PUBTATOR		SV2	9900		The glycan-binding interface on SV2 is targeted by a human BoNT/A1-neutralizing antibody currently licensed as an antibotulism drug.
23187000	8	37	gly	glycosylation	1415:1427	arg1	TIMP-1	TIMP-1				PUBTATOR		TIMP-1	7076		The aberrant glycosylation of TIMP-1 can thus be used as staging and/or prognostic biomarker in colon cancer.
16186819	2	5	gly	glycosylated	269:280	arg1	human THBS2	THBS2		domain		PUBTATOR		THBS2	7058	domain	Here, we describe the 2.6-A-resolution crystal structure of the glycosylated signature domain of human THBS2, which includes three epidermal growth factor-like modules, 13 aspartate-rich repeats and a lectin-like module.
11912203	6	24	gly	glycosylation	676:688	arg2	The glycosylation sites			The glycosylation sites						sites	The glycosylation sites were mapped to several lysines (residues 68, 71, 80, and 104) located in the collagenous domain of adiponectin, each having the surrounding motif of GXKGE(D).
22660477	8	26	part_of	GBR2	989:992	arg1	the GBR2 ectodomain	GBR2		the GBR2 ectodomain		Cterm	Site	GBR2		ectodomain	Lastly, our structural and functional data indicate that the GBR2 ectodomain adopts a constitutively open conformation, suggesting a structural asymmetry in the active state of GABA(B) receptor that is unique to the GABAergic system.
2215480	2	93	part_of	IL-5	302:305	arg1	IL-5 polypeptide	IL-5		IL-5 polypeptide		PUBTATOR	Site	IL-5	P05113	polypeptide	IL-5 polypeptide translated into Xenopus oocytes are heterogeneous in molecular size (40,000 to 60,000 under nonreducing conditions) and yields a monomeric form (Mr of 25,000 to 30,000) under reducing conditions (J. Immun., 140, 1175-1181, 1988).
1544894	3	62	part_of	residues	646:653	arg1	protein C	In protein C		residues		OGER	Site	In protein C	P02810	residues	In protein C, this site is 3 residues from the position of another post-translational modification, beta-hydroxylation of Asp-71.
12218058	2	34	part_of	metalloproteinase	474:490	arg1	Asn(142)	metalloproteinase		Asn(142)		Fterm	SpecificSite	metalloproteinase		Asn(142)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	34	part_of	metalloproteinase	474:490	arg1	metalloproteinase domain	metalloproteinase		metalloproteinase domain		Fterm	Site	metalloproteinase		domain	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	38	part_of	has	375:377	arg1	BMP-1 AND Asn(91)	BMP-1		Asn(91)		PUBTATOR	SpecificSite	BMP-1	649	Asn(91)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	38	part_of	has	375:377	arg1	BMP-1 AND six potential N-linked glycosylation sites	BMP-1		six potential N-linked glycosylation sites		PUBTATOR	Site	BMP-1	649	sites	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	38	part_of	has	375:377	arg1	BMP-1 AND Asn(599)	BMP-1		Asn(599)		PUBTATOR	SpecificSite	BMP-1	649	Asn(599)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	38	part_of	has	375:377	arg1	BMP-1 AND Asn(142)	BMP-1		Asn(142)		PUBTATOR	SpecificSite	BMP-1	649	Asn(142)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	38	part_of	has	375:377	arg1	BMP-1 AND Asn(332)	BMP-1		Asn(332)		PUBTATOR	SpecificSite	BMP-1	649	Asn(332) and Asn(363)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12022871	8	4	gly	glycosylated	1241:1252	arg1	Human TGH	Human TGH				PUBTATOR		Human TGH	1066		Human TGH was glycosylated in the insect cells.
20507882	5	42	part_of	Hex-O-Thr	899:907	arg1	Hex-O-Thr glycopeptides	Hex		Hex-O-Thr glycopeptides		OGER	AminoAcid	Hex		Thr glycopeptides	The HexNAc-O-Ser/Thr, but not Hex-O-Thr glycopeptides, displayed heterogeneity regarding glycan core structures and level of glycosylation site occupancy.
16847056	13	64	gly	beta2	1583:1587	arg1	only the sialic acid-independent depolarizing effects	beta2			only the sialic acid-independent depolarizing effects	Cterm		beta2			When sialylation was reduced, only the sialic acid-independent depolarizing effects of beta2 on Nav1.2 gating were apparent.
3571235	2	2	gly	sialoglycoproteins	157:174	arg1	glycophorins B and C	glycophorins B and C				PUBTATOR		glycophorins B and C	2994		We have developed methods for the preparative purification of two sialoglycoproteins (glycophorins B and C) from human erythrocyte membranes by high-performance ion exchange and gel permeation chromatography in the presence of Triton X-100.
3571235	2	2	gly	sialoglycoproteins	157:174	arg1	two sialoglycoproteins	two sialoglycoproteins				Fterm		sialoglycoproteins			We have developed methods for the preparative purification of two sialoglycoproteins (glycophorins B and C) from human erythrocyte membranes by high-performance ion exchange and gel permeation chromatography in the presence of Triton X-100.
10871631	5	73	gly	glycoproteins	873:885	arg1	lumenally oriented glycoproteins	lumenally oriented glycoproteins				Fterm		glycoproteins			When transfected into mammalian cells, both torsin A and DeltaE-torsin A were found to behave as lumenally oriented glycoproteins.
7654718	5	47	gly	O-glycosylated	782:795	arg1	The O-glycosylated carbohydrates				The O-glycosylated carbohydrates						The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	5	68	gly	fragment	825:832	arg1	The O-glycosylated carbohydrates			fragment	The O-glycosylated carbohydrates					fragment	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
21712440	4	0	part_of	APP/Aβ	868:873	arg1	37 APP/Aβ glycopeptides	37 APP/Aβ 		37 APP/Aβ glycopeptides		PUBTATOR	Site	37 APP/Aβ 	351	glycopeptides	In addition to 33 unglycosylated APP/Aβ peptides, we identified 37 APP/Aβ glycopeptides with sialylated core 1 like O-glycans attached to Thr(-39, -21, -20, and -13), in a series of APP/AβX-15 glycopeptides, where X was -63, -57, -52, and -45, in relation to Asp1 of the Aβ sequence.
21712440	4	43	part_of	APP/Aβ	834:839	arg1	33 unglycosylated APP/Aβ peptides	APP/Aβ 		33 unglycosylated APP/Aβ peptides		PUBTATOR	Site	APP/Aβ 	351	peptides	In addition to 33 unglycosylated APP/Aβ peptides, we identified 37 APP/Aβ glycopeptides with sialylated core 1 like O-glycans attached to Thr(-39, -21, -20, and -13), in a series of APP/AβX-15 glycopeptides, where X was -63, -57, -52, and -45, in relation to Asp1 of the Aβ sequence.
7620335	10	18	gly	disialylated	1650:1661	arg1	disialylated Gal beta 3GalNAc				disialylated Gal beta 3GalNAc						In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	10	92	gly	residues	1620:1627	arg1	disialylated Gal beta 3GalNAc sequences			Thr17 and Thr29 residues	disialylated Gal beta 3GalNAc sequences					Thr17 and Thr29 residues	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
1457969	4	53	part_of	hTSH	663:666	arg1	hTSH alpha glycopeptides	hTSH		hTSH alpha glycopeptides		OGER	Site	hTSH		glycopeptides	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
15807535	8	66	gly	glycosylated	1513:1524	arg1	glycosylated ABCG2	glycosylated ABCG2				PUBTATOR		ABCG2	Q9UNQ0		The ABCG2 (N596Q) variant is also functional, demonstrating rhodamine 123 transport in intact cells comparable to that in cells expressing glycosylated ABCG2.
14718370	6	26	gly	motif	931:935	arg1	the putative C-mannosylation acceptor motif WXXW				the putative C-mannosylation acceptor motif WXXW						Lectin binding was prevented by mutation of the first tryptophan residue in the putative C-mannosylation acceptor motif WXXW, indicating that C-mannosylation is responsible for lectin binding.
14718370	6	95	gly	residue	882:888	arg1	the putative C-mannosylation acceptor motif WXXW			tryptophan residue	the putative C-mannosylation acceptor motif WXXW					tryptophan residue	Lectin binding was prevented by mutation of the first tryptophan residue in the putative C-mannosylation acceptor motif WXXW, indicating that C-mannosylation is responsible for lectin binding.
9677337	5	48	gly	N-glycan	872:879	arg1	the N-terminal region			the N-terminal region	the N-terminal region		Site			region	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	5	54	gly	di-sialylated	988:1000	arg1	the N-terminal region			the N-terminal region						region	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
8068684	7	84	gly	contains	1270:1277	arg1	NHE-1 AND O-linked oligosaccharide	NHE-1			O-linked oligosaccharide	PUBTATOR		NHE-1	6548		In addition, treatment of NHE-1 with neuraminidase and O-glycosidase demonstrated that NHE-1 also contains O-linked oligosaccharide.
25826155	0	67	part_of	transcript	63:72	arg1	extracellular domain	lectin-like transcript 1		extracellular domain		PUBTATOR	Site	lectin-like transcript 1	29121	domain	Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A.
3555489	3	36	part_of	enzyme	573:578	arg1	the N-terminal transmembrane region	enzyme		the N-terminal transmembrane region		Fterm	Site	enzyme		region	Because enkephalinase has it active site located extracellularly and is thus an ectopeptidase, we suggest that the N-terminal transmembrane region of the enzyme anchors the protein in membranes and that the majority of the protein, including the carboxy terminus, is extracellular.
3555489	3	32	part_of	has	441:443	arg1	enkephalinase AND it active site	enkephalinase		it active site		PUBTATOR	Site	Because enkephalinase	24590	site	Because enkephalinase has it active site located extracellularly and is thus an ectopeptidase, we suggest that the N-terminal transmembrane region of the enzyme anchors the protein in membranes and that the majority of the protein, including the carboxy terminus, is extracellular.
12154198	0	31	part_of	HER3	41:44	arg1	the extracellular region	HER3		the extracellular region		PUBTATOR	Site	HER3	2065	region	Structure of the extracellular region of HER3 reveals an interdomain tether.
22745122	7	14	part_of	serine	884:889	arg1	DRP1	DRP1		serine		PUBTATOR	SpecificSite	DRP1	10059	serine 637	Increased O-GlcNAcylation decreases the phosphorylation of DRP1 at serine 637, which is known to regulate DRP1 function.
25187573	9	32	gly	O-glycosylation	1717:1731	arg1	lubricin	lubricin				PUBTATOR		lubricin	10216		This suggests that there is a unique combination of transferase genes important for the O-glycosylation of lubricin.
21264968	5	79	part_of	MUC5AC	1749:1754	arg1	naked MUC5AC peptide	MUC5AC		naked MUC5AC peptide		PUBTATOR	Site	MUC5AC	4586	peptide	On the contrary, O-glycosylation of naked MUC5AC peptide occurred predominantly at consecutive Thr residues and led to MUC5AC with four α-GalNAc residues at Thr2, Thr3, Thr7, and Thr8.
1421756	8	46	gly	present	1303:1309	arg1	the TfR AND only one O-linked oligosaccharide	TfR			only one O-linked oligosaccharide	PUBTATOR		TfR	7037		These and other results demonstrate that only one O-linked oligosaccharide is present in the TfR and that it occurs on either Thr96 or Thr104.
8670172	10	46	gly	fucosylated	1453:1463	arg1	The predominant oligosaccharide chains				The predominant oligosaccharide chains						The predominant oligosaccharide chains were fucosylated biantennary and triantennary complexes with variable sialylation.
26117840	1	26	gly	glycoproteins	232:244	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	1	53	gly	containing	246:255	arg1	glycoproteins AND x	glycoproteins			x	Fterm		glycoproteins			E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	1	53	gly	containing	246:255	arg1	glycoproteins AND the tetrasaccharide sialyl Lewis	glycoproteins			the tetrasaccharide sialyl Lewis	Fterm		glycoproteins			E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
20837471	7	53	gly	glycosylation	1211:1223	arg1	Thr(226)			Thr(226)						Thr(226)	We demonstrated that GalNAc-T2 glycosylation of Thr(226) in a peptide with the RAPR(224)↓TT processing site blocks in vitro furin cleavage.
20837471	7	71	gly	Thr	1228:1230	arg1	GalNAc-T2 glycosylation			Thr(226)	GalNAc-T2 glycosylation					Thr(226)	We demonstrated that GalNAc-T2 glycosylation of Thr(226) in a peptide with the RAPR(224)↓TT processing site blocks in vitro furin cleavage.
20837471	7	63	gly	glycosylation	1211:1223	arg1	a peptide			peptide	a peptide		Site			peptide	We demonstrated that GalNAc-T2 glycosylation of Thr(226) in a peptide with the RAPR(224)↓TT processing site blocks in vitro furin cleavage.
18491227	9	20	gly	N-glycosylation	1457:1471	arg1	Asn-633			Asn-633						Asn-633	In conclusion, this study revealed that N-glycosylation at Asn-633 is essential for E-cadherin expression, folding and trafficking.
18491227	9	20	gly	N-glycosylation	1457:1471	arg1	E-cadherin expression	E-cadherin		Asn-633		PUBTATOR		E-cadherin	999	Asn-633	In conclusion, this study revealed that N-glycosylation at Asn-633 is essential for E-cadherin expression, folding and trafficking.
18491227	9	20	gly	N-glycosylation	1457:1471	arg1	E-cadherin expression	E-cadherin		Asn-633		PUBTATOR		E-cadherin	999	Asn-633	In conclusion, this study revealed that N-glycosylation at Asn-633 is essential for E-cadherin expression, folding and trafficking.
9169007	1	3	gly	glycoforms	166:175	arg1	recombinant antithrombin	recombinant antithrombin				PUBTATOR		antithrombin	462		Two major glycoforms of recombinant antithrombin which differ 10-fold in their affinity for the effector glycosaminoglycan, heparin, were previously shown to be expressed in BHK or CHO mammalian cell lines (I. Björk, et al., 1992, Biochem.
14658030	4	58	gly	N-glycosylation	1093:1107	arg2	the six potential N-glycosylation sites			the six potential N-glycosylation sites						sites	Here we report the mass spectrometric analysis of the six potential N-glycosylation sites of the neural cell adhesion molecule NCAM from adult mouse brain.
12718853	3	37	part_of	receptor	581:588	arg1	a soluble extracellular domain	Nogo receptor		a soluble extracellular domain		PUBTATOR	Site	Nogo receptor	65078	domain	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
3514617	12	99	gly	Asn-linked	2145:2154	arg1	the Asn-linked carbohydrate			Asn	the Asn-linked carbohydrate					Asn	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	12	154	gly	glycopeptides	2020:2032	arg2	two CNBr glycopeptides B			two CNBr glycopeptides B						glycopeptides	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
8942648	2	94	part_of	Full	202:205	arg1	332 residues	Full		332 residues		OGER	Site	Full	Q8N1N2	residues	Full length recombinant human TPO (332 residues) has been expressed in BHK cells and purified to homogeneity using conventional means.
26993603	2	4	gly	glycosylation	303:315	arg2	glycosylation sites			glycosylation sites						sites	In this study, we used mass spectrometry to identify glycosylation sites and the glycan structure, high-throughput lectin microarray to provide rapid and sensitive profiling of glycoconjugates, and site-directed mutagenesis to clarify the impact of glycans on target glycoproteins in vivo.
26993603	2	24	gly	glycoproteins	517:529	arg1	target glycoproteins	target glycoproteins				Fterm		glycoproteins			In this study, we used mass spectrometry to identify glycosylation sites and the glycan structure, high-throughput lectin microarray to provide rapid and sensitive profiling of glycoconjugates, and site-directed mutagenesis to clarify the impact of glycans on target glycoproteins in vivo.
1737041	7	54	gly	glycoprotein	1547:1558	arg1	glycoprotein hormones	glycoprotein hormones				Fterm		glycoprotein			These studies help to point out the range of roles played by carbohydrate modification in the biosynthesis, assembly, and secretion of glycoprotein hormones.
2387072	6	42	gly	fucosylation	1542:1553	arg1	the CF peripheral membrane glycoproteins	the CF peripheral membrane glycoproteins				Fterm		glycoproteins			These results define further the altered fucosylation of the CF peripheral membrane glycoproteins.
2387072	6	81	gly	glycoproteins	1585:1597	arg1	the altered fucosylation	glycoproteins			the altered fucosylation	Fterm		glycoproteins			These results define further the altered fucosylation of the CF peripheral membrane glycoproteins.
10677208	8	17	part_of	fibrillin-1	1461:1471	arg1	an eight-cysteine domain	fibrillin-1		an eight-cysteine domain		OGER	AminoAcid	fibrillin-1	P35555	cysteine domain	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
17040911	6	33	gly	glycans	1021:1027	arg1	Asn-270			Asn-270	Asn-270		SpecificSite			Asn-234 and Asn-270	The removal of two glycans in the protease domain at Asn-234 and Asn-270, as well as one in the tumor necrosis factor receptor-associated factor domain at Asn-452, by a deglycosidase under nondenaturing conditions decreased the chemical and thermal stability of the homo-oligomer without affecting quaternary structure.
17040911	6	33	gly	glycans	1021:1027	arg1	Asn-234			Asn-234	Asn-234		SpecificSite			Asn-234 and Asn-270	The removal of two glycans in the protease domain at Asn-234 and Asn-270, as well as one in the tumor necrosis factor receptor-associated factor domain at Asn-452, by a deglycosidase under nondenaturing conditions decreased the chemical and thermal stability of the homo-oligomer without affecting quaternary structure.
17040911	6	33	gly	glycans	1021:1027	arg1	the protease domain			the protease domain	the protease domain		Site			domain	The removal of two glycans in the protease domain at Asn-234 and Asn-270, as well as one in the tumor necrosis factor receptor-associated factor domain at Asn-452, by a deglycosidase under nondenaturing conditions decreased the chemical and thermal stability of the homo-oligomer without affecting quaternary structure.
17040911	6	72	gly	Asn-234	1055:1061	arg1	two glycans			Asn-234 and Asn-270	two glycans					Asn-234 and Asn-270	The removal of two glycans in the protease domain at Asn-234 and Asn-270, as well as one in the tumor necrosis factor receptor-associated factor domain at Asn-452, by a deglycosidase under nondenaturing conditions decreased the chemical and thermal stability of the homo-oligomer without affecting quaternary structure.
17040911	6	82	gly	Asn-270	1067:1073	arg1	two glycans			Asn-234 and Asn-270	two glycans					Asn-234 and Asn-270	The removal of two glycans in the protease domain at Asn-234 and Asn-270, as well as one in the tumor necrosis factor receptor-associated factor domain at Asn-452, by a deglycosidase under nondenaturing conditions decreased the chemical and thermal stability of the homo-oligomer without affecting quaternary structure.
9054441	6	3	gly	glycosylation	952:964	arg1	Ser-248	plasminogen 2		Ser-248		OGER		plasminogen 2	P00747	Ser-248	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	6	3	gly	glycosylation	952:964	arg2	Ser-248	plasminogen 2		Ser-248		OGER		plasminogen 2	P00747	Ser-248	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	6	3	gly	glycosylation	952:964	arg2	Ser-248			Ser-248						Ser-248	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
8999954	4	7	gly	detected	483:490	arg2	mouse ER AND O-GlcNAc moieties	mouse ER			O-GlcNAc moieties	PUBTATOR		ER	17289		O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
21300292	4	48	part_of	E-cadherin	669:678	arg1	E-cadherin ectodomains	E-cadherin		E-cadherin ectodomains		PUBTATOR	Site	E-cadherin	12550	ectodomains	Assemblies formed by E-cadherin ectodomains coated on liposomes also appear to adopt this structure.
208636	4	12	gly	desialylated	671:682	arg1	desialylated apolipoproteins	desialylated apolipoproteins				Fterm		apolipoproteins			Treatment of desialylated apolipoproteins with alkaline borohydride released the reduced disaccharide beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography.
1544894	1	7	part_of	EGF	406:408	arg1	their EGF domains	EGF		their EGF domains		OGER	Site	EGF	P01133	domains	We and others have demonstrated that tissue plasminogen activator (t-PA) and prourokinase are modified by the attachment of fucose to equivalent threonine residues within their EGF domains.
22547800	0	48	gly	leucine-rich	35:46	arg1	leucine-rich repeat-containing proteins			leucine	leucine-rich repeat-containing proteins					leucine	BK potassium channel modulation by leucine-rich repeat-containing proteins.
17662946	1	47	part_of	KIT	186:188	arg1	the ectodomain	KIT		the ectodomain		PUBTATOR	Site	KIT	3815	ectodomain	Stem Cell Factor (SCF) initiates its multiple cellular responses by binding to the ectodomain of KIT, resulting in tyrosine kinase activation.
12839991	3	45	gly	NgR	568:570	arg1	the entire leucine-rich repeat (LRR) region	NgR			the entire leucine-rich repeat (LRR) region	OGER		NgR	Q9BZR6		By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	3	56	gly	leucine-rich	532:543	arg1	leucine-rich repeat			leucine	leucine-rich repeat					leucine	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	3	56	gly	leucine-rich	532:543	arg1	LRR			leucine	LRR					leucine	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
16847056	3	75	gly	beta2	411:415	arg1	essentially no sialylation	beta2			essentially no sialylation	Cterm		beta2			To determine whether beta2-linked sialic acids similarly impact Nav gating, we co-expressed beta2 with Nav1.5 or Nav1.2 in Pro5 (complete sialylation) and in Lec2 (essentially no sialylation) cells.
16847056	3	75	gly	beta2	411:415	arg1	complete sialylation	beta2			complete sialylation	Cterm		beta2			To determine whether beta2-linked sialic acids similarly impact Nav gating, we co-expressed beta2 with Nav1.5 or Nav1.2 in Pro5 (complete sialylation) and in Lec2 (essentially no sialylation) cells.
16847056	3	75	gly	beta2	411:415	arg1	Lec2 (essentially no sialylation) cells	beta2			Lec2 (essentially no sialylation) cells	Cterm		beta2			To determine whether beta2-linked sialic acids similarly impact Nav gating, we co-expressed beta2 with Nav1.5 or Nav1.2 in Pro5 (complete sialylation) and in Lec2 (essentially no sialylation) cells.
3881423	7	42	gly	glycoproteins	1259:1271	arg1	neutral alpha-glucosidase AB	neutral alpha-glucosidase AB				PUBTATOR		neutral alpha-glucosidase AB	23193		Both glucosidase II and neutral alpha-glucosidase AB are high-molecular mass (greater than 200,000 dalton) anionic glycoproteins which bind to concanavalin A, have a broad pH optima (5.5-8.5), and have a similar Km for maltose (4.8 versus 2.1 mM) and the artificial substrate 4-methylumbelliferyl-alpha-D-glucopyranoside (35 versus 19 microM).
3881423	7	42	gly	glycoproteins	1259:1271	arg1	high-molecular mass (greater than 200,000 dalton) anionic glycoproteins	high-molecular mass (greater than 200,000 dalton) anionic glycoproteins				Fterm		glycoproteins			Both glucosidase II and neutral alpha-glucosidase AB are high-molecular mass (greater than 200,000 dalton) anionic glycoproteins which bind to concanavalin A, have a broad pH optima (5.5-8.5), and have a similar Km for maltose (4.8 versus 2.1 mM) and the artificial substrate 4-methylumbelliferyl-alpha-D-glucopyranoside (35 versus 19 microM).
3881423	7	42	gly	glycoproteins	1259:1271	arg1	glucosidase II	glucosidase II				OGER		glucosidase II			Both glucosidase II and neutral alpha-glucosidase AB are high-molecular mass (greater than 200,000 dalton) anionic glycoproteins which bind to concanavalin A, have a broad pH optima (5.5-8.5), and have a similar Km for maltose (4.8 versus 2.1 mM) and the artificial substrate 4-methylumbelliferyl-alpha-D-glucopyranoside (35 versus 19 microM).
3881423	7	48	gly	have	1341:1344	arg1	high-molecular mass (greater than 200,000 dalton) anionic glycoproteins AND the artificial substrate 4-methylumbelliferyl-alpha-D-glucopyranoside	high-molecular mass (greater than 200,000 dalton) anionic glycoproteins			the artificial substrate 4-methylumbelliferyl-alpha-D-glucopyranoside	Fterm		glycoproteins			Both glucosidase II and neutral alpha-glucosidase AB are high-molecular mass (greater than 200,000 dalton) anionic glycoproteins which bind to concanavalin A, have a broad pH optima (5.5-8.5), and have a similar Km for maltose (4.8 versus 2.1 mM) and the artificial substrate 4-methylumbelliferyl-alpha-D-glucopyranoside (35 versus 19 microM).
3881423	7	48	gly	have	1341:1344	arg1	neutral alpha-glucosidase AB AND the artificial substrate 4-methylumbelliferyl-alpha-D-glucopyranoside	neutral alpha-glucosidase AB			the artificial substrate 4-methylumbelliferyl-alpha-D-glucopyranoside	PUBTATOR		neutral alpha-glucosidase AB	23193		Both glucosidase II and neutral alpha-glucosidase AB are high-molecular mass (greater than 200,000 dalton) anionic glycoproteins which bind to concanavalin A, have a broad pH optima (5.5-8.5), and have a similar Km for maltose (4.8 versus 2.1 mM) and the artificial substrate 4-methylumbelliferyl-alpha-D-glucopyranoside (35 versus 19 microM).
3881423	7	48	gly	have	1341:1344	arg1	glucosidase II AND the artificial substrate 4-methylumbelliferyl-alpha-D-glucopyranoside	glucosidase II			the artificial substrate 4-methylumbelliferyl-alpha-D-glucopyranoside	OGER		glucosidase II			Both glucosidase II and neutral alpha-glucosidase AB are high-molecular mass (greater than 200,000 dalton) anionic glycoproteins which bind to concanavalin A, have a broad pH optima (5.5-8.5), and have a similar Km for maltose (4.8 versus 2.1 mM) and the artificial substrate 4-methylumbelliferyl-alpha-D-glucopyranoside (35 versus 19 microM).
14699159	6	52	gly	N-glycoprotein	1256:1269	arg1	N-glycoprotein	N-glycoprotein				Fterm		N-glycoprotein			This mutation sharply reduces p90ATF6 association with calreticulin, a major Ca(2+)-binding chaperone for N-glycoprotein.
1567356	11	28	gly	glycosylation	1641:1653	arg2	the individual glycosylation sites	OMD		sites		OGER		OMD	Q99983	sites	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
24161696	8	71	part_of	Kv3.1b	1517:1522	arg1	the N-glycosylation sites	Kv3.1b		the N-glycosylation sites		Cterm	Site	Kv3.1b		sites	CONCLUSIONS: Our findings provide direct evidence that occupancy of the N-glycosylation sites of Kv3.1b contributes significantly to its lateral heterogeneity in membranes of neuronal-derived cells, and in turn alters cellular properties.
27349982	0	4	part_of	Saposin	65:71	arg1	the Saposin Domain	Saposin		the Saposin Domain		Cterm		Saposin			Structure of Human Acid Sphingomyelinase Reveals the Role of the Saposin Domain in Activating Substrate Hydrolysis.
22678432	1	4	gly	glycoprotein	256:267	arg1	recombinant glycoprotein therapeutics	recombinant glycoprotein therapeutics				Fterm		glycoprotein			The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	1	42	gly	glycoprotein	163:174	arg1	glycoprotein function	glycoprotein function				Fterm		glycoprotein			The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
15331613	0	67	gly	site	14:17	arg1	neuroglycan C. Neuroglycan C			site	neuroglycan C. Neuroglycan C					site	Glycosylation site for chondroitin sulfate on the neural part-time proteoglycan, neuroglycan C. Neuroglycan C (NGC) is a membrane-spanning chondroitin sulfate (CS) proteoglycan that is expressed predominantly in the central nervous system (CNS).
15331613	0	67	gly	site	14:17	arg1	the neural part-time proteoglycan			site	the neural part-time proteoglycan					site	Glycosylation site for chondroitin sulfate on the neural part-time proteoglycan, neuroglycan C. Neuroglycan C (NGC) is a membrane-spanning chondroitin sulfate (CS) proteoglycan that is expressed predominantly in the central nervous system (CNS).
9767079	4	60	gly	deglycosylated	642:655	arg1	a 65 kDa protein	a 65 kDa protein				Fterm		protein			A deglycosylated RFC cDNA construct in which asparagine-58 was replaced by glutamine (Gln58-RFC) was expressed in K500E cells as a 65 kDa protein and restored transport capacity for methotrexate and (6S)5-formyl tetrahydrofolate.
17330941	4	76	gly	glycoproteins	481:493	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			First, glycoproteins are coupled to an azlactone copolymer gel using hydrazide chemistry and cysteine residues are then biotinylated.
19478079	4	20	gly	found	671:675	arg2	nucleocytoplasmic proteins AND O-GlcNAc	nucleocytoplasmic proteins			O-GlcNAc	Fterm		proteins			Here we show that C/EBPbeta is modified by O-GlcNAc, a dynamic single sugar modification found on nucleocytoplasmic proteins.
19478079	4	20	gly	found	671:675	arg2	nucleocytoplasmic proteins AND a dynamic single sugar modification	nucleocytoplasmic proteins			a dynamic single sugar modification	Fterm		proteins			Here we show that C/EBPbeta is modified by O-GlcNAc, a dynamic single sugar modification found on nucleocytoplasmic proteins.
19478079	4	26	gly	modified	613:620	arg1	C/EBPbeta AND a dynamic single sugar modification	C/EBPbeta			a dynamic single sugar modification	PUBTATOR		C/EBPbeta	1051		Here we show that C/EBPbeta is modified by O-GlcNAc, a dynamic single sugar modification found on nucleocytoplasmic proteins.
19478079	4	26	gly	modified	613:620	arg1	C/EBPbeta AND O-GlcNAc	C/EBPbeta			O-GlcNAc	PUBTATOR		C/EBPbeta	1051		Here we show that C/EBPbeta is modified by O-GlcNAc, a dynamic single sugar modification found on nucleocytoplasmic proteins.
22387313	3	18	gly	N-glycosylation	524:538	arg2	eight predicted N-glycosylation sites			eight predicted N-glycosylation sites						sites	DPP10 is a glycoprotein containing eight predicted N-glycosylation sites in the extracellular domain.
22387313	3	52	gly	glycoprotein	484:495	arg1	DPP10	DPP10				PUBTATOR		DPP10	57628		DPP10 is a glycoprotein containing eight predicted N-glycosylation sites in the extracellular domain.
22387313	3	52	gly	glycoprotein	484:495	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			DPP10 is a glycoprotein containing eight predicted N-glycosylation sites in the extracellular domain.
8507662	1	3	gly	glycosylation	233:245	arg2	glycosylation sites			glycosylation sites						sites	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
18533687	1	73	gly	leucine-rich	179:190	arg1	the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family			leucine	the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family					leucine	The relaxin receptor, RXFP1, is a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family.
16263699	1	48	gly	glycoprotein	186:197	arg1	glycoprotein isoforms	glycoprotein isoforms				Fterm		glycoprotein			Among known platelet proteins, a prominent and functionally important group is represented by glycoprotein isoforms.
7613477	0	59	gly	glycosylation	63:75	arg1	apolipoprotein D	apolipoprotein D				PUBTATOR		apolipoprotein D	347		Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	59	gly	glycosylation	63:75	arg1	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D				Fterm		proteins			Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	59	gly	glycosylation	63:75	arg1	lecithin:cholesterol acyltransferase	lecithin:cholesterol acyltransferase				PUBTATOR		lecithin:cholesterol acyltransferase	3931		Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
20145116	13	54	part_of	VEGFR-2	1656:1662	arg1	VEGFR-2 residues	VEGFR-2		VEGFR-2 residues		PUBTATOR	Site	VEGFR-2	3791	residues	This biochemical analysis, together with our structural data, defined VEGFR-2 residues critical for the binding of VEGF-A and VEGF-C.
17980170	0	42	gly	glycosylation	27:39	arg1	N-acylethanolamine-hydrolyzing acid amidase	N-acylethanolamine-hydrolyzing acid amidase				PUBTATOR		N-acylethanolamine-hydrolyzing acid amidase	27163		Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
1281977	11	0	gly	glycosylated	1888:1899	arg1	two non-identical polypeptides			two non-identical polypeptides						polypeptides	These studies indicate that human liver aspartylglucosaminidase is composed of two non-identical polypeptides, each of which is glycosylated.
8636209	5	4	part_of	gamma	673:677	arg1	the EC domain	CD3 gamma		the EC domain		PUBTATOR	Site	CD3 gamma	917	domain	Based on this model and on alignment studies, two potential interaction sites were predicted in the EC domain of CD3 gamma.
11326277	6	24	part_of	receptor	905:912	arg1	this region	G protein-coupled receptor		this region		PUBTATOR	Site	G protein-coupled receptor	23890	region	From this search, we identified a likely candidate: T1R3, a previously unknown G protein-coupled receptor (GPCR) and the only GPCR in this region.
11326277	6	33	part_of	GPCR	934:937	arg1	this region	GPCR		this region		PUBTATOR	Site	GPCR	23890	region	From this search, we identified a likely candidate: T1R3, a previously unknown G protein-coupled receptor (GPCR) and the only GPCR in this region.
8349699	6	16	gly	glycosylation	850:862	arg1	ovine PGH synthase-1	PGH synthase-1		sites		PUBTATOR		PGH synthase-1	19224	sites	N-Glycosylation consensus sequences corresponding to the three glycosylation sites of ovine PGH synthase-1 are conserved in the deduced amino acid sequences of PGH synthases-2.
21308849	3	29	gly	glycoprotein	516:527	arg1	MAG	MAG				PUBTATOR		MAG	4099		It has been shown by others that the LRR and stalk regions of NgR1 and NgR2 have distinct roles in conferring binding affinity to the myelin associated glycoprotein (MAG) in vivo.
21308849	3	29	gly	glycoprotein	516:527	arg1	the myelin associated glycoprotein	the myelin associated glycoprotein				PUBTATOR		myelin associated glycoprotein	4099		It has been shown by others that the LRR and stalk regions of NgR1 and NgR2 have distinct roles in conferring binding affinity to the myelin associated glycoprotein (MAG) in vivo.
25765764	1	28	gly	leucine-rich	178:189	arg1	the LRIG1-LRR (leucine-rich repeat) domain			leucine	the LRIG1-LRR (leucine-rich repeat) domain					leucine	We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells.
25765764	1	28	gly	leucine-rich	178:189	arg1	leucine-rich repeat			leucine	leucine-rich repeat					leucine	We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells.
25765764	1	42	gly	LRIG1-ECD	129:137	arg1	the LRIG1-LRR (leucine-rich repeat) domain	LRIG1			the LRIG1-LRR (leucine-rich repeat) domain	PUBTATOR		LRIG1	26018		We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells.
11502179	4	30	gly	N-glycosylation	699:713	arg2	the six potential N-glycosylation sites			the six potential N-glycosylation sites						sites	This allowed the identification of four out of the six potential N-glycosylation sites as being effectively glycosylated.
15823095	10	1	gly	N-glycosylation	1325:1339	arg1	some Lass proteins	some Lass proteins				Fterm		proteins			The occurrence of N-glycosylation of some Lass proteins provides topological insight, indicating that the N-termini of Lass family members probably face the luminal side of the endoplasmic reticulum membrane.
10704524	2	15	gly	occupied	427:434	arg2	the six potential N-glycosylation sites			the six potential N-glycosylation sites						sites	Mutagenesis studies indicated that the first five (N124, N177, N201, N359, and N385) of the six potential N-glycosylation sites were occupied.
10704524	2	22	gly	N-glycosylation	400:414	arg2	the six potential N-glycosylation sites			the six potential N-glycosylation sites						sites	Mutagenesis studies indicated that the first five (N124, N177, N201, N359, and N385) of the six potential N-glycosylation sites were occupied.
27313224	11	13	part_of	SV2C-LD4	1906:1913	arg1	the SV2C-LD4 peptide	SV2C		the SV2C-LD4 peptide		PUBTATOR	Site	SV2C	22987	peptide	In conclusion, we show the importance of the complex N559-glycan of SV2C-LD4, adding a third anchor point beside a ganglioside and the SV2C-LD4 peptide, for BoNT/A neuronal cell surface binding and uptake.
18729387	2	40	gly	N-glycosylation	464:478	arg2	six or seven potential N-glycosylation sites			six or seven potential N-glycosylation sites						sites	These molecules are composed of three Ig domains and a glycosylphosphatidylinositol (GPI) anchor and contain six or seven potential N-glycosylation sites.
3571205	0	3	gly	Asn-linked	84:93	arg1	the major Asn-linked sugar chains			Asn	the major Asn-linked sugar chains					Asn	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.
3571205	0	37	gly	glycocalicin	42:53	arg1	The carbohydrate moiety	glycocalicin			The carbohydrate moiety	Fterm		glycocalicin			The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.
10764840	3	44	gly	rHuEpo	542:547	arg1	the glycan chains	rHuEpo			the glycan chains	Cterm		rHuEpo	2056		The structure of the glycan chains of this rHuEpo slightly differ of those of the urinary human Epo (uHuEpo), considered as the natural Epo molecule.
23376777	3	38	part_of	KCC4	416:419	arg1	the four putative extracellular N-linked glycosylation sites	KCC4		the four putative extracellular N-linked glycosylation sites		PUBTATOR	Site	KCC4	20499	sites	Site-directed mutagenesis was performed on the four putative extracellular N-linked glycosylation sites of KCC4 to determine the role of these sites in KCC4 half-life, cell surface expression, and transporter activity, as well as in KCC4-dependent tumor formation.
7613477	9	74	gly	glycosylation	1830:1842	arg2	the glycosylation site			the glycosylation site						site	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
11279095	5	33	gly	polysialylate	979:991	arg1	"autopolysialylation"				"autopolysialylation"						To obtain insight into the structure/function of ST8Sia IV, we expressed human ST8Sia IV in insect cells, Trichoplusia ni, and found that the enzyme produced in the insect cells catalyzes NCAM polysialylation, although it cannot polysialylate itself ("autopolysialylation").
2963625	0	52	part_of	H	60:60	arg1	The complete amino acid sequence	complement factor H		The complete amino acid sequence		PUBTATOR	Site	complement factor H	3075	sequence	The complete amino acid sequence of human complement factor H.
1823160	6	30	gly	sialylated	990:999	arg1	The sialylated GalNAc moiety				The sialylated GalNAc moiety						The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	6	81	gly	glycoproteins	1037:1049	arg1	N-linked glycoproteins	glycoproteins			The sialylated GalNAc moiety	Fterm		glycoproteins			The sialylated GalNAc moiety is unique in N-linked glycoproteins.
15807535	10	102	gly	N-glycosylation	1843:1857	arg1	ABCG2	ABCG2		arginine 596		PUBTATOR		ABCG2	Q9UNQ0	arginine 596	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	10	102	gly	N-glycosylation	1843:1857	arg1	arginine 596			arginine 596						arginine 596	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	10	102	gly	N-glycosylation	1843:1857	arg1	arginine 596	ABCG2		arginine 596		PUBTATOR		ABCG2	Q9UNQ0	arginine 596	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
14699159	5	28	gly	glycosylation	1064:1076	arg2	the N-linked glycosylation site			the N-linked glycosylation site						site	By mutating a single amino acid within the N-linked glycosylation site closest to the carboxyl terminus of p90ATF6, we recreated ATF6(f).
7918467	7	32	part_of	apoA-II	810:816	arg1	Cys6	apoA-II		Cys6		PUBTATOR	AminoAcid	apoA-II	336	Cys6	Using a combination of manual Edman degradations and mass spectrometric analysis on a purified cluster of chymotryptic fragments, we identified an intramolecular disulfide bridge between Cys8 and Cys114 and an intermolecular bridge between Cys116 of apoD and Cys6 of apoA-II.
7918467	7	21	part_of	apoD	793:796	arg1	Cys114	apoD		Cys8 and Cys114		PUBTATOR	AminoAcid	apoD	347	Cys8 and Cys114	Using a combination of manual Edman degradations and mass spectrometric analysis on a purified cluster of chymotryptic fragments, we identified an intramolecular disulfide bridge between Cys8 and Cys114 and an intermolecular bridge between Cys116 of apoD and Cys6 of apoA-II.
20507882	7	7	gly	glycopeptides	1308:1320	arg2	Twenty-five glycopeptides			Twenty-five glycopeptides						glycopeptides	Twenty-five glycopeptides were characterized from human alpha-dystroglycan, which provide insight to the complex in vivo O-glycosylation of alpha-dystroglycan.
20507882	7	10	gly	O-glycosylation	1417:1431	arg1	alpha-dystroglycan				alpha-dystroglycan						Twenty-five glycopeptides were characterized from human alpha-dystroglycan, which provide insight to the complex in vivo O-glycosylation of alpha-dystroglycan.
17331201	3	48	gly	glycoproteins	621:633	arg1	Cbln2	Cbln2				PUBTATOR		Cbln2	147381		Here, we demonstrated that in mammalian heterologous cells, Cbln2 and Cbln4 were secreted as N-linked glycoproteins, like Cbln1.
17331201	3	48	gly	glycoproteins	621:633	arg1	N-linked glycoproteins	N-linked glycoproteins				Fterm		glycoproteins			Here, we demonstrated that in mammalian heterologous cells, Cbln2 and Cbln4 were secreted as N-linked glycoproteins, like Cbln1.
17331201	3	48	gly	glycoproteins	621:633	arg1	Cbln4	Cbln4				PUBTATOR		Cbln4	140689		Here, we demonstrated that in mammalian heterologous cells, Cbln2 and Cbln4 were secreted as N-linked glycoproteins, like Cbln1.
8069634	6	31	gly	glycoprotein	1123:1134	arg1	the glycoprotein	the glycoprotein				Fterm		glycoprotein			Comparison between the two structures showed that the protein part of the glycoprotein has little influence on either the stabilization of the complex or the sugar conformation.
29794134	3	60	part_of	apo-WT	596:601	arg1	the extracellular ligand-binding domains	apo		the extracellular ligand-binding domains		OGER	Site	apo	Q8N6M6	domains	Here, we report three high-resolution structures of the extracellular ligand-binding domains (ECDs) of R47H TREM2, apo-WT, and phosphatidylserine (PS)-bound WT TREM2 at 1.8, 2.2, and 2.2 Å, respectively.
29794134	3	67	part_of	TREM2	641:645	arg1	the extracellular ligand-binding domains	WT TREM2		the extracellular ligand-binding domains		PUBTATOR	Site	WT TREM2	54209	domains	Here, we report three high-resolution structures of the extracellular ligand-binding domains (ECDs) of R47H TREM2, apo-WT, and phosphatidylserine (PS)-bound WT TREM2 at 1.8, 2.2, and 2.2 Å, respectively.
29794134	3	69	part_of	TREM2	589:593	arg1	the extracellular ligand-binding domains	TREM2		the extracellular ligand-binding domains		PUBTATOR	Site	TREM2	54209	domains	Here, we report three high-resolution structures of the extracellular ligand-binding domains (ECDs) of R47H TREM2, apo-WT, and phosphatidylserine (PS)-bound WT TREM2 at 1.8, 2.2, and 2.2 Å, respectively.
16046623	4	19	part_of	channel	703:709	arg1	Leu469	channel		Leu469		Fterm	AminoAcid	channel		Leu469	Firstly, Leu469 at the substrate channel may play a key role in controlling the substrate entry; depending on its conformation, it either blocks or gives access to the active site.
2001369	10	28	gly	attached	1531:1538	arg1	Asn-300 AND the oligosaccharides			Asn-300	the oligosaccharides					Asn-300	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
28775322	4	54	part_of	EGF-like	795:802	arg1	folded EGF-like domains	EGF		folded EGF-like domains		OGER	Site	EGF	P01133	domains	Notably, we show that Protein O-glucosyltransferase 1's requirement for folded EGF-like domains also leads to its serine specificity and that two distinct local conformational states are likely responsible for its ability to transfer both glucose and xylose.
21965667	1	7	part_of	G	240:240	arg1	the Fc region	immunoglobulin G		the Fc region		Cterm	Site	immunoglobulin G		region	Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG).
7776966	5	24	part_of	FSHR	716:719	arg1	other regions	FSHR		other regions		PUBTATOR	Site	FSHR	2492	regions	Therefore, although other regions of the FSHR may contribute to hormone binding, the extracellular domain alone can confer high affinity binding.
7654718	10	3	part_of	C-tail	1520:1525	arg1	C-tail fragment	C-tail		C-tail fragment		Cterm	Site	C-tail		fragment	C-tail fragment was also found to bind jacalin lectin.
21500857	2	56	gly	glycoprotein	372:383	arg1	modified glycoprotein	modified glycoprotein				Fterm		glycoprotein			Assembly protein AP180 is a synapse-specific phosphoprotein and O-linked beta-N-acetylglucosamine (O-GlcNAc) modified glycoprotein.
7694285	2	76	gly	[CGT	334:337	arg1	UDPgalactose	UDPgalactosyltransferase [CGT			UDPgalactose	PUBTATOR		UDPgalactosyltransferase [CGT	7368		Cerebrosides are synthesized by ceramide UDPgalactosyltransferase [CGT; 2-hydroxyacylsphinogosine 1-beta-galactosyl-transferase; UDPgalactose:2-(2-hydroxyacyl)sphingosine 1-beta-D-galactosyltransferase; UDPgalactose:2-(2-hydroxyacyl)sphingosine 1-beta-D-galactosyltransferase, EC 2.4.1.45] with UDPgalactose and ceramide as substrates.
7613477	4	25	gly	glycopeptides	1032:1044	arg2	the glycopeptides			the glycopeptides						glycopeptides	Structural information on the oligosaccharides from all eight glycopeptides was obtained by sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS.
7613477	4	103	gly	glycopeptides	962:974	arg1	the oligosaccharides			glycopeptides	the oligosaccharides					glycopeptides	Structural information on the oligosaccharides from all eight glycopeptides was obtained by sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS.
22226965	0	28	gly	PPARγ	25:29	arg1	O-GlcNAc modification	PPARγ 			O-GlcNAc modification	PUBTATOR		PPARγ 	19016		O-GlcNAc modification of PPARγ reduces its transcriptional activity.
7774715	5	1	gly	alpha-1,6-fucosylated	673:693	arg1	total glycans				total glycans						Moreover, 70% of total glycans were alpha-1,6-fucosylated at the GlcNAc residue linked to asparagine.
7774715	5	47	gly	linked	717:722	arg1	asparagine AND the GlcNAc residue			asparagine	the GlcNAc residue					asparagine	Moreover, 70% of total glycans were alpha-1,6-fucosylated at the GlcNAc residue linked to asparagine.
19299457	0	14	part_of	receptor	113:120	arg1	the receptor hinge region	receptor		the receptor hinge region		Fterm	Site	receptor		region	A monoclonal antibody with thyrotropin (TSH) receptor inverse agonist and TSH antagonist activities binds to the receptor hinge region as well as to the leucine-rich domain.
17286803	5	39	gly	non-glycosylated	585:600	arg1	Both partially and non-glycosylated CLN3	Both partially and non-glycosylated CLN3				OGER		CLN3	Q13286		Both partially and non-glycosylated CLN3 were transported correctly to lysosomes.
17293352	6	104	gly	GAA	667:669	arg1	The N-linked glycans	GAA			The N-linked glycans	PUBTATOR		GAA	2548		The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
15536627	0	42	gly	transferrin	46:56	arg1	Site-specific carbohydrate profiling	transferrin			Site-specific carbohydrate profiling	PUBTATOR		transferrin	7018		Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry.
24161696	1	14	part_of	glycoproteins	195:207	arg1	occupied N-glycosylation sites	glycoproteins		occupied N-glycosylation sites		Fterm	Site	glycoproteins		sites	BACKGROUND: Vacancy of occupied N-glycosylation sites of glycoproteins is quite disruptive to a multicellular organism, as underlined by congenital disorders of glycosylation.
2813359	4	62	part_of	had	711:713	arg1	EPO-tetra AND the same amino acid composition	EPO		position		PUBTATOR	Site	EPO	2056	position	EPO-bi, EPO-tetra, and the standard EPO had the same amino acid composition and immunoreactivity.
2813359	4	62	part_of	had	711:713	arg1	EPO-bi AND the same amino acid composition	EPO		position		PUBTATOR	Site	EPO	2056	position	EPO-bi, EPO-tetra, and the standard EPO had the same amino acid composition and immunoreactivity.
2813359	4	62	part_of	had	711:713	arg1	EPO-bi AND the same amino acid composition	EPO		position		PUBTATOR	Site	EPO	2056	position	EPO-bi, EPO-tetra, and the standard EPO had the same amino acid composition and immunoreactivity.
24530628	7	61	gly	glycopeptide	1095:1106	arg2	glycopeptide enrichment			glycopeptide enrichment						glycopeptide	BIOLOGICAL SIGNIFICANCE: In this study, we established a versatile method for glycopeptide enrichment to acquire reliable mass spectra because of the limitation of conventional enrichment methods, such as lectin affinity chromatography.
29666272	4	32	gly	GlcNAcMan3GlcNAc2-Asn	876:896	arg1	a GlcNAcMan3GlcNAc2-Asn acceptor complex to reveal the structural basis for substrate recognition and catalysis			Asn	a GlcNAcMan3GlcNAc2-Asn acceptor complex to reveal the structural basis for substrate recognition and catalysis					Asn	We determined the structure of human MGAT2 as a Mn2+-UDP donor analog complex and as a GlcNAcMan3GlcNAc2-Asn acceptor complex to reveal the structural basis for substrate recognition and catalysis.
447737	4	34	gly	glycopeptide	839:850	arg2	the pronase glycopeptide			the pronase glycopeptide						glycopeptide	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
22678432	4	60	gly	glycopeptide	819:830	arg2	specific glycopeptide enrichment steps			specific glycopeptide enrichment steps						glycopeptide	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
25153361	5	27	gly	glycoproteins	801:813	arg1	human alpha-1-acid glycoprotein	human alpha-1-acid glycoprotein				OGER		glycoprotein (5	P40197		We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	27	gly	glycoproteins	801:813	arg1	human transferrin	human transferrin				PUBTATOR		transferrin	7018		We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	27	gly	glycoproteins	801:813	arg1	influenza A virus hemagglutinin	influenza A virus hemagglutinin				Fterm		hemagglutinin			We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	27	gly	glycoproteins	801:813	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	55	gly	glycoprotein	875:886	arg1	5 sequons	glycoprotein (5				OGER		glycoprotein (5	P40197		We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
18952059	2	25	gly	glycosylation	207:219	arg2	a conserved glycosylation site			a conserved glycosylation site						site	It contains one immunoglobulin-like domain with a conserved glycosylation site within.
22809326	12	10	gly	glycoprotein	1521:1532	arg1	the lysosomal glycoprotein coat	the lysosomal glycoprotein coat				Fterm		glycoprotein			The models correspond to the thickness of the lysosomal glycoprotein coat of only 5 to 12 nm, according to electron microscopy.
8416919	1	2	gly	kallidinogenase	223:237	arg1	terminal GalNAc-containing N-linked oligosaccharides	kallidinogenase			terminal GalNAc-containing N-linked oligosaccharides	Fterm		kallidinogenase			Fifteen different structures of terminal GalNAc-containing N-linked oligosaccharides from human urinary kallidinogenase have been identified.
9450956	5	36	gly	nonglycosylated	561:575	arg1	nonglycosylated RNase 4	nonglycosylated RNase 4				PUBTATOR		RNase 4	6038		Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1-13 to be sufficient for C-mannosylation.
1823160	0	80	gly	sialylated	8:17	arg1	the major complex-type structure				the major complex-type structure						A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	0	80	gly	sialylated	8:17	arg1	A novel sialylated N-acetylgalactosamine-containing oligosaccharide				A novel sialylated N-acetylgalactosamine-containing oligosaccharide						A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
8631363	3	11	gly	contained	418:426	arg1	the tumor necrosis factor-alpha AND galactose	the tumor necrosis factor-alpha			galactose	PUBTATOR		tumor necrosis factor-alpha	7124		Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	11	gly	contained	418:426	arg1	the tumor necrosis factor-alpha AND N-acetylneuraminic acid	the tumor necrosis factor-alpha			N-acetylneuraminic acid	PUBTATOR		tumor necrosis factor-alpha	7124		Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	11	gly	contained	418:426	arg1	the tumor necrosis factor-alpha AND N-acetylgalactosamine	the tumor necrosis factor-alpha			N-acetylgalactosamine	PUBTATOR		tumor necrosis factor-alpha	7124		Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	11	gly	contained	418:426	arg1	the tumor necrosis factor-alpha AND sugar components	the tumor necrosis factor-alpha			sugar components	PUBTATOR		tumor necrosis factor-alpha	7124		Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
9395518	3	10	part_of	glycoprotein	504:515	arg1	five putative transmembrane domains	glycoprotein		five putative transmembrane domains		Fterm	Site	glycoprotein		domains	It codes for a 30-kDa plasma membrane glycoprotein with five putative transmembrane domains.
11805077	2	43	gly	found	386:390	arg1	EPO AND sulfated N-linked oligosaccharides	EPO			sulfated N-linked oligosaccharides	OGER		EPO	P01588		Using LC/MS with GCC, sulfated N-linked oligosaccharides were found in erythropoietin (EPO) expressed in baby hamster kidney cells.
11805077	2	43	gly	found	386:390	arg1	erythropoietin AND sulfated N-linked oligosaccharides	erythropoietin			sulfated N-linked oligosaccharides	OGER		erythropoietin	P01588		Using LC/MS with GCC, sulfated N-linked oligosaccharides were found in erythropoietin (EPO) expressed in baby hamster kidney cells.
19358553	0	97	gly	glycopeptides	41:53	arg2	N-linked glycopeptides			N-linked glycopeptides						glycopeptides	Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS: strong correlation between signal strength and glycoform quantities.
1533633	1	70	gly	glycosylation	153:165	arg1	mannose residues				mannose residues						The glycosylation and subsequent phosphorylation of mannose residues is a pivotal modification during the biosynthesis of lysosomal enzymes.
7518437	0	17	gly	glycosylation	84:96	arg2	glycosylation site insertion			glycosylation site insertion						site	Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion.
10894551	8	32	part_of	domain	1184:1189	arg1	A conserved chloride-binding site	domain		A conserved chloride-binding site						site	A conserved chloride-binding site is located in the membrane distal domain, and we found that hormone binding is chloride dependent.
23602662	5	40	part_of	contain	630:636	arg1	CD200 AND two Ig-like domains	CD200		two Ig-like domains		PUBTATOR	Site	Both CD200	4345	domains	Both CD200 and CD200R contain two Ig-like domains and interact through their NH₂ terminal domains compatible with immunological synapse-like interactions occurring between myeloid cells and other CD200-expressing cells.
23602662	5	40	part_of	contain	630:636	arg1	CD200R AND two Ig-like domains	CD200R		two Ig-like domains		PUBTATOR	Site	CD200R	131450	domains	Both CD200 and CD200R contain two Ig-like domains and interact through their NH₂ terminal domains compatible with immunological synapse-like interactions occurring between myeloid cells and other CD200-expressing cells.
22846996	5	10	part_of	BTN3A	1032:1036	arg1	the BTN3A Ig-V domain	BTN3A		the BTN3A Ig-V domain		Cterm	Site	BTN3A	10384	domain	The 20.1 and 103.2 antibodies bind to separate epitopes on the BTN3A Ig-V domain with high affinity but likely with different valencies based on their binding orientation.
22846996	5	34	part_of	epitopes	1016:1023	arg1	the BTN3A Ig-V domain	epitopes		the BTN3A Ig-V domain						domain	The 20.1 and 103.2 antibodies bind to separate epitopes on the BTN3A Ig-V domain with high affinity but likely with different valencies based on their binding orientation.
16877748	7	55	gly	sialylated	1222:1231	arg1	some sialylated N-glycans				some sialylated N-glycans						In some sialylated N-glycans, one N-acetylneuraminic acid was replaced by N-glycolylneuraminic acid, and approximately 4% carried a higher number of sialic acid residues than of antennae.
30140003	5	52	part_of	GnT-V	580:584	arg1	GnT-V luminal domain	GnT-V		GnT-V luminal domain		PUBTATOR	Site	GnT-V	4249	domain	GnT-V luminal domain is composed of a GT-B fold and two accessary domains.
25081999	1	24	part_of	subunit	267:273	arg1	the C-terminal domain	subunit		the C-terminal domain		Fterm	Site	subunit		domain	RNA polymerase II carboxyl-terminal domain (RNAPII CTD) phosphatases are responsible for the dephosphorylation of the C-terminal domain of the small subunit of RNAPII in eukaryotes.
25081999	1	48	part_of	RNA	118:120	arg1	RNA polymerase II carboxyl-terminal domain	RNA polymerase II		RNA polymerase II carboxyl-terminal domain		OGER	Site	RNA polymerase II		domain	RNA polymerase II carboxyl-terminal domain (RNAPII CTD) phosphatases are responsible for the dephosphorylation of the C-terminal domain of the small subunit of RNAPII in eukaryotes.
25081999	1	51	part_of	polymerase	122:131	arg1	RNA polymerase II carboxyl-terminal domain	RNA polymerase II		RNA polymerase II carboxyl-terminal domain		OGER	Site	RNA polymerase II		domain	RNA polymerase II carboxyl-terminal domain (RNAPII CTD) phosphatases are responsible for the dephosphorylation of the C-terminal domain of the small subunit of RNAPII in eukaryotes.
25728924	3	20	part_of	Olf	416:418	arg1	olfactomedin-like (Olf) domains	Olf		olfactomedin-like (Olf) domains		PUBTATOR	Site	Olf	83857	domains	We present crystallographic data for the mouse Latrophilin3 lectin and olfactomedin-like (Olf) domains, thereby revealing the Olf β-propeller fold and conserved calcium-binding site.
9689040	0	33	part_of	fibrinogen-420	61:74	arg1	a recombinant alphaEC domain	fibrinogen		a recombinant alphaEC domain		PUBTATOR	Site	fibrinogen	2244	domain	Crystal structure of a recombinant alphaEC domain from human fibrinogen-420.
21932778	8	31	gly	N-glycosylation	1430:1444	arg2	the N-glycosylation sites			the N-glycosylation sites						sites	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	8	64	gly	N-deglycosylated	1374:1389	arg1	N-deglycosylated glypican-1	N-deglycosylated glypican-1				PUBTATOR		N-deglycosylated glypican-1	2817		A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
30237853	4	73	gly	O-glycoproteins	653:667	arg1	O-glycoproteins	O-glycoproteins				Fterm		O-glycoproteins			Here, we describe a glycoproteomics strategy for deep quantitative mapping of N- and O-glycoproteins in urine with a view to investigate the diagnostic value of the glycoproteome to discriminate PCa from benign prostatic hyperplasia (BPH), two conditions that remain difficult to clinically stratify.
3200844	8	11	gly	glycopeptide	1100:1111	arg2	the original glycopeptide sequence			the original glycopeptide sequence						glycopeptide sequence	This open reading frame contained a CNBr fragment identical to the original glycopeptide sequence and a second CNBr fragment corresponding to a nonglycosylated peptide that was also isolated from the purified pore glycoprotein.
3200844	8	20	gly	nonglycosylated	1168:1182	arg1	a nonglycosylated peptide			a nonglycosylated peptide						peptide	This open reading frame contained a CNBr fragment identical to the original glycopeptide sequence and a second CNBr fragment corresponding to a nonglycosylated peptide that was also isolated from the purified pore glycoprotein.
3200844	8	33	gly	glycoprotein	1238:1249	arg1	the purified pore glycoprotein	the purified pore glycoprotein				Fterm		glycoprotein			This open reading frame contained a CNBr fragment identical to the original glycopeptide sequence and a second CNBr fragment corresponding to a nonglycosylated peptide that was also isolated from the purified pore glycoprotein.
8962717	1	63	gly	glycosylation	290:302	arg2	eleven consensus N-linked glycosylation sites			eleven consensus N-linked glycosylation sites						sites	The extracellular domain (621 N-terminal amino acids) of the p170 epidermal growth factor (EGF) receptor has eleven consensus N-linked glycosylation sites.
20188224	3	40	gly	N-glycosylation	419:433	arg2	five N-glycosylation consensus sequons			five N-glycosylation consensus sequons							PGRN is a glycoprotein, containing five N-glycosylation consensus sequons, three of which fall within granulin domains.
20188224	3	46	gly	glycoprotein	389:400	arg1	PGRN	PGRN				PUBTATOR		PGRN	2896		PGRN is a glycoprotein, containing five N-glycosylation consensus sequons, three of which fall within granulin domains.
20188224	3	46	gly	glycoprotein	389:400	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			PGRN is a glycoprotein, containing five N-glycosylation consensus sequons, three of which fall within granulin domains.
7309709	0	1	gly	prothrombin	62:72	arg1	the carbohydrate moiety	prothrombin			the carbohydrate moiety	PUBTATOR		prothrombin	2147		Studies on the structures of the carbohydrate moiety of human prothrombin.
7574684	0	15	gly	N-glycosylation	73:87	arg2	N-glycosylation sites			N-glycosylation sites						sites	Extracellular domain of neurotrophin receptor trkB: disulfide structure, N-glycosylation sites, and ligand binding.
2943741	4	21	gly	Gal	750:752	arg1	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	GalNAcOH, Gal beta			NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	OGER		GalNAcOH, Gal beta	Q8N6F7		Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	4	74	gly	beta	754:757	arg1	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	GalNAcOH, Gal beta			NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	OGER		GalNAcOH, Gal beta	Q8N6F7		Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
22041449	2	44	gly	leucine-rich	310:321	arg1	the leucine-rich repeat proteins			leucine	the leucine-rich repeat proteins					leucine	Two netrin G proteins are encoded in vertebrate genomes, netrins G1 and G2, which are known to bind the leucine-rich repeat proteins netrin G ligand (NGL)-1 and NGL-2, respectively.
26828122	5	1	gly	Glycosylation	967:979	arg1	hTPPT	hTPPT				PUBTATOR		hTPPT	80736		Glycosylation of hTPPT was shown, by mean of site-directed mutagenesis, to occur at Asn(69), Asn(155), Asn(197), Asn(393), and Asn(416).
14693913	5	41	part_of	hBSSL	862:866	arg1	The C-terminal 192 residues	hBSSL		The C-terminal 192 residues		PUBTATOR	Site	hBSSL	1056	residues	The C-terminal 192 residues of hBSSL contain 16 Pro-rich 11-amino-acid repeats, which include 32 Ser/Thr residues as potential O-glycosylation sites.
1991473	7	79	part_of	subunit	1181:1187	arg1	Asn52	subunit		Asn52		Fterm	AminoAcid	subunit		Asn52	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	7	79	part_of	subunit	1181:1187	arg1	Asn78	subunit		Asn78		Fterm	AminoAcid	subunit		Asn78	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
8615697	5	107	part_of	thyroglobulin	791:803	arg1	the amino acid sequence	thyroglobulin		the amino acid sequence		OGER	Site	thyroglobulin	P01266	sequence	The purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin.
18988733	2	24	part_of	site	411:414	arg1	NFkappaB p65	NFkappaB p65		site		PUBTATOR	Site	NFkappaB p65	4790	site	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
20356926	8	6	gly	deglycosylated	871:884	arg1	unglycosylated or deglycosylated CREB-H	unglycosylated or deglycosylated CREB-H				PUBTATOR		CREB-H	84699		Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	8	51	gly	unglycosylated	853:866	arg1	unglycosylated or deglycosylated CREB-H	unglycosylated or deglycosylated CREB-H				PUBTATOR		CREB-H	84699		Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
24190431	1	14	part_of	susceptibility	228:241	arg1	the shared susceptibility epitope	us		the shared susceptibility epitope		PUBTATOR	Site	us	3123	epitope	Rheumatoid arthritis (RA) is strongly associated with the human leukocyte antigen (HLA)-DRB1 locus that possesses the shared susceptibility epitope (SE) and the citrullination of self-antigens.
24190431	1	67	part_of	possesses	207:215	arg1	the human leukocyte antigen (HLA)-DRB1 locus AND the shared susceptibility epitope	the human leukocyte antigen (HLA)-DRB1 locus		the shared susceptibility epitope		PUBTATOR	Site	us	3123	epitope	Rheumatoid arthritis (RA) is strongly associated with the human leukocyte antigen (HLA)-DRB1 locus that possesses the shared susceptibility epitope (SE) and the citrullination of self-antigens.
1694179	9	28	gly	glycosylated	1241:1252	arg1	beta protein C	beta protein C		asparagine 329		Cterm		beta protein C		asparagine 329	It is asparagine 329 that is not glycosylated in beta protein C since antibodies to a synthetic peptide based on the sequence around this amino acid react only with beta protein C.
1694179	9	28	gly	glycosylated	1241:1252	arg1	asparagine 329			asparagine 329						asparagine 329	It is asparagine 329 that is not glycosylated in beta protein C since antibodies to a synthetic peptide based on the sequence around this amino acid react only with beta protein C.
1694179	9	28	gly	glycosylated	1241:1252	arg1	asparagine 329	beta protein C		asparagine 329		Cterm		beta protein C		asparagine 329	It is asparagine 329 that is not glycosylated in beta protein C since antibodies to a synthetic peptide based on the sequence around this amino acid react only with beta protein C.
27416963	6	52	part_of	JUNO	907:910	arg1	the conserved, surface-exposed tryptophan residue	JUNO		the conserved, surface-exposed tryptophan residue		PUBTATOR	AminoAcid	JUNO	64931	tryptophan residue	Further complementation of Juno knockout eggs with mutant Juno messenger RNAs revealed that the conserved, surface-exposed tryptophan residue of JUNO is required for sperm binding and fertilization.
1567356	0	19	gly	glycoprotein	63:74	arg1	human alpha 1-acid glycoprotein	human alpha 1-acid glycoprotein				Fterm		glycoprotein			Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	0	67	gly	glycosylation	21:33	arg2	the five glycosylation sites	glycoprotein		sites		Fterm		glycoprotein		sites	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1991473	1	47	gly	glycoprotein	168:179	arg1	a heterodimeric glycoprotein	a heterodimeric glycoprotein				Fterm		glycoprotein			Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	1	47	gly	glycoprotein	168:179	arg1	Human lutropin	Human lutropin				Fterm		lutropin			Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
2040278	0	0	gly	glycoproteins	107:119	arg1	respiratory-mucus glycoproteins	respiratory-mucus glycoproteins				Fterm		glycoproteins			Isolation and structural characterization of novel neutral oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
1463457	5	8	part_of	contains	887:894	arg1	The predicted sequence AND 13 potential N-glycosylation sites	The predicted sequence		13 potential N-glycosylation sites						sites	The predicted sequence has 552 amino acids with a leader peptide of 36 amino acids and contains 13 potential N-glycosylation sites, of which it is likely that 10 are used.
7776966	3	92	gly	glycosylated	445:456	arg1	this truncated receptor	this truncated receptor				Fterm		receptor			We show that this truncated receptor is glycosylated, through the carbohydrates are not as fully processed as those of the full-length receptor.
10066782	0	57	gly	N-glycosylation	29:43	arg1	the human interleukin-6 receptor	interleukin-6 receptor		sites		PUBTATOR		interleukin-6 receptor	3570	sites	Disulfide bond structure and N-glycosylation sites of the extracellular domain of the human interleukin-6 receptor.
10066782	0	57	gly	N-glycosylation	29:43	arg1	the extracellular domain	interleukin-6 receptor		domain		PUBTATOR		interleukin-6 receptor	3570	domain	Disulfide bond structure and N-glycosylation sites of the extracellular domain of the human interleukin-6 receptor.
10066782	0	57	gly	N-glycosylation	29:43	arg2	the extracellular domain	interleukin-6 receptor		domain		PUBTATOR		interleukin-6 receptor	3570	domain	Disulfide bond structure and N-glycosylation sites of the extracellular domain of the human interleukin-6 receptor.
10066782	0	57	gly	N-glycosylation	29:43	arg2	the extracellular domain			domain						domain	Disulfide bond structure and N-glycosylation sites of the extracellular domain of the human interleukin-6 receptor.
10704524	10	53	part_of	enzymes	2024:2030	arg1	enzyme structure/domains	enzymes		enzyme structure/domains		Fterm	Site	enzymes		structure/domains	Comparison of the oligosaccharide structures of alpha-GalNAc and alpha-galactosidase A, an evolutionary-related and highly homologous exoglycosidase, indicated that alpha-GalNAc had more completed complex chains, presumably due to differences in enzyme structure/domains, rate of biosynthesis, and/or aggregation of the overexpressed recombinant enzymes.
10704524	10	85	part_of	enzyme	1924:1929	arg1	enzyme structure/domains	enzyme		enzyme structure/domains		Fterm	Site	enzyme		structure/domains	Comparison of the oligosaccharide structures of alpha-GalNAc and alpha-galactosidase A, an evolutionary-related and highly homologous exoglycosidase, indicated that alpha-GalNAc had more completed complex chains, presumably due to differences in enzyme structure/domains, rate of biosynthesis, and/or aggregation of the overexpressed recombinant enzymes.
9530955	5	42	gly	deglycosylation	815:829	arg1	[125I]-labeled urine epitectin	epitectin				Fterm		epitectin			Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin resulted in extremely polydisperse products.
19556306	6	18	gly	TLR4	975:978	arg1	complex type N-glycans	TLR4			complex type N-glycans	PUBTATOR		TLR4	7099		The amount of the 130 kDa TLR4(C88A) with complex type N-glycans expressed on the cell surface depended on that of MD-2 transfected.
11710528	3	19	part_of	hTR	512:514	arg1	hTR glycopeptides	hTR		hTR glycopeptides		PUBTATOR	Site	hTR	P25116	glycopeptides	The composition analysis of hTR glycopeptides revealed that Con A-I contains both mannose and fucose, whereas Con A-III has mannose exclusively.
6619128	3	32	part_of	protein	291:297	arg1	the 3 asparagine glycosylation sites	protein		the 3 asparagine glycosylation sites		Fterm	Site	protein		sites	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
24125761	8	14	gly	unglycosylated	1160:1173	arg1	unglycosylated protein	unglycosylated protein				Fterm		protein			The treatment of wild-type AADAC-expressing HuH-7 cells with tunicamycin, which produces unglycosylated protein, decreased AADAC enzyme activity.
1567356	7	70	gly	glycosylation	1019:1031	arg2	Only glycosylation site II			Only glycosylation site II						site	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
16944957	1	2	gly	N-glycosylation	104:118	arg2	map N-glycosylation sites			map N-glycosylation sites						sites	A procedure to map N-glycosylation sites is presented here.
1731338	3	81	part_of	galactoglycoprotein	606:624	arg1	peptide sequences	galactoglycoprotein		peptide sequences		PUBTATOR	Site	galactoglycoprotein	6693	sequences	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
19379732	3	5	gly	glycosylated	512:523	arg1	WT hSVCT1	WT hSVCT1				PUBTATOR		WT hSVCT1	9963		PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	50	gly	N-glycosylation	577:591	arg2	the three putative N-glycosylation sites			the three putative N-glycosylation sites						sites, Asn138, Asn144, Asn230	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	60	gly	and	525:527	arg1	Asn230			sites, Asn138, Asn144, Asn230						sites, Asn138, Asn144, Asn230	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	60	gly	and	525:527	arg1	Asn144			sites, Asn138, Asn144, Asn230						sites, Asn138, Asn144, Asn230	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	60	gly	and	525:527	arg1	Asn144			sites, Asn138, Asn144, Asn230						sites, Asn138, Asn144, Asn230	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
23319596	8	74	gly	N-glycosylation	1238:1252	arg2	Asn-644			Asn-644						Asn-644	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	8	74	gly	N-glycosylation	1238:1252	arg2	The N-glycosylation site			The N-glycosylation site						site	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
27966990	6	61	part_of	VEGFR-2	1013:1019	arg1	all seven VEGFR-2 immunoglobulin-like domains	VEGFR-2		all seven VEGFR-2 immunoglobulin-like domains		PUBTATOR	Site	VEGFR-2	P35968	domains	The data demonstrated that all seven VEGFR-2 immunoglobulin-like domains have at least one occupied N-glycosylation site.
27966990	6	34	part_of	have	1049:1052	arg1	all seven VEGFR-2 immunoglobulin-like domains AND at least one occupied N-glycosylation site	all seven VEGFR-2 immunoglobulin-like domains		at least one occupied N-glycosylation site						site	The data demonstrated that all seven VEGFR-2 immunoglobulin-like domains have at least one occupied N-glycosylation site.
9530955	1	2	gly	glycoprotein	159:170	arg1	epitectin	epitectin				Fterm		epitectin			The MUC1 glycoprotein, epitectin, a component of the human bladder epithelium, was purified from human urine.
9530955	1	2	gly	glycoprotein	159:170	arg1	The MUC1 glycoprotein	The MUC1 glycoprotein				PUBTATOR		MUC1 glycoprotein	4582		The MUC1 glycoprotein, epitectin, a component of the human bladder epithelium, was purified from human urine.
29741879	7	8	gly	glycopeptides	1620:1632	arg2	4 554 glycopeptides			4 554 glycopeptides						glycopeptides	Reanalysis of the CPTAC data set resulted in the identification of 2 683 glycopeptides from the global proteomic data set and 4 554 glycopeptides from phosphoproteomic data set, respectively.
29741879	7	49	gly	glycopeptides	1561:1573	arg2	2 683 glycopeptides			2 683 glycopeptides						glycopeptides	Reanalysis of the CPTAC data set resulted in the identification of 2 683 glycopeptides from the global proteomic data set and 4 554 glycopeptides from phosphoproteomic data set, respectively.
17591618	11	37	gly	disialylated	1687:1698	arg1	diantennary disialylated structures				diantennary disialylated structures						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn1011			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn511			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn804			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn1077			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn700			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn511			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn804			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn1077			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn700			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn804			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn1077			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn700			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn1077			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn700			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn700			Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077						Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
18508581	4	12	gly	hyperglycosylated	588:604	arg1	EpCAM	EpCAM				PUBTATOR		EpCAM	4072		EpCAM was hyperglycosylated in carcinoma tissue as compared with autologous normal epithelia.
8942648	3	29	gly	mapping	375:381	arg1	human TPO	human TPO				PUBTATOR		TPO	7066		Peptide, disulfide, and glycosylation mapping of human TPO from residues 1 to 246 has been carried out using liquid chromatography-electrospray mass spectrometry (LC-ESMS).
29671580	2	28	gly	glycosylation	548:560	arg1	glycosite-containing peptides			peptides	N-linked glycans					peptides	In this study, we profiled serum N-glycoproteome by our recently developed N-glycoproteomic method using solid-phase extraction of N-linked glycans and glycosite-containing peptides (NGAG) coupled with LC-MS/MS and site-specific glycosylation analysis using GPQuest software.
26791533	6	68	gly	glycoproteins	885:897	arg1	human seminal plasma total glycoproteins	human seminal plasma total glycoproteins				Fterm		glycoproteins			This strategy has been applied to human seminal plasma total glycoproteins.
25092234	6	82	gly	glycosites	920:929	arg2	the three heavy-chain glycosites			the three heavy-chain glycosites						glycosites	MS analyses of intact hFXI revealed full occupation of two of the three heavy-chain glycosites and almost full-site occupancy of the light chain.
16698036	6	23	part_of	alpha-subunit	1016:1028	arg1	Only the alpha-subunit active site	alpha-subunit		Only the alpha-subunit active site		Fterm	Site	alpha-subunit		site	Only the alpha-subunit active site can hydrolyze GM2 gangliosides due to a flexible loop structure that is removed post-translationally from beta, and to the presence of alphaAsn423 and alphaArg424.
29251719	1	5	gly	glycoproteins	99:111	arg1	Vertebrate glycoproteins	Vertebrate glycoproteins				Fterm		glycoproteins			Vertebrate glycoproteins and glycolipids are synthesized in complex biosynthetic pathways localized predominantly within membrane compartments of the secretory pathway.
1823160	7	33	gly	structures	1076:1085	arg1	rmt-PA	mt-PA			structures	Cterm		mt-PA			The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	7	55	gly	sites	1166:1170	arg1	the novel oligosaccharide			Asn-184 and Asn-448 sites	the novel oligosaccharide					Asn-184 and Asn-448 sites	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	7	12	gly	contain	1097:1103	arg1	both the Asn-184 and Asn-448 sites AND N-acetyllactosamine moieties			both the Asn-184 and Asn-448 sites	N-acetyllactosamine moieties					Asn-184 and Asn-448 sites	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
21949356	2	12	part_of	protein	291:297	arg1	a CAP10 domain	protein		a CAP10 domain		Fterm	Site	protein		domain	Drosophila Rumi is a soluble, endoplasmic reticulum-retained protein with a CAP10 domain that functions as a protein O-glucosyltransferase.
21949356	2	48	part_of	protein	243:249	arg1	a CAP10 domain	protein		a CAP10 domain		Fterm	Site	protein		domain	Drosophila Rumi is a soluble, endoplasmic reticulum-retained protein with a CAP10 domain that functions as a protein O-glucosyltransferase.
17322565	0	38	gly	Glycosylation	0:12	arg1	endothelial lipase	endothelial lipase		asparagine-116		PUBTATOR		endothelial lipase	9388	asparagine-116	Glycosylation of endothelial lipase at asparagine-116 reduces activity and the hydrolysis of native lipoproteins in vitro and in vivo.
18988733	4	32	gly	modified	732:739	arg1	Thr-322 AND O-GlcNAc			Thr-322 and Thr-352	O-GlcNAc					Thr-322 and Thr-352	Also, we demonstrate that both Thr-322 and Thr-352 of NFkappaB p65 can be modified with O-GlcNAc, but modification on Thr-352, not Thr-322, is important for transcriptional activation.
16895906	4	44	gly	-disialylated	565:577	arg1	the alpha(2,8)-disialylated ganglioside GT1b				the alpha(2,8)-disialylated ganglioside GT1b						We have co-crystallized Siglec-7 with a synthetic oligosaccharide corresponding to the alpha(2,8)-disialylated ganglioside GT1b.
7505568	2	26	gly	glycosylated	217:228	arg1	MAG	MAG				PUBTATOR		MAG	4099		MAG is heavily glycosylated containing 30% carbohydrate by weight.
479158	15	30	gly	glycosylated	1326:1337	arg1	Thr 345			Thr 345						Thr 345	Again Thr 345 was the glycosylated amino acid.
11180632	1	15	gly	residues	140:147	arg1	pig kidney and human urine cerebroside sulfate activator proteins	proteins			residues	Fterm		proteins			The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	15	gly	residues	140:147	arg1	saposin B	saposin B			residues	Cterm		saposin B			The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	44	gly	proteins	254:261	arg1	the oligosaccharides	proteins			the oligosaccharides	Fterm		proteins			The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	44	gly	proteins	254:261	arg1	The specific sugar residues	proteins			The specific sugar residues	Fterm		proteins			The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
20237569	5	46	part_of	Cbl	865:867	arg1	several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains	Cbl		several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains		OGER	Site	Cbl	P22681	domains	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	5	46	part_of	Cbl	865:867	arg1	modular ligand-binding regions	Cbl		modular ligand-binding regions		OGER	Site	Cbl	P22681	regions	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
7514386	7	23	gly	asparagine-linked	866:882	arg1	an asparagine-linked sugar chain			asparagine	an asparagine-linked sugar chain					asparagine	The peptide containing an asparagine-linked sugar chain and the peptide containing a glycan portion of the GPI anchor were isolated after trypsin digestion of U-CD59.
7514386	7	3	gly	containing	912:921	arg1	the peptide AND a glycan portion			the peptide	a glycan portion						The peptide containing an asparagine-linked sugar chain and the peptide containing a glycan portion of the GPI anchor were isolated after trypsin digestion of U-CD59.
7514386	7	18	gly	containing	852:861	arg1	The peptide AND an asparagine-linked sugar chain			The peptide	an asparagine-linked sugar chain					peptide	The peptide containing an asparagine-linked sugar chain and the peptide containing a glycan portion of the GPI anchor were isolated after trypsin digestion of U-CD59.
1371281	5	31	gly	contain	678:684	arg1	cytokeratin 8 and 18 AND single O-linked N-acetylglucosamine residues	cytokeratin 8 and 18			single O-linked N-acetylglucosamine residues	PUBTATOR		cytokeratin 8	3856		beta-Elimination of the [3H]galactose- labeled CK8/18 generated the disaccharide N-acetyllactosaminitol, indicating that cytokeratin 8 and 18 contain single O-linked N-acetylglucosamine residues.
2049076	8	20	part_of	IFN-alpha	1198:1206	arg1	Thr-106	IFN-alpha 2		Thr-106		PUBTATOR	SpecificSite	IFN-alpha 2	3440	Thr-106	These results suggested that Thr-106 of natural IFN-alpha 2 carries O-linked carbohydrates.
16263699	5	63	gly	glycopeptides	702:714	arg2	glycopeptides			glycopeptides						glycopeptides	For the enrichment of glycopeptides, lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides was used.
9677337	3	29	gly	glycosylation	614:626	arg1	both heavy chains	both heavy chains				OGER		chains	P19827		In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
16474139	5	45	gly	glycosylation	937:949	arg1	the coronavirus M proteins	the coronavirus M proteins				Fterm		proteins			The conserved glycosylation of the coronavirus M proteins and the resemblance of the 3a protein to them led us to investigate the glycosylation of these two SARS-CoV membrane proteins.
16474139	5	90	gly	glycosylation	1053:1065	arg1	these two SARS-CoV membrane proteins	these two SARS-CoV membrane proteins				Fterm		proteins			The conserved glycosylation of the coronavirus M proteins and the resemblance of the 3a protein to them led us to investigate the glycosylation of these two SARS-CoV membrane proteins.
17065148	7	48	gly	glycosylation	1145:1157	arg2	the relevant N-linked glycosylation site			the relevant N-linked glycosylation site						site	To separate assembly from trafficking, we investigated the maturation of TRPM8 protein by identifying and mutating the relevant N-linked glycosylation site and showing that glycosylation is neither essential for multimerization nor for transport to the plasma membrane per se but appears to facilitate efficient multimerization and transport.
8174273	3	67	gly	fucosylated	637:647	arg1	a fucosylated trimannosyl core				a fucosylated trimannosyl core						Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
23209641	3	14	part_of	adiponectin	587:597	arg1	the lysine residues	adiponectin		the lysine residues		PUBTATOR	AminoAcid	adiponectin	Q15848	lysine residues	Hydroxylation and, especially, glycosylation of the lysine residues of adiponectin have been shown to be essential for the formation of the more active high molecular weight adiponectin oligomers and thus for its function.
17065148	6	32	part_of	TRPM8	1001:1005	arg1	the membrane-attached C-terminal region	TRPM8		the membrane-attached C-terminal region		PUBTATOR	Site	TRPM8	79054	region	Furthermore, wild-type currents can be suppressed by expressing the membrane-attached C-terminal region of TRPM8.
22848655	12	40	part_of	MSPβ	1807:1810	arg1	the putative MSPβ binding site	MSPβ 		the putative MSPβ binding site		PUBTATOR	Site	MSPβ 	4477	site	Mapping of the dimer interface using the RON homology to Met, MSP homology to Hepatocyte Growth Factor (HGF), and the structure of the Met/HGF complex shows the dimer interface overlapping with the putative MSPβ binding site.
16169851	7	16	part_of	BTLA	893:896	arg1	the extracellular domain	BTLA		the extracellular domain		PUBTATOR	Site	BTLA	151888	domain	Light scattering analysis demonstrates that the extracellular domain of BTLA is monomeric and that BTLA and HVEM form a 1:1 complex.
22387313	0	42	gly	N-glycosylation	0:14	arg1	the mammalian dipeptidyl aminopeptidase-like protein 10	the mammalian dipeptidyl aminopeptidase-like protein 10				PUBTATOR		dipeptidyl aminopeptidase-like protein 10	57628		N-glycosylation of the mammalian dipeptidyl aminopeptidase-like protein 10 (DPP10) regulates trafficking and interaction with Kv4 channels.
22387313	0	42	gly	N-glycosylation	0:14	arg1	DPP10	DPP10				PUBTATOR		DPP10	57628		N-glycosylation of the mammalian dipeptidyl aminopeptidase-like protein 10 (DPP10) regulates trafficking and interaction with Kv4 channels.
25153361	8	85	gly	N-glycosylation	1475:1489	arg2	9 N-glycosylation sequons			9 N-glycosylation sequons							We demonstrated the value of our system to define site-specific glycosylation using a hemagglutinin containing 9 N-glycosylation sequons from a single HILIC-C18-MS acquisition.
29992770	6	67	gly	glycosylation	911:923	arg2	glycosylation site			glycosylation site						site	RESULTS: Combined with a database search using web-based software (GlycopeptideID), MS/MS provided detailed N-glycopeptide information, including glycosylation site, glycan composition, and proposed structures.
29992770	6	40	gly	N-glycopeptide	873:886	arg1	detailed N-glycopeptide information			N-glycopeptide	detailed N-glycopeptide information					N-glycopeptide	RESULTS: Combined with a database search using web-based software (GlycopeptideID), MS/MS provided detailed N-glycopeptide information, including glycosylation site, glycan composition, and proposed structures.
22171320	11	23	part_of	glycoproteins	1846:1858	arg1	58 N-	glycoproteins		58 N-		Fterm	SpecificSite	glycoproteins		N- and 63	In total, 58 N- and 63 O-linked glycopeptides from 53 glycoproteins were characterized with respect to glycan- and peptide sequences.
22171320	11	23	part_of	glycoproteins	1846:1858	arg1	63 O-linked glycopeptides	glycoproteins		63 O-linked glycopeptides		Fterm	Site	glycoproteins		glycopeptides	In total, 58 N- and 63 O-linked glycopeptides from 53 glycoproteins were characterized with respect to glycan- and peptide sequences.
18676855	9	76	part_of	NGEP	1636:1639	arg1	the extracellular regions	NGEP		the extracellular regions		PUBTATOR	Site	NGEP	Q6IWH7	regions	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
7654718	3	16	part_of	C-tail	589:594	arg1	C-tail fragment	C-tail		C-tail fragment		Cterm	Site	C-tail		fragment	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
1581307	8	19	part_of	protein	1498:1504	arg1	the protein domains	protein		the protein domains		Fterm	Site	protein		domains	The protein structure is the same as for the diferric protein, Fe2Lf, demonstrating that the closure of the protein domains over the metal is the same in each case irrespective of whether Fe3+ or Cu2+ is bound and that copper could be transported and delivered to cells equally well as iron.
24721674	1	80	gly	Glycosylation	156:168	arg1	membrane proteins	membrane proteins				Fterm		proteins			Glycosylation of membrane proteins plays an important role in cellular behaviors such as cell-cell interaction, immunologic recognition and cell signaling.
9690478	0	6	part_of	receptor	86:93	arg1	the first three domains	receptor		the first three domains		Fterm	Site	receptor		domains	Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor.
12956774	1	8	gly	glycoprotein	233:244	arg1	a seven-transmembrane glycoprotein	a seven-transmembrane glycoprotein				Fterm		glycoprotein			The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	1	8	gly	glycoprotein	233:244	arg1	chemokines	chemokines				PUBTATOR		Duffy antigen/receptor for chemokines	2532		The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
7613477	1	31	gly	glycosylation	289:301	arg1	human lecithin	human lecithin				PUBTATOR		lecithin:cholesterol acyltransferase	3931		Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
10889209	3	54	gly	N-glycosylation	526:540	arg2	one extracellular consensus N-glycosylation site			one extracellular consensus N-glycosylation site						site	Both GIRK1 and GIRK4 have one extracellular consensus N-glycosylation site.
15152093	8	31	gly	N-glycosylation	1163:1177	arg2	all predicted N-glycosylation sites			all predicted N-glycosylation sites						sites	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	8	36	gly	occupied	1189:1196	arg2	all predicted N-glycosylation sites			all predicted N-glycosylation sites						sites	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	8	32	gly	glycosylation	1241:1253	arg2	sites			sites						sites	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
22052913	7	58	part_of	Fstl3	851:855	arg1	the N-terminal domain	Fstl3		the N-terminal domain		PUBTATOR	Site	Fstl3	10272	domain	The structure reveals that the N-terminal domain (ND) of Fstl3 interacts uniquely with myostatin as compared with activin A, because it utilizes different surfaces on the ligand.
16170054	7	10	gly	N-glycosylation	1144:1158	arg2	19 N-glycosylation sites			19 N-glycosylation sites						sites	We identified 15 glycoproteins with 19 N-glycosylation sites that carry high mannose type glycans by off-line LC-MALDI-TOF/TOF mass spectrometry.
16170054	7	89	gly	glycoproteins	1122:1134	arg1	15 glycoproteins	15 glycoproteins				Fterm		glycoproteins			We identified 15 glycoproteins with 19 N-glycosylation sites that carry high mannose type glycans by off-line LC-MALDI-TOF/TOF mass spectrometry.
16170054	7	34	gly	carry	1171:1175	arg1	15 glycoproteins AND high mannose type glycans	15 glycoproteins			high mannose type glycans	Fterm		glycoproteins			We identified 15 glycoproteins with 19 N-glycosylation sites that carry high mannose type glycans by off-line LC-MALDI-TOF/TOF mass spectrometry.
24279413	8	77	gly	glycopeptides	1427:1439	arg2	103 highly confident N-linked glycopeptides			103 highly confident N-linked glycopeptides						glycopeptides	Using this framework, 103 highly confident N-linked glycopeptides from 53 sites across 33 glycoproteins were identified in complex human serum proteome samples using conventional proteomic platforms with standard depletion of the 7-most abundant proteins.
24279413	8	77	gly	glycopeptides	1427:1439	arg1	53 sites			53 sites						sites	Using this framework, 103 highly confident N-linked glycopeptides from 53 sites across 33 glycoproteins were identified in complex human serum proteome samples using conventional proteomic platforms with standard depletion of the 7-most abundant proteins.
24279413	8	85	gly	glycoproteins	1465:1477	arg1	33 glycoproteins	33 glycoproteins				Fterm		glycoproteins			Using this framework, 103 highly confident N-linked glycopeptides from 53 sites across 33 glycoproteins were identified in complex human serum proteome samples using conventional proteomic platforms with standard depletion of the 7-most abundant proteins.
19671700	0	32	gly	tryptophan	114:123	arg1	C-mannosylation			tryptophan	C-mannosylation					tryptophan	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
19671700	0	92	gly	C-mannosylation	95:109	arg1	tryptophan			tryptophan						tryptophan	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
19671700	0	94	gly	repeats	57:63	arg1	ADAMTS-like 1/punctin-1	ADAMTS-like 1			repeats	PUBTATOR		ADAMTS-like 1	100757121		Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
1380064	7	85	gly	O-glycosylation	1371:1385	arg2	these serine residues			serine residues						serine residues	Upon ESP-MS, EoCP-1 showed an average molecular mass of 8,355 +/- 10 daltons, suggesting O-glycosylation at these serine residues.
30552791	1	32	gly	N-glycosylated	238:251	arg1	N-glycosylated proteins	N-glycosylated proteins				Fterm		proteins			β-Mannosidase is a lysosomal enzyme from the glycosyl hydrolase family 2 that cleaves the single β(1-4)-linked mannose at the nonreducing end of N-glycosylated proteins, and plays an important role in the polysaccharide degradation pathway.
27313224	8	15	gly	core-fucosylated	1315:1330	arg1	The N559-glycan				The N559-glycan						The N559-glycan was characterised as a complex core-fucosylated type with a heterogeneity ranging up to tetra-antennary structure with bisecting N-acetylglucosamine which can establish extensive interactions with BoNT/A.
7780197	3	41	gly	present	401:407	arg2	this site AND The oligosaccharide(s)			this site	The oligosaccharide(s)					site	The oligosaccharide(s) present at this site have been analysed using a combination of site-directed mutagenesis and chemical analysis.
26993603	4	27	gly	glycoforms	629:638	arg2	Asn144			Asn144						Asn144	We found five glycoforms on Asn144, including biantennary, triantennary and fucosylated glycans.
26993603	4	42	gly	fucosylated	691:701	arg1	fucosylated glycans				fucosylated glycans						We found five glycoforms on Asn144, including biantennary, triantennary and fucosylated glycans.
14760718	5	15	gly	N-glycosylation	655:669	arg2	N-glycosylation sites			N-glycosylation sites						sites	Here we demonstrate a procedure for mapping N-glycosylation sites in complex mixtures by reducing sample complexity and enriching glycoprotein content.
14760718	5	52	gly	glycoprotein	741:752	arg1	glycoprotein content	glycoprotein content				Fterm		glycoprotein			Here we demonstrate a procedure for mapping N-glycosylation sites in complex mixtures by reducing sample complexity and enriching glycoprotein content.
1694784	1	40	gly	isolated	205:212	arg2	the reduced and carboxymethylated human protein HC AND Three different carbohydrate prosthetic groups	the reduced and carboxymethylated human protein HC			Three different carbohydrate prosthetic groups	PUBTATOR		protein HC	259		Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1904059	10	43	gly	linked	1489:1494	arg2	a single fucose AND serine 60			serine 60	a single fucose					serine 60	In addition to the O-linked glycan structures observed at serine 52, a single fucose was found to be covalently linked at serine 60 in both human plasma and recombinant factor VII.
1904059	10	126	gly	observed	1423:1430	arg1	serine 52 AND the O-linked glycan structures			serine 52	the O-linked glycan structures					serine 52	In addition to the O-linked glycan structures observed at serine 52, a single fucose was found to be covalently linked at serine 60 in both human plasma and recombinant factor VII.
25802287	14	12	gly	found	2307:2311	arg1	in traces Asn 332 AND hybrid type glycans			in traces Asn 332	hybrid type glycans					Asn 332	Furthermore, hybrid type glycans were found on Asn 402, Asn 171 and in traces Asn 332.
25802287	14	12	gly	found	2307:2311	arg1	Asn 171 AND hybrid type glycans			Asn 402, Asn 171	hybrid type glycans					Asn 402, Asn 171	Furthermore, hybrid type glycans were found on Asn 402, Asn 171 and in traces Asn 332.
3264725	6	106	part_of	found	1243:1247	arg2	human plasma factor VIIa AND the 10 N-terminally located glutamic acid residues	human plasma factor VIIa		the 10 N-terminally located glutamic acid residues		Cterm	AminoAcid	factor VIIa		glutamic acid residues	In human plasma factor VIIa, the 10 N-terminally located glutamic acid residues were found to be fully gamma-carboxylated whereas 9 full and 1 partial gamma-carboxylated residues were found in the corresponding positions of the recombinant factor VIIa molecule.
19122660	1	19	part_of	Sortilin	99:106	arg1	the Sortilin ectodomain	structure of the Sortilin		the Sortilin ectodomain		PUBTATOR	Site	structure of the Sortilin	6272	ectodomain	The structure of the Sortilin ectodomain in complex with neurotensin has been determined at 2-A resolution, revealing that the C-terminal part of neurotensin binds in the tunnel of a ten-bladed beta-propeller domain.
10715549	5	18	gly	Removal	1072:1078	arg3	the carbohydrate unit AND the Asn			Asn(13)	the carbohydrate unit					Asn(13)	Removal of the carbohydrate unit at the Asn(13) of CGbeta caused aggregation, although the amount was less than 10% of monomer.
8627329	2	16	part_of	NTR	265:267	arg1	the ligand-binding domain	NTR		the ligand-binding domain		PUBTATOR	Site	NTR	4923	domain	An O-glycosylated peptide connects the ligand-binding domain of NTR to its transmembrane helix.
20237569	5	19	gly	domains	900:906	arg1	a Ca(2+)-dependent manner				a Ca(2+)-dependent manner						The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
1472036	4	21	part_of	receptor	763:770	arg1	the extracellular domain	insulin receptor		the extracellular domain		PUBTATOR	Site	insulin receptor	3643	domain	Since it has been shown that the extracellular domain of the insulin receptor has no free thiols and since no other sequences containing cysteine were found in these fractions, we conclude that Cys524 forms a disulfide bond to the Cys524 in the other alpha-subunit.
1472036	4	25	part_of	Cys524	925:930	arg1	the other alpha-subunit	subunit		Cys524		OGER	AminoAcid	subunit	3643	Cys524	Since it has been shown that the extracellular domain of the insulin receptor has no free thiols and since no other sequences containing cysteine were found in these fractions, we conclude that Cys524 forms a disulfide bond to the Cys524 in the other alpha-subunit.
1472036	4	35	part_of	containing	820:829	arg1	no other sequences AND cysteine	no other sequences		cysteine						cysteine	Since it has been shown that the extracellular domain of the insulin receptor has no free thiols and since no other sequences containing cysteine were found in these fractions, we conclude that Cys524 forms a disulfide bond to the Cys524 in the other alpha-subunit.
16905106	6	12	part_of	OX40L	804:808	arg1	the interfacial residues	OX40L		the interfacial residues		PUBTATOR	Site	OX40L	7292	residues	Site-directed changes of the interfacial residues of OX40L suggest this interface lacks a single "hot spot" and that instead, binding energy is dispersed over at least two distinct areas.
10842180	4	61	gly	has	660:662	arg1	wild type (wt) Dpl AND two N-linked oligosaccharides	wild type (wt) Dpl			two N-linked oligosaccharides	PUBTATOR		Dpl	26434		Using recombinant Dpl expressed in Escherichia coli and mouse neuroblastoma cells we demonstrate that wild type (wt) Dpl, like PrP(C), adopts a predominantly alpha-helical conformation, forms intramolecular disulfide bonds, has two N-linked oligosaccharides, and is presented on the cell surface via a glycosylphosphatidylinositol anchor.
9884403	0	15	gly	glycoprotein	75:86	arg1	human Tamm-Horsfall glycoprotein	human Tamm-Horsfall glycoprotein				OGER		Tamm-Horsfall glycoprotein	P07911		Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein.
9884403	0	67	gly	glycosylation	38:50	arg1	human Tamm-Horsfall glycoprotein	human Tamm-Horsfall glycoprotein				OGER		Tamm-Horsfall glycoprotein	P07911		Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein.
26791533	10	65	part_of	epitopes	1329:1336	arg1	multiple seminal plasma glycoproteins	glycoproteins		epitopes		Fterm	Site	glycoproteins		epitopes	Many Lewis x/a and y/b epitopes bearing glycans were found, suggesting immune-modulating epitopes on multiple seminal plasma glycoproteins.
15498570	5	31	gly	N-glycosylation	1068:1082	arg1	hPAP21	hPAP21				PUBTATOR		hPAP21	84279		Interestingly, the extracellular forms were primarily sensitive to PNG F, not Endo H, implying that complex N-glycosylation could be required for the secretion of hPAP21.
9295302	2	15	gly	phosphoglycoprotein	205:223	arg1	Multidrug resistance protein	Multidrug resistance protein				PUBTATOR		Multidrug resistance protein	4363		Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	15	gly	phosphoglycoprotein	205:223	arg1	a 190-kDa integral membrane phosphoglycoprotein	a 190-kDa integral membrane phosphoglycoprotein				Fterm		phosphoglycoprotein			Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
16834341	0	14	gly	glycopeptide	72:83	arg2	glycopeptide analysis			glycopeptide analysis						glycopeptide	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	0	60	gly	glycoprotein	29:40	arg1	the glycoprotein follicle stimulating hormone	the glycoprotein follicle stimulating hormone				Fterm		glycoprotein			Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
8390218	4	96	gly	AAT	1354:1356	arg1	the carbohydrate chains	AAT			the carbohydrate chains	PUBTATOR		AAT	5265		These results indicate that a characteristic feature of the carbohydrate chains of AAT from patients with HCC is an increment in fucosylation.
11390601	3	42	part_of	gp120	845:849	arg1	N301	gp120		N301		PUBTATOR	SpecificSite	gp120	3700	N301	Of the glycosylation sites that were evaluated, those proximal to the V1/V2 loops (N135, N141, N156, N160) and the V3 loops (N301) of gp120 were functionally critical.
10894551	4	9	part_of	receptor	589:596	arg1	the glycosylated dimerized hormone-binding domain	ANP receptor		the glycosylated dimerized hormone-binding domain		OGER	Site	ANP receptor	P01160	domain	Here we present the crystal structure of the glycosylated dimerized hormone-binding domain of the ANP receptor at 2.0-A resolution.
1517205	1	13	part_of	protein	341:347	arg1	Ser-53	protein Z		Ser-53		Cterm	SpecificSite	protein Z		Ser-53	We have recently discovered unusual sugar chains (xylose (Xyl)-glucose (Glc) and (Xyl)2-Glc) linked to a serine residue in the epidermal growth factor (EGF)-like domains of human and bovine clotting factors VII (Ser-52), IX (Ser-53), and protein Z (Ser-53), in addition to bovine platelet glycoprotein thrombospondin.
1517205	1	19	part_of	factors	302:308	arg1	the epidermal growth factor (EGF)-like domains	factors		the epidermal growth factor (EGF)-like domains		Fterm	Site	factors		domains	We have recently discovered unusual sugar chains (xylose (Xyl)-glucose (Glc) and (Xyl)2-Glc) linked to a serine residue in the epidermal growth factor (EGF)-like domains of human and bovine clotting factors VII (Ser-52), IX (Ser-53), and protein Z (Ser-53), in addition to bovine platelet glycoprotein thrombospondin.
1517205	1	59	part_of	residue	215:221	arg1	human and bovine clotting factors VII (Ser-52), IX (Ser-53), and protein Z (Ser-53)	factors		residue		Fterm	AminoAcid	factors		serine residue	We have recently discovered unusual sugar chains (xylose (Xyl)-glucose (Glc) and (Xyl)2-Glc) linked to a serine residue in the epidermal growth factor (EGF)-like domains of human and bovine clotting factors VII (Ser-52), IX (Ser-53), and protein Z (Ser-53), in addition to bovine platelet glycoprotein thrombospondin.
1517205	1	99	part_of	factor	247:252	arg1	the epidermal growth factor (EGF)-like domains	factor		the epidermal growth factor (EGF)-like domains		Fterm	Site	factor		domains	We have recently discovered unusual sugar chains (xylose (Xyl)-glucose (Glc) and (Xyl)2-Glc) linked to a serine residue in the epidermal growth factor (EGF)-like domains of human and bovine clotting factors VII (Ser-52), IX (Ser-53), and protein Z (Ser-53), in addition to bovine platelet glycoprotein thrombospondin.
12610629	7	52	part_of	HER2	1301:1304	arg1	the juxtamembrane region	HER2		the juxtamembrane region		PUBTATOR	Site	HER2	2064	region	Herceptin binds to the juxtamembrane region of HER2, identifying this site as a target for anticancer therapies.
8393577	4	53	gly	glycosylation	1060:1072	arg2	Asn-70			Asn-70						Asn-70	Mutagenesis studies have identified a phosphotransferase recognition region that is required for oligosaccharide phosphorylation but is 32 A distant from the N-domain glycosylation site at Asn-70.
8393577	4	53	gly	glycosylation	1060:1072	arg2	the N-domain glycosylation site			the N-domain glycosylation site						site	Mutagenesis studies have identified a phosphotransferase recognition region that is required for oligosaccharide phosphorylation but is 32 A distant from the N-domain glycosylation site at Asn-70.
23001782	6	4	gly	occupied	999:1006	arg2	Both sites			Both sites						sites	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
9786864	3	8	part_of	cytokine-receptor	383:399	arg1	two immunoglobulin-like and cytokine-receptor homology domains	receptor		two immunoglobulin-like and cytokine-receptor homology domains		Fterm	Site	receptor		domains	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
9786864	3	13	part_of	receptor	330:337	arg1	The extracellular domain	receptor		The extracellular domain		Fterm	Site	receptor		domain	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
9786864	3	16	part_of	fibronectin	436:446	arg1	type III fibronectin domains	III fibronectin		type III fibronectin domains		OGER	Site	III fibronectin	P02751	domains	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
10441114	13	23	gly	glycosylated	1749:1760	arg1	three glycosylated polypeptides			three glycosylated polypeptides						polypeptides	ESMS and immunoblotting analyses reveal three glycosylated polypeptides with a molecular mass ranging from 16 to 21 kDa.
1388166	0	23	gly	oligosaccharides	22:37	arg1	tissue factor pathway inhibitor	tissue factor pathway inhibitor			oligosaccharides	PUBTATOR		tissue factor pathway inhibitor	7035		The asparagine-linked oligosaccharides on tissue factor pathway inhibitor terminate with SO4-4GalNAc beta 1, 4GlcNAc beta 1,2 Mana alpha.
1388166	0	79	gly	asparagine-linked	4:20	arg1	The asparagine-linked oligosaccharides			asparagine	The asparagine-linked oligosaccharides					asparagine	The asparagine-linked oligosaccharides on tissue factor pathway inhibitor terminate with SO4-4GalNAc beta 1, 4GlcNAc beta 1,2 Mana alpha.
11696579	4	9	gly	modification	752:763	arg3	eNOS AND O-linked N-acetylglucosamine modification	eNOS			O-linked N-acetylglucosamine modification	OGER		eNOS	P29474		Hyperglycemia-associated inhibition of eNOS was accompanied by a twofold increase in O-linked N-acetylglucosamine modification of eNOS and a reciprocal decrease in O-linked serine phosphorylation at residue 1177.
11696579	4	86	gly	eNOS	768:771	arg1	O-linked N-acetylglucosamine modification	eNOS			O-linked N-acetylglucosamine modification	OGER		eNOS	P29474		Hyperglycemia-associated inhibition of eNOS was accompanied by a twofold increase in O-linked N-acetylglucosamine modification of eNOS and a reciprocal decrease in O-linked serine phosphorylation at residue 1177.
9722584	0	4	part_of	protein	61:67	arg1	deduced amino acid sequence	protein		deduced amino acid sequence		Fterm	Site	protein		sequence	Cloning and deduced amino acid sequence of a novel cartilage protein (CILP) identifies a proform including a nucleotide pyrophosphohydrolase.
17711303	12	66	gly	N-glycosylation	1808:1822	arg1	the hKOR	the hKOR				PUBTATOR		hKOR	4986		Thus, N-glycosylation of the hKOR plays important roles in stability and trafficking along the biosynthesis pathway of the receptor protein as well as agonist-induced receptor regulation.
26828122	3	29	part_of	have	525:528	arg1	The hTPPT protein AND multiple TM domains	The hTPPT protein		multiple TM domains		PUBTATOR	Site	hTPPT protein	80736	domains	The hTPPT protein is predicted to have multiple TM domains with a number of putative N-glycosylation sites, but it is not known if the protein is actually glycosylated, and if so at which site, and their role in the functionality of the transporter.
3497398	6	55	part_of	Ib	942:943	arg1	This region	Ib		This region		Cterm	Site	Ib		region	This region of glycoprotein Ib is largely hydrophobic and contains only two N-linked and one O-linked carbohydrate chains.
11320094	2	37	part_of	multi-spanning	456:469	arg1	a multi-spanning membrane domain	multi		a multi-spanning membrane domain		OGER	Site	multi		domain	It consists of a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain.
3402609	2	10	gly	contains	253:260	arg1	The deduced 131 amino acid long protein AND eight Ser-Gly repeats	The deduced 131 amino acid long protein			eight Ser-Gly repeats	Fterm		protein			The deduced 131 amino acid long protein contains eight Ser-Gly repeats.
7607222	11	84	gly	disialylated	1569:1580	arg1	one disialylated form				one disialylated form						All the glycans, except one, carry a sialic acid in (alpha 2-3) linkage to Gal, with one disialylated form which displays a supplementary (alpha 2-6) linkage.
16036915	4	2	part_of	containing	731:740	arg1	Wild type ELOVL4 AND an endoplasmic reticulum retention sequence	Wild type ELOVL4		an endoplasmic reticulum retention sequence		PUBTATOR	Site	ELOVL4	6785	sequence	Wild type ELOVL4 containing an endoplasmic reticulum retention sequence was localized to the endoplasmic reticulum as expected.
23269669	4	19	gly	glycosylated	685:696	arg1	GC-C	GC-C		domain		PUBTATOR		GC-C	2984	domain	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
8384526	4	29	gly	desialylated	792:803	arg1	a desialylated tetrasaccharide				a desialylated tetrasaccharide						The structures of a desialylated tetrasaccharide, two monosialylated trisaccharides, and five other minor products were defined.
8384526	4	42	gly	monosialylated	826:839	arg1	two monosialylated trisaccharides				two monosialylated trisaccharides						The structures of a desialylated tetrasaccharide, two monosialylated trisaccharides, and five other minor products were defined.
7642555	9	10	gly	c-Myc	1120:1124	arg1	the major O-GlcNAc glycosylation site	c-Myc			the major O-GlcNAc glycosylation site	PUBTATOR		c-Myc	4609		These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	63	gly	glycosylation	1098:1110	arg2	threonine 58	c-Myc		threonine 58		PUBTATOR		c-Myc	4609	threonine 58	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
8636209	11	33	part_of	gamma	1459:1463	arg1	TM domain	CD3 gamma		TM domain		PUBTATOR	Site	CD3 gamma	917	domain	In conclusion, this study demonstrated that specific TCR interaction sites exist in both the EC and TM domain of CD3 gamma.
8636209	11	97	part_of	TCR	1395:1397	arg1	specific TCR interaction sites	TCR		specific TCR interaction sites		PUBTATOR	Site	TCR	6962	sites	In conclusion, this study demonstrated that specific TCR interaction sites exist in both the EC and TM domain of CD3 gamma.
15003450	3	31	gly	glycoprotein	465:476	arg1	the human alpha-GAL glycoprotein	the human alpha-GAL glycoprotein				OGER		GAL glycoprotein	Q8N6F7		Here, we present the structure of the human alpha-GAL glycoprotein determined by X-ray crystallography.
18227435	5	30	part_of	P16	839:841	arg1	the sixth position	P16		the sixth position		PUBTATOR	Site	P16	1029	position	Our findings are as follows: (1) the N-terminal amino acid of P16 and P17 is pyroglutamic acid; (2) the Ser residue at the sixth position of P16 is phosphorylated; (3) P17 is O-glycosylated at Thr10; and (4) the C-terminal amino acid of P16 and P17 is truncated.
16321355	4	53	gly	glycopeptides	623:635	arg2	the glycopeptides			the glycopeptides						glycopeptides	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	4	53	gly	glycopeptides	623:635	arg1	the peptides			the peptides						peptides	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	4	57	gly	glycopeptide	784:795	arg2	the glycopeptide			the glycopeptide						glycopeptide	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
9535843	10	39	gly	glycosylated	1451:1462	arg1	A site			A site						site	A site placed in the center of the putative pore region was glycosylated, suggesting that this region may have been luminal and was reinserted into the membrane at a late stage of channel assembly.
25759508	4	1	gly	threonine	606:614	arg1	The repeat regions			threonine	The repeat regions					threonine	The repeat regions within the IgG3 hinge were found to be in part O-glycosylated at the threonine in the triple repeat motif.
25759508	4	1	gly	threonine	606:614	arg1	the triple repeat motif			threonine	the triple repeat motif					threonine	The repeat regions within the IgG3 hinge were found to be in part O-glycosylated at the threonine in the triple repeat motif.
25759508	4	49	gly	O-glycosylated	584:597	arg2	The repeat regions										The repeat regions within the IgG3 hinge were found to be in part O-glycosylated at the threonine in the triple repeat motif.
25759508	4	49	gly	O-glycosylated	584:597	arg2	the threonine			threonine						threonine	The repeat regions within the IgG3 hinge were found to be in part O-glycosylated at the threonine in the triple repeat motif.
25759508	4	49	gly	O-glycosylated	584:597	arg2	the threonine			threonine						threonine	The repeat regions within the IgG3 hinge were found to be in part O-glycosylated at the threonine in the triple repeat motif.
11710528	2	38	gly	glycopeptides	383:395	arg2	The radiolabeled hTR glycopeptides			The radiolabeled hTR glycopeptides						glycopeptides	The radiolabeled hTR glycopeptides were prepared and fractionated by a lectin chromatography of Concanavalin A-Sepharose.
23662732	5	12	gly	N-	839:840	arg1	sites			sites						sites	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	5	16	gly	glycopeptide	1031:1042	arg2	nonrandom glycopeptide matches			nonrandom glycopeptide matches						glycopeptide	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
19592704	6	21	gly	Glycosylation	874:886	arg2	Asn			Asn(270)						Asn(270)	Glycosylation at Asn(270), which is located closest to the catalytic serine motif, is important for the enzymatic activity.
17956937	4	91	gly	fucosylated	887:897	arg1	fucosylated biantennary oligosaccharides				fucosylated biantennary oligosaccharides						The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
21733844	7	5	gly	nonglycosylated	1069:1083	arg1	the nonglycosylated protein	the nonglycosylated protein				Fterm		protein			In contrast, glycosylated hAQP10 showed increased thermostability of 3-6 °C compared with the nonglycosylated protein, suggesting a stabilizing effect of the N-linked glycan.
21733844	7	45	gly	glycosylated	988:999	arg1	glycosylated hAQP10	glycosylated hAQP10				PUBTATOR		hAQP10	89872		In contrast, glycosylated hAQP10 showed increased thermostability of 3-6 °C compared with the nonglycosylated protein, suggesting a stabilizing effect of the N-linked glycan.
17525160	7	49	gly	glycosylation	885:897	arg2	the site			the site						site	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
16037490	2	11	gly	glycopeptides	440:452	arg2	glycopeptides			glycopeptides						glycopeptides	In this study, recovery of glycopeptides was improved by including divalent cations or increasing the organic solvent in the binding solution, without losing specificity, whereas it was still less effective for those with a long peptide backbone exceeding 50 amino acid residues.
8069634	0	75	gly	glycopeptide	118:129	arg2	an isolated biantennary glycopeptide			an isolated biantennary glycopeptide						glycopeptide	Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety.
9883900	5	2	part_of	IGFBP-5	661:667	arg1	C-terminal peptides	IGFBP-5		C-terminal peptides		PUBTATOR	Site	IGFBP-5	3488	peptides	C-terminal peptides of IGFBP-5 with molecular masses of 13.3 and 13.5 kDa were purified by consecutive chromatographic steps and sequenced.
8033893	5	26	part_of	sequence	642:649	arg1	their amino acid composition	sequence		their amino acid composition						position	Although their amino acid composition was found to be the same, in the N-terminal sequence of the 9-kDa protein, the second threonine residue could not be detected and a difference of 976Da was determined by mass spectrometry.
8033893	5	41	part_of	protein	664:670	arg1	the N-terminal sequence	9-kDa protein		the N-terminal sequence		OGER	Site	9-kDa protein	P13994	sequence	Although their amino acid composition was found to be the same, in the N-terminal sequence of the 9-kDa protein, the second threonine residue could not be detected and a difference of 976Da was determined by mass spectrometry.
18490449	0	100	gly	sialylglycoprotein	24:41	arg1	Opalin	Opalin				PUBTATOR		Opalin	226115		Opalin, a transmembrane sialylglycoprotein located in the central nervous system myelin paranodal loop membrane.
18490449	0	100	gly	sialylglycoprotein	24:41	arg1	a transmembrane sialylglycoprotein	a transmembrane sialylglycoprotein				Fterm		sialylglycoprotein			Opalin, a transmembrane sialylglycoprotein located in the central nervous system myelin paranodal loop membrane.
10089882	2	2	part_of	contains	314:321	arg1	these otherwise diverse coreceptors AND an N-terminal region	these otherwise diverse coreceptors		an N-terminal region		Fterm	Site	coreceptors		region	Each of these otherwise diverse coreceptors contains an N-terminal region that is acidic and tyrosine rich.
1457969	3	23	gly	glycopeptides	505:517	arg2	two glycopeptides			two glycopeptides						glycopeptides	The alpha-subunit was further treated with trypsin which gave two glycopeptides that were subsequently separated by reverse-phase HPLC and identified by amino acid sequence analysis.
25826155	4	55	part_of	LLT1	590:593	arg1	the ectodomain	LLT1		the ectodomain		PUBTATOR	Site	LLT1	29121	ectodomain	Here, we report the crystal structure of the ectodomain of LLT1.
10889209	0	50	part_of	Asn117	46:51	arg1	ROMK1	ROMK1		Asn117		PUBTATOR	AminoAcid	ROMK1	3758	Asn117	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
7694285	11	50	part_of	CGT	1606:1608	arg1	The amino acid sequence	CGT		The amino acid sequence		PUBTATOR	Site	CGT	7368	sequence	The amino acid sequence of CGT shows significant homology to mammalian UDPglucuronyltransferases, which suggests a common evolutionary origin of these enzymes.
8687384	2	55	gly	glycans	552:558	arg1	Bowes t-PA	t-PA			glycans	PUBTATOR		t-PA	P00750		This study clarified an earlier discrepancy in the literature and confirmed that the major complex N-linked glycans on Bowes t-PA that carry sialic acid as their sole charged group are bi-antennary, core fucosylated, with terminal N-acetylgalactosamine residues.
8687384	2	25	gly	carry	579:583	arg1	Bowes t-PA AND sialic acid	Bowes t-PA			sialic acid	PUBTATOR		t-PA	P00750		This study clarified an earlier discrepancy in the literature and confirmed that the major complex N-linked glycans on Bowes t-PA that carry sialic acid as their sole charged group are bi-antennary, core fucosylated, with terminal N-acetylgalactosamine residues.
16043704	4	38	part_of	TLR3	565:568	arg1	the ectodomain	TLR3		the ectodomain		PUBTATOR	Site	TLR3	7098	ectodomain	In this study, we have expressed and crystallized the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution.
25092234	0	28	gly	glycosite	96:104	arg2	a noncanonical NXC glycosite			a noncanonical NXC glycosite						glycosite	Site-specific N-glycosylation analysis of human factor XI: Identification of a noncanonical NXC glycosite.
25092234	0	34	gly	N-glycosylation	14:28	arg1	human factor XI	human factor XI				OGER		factor XI	P03951		Site-specific N-glycosylation analysis of human factor XI: Identification of a noncanonical NXC glycosite.
9597769	4	19	gly	O-glycosylation	868:882	arg2	O-glycosylation sites			O-glycosylation sites						sites	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
28531887	6	55	gly	Glycosylation	791:803	arg1	the SK-Mel-28 protein	the SK-Mel-28 protein				Fterm		protein			Glycosylation of the SK-Mel-28 protein was studied via glucosidases and site directed mutagenesis of the MT4-MMP cDNA prior to transfection.
8615697	5	72	gly	glycopeptides	662:674	arg2	The purified tryptic glycopeptides			The purified tryptic glycopeptides						glycopeptides	The purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin.
18729387	9	1	gly	glycosylations	1596:1609	arg1	four proteins	four proteins				Fterm		proteins			The site-specific glycosylations of four proteins were elucidated as follows.
20837471	7	60	part_of	peptide	1242:1248	arg1	the RAPR(224)↓TT processing site	peptide		the RAPR(224)↓TT processing site						site	We demonstrated that GalNAc-T2 glycosylation of Thr(226) in a peptide with the RAPR(224)↓TT processing site blocks in vitro furin cleavage.
8069634	5	12	part_of	N2	864:865	arg1	the N2 monoglycosylated fragment	N2		the N2 monoglycosylated fragment		Cterm	Site	N2		fragment	RESULTS: We have determined the crystal structures of Lathyrus ochrus isolectin II complexed with the N2 monoglycosylated fragment of human lactotransferrin (18 kDa) and an isolated glycopeptide (2.1 kDa) fragment of human lactotransferrin (at 3.3 A and 2.8 A resolution, respectively).
8069634	5	13	part_of	lactotransferrin	902:917	arg1	an isolated glycopeptide (2.1 kDa) fragment	lactotransferrin		fragment		PUBTATOR	Site	lactotransferrin	4057	fragment	RESULTS: We have determined the crystal structures of Lathyrus ochrus isolectin II complexed with the N2 monoglycosylated fragment of human lactotransferrin (18 kDa) and an isolated glycopeptide (2.1 kDa) fragment of human lactotransferrin (at 3.3 A and 2.8 A resolution, respectively).
8069634	5	36	part_of	lactotransferrin	985:1000	arg1	an isolated glycopeptide (2.1 kDa) fragment	lactotransferrin		fragment		PUBTATOR	Site	lactotransferrin	4057	fragment	RESULTS: We have determined the crystal structures of Lathyrus ochrus isolectin II complexed with the N2 monoglycosylated fragment of human lactotransferrin (18 kDa) and an isolated glycopeptide (2.1 kDa) fragment of human lactotransferrin (at 3.3 A and 2.8 A resolution, respectively).
3665914	3	57	gly	residue	613:619	arg1	6-deoxyaltrose			residue in	6-deoxyaltrose					residue in	First, the structure of the terminal dHex residue in the above pentasaccharide has been assigned as 6-deoxyaltrose (= dAlt in pyranoid form) by a combination of structural methods (GLC, TLC, mass spectrometry, and 400-MHz 1H-NMR spectroscopy).
3665914	3	79	gly	residue	613:619	arg1	the above pentasaccharide			residue in	the above pentasaccharide					residue in	First, the structure of the terminal dHex residue in the above pentasaccharide has been assigned as 6-deoxyaltrose (= dAlt in pyranoid form) by a combination of structural methods (GLC, TLC, mass spectrometry, and 400-MHz 1H-NMR spectroscopy).
21712440	0	34	part_of	precursor	92:100	arg1	amyloid precursor protein/amyloid beta-peptides	amyloid precursor protein		amyloid precursor protein/amyloid beta-peptides		OGER	Site	amyloid precursor protein	P05067	beta-peptides	Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid beta-peptides in human cerebrospinal fluid.
21712440	0	85	part_of	amyloid	84:90	arg1	amyloid precursor protein/amyloid beta-peptides	amyloid precursor protein		amyloid precursor protein/amyloid beta-peptides		OGER	Site	amyloid precursor protein	P05067	beta-peptides	Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid beta-peptides in human cerebrospinal fluid.
21712440	0	87	part_of	protein/amyloid	102:116	arg1	amyloid precursor protein/amyloid beta-peptides	amyloid precursor protein		amyloid precursor protein/amyloid beta-peptides		OGER	Site	amyloid precursor protein	P05067	beta-peptides	Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid beta-peptides in human cerebrospinal fluid.
2056274	2	113	part_of	containing	461:470	arg1	novel CD44 isoforms AND additional protein sequence	novel CD44 isoforms		additional protein sequence		PUBTATOR	Site	CD44 isoforms	960	sequence	The possibility that these higher molecular weight species may represent novel CD44 isoforms containing additional protein sequence was investigated.
3542989	5	0	part_of	cholinesterase	490:503	arg1	The sequence	cholinesterase		The sequence		PUBTATOR	Site	cholinesterase	534616	sequence	The sequence of human serum cholinesterase is 53.8% identical with the sequence of acetylcholinesterase from Torpedo californica and 28% identical with the carboxyl-terminal portion of bovine thyroglobulin.
3542989	5	2	part_of	acetylcholinesterase	545:564	arg1	the sequence	acetylcholinesterase		the sequence		OGER	Site	acetylcholinesterase	P22303	sequence	The sequence of human serum cholinesterase is 53.8% identical with the sequence of acetylcholinesterase from Torpedo californica and 28% identical with the carboxyl-terminal portion of bovine thyroglobulin.
22235133	6	36	gly	C-mannosylated	896:909	arg2	the first tryptophan			the first tryptophan						tryptophan	Here, we present the crystal structure of IL-21 bound to IL-21R and reveal that the WSXWS motif of IL-21R is C-mannosylated at the first tryptophan.
22235133	6	36	gly	C-mannosylated	896:909	arg1	the WSXWS motif			the WSXWS motif						motif	Here, we present the crystal structure of IL-21 bound to IL-21R and reveal that the WSXWS motif of IL-21R is C-mannosylated at the first tryptophan.
16342937	11	84	part_of	furin	1819:1823	arg1	a conserved dibasic residue	furin		a conserved dibasic residue		OGER	Site	furin	P23377	residue	The mature C-termini of ZP1 and ZP3 end two amino acids upstream of a conserved dibasic residue that is part of, but distinct from, the consensus furin cleavage sequence, while the C-terminus of ZP2 was not determined.
16342937	11	84	part_of	furin	1819:1823	arg1	the consensus furin cleavage sequence	furin		the consensus furin cleavage sequence		OGER	Site	furin	P23377	sequence	The mature C-termini of ZP1 and ZP3 end two amino acids upstream of a conserved dibasic residue that is part of, but distinct from, the consensus furin cleavage sequence, while the C-terminus of ZP2 was not determined.
23187000	3	21	part_of	N30	581:583	arg1	the only N-linked glycoprotein	glycoprotein		N30		Fterm	SpecificSite	glycoprotein		N30 and N78	Among TIMPs, TIMP-1, a 184-residue protein, is the only N-linked glycoprotein with glycosylation sites at N30 and N78.
23187000	3	21	part_of	N30	581:583	arg1	TIMP-1	TIMP-1		N30		PUBTATOR	SpecificSite	TIMP-1	7076	N30 and N78	Among TIMPs, TIMP-1, a 184-residue protein, is the only N-linked glycoprotein with glycosylation sites at N30 and N78.
23187000	3	66	part_of	N78	589:591	arg1	the only N-linked glycoprotein	glycoprotein		N78		Fterm	SpecificSite	glycoprotein		N30 and N78	Among TIMPs, TIMP-1, a 184-residue protein, is the only N-linked glycoprotein with glycosylation sites at N30 and N78.
23187000	3	66	part_of	N78	589:591	arg1	TIMP-1	TIMP-1		N78		PUBTATOR	SpecificSite	TIMP-1	7076	N30 and N78	Among TIMPs, TIMP-1, a 184-residue protein, is the only N-linked glycoprotein with glycosylation sites at N30 and N78.
23187000	3	71	part_of	glycoprotein	540:551	arg1	glycosylation sites	glycoprotein		glycosylation sites		Fterm	Site	glycoprotein		sites	Among TIMPs, TIMP-1, a 184-residue protein, is the only N-linked glycoprotein with glycosylation sites at N30 and N78.
2001369	1	24	gly	glycoprotein	227:238	arg1	the HIV envelope glycoprotein	the HIV envelope glycoprotein				Fterm		glycoprotein			Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	1	62	gly	glycoprotein	269:280	arg1	the cell-surface receptor glycoprotein CD4	the cell-surface receptor glycoprotein CD4				Fterm		glycoprotein			Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
18533687	10	61	part_of	RXFP1	1661:1665	arg1	Asn-303	RXFP1		Asn-303		PUBTATOR	SpecificSite	RXFP1	59350	Asn-303	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
3342889	1	40	part_of	L	165:165	arg1	The complete amino acid sequences	cathepsin L 		The complete amino acid sequences		PUBTATOR	Site	cathepsin L 	1514	sequences	The complete amino acid sequences of human kidney cathepsin H (EC 3.4.22.16) and human kidney cathepsin L (EC 3.4.22.15) were determined.
3342889	1	64	part_of	cathepsin	111:119	arg1	The complete amino acid sequences	cathepsin H		The complete amino acid sequences		Fterm	Site	cathepsin H	1512	sequences	The complete amino acid sequences of human kidney cathepsin H (EC 3.4.22.16) and human kidney cathepsin L (EC 3.4.22.15) were determined.
19038966	5	72	part_of	terminus	1060:1067	arg1	tripeptides	terminus		tripeptides						tripeptides	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
21757702	4	20	gly	occupancy	640:648	arg2	the site			the site						site	For instance, although most sites are modified at high stoichiometries, the site at EGF 27 is only partially glucosylated, and the occupancy of the site at EGF 4 varies with cell type.
26563299	6	33	gly	α1-6-core-fucosylated	995:1015	arg1	mostly α1-6-core-fucosylated and β-GlcNAc-terminating complex-type structures				mostly α1-6-core-fucosylated and β-GlcNAc-terminating complex-type structures						IL-15 Asn79 and sIL-15Rα Asn107 carried the same repertoire of biosynthetically-related N-glycans covering mostly α1-6-core-fucosylated and β-GlcNAc-terminating complex-type structures.
26563299	6	21	gly	carried	913:919	arg1	IL-15 Asn79 AND biosynthetically-related N-glycans			IL-15 Asn79	biosynthetically-related N-glycans					Asn79	IL-15 Asn79 and sIL-15Rα Asn107 carried the same repertoire of biosynthetically-related N-glycans covering mostly α1-6-core-fucosylated and β-GlcNAc-terminating complex-type structures.
26563299	6	21	gly	carried	913:919	arg1	sIL-15Rα Asn107 AND biosynthetically-related N-glycans			sIL-15Rα Asn107	biosynthetically-related N-glycans					Asn107	IL-15 Asn79 and sIL-15Rα Asn107 carried the same repertoire of biosynthetically-related N-glycans covering mostly α1-6-core-fucosylated and β-GlcNAc-terminating complex-type structures.
11447134	8	18	gly	glycopeptides	1014:1026	arg2	glycopeptides			glycopeptides						glycopeptides	The analysis of the N-glycosylation was performed by tryptic digestion of the protein, isolation of glycopeptides by lectin chromatography and mass measurement before and after enzymatic deglycosylation.
8172892	0	94	gly	linked	76:81	arg1	threonine residues AND oligosaccharides			threonine residues	oligosaccharides					threonine residues	Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to threonine residues at 159 and 169.
8172892	0	0	gly	has	38:40	arg1	Activation peptide AND oligosaccharides			Activation peptide	oligosaccharides					peptide	Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to threonine residues at 159 and 169.
23234360	6	68	part_of	sites	1228:1232	arg1	glycoproteins	glycoproteins		sites		Fterm	Site	glycoproteins		sites	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
15869464	4	45	part_of	OPN	776:778	arg1	the sequence	OPN		the sequence		PUBTATOR	Site	OPN	6696	sequence	A total of 36 phosphoresidues have been localized in the sequence of OPN.
17534424	9	80	gly	glycoprotein	2188:2199	arg1	human ClC-6	human ClC-6				OGER		ClC	Q05315		CONCLUSIONS: We conclude that human ClC-6 is an endosomal glycoprotein that partitions in detergent resistant lipid domains.
17534424	9	80	gly	glycoprotein	2188:2199	arg1	an endosomal glycoprotein	an endosomal glycoprotein				Fterm		glycoprotein			CONCLUSIONS: We conclude that human ClC-6 is an endosomal glycoprotein that partitions in detergent resistant lipid domains.
14699159	4	74	gly	glycosylation	968:980	arg1	newly synthesized p90ATF6	newly synthesized p90ATF6				Cterm		p90ATF6	22926		Here we show that ER Ca(2+) depletion stress, a triggering mechanism for the UPR, induces the formation of ATF6(f), which represents de novo partial glycosylation of newly synthesized p90ATF6.
17960739	5	3	gly	deglycosylated	641:654	arg1	deglycosylated peptides			deglycosylated peptides						peptides	Thus, following protease digestion, deglycosylated peptides were selectively identified by high mass accuracy FTICR-MS, using this conversion as a signature.
19343721	0	7	gly	occupancy	44:52	arg2	site occupancy			site occupancy						site	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	35	gly	microheterogeneity	16:33	arg1	an Asn-X-Cys sequon			an Asn-X-Cys sequon						sequon	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	63	gly	glycosylated	147:158	arg2	Asn-X-Cys			Asn-X-Cys						Asn-X-Cys	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	63	gly	glycosylated	147:158	arg2	Asn-X-Ser/Thr			Asn-X-Ser/Thr						Asn	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	77	gly	N-glycosylation	0:14	arg1	an Asn-X-Cys sequon			an Asn-X-Cys sequon						sequon	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	7	gly	occupancy	44:52	arg1	an Asn-X-Cys sequon			sequon						sequon	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19413349	2	80	part_of	contains	268:275	arg1	Rat melanopsin AND two potential sites	Rat melanopsin		two potential sites		PUBTATOR	Site	Rat melanopsin	192223	sites	Rat melanopsin contains two potential sites (Asn31 and Asn35) for N-linked glycosylation in the N-terminal extracellular part.
19413349	2	80	part_of	contains	268:275	arg1	Rat melanopsin AND Asn31	Rat melanopsin		Asn31 and Asn35		PUBTATOR	AminoAcid	Rat melanopsin	192223	Asn31 and Asn35	Rat melanopsin contains two potential sites (Asn31 and Asn35) for N-linked glycosylation in the N-terminal extracellular part.
29741879	5	33	gly	glycoproteins	1211:1223	arg1	617 glycoproteins	617 glycoproteins				Fterm		glycoproteins			Collectively, combined tandem mass spectrometry (MS/MS) analyses of global proteomic and phosphoproteomic data sets resulted in the identification of 6 724 N-linked glycopeptides from 617 glycoproteins derived from two breast cancer xenograft tissues.
29741879	5	78	gly	glycopeptides	1188:1200	arg1	617 glycoproteins	glycoproteins		glycopeptides		Fterm		glycoproteins		glycopeptides	Collectively, combined tandem mass spectrometry (MS/MS) analyses of global proteomic and phosphoproteomic data sets resulted in the identification of 6 724 N-linked glycopeptides from 617 glycoproteins derived from two breast cancer xenograft tissues.
2387072	0	43	gly	glycoproteins	40:52	arg1	membrane glycoproteins	membrane glycoproteins				Fterm		glycoproteins			Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	0	75	gly	glycoprotein	73:84	arg1	a secreted glycoprotein	a secreted glycoprotein				Fterm		glycoprotein			Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
7430095	0	5	gly	A	79:79	arg1	the asparagine-linked sugar chains	Glycophorin A			the asparagine-linked sugar chains	PUBTATOR		Glycophorin A	2993		Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	0	29	gly	asparagine-linked	18:34	arg1	the asparagine-linked sugar chains			asparagine	the asparagine-linked sugar chains					asparagine	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	0	31	gly	asparagine-linked	127:143	arg1	one asparagine-linked sugar chain			asparagine	one asparagine-linked sugar chain					asparagine	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
16335952	4	38	gly	glycoproteins	793:805	arg1	N-linked glycoproteins	N-linked glycoproteins				Fterm		glycoproteins			N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	4	68	gly	glycopeptides	924:936	arg2	the bound N-linked glycopeptides			the bound N-linked glycopeptides						glycopeptides	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
6725284	4	35	gly	protein	565:571	arg1	the oligosaccharide units	protein			the oligosaccharide units	Fterm		protein			The aim of the present investigation was to elucidate the primary structure of the oligosaccharide units of this protein.
22809326	8	89	gly	glycosylated	1032:1043	arg1	a heavily glycosylated lysosomal membrane protein	a heavily glycosylated lysosomal membrane protein				OGER		glycosylated lysosomal membrane protein	Q8WWB7		It is the first high-resolution structure of a heavily glycosylated lysosomal membrane protein.
27966990	5	42	part_of	sites	681:685	arg1	VEGFR-2	VEGFR-2		sites		PUBTATOR	Site	VEGFR-2	P35968	sites	The objectives of the present study were to characterize N-glycosylation sites in VEGFR-2 via enzymatic release of the glycans and concomitant incorporation of 18O into formerly N-glycosylated sites followed by tandem mass spectrometry (MS/MS) analysis to determine N-glycosylation site occupancy and the site-specific N-glycan heterogeneity of VEGFR-2 glycopeptides.
27966990	5	64	part_of	VEGFR-2	953:959	arg1	VEGFR-2 glycopeptides	VEGFR-2		VEGFR-2 glycopeptides		PUBTATOR	Site	VEGFR-2	P35968	glycopeptides	The objectives of the present study were to characterize N-glycosylation sites in VEGFR-2 via enzymatic release of the glycans and concomitant incorporation of 18O into formerly N-glycosylated sites followed by tandem mass spectrometry (MS/MS) analysis to determine N-glycosylation site occupancy and the site-specific N-glycan heterogeneity of VEGFR-2 glycopeptides.
15606899	3	29	part_of	BACE1	595:599	arg1	the cytosolic tail	BACE1		the cytosolic tail		PUBTATOR	Site	BACE1	23621	tail	Co-localization and co-immunoprecipitation experiments confirmed that BACE1 and BRI3 co-localize and interact with each other via the cytosolic tail of BACE1.
18795891	2	1	part_of	tetraspanin-enriched	470:489	arg1	tetraspanin-enriched microdomains	tetraspanin		tetraspanin-enriched microdomains		Fterm	Site	tetraspanin		microdomains	Normal platelet activation is dependent on tetraspanins, a superfamily of glycoproteins that function as 'organisers' of cell membranes by recruiting other receptors and signalling proteins into tetraspanin-enriched microdomains.
11805077	5	47	gly	position	692:699	arg1	the tetraantennary oligosaccharide			position	the tetraantennary oligosaccharide					position	The linkage position and branch-location of the sulfate group in the tetraantennary oligosaccharide were analyzed by (1)H-nuclear magnetic resonance.
20068230	1	38	part_of	threonine	238:246	arg1	nuclear and cytoplasmic proteins	proteins		threonine		Fterm	AminoAcid	proteins		serine and threonine residues	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	1	45	part_of	serine	227:232	arg1	nuclear and cytoplasmic proteins	proteins		serine		Fterm	AminoAcid	proteins		serine and threonine residues	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
3484330	5	16	part_of	contains	825:832	arg1	The core protein AND three Ser-Gly dipeptide sequences	The core protein		three Ser-Gly dipeptide sequences		Fterm	Site	protein		sequences	The core protein contains three Ser-Gly dipeptide sequences, of which one is substituted with glycosaminoglycan.
20378933	2	61	part_of	protein	216:222	arg1	six potential N-linked glycosylation sites	protein		six potential N-linked glycosylation sites		Fterm	Site	protein		sites	It is a heavily glycosylated protein with six potential N-linked glycosylation sites.
30630874	2	2	part_of	TM	276:277	arg1	a transmembrane (TM) APP fragment	TM) APP		a transmembrane (TM) APP fragment		OGER	Site	TM) APP	P05067	fragment	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
30630874	2	33	part_of	APP	280:282	arg1	a transmembrane (TM) APP fragment	TM) APP		a transmembrane (TM) APP fragment		OGER	Site	TM) APP	P05067	fragment	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
1445902	0	41	gly	glycosylation	21:33	arg1	baculovirus-expressed mouse interleukin-3	baculovirus-expressed mouse interleukin-3				PUBTATOR		interleukin-3	16187		Determination of the glycosylation patterns, disulfide linkages, and protein heterogeneities of baculovirus-expressed mouse interleukin-3 by mass spectrometry.
12218058	7	44	gly	glycosylation	1285:1297	arg2	the CUB-specific glycosylation sites			the CUB-specific glycosylation sites						sites	BMP-1 molecules lacking any one of the CUB-specific glycosylation sites were sensitive to thermal denaturation.
1883960	4	63	part_of	terminus	1094:1101	arg1	the 28- to 30-kD N- and O-glycosylated IL-6	IL-6		terminus		PUBTATOR	Site	IL-6	3569	terminus	Amino acid sequencing revealed that the major amino terminus in the fibroblast-derived 23- to 25-kD O-glycosylated IL-6 was at Ala28 whereas the major amino terminus in the 28- to 30-kD N- and O-glycosylated IL-6 was at Val30, suggesting that targeting of newly synthesized IL-6 polypeptides into the two different processing pathways in fibroblasts may be keyed to differences in the signal peptide cleavage site.
1883960	4	72	part_of	IL-6	1211:1214	arg1	newly synthesized IL-6 polypeptides	IL-6		newly synthesized IL-6 polypeptides		PUBTATOR	Site	IL-6	3569	polypeptides	Amino acid sequencing revealed that the major amino terminus in the fibroblast-derived 23- to 25-kD O-glycosylated IL-6 was at Ala28 whereas the major amino terminus in the 28- to 30-kD N- and O-glycosylated IL-6 was at Val30, suggesting that targeting of newly synthesized IL-6 polypeptides into the two different processing pathways in fibroblasts may be keyed to differences in the signal peptide cleavage site.
3980466	11	71	gly	glycoproteins	2008:2020	arg1	structurally related glycoproteins	structurally related glycoproteins				Fterm		glycoproteins			First, the overall distributions of oligosaccharides at corresponding sites on structurally related glycoproteins are similar.
3980466	11	91	gly	sites	1978:1982	arg1	oligosaccharides			sites	oligosaccharides					sites	First, the overall distributions of oligosaccharides at corresponding sites on structurally related glycoproteins are similar.
8329384	5	1	gly	IX	1016:1017	arg1	residues 57-65			residues 57-65						residues 57-65	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	5	71	gly	glycopeptide	985:996	arg2	the glycopeptide			the glycopeptide						glycopeptide	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
20133774	4	37	part_of	PTPRG	907:911	arg1	the carbonic anhydrase-like domain	PTPRG		the carbonic anhydrase-like domain		PUBTATOR	Site	PTPRG	19270	domain	Furthermore, we present crystal structures of the four N-terminal immunoglobulin repeats of mouse CNTN4 both alone and in complex with the carbonic anhydrase-like domain of mouse PTPRG.
8329384	2	25	part_of	EGF	502:504	arg1	the first EGF domain	EGF		the first EGF domain		OGER	Site	EGF	P01133	domain	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	40	part_of	IX	529:530	arg1	the first EGF domain	factor IX		the first EGF domain		OGER	Site	factor IX	P00740	domain	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	18	part_of	containing	446:455	arg1	tryptic and thermolytic peptides AND Ser-61	tryptic and thermolytic peptides		Ser-61						Ser-61	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	18	part_of	containing	446:455	arg1	tryptic and thermolytic peptides AND the corresponding site	tryptic and thermolytic peptides		the corresponding site						site	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
7613477	3	65	part_of	LCAT	810:813	arg1	the four expected N-linked glycopeptides	LCAT		the four expected N-linked glycopeptides		PUBTATOR	Site	LCAT	3931	glycopeptides	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
21980294	4	26	part_of	site	490:493	arg1	gD	gD		site		Cterm	Site	gD	2532	site	The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor.
21980294	4	35	part_of	receptor	543:550	arg1	the binding site	HVEM receptor		the binding site		PUBTATOR	Site	HVEM receptor	8764	site	The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor.
21980294	4	51	part_of	nectin-1	473:480	arg1	the nectin-1 binding site	nectin-1		the nectin-1 binding site		PUBTATOR	Site	nectin-1	Q15223	site	The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor.
6966283	0	37	gly	alpha	47:51	arg1	the oligosaccharide chains	alpha 1-protease inhibitor			the oligosaccharide chains	PUBTATOR		alpha 1-protease inhibitor	5265		Studies on the oligosaccharide chains of human alpha 1-protease inhibitor.
17222411	4	43	part_of	l-3	637:639	arg1	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	l-3		NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr		OGER	AminoAcid	l-3	Q96MH2	Thr	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
26412745	3	28	part_of	AKT	516:518	arg1	Ser473	AKT		Ser473		PUBTATOR	AminoAcid	AKT	11651	Thr308 and Ser473	By using co-immunoprecipitation and mutagenesis techniques, we identified O-GlcNAc modification at both Thr308 and Ser473 of AKT.
19276170	0	0	part_of	protein	77:83	arg1	the signature domain	cartilage oligomeric matrix protein		the signature domain		OGER	Site	cartilage oligomeric matrix protein	P49747	domain	The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding.
9343410	0	40	part_of	Sp1-derived	22:32	arg1	an Sp1-derived peptide	Sp1		an Sp1-derived peptide		OGER	Site	Sp1	Q8N907	peptide	O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions.
22848655	0	33	part_of	kinase	86:91	arg1	the Sema-PSI extracellular domain	kinase		the Sema-PSI extracellular domain		Fterm	Site	kinase		domain	Crystal structure of the Sema-PSI extracellular domain of human RON receptor tyrosine kinase.
22848655	0	46	part_of	Sema-PSI	25:32	arg1	the Sema-PSI extracellular domain	structure of the Sema		the Sema-PSI extracellular domain		Cterm	Site	structure of the Sema	57556	domain	Crystal structure of the Sema-PSI extracellular domain of human RON receptor tyrosine kinase.
3497398	9	20	gly	macroglycopeptide	1349:1365	arg2	the previously described "macroglycopeptide"			the previously described "macroglycopeptide"						macroglycopeptide	The hydrophilic, highly glycosylated (at serine and threonine residues) region corresponding to the previously described "macroglycopeptide" and representing the carboxyl-terminal half of the alpha chain is likely to begin at residue 292.
3497398	9	78	gly	serine	1268:1273	arg1	residues			residues						serine and threonine residues	The hydrophilic, highly glycosylated (at serine and threonine residues) region corresponding to the previously described "macroglycopeptide" and representing the carboxyl-terminal half of the alpha chain is likely to begin at residue 292.
3497398	9	26	gly	glycosylated	1251:1262	arg1	serine			serine and threonine residues						serine and threonine residues	The hydrophilic, highly glycosylated (at serine and threonine residues) region corresponding to the previously described "macroglycopeptide" and representing the carboxyl-terminal half of the alpha chain is likely to begin at residue 292.
18203274	8	11	gly	monosialylated	989:1002	arg1	monosialylated N-glycans				monosialylated N-glycans						On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
22159084	7	19	gly	Deglycosylation	821:835	arg1	SLC26A3	SLC26A3				PUBTATOR		SLC26A3	1811		Deglycosylation of SLC26A3 causes depression of transport activity compared with wild-type, although robust intracellular pH changes were still observed, suggesting that N-glycosylation is not absolutely necessary for transport activity.
12901863	5	34	gly	N-glycosylation	891:905	arg2	Asn15			Asn15						Asn15	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	5	34	gly	N-glycosylation	891:905	arg2	the only N-glycosylation site			the only N-glycosylation site						site	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
23234360	0	23	part_of	glycoproteins	102:114	arg1	O-glycosylation sites	glycoproteins		O-glycosylation sites		Fterm	Site	glycoproteins		sites	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
9136890	10	20	gly	sialylated	1174:1183	arg1	sialylated hybrid oligosaccharides				sialylated hybrid oligosaccharides						FACE analysis reveals predominantly a family of sialylated hybrid oligosaccharides.
2721499	3	30	gly	glycosylation	579:591	arg2	six N-linked glycosylation sites			six N-linked glycosylation sites						sites	The precursor is preceded by a signal sequence for vectorial export and contains six N-linked glycosylation sites distributed equally between the two chains of the structure.
21669976	5	3	gly	N-	663:664	arg1	sites			sites						sites	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	5	33	gly	unglycosylated	802:815	arg1	mostly unglycosylated protein	mostly unglycosylated protein				Fterm		protein			For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	5	55	gly	mono-N-glycosylated	849:867	arg1	mono-N-glycosylated protein	mono-N-glycosylated protein				Fterm		protein			For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
12731890	5	55	part_of	site	1029:1032	arg1	the secreted form	form of the receptor		site		Fterm	Site	form of the receptor		site	We show that an additional canonical site in the secreted form of the receptor is fully glycosylated.
15099525	1	29	part_of	ICAM-1	159:164	arg1	the three C-terminal domains 3-5 (D3-D5)	ICAM-1		the three C-terminal domains 3-5 (D3-D5)		PUBTATOR	Site	ICAM-1	3383	domains	We have determined the 3.0 A crystal structure of the three C-terminal domains 3-5 (D3-D5) of ICAM-1.
2243102	3	56	gly	polylactosaminoglycans	306:327	arg1	lamp-2	lamp-2			polylactosaminoglycans	PUBTATOR		lamp-2	3920		We have localized the polylactosaminoglycans to specific sites on lamp-1 and lamp-2 purified from human chronic myelogenous leukemia cells.
2243102	3	56	gly	polylactosaminoglycans	306:327	arg1	lamp-1	lamp-1			polylactosaminoglycans	PUBTATOR		lamp-1	3916		We have localized the polylactosaminoglycans to specific sites on lamp-1 and lamp-2 purified from human chronic myelogenous leukemia cells.
10207177	11	67	gly	glycoproteins	2296:2308	arg1	the glycoproteins	the glycoproteins				Fterm		glycoproteins			In addition, glycans located close to the cell membrane are likely to affect crucially the orientation of the glycoproteins to which they are attached.
22448645	4	11	gly	N-glycosylated	826:839	arg1	both asparagines			both asparagines						asparagines	To further investigate this, we mutated the two predicted N-glycosylation sites (N5Q and N66Q) and compared the molecular mass of the immunoreactive bands with those of the wild-type receptor, indicating that both asparagines were N-glycosylated.
22448645	4	22	gly	N-glycosylation	653:667	arg2	the two predicted N-glycosylation sites			the two predicted N-glycosylation sites						sites	To further investigate this, we mutated the two predicted N-glycosylation sites (N5Q and N66Q) and compared the molecular mass of the immunoreactive bands with those of the wild-type receptor, indicating that both asparagines were N-glycosylated.
2209609	1	16	gly	glycoprotein	251:262	arg1	sCD4	sCD4				PUBTATOR		sCD4	79966		Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	1	16	gly	glycoprotein	251:262	arg1	human CD4 glycoprotein	human CD4 glycoprotein				PUBTATOR		CD4 glycoprotein	P01730		Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
29741879	10	15	gly	glycopeptides	2128:2140	arg2	glycopeptides			glycopeptides						glycopeptides	The reanalysis described herein can be readily applied to identify glycopeptides from already existing data sets, providing insight into many important facets of protein glycosylation in different biological, physiological, and pathological processes.
10894551	0	56	part_of	receptor	80:87	arg1	the dimerized hormone-binding domain	receptor		the dimerized hormone-binding domain		Fterm	Site	receptor		domain	Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor.
10200178	10	79	gly	epitopes	1845:1852	arg1	murine PrPSc	PrPSc			epitopes	PUBTATOR		PrPSc	19122		The abundance of the Lewisx and sialyl Lewisx epitopes on murine PrPSc may indicate a role for these structures in the normal function of PrPC or the pathophysiology of PrPSc.
2049076	0	66	gly	O-glycosylated	36:49	arg1	Natural human interferon-alpha 2	Natural human interferon-alpha 2				PUBTATOR		interferon-alpha 2	3440		Natural human interferon-alpha 2 is O-glycosylated.
29666272	8	53	gly	Asn-linked	1603:1612	arg1	the Asn-linked glycan biosynthetic pathway			Asn	the Asn-linked glycan biosynthetic pathway					Asn	Recognition arm interactions are similar to the enzyme-substrate interactions for Golgi α-mannosidase II, a glycoside hydrolase that acts just before MGAT2 in the Asn-linked glycan biosynthetic pathway.
9336835	12	75	part_of	Clusterin	2181:2189	arg1	Clusterin peptides	Clusterin		Clusterin peptides		PUBTATOR	Site	Clusterin	1191	peptides	Clusterin peptides accounting for 99% of the primary structure were identified from analysis of the isolated alpha and beta subunits, including all Ser- and Thr-containing peptides.
16342937	3	7	gly	glycoproteins	255:267	arg1	ZP2	ZP2				PUBTATOR		ZP2	22787		Mouse zonae are composed of three glycoproteins (ZP1, ZP2, and ZP3), while rat zonae contain four (ZP1, ZP2, ZP3, and ZP4/ZPB).
16342937	3	7	gly	glycoproteins	255:267	arg1	ZP3	ZP3				PUBTATOR		ZP3	22788		Mouse zonae are composed of three glycoproteins (ZP1, ZP2, and ZP3), while rat zonae contain four (ZP1, ZP2, ZP3, and ZP4/ZPB).
16342937	3	7	gly	glycoproteins	255:267	arg1	ZP1	ZP1				PUBTATOR		ZP1	22786		Mouse zonae are composed of three glycoproteins (ZP1, ZP2, and ZP3), while rat zonae contain four (ZP1, ZP2, ZP3, and ZP4/ZPB).
16342937	3	7	gly	glycoproteins	255:267	arg1	three glycoproteins	three glycoproteins				Fterm		glycoproteins			Mouse zonae are composed of three glycoproteins (ZP1, ZP2, and ZP3), while rat zonae contain four (ZP1, ZP2, ZP3, and ZP4/ZPB).
8172892	9	19	part_of	IX	1547:1548	arg1	the activation peptide	factor IX		the activation peptide		OGER	Site	factor IX	P00740	peptide	From these results, it was concluded that a part of the activation peptide of human factor IX in circulating blood has tri- and tetrasaccharides O-glycosidically linked to the threonine residues at 159 and 169.
3514617	11	82	gly	glycopeptide	1739:1750	arg2	The tryptic glycopeptide pattern			The tryptic glycopeptide pattern						glycopeptide	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
20540760	5	78	part_of	PRCP	739:742	arg1	the S1 proline binding site	PRCP		the S1 proline binding site		PUBTATOR	Site	PRCP	5547	site	Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP.
12604466	2	38	part_of	sites	340:344	arg1	NBCe1	NBCe1		sites		OGER	Site	NBCe1	Q9JI66	sites	In the present study, we investigate glycosylation sites in NBCe1.
7107587	9	42	gly	glycopeptides	1007:1019	arg2	fibrinogen glycopeptides			fibrinogen glycopeptides						glycopeptides	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7574684	1	20	gly	glycoprotein	241:252	arg1	An extracellular domain	glycoprotein		domain		Fterm		glycoprotein		domain	An extracellular domain of a human neurotrophin receptor trkB was expressed in Chinese hamster ovary cells and isolated as a glycoprotein possessing binding activity for brain-derived neurotrophic factor.
7574684	1	20	gly	glycoprotein	241:252	arg1	a human neurotrophin receptor trkB	trkB		domain		PUBTATOR		trkB	4915	domain	An extracellular domain of a human neurotrophin receptor trkB was expressed in Chinese hamster ovary cells and isolated as a glycoprotein possessing binding activity for brain-derived neurotrophic factor.
1581307	4	42	part_of	protein	720:726	arg1	691 residues	protein		691 residues		Fterm	Site	protein		residues	The final model, comprising 5321 protein atoms (691 residues), 2 Cu2+ ions, 2 (bi)carbonate ions, and 308 solvent molecules has good stereochemistry (rms deviation of bond lengths from standard values of 0.018 A) and gives a crystallographic R value of 0.196 for 43,525 reflections in the range 7.5-2.1-A resolution.
9722584	6	36	part_of	has	905:907	arg1	CILP AND six putative N-glycosylation sites	CILP		six putative N-glycosylation sites		PUBTATOR	Site	CILP	8483	sites	CILP has 30 cysteines and six putative N-glycosylation sites.
9722584	6	36	part_of	has	905:907	arg1	CILP AND 30 cysteines	CILP		30 cysteines		PUBTATOR	AminoAcid	CILP	8483	cysteines	CILP has 30 cysteines and six putative N-glycosylation sites.
8243461	4	82	gly	linked	763:768	arg2	Thr26 AND an O-linked oligosaccharide chain			Thr26	an O-linked oligosaccharide chain					Thr26	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	4	5	gly	had	725:727	arg1	bovine factor X AND an O-linked oligosaccharide chain	bovine factor X			an O-linked oligosaccharide chain	OGER		factor X	P00742		By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	4	84	gly	had	799:801	arg1	human factor X AND four carbohydrate-attachment sites	human factor X			four carbohydrate-attachment sites	OGER		factor X	P00742		By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
12063277	4	27	gly	glycosylation	590:602	arg1	HERG channels	HERG channels				PUBTATOR		HERG channels	3757		In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
11168369	3	66	part_of	variant	562:568	arg1	The CNBr peptides	variant		The CNBr peptides		Fterm	Site	variant		peptides	The CNBr peptides of the variant were purified by reverse-phase high performance liquid chromatography and submitted to sequence analysis.
11788899	5	13	part_of	WNT8B	658:662	arg1	C-terminal region	WNT8B		C-terminal region		PUBTATOR	Site	WNT8B	7479	region	C-terminal region of WNT8B, WNT8A, WNT2, and WNT2B were longer than that of other human WNTs.
11788899	5	14	part_of	WNT8A	665:669	arg1	C-terminal region	WNT8A		C-terminal region		PUBTATOR	Site	WNT8A	7478	region	C-terminal region of WNT8B, WNT8A, WNT2, and WNT2B were longer than that of other human WNTs.
11788899	5	26	part_of	WNT2	672:675	arg1	C-terminal region	WNT2		C-terminal region		PUBTATOR	Site	WNT2	7472	region	C-terminal region of WNT8B, WNT8A, WNT2, and WNT2B were longer than that of other human WNTs.
11788899	5	68	part_of	WNT2B	682:686	arg1	C-terminal region	WNT2B		C-terminal region		PUBTATOR	Site	WNT2B	7482	region	C-terminal region of WNT8B, WNT8A, WNT2, and WNT2B were longer than that of other human WNTs.
6177036	1	9	gly	glycoproteins	110:122	arg1	mouse brain Thy-1 glycoproteins	mouse brain Thy-1 glycoproteins				PUBTATOR		Thy-1 glycoproteins	21838		The amino acid sequences of mouse brain Thy-1 glycoproteins are shown to be homologous to those of variable-region immunoglobulin domains.
1577715	2	57	gly	asparagine-linked	148:164	arg1	The asparagine-linked oligosaccharide chains			asparagine	The asparagine-linked oligosaccharide chains					asparagine	The asparagine-linked oligosaccharide chains of human von Willebrand factor (vWF) purified from pooled plasma were quantitatively liberated from the polypeptide moiety by hydrazinolysis.
1577715	2	74	gly	factor	213:218	arg1	The asparagine-linked oligosaccharide chains	von Willebrand factor			The asparagine-linked oligosaccharide chains	PUBTATOR		von Willebrand factor	7450		The asparagine-linked oligosaccharide chains of human von Willebrand factor (vWF) purified from pooled plasma were quantitatively liberated from the polypeptide moiety by hydrazinolysis.
24530628	1	16	gly	glycosylation	107:119	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			LC/MS is commonly used for site-specific glycosylation analysis of glycoproteins in cells and tissues.
24530628	1	53	gly	glycoproteins	133:145	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			LC/MS is commonly used for site-specific glycosylation analysis of glycoproteins in cells and tissues.
12944413	3	8	gly	SERT	591:594	arg1	sialic acid-defective Lec4 Chinese hamster ovary (CHO) cells	SERT			sialic acid-defective Lec4 Chinese hamster ovary (CHO) cells	PUBTATOR		SERT	6532		In this study, we investigated the contribution of N-glycosyl modification to the structure and function of SERT in two model systems: wild-type SERT expressed in sialic acid-defective Lec4 Chinese hamster ovary (CHO) cells and a mutant form (after site-directed mutagenesis of Asn-208 and Asn-217 to Gln) of SERT, QQ, expressed in parental CHO cells.
11459848	8	6	part_of	protein	1032:1038	arg1	the C terminus	protein		the C terminus		Fterm	Site	protein		terminus	We could identify eight threonines modified by O-glycans, leaving the C terminus of the protein free of glycans.
7538124	4	11	gly	glycosylation	681:693	arg2	potential glycosylation sites			potential glycosylation sites						sites	For this, we generated a panel of K18 Ser and Thr-->Ala mutants at potential glycosylation sites followed by expression in a baculovirus-insect cell system.
6546754	1	62	part_of	B	125:125	arg1	The entire amino acid sequence	complement factor B		The entire amino acid sequence		PUBTATOR	Site	complement factor B	629	sequence	The entire amino acid sequence of complement factor B has been established combining both protein and DNA sequencing strategies.
7538124	2	85	gly	linked	402:407	arg1	Ser/Thr AND O-GlcNAc			Ser/Thr	O-GlcNAc					Ser/Thr	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
25153361	0	43	gly	glycoproteins	63:75	arg1	complex glycoproteins	complex glycoproteins				Fterm		glycoproteins			Confident assignment of site-specific glycosylation in complex glycoproteins in a single step.
19276170	3	54	gly	COMP	612:615	arg1	the type 3 repeats	COMP			the type 3 repeats	OGER		COMP	P49747		In this study, we determined the structure of a recombinant protein that contains the last epidermal growth factor repeat, the type 3 repeats and the C-terminal domain (CTD) of COMP to 3.15-A resolution limit by X-ray crystallography.
19276170	3	49	gly	contains	508:515	arg1	a recombinant protein AND the last epidermal growth factor repeat	a recombinant protein			the last epidermal growth factor repeat	Fterm		protein			In this study, we determined the structure of a recombinant protein that contains the last epidermal growth factor repeat, the type 3 repeats and the C-terminal domain (CTD) of COMP to 3.15-A resolution limit by X-ray crystallography.
15616124	7	18	gly	N-glycosylation	957:971	arg2	N-glycosylation site knockout mutants			N-glycosylation site knockout mutants						site	Pulse-chase analysis of N-glycosylation site knockout mutants demonstrated cotranslational glycosylation of N145 but primarily or exclusively posttranslational glycosylation of N322.
15616124	7	40	gly	glycosylation	1024:1036	arg1	N145			N145						N145	Pulse-chase analysis of N-glycosylation site knockout mutants demonstrated cotranslational glycosylation of N145 but primarily or exclusively posttranslational glycosylation of N322.
15616124	7	63	gly	glycosylation	1093:1105	arg1	N322			N322						N322	Pulse-chase analysis of N-glycosylation site knockout mutants demonstrated cotranslational glycosylation of N145 but primarily or exclusively posttranslational glycosylation of N322.
21712440	3	101	gly	glycopeptides	618:630	arg2	glycopeptides			glycopeptides						peptides and glycopeptides	We used the 6E10 antibody and immunopurified Aβ peptides and glycopeptides from CSF samples and then liquid chromatography-tandem mass spectrometry for structural analysis using collision-induced dissociation and electron capture dissociation.
1567356	1	10	gly	contains	95:102	arg1	Orosomucoid AND tetra-antennary glycan chains	Orosomucoid (OMD			tetra-antennary glycan chains	OGER		Orosomucoid (OMD	Q99983		Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains.
1567356	1	10	gly	contains	95:102	arg1	Orosomucoid AND tri-	Orosomucoid (OMD			tri-	OGER		Orosomucoid (OMD	Q99983		Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains.
1567356	1	10	gly	contains	95:102	arg1	Orosomucoid AND complex bi-	Orosomucoid (OMD			complex bi-	OGER		Orosomucoid (OMD	Q99983		Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains.
7538124	0	25	part_of	keratin	75:81	arg1	the glycosylation sites	keratin 18		the glycosylation sites		PUBTATOR	Site	keratin 18	3875	sites	Identification and mutational analysis of the glycosylation sites of human keratin 18.
12218058	1	1	gly	glycosylated	160:171	arg1	a glycosylated metalloproteinase	a glycosylated metalloproteinase				Fterm		metalloproteinase			Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	1	1	gly	glycosylated	160:171	arg1	Bone morphogenetic protein (BMP)-1	Bone morphogenetic protein (BMP)-1				PUBTATOR		Bone morphogenetic protein (BMP)-1	649		Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
23345538	9	72	gly	glycoprotein	1627:1638	arg1	glycoprotein enrichment	glycoprotein enrichment				Fterm		glycoprotein			Validation was performed by means of glycoprotein enrichment and analysis of the input, the flow-through, and the bound fraction.
15014436	2	55	part_of	TSPs	242:245	arg1	The most highly conserved region	TSPs		The most highly conserved region		Cterm	Site	TSPs	7057	region	The most highly conserved region of all TSPs are the calcium-binding type 3 (T3) repeats and the C-terminal globular domain (CTD).
22448645	3	13	gly	N-glycosylated	547:560	arg1	an N-glycosylated form	an N-glycosylated form				OGER		N-glycosylated form of the 5-HT(7	P34969		Western blot analysis of HEK293T cells transiently expressing the 5-HT(7(a)) receptor in the presence of tunicamycin gave rise to a band shift, indicating the existence of an N-glycosylated form of the 5-HT(7(a)) receptor.
22448645	3	13	gly	N-glycosylated	547:560	arg1	the 5-HT(7(a)) receptor	the 5-HT(7(a)) receptor				Fterm		receptor			Western blot analysis of HEK293T cells transiently expressing the 5-HT(7(a)) receptor in the presence of tunicamycin gave rise to a band shift, indicating the existence of an N-glycosylated form of the 5-HT(7(a)) receptor.
18952059	4	21	gly	glycosylation	461:473	arg1	IZUMO	IZUMO				PUBTATOR		IZUMO	73456		The expression of N204Q-IZUMO rescued the infertile phenotype of IZUMO disrupted mice, indicating glycosylation is not essential for fusion-facilitating activity of IZUMO.
8336134	7	55	gly	fucosylated	1382:1392	arg1	complex-type oligosaccharide structures				complex-type oligosaccharide structures						Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	69	gly	sialylated	1265:1274	arg1	complex-type oligosaccharide structures				complex-type oligosaccharide structures						Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	77	gly	bear	1197:1200	arg1	Asn29 AND complex-type oligosaccharide structures			Asn29 and Asn56	complex-type oligosaccharide structures					Asn29 and Asn56	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
7524900	2	15	gly	contains	328:335	arg1	proMBP AND O-linked glycan	proMBP			O-linked glycan	PUBTATOR		proMBP	5553		It is shown that proMBP contains O-linked glycan bound to Ser-24, Thr-25 (fully substituted), and to Thr-23 and Thr-34 (partially substituted).
10207177	9	39	gly	glycoproteins	1920:1932	arg1	the glycoproteins	the glycoproteins				Fterm		glycoproteins			The glycans invariably shield large regions of the protein surfaces although, for the glycoproteins examined here, these did not hinder the known active sites of the molecules.
23242014	7	59	gly	glycosylated	871:882	arg1	the glycosylated sites			the glycosylated sites						sites	Detailed characterization of the glycosylated sites is helpful for the understanding of different phenotypes as well as for the development of E1/E2-related treatments of HCV infection.
32363391	3	52	part_of	possess	550:556	arg1	two protein subunits AND 22 potential N-glycosylation sites	two protein subunits		22 potential N-glycosylation sites		Fterm	Site	subunits		sites	The spike protein is comprised of two protein subunits (S1 and S2), which together possess 22 potential N-glycosylation sites.
1904059	8	4	gly	linked	1127:1132	arg2	serine 52 AND three different glycan structures			serine 52	three different glycan structures					serine 52	Using a combined strategy of amino acid sequencing, carbohydrate and amino acid composition analysis, and mass spectrometry, three different glycan structures consisting of either glucose, glucose-xylose, or glucose-(xylose)2 were detected O-glycosidically linked to serine 52 in plasma and recombinant factor VII.
17082223	3	0	gly	glycosylated	795:806	arg1	each site			each site						site	Immunoblot and glycosidase cleavage analysis demonstrated that each site was glycosylated.
18514042	6	29	gly	glycoproteins	1042:1054	arg1	abundant serum glycoproteins	abundant serum glycoproteins				Fterm		glycoproteins			We successfully demonstrated site-specific glycosylation of 23 sites in abundant serum glycoproteins.
18514042	6	63	gly	glycosylation	998:1010	arg1	abundant serum glycoproteins	glycoproteins		sites		Fterm		glycoproteins		sites	We successfully demonstrated site-specific glycosylation of 23 sites in abundant serum glycoproteins.
8407981	6	14	gly	glycosylation	937:949	arg1	the two mutant proteins	the two mutant proteins				Fterm		proteins			Since the P-450(arom) molecule has two potential glycosylation sites (Asn-12 and Asn-180), we replaced each of the 2 asparagine residues with alanine by site-directed mutagenesis and examined the glycosylation of the two mutant proteins in the cell-free system.
8407981	6	19	gly	glycosylation	790:802	arg2	two potential glycosylation sites			two potential glycosylation sites						sites	Since the P-450(arom) molecule has two potential glycosylation sites (Asn-12 and Asn-180), we replaced each of the 2 asparagine residues with alanine by site-directed mutagenesis and examined the glycosylation of the two mutant proteins in the cell-free system.
8407981	6	54	gly	sites	804:808	arg1	two potential glycosylation sites			two potential glycosylation sites						sites	Since the P-450(arom) molecule has two potential glycosylation sites (Asn-12 and Asn-180), we replaced each of the 2 asparagine residues with alanine by site-directed mutagenesis and examined the glycosylation of the two mutant proteins in the cell-free system.
8407981	6	19	gly	glycosylation	790:802	arg2	Asn-12			Asn-12 and Asn-180						Asn-12 and Asn-180	Since the P-450(arom) molecule has two potential glycosylation sites (Asn-12 and Asn-180), we replaced each of the 2 asparagine residues with alanine by site-directed mutagenesis and examined the glycosylation of the two mutant proteins in the cell-free system.
8407981	6	54	gly	sites	804:808	arg1	Asn-12			Asn-12 and Asn-180						Asn-12 and Asn-180	Since the P-450(arom) molecule has two potential glycosylation sites (Asn-12 and Asn-180), we replaced each of the 2 asparagine residues with alanine by site-directed mutagenesis and examined the glycosylation of the two mutant proteins in the cell-free system.
19358553	6	87	gly	glycopeptides	1527:1539	arg2	glycopeptides			glycopeptides						glycopeptides	In conclusion, MALDI-TOF MS signal strength of glycopeptides has been found to accurately reflect the relative quantities of glycoforms, providing that certain technical issues are considered, i.e., nonbiased sample handling, matrix choice, and instrumental settings.
7827751	2	11	gly	residues	298:305	arg1	the Col 1 and 149 residues			residues in	the Col 1 and 149 residues					residues in	Edman degradation demonstrated 106 amino acids residues in the Col 1 and 149 residues in the Col 2 domain.
7827751	2	29	gly	residues	328:335	arg1	the Col 2 domain			residues in	the Col 2 domain					residues in	Edman degradation demonstrated 106 amino acids residues in the Col 1 and 149 residues in the Col 2 domain.
23001782	8	66	gly	occupied	1355:1362	arg2	The N-terminal Thr			Thr(7)						Thr(7)	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
8407981	7	4	gly	glycosylated	1138:1149	arg1	the mutant protein	the mutant protein				Fterm		protein			The core glycosylation did not occur when the Asn-12 residue was mutated, whereas the mutant protein with modified Asn-180 residue was glycosylated.
19358553	3	26	gly	glycoproteins	603:615	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Glycopeptides derived from glycoproteins containing neutral glycans (ribonuclease B, IgG, and ovalbumin) were initially profiled and yielded excellent and reproducible quantitation (correlation coefficient r = 0.9958, n = 5) when evaluated against a normal phase HPLC 2-AB glycan profile.
19358553	3	64	gly	ribonuclease	645:656	arg1	neutral glycans	ribonuclease B			neutral glycans	Cterm		ribonuclease B			Glycopeptides derived from glycoproteins containing neutral glycans (ribonuclease B, IgG, and ovalbumin) were initially profiled and yielded excellent and reproducible quantitation (correlation coefficient r = 0.9958, n = 5) when evaluated against a normal phase HPLC 2-AB glycan profile.
19358553	3	40	gly	containing	617:626	arg1	glycoproteins AND neutral glycans	glycoproteins			neutral glycans	Fterm		glycoproteins			Glycopeptides derived from glycoproteins containing neutral glycans (ribonuclease B, IgG, and ovalbumin) were initially profiled and yielded excellent and reproducible quantitation (correlation coefficient r = 0.9958, n = 5) when evaluated against a normal phase HPLC 2-AB glycan profile.
21550978	5	24	gly	ligand	967:972	arg1	Asn			Asn(75)						Asn(75)	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	5	84	gly	glycosylation	897:909	arg1	the N terminus			terminus						terminus	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
24417605	1	15	gly	glycosylated	185:196	arg1	functional proteins	functional proteins				Fterm		proteins			Many of the functional proteins and lipids in high density lipoprotein (HDL) particles are potentially glycosylated, yet very little is known about the glycoconjugates of HDL.
8404899	4	21	gly	glycosylated	636:647	arg1	the glycosylated proteins	the glycosylated proteins				Fterm		proteins			Among the glycosylated proteins present in human pancreatic juice, only the glycosylation of bile-salt-dependent lipase differs between individuals.
8404899	4	63	gly	glycosylation	702:714	arg1	bile-salt-dependent lipase	bile-salt-dependent lipase				Fterm		lipase			Among the glycosylated proteins present in human pancreatic juice, only the glycosylation of bile-salt-dependent lipase differs between individuals.
3667593	4	50	gly	IFN-beta	714:721	arg1	The major oligosaccharide	IFN-beta			The major oligosaccharide	PUBTATOR		IFN-beta	3456		The major oligosaccharide of the recombinant IFN-beta is remarkably homogeneous with respect to terminal galactose sialylation.
19855092	4	6	part_of	adiponectin	756:766	arg1	Thr residues	adiponectin		Thr residues		PUBTATOR	AminoAcid	adiponectin	9370	Thr residues	Using a variety of biochemical approaches we demonstrated that sialylation occurs on previously unidentified O-linked glycans on Thr residues of the variable domain in human adiponectin.
19855092	4	6	part_of	adiponectin	756:766	arg1	the variable domain	adiponectin		the variable domain		PUBTATOR	Site	adiponectin	9370	domain	Using a variety of biochemical approaches we demonstrated that sialylation occurs on previously unidentified O-linked glycans on Thr residues of the variable domain in human adiponectin.
19855092	4	66	part_of	domain	740:745	arg1	human adiponectin	adiponectin		domain		PUBTATOR	Site	adiponectin	9370	domain	Using a variety of biochemical approaches we demonstrated that sialylation occurs on previously unidentified O-linked glycans on Thr residues of the variable domain in human adiponectin.
19855092	4	75	part_of	residues	715:722	arg1	human adiponectin	adiponectin		residues		PUBTATOR	AminoAcid	adiponectin	9370	Thr residues	Using a variety of biochemical approaches we demonstrated that sialylation occurs on previously unidentified O-linked glycans on Thr residues of the variable domain in human adiponectin.
32155444	3	32	part_of	S	376:376	arg1	the receptor-binding domains	S		the receptor-binding domains		Cterm	Site	S	43740568	domains	We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating with the efficient spread of SARS-CoV-2 among humans.
12063277	7	23	gly	nonglycosylated	1058:1072	arg1	nonglycosylated HERG channel	nonglycosylated HERG channel				PUBTATOR		HERG channel	3757		Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
17395589	3	50	gly	contains	259:266	arg1	ADAMTS13 AND eight thrombospondin type 1 repeats	ADAMTS13			eight thrombospondin type 1 repeats	PUBTATOR		ADAMTS13	11093		ADAMTS13 contains eight thrombospondin type 1 repeats (TSR), seven of which contain a consensus sequence for the direct addition of fucose to the hydroxyl group of serine or threonine.
10899108	3	26	part_of	found	506:510	arg1	the p40 subunit AND an N-terminal immunoglobulin-like domain	the p40 subunit		an N-terminal immunoglobulin-like domain		PUBTATOR	Site	p40 subunit	3578	domain	They also include the first description of an N-terminal immunoglobulin-like domain, found on the p40 subunit.
21917917	8	58	gly	N-glycosylated	1320:1333	arg1	Asn-260			residues, Asn-260 and Asn-264						residues, Asn-260 and Asn-264	The orientation of this domain was further confirmed by the identification of two N-glycosylated residues, Asn-260 and Asn-264.
21917917	8	58	gly	N-glycosylated	1320:1333	arg1	two N-glycosylated residues			residues, Asn-260 and Asn-264						residues, Asn-260 and Asn-264	The orientation of this domain was further confirmed by the identification of two N-glycosylated residues, Asn-260 and Asn-264.
21917917	8	58	gly	N-glycosylated	1320:1333	arg1	two N-glycosylated residues			residues, Asn-260 and Asn-264						residues, Asn-260 and Asn-264	The orientation of this domain was further confirmed by the identification of two N-glycosylated residues, Asn-260 and Asn-264.
21037563	6	18	part_of	perforin-like	1096:1108	arg1	an amino-terminal membrane attack complex perforin-like (MACPF)/cholesterol dependent cytolysin (CDC) domain	perforin		an amino-terminal membrane attack complex perforin-like (MACPF)/cholesterol dependent cytolysin (CDC) domain		Fterm	Site	perforin		domain	Perforin is a thin 'key-shaped' molecule, comprising an amino-terminal membrane attack complex perforin-like (MACPF)/cholesterol dependent cytolysin (CDC) domain followed by an epidermal growth factor (EGF) domain that, together with the extreme carboxy-terminal sequence, forms a central shelf-like structure.
21037563	6	57	part_of	factor	1195:1200	arg1	an epidermal growth factor (EGF) domain	factor		an epidermal growth factor (EGF) domain		Fterm	Site	factor		domain	Perforin is a thin 'key-shaped' molecule, comprising an amino-terminal membrane attack complex perforin-like (MACPF)/cholesterol dependent cytolysin (CDC) domain followed by an epidermal growth factor (EGF) domain that, together with the extreme carboxy-terminal sequence, forms a central shelf-like structure.
11080501	8	31	gly	domains	1670:1676	arg1	GA733 type 3 motif			GA733 type 3 motif						motif	These data show that the extracellular domain of the GA733-2 antigen consists of three distinct domains; a novel cysteine-rich N-terminal domain (GA733 type 1 motif), a cysteine-rich thyroglobulin type 1A domain (GA733 type 2 motif), and a unique nonglycosylated domain without cysteines (GA733 type 3 motif).
11080501	8	31	gly	domains	1670:1676	arg1	a unique nonglycosylated domain			a unique nonglycosylated domain						domain	These data show that the extracellular domain of the GA733-2 antigen consists of three distinct domains; a novel cysteine-rich N-terminal domain (GA733 type 1 motif), a cysteine-rich thyroglobulin type 1A domain (GA733 type 2 motif), and a unique nonglycosylated domain without cysteines (GA733 type 3 motif).
11080501	8	86	gly	nonglycosylated	1821:1835	arg1	a unique nonglycosylated domain			a unique nonglycosylated domain						domain	These data show that the extracellular domain of the GA733-2 antigen consists of three distinct domains; a novel cysteine-rich N-terminal domain (GA733 type 1 motif), a cysteine-rich thyroglobulin type 1A domain (GA733 type 2 motif), and a unique nonglycosylated domain without cysteines (GA733 type 3 motif).
11080501	8	86	gly	nonglycosylated	1821:1835	arg1	three distinct domains			three distinct domains						domains	These data show that the extracellular domain of the GA733-2 antigen consists of three distinct domains; a novel cysteine-rich N-terminal domain (GA733 type 1 motif), a cysteine-rich thyroglobulin type 1A domain (GA733 type 2 motif), and a unique nonglycosylated domain without cysteines (GA733 type 3 motif).
11080501	8	86	gly	nonglycosylated	1821:1835	arg1	GA733 type 3 motif			GA733 type 3 motif						motif	These data show that the extracellular domain of the GA733-2 antigen consists of three distinct domains; a novel cysteine-rich N-terminal domain (GA733 type 1 motif), a cysteine-rich thyroglobulin type 1A domain (GA733 type 2 motif), and a unique nonglycosylated domain without cysteines (GA733 type 3 motif).
27374339	5	26	part_of	Izumo1	867:872	arg1	different regions	Izumo1		different regions		PUBTATOR	Site	Izumo1	284359	regions	Remarkably, different regions of Izumo1 display significant structural similarities to two proteins expressed by the invasive sporozoite stage of Plasmodium parasites: SPECT1, which is essential for host cell traversal and hepatocyte invasion [3]; and TRAP, which is necessary for gliding motility and invasion [4].
22171320	6	45	gly	glycoproteins	968:980	arg1	Sialylated urinary glycoproteins	Sialylated urinary glycoproteins				Fterm		glycoproteins			Sialylated urinary glycoproteins were conjugated to a solid support by hydrazide chemistry and trypsin digested.
21525977	0	24	part_of	NPC1L1	21:26	arg1	the NPC1L1 N-terminal domain	structure of the NPC1L1		the NPC1L1 N-terminal domain		PUBTATOR	Site	structure of the NPC1L1	29881	domain	The structure of the NPC1L1 N-terminal domain in a closed conformation.
18702514	1	3	part_of	lipase	133:138	arg1	the active site	pancreatic lipase		the active site		PUBTATOR	Site	pancreatic lipase	5406	site	Access to the active site of pancreatic lipase (PL) is controlled by a surface loop, the lid, which normally undergoes conformational changes only upon addition of lipids or amphiphiles.
1740433	8	5	part_of	C-SAA	1078:1082	arg1	The C-SAA octapeptide	SAA		The C-SAA octapeptide		PUBTATOR	Site	SAA	6291	octapeptide	The C-SAA octapeptide specifies the first two residues of a NSS tripeptide, the only potential N-linked glycosylation site in the molecule.
8243461	0	0	gly	chains	43:48	arg1	the activation peptides			the activation peptides	the activation peptides		Site			peptides	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
16335952	8	44	gly	glycosylation	1729:1741	arg2	these glycosylation site assignments			these glycosylation site assignments						site	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	8	91	gly	N-glycosylation	1651:1665	arg2	639 N-glycosylation sites			639 N-glycosylation sites						sites	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
18642129	4	66	gly	glycosylation	665:677	arg2	each glycosylation site			each glycosylation site						site	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	4	93	gly	FVII	604:607	arg1	N-	FVII			N-	OGER		FVII	P08709		Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
8053566	2	49	gly	glycosylation	417:429	arg2	two glycosylation sites			two glycosylation sites						sites	Recombinant human tissue inhibitor of metalloproteinases (TIMP), which has two glycosylation sites, has been characterized to illustrate this new approach for obtaining site-specific information.
3980466	11	91	part_of	sites	1978:1982	arg1	structurally related glycoproteins	glycoproteins		sites		Fterm	Site	glycoproteins		sites	First, the overall distributions of oligosaccharides at corresponding sites on structurally related glycoproteins are similar.
8435067	0	11	gly	glycosylation	70:82	arg2	the glycosylation sites			the glycosylation sites						sites	Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites.
6118137	2	43	part_of	glycoprotein	147:158	arg1	The full sequence	Thy-1 membrane glycoprotein		The full sequence		OGER	Site	Thy-1 membrane glycoprotein	P01830	sequence	The full sequence of the Thy-1 membrane glycoprotein of rat brain is reported.
12878160	1	54	gly	glycoproteins	135:147	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Subsets of glycoproteins are thought to require lectin-like membrane receptors for efficient export out of the endoplasmic reticulum (ER).
18340083	3	34	part_of	Ly-6	541:544	arg1	the Ly-6 domain	Ly-6		the Ly-6 domain		PUBTATOR	Site	Ly-6	17062	domain	Here, we show that mouse GPIHBP1 is N-glycosylated at Asn-76 within the Ly-6 domain.
8349699	2	104	gly	glycosylated	335:346	arg1	A fourth consensus N-glycosylation sequence			A fourth consensus N-glycosylation sequence						sequence	A fourth consensus N-glycosylation sequence at Asn104 is not glycosylated.
7505568	1	0	gly	glycoprotein	102:113	arg1	MAG	MAG				PUBTATOR		MAG	4099		Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	1	0	gly	glycoprotein	102:113	arg1	Myelin-associated glycoprotein	Myelin-associated glycoprotein				PUBTATOR		Myelin-associated glycoprotein	4099		Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
14749323	11	82	gly	glycosylation	2054:2066	arg1	OAT1	OAT1				PUBTATOR		OAT1	9356		This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
26192331	2	13	part_of	polysialyltransferase-specific	539:568	arg1	polysialyltransferase-specific structural motifs	polysialyltransferase		polysialyltransferase-specific structural motifs		Fterm	Site	polysialyltransferase		motifs	The crystal structure of human ST8SiaIII at 1.85-Å resolution presented here is, to our knowledge, the first solved structure of a polysialyltransferase from any species, and it reveals a cluster of polysialyltransferase-specific structural motifs that collectively provide an extended electropositive surface groove for binding of oligo-polysialic acid chain products.
16877748	5	75	gly	N-glycosylation	931:945	arg2	N-glycosylation sites			N-glycosylation sites						sites	The present study was aimed at elucidating the N-glycosylation of mouse sICAM-1 expressed in wild-type CHO cells with regard to sialylation, N-glycan profile, and N-glycosylation sites.
16877748	5	102	gly	N-glycosylation	815:829	arg1	mouse sICAM-1	mouse sICAM-1				Cterm		sICAM-1	3383		The present study was aimed at elucidating the N-glycosylation of mouse sICAM-1 expressed in wild-type CHO cells with regard to sialylation, N-glycan profile, and N-glycosylation sites.
16037490	0	71	gly	glycopeptide	133:144	arg2	glycopeptide enrichment			glycopeptide enrichment						glycopeptide	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
18984734	10	51	gly	occupancy	1515:1523	arg1	erythrocyte proteins	proteins			occupancy	Fterm		proteins			These data suggest not only that site-specific O-GlcNAc levels reflect the glycemic status of an individual but also that O-GlcNAc site occupancy on erythrocyte proteins may be eventually useful as a diagnostic tool for the early detection of diabetes.
1457969	6	42	gly	2-3-sialylated	1124:1137	arg1	chiefly alpha 2-3-sialylated Gal				chiefly alpha 2-3-sialylated Gal						The Man alpha 1-6 branch displayed structural heterogeneity in the terminal sequence, with chiefly alpha 2-3-sialylated Gal and/or 4-O-sulphated GalNAc.
19159218	3	15	gly	N-glycopeptides	600:614	arg2	tryptic N-glycopeptides			tryptic N-glycopeptides						N-glycopeptides	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
17330941	8	15	gly	glycopeptides	1100:1112	arg2	glycopeptides			glycopeptides						glycopeptides	Only 42 proteins were seen when the same plasma sample was analyzed by glycopeptides only.
12731890	0	70	part_of	receptor	71:78	arg1	glycosylation sites	epidermal growth factor receptor		glycosylation sites		PUBTATOR	Site	epidermal growth factor receptor	1956	sites	Characterization of glycosylation sites of the epidermal growth factor receptor.
1991473	8	59	part_of	hLH	1255:1257	arg1	Asn78	hLH alpha		Asn78		PUBTATOR	AminoAcid	hLH alpha	1081	Asn78	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
24927598	4	36	gly	deglycosylated	580:593	arg1	ZIP14	ZIP14				PUBTATOR		ZIP14	23516		In an attempt to dissect the molecular mechanisms by which iron regulates ZIP14 levels, we found that ZIP14 is endocytosed, extracted from membranes, deglycosylated, and degraded by proteasomes.
30061605	3	0	part_of	SorCS2-NGF	341:350	arg1	the SorCS2-NGF complex and unliganded SorCS2 ectodomain	SorCS2		the SorCS2-NGF complex and unliganded SorCS2 ectodomain		OGER	Site	SorCS2	Q96PQ0	ectodomain	Here we report crystal structures of the SorCS2-NGF complex and unliganded SorCS2 ectodomain, revealing cross-braced SorCS2 homodimers with two NGF dimers bound in a 2:4 stoichiometry.
30061605	3	10	part_of	SorCS2	375:380	arg1	the SorCS2-NGF complex and unliganded SorCS2 ectodomain	SorCS2		the SorCS2-NGF complex and unliganded SorCS2 ectodomain		OGER	Site	SorCS2	Q96PQ0	ectodomain	Here we report crystal structures of the SorCS2-NGF complex and unliganded SorCS2 ectodomain, revealing cross-braced SorCS2 homodimers with two NGF dimers bound in a 2:4 stoichiometry.
12589760	5	54	part_of	CLIP	834:837	arg1	the CLIP peptide	CLIP		the CLIP peptide		PUBTATOR	Site	CLIP	6249	peptide	When compared to the related HLA-DR3/CLIP complex structure, the CLIP peptide displays a slightly different conformation and distinct interaction pattern with residues in I-A(b).
3202829	6	15	gly	Glycosylation	772:784	arg2	Asn-88			Asn-88						Asn-88	Glycosylation at Asn-88 has not been observed previously in mammalian secretory RNases.
3521732	1	25	part_of	prekallikrein	134:146	arg1	The amino acid sequence	plasma prekallikrein		The amino acid sequence		PUBTATOR	Site	plasma prekallikrein	3818	sequence	The amino acid sequence of human plasma prekallikrein was determined by a combination of automated Edman degradation and cDNA sequencing techniques.
22235133	3	2	part_of	receptor	444:451	arg1	the class I cytokine receptor signature motif	receptor		the class I cytokine receptor signature motif		Fterm	Site	receptor		motif	A hallmark of the class I cytokine receptors is the class I cytokine receptor signature motif (WSXWS).
22235133	3	54	part_of	receptors	410:418	arg1	the class I cytokine receptor signature motif	receptors		the class I cytokine receptor signature motif		Fterm	Site	receptors		motif	A hallmark of the class I cytokine receptors is the class I cytokine receptor signature motif (WSXWS).
15477100	1	67	gly	Zn-alpha2-glycoprotein	70:91	arg1	ZAG	ZAG				PUBTATOR		ZAG	563		Zn-alpha2-glycoprotein (ZAG) is a 41 kDa soluble protein that is present in most bodily fluids.
15477100	1	67	gly	Zn-alpha2-glycoprotein	70:91	arg1	Zn-alpha2-glycoprotein	Zn-alpha2-glycoprotein				PUBTATOR		Zn-alpha2-glycoprotein	563		Zn-alpha2-glycoprotein (ZAG) is a 41 kDa soluble protein that is present in most bodily fluids.
15477100	1	67	gly	Zn-alpha2-glycoprotein	70:91	arg1	a 41 kDa soluble protein	a 41 kDa soluble protein				Fterm		protein			Zn-alpha2-glycoprotein (ZAG) is a 41 kDa soluble protein that is present in most bodily fluids.
19167329	6	62	part_of	site	985:988	arg1	an unfolded protein	protein		site		Fterm	Site	protein		site	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
12901863	5	8	part_of	ABCC6	872:876	arg1	the extracellular N-terminal region	ABCC6		the extracellular N-terminal region		PUBTATOR	Site	ABCC6	368	region	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	5	21	part_of	site	907:910	arg1	this protein	protein		site		Fterm	Site	protein		site	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
19343721	6	13	gly	predominant	1129:1139	arg2	the Asn-329 site AND glycans			the Asn-329 site	glycans					Asn-329 site	Interestingly, glycans with GalNAc in the antennae were predominant at the Asn-329 site.
18036614	5	42	part_of	NtMGAM	997:1002	arg1	the NtMGAM active site	NtMGAM		the NtMGAM active site		Cterm	Site	NtMGAM	8972	site	These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship.
479158	0	43	gly	variants	38:45	arg1	Carbohydrate	plasminogen variants			Carbohydrate	OGER		plasminogen variants	P00747		Carbohydrate of the human plasminogen variants.
16368742	6	13	gly	glycosylation	1366:1378	arg2	a nearly identically situated and experimentally confirmed N-linked glycosylation site			a nearly identically situated and experimentally confirmed N-linked glycosylation site						site	Although glycosylation in this vicinity has not been reported for a TRP channel, the structurally related hexahelical hyperpolarization-activated cyclic nucleotide-gated channel, HCN2, and the voltage-gated potassium channel, human ether-a-go-go-related (HERG), share a nearly identically situated and experimentally confirmed N-linked glycosylation site which promotes rather than limits channel insertion into the plasma membrane.
10756055	0	45	gly	glycosylation	9:21	arg1	CXCR4	CXCR4				PUBTATOR		CXCR4	7852		N-linked glycosylation of CXCR4 masks coreceptor function for CCR5-dependent human immunodeficiency virus type 1 isolates.
28450392	8	11	gly	NSL3	1347:1350	arg1	O-GlcNAcylation	NSL3			O-GlcNAcylation	PUBTATOR		NSL3	55683		Moreover, O-GlcNAcylation of NSL3 by wild-type OGT1 (OGT1-WT) stabilized NSL3.
10861210	5	15	part_of	AE1	819:821	arg1	N555	AE1		N555		PUBTATOR	SpecificSite	AE1	6521	N555	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
7620335	0	22	part_of	factor	70:75	arg1	human coagulation factor X activation peptide	factor X		human coagulation factor X activation peptide		OGER	Site	factor X	P00742	peptide	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	0	72	part_of	X	77:77	arg1	human coagulation factor X activation peptide	factor X		human coagulation factor X activation peptide		OGER	Site	factor X	P00742	peptide	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	0	94	part_of	coagulation	58:68	arg1	human coagulation factor X activation peptide	coagulation factor X		human coagulation factor X activation peptide		OGER	Site	coagulation factor X	P00742	peptide	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
8639592	10	28	gly	glycosylated	1949:1960	arg1	the region			the region						region	Thus, the region between Kunitz domains 2 and 3 encoded by exon 7 was highly glycosylated by two O-linked carbohydrate chains at Ser174 and Thr175 and one N-linked carbohydrate chain at Asn167.
8639592	10	35	gly	Ser174	2001:2006	arg1	two O-linked carbohydrate chains			Ser174 and Thr175	two O-linked carbohydrate chains					Ser174 and Thr175	Thus, the region between Kunitz domains 2 and 3 encoded by exon 7 was highly glycosylated by two O-linked carbohydrate chains at Ser174 and Thr175 and one N-linked carbohydrate chain at Asn167.
8639592	10	39	gly	Thr175	2012:2017	arg1	two O-linked carbohydrate chains			Ser174 and Thr175	two O-linked carbohydrate chains					Ser174 and Thr175	Thus, the region between Kunitz domains 2 and 3 encoded by exon 7 was highly glycosylated by two O-linked carbohydrate chains at Ser174 and Thr175 and one N-linked carbohydrate chain at Asn167.
8639592	10	107	gly	Asn167	2058:2063	arg1	one N-linked carbohydrate chain			Asn167	one N-linked carbohydrate chain					Asn167	Thus, the region between Kunitz domains 2 and 3 encoded by exon 7 was highly glycosylated by two O-linked carbohydrate chains at Ser174 and Thr175 and one N-linked carbohydrate chain at Asn167.
15869464	0	76	gly	O-glycosylation	138:152	arg2	36 phosphorylation and five O-glycosylation sites			36 phosphorylation and five O-glycosylation sites						sites	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
14981520	9	34	gly	glycosylation	1494:1506	arg1	seipin	seipin				PUBTATOR		seipin	26580		The amino acid substitutions N88S and S90L affect glycosylation of seipin and result in aggregate formation leading to neurodegeneration.
10764840	1	3	gly	glycosylation	277:289	arg2	1 O- glycosylation site			1 O- glycosylation site						site	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	3	gly	glycosylation	277:289	arg2	Ser-126			Ser-126						Ser-126	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	10	gly	N-glycosylation	217:231	arg2	three N-glycosylation sites			three N-glycosylation sites						sites	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	39	gly	sites	233:237	arg1	three N-glycosylation sites			three N-glycosylation sites						sites	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	10	gly	N-glycosylation	217:231	arg2	Asn-24			Asn-24, Asn-38, and Asn-83						Asn-24, Asn-38, and Asn-83	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	10	gly	N-glycosylation	217:231	arg2	Asn-83			Asn-24, Asn-38, and Asn-83						Asn-24, Asn-38, and Asn-83	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	10	gly	N-glycosylation	217:231	arg2	Asn-83			Asn-24, Asn-38, and Asn-83						Asn-24, Asn-38, and Asn-83	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	39	gly	sites	233:237	arg1	Asn-83			Asn-24, Asn-38, and Asn-83						Asn-24, Asn-38, and Asn-83	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	39	gly	sites	233:237	arg1	Asn-24			Asn-24, Asn-38, and Asn-83						Asn-24, Asn-38, and Asn-83	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	39	gly	sites	233:237	arg1	Asn-24			Asn-24, Asn-38, and Asn-83						Asn-24, Asn-38, and Asn-83	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
8617200	4	19	part_of	TGF-beta1	887:895	arg1	the LAP region	TGF-beta1		the LAP region		PUBTATOR	Site	TGF-beta1	4052	region	Immunoblotting of the fusion protein complexes indicated that the third 8-Cys repeat of LTBP-1 bound covalently to the LAP region of TGF-beta1.
8617200	4	39	part_of	LAP	873:875	arg1	the LAP region	LAP		the LAP region		PUBTATOR	Site	LAP	P11117	region	Immunoblotting of the fusion protein complexes indicated that the third 8-Cys repeat of LTBP-1 bound covalently to the LAP region of TGF-beta1.
10995228	5	25	gly	moieties	727:734	arg1	mER-beta	mER			moieties	PUBTATOR		mER	13983		Structural characterization of the carbohydrate moieties on mER-beta, overexpressed in insect Sf9 cells, confirmed the presence of O-GlcNAc.
18676855	7	15	gly	glycoprotein	1275:1286	arg1	NGEP	NGEP				PUBTATOR		NGEP	Q6IWH7		NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	7	15	gly	glycoprotein	1275:1286	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	7	27	gly	glycosylation	1303:1315	arg2	predicted glycosylation sites			predicted glycosylation sites						sites	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	7	27	gly	glycosylation	1303:1315	arg2	N809			N809 and N824						N809 and N824	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
9572875	0	37	gly	factor	147:152	arg1	carbohydrate structure	factor			carbohydrate structure	Fterm		factor			Identification of O-glycosylation sites and partial characterization of carbohydrate structure and disulfide linkages of human insulin-like growth factor binding protein 6.
9572875	0	57	gly	O-glycosylation	18:32	arg2	O-glycosylation sites			O-glycosylation sites						sites	Identification of O-glycosylation sites and partial characterization of carbohydrate structure and disulfide linkages of human insulin-like growth factor binding protein 6.
19528533	3	60	part_of	region	688:693	arg1	a negatively charged residue	region		a negatively charged residue						residue	ZPI has an unusual shutter region with a negatively charged residue buried within the hydrophobic core of the molecule.
19528533	3	12	part_of	has	665:667	arg1	ZPI AND an unusual shutter region	ZPI		an unusual shutter region		PUBTATOR	Site	ZPI	51156	region	ZPI has an unusual shutter region with a negatively charged residue buried within the hydrophobic core of the molecule.
21053369	8	61	gly	glycosylation	1275:1287	arg2	Eight glycosylation sites			Eight glycosylation sites						sites	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	gly	identified	1300:1309	arg1	Asn250			Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6						Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	gly	identified	1300:1309	arg1	Asn209			Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6						Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	gly	identified	1300:1309	arg1	Asn6			Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6						Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	gly	identified	1300:1309	arg1	Asn157			Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6						Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	gly	identified	1300:1309	arg1	Asn209			Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6						Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	gly	identified	1300:1309	arg1	Asn6			Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6						Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	gly	identified	1300:1309	arg1	Asn157			Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6						Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	gly	identified	1300:1309	arg1	Asn6			Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6						Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	gly	identified	1300:1309	arg1	Asn157			Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6						Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	gly	identified	1300:1309	arg1	Asn157			Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6						Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
25802287	12	100	gly	glycopeptide	2002:2013	arg2	glycopeptide			glycopeptide						glycopeptide	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
7744025	5	38	gly	glycosylation	1107:1119	arg2	the preferred sites			the preferred sites						sites	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	38	gly	glycosylation	1107:1119	arg2	the threonine residues			the threonine residues						threonine residues Thr9	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
23302862	5	24	part_of	L1	1176:1177	arg1	the face	L1		the face		PUBTATOR	Site	L1	3897	face	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23999306	2	24	gly	sialylation	281:291	arg1	protein stability	protein stability				Fterm		protein			Complete sialylation of therapeutic immunoglobulins is essential for their anti-inflammatory activity and protein stability, but is difficult to achieve in vitro owing to the limited activity of ST6Gal-I towards some galactose acceptors.
24058541	9	31	gly	N-glycosylation	1293:1307	arg1	CLN5	CLN5		sites		PUBTATOR		CLN5	O75503	sites	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
14764083	0	50	gly	glycosylation	21:33	arg1	human and bovine lactoferrin	human and bovine lactoferrin				PUBTATOR		lactoferrin	280846		The role of N-linked glycosylation in the protection of human and bovine lactoferrin against tryptic proteolysis.
19805286	4	12	part_of	IX	595:596	arg1	the catalytic domain	CA IX		the catalytic domain		PUBTATOR	Site	CA IX	768	domain	Here we report the X-ray structure of the catalytic domain of CA IX in complex with a classical, clinically used sulfonamide inhibitor, acetazolamide.
1885588	0	72	part_of	glycoprotein	53:64	arg1	a luminal catalytic domain	glycoprotein		a luminal catalytic domain		Fterm	Site	glycoprotein		domain	Glucosidase I, a transmembrane endoplasmic reticular glycoprotein with a luminal catalytic domain.
9336835	5	19	gly	contains	874:881	arg1	the beta subunit AND 27-30% carbohydrate	the beta subunit			27-30% carbohydrate	OGER		subunit	1191		The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	5	90	gly	contains	825:832	arg1	the alpha subunit AND 0-30% carbohydrate	the alpha subunit			0-30% carbohydrate	OGER		subunit	1191		The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	5	51	gly	contains	767:774	arg1	clusterin AND 17-27% carbohydrate	clusterin			17-27% carbohydrate	PUBTATOR		clusterin	1191		The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
18702514	8	12	part_of	PLRP2	1676:1680	arg1	the active site	PLRP2		the active site		PUBTATOR	Site	PLRP2	117554	site	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
25458834	6	42	part_of	residues	781:788	arg1	CLEC-2	CLEC-2		residues		PUBTATOR	Site	CLEC-2	51266	residues	There is a common interaction mode between consecutive acidic residues on the ligands and the same arginine residues on CLEC-2.
25458834	6	51	part_of	residues	827:834	arg1	CLEC-2	CLEC-2		residues		PUBTATOR	AminoAcid	CLEC-2	51266	arginine residues	There is a common interaction mode between consecutive acidic residues on the ligands and the same arginine residues on CLEC-2.
12788922	4	26	part_of	C1s	500:502	arg1	the interaction domain	C1s		the interaction domain		PUBTATOR	Site	C1s	P09871	domain	The crystal structure of the interaction domain of C1s has been solved and refined to 1.5 A resolution.
16170054	5	85	gly	glycoproteins	930:942	arg1	murine epidermis glycoproteins	murine epidermis glycoproteins				Fterm		glycoproteins			A high abundance of high mannose type oligosaccharides was found to be characteristic of murine epidermis glycoproteins.
27966990	4	63	gly	N-glycosylation	554:568	arg1	VEGFR-2	VEGFR-2				PUBTATOR		VEGFR-2	P35968		However, despite its importance, the functional role of N-glycosylation of VEGFR-2 remains poorly understood.
10200178	7	65	gly	Asn-196	1297:1303	arg1	the glycans			Asn-180 and Asn-196	the glycans					Asn-180 and Asn-196	This performance coupled with stepwise exoglycosidase digestion has been employed to establish the differential nature of the structural complexity (glycoforms) of the glycans at Asn-180 and Asn-196 from a single strain infected with the ME7 strain.
10200178	7	76	gly	Asn-180	1285:1291	arg1	the glycans			Asn-180 and Asn-196	the glycans					Asn-180 and Asn-196	This performance coupled with stepwise exoglycosidase digestion has been employed to establish the differential nature of the structural complexity (glycoforms) of the glycans at Asn-180 and Asn-196 from a single strain infected with the ME7 strain.
15014436	3	40	part_of	TSP-1	373:377	arg1	a cell-binding TSP-1 fragment	TSP		a cell-binding TSP-1 fragment		PUBTATOR	Site	TSP	7057	fragment	The crystal structure of a cell-binding TSP-1 fragment, spanning three T3 repeats and the CTD, reveals a compact assembly.
25327667	5	52	gly	glycosylation	651:663	arg2	Asn69			Asn69						Asn69	PSA has a single glycosylation site at Asn69, with glycans constituting approximately 8% of the protein by weight.
25327667	5	52	gly	glycosylation	651:663	arg2	a single glycosylation site			a single glycosylation site						site	PSA has a single glycosylation site at Asn69, with glycans constituting approximately 8% of the protein by weight.
25374123	2	78	gly	glycoprotein	333:344	arg1	a multifunctional glycoprotein	a multifunctional glycoprotein				Fterm		glycoprotein			Vitronectin is well known to be a multifunctional glycoprotein in the blood and the extracellular matrix, which is related to hepatocellular carcinoma (HCC).
25374123	2	78	gly	glycoprotein	333:344	arg1	Vitronectin	Vitronectin				PUBTATOR		Vitronectin	7448		Vitronectin is well known to be a multifunctional glycoprotein in the blood and the extracellular matrix, which is related to hepatocellular carcinoma (HCC).
22387313	6	15	gly	Glycosylation	777:789	arg2	these specific residues			these specific residues						residues	Glycosylation at these specific residues was necessary for DPP10 trafficking to the plasma membrane as observed by flow cytometry.
2361960	5	1	gly	glycosylated	822:833	arg1	Thr-3			Thr-3 and Asn-28						Thr-3 and Asn-28	In addition, we concluded that Thr-3 and Asn-28 were glycosylated.
7460900	1	10	gly	glycopeptides	76:88	arg2	glycopeptides			glycopeptides						glycopeptides	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	1	13	gly	kappa-caseinoglycopeptides	315:340	arg2	cow and sheep kappa-caseinoglycopeptides			cow and sheep kappa-caseinoglycopeptides						kappa-caseinoglycopeptides	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	1	31	gly	caseinoglycopeptide	133:151	arg2	human caseinoglycopeptide			human caseinoglycopeptide						caseinoglycopeptide	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
23829323	9	57	gly	glycosylation	2048:2060	arg2	the four N-linked glycosylation sites			the four N-linked glycosylation sites						sites	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	9	67	gly	glycopeptide	1914:1925	arg2	136 N-linked glycopeptide spectra			136 N-linked glycopeptide spectra						glycopeptide	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	9	90	gly	glycopeptides	1995:2007	arg2	15 distinct glycopeptides			15 distinct glycopeptides						glycopeptides	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
6546754	8	15	part_of	convertase	1273:1282	arg1	the catalytic region	convertase		the catalytic region		Fterm	Site	convertase		region	It is suggested that these "altered" regions contribute at least in part to the formation of the catalytic region of the C3 convertase.
1517205	6	22	gly	glycopeptides	1287:1299	arg2	These glycopeptides			These glycopeptides						glycopeptides	These glycopeptides were both composed of 1 mol each of Gal, Fuc, GlcNAc, and NeuAc but did not contain Xyl and Glc.
1517205	6	1	gly	contain	1377:1383	arg1	These glycopeptides AND Xyl			These glycopeptides	Xyl					glycopeptides	These glycopeptides were both composed of 1 mol each of Gal, Fuc, GlcNAc, and NeuAc but did not contain Xyl and Glc.
1517205	6	1	gly	contain	1377:1383	arg1	These glycopeptides AND Glc			These glycopeptides	Glc					glycopeptides	These glycopeptides were both composed of 1 mol each of Gal, Fuc, GlcNAc, and NeuAc but did not contain Xyl and Glc.
30598546	3	22	part_of	PS1	413:415	arg1	three transmembrane domains	PS1		three transmembrane domains		PUBTATOR	Site	PS1	5663	domains	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	3	39	part_of	Notch	460:464	arg1	the Notch fragment	Notch		the Notch fragment		Cterm	Site	Notch		fragment	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
20622017	3	35	gly	glycoproteins	464:476	arg1	renal membrane glycoproteins	renal membrane glycoproteins				Fterm		glycoproteins			The spectrum of N-glycans released from kidney GGT constituted a subset of the N-glycans identified from renal membrane glycoproteins.
20622017	3	72	gly	released	370:377	arg2	kidney GGT AND N-glycans	kidney GGT			N-glycans	OGER		GGT			The spectrum of N-glycans released from kidney GGT constituted a subset of the N-glycans identified from renal membrane glycoproteins.
6619126	2	86	gly	glycoprotein	227:238	arg1	This glycoprotein	glycoprotein			a carbohydrate variant	Fterm		glycoprotein			This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	2	108	gly	glycoproteins	481:493	arg1	the MN glycoproteins	glycoproteins			all O-linked saccharides	Fterm		glycoproteins			This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
23242014	11	69	gly	O-glycosylated	1618:1631	arg1	Ser479			Ser479						Ser479	In addition, we could show that Ser479 within the hyper variable region (HVR) I is not O-glycosylated.
26828122	7	52	gly	glycosylation	1515:1527	arg2	multiple sites			multiple sites						sites	Results of this study showed, for the first time, that the hTPPT is glycosylated and that N-linked glycosylation occurs at multiple sites with some of them being important for function.
26828122	7	64	gly	glycosylated	1484:1495	arg1	the hTPPT	the hTPPT				PUBTATOR		hTPPT	80736		Results of this study showed, for the first time, that the hTPPT is glycosylated and that N-linked glycosylation occurs at multiple sites with some of them being important for function.
17563389	1	29	gly	glycosylation	252:264	arg2	Asn-18			sites, Asn-14 and Asn-18						sites, Asn-14 and Asn-18	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	29	gly	glycosylation	252:264	arg2	Asn-14			sites, Asn-14 and Asn-18						sites, Asn-14 and Asn-18	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	29	gly	glycosylation	252:264	arg2	Asn-14			sites, Asn-14 and Asn-18						sites, Asn-14 and Asn-18	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
22629392	7	19	gly	Akt	1390:1392	arg1	O-GlcNAcylations	Akt			O-GlcNAcylations	PUBTATOR		Akt	207		Together, this study revealed an extensive crosstalk between O-GlcNAcylations and phosphorylations of Akt and demonstrated O-GlcNAcylation as a new regulatory modification for Akt signaling.
20837471	6	0	part_of	Thr	1105:1107	arg1	ANGPTL3	ANGPTL3		Thr		PUBTATOR	SpecificSite	ANGPTL3	Q9Y5C1	Thr(226)	Screening of a panel of proteins known to affect lipid metabolism for potential sites glycosylated by GalNAc-T2 led to identification of Thr(226) adjacent to the proprotein convertase processing site in ANGPTL3.
21980294	1	61	gly	glycoprotein	125:136	arg1	herpes simplex virus (HSV) glycoprotein D	herpes simplex virus (HSV) glycoprotein D				PUBTATOR		glycoprotein D	2532		Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
16492764	1	8	part_of	receptor	259:266	arg1	a ligand binding region	GCSF receptor		a ligand binding region		PUBTATOR	Site	GCSF receptor	1441	region	A crystal structure of the signaling complex between human granulocyte colony-stimulating factor (GCSF) and a ligand binding region of GCSF receptor (GCSF-R), has been determined to 2.8 A resolution.
8407981	9	8	part_of	P-450	1332:1336	arg1	the N terminus	P-450(arom)		the N terminus		PUBTATOR	Site	P-450(arom)	55010	terminus	We conclude that the N terminus of P-450(arom) is translocated across the endoplasmic reticulum membrane to be glycosylated at the luminal side.
7947762	0	16	gly	C-glycosylation	58:72	arg1	human RNase Us	RNase		tryptophan residue		OGER		RNase	P07998	tryptophan residue	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.
1482348	3	8	gly	O-glycosylated	431:444	arg1	O-glycosylated oligosaccharide				O-glycosylated oligosaccharide						Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	3	28	gly	linked	462:467	arg1	Thr445 AND O-glycosylated oligosaccharide			Thr445	O-glycosylated oligosaccharide					Thr445	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
10201933	4	63	part_of	GPI-anchor	704:713	arg1	the GPI-anchor motif	GPI		the GPI-anchor motif		OGER	Site	GPI	P06744	motif	The 1998-base pairs of the open reading frame of the cloned cDNA encoded a protein of 666 amino acids (aa), including the 46 aa of the signal peptide and the 19 aa of the GPI-anchor motif.
17960739	9	55	gly	glycosylated	1248:1259	arg1	CD9P-1	CD9P-1				PUBTATOR		CD9P-1	5738		Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	9	55	gly	glycosylated	1248:1259	arg1	at least 17 glycosylated isoforms	at least 17 glycosylated isoforms				Fterm		isoforms			Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
30899004	5	25	part_of	glycosites	1065:1074	arg1	the same protein	protein		glycosites		Fterm	Site	protein		glycosites	Our data reveal that N-glycosylation profiles can differ between subcellular regions and structural domains and that N-glycosite heterogeneity manifests in several different forms, including dramatic differences in glycosites on the same protein.
9118998	6	14	gly	glycosylated	1204:1215	arg1	the glycosylated asparagine residues			the glycosylated asparagine residues						asparagine residues	Fucosylated biantennary complex-type and small amounts (less than 5%) of triantennary complex-type structures were identified on the glycosylated asparagine residues using sequential exoglycosidase and endoglycosidase digestions combined with matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS).
2243102	4	16	gly	glycoproteins	534:546	arg1	the glycoproteins	the glycoproteins				Fterm		glycoproteins			Polylactosaminoglycan-containing glycopeptides, obtained by trypsin, pepsin, and V8 protease digestion of the glycoproteins, were isolated by Datura stramonium agglutinin affinity chromatography, gel filtration, and reverse phase high performance liquid chromatography.
6327299	4	17	gly	contain	666:672	arg1	Glycocalicin AND 40% carbohydrate	Glycocalicin			40% carbohydrate	Fterm		Glycocalicin			Glycocalicin was found to contain 40% carbohydrate by weight, representing N- as well as O-glycosidically linked carbohydrate chains.
8436110	2	8	gly	sialylated	441:450	arg1	sialylated oligosaccharides				sialylated oligosaccharides						The structures of 82 neutral and low-molecular-mass sialylated oligosaccharides have been described previously [van Kuik A., de Waard P., Vliegenthart J. F. G., Klein A., Carnoy C., Lamblin G. Roussel P. (1991) Eur.
9030779	5	70	gly	glycosylation	669:681	arg2	the four N-terminal glycosylation sites			the four N-terminal glycosylation sites						sites	Elimination of the four N-terminal glycosylation sites does not disturb lysosomal targeting, processing, or enzymatic activity.
1421756	10	3	gly	contains	1577:1584	arg1	the s-TfR AND an O-linked oligosaccharide	the s-TfR			an O-linked oligosaccharide	PUBTATOR		TfR	7037		The s-TfR was sensitive to O-glycanase and bound to Jacalin lectin, indicating that the s-TfR contains an O-linked oligosaccharide.
1694784	0	12	gly	HC	91:92	arg1	the three carbohydrate prosthetic groups	protein HC			the three carbohydrate prosthetic groups	PUBTATOR		protein HC	259		Location and characterization of the three carbohydrate prosthetic groups of human protein HC.
15961631	2	3	gly	leucine-rich	271:282	arg1	23 leucine-rich repeats			leucine	23 leucine-rich repeats					leucine	The human TLR3 ectodomain structure at 2.1 angstroms reveals a large horseshoe-shaped solenoid assembled from 23 leucine-rich repeats (LRRs).
14711516	4	49	part_of	Thy-1	796:800	arg1	each N-glycosylation site	Thy-1		each N-glycosylation site		PUBTATOR	Site	Thy-1	P04216	site	The disulfide linkage pattern and glycoform distribution on each N-glycosylation site of recombinant chicken Thy-1 from both cell lines were determined by a combination of amino-terminal sequencing and mass spectrometry.
11320094	3	0	gly	glycosylation	664:676	arg2	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites			the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites						sites	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
9524075	11	66	gly	non-glycosylated	1245:1260	arg1	non-glycosylated procathepsin S	non-glycosylated procathepsin S				Cterm		non-glycosylated procathepsin S	1520		Subcellular fractionation showed non-glycosylated procathepsin S in the membrane fraction.
29992770	7	18	gly	N-glycopeptides	997:1011	arg2	Thirty-eight tryptic N-glycopeptides			Thirty-eight tryptic N-glycopeptides						N-glycopeptides	Thirty-eight tryptic N-glycopeptides are identified, having 19 unique N-glycosylation sites representing 14 glycoproteins.
29992770	7	28	gly	N-glycosylation	1046:1060	arg2	19 unique N-glycosylation sites			19 unique N-glycosylation sites						sites	Thirty-eight tryptic N-glycopeptides are identified, having 19 unique N-glycosylation sites representing 14 glycoproteins.
29992770	7	62	gly	glycoproteins	1084:1096	arg1	14 glycoproteins	14 glycoproteins				Fterm		glycoproteins			Thirty-eight tryptic N-glycopeptides are identified, having 19 unique N-glycosylation sites representing 14 glycoproteins.
12154198	1	14	part_of	HER3	175:178	arg1	the entire extracellular region	HER3		the entire extracellular region		PUBTATOR	Site	HER3	2065	region	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
20805301	5	69	part_of	CYP2W1	711:716	arg1	Asn177	CYP2W1		Asn177		PUBTATOR	AminoAcid	CYP2W1	54905	Asn177	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	69	part_of	CYP2W1	711:716	arg1	the only possible glycosylation site	CYP2W1		the only possible glycosylation site		PUBTATOR	Site	CYP2W1	54905	site	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
1569071	0	58	gly	O-glycosylated	22:35	arg1	O-glycosylated precursors	O-glycosylated precursors				Fterm		precursors			The identification of O-glycosylated precursors of insulin-like growth factor II.
2015821	5	43	gly	deglycosylation	980:994	arg1	the unfractionated alpha 1-antichymotrypsin	the unfractionated alpha 1-antichymotrypsin				PUBTATOR		alpha 1-antichymotrypsin	12		The N-glycanase was used for the deglycosylation of the unfractionated alpha 1-antichymotrypsin; the successive removal of the N-linked complex-type oligosaccharide side chains of alpha 1-antichymotrypsin was studied in the presence of detergents.
2015821	5	60	gly	1-antichymotrypsin	1133:1150	arg1	the N-linked complex-type oligosaccharide side chains	alpha 1-antichymotrypsin			the N-linked complex-type oligosaccharide side chains	PUBTATOR		alpha 1-antichymotrypsin	12		The N-glycanase was used for the deglycosylation of the unfractionated alpha 1-antichymotrypsin; the successive removal of the N-linked complex-type oligosaccharide side chains of alpha 1-antichymotrypsin was studied in the presence of detergents.
16754968	1	36	part_of	receptor	299:306	arg1	the extracellular domains	receptor		the extracellular domains		Fterm	Site	receptor		domains	X-ray diffraction has been used to produce and refine a model of the extracellular domains of the beta common cytokine receptor.
15702487	5	31	gly	glycopeptides	994:1006	arg2	glycopeptides			glycopeptides						glycopeptides	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	5	47	gly	glycopeptide	1042:1053	arg2	glycopeptide			glycopeptide						glycopeptide	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	5	73	gly	glycoproteins	922:934	arg1	either whole glycoproteins	either whole glycoproteins				Fterm		glycoproteins			In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
12847106	5	16	part_of	plakoglobin	658:668	arg1	the N-terminal domain	plakoglobin		the N-terminal domain		Fterm	Site	plakoglobin		domain	This destruction box is also found in the N-terminal domain of plakoglobin.
19671700	7	71	gly	TSR1	1247:1250	arg1	C-Mannosylation	TSR1			C-Mannosylation	PUBTATOR		TSR1	Q2NL82		C-Mannosylation of TSR1 of the related protease ADAMTS5 was also identified.
4319110	0	0	gly	glycopeptides	23:35	arg2	glycopeptides			glycopeptides						glycopeptides	A comparative study of glycopeptides derived from selected vertebrate collagens.
19119025	1	43	gly	glycoprotein	129:140	arg1	Tapasin	Tapasin				PUBTATOR		Tapasin	6892		Tapasin is a glycoprotein critical for loading major histocompatibility complex (MHC) class I molecules with high-affinity peptides.
19119025	1	43	gly	glycoprotein	129:140	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Tapasin is a glycoprotein critical for loading major histocompatibility complex (MHC) class I molecules with high-affinity peptides.
16894147	2	38	part_of	IR	419:420	arg1	the first three domains	IR		the first three domains		PUBTATOR	Site	IR	3643	domains	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	2	39	part_of	IGF1R	531:535	arg1	the corresponding fragment	IGF1R		the corresponding fragment		PUBTATOR	Site	IGF1R	3480	fragment	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
15532026	7	28	gly	glycosylation	1347:1359	arg2	a potential N-linked glycosylation site			a potential N-linked glycosylation site						site	By direct sequencing a novel homozygous mutation, c.347_349delACA (p.Asn116del), was identified affecting a potential N-linked glycosylation site.
12731887	0	35	gly	glycosylation	2:14	arg2	A glycosylation site	p67		site		PUBTATOR		p67	64370	site	A glycosylation site, 60SGTS63, of p67 is required for its ability to regulate the phosphorylation and activity of eukaryotic initiation factor 2alpha.
9722584	4	12	part_of	has	492:494	arg1	The protein AND a putative signal peptide	The protein		a putative signal peptide		Fterm	Site	protein		peptide	The protein has a putative signal peptide of 21 amino acids, and is a proform of two polypeptides.
19196183	0	70	part_of	sites	34:38	arg1	secreted proteins	proteins		sites		Fterm	Site	proteins		sites	Identification of N-glycosylation sites on secreted proteins of human hepatocellular carcinoma cells with a complementary proteomics approach.
1517205	2	62	part_of	EGF-like	479:486	arg1	the first EGF-like domain	EGF		the first EGF-like domain		OGER	Site	EGF	P01133	domain	We now have evidence of another modification in the first EGF-like domain of human factor IX, which proved to be a tetrasaccharide O-fucosidically linked to Ser-61.
1517205	2	77	part_of	IX	511:512	arg1	the first EGF-like domain	factor IX		the first EGF-like domain		OGER	Site	factor IX	P00740	domain	We now have evidence of another modification in the first EGF-like domain of human factor IX, which proved to be a tetrasaccharide O-fucosidically linked to Ser-61.
28775322	3	46	part_of	EGF-like	497:504	arg1	several EGF-like domains	EGF		several EGF-like domains		OGER	Site	EGF	P01133	domains	Using several EGF-like domains and donor substrate analogs, we have determined the structures of human Protein O-glucosyltransferase 1 substrate/product complexes that provide mechanistic insight into the basis for these properties.
24365146	5	11	gly	glycosylation	772:784	arg1	Nox1	Nox1				PUBTATOR		Nox1	27035		These findings indicate that glycosylation and subsequent N-glycan maturation of Nox1 are both dispensable for its cell surface recruitment.
24365146	5	14	gly	Nox1	824:827	arg1	subsequent N-glycan maturation	Nox1			subsequent N-glycan maturation	PUBTATOR		Nox1	27035		These findings indicate that glycosylation and subsequent N-glycan maturation of Nox1 are both dispensable for its cell surface recruitment.
18467335	9	27	gly	N-glycosylated	997:1010	arg2	Asn-243	PCI		sites, Asn-230, Asn-243, and Asn-319		OGER		PCI	P05154	sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	27	gly	N-glycosylated	997:1010	arg2	Asn-230	PCI		sites, Asn-230, Asn-243, and Asn-319		OGER		PCI	P05154	sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	27	gly	N-glycosylated	997:1010	arg2	Asn-319	PCI		sites, Asn-230, Asn-243, and Asn-319		OGER		PCI	P05154	sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	27	gly	N-glycosylated	997:1010	arg2	all three potential N-glycosylation sites	PCI		sites, Asn-230, Asn-243, and Asn-319		OGER		PCI	P05154	sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	27	gly	N-glycosylated	997:1010	arg2	Asn-230			sites, Asn-230, Asn-243, and Asn-319						sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	27	gly	N-glycosylated	997:1010	arg2	Asn-319			sites, Asn-230, Asn-243, and Asn-319						sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	27	gly	N-glycosylated	997:1010	arg2	all three potential N-glycosylation sites			sites, Asn-230, Asn-243, and Asn-319						sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	27	gly	N-glycosylated	997:1010	arg2	Asn-319			sites, Asn-230, Asn-243, and Asn-319						sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	27	gly	N-glycosylated	997:1010	arg2	all three potential N-glycosylation sites			sites, Asn-230, Asn-243, and Asn-319						sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	27	gly	N-glycosylated	997:1010	arg2	all three potential N-glycosylation sites			sites, Asn-230, Asn-243, and Asn-319						sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	83	gly	N-glycosylation	1035:1049	arg2	Asn-230			sites, Asn-230, Asn-243, and Asn-319						sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	83	gly	N-glycosylation	1035:1049	arg2	Asn-319			sites, Asn-230, Asn-243, and Asn-319						sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	83	gly	N-glycosylation	1035:1049	arg2	all three potential N-glycosylation sites			sites, Asn-230, Asn-243, and Asn-319						sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	83	gly	N-glycosylation	1035:1049	arg2	Asn-319			sites, Asn-230, Asn-243, and Asn-319						sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	83	gly	N-glycosylation	1035:1049	arg2	all three potential N-glycosylation sites			sites, Asn-230, Asn-243, and Asn-319						sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
18467335	9	83	gly	N-glycosylation	1035:1049	arg2	all three potential N-glycosylation sites			sites, Asn-230, Asn-243, and Asn-319						sites, Asn-230, Asn-243, and Asn-319	PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243.
24509848	6	32	gly	N-glycosylation	899:913	arg2	other N-glycosylation sites			other N-glycosylation sites						sites	Using site-directed mutagenesis, we found that mutations that disrupt the conserved (211)NDS N-glycosylation motif, but not other N-glycosylation sites (Asn(260), Asn(371), and Asn(394)), result in collagen I-independent constitutive phosphorylation.
24509848	6	64	gly	sites	915:919	arg1	other N-glycosylation sites			other N-glycosylation sites						sites	Using site-directed mutagenesis, we found that mutations that disrupt the conserved (211)NDS N-glycosylation motif, but not other N-glycosylation sites (Asn(260), Asn(371), and Asn(394)), result in collagen I-independent constitutive phosphorylation.
24509848	6	82	gly	N-glycosylation	862:876	arg2	the conserved (211)NDS N-glycosylation motif			the conserved (211)NDS N-glycosylation motif						motif	Using site-directed mutagenesis, we found that mutations that disrupt the conserved (211)NDS N-glycosylation motif, but not other N-glycosylation sites (Asn(260), Asn(371), and Asn(394)), result in collagen I-independent constitutive phosphorylation.
24509848	6	32	gly	N-glycosylation	899:913	arg2	Asn(371)			Asn(260), Asn(371), and Asn(394)						Asn(260), Asn(371), and Asn(394)	Using site-directed mutagenesis, we found that mutations that disrupt the conserved (211)NDS N-glycosylation motif, but not other N-glycosylation sites (Asn(260), Asn(371), and Asn(394)), result in collagen I-independent constitutive phosphorylation.
24509848	6	32	gly	N-glycosylation	899:913	arg2	Asn(394)			Asn(260), Asn(371), and Asn(394)						Asn(260), Asn(371), and Asn(394)	Using site-directed mutagenesis, we found that mutations that disrupt the conserved (211)NDS N-glycosylation motif, but not other N-glycosylation sites (Asn(260), Asn(371), and Asn(394)), result in collagen I-independent constitutive phosphorylation.
24509848	6	32	gly	N-glycosylation	899:913	arg2	Asn(394)			Asn(260), Asn(371), and Asn(394)						Asn(260), Asn(371), and Asn(394)	Using site-directed mutagenesis, we found that mutations that disrupt the conserved (211)NDS N-glycosylation motif, but not other N-glycosylation sites (Asn(260), Asn(371), and Asn(394)), result in collagen I-independent constitutive phosphorylation.
24509848	6	64	gly	sites	915:919	arg1	Asn(371)			Asn(260), Asn(371), and Asn(394)						Asn(260), Asn(371), and Asn(394)	Using site-directed mutagenesis, we found that mutations that disrupt the conserved (211)NDS N-glycosylation motif, but not other N-glycosylation sites (Asn(260), Asn(371), and Asn(394)), result in collagen I-independent constitutive phosphorylation.
24509848	6	64	gly	sites	915:919	arg1	Asn(260)			Asn(260), Asn(371), and Asn(394)						Asn(260), Asn(371), and Asn(394)	Using site-directed mutagenesis, we found that mutations that disrupt the conserved (211)NDS N-glycosylation motif, but not other N-glycosylation sites (Asn(260), Asn(371), and Asn(394)), result in collagen I-independent constitutive phosphorylation.
24509848	6	64	gly	sites	915:919	arg1	Asn(260)			Asn(260), Asn(371), and Asn(394)						Asn(260), Asn(371), and Asn(394)	Using site-directed mutagenesis, we found that mutations that disrupt the conserved (211)NDS N-glycosylation motif, but not other N-glycosylation sites (Asn(260), Asn(371), and Asn(394)), result in collagen I-independent constitutive phosphorylation.
10814696	7	18	gly	possesses	1476:1484	arg1	human placental arylsulfatase A AND only high-mannose-type oligosaccharides	human placental arylsulfatase A			only high-mannose-type oligosaccharides	PUBTATOR		arylsulfatase A	410		The results indicated that human placental arylsulfatase A possesses only high-mannose-type oligosaccharides, of which almost half are core fucosylated.
19951703	10	69	gly	deglycosylated	1375:1388	arg1	deglycosylated UGT1A9 proteins	deglycosylated UGT1A9 proteins				PUBTATOR		UGT1A9 proteins	54600		The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins supported the findings.
18420026	6	20	gly	glycoprotein	1539:1550	arg1	an N-linked glycoprotein	an N-linked glycoprotein				Fterm		glycoprotein			Based on the results of N-Glycosidase F treatment with human fetal brain tissue and lysates from transient transfection with human wild-type or glycosylation site mutant NECL1 in 293ET cells, we demonstrated that human NECL1 is an N-linked glycoprotein with a single glycosylation site at position N290KS.
18420026	6	20	gly	glycoprotein	1539:1550	arg1	human NECL1	human NECL1				PUBTATOR		NECL1	57863		Based on the results of N-Glycosidase F treatment with human fetal brain tissue and lysates from transient transfection with human wild-type or glycosylation site mutant NECL1 in 293ET cells, we demonstrated that human NECL1 is an N-linked glycoprotein with a single glycosylation site at position N290KS.
18420026	6	43	gly	glycosylation	1443:1455	arg2	glycosylation site mutant			glycosylation site mutant						site	Based on the results of N-Glycosidase F treatment with human fetal brain tissue and lysates from transient transfection with human wild-type or glycosylation site mutant NECL1 in 293ET cells, we demonstrated that human NECL1 is an N-linked glycoprotein with a single glycosylation site at position N290KS.
18420026	6	104	gly	glycosylation	1566:1578	arg2	position			position						position	Based on the results of N-Glycosidase F treatment with human fetal brain tissue and lysates from transient transfection with human wild-type or glycosylation site mutant NECL1 in 293ET cells, we demonstrated that human NECL1 is an N-linked glycoprotein with a single glycosylation site at position N290KS.
18420026	6	104	gly	glycosylation	1566:1578	arg2	a single glycosylation site			a single glycosylation site						site	Based on the results of N-Glycosidase F treatment with human fetal brain tissue and lysates from transient transfection with human wild-type or glycosylation site mutant NECL1 in 293ET cells, we demonstrated that human NECL1 is an N-linked glycoprotein with a single glycosylation site at position N290KS.
18514042	3	15	gly	glycopeptide	419:430	arg2	glycopeptide			glycopeptide						glycopeptide	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	3	41	gly	glycopeptides	626:638	arg2	characterized glycopeptides			glycopeptides	glycan units					glycopeptides	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
7994575	0	15	part_of	CD2	82:84	arg1	the extracellular region	CD2		the extracellular region		PUBTATOR	Site	CD2	914	region	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
21569239	6	32	part_of	mindin	838:843	arg1	the FS domains	mindin		the FS domains		PUBTATOR	Site	mindin	10417	domains	Though the primary sequences of the FS domains of F-spondin and mindin are less than 36% identical, their overall structures are very similar.
21569239	6	38	part_of	F-spondin	824:832	arg1	the FS domains	F-spondin		the FS domains		PUBTATOR	Site	F-spondin	10418	domains	Though the primary sequences of the FS domains of F-spondin and mindin are less than 36% identical, their overall structures are very similar.
9822688	12	52	part_of	contains	1753:1760	arg1	a PLRP2 lipase AND a lid domain	a PLRP2 lipase		a lid domain		PUBTATOR	Site	PLRP2 lipase	117554	domain	In summary, we confirmed and extended the observation that PLRP2 lipases have a broader substrate specificity than PTL, we demonstrated that PLRP2 lipases show interfacial activation, and we solved the first crystal structure of a PLRP2 lipase that contains a lid domain.
22678432	0	56	gly	glycoproteins	55:67	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Determination of site-specific glycan heterogeneity on glycoproteins.
8344280	11	16	gly	N-glycosylation	1742:1756	arg2	its only N-glycosylation site			its only N-glycosylation site						site	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	11	59	gly	fucosylated	1801:1811	arg1	truncated proximally fucosylated oligomannosidic glycans				truncated proximally fucosylated oligomannosidic glycans						An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
1820200	1	1	gly	glycoprotein	231:242	arg1	the heterodimeric glycoprotein hormone	the heterodimeric glycoprotein hormone				PUBTATOR		glycoprotein hormone human chorionic gonadotrophin (hCG)	93659		Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	18	gly	N-glycosylated	378:391	arg2	Asn-30	hCG beta		Asn-13 and Asn-30		PUBTATOR		hCG beta	1082	Asn-13 and Asn-30	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	18	gly	N-glycosylated	378:391	arg2	Asn-13	hCG beta		Asn-13 and Asn-30		PUBTATOR		hCG beta	1082	Asn-13 and Asn-30	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	18	gly	N-glycosylated	378:391	arg2	Asn-13			Asn-13 and Asn-30						Asn-13 and Asn-30	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	18	gly	N-glycosylated	378:391	arg1	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	subunits hCG alpha		Asn-13 and Asn-30		OGER		subunits hCG alpha	P01215	Asn-13 and Asn-30	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	18	gly	N-glycosylated	378:391	arg1	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	subunits hCG alpha		Asn-13 and Asn-30		OGER		subunits hCG alpha	P01215	Asn-13 and Asn-30	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	39	gly	N-glycosylated	327:340	arg2	Asn-78	subunits hCG alpha		Asn-52 and Asn-78		OGER		subunits hCG alpha	P01215	Asn-52 and Asn-78	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	39	gly	N-glycosylated	327:340	arg1	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	subunits hCG alpha				OGER		subunits hCG alpha	P01215		Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	39	gly	N-glycosylated	327:340	arg2	Asn-52	subunits hCG alpha		Asn-52 and Asn-78		OGER		subunits hCG alpha	P01215	Asn-52 and Asn-78	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	39	gly	N-glycosylated	327:340	arg1	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	subunits hCG alpha		Asn-52 and Asn-78		OGER		subunits hCG alpha	P01215	Asn-52 and Asn-78	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	39	gly	N-glycosylated	327:340	arg2	Asn-52			Asn-52 and Asn-78						Asn-52 and Asn-78	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	39	gly	N-glycosylated	327:340	arg2	Asn-52	subunits hCG alpha		Asn-52 and Asn-78		OGER		subunits hCG alpha	P01215	Asn-52 and Asn-78	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	42	gly	N-glycosylation	188:202	arg2	individual N-glycosylation sites	glycoprotein hormone human chorionic gonadotrophin (hCG)		sites		PUBTATOR		glycoprotein hormone human chorionic gonadotrophin (hCG)	93659	sites	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	42	gly	N-glycosylation	188:202	arg1	hCG	glycoprotein hormone human chorionic gonadotrophin (hCG)				PUBTATOR		glycoprotein hormone human chorionic gonadotrophin (hCG)	93659		Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	42	gly	N-glycosylation	188:202	arg1	hCG	glycoprotein hormone human chorionic gonadotrophin (hCG)		sites		PUBTATOR		glycoprotein hormone human chorionic gonadotrophin (hCG)	93659	sites	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
9786864	6	3	part_of	receptor	912:919	arg1	The determined disulfide motif	leptin receptor		The determined disulfide motif		PUBTATOR	Site	leptin receptor	3953	motif	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	6	44	part_of	contained	921:929	arg1	The determined disulfide motif AND 10 free cysteines	The determined disulfide motif		10 free cysteines						cysteines	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9169007	11	11	gly	antithrombin	2012:2023	arg1	all carbohydrate chains	antithrombin			all carbohydrate chains	PUBTATOR		antithrombin	462		These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin.
21264968	0	114	part_of	mucin	139:143	arg1	synthetic mucin peptides	mucin		synthetic mucin peptides		PUBTATOR	Site	mucin	100508689	peptides	An efficient approach for the characterization of mucin-type glycopeptides: the effect of O-glycosylation on the conformation of synthetic mucin peptides.
21264968	0	120	part_of	mucin-type	50:59	arg1	mucin-type glycopeptides	mucin		mucin-type glycopeptides		PUBTATOR	Site	mucin	100508689	glycopeptides	An efficient approach for the characterization of mucin-type glycopeptides: the effect of O-glycosylation on the conformation of synthetic mucin peptides.
8407981	4	34	gly	glycosylated	500:511	arg1	The P-450(arom) protein	The P-450(arom) protein				PUBTATOR		P-450(arom) protein	55010		The P-450(arom) protein expressed in the insect cells was glycosylated, and the sugar chain was sensitive to Endo H.
1150658	0	34	part_of	gonadotropin	43:54	arg1	The amino acid sequence	chorionic gonadotropin		The amino acid sequence		OGER	Site	chorionic gonadotropin		sequence	The amino acid sequence of human chorionic gonadotropin.
10358049	5	52	gly	N-glycosylation	783:797	arg2	Four N-glycosylation sites			Four N-glycosylation sites						sites	Four N-glycosylation sites were identified on the electron density maps.
14658030	5	22	gly	glycopeptides	1205:1217	arg2	glycopeptides			glycopeptides						peptides and glycopeptides	Unmodified peptides and glycopeptides each carrying a single glycosylation site were generated from NCAM by AspN and trypsin treatment and submitted to reversed-phase HPLC with or without prior enzymatic release of N-glycans.
14658030	5	56	gly	glycosylation	1242:1254	arg2	a single glycosylation site			a single glycosylation site						site	Unmodified peptides and glycopeptides each carrying a single glycosylation site were generated from NCAM by AspN and trypsin treatment and submitted to reversed-phase HPLC with or without prior enzymatic release of N-glycans.
9169007	0	100	gly	antithrombin	56:67	arg1	individual carbohydrate chains	antithrombin			individual carbohydrate chains	PUBTATOR		antithrombin	462		Effect of individual carbohydrate chains of recombinant antithrombin on heparin affinity and on the generation of glycoforms differing in heparin affinity.
19413349	9	41	gly	glycosylated	1646:1657	arg1	heterologously expressed rat melanopsin	heterologously expressed rat melanopsin				PUBTATOR		melanopsin	192223		In conclusion, we have shown that heterologously expressed rat melanopsin is both N-linked and O-linked glycosylated and that N-linked glycosylation is not crucial for the melanopsin response to light.
16750161	0	9	gly	glycoprotein	59:70	arg1	an O-linked glycoprotein	an O-linked glycoprotein				Fterm		glycoprotein			The precursor to B-type natriuretic peptide is an O-linked glycoprotein.
16750161	0	9	gly	glycoprotein	59:70	arg1	The precursor	The precursor				Fterm		precursor			The precursor to B-type natriuretic peptide is an O-linked glycoprotein.
25458834	5	48	part_of	CLEC-2	711:716	arg1	the noncanonical "side" face	CLEC-2		the noncanonical "side" face		PUBTATOR	Site	CLEC-2	51266	face	Both podoplanin and rhodocytin bind to the noncanonical "side" face of CLEC-2.
1374031	0	45	gly	subunit	36:42	arg1	The carbohydrate chains	subunit			The carbohydrate chains	OGER		subunit	P0DN86		The carbohydrate chains of the beta subunit of human chorionic gonadotropin produced by the choriocarcinoma cell line BeWo.
9884403	0	8	part_of	sites	14:18	arg1	human Tamm-Horsfall glycoprotein	Tamm-Horsfall glycoprotein		sites		OGER	Site	Tamm-Horsfall glycoprotein	P07911	sites	Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein.
22908259	5	16	part_of	Fab	698:700	arg1	the Fab fragment	Fab		the Fab fragment		PUBTATOR	Site	Fab	2187	fragment	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1, reveals that this antibody inhibits glucagon receptor by occluding a surface extending across the entire hormone-binding cleft.
22041449	7	8	part_of	Ca	1285:1286	arg1	a Ca(2+) binding site	Ca(2		a Ca(2+) binding site		OGER	Site	Ca(2	P00918	site	The structure reveals an overall architecture similar to that of laminin α chain LN domains but includes significant differences including a Ca(2+) binding site in the LN domain.
12063277	3	65	part_of	HERG	330:333	arg1	HERG protein sequence	HERG protein		HERG protein sequence		PUBTATOR	Site	HERG protein	3757	sequence	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
12063277	3	69	part_of	protein	335:341	arg1	HERG protein sequence	HERG protein		HERG protein sequence		PUBTATOR	Site	HERG protein	3757	sequence	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
12063277	3	44	part_of	contains	352:359	arg1	HERG protein sequence AND two extracellular consensus sites	HERG protein sequence		two extracellular consensus sites						sites	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
3497398	0	54	part_of	Willebrand	31:40	arg1	the von Willebrand factor-binding domain	von Willebrand factor		the von Willebrand factor-binding domain		OGER	Site	von Willebrand factor	P04275	domain	Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib.
3497398	0	80	part_of	Ib	98:99	arg1	the von Willebrand factor-binding domain	Ib		the von Willebrand factor-binding domain		Cterm	Site	Ib		domain	Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib.
3497398	0	90	part_of	von	27:29	arg1	the von Willebrand factor-binding domain	von Willebrand factor		the von Willebrand factor-binding domain		OGER	Site	von Willebrand factor	P04275	domain	Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib.
3497398	0	93	part_of	factor-binding	42:55	arg1	the von Willebrand factor-binding domain	von Willebrand factor		the von Willebrand factor-binding domain		OGER	Site	von Willebrand factor	P04275	domain	Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib.
1900431	6	20	gly	residue	824:830	arg1	Fucosylation			residue in	Fucosylation					residue in	Fucosylation of the homologous residue in prourokinase has also been reported recently.
1900431	6	54	gly	Fucosylation	793:804	arg1	prourokinase	prourokinase		residue in	Fucosylation	Fterm		prourokinase		residue in	Fucosylation of the homologous residue in prourokinase has also been reported recently.
7538124	9	37	part_of	K18	1489:1491	arg1	K18 glycosylation sites	K18		K18 glycosylation sites		PUBTATOR	Site	K18	3875	sites	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	9	48	part_of	proteins	1659:1666	arg1	glycosylation sites	proteins		glycosylation sites		Fterm	Site	proteins		sites	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
19656770	5	3	gly	glycosylation	1141:1153	arg2	235 N-linked glycosylation sites			235 N-linked glycosylation sites						sites	The data set revealed 36 cluster of differentiation-annotated proteins and confirmed the occupancy for 235 N-linked glycosylation sites.
7599134	0	35	part_of	antithrombin	25:36	arg1	antithrombin III asparagine-135	antithrombin III		antithrombin III asparagine-135		PUBTATOR	SpecificSite	antithrombin III	462	asparagine-135	Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity.
12859190	0	34	part_of	form	46:49	arg1	The WSAWS motif	form of the erythropoietin receptor		The WSAWS motif		PUBTATOR	Site	form of the erythropoietin receptor	2057	motif	The WSAWS motif is C-hexosylated in a soluble form of the erythropoietin receptor.
16964247	2	19	part_of	p53	294:296	arg1	Ser 149	p53		Ser 149		PUBTATOR	SpecificSite	p53	7157	Ser 149	Here, we show that Ser 149 of p53 is O-GlcNAcylated and that this modification is associated with decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination.
3497198	5	32	part_of	H-2Kb	769:773	arg1	Asn86	H-2Kb		Asn86		PUBTATOR	AminoAcid	H-2Kb	14972	Asn86	However, Asn86 of H-2Kb contained a higher ratio (5 to 1), while Asn86 of H-2Kk a lower ratio (1.5 to 1).
3497198	5	40	part_of	H-2Kk	825:829	arg1	Asn86	H-2Kk a		Asn86		PUBTATOR	AminoAcid	H-2Kk a	14972	Asn86	However, Asn86 of H-2Kb contained a higher ratio (5 to 1), while Asn86 of H-2Kk a lower ratio (1.5 to 1).
2528451	6	60	part_of	P40	1023:1025	arg1	the amino acid sequence	P40		the amino acid sequence		PUBTATOR	Site	P40	16198	sequence	No similarity was revealed when the amino acid sequence of P40 was compared with other proteins whose biochemical structure is known.
12391027	1	8	gly	metalloproteinases	297:314	arg1	glycosaminoglycan binding	metalloproteinases			glycosaminoglycan binding	Fterm		metalloproteinases			Thrombospondin-1 (TSP-1) contains three type 1 repeats (TSRs), which mediate cell attachment, glycosaminoglycan binding, inhibition of angiogenesis, activation of TGFbeta, and inhibition of matrix metalloproteinases.
12391027	1	35	gly	TGFbeta	263:269	arg1	glycosaminoglycan binding	TGFbeta			glycosaminoglycan binding	PUBTATOR		TGFbeta	7040		Thrombospondin-1 (TSP-1) contains three type 1 repeats (TSRs), which mediate cell attachment, glycosaminoglycan binding, inhibition of angiogenesis, activation of TGFbeta, and inhibition of matrix metalloproteinases.
12391027	1	14	gly	contains	125:132	arg1	Thrombospondin-1 AND three type 1 repeats	Thrombospondin-1			three type 1 repeats	PUBTATOR		Thrombospondin-1	7057		Thrombospondin-1 (TSP-1) contains three type 1 repeats (TSRs), which mediate cell attachment, glycosaminoglycan binding, inhibition of angiogenesis, activation of TGFbeta, and inhibition of matrix metalloproteinases.
12391027	1	14	gly	contains	125:132	arg1	TSP-1 AND three type 1 repeats	TSP-1			three type 1 repeats	PUBTATOR		TSP-1	7057		Thrombospondin-1 (TSP-1) contains three type 1 repeats (TSRs), which mediate cell attachment, glycosaminoglycan binding, inhibition of angiogenesis, activation of TGFbeta, and inhibition of matrix metalloproteinases.
25765764	4	9	part_of	LRIG1-LRR	574:582	arg1	The LRIG1-LRR domain	LRIG1		The LRIG1-LRR domain		PUBTATOR	Site	LRIG1	26018	domain	The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric.
25765764	4	9	part_of	LRIG1-LRR	574:582	arg1	the LRIG1-LRR-1Ig fragment	LRIG1		the LRIG1-LRR-1Ig fragment		PUBTATOR	Site	LRIG1	26018	fragment	The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric.
25765764	4	19	part_of	LRIG1-3Ig	660:668	arg1	the LRIG1-3Ig domain	LRIG1		the LRIG1-3Ig domain		PUBTATOR	Site	LRIG1	26018	domain	The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric.
25765764	4	45	part_of	LRIG1-LRR-1Ig	599:611	arg1	The LRIG1-LRR domain	LRIG1		The LRIG1-LRR domain		PUBTATOR	Site	LRIG1	26018	domain	The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric.
25765764	4	45	part_of	LRIG1-LRR-1Ig	599:611	arg1	the LRIG1-LRR-1Ig fragment	LRIG1		the LRIG1-LRR-1Ig fragment		PUBTATOR	Site	LRIG1	26018	fragment	The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric.
24548619	2	29	part_of	domain	265:270	arg1	some membrane-type (MT)-MMPs	membrane-type (MT)-MMPs		domain		PUBTATOR	Site	membrane-type (MT)-MMPs	4323	domain	Sequence comparison suggests that a C-terminal extension (CTE) includes a potential transmembrane domain as in some membrane-type (MT)-MMPs.
1544894	2	40	part_of	EGF	461:463	arg1	two EGF domains	EGF		two EGF domains		OGER	Site	EGF	P01133	domains	Factor XII and protein C each contain two EGF domains; in both proteins, the EGF domain nearest the N terminus has a threonine residue in a position homologous to that which is fucosylated in t-PA.
1544894	2	57	part_of	EGF	496:498	arg1	the EGF domain	EGF		the EGF domain		OGER	Site	EGF	P01133	domain	Factor XII and protein C each contain two EGF domains; in both proteins, the EGF domain nearest the N terminus has a threonine residue in a position homologous to that which is fucosylated in t-PA.
1544894	2	49	part_of	contain	449:455	arg1	Factor XII AND two EGF domains	Factor XII		two EGF domains		OGER	Site	Factor XII	P00748	domains	Factor XII and protein C each contain two EGF domains; in both proteins, the EGF domain nearest the N terminus has a threonine residue in a position homologous to that which is fucosylated in t-PA.
1544894	2	49	part_of	contain	449:455	arg1	protein C AND two EGF domains	protein C		two EGF domains		OGER	Site	protein C	P02810	domains	Factor XII and protein C each contain two EGF domains; in both proteins, the EGF domain nearest the N terminus has a threonine residue in a position homologous to that which is fucosylated in t-PA.
20450227	4	86	gly	glycosylated	703:714	arg1	the receptor	the receptor				Fterm		receptor			However, little is known about the biochemistry of P2X(7), including whether the receptor is N-linked glycosylated and if this modification affects receptor function.
15477100	0	64	gly	Zn-alpha2-glycoprotein	46:67	arg1	Zn-alpha2-glycoprotein	Zn-alpha2-glycoprotein				PUBTATOR		Zn-alpha2-glycoprotein	563		Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein.
9535843	6	71	gly	glycosylation	913:925	arg2	a unique glycosylation site			a unique glycosylation site						site	We also demonstrate presence of a unique glycosylation site in position 418, which defines one extracellular loop between H2 and H3.
17591618	7	51	gly	disialylated	1206:1217	arg1	complex, diantennary disialylated, non-fucosylated glycans				complex, diantennary disialylated, non-fucosylated glycans						Quantitative analysis showed that CFH is mainly glycosylated by complex, diantennary disialylated, non-fucosylated glycans.
17591618	7	76	gly	glycosylated	1169:1180	arg1	CFH	CFH				PUBTATOR		CFH	P08603		Quantitative analysis showed that CFH is mainly glycosylated by complex, diantennary disialylated, non-fucosylated glycans.
19683538	3	2	gly	glycoproteins	605:617	arg1	wild-type and glycosylation-deficient glycoproteins	wild-type and glycosylation-deficient glycoproteins				Fterm		glycoproteins			To better understand the molecular defects in the diseases, we determined the crystal structure of human alpha-NAGAL after expressing wild-type and glycosylation-deficient glycoproteins in recombinant insect cell expression systems.
14718370	2	33	part_of	subdomains	233:242	arg1	MUC5B	MUC5B		subdomains		PUBTATOR	AminoAcid	MUC5B	Q9HC84	Cys1 and Cys5 and Cys1 and Cys3 subdomains	The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium.
14718370	2	33	part_of	subdomains	233:242	arg1	MUC5AC	MUC5AC		subdomains		PUBTATOR	AminoAcid	MUC5AC	P98088	Cys1 and Cys5 and Cys1 and Cys3 subdomains	The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium.
14718370	2	75	part_of	Cys1	201:204	arg1	MUC5B	MUC5B		Cys1		PUBTATOR	AminoAcid	MUC5B	Q9HC84	Cys1 and Cys5 and Cys1 and Cys3 subdomains	The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium.
14718370	2	75	part_of	Cys1	201:204	arg1	MUC5AC	MUC5AC		Cys1		PUBTATOR	AminoAcid	MUC5AC	P98088	Cys1 and Cys5 and Cys1 and Cys3 subdomains	The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium.
14718370	2	80	part_of	Cys5	210:213	arg1	MUC5B	MUC5B		Cys5		PUBTATOR	AminoAcid	MUC5B	Q9HC84	Cys1 and Cys5 and Cys1 and Cys3 subdomains	The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium.
14718370	2	80	part_of	Cys5	210:213	arg1	MUC5AC	MUC5AC		Cys5		PUBTATOR	AminoAcid	MUC5AC	P98088	Cys1 and Cys5 and Cys1 and Cys3 subdomains	The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium.
14718370	2	84	part_of	Cys1	219:222	arg1	MUC5B	MUC5B		Cys1		PUBTATOR	AminoAcid	MUC5B	Q9HC84	Cys1 and Cys5 and Cys1 and Cys3 subdomains	The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium.
14718370	2	84	part_of	Cys1	219:222	arg1	MUC5AC	MUC5AC		Cys1		PUBTATOR	AminoAcid	MUC5AC	P98088	Cys1 and Cys5 and Cys1 and Cys3 subdomains	The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium.
8323299	4	18	gly	glycosylated	663:674	arg1	Ser-169			Ser-169						Ser-169	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Thr-171			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-179			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Thr-172			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-171			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-181			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	lamp-1	In lamp-1		Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183		PUBTATOR		In lamp-1	3916	Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-179			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-172			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-179			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Thr-172			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-171			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-181			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	lamp-1	In lamp-1		Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183		PUBTATOR		In lamp-1	3916	Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-179			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-172			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Thr-172			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-171			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-181			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	lamp-1	In lamp-1		Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183		PUBTATOR		In lamp-1	3916	Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-179			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-172			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-171			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-181			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	lamp-1	In lamp-1		Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183		PUBTATOR		In lamp-1	3916	Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-179			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-172			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-171			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-181			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	lamp-1	In lamp-1		Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183		PUBTATOR		In lamp-1	3916	Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-179			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-172			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-181			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	lamp-1	In lamp-1		Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183		PUBTATOR		In lamp-1	3916	Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-179			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-172			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	lamp-1	In lamp-1		Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183		PUBTATOR		In lamp-1	3916	Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-179			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-172			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-179	In lamp-1		Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183		PUBTATOR		In lamp-1	3916	Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-172	In lamp-1		Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183		PUBTATOR		In lamp-1	3916	Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-183	In lamp-1		Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183		PUBTATOR		In lamp-1	3916	Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-172			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-183			Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183						Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
16834341	4	5	gly	glycosylation	619:631	arg2	each glycosylation site			each glycosylation site						site	The characteristic pattern of glycan distribution at each glycosylation site has been deduced and compared between horse and human FSH preparations.
8069634	5	16	gly	glycopeptide	944:955	arg2	glycopeptide			glycopeptide						glycopeptide	RESULTS: We have determined the crystal structures of Lathyrus ochrus isolectin II complexed with the N2 monoglycosylated fragment of human lactotransferrin (18 kDa) and an isolated glycopeptide (2.1 kDa) fragment of human lactotransferrin (at 3.3 A and 2.8 A resolution, respectively).
8069634	5	41	gly	monoglycosylated	867:882	arg1	the N2 monoglycosylated fragment			the N2 monoglycosylated fragment						fragment	RESULTS: We have determined the crystal structures of Lathyrus ochrus isolectin II complexed with the N2 monoglycosylated fragment of human lactotransferrin (18 kDa) and an isolated glycopeptide (2.1 kDa) fragment of human lactotransferrin (at 3.3 A and 2.8 A resolution, respectively).
25485983	4	16	gly	glycosylation	615:627	arg2	this defective glycosylation site	antithrombin		site		PUBTATOR		antithrombin	462	site	We evaluated the effect of the aromatic sequon in this defective glycosylation site of antithrombin, despite of being located in a loop between the helix D and the strand 2A.
7780197	1	21	gly	contains	140:147	arg1	TfR AND three N-linked oligosaccharides	TfR			three N-linked oligosaccharides	PUBTATOR		TfR	7037		The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	1	21	gly	contains	140:147	arg1	The human transferrin receptor AND three N-linked oligosaccharides	The human transferrin receptor			three N-linked oligosaccharides	PUBTATOR		transferrin receptor	7037		The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
23001782	3	36	gly	glycosylation	495:507	arg1	serum-derived hSHBG	serum-derived hSHBG				PUBTATOR		hSHBG	6462		Here, we perform a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG.
23661698	2	41	gly	glycosylation	337:349	arg1	the Asn-26			Asn-26						Asn-26	The crystal structure of the ligand-receptor complex revealed a glycosylation on the Asn-26 of ephrin-A1.
10207176	0	8	gly	C-mannosylated	60:73	arg1	a C-mannosylated protein	a C-mannosylated protein				Fterm		protein			Recombinant human interleukin-12 is the second example of a C-mannosylated protein.
10209036	3	10	gly	glycoprotein	482:493	arg1	a disulfide-linked homodimeric glycoprotein	a disulfide-linked homodimeric glycoprotein				Fterm		glycoprotein			SIT is a disulfide-linked homodimeric glycoprotein that is expressed in lymphocytes.
10209036	3	10	gly	glycoprotein	482:493	arg1	SIT	SIT				PUBTATOR		SIT	27240		SIT is a disulfide-linked homodimeric glycoprotein that is expressed in lymphocytes.
8349699	10	17	part_of	PGH	1590:1592	arg1	Arg277	PGH synthase-1		Arg277		PUBTATOR	AminoAcid	PGH synthase-1	19224	Arg277	Assuming that the N-glycosylation sites of PGH synthase-1 are on the luminal side of the endoplasmic reticulum (ER), and that the site of tryptic cleavage of ovine PGH synthase-1 (Arg277) is on the cytoplasmic side of the ER, we propose that both the NH2 and COOH termini of PGH synthase-1 are located in the lumen of the ER and that there are two transmembrane domains located between Asn144 and Arg277 and between Arg277 and Asn410, respectively.
8349699	10	37	part_of	synthase-1	1473:1482	arg1	the N-glycosylation sites	PGH synthase-1		the N-glycosylation sites		PUBTATOR	Site	PGH synthase-1	19224	sites	Assuming that the N-glycosylation sites of PGH synthase-1 are on the luminal side of the endoplasmic reticulum (ER), and that the site of tryptic cleavage of ovine PGH synthase-1 (Arg277) is on the cytoplasmic side of the ER, we propose that both the NH2 and COOH termini of PGH synthase-1 are located in the lumen of the ER and that there are two transmembrane domains located between Asn144 and Arg277 and between Arg277 and Asn410, respectively.
8349699	10	68	part_of	synthase-1	1705:1714	arg1	COOH termini	PGH synthase-1		COOH termini		PUBTATOR	Site	PGH synthase-1	19224	termini	Assuming that the N-glycosylation sites of PGH synthase-1 are on the luminal side of the endoplasmic reticulum (ER), and that the site of tryptic cleavage of ovine PGH synthase-1 (Arg277) is on the cytoplasmic side of the ER, we propose that both the NH2 and COOH termini of PGH synthase-1 are located in the lumen of the ER and that there are two transmembrane domains located between Asn144 and Arg277 and between Arg277 and Asn410, respectively.
21886772	3	27	gly	O-glycosylation	560:574	arg1	the membrane/extracellular matrix (ECM) protein α-dystroglycan				the membrane/extracellular matrix (ECM) protein α-dystroglycan						These four disorders share in common an incomplete/aberrant O-glycosylation of the membrane/extracellular matrix (ECM) protein α-dystroglycan.
9295302	6	73	part_of	MRP	1056:1058	arg1	specific regions	MRP		specific regions		PUBTATOR	Site	MRP	4363	regions	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
15498570	1	61	part_of	contains	357:364	arg1	C2orf7 AND signal peptide	C2orf7		signal peptide		PUBTATOR	Site	7 (C2orf7	84279	peptide	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
1731338	1	2	gly	galactoglycoprotein	146:164	arg1	galactoglycoprotein	galactoglycoprotein				PUBTATOR		galactoglycoprotein	6693		The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	1	68	gly	glycopeptides	274:286	arg2	glycopeptides			glycopeptides						peptides and glycopeptides	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
28668641	2	23	gly	glycosylation	395:407	arg1	human vaspin	human vaspin				PUBTATOR		vaspin	145264		In this study, we have investigated the glycosylation of human vaspin and its effects on biochemical properties relevant to vaspin function.
21269602	3	52	part_of	VE-cadherin	497:507	arg1	mammalian-produced VE-cadherin ectodomains	VE-cadherin		mammalian-produced VE-cadherin ectodomains		PUBTATOR	Site	VE-cadherin	1003	ectodomains	Here we report studies of mammalian-produced VE-cadherin ectodomains suggesting that, like other classical cadherins, VE-cadherin forms adhesive trans dimers between monomers located on opposing cell surfaces.
19343721	5	42	gly	glycosylation	1029:1041	arg2	the four glycosylation sites			the four glycosylation sites						sites	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
16474139	9	43	gly	contain	1588:1594	arg1	The SARS-CoV 3a protein AND sialic acids	The SARS-CoV 3a protein			sialic acids	Fterm		protein			The SARS-CoV 3a protein, however, was demonstrated to contain sialic acids, indicating the presence of oligosaccharides.
12654314	3	51	gly	N-glycosylation	661:675	arg2	the six potential N-glycosylation sites			the six potential N-glycosylation sites						sites	Peptide mapping studies covering 88% of the deduced amino acid sequence indicated that of the six potential N-glycosylation sites in this antibody only five were utilized, as the tryptic peptide derived from monoclonal IgM 12A1 containing Asn-260 was recovered without carbohydrates.
15532026	8	91	gly	glycosylated	1442:1453	arg1	a 97 kDa glycosylated dimer	a 97 kDa glycosylated dimer				Fterm		dimer			Western blot analysis of extracts from control fibroblasts detect a 97 kDa glycosylated dimer whereas ML III cells contain a GNPTAG dimer of reduced molecular mass.
10878002	10	11	gly	C-mannosylated	1110:1123	arg1	C-mannosylated proteins	C-mannosylated proteins				Fterm		proteins			These results show that C-mannosylated proteins occur at several steps along the complement activation cascade.
22333914	1	3	part_of	conserved	239:247	arg1	a highly conserved autoproteolysis sequence	d		a highly conserved autoproteolysis sequence		PUBTATOR	Site	d	23218	sequence	The G protein-coupled receptor (GPCR) Proteolysis Site (GPS) of cell-adhesion GPCRs and polycystic kidney disease (PKD) proteins constitutes a highly conserved autoproteolysis sequence, but its catalytic mechanism remains unknown.
19656770	5	57	part_of	N-linked	1132:1139	arg1	235 N-linked glycosylation sites	235 N-linked		235 N-linked glycosylation sites		Cterm	Site	235 N-linked		sites	The data set revealed 36 cluster of differentiation-annotated proteins and confirmed the occupancy for 235 N-linked glycosylation sites.
9449027	7	70	gly	fucosylated	1708:1718	arg1	fucosylated and nonfucosylated biantennary N-linked structures				fucosylated and nonfucosylated biantennary N-linked structures						The beta-subunit from normal pregnancy hCG contained fucosylated and nonfucosylated biantennary N-linked structures; however, mono- and triantennary oligosaccharides were also identified (4.6 and 13.7%).
9449027	7	83	gly	nonfucosylated	1724:1737	arg1	fucosylated and nonfucosylated biantennary N-linked structures				fucosylated and nonfucosylated biantennary N-linked structures						The beta-subunit from normal pregnancy hCG contained fucosylated and nonfucosylated biantennary N-linked structures; however, mono- and triantennary oligosaccharides were also identified (4.6 and 13.7%).
9449027	7	171	gly	contained	1698:1706	arg1	The beta-subunit AND fucosylated and nonfucosylated biantennary N-linked structures	The beta-subunit			fucosylated and nonfucosylated biantennary N-linked structures	OGER		subunit	P0DN86		The beta-subunit from normal pregnancy hCG contained fucosylated and nonfucosylated biantennary N-linked structures; however, mono- and triantennary oligosaccharides were also identified (4.6 and 13.7%).
29681470	3	17	part_of	residues	476:483	arg1	the core proteins	proteins		residues		Fterm	AminoAcid	proteins	64131	serine residues	GAG biosynthesis is initiated by peptide O-xylosyltransferases, which transfer xylose onto selected serine residues in the core proteins.
1512232	10	58	gly	Glycosylation	1796:1808	arg1	peptides			peptides						peptides	Glycosylation of peptides (274-283) and (313-324) was found to occur on the serine in the TTST tandem repeat and on serine 316 in the SS repeat, respectively.
1512232	10	59	gly	serine	1872:1877	arg1	the TTST tandem repeat			serine	the TTST tandem repeat					serine	Glycosylation of peptides (274-283) and (313-324) was found to occur on the serine in the TTST tandem repeat and on serine 316 in the SS repeat, respectively.
16763549	0	13	gly	neuropilin-1	34:45	arg1	Glycosaminoglycan modification	neuropilin-1			Glycosaminoglycan modification	OGER		neuropilin-1	O14786		Glycosaminoglycan modification of neuropilin-1 modulates VEGFR2 signaling.
16763549	0	31	gly	modification	18:29	arg1	neuropilin-1 AND Glycosaminoglycan modification	neuropilin-1			Glycosaminoglycan modification	OGER		neuropilin-1	O14786		Glycosaminoglycan modification of neuropilin-1 modulates VEGFR2 signaling.
24125761	12	36	gly	N-glycosylation	1724:1738	arg1	AADAC	AADAC				PUBTATOR		AADAC	13		Overall, this study found that the translational, but not post-translational, N-glycosylation of AADAC plays a crucial role in regulating AADAC enzyme activity.
24417605	2	28	gly	glycoprotein	355:366	arg1	glycoprotein	glycoprotein				Fterm		glycoprotein			In this study, HDL was isolated from plasma by sequential micro-ultracentrifugation, followed by glycoprotein and glycolipid analysis.
8286855	0	12	gly	glycosylation	74:86	arg2	O-linked glycosylation motifs			O-linked glycosylation motifs						motifs	Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.
8068684	9	33	part_of	possess	1695:1701	arg1	NHE-3 AND the N75 N-linked putative glycosylation site	NHE-3		the N75 N-linked putative glycosylation site		PUBTATOR	Site	NHE-3	6550	site	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	9	33	part_of	possess	1695:1701	arg1	an apically-expressed epithelial isoform AND the N75 N-linked putative glycosylation site	an apically-expressed epithelial isoform		the N75 N-linked putative glycosylation site		Fterm	Site	isoform		site	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
19196183	2	11	gly	glycosylation	310:322	arg2	their glycosylation sites			their glycosylation sites						sites	However, with respect to their glycosylation sites, little attention has been paid.
7592613	3	75	gly	glycosylated	558:569	arg1	glycodelin	glycodelin		Asn-28 and Asn-63		PUBTATOR		glycodelin	5047	Asn-28 and Asn-63	Using strategies based upon fast atom bombardment and electrospray mass spectrometry we have established that glycodelin is glycosylated at Asn-28 and Asn-63.
7592613	3	75	gly	glycosylated	558:569	arg2	Asn-63			Asn-28 and Asn-63						Asn-28 and Asn-63	Using strategies based upon fast atom bombardment and electrospray mass spectrometry we have established that glycodelin is glycosylated at Asn-28 and Asn-63.
7592613	3	75	gly	glycosylated	558:569	arg2	Asn-63	glycodelin		Asn-28 and Asn-63		PUBTATOR		glycodelin	5047	Asn-28 and Asn-63	Using strategies based upon fast atom bombardment and electrospray mass spectrometry we have established that glycodelin is glycosylated at Asn-28 and Asn-63.
21237175	1	4	gly	glycoprotein	161:172	arg1	The translocating chain-associating membrane protein	The translocating chain-associating membrane protein				PUBTATOR		translocating chain-associating membrane protein	23471		The translocating chain-associating membrane protein (TRAM) is a glycoprotein involved in the translocation of secreted proteins into the endoplasmic reticulum (ER) lumen and in the insertion of integral membrane proteins into the lipid bilayer.
21237175	1	4	gly	glycoprotein	161:172	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			The translocating chain-associating membrane protein (TRAM) is a glycoprotein involved in the translocation of secreted proteins into the endoplasmic reticulum (ER) lumen and in the insertion of integral membrane proteins into the lipid bilayer.
12878160	7	10	gly	VIPL	890:893	arg1	The single N-linked glycan	VIPL			The single N-linked glycan	PUBTATOR		VIPL	81562		The single N-linked glycan of VIPL remained endoglycosidase H-sensitive during a 2-h pulse-chase, even when the protein was overexpressed or mutated to allow export to the plasma membrane.
30659065	9	80	part_of	variants	1579:1586	arg1	proline	IgA2 variants		proline		OGER	AminoAcid	IgA2 variants	P01877	proline	IgA2 variants with the either serine (S93) or proline (P93) were detected.
30659065	9	80	part_of	variants	1579:1586	arg1	serine	IgA2 variants		serine		OGER	AminoAcid	IgA2 variants	P01877	serine	IgA2 variants with the either serine (S93) or proline (P93) were detected.
1737041	1	14	gly	glycoproteins	236:248	arg1	acidic glycoproteins	acidic glycoproteins				Fterm		glycoproteins			Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
7505568	4	20	part_of	MAG	346:348	arg1	the 9 MAG sequons	9 MAG		the 9 MAG sequons		PUBTATOR		9 MAG	4099		Of the 9 MAG sequons 7 were glycosylated and 1 was partially glycosylated at Asn106.
18703501	8	44	gly	glycosylation	1520:1532	arg2	Thr(78)			Thr(78)						Thr(78)	Parallel experiments on a recombinant protein obtained by a mammalian cell expression system demonstrated the occurrence of an additional O-linked glycosylation site (Thr(78)) and characterized the nature of the oligosaccharide structures.
18703501	8	44	gly	glycosylation	1520:1532	arg2	an additional O-linked glycosylation site			an additional O-linked glycosylation site						site	Parallel experiments on a recombinant protein obtained by a mammalian cell expression system demonstrated the occurrence of an additional O-linked glycosylation site (Thr(78)) and characterized the nature of the oligosaccharide structures.
29671580	6	5	gly	glycosites	1042:1051	arg2	these two glycosites			these two glycosites						glycosites	The widespread presence of these two glycosites among individuals was further confirmed by individual serum analyses.
15807535	2	81	gly	glycosylated	383:394	arg1	Both transiently and stably expressed ABCG2	Both transiently and stably expressed ABCG2				PUBTATOR		ABCG2	9429		Both transiently and stably expressed ABCG2 are glycosylated, and treatment with peptide N-glycosidase F reduces the apparent molecular mass on SDS-PAGE gels to approximately 60 kDa.
16263699	3	58	gly	glycosylation	578:590	arg2	their glycosylation sites			their glycosylation sites						sites	Although many of those proteins have been studied for some time with regard to their function, little attention has been paid with respect to their glycosylation sites.
3886654	6	38	part_of	factor	841:846	arg1	" a "growth factor" domain	factor		" a "growth factor" domain		Fterm	Site	factor		domain	The heavy chain of alpha-factor XIIa appears to contain four different domains including a "kringle," a "growth factor" domain, and the "type I" and "type II" domains of fibronectin.
3886654	6	68	part_of	fibronectin	899:909	arg1	" a "growth factor" domain	fibronectin		" a "growth factor" domain		PUBTATOR	Site	fibronectin	2335	domain	The heavy chain of alpha-factor XIIa appears to contain four different domains including a "kringle," a "growth factor" domain, and the "type I" and "type II" domains of fibronectin.
3886654	6	68	part_of	fibronectin	899:909	arg1	four different domains	fibronectin		four different domains		PUBTATOR	Site	fibronectin	2335	domains	The heavy chain of alpha-factor XIIa appears to contain four different domains including a "kringle," a "growth factor" domain, and the "type I" and "type II" domains of fibronectin.
14764083	3	29	part_of	hLF	485:487	arg1	Gly404-->Cys	hLF		Gly404-->Cys		PUBTATOR	AminoAcid	hLF	3131	Cys	The analysis revealed that recombinant hLF (rhLF) with mutations Ile130-->Thr and Gly404-->Cys was about twofold more susceptible than glycosylated and unglycosylated variants with the naturally occurring Ile130 and Gly404.
14764083	3	29	part_of	hLF	485:487	arg1	Ile130-->Thr	hLF		Ile130-->Thr		PUBTATOR	AminoAcid	hLF	3131	Ile130	The analysis revealed that recombinant hLF (rhLF) with mutations Ile130-->Thr and Gly404-->Cys was about twofold more susceptible than glycosylated and unglycosylated variants with the naturally occurring Ile130 and Gly404.
14764083	3	27	part_of	variants	613:620	arg1	the naturally occurring Ile130	variants		Ile130 and Gly404		Fterm	AminoAcid	variants		Ile130 and Gly404	The analysis revealed that recombinant hLF (rhLF) with mutations Ile130-->Thr and Gly404-->Cys was about twofold more susceptible than glycosylated and unglycosylated variants with the naturally occurring Ile130 and Gly404.
15702487	8	22	gly	Glycosylation	1462:1474	arg1	alpha 5 beta 1 subunits	alpha 5 beta 1 subunits				OGER		subunits	P08648		Glycosylation of alpha 5 beta 1 subunits of human integrin was studied to test the methodology.
9343410	0	37	gly	glycosylation	2:14	arg1	an Sp1-derived peptide			an Sp1-derived peptide						peptide	O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions.
1421757	0	32	gly	glycosylation	31:43	arg2	the O-linked glycosylation site	transferrin receptor		site		PUBTATOR		transferrin receptor	7037	site	Identification of the O-linked glycosylation site of the human transferrin receptor.
10383441	6	7	gly	glycosylation	1027:1039	arg2	the Asn106 glycosylation site			the Asn106 glycosylation site						site	We show that Val23 inhibits phosphorylation at the Asn18 glycosylation site, whereas Tyr54, Lys124, and Ser190 enhance phosphorylation at the Asn106 glycosylation site.
10383441	6	37	gly	glycosylation	935:947	arg2	the Asn18 glycosylation site			the Asn18 glycosylation site						site	We show that Val23 inhibits phosphorylation at the Asn18 glycosylation site, whereas Tyr54, Lys124, and Ser190 enhance phosphorylation at the Asn106 glycosylation site.
9786864	1	65	gly	N-glycosylation	64:78	arg2	N-glycosylation sites			N-glycosylation sites						sites	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	65	gly	N-glycosylation	64:78	arg1	the extracellular domain			domain						domain	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
7613477	5	92	gly	sites	1112:1116	arg1	All four potential N-linked glycosylation sites			All four potential N-linked glycosylation sites						sites	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	All four potential N-linked glycosylation sites AND triantennary	LCAT		All four potential N-linked glycosylation sites	triantennary	PUBTATOR		LCAT	3931	sites	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	All four potential N-linked glycosylation sites AND sialylated triantennary and/or biantennary complex structures	LCAT		All four potential N-linked glycosylation sites	sialylated triantennary and/or biantennary complex structures	PUBTATOR		LCAT	3931	sites	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	92	gly	sites	1112:1116	arg1	Asn384			Asn20, Asn84, Asn272, and Asn384						Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	92	gly	sites	1112:1116	arg1	Asn84			Asn20, Asn84, Asn272, and Asn384						Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	92	gly	sites	1112:1116	arg1	Asn84			Asn20, Asn84, Asn272, and Asn384						Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg1	LCAT	LCAT		sites		PUBTATOR		LCAT	3931	sites	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg1	LCAT	LCAT		Asn20, Asn84, Asn272, and Asn384		PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg2	Asn84			Asn20, Asn84, Asn272, and Asn384						Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg2	Asn384			Asn20, Asn84, Asn272, and Asn384						Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg2	Asn84	LCAT		Asn20, Asn84, Asn272, and Asn384		PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg2	Asn384	LCAT		Asn20, Asn84, Asn272, and Asn384		PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg2	Asn384			Asn20, Asn84, Asn272, and Asn384						Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	Asn84 AND triantennary			Asn20, Asn84, Asn272, and Asn384	triantennary					Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	LCAT AND triantennary	LCAT		Asn20, Asn84, Asn272, and Asn384	triantennary	PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	Asn272 AND triantennary	LCAT		Asn20, Asn84, Asn272, and Asn384	triantennary	PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	Asn84 AND sialylated triantennary and/or biantennary complex structures			Asn20, Asn84, Asn272, and Asn384	sialylated triantennary and/or biantennary complex structures					Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	LCAT AND sialylated triantennary and/or biantennary complex structures	LCAT		Asn20, Asn84, Asn272, and Asn384	sialylated triantennary and/or biantennary complex structures	PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	Asn272 AND sialylated triantennary and/or biantennary complex structures	LCAT		Asn20, Asn84, Asn272, and Asn384	sialylated triantennary and/or biantennary complex structures	PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	LCAT AND triantennary	LCAT		Asn20, Asn84, Asn272, and Asn384	triantennary	PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	Asn272 AND triantennary	LCAT		Asn20, Asn84, Asn272, and Asn384	triantennary	PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	LCAT AND sialylated triantennary and/or biantennary complex structures	LCAT		Asn20, Asn84, Asn272, and Asn384	sialylated triantennary and/or biantennary complex structures	PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	Asn272 AND sialylated triantennary and/or biantennary complex structures	LCAT		Asn20, Asn84, Asn272, and Asn384	sialylated triantennary and/or biantennary complex structures	PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	Asn272 AND triantennary	LCAT		Asn20, Asn84, Asn272, and Asn384	triantennary	PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	gly	contain	1180:1186	arg1	Asn272 AND sialylated triantennary and/or biantennary complex structures	LCAT		Asn20, Asn84, Asn272, and Asn384	sialylated triantennary and/or biantennary complex structures	PUBTATOR		LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
28279966	1	73	part_of	factor	220:225	arg1	plasma von Willebrand factor (VWF) multimer composition	von Willebrand factor		plasma von Willebrand factor (VWF) multimer composition		PUBTATOR	Site	von Willebrand factor	7450	position	Previous studies have demonstrated a role for plasmin in regulating plasma von Willebrand factor (VWF) multimer composition.
19358553	4	46	part_of	fetuin	1052:1057	arg1	three different sialoglycopeptides	fetuin		three different sialoglycopeptides		Fterm	Site	fetuin		sialoglycopeptides	Similarly, precise quantitation was observed for various forms of N-glycans (free, permethylated, and fluorescence-labeled) using MS. In addition, three different sialoglycopeptides from fetuin were site-specifically profiled, and good correlation between peak intensities and relative abundances was found with only a minor loss of sialic acids (r = 0.9664, n = 5).
8672508	4	14	part_of	has	756:758	arg1	Pore membrane glycoprotein gp210 AND a cytoplasmic, carboxyl-terminal domain	Pore membrane glycoprotein gp210		a cytoplasmic, carboxyl-terminal domain		Fterm	Site	glycoprotein		domain	Pore membrane glycoprotein gp210, that has a cytoplasmic, carboxyl-terminal domain facing the pore, was not phosphorylated in interphase but specifically phosphorylated in mitosis.
10929010	1	1	gly	transferrin	154:164	arg1	The N-glycans	transferrin			The N-glycans	PUBTATOR		transferrin	7018		The N-glycans of human serum transferrin produced in Trichopulsia ni cells were analyzed to examine N-linked oligosaccharide processing in insect cells.
8323299	6	19	gly	O-glycosylation	905:919	arg2	these O-glycosylation sites			these O-glycosylation sites						sites	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
19692335	5	20	part_of	metalloproteinase-like	1029:1050	arg1	the metalloproteinase-like domain	metalloproteinase		the metalloproteinase-like domain		Fterm	Site	metalloproteinase		domain	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	5	30	part_of	ADAM22	969:974	arg1	the full ectodomain	ADAM22		the full ectodomain		PUBTATOR	Site	ADAM22	53616	ectodomain	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	5	60	part_of	disintegrin	1116:1126	arg1	the disintegrin, cysteine-rich, and epidermal growth factor-like domains	disintegrin		the disintegrin, cysteine-rich, and epidermal growth factor-like domains		Fterm	Site	disintegrin		domains	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
24884609	5	57	gly	glycopeptides	764:776	arg2	ITIH4 tryptic/GluC glycopeptides			ITIH4 tryptic/GluC glycopeptides						glycopeptides	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	the four ITIH4 N-X-S/T sequons			N81, N207, N517, and N577						N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	N517			N81, N207, N517, and N577						N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	N577			N81, N207, N517, and N577						N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	N207			N81, N207, N517, and N577						N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	N517			N81, N207, N517, and N577						N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	N577			N81, N207, N517, and N577						N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	N207			N81, N207, N517, and N577						N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	N577			N81, N207, N517, and N577						N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	N207			N81, N207, N517, and N577						N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	N207			N81, N207, N517, and N577						N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
19119025	4	10	part_of	ERp57	610:614	arg1	both ERp57 catalytic domains	ERp57		both ERp57 catalytic domains		OGER	Site	ERp57	P30101	domains	The structure revealed that tapasin interacts with both ERp57 catalytic domains, accounting for the stability of the heterodimer, and provided an example of a protein disulfide isomerase family member interacting with substrate.
23345538	5	55	gly	glycosylation	1130:1142	arg2	121 glycosylation sites			121 glycosylation sites						sites	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
2808371	4	12	part_of	protein	788:794	arg1	the 22/24-kDa carboxyl-terminal domain	protein 4.1		the 22/24-kDa carboxyl-terminal domain		PUBTATOR	Site	protein 4.1	281753	domain	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	4	30	part_of	peptide	735:741	arg1	the 22/24-kDa carboxyl-terminal domain	peptide		the 22/24-kDa carboxyl-terminal domain						domain	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	4	30	part_of	peptide	735:741	arg1	protein 4.1	protein 4.1		peptide		PUBTATOR	Site	protein 4.1	281753	peptide	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
20511397	4	10	gly	sialylation	768:778	arg1	cellular and secreted apoE	cellular and secreted apoE				PUBTATOR		apoE	348		We investigated glycosylation and sialylation of cellular and secreted apoE from primary human macrophages by one- and two-dimensional gel electrophoresis and mass spectrometry.
20511397	4	47	gly	glycosylation	750:762	arg1	cellular and secreted apoE	cellular and secreted apoE				PUBTATOR		apoE	348		We investigated glycosylation and sialylation of cellular and secreted apoE from primary human macrophages by one- and two-dimensional gel electrophoresis and mass spectrometry.
20511397	4	72	gly	apoE	805:808	arg1	sialylation	apoE			sialylation	PUBTATOR		apoE	348		We investigated glycosylation and sialylation of cellular and secreted apoE from primary human macrophages by one- and two-dimensional gel electrophoresis and mass spectrometry.
21569239	10	79	part_of	F-spondin	1413:1421	arg1	the F-spondin FS domain	F-spondin		the F-spondin FS domain		PUBTATOR	Site	F-spondin	10418	domain	The homology of its core structure to a common Ca2+- and lipid-binding C2 domain suggests that the F-spondin FS domain may be responsible for part of the membrane targeting of F-spondin in its regulation of axon development.
2129367	3	46	part_of	VII	414:416	arg1	the first epidermal growth factor-like domain	factor VII		the first epidermal growth factor-like domain		OGER	Site	factor VII	P08709	domain	In the course of the studies, we found an unknown serine derivative at position 52 in the first epidermal growth factor-like domain of factor VII.
21053369	6	69	gly	glycopeptides	883:895	arg2	the glycopeptides			the glycopeptides						glycopeptides	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	6	88	gly	glycosylation	1067:1079	arg2	glycosylation site profiling			glycosylation site profiling						site	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
3345749	0	6	gly	derived	46:52	arg2	respiratory-mucus glycoproteins AND neutral oligosaccharides	respiratory-mucus glycoproteins			neutral oligosaccharides	Fterm		glycoproteins			Primary structure of neutral oligosaccharides derived from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis, determined by combination of 500-MHz 1H-NMR spectroscopy and quantitative sugar analysis.
3345749	0	69	gly	glycoproteins	77:89	arg1	respiratory-mucus glycoproteins	respiratory-mucus glycoproteins				Fterm		glycoproteins			Primary structure of neutral oligosaccharides derived from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis, determined by combination of 500-MHz 1H-NMR spectroscopy and quantitative sugar analysis.
7512967	3	34	gly	sialylation	571:581	arg1	the N-linked oligosaccharides				the N-linked oligosaccharides						In the N-linked oligosaccharides from all of the IgG2b phenotypes, virtually no sialylation was detected.
26536155	7	8	gly	O-glycopeptide	1715:1728	arg2	O-glycopeptide analysis			O-glycopeptide analysis						O-glycopeptide	This analytical tool can be applied to a variety of glycoproteins for site-specific N- and O-glycopeptide analysis, resulting in a good glycopeptide coverage within a single sample run and, thus, requiring only small amounts of sample.
26536155	7	17	gly	glycoproteins	1676:1688	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			This analytical tool can be applied to a variety of glycoproteins for site-specific N- and O-glycopeptide analysis, resulting in a good glycopeptide coverage within a single sample run and, thus, requiring only small amounts of sample.
26536155	7	39	gly	glycopeptide	1760:1771	arg2	a good glycopeptide coverage			a good glycopeptide coverage						glycopeptide	This analytical tool can be applied to a variety of glycoproteins for site-specific N- and O-glycopeptide analysis, resulting in a good glycopeptide coverage within a single sample run and, thus, requiring only small amounts of sample.
18780401	2	6	gly	glycoproteins	445:457	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
1898736	5	37	gly	containing	897:906	arg1	proteins AND glycosaminoglycan	proteins			glycosaminoglycan	Fterm		proteins			This PGP cross-link may be present in other proteins, but could have been overlooked due to the heterogeneous behavior of proteins containing glycosaminoglycan.
12545205	11	32	gly	N-cadherin	1793:1802	arg1	N-glycans	N-cadherin			N-glycans	PUBTATOR		N-cadherin	1000		The results demonstrated that N-glycans of N-cadherin are altered in metastatic melanomas in a way characteristic for invasive tumor cells.
30598546	2	24	part_of	Notch	291:295	arg1	a Notch fragment	Notch		a Notch fragment		Cterm	Site	Notch		fragment	Here we report the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å.
9136890	14	19	gly	found	1817:1821	arg2	each site AND oligosaccharide			each site	oligosaccharide					site	These results indicate that the type of oligosaccharide found at each site is most dependent on the environment surrounding it.
23001782	5	6	gly	N-glycosylated	880:893	arg2	367			Asn(351) and Asn(367)						Asn(351) and Asn(367)	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg2	Asn			Asn(351) and Asn(367)						Asn(351) and Asn(367)	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg1	serum-derived hSHBG	hSHBG		Asn(351) and Asn(367)		PUBTATOR		hSHBG	6462	Asn(351) and Asn(367)	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg2	Asn			Asn(351) and Asn(367)						Asn(351) and Asn(367)	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg2	Asn			Asn(351) and Asn(367)						Asn(351) and Asn(367)	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg1	serum-derived hSHBG	hSHBG		Asn(351) and Asn(367)		PUBTATOR		hSHBG	6462	Asn(351) and Asn(367)	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg2	Asn			Asn(351) and Asn(367)						Asn(351) and Asn(367)	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg1	serum-derived hSHBG	hSHBG		Asn(351) and Asn(367)		PUBTATOR		hSHBG	6462	Asn(351) and Asn(367)	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg2	Asn			Asn(351) and Asn(367)						Asn(351) and Asn(367)	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg2	Asn	hSHBG		Asn(351) and Asn(367)		PUBTATOR		hSHBG	6462	Asn(351) and Asn(367)	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
18775496	2	59	gly	O-fucosylated	307:319	arg1	agrin	agrin				PUBTATOR		agrin	O00468		Here we demonstrate that agrin is O-fucosylated in a Pofut1-dependent manner, and that this glycosylation can regulate agrin function.
25802287	7	90	gly	glycopeptide	1188:1199	arg2	the "intact" glycopeptide clusters			the "intact" glycopeptide clusters						glycopeptide	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
22451694	5	34	gly	glycosylation	955:967	arg2	glycosylation sites			glycosylation sites						sites	The RGD-binding pocket is situated at the center of a trenchlike exposed surface on the top face of α5β1 devoid of glycosylation sites.
23395175	5	25	gly	modified	755:762	arg3	Clock AND O-GlcNAcylation	Clock			O-GlcNAcylation	PUBTATOR		Clock	12753		Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
23395175	5	25	gly	modified	755:762	arg3	Central clock proteins AND O-GlcNAcylation	Central clock proteins			O-GlcNAcylation	PUBTATOR		Central clock proteins	12753		Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
16083266	8	86	gly	glycosylated	2417:2428	arg1	two heavily phosphorylated and glycosylated proteins	two heavily phosphorylated and glycosylated proteins				Fterm		proteins			Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	86	gly	glycosylated	2417:2428	arg1	beta-casein	beta-casein				OGER		beta-casein	P05814		Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	86	gly	glycosylated	2417:2428	arg1	the epidermal growth factor receptor	the epidermal growth factor receptor				PUBTATOR		epidermal growth factor receptor	1956		Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
11390601	1	70	gly	glycosylation	346:358	arg2	approximately 23 asparagine (N)-linked glycosylation sites			approximately 23 asparagine (N)-linked glycosylation sites						sites	The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) is extensively glycosylated, containing approximately 23 asparagine (N)-linked glycosylation sites on its gp120 subunit.
11390601	1	80	gly	glycosylated	282:293	arg1	The envelope glycoprotein	The envelope glycoprotein				Fterm		glycoprotein			The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) is extensively glycosylated, containing approximately 23 asparagine (N)-linked glycosylation sites on its gp120 subunit.
11390601	1	88	gly	glycoprotein	207:218	arg1	The envelope glycoprotein	The envelope glycoprotein				Fterm		glycoprotein			The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) is extensively glycosylated, containing approximately 23 asparagine (N)-linked glycosylation sites on its gp120 subunit.
1900431	2	31	part_of	factor	299:304	arg1	the epidermal growth factor region	factor		the epidermal growth factor region		Fterm	Site	factor		region	The monosaccharide fucose is glycosidically linked to threonine-61 in the epidermal growth factor region of t-PA.
1900431	2	52	part_of	t-PA	316:319	arg1	the epidermal growth factor region	t-PA		the epidermal growth factor region		PUBTATOR	Site	t-PA	5327	region	The monosaccharide fucose is glycosidically linked to threonine-61 in the epidermal growth factor region of t-PA.
21908432	4	30	part_of	GPIX	594:597	arg1	the GPIX ectodomain sequence	GPIX		the GPIX ectodomain sequence		PUBTATOR	Site	GPIX	2815	sequence	The structure of a chimera of GPIbβ(E) and 3 loops (a,b,c) taken from the GPIX ectodomain sequence was also determined.
21317871	0	47	part_of	receptor	46:53	arg1	the AMPA receptor N-terminal domain	AMPA receptor N-terminal		the AMPA receptor N-terminal domain		OGER	Site	AMPA receptor N-terminal	P19493	domain	Dynamics and allosteric potential of the AMPA receptor N-terminal domain.
21317871	0	50	part_of	AMPA	41:44	arg1	the AMPA receptor N-terminal domain	AMPA receptor N-terminal		the AMPA receptor N-terminal domain		OGER	Site	AMPA receptor N-terminal	P19493	domain	Dynamics and allosteric potential of the AMPA receptor N-terminal domain.
21317871	0	65	part_of	N-terminal	55:64	arg1	the AMPA receptor N-terminal domain	AMPA receptor N-terminal		the AMPA receptor N-terminal domain		OGER	Site	AMPA receptor N-terminal	P19493	domain	Dynamics and allosteric potential of the AMPA receptor N-terminal domain.
23285087	7	20	gly	glycosylation	1388:1400	arg1	the transporter protein	the transporter protein				Fterm		protein			Further studies revealed that glycosylation affected stability of the transporter protein and the unglycosylated mutant was retained within endoplasmic reticulum.
26146185	4	49	part_of	CD6	580:582	arg1	the three SRCR domains	CD6		the three SRCR domains		PUBTATOR	Site	CD6	923	domains	We have solved the X-ray crystal structures of the three SRCR domains of CD6 and two N-terminal domains of CD166.
26146185	4	47	part_of	CD166	614:618	arg1	the three SRCR domains	CD166		domains		PUBTATOR	Site	CD166	214	domains	We have solved the X-ray crystal structures of the three SRCR domains of CD6 and two N-terminal domains of CD166.
2511201	9	12	part_of	Z	1565:1565	arg1	Bovine protein Z glycopeptide	Bovine protein Z		Bovine protein Z glycopeptide		Cterm	Site	Bovine protein Z		glycopeptide	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	9	44	part_of	Bovine	1550:1555	arg1	Bovine protein Z glycopeptide	Bovine protein Z		Bovine protein Z glycopeptide		Cterm	Site	Bovine protein Z		glycopeptide	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	9	69	part_of	protein	1557:1563	arg1	Bovine protein Z glycopeptide	Bovine protein Z		Bovine protein Z glycopeptide		Cterm	Site	Bovine protein Z		glycopeptide	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
11150294	6	27	part_of	MUPP1	975:979	arg1	a C-terminal vesicular stomatitis virus epitope	MUPP1		a C-terminal vesicular stomatitis virus epitope		OGER	Site	MUPP1	O55164	epitope	A 5-HT(2C) receptor-dependent unmasking of a C-terminal vesicular stomatitis virus epitope of MUPP1 suggests that the interaction triggers a conformational change within the MUPP1 protein.
22848655	7	2	part_of	Sema-PSI	1096:1103	arg1	RON Sema-PSI domains	RON Sema-PSI		RON Sema-PSI domains		OGER	Site	RON Sema-PSI	Q04912	domains	Here, we report the structure of RON Sema-PSI domains at 1.85 Å resolution.
22848655	7	56	part_of	RON	1092:1094	arg1	RON Sema-PSI domains	RON Sema-PSI		RON Sema-PSI domains		OGER	Site	RON Sema-PSI	Q04912	domains	Here, we report the structure of RON Sema-PSI domains at 1.85 Å resolution.
21669976	4	27	gly	N-glycosylation	600:614	arg1	Asn-5			Asn-5						Asn-5	Our results show that KCNE1 is exclusively O-glycosylated at Thr-7, which is also required for N-glycosylation at Asn-5.
21669976	4	28	gly	O-glycosylated	548:561	arg1	KCNE1	KCNE1		Thr-7		PUBTATOR		KCNE1	3753	Thr-7	Our results show that KCNE1 is exclusively O-glycosylated at Thr-7, which is also required for N-glycosylation at Asn-5.
27966990	2	37	gly	N-glycosylation	377:391	arg2	sequons			sites						sites	The extracellular domain of VEGFR-2 is composed of seven immunoglobulin-like domains, each with multiple potential N-glycosylation sites (sequons).
18490449	1	27	part_of	myelin	217:222	arg1	the outermost lateral region	myelin		the outermost lateral region		Fterm	Site	myelin		region	In contrast to compact myelin, the series of paranodal loops located in the outermost lateral region of myelin is non-compact; the intracellular space is filled by a continuous channel of cytoplasm, the extracellular surfaces between neighboring loops keep a definite distance, but the loop membranes have junctional specializations.
2642896	6	23	part_of	enzyme	779:784	arg1	tryptic peptides	enzyme		tryptic peptides		Fterm	Site	enzyme		peptides	About 60% of the deduced amino acid sequence was confirmed by partial amino acid sequencing of tryptic peptides of the purified enzyme.
19196183	8	44	gly	N-glycosylated	1206:1219	arg1	bovine serum albumin	bovine serum albumin				OGER		albumin	P02768		Furthermore, unavoidable contaminants such as actin and bovine serum albumin which are not N-glycosylated could be easily depleted by using this glycoproteomic strategy.
1883960	0	91	gly	glycosylation	41:53	arg1	human interleukin-6	human interleukin-6				PUBTATOR		interleukin-6	3569		Marked cell-type-specific differences in glycosylation of human interleukin-6.
10531415	4	33	gly	glycosylation	705:717	arg2	the three predicted sites			the three predicted sites						sites	Polymerase chain reaction mutagenesis was used to generate a panel of D5 receptors containing mutations in the three predicted sites of N-linked glycosylation.
9054441	2	74	gly	Thr-345	273:279	arg1	an O-linked oligosaccharide			Thr-345	an O-linked oligosaccharide					Thr-345	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
9054441	2	49	gly	contains	190:197	arg1	Asn-289 AND an N-linked oligosaccharide	Plasminogen 1		Asn-289	an N-linked oligosaccharide	OGER		Plasminogen 1	P00747	Asn-289	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
10413465	10	66	part_of	apoE	1997:2000	arg1	carboxy-terminal residues	apoE		carboxy-terminal residues		PUBTATOR	Site	apoE	348	residues	These findings suggest that the amino- and carboxy-terminal residues of apoE are required for SDS-stable binding of apoE to Abeta and that the presence of at least one cysteine contributes to the efficient Abeta binding.
208636	0	16	gly	chain	45:49	arg1	human plasma very low density lipoproteins	lipoproteins			chain	Fterm		lipoproteins			Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	0	45	gly	lipoproteins	110:121	arg1	the oligosaccharide side chain	lipoproteins			the oligosaccharide side chain	Fterm		lipoproteins			Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	0	57	gly	C-III	69:73	arg1	the oligosaccharide side chain	apolipoprotein C-III			the oligosaccharide side chain	PUBTATOR		apolipoprotein C-III	345		Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
26563299	7	30	part_of	IL-15	1085:1089	arg1	The two potential IL-15 N-glycosylation sites	IL-15		The two potential IL-15 N-glycosylation sites		PUBTATOR	Site	IL-15	3600	sites	The two potential IL-15 N-glycosylation sites (Asn71 and Asn112) located at the IL-2 receptor interface were unoccupied.
26563299	7	30	part_of	IL-15	1085:1089	arg1	Asn112	IL-15		Asn71 and Asn112		PUBTATOR	AminoAcid	IL-15	3600	Asn71 and Asn112	The two potential IL-15 N-glycosylation sites (Asn71 and Asn112) located at the IL-2 receptor interface were unoccupied.
17956937	2	98	gly	glycoprotein	428:439	arg1	alpha(1)-antichymotrypsin	alpha(1)-antichymotrypsin				PUBTATOR		alpha(1)-antichymotrypsin	12		A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood.
17956937	2	98	gly	glycoprotein	428:439	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood.
25327667	5	49	part_of	has	638:640	arg1	PSA AND a single glycosylation site	PSA		a single glycosylation site		OGER	Site	PSA	P07288	site	PSA has a single glycosylation site at Asn69, with glycans constituting approximately 8% of the protein by weight.
12970363	11	17	part_of	site	1668:1671	arg1	TRPC3	TRPC3		site		PUBTATOR	Site	TRPC3	7222	site	Reciprocally, engineering of an additional second glycosylated site in TRPC3 to mimic the glycosylation status in TRPC6 markedly reduced TRPC3 basal activity.
2592374	5	68	gly	glycosylation	942:954	arg2	both potential Asn-linked glycosylation sites			both potential Asn-linked glycosylation sites						sites	Carbohydrate mapping by mass spectrometry was used to establish that both potential Asn-linked glycosylation sites in sCD4 (Asn271 and Asn300) have oligosaccharides attached.
2592374	5	46	gly	have	990:993	arg1	both potential Asn-linked glycosylation sites AND oligosaccharides			both potential Asn-linked glycosylation sites	oligosaccharides					sites	Carbohydrate mapping by mass spectrometry was used to establish that both potential Asn-linked glycosylation sites in sCD4 (Asn271 and Asn300) have oligosaccharides attached.
2592374	5	61	gly	sCD4	965:968	arg1	Asn271			Asn271 and Asn300						Asn271 and Asn300	Carbohydrate mapping by mass spectrometry was used to establish that both potential Asn-linked glycosylation sites in sCD4 (Asn271 and Asn300) have oligosaccharides attached.
8034632	1	37	gly	glycopeptides	118:130	arg2	Mucin glycopeptides			Mucin glycopeptides						glycopeptides	Mucin glycopeptides were prepared from the sputum of a patient suffering from cystic fibrosis.
8407981	8	39	gly	glycosylation	1198:1210	arg2	Asn-12			Asn-12						Asn-12	These results demonstrated that the potential glycosylation site (Asn-12) in the N-terminal portion of P-450(arom) is the site of glycosylation.
8407981	8	39	gly	glycosylation	1198:1210	arg2	the site			site						site	These results demonstrated that the potential glycosylation site (Asn-12) in the N-terminal portion of P-450(arom) is the site of glycosylation.
8407981	8	72	gly	glycosylation	1282:1294	arg2	the site			site						site	These results demonstrated that the potential glycosylation site (Asn-12) in the N-terminal portion of P-450(arom) is the site of glycosylation.
24141704	0	48	gly	glycosylation	38:50	arg1	Rho	Rho				OGER		Rho	P08100		A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
12034737	0	42	part_of	CXCR4	52:56	arg1	the CXCR4 amino terminus	CXCR4		the CXCR4 amino terminus		PUBTATOR	Site	CXCR4	7852	terminus	The role of post-translational modifications of the CXCR4 amino terminus in stromal-derived factor 1 alpha association and HIV-1 entry.
8962717	3	53	part_of	EGF-binding	567:577	arg1	the EGF-binding domain	EGF		the EGF-binding domain		OGER	Site	EGF	P01133	domain	The latter chains were shown by chromatographic separation and mass spectrometric analysis of tryptic digests to be clustered in the EGF-binding domain.
1456441	12	5	gly	attached	1707:1714	arg1	glycosylation site Asn413 AND 2,4-triantennary vs 2,6-triantennary oligosaccharides			glycosylation site Asn413	2,4-triantennary vs 2,6-triantennary oligosaccharides					site Asn413	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	12	25	gly	attached	1852:1859	arg2	glycosylation site Asn611 AND the two isomeric triantennary oligosaccharides			glycosylation site Asn611	the two isomeric triantennary oligosaccharides					site Asn611	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	12	46	gly	glycosylation	1719:1731	arg2	Asn413			site Asn413						site Asn413	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	12	52	gly	glycosylation	1864:1876	arg2	Asn611			site Asn611						site Asn611	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
30127001	2	40	part_of	NOTCH1	317:322	arg1	the mammalian NOTCH1 core ligand-binding domain	NOTCH1		the mammalian NOTCH1 core ligand-binding domain		PUBTATOR	Site	NOTCH1	4851	domain	A recent structural analysis suggested that a novel O-linked hexose modification on serine 435 of the mammalian NOTCH1 core ligand-binding domain lies at the interface with its ligands.
16321355	8	17	gly	linked	1362:1367	arg2	alpha1-3 AND fucose residues	alpha1-3			fucose residues	PUBTATOR		alpha1-3	146		Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	8	51	gly	arms	1469:1472	arg1	outer arms GlcNAc				outer arms GlcNAc						Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
21752865	4	58	part_of	bears	784:788	arg1	BRI2 AND the consensus sequence	BRI2		the consensus sequence		PUBTATOR	Site	BRI2	9445	sequence	In support, bioinformatics analysis indicated that BRI2 bears the consensus sequence Asn-Thr-Ser (residues 170-173) and could be N-glycosylated at Asn170.
17196528	2	3	part_of	TrkA	469:472	arg1	a complete extracellular domain	TrkA		a complete extracellular domain		PUBTATOR	Site	TrkA	4914	domain	To define a structural basis for the high-affinity site, we have determined the three-dimensional structure of a complete extracellular domain of TrkA complexed with NGF.
1371281	1	15	gly	glycosylation	91:103	arg1	CK	CK				OGER		CK) 8	P05787		The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	1	15	gly	glycosylation	91:103	arg1	human cytokeratin	human cytokeratin				Fterm		cytokeratin			The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
19285951	2	28	gly	glycopeptide	272:283	arg2	the Arg23-Lys66 glycopeptide			the Arg23-Lys66 glycopeptide						glycopeptide	In recent studies, we showed that either HRG, or the Arg23-Lys66 glycopeptide derived from HRG, in concert with concanavalin A (Con A), promotes a morphological change and adhesion of the human leukemic T-cell line MOLT-4 to culture dishes, and that cell surface glycosaminoglycan or Fcgamma receptors do not participate in this cellular event.
9524075	12	50	gly	Non-glycosylated	1303:1318	arg1	Non-glycosylated procathepsin S	Non-glycosylated procathepsin S				Cterm		Non-glycosylated procathepsin S	1520		Non-glycosylated procathepsin S was bound to the plasma membrane at 2 degrees C, suggesting an additional sorting motif in the cathepsin S molecule besides the Man-6-phosphate residue.
1512232	8	67	part_of	SRF	1630:1632	arg1	the transcriptional activation domain	SRF		the transcriptional activation domain		PUBTATOR	Site	SRF	6722	domain	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
21805521	5	96	gly	Asn²²⁵	846:851	arg1	three N-linked glycans			Asn²²⁵	three N-linked glycans					Asn²²⁵	LC-MS/MS peptide mapping indicates that ∼ 92% of huDKK1 is glycosylated at Asn²²⁵ with three N-linked glycans composed of two biantennary forms with 1 and 2 sialic acid (23% and 60%, respectively), and one triantennary structure with 2 sialic acids (9%).
21805521	5	27	gly	glycosylated	830:841	arg1	huDKK1	huDKK1		Asn²²⁵		Cterm		huDKK1	22943	Asn²²⁵	LC-MS/MS peptide mapping indicates that ∼ 92% of huDKK1 is glycosylated at Asn²²⁵ with three N-linked glycans composed of two biantennary forms with 1 and 2 sialic acid (23% and 60%, respectively), and one triantennary structure with 2 sialic acids (9%).
8174273	2	28	gly	desialylated	358:369	arg1	desialylated and pepsin-digested transferrin	desialylated and pepsin-digested transferrin				PUBTATOR		transferrin	7018		Sugar chains released with N-glycanase from desialylated and pepsin-digested transferrin were derivatized by reductive pyridylamination.
8174273	2	53	gly	released	327:334	arg2	desialylated and pepsin-digested transferrin AND Sugar chains	desialylated and pepsin-digested transferrin			Sugar chains	PUBTATOR		transferrin	7018		Sugar chains released with N-glycanase from desialylated and pepsin-digested transferrin were derivatized by reductive pyridylamination.
15616124	6	12	gly	N-glycosylation	908:922	arg1	FVII	FVII				Cterm		FVII	2155		Immediately after pulse, most labeled intracellular FVII had one N-glycan, but during a 1-h chase, the vast majority was processed into FVII with two N-glycans, demonstrating posttranslational N-glycosylation of FVII.
15616124	6	79	gly	FVII	851:854	arg1	two N-glycans	FVII			two N-glycans	Cterm		FVII	2155		Immediately after pulse, most labeled intracellular FVII had one N-glycan, but during a 1-h chase, the vast majority was processed into FVII with two N-glycans, demonstrating posttranslational N-glycosylation of FVII.
15616124	6	39	gly	had	772:774	arg1	most labeled intracellular FVII AND one N-glycan	most labeled intracellular FVII			one N-glycan	Cterm		FVII	2155		Immediately after pulse, most labeled intracellular FVII had one N-glycan, but during a 1-h chase, the vast majority was processed into FVII with two N-glycans, demonstrating posttranslational N-glycosylation of FVII.
15628971	2	47	gly	glycoprotein	335:346	arg1	purified C4ST-1	purified C4ST-1				PUBTATOR		C4ST-1	314694		We showed previously that purified C4ST-1 from the culture medium of rat chondrosarcoma cells was a glycoprotein containing approx.
15628971	2	47	gly	glycoprotein	335:346	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			We showed previously that purified C4ST-1 from the culture medium of rat chondrosarcoma cells was a glycoprotein containing approx.
9233787	0	36	part_of	domains	76:82	arg1	BM-40	BM-40		domains		OGER	Site	BM-40	P09486	domains	Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40.
9233787	0	45	part_of	follistatin-like	31:46	arg1	follistatin-like and EF-hand calcium-binding domains	follistatin		follistatin-like and EF-hand calcium-binding domains		OGER	Site	follistatin	P19883	domains	Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40.
6371807	7	31	part_of	contains	1182:1189	arg1	four regions AND three or four tryptophan residues	four regions		three or four tryptophan residues						tryptophan residues	Clusters of tryptophan residues occur in four regions, each of which contains three or four tryptophan residues separated by 0-12 other residues.
15750791	4	0	part_of	Edg-1/S1P1	620:629	arg1	the N-terminal ectodomain	Edg-1		the N-terminal ectodomain		PUBTATOR	Site	Edg-1	1901	ectodomain	We also demonstrated that the structure of the N-terminal ectodomain of Edg-1/S1P1 affects both its transport to the cell surface and the N-glycosylation process.
25568315	1	29	gly	N-glycosylation	237:251	arg2	multiple N-glycosylation consensus sites			multiple N-glycosylation consensus sites						sites	The extracellular loop 3 (EL-3) of SLC4 Na(+)-coupled transporters contains 4 highly conserved cysteines and multiple N-glycosylation consensus sites.
11226831	10	38	gly	glycosylation	942:954	arg2	The major glycosylation sites			The major glycosylation sites						sites	The major glycosylation sites are within or near PEST regions, suggesting that O-GlcNAc may regulate mER-alpha turnover.
1823160	1	3	gly	activator	303:311	arg1	the N-linked oligosaccharides	tissue plasminogen activator			the N-linked oligosaccharides	OGER		tissue plasminogen activator	P00750		We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
11588155	6	45	gly	desialylated	1252:1263	arg1	"desialylated" apoB100 glycans				"desialylated" apoB100 glycans						Furthermore, we found no evidence for "desialylated" apoB100 glycans in any of the samples analyzed.
14699159	5	58	part_of	p90ATF6	1119:1125	arg1	the carboxyl terminus	p90ATF6		the carboxyl terminus		Cterm	Site	p90ATF6	22926	terminus	By mutating a single amino acid within the N-linked glycosylation site closest to the carboxyl terminus of p90ATF6, we recreated ATF6(f).
16834341	7	2	part_of	hFSH	964:967	arg1	Asn52	hFSH		Asn52		OGER	AminoAcid	hFSH		Asn52	Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site.
2129367	0	9	gly	linked	32:37	arg1	a serine residue AND A new trisaccharide sugar chain			a serine residue	A new trisaccharide sugar chain					serine residue	A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z. Recently, we determined the complete amino acid sequence of bovine factor VII (Takeya, H. et al. (1988) J. Biol.
9336835	0	94	gly	glycosylation	39:51	arg2	glycosylation sites			glycosylation sites						sites	Identification and characterization of glycosylation sites in human serum clusterin.
23050552	1	55	gly	glycoprotein	132:143	arg1	Human fibrinogen	Human fibrinogen				PUBTATOR		Human fibrinogen	2244		Human fibrinogen is a 340 kDa, soluble plasma glycoprotein composed of paired sets of three subunits (α, β, γ).
23050552	1	55	gly	glycoprotein	132:143	arg1	a 340 kDa, soluble plasma glycoprotein	a 340 kDa, soluble plasma glycoprotein				Fterm		glycoprotein			Human fibrinogen is a 340 kDa, soluble plasma glycoprotein composed of paired sets of three subunits (α, β, γ).
8617200	3	1	part_of	LTBP-1	645:650	arg1	various fragments	LTBP-1		various fragments		PUBTATOR	Site	LTBP-1	4052	fragments	The association of beta1-LAP with LTBP-1 was characterized at the molecular level with an expression system in mammalian cells, where TGF-beta1 and various fragments of LTBP-1 were co-expressed and secreted with the aid of a signal peptide synthesized to the LTBP-1 constructs.
21308849	3	0	part_of	NgR2	435:438	arg1	the LRR and stalk regions	NgR2		the LRR and stalk regions		PUBTATOR	Site	NgR2	349667	regions	It has been shown by others that the LRR and stalk regions of NgR1 and NgR2 have distinct roles in conferring binding affinity to the myelin associated glycoprotein (MAG) in vivo.
19671700	1	53	gly	attachment	157:166	arg2	tryptophan AND alpha-mannopyranose			tryptophan	alpha-mannopyranose					tryptophan	Protein C-mannosylation is the attachment of alpha-mannopyranose to tryptophan via a C-C linkage.
8404899	8	19	gly	variant	1101:1107	arg1	the N-linked oligosaccharides	variant			the N-linked oligosaccharides	Fterm		variant			The structure of the N-linked oligosaccharides of the variant from the pancreatic juice of a normal donor correlated with complete processing and maturation of a complex-type N-glycan.
2065054	3	54	gly	fucosylated	1382:1392	arg1	3%				3%						We found that approximately 63% of the total N-linked oligosaccharides were of the complex type, with bisialo-biantennary (28%), asialo-biantennary (7%), fucosylated bisialo-biantennary (25%), and fucosylated asialo-biantennary (3%) oligosaccharides representing the major complex-type carbohydrate species.
2065054	3	54	gly	fucosylated	1382:1392	arg1	fucosylated asialo-biantennary (3%) oligosaccharides				fucosylated asialo-biantennary (3%) oligosaccharides						We found that approximately 63% of the total N-linked oligosaccharides were of the complex type, with bisialo-biantennary (28%), asialo-biantennary (7%), fucosylated bisialo-biantennary (25%), and fucosylated asialo-biantennary (3%) oligosaccharides representing the major complex-type carbohydrate species.
2071582	8	84	part_of	chymase	1352:1358	arg1	chymase gene-specific fragments	chymase		chymase gene-specific fragments		PUBTATOR	Site	chymase	1215	fragments	Amplification of chymase gene-specific fragments from hamster/human hybrid cell line DNA suggests localization of the chymase gene to human chromosome 14.
25561468	3	19	part_of	β4-strands	490:499	arg1	the mature ectodomain	4		the mature ectodomain		PUBTATOR	Site	4	10381	ectodomain	Structural studies indicated that β2- or β4-strands in the mature ectodomain (ME ICA512) form dimers in vitro.
25561468	3	50	part_of	β2-	483:485	arg1	the mature ectodomain	2		the mature ectodomain		PUBTATOR	Site	2	10242	ectodomain	Structural studies indicated that β2- or β4-strands in the mature ectodomain (ME ICA512) form dimers in vitro.
2737288	3	17	gly	glycosylated	389:400	arg1	only Asn-86			only Asn-86						Asn-86	The results demonstrate that only Asn-86 is glycosylated.
20739279	12	34	gly	N-glycosylation	1524:1538	arg1	SynCAM proteins	SynCAM proteins				PUBTATOR		SynCAM proteins	23705		These results demonstrate that N-glycosylation of SynCAM proteins differentially affects their binding interface and implicate post-translational modification as a mechanism to regulate trans-synaptic adhesion.
8323299	2	90	part_of	lamp-2	429:434	arg1	the hinge-like regions	lamp-2		the hinge-like regions		PUBTATOR	Site	lamp-2	3920	regions	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	2	93	part_of	lamp-1	418:423	arg1	the hinge-like regions	lamp-1		the hinge-like regions		PUBTATOR	Site	lamp-1	3916	regions	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
12911312	4	13	gly	N-glycosylation	506:520	arg2	the potential N-glycosylation sites			the potential N-glycosylation sites						sites	Of the potential N-glycosylation sites, three located at residues 64, 155, and 169 were occupied, while the two at residues 351 and 356 were not occupied.
12911312	4	44	gly	occupied	634:641	arg2	the two at residues 351 and 356			the two at residues 351 and 356						residues 351 and 356	Of the potential N-glycosylation sites, three located at residues 64, 155, and 169 were occupied, while the two at residues 351 and 356 were not occupied.
2059624	2	75	gly	oligosaccharides	441:456	arg1	Asn289			Asn289	Asn289		AminoAcid			Asn289	Previous studies from this laboratory have established that lepidopteran insect cells possess the glycosylation machinery needed to assemble N-linked complex-type oligosaccharides on Asn289 of recombinant human plasminogen (r-HPg).
2386787	2	14	gly	contained	731:739	arg1	the human plasma protein AND only bisialo-biantennary complex-type carbohydrate and asialo-biantennary complex carbohydrate	protein			only bisialo-biantennary complex-type carbohydrate and asialo-biantennary complex carbohydrate	Fterm		protein			Using anion-exchange liquid chromatography mapping of the oligosaccharide units cleaved from the proteins by glycopeptidase F, compared with elution positions of standard oligosaccharide structures, coupled with monosaccharide compositional analysis, we find that the human plasma protein contained only bisialo-biantennary complex-type carbohydrate and asialo-biantennary complex carbohydrate, confirming earlier work published by this laboratory.
22159084	10	58	gly	Deglycosylation	1249:1263	arg1	SLC26A3	SLC26A3				PUBTATOR		SLC26A3	1811		Deglycosylation of SLC26A3 causes a defect in cell surface processing with decreased cell surface expression.
23829323	8	53	part_of	N-linked	1760:1767	arg1	the four haptoglobin N-linked glycosylation sites	haptoglobin N-linked		the four haptoglobin N-linked glycosylation sites		PUBTATOR	Site	haptoglobin N-linked	3240	sites	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	8	109	part_of	haptoglobin	1748:1758	arg1	the four haptoglobin N-linked glycosylation sites	haptoglobin N-linked		the four haptoglobin N-linked glycosylation sites		PUBTATOR	Site	haptoglobin N-linked	3240	sites	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
18533687	0	29	part_of	receptor	72:79	arg1	the N-linked glycosylation sites	receptor		the N-linked glycosylation sites		Fterm	Site	receptor		sites	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
11320094	5	23	part_of	multi-spanning	1134:1147	arg1	the second multi-spanning membrane domain	multi		the second multi-spanning membrane domain		OGER	Site	multi		domain	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	81	part_of	multi-spanning	994:1007	arg1	the first multi-spanning membrane domain	multi		the first multi-spanning membrane domain		OGER	Site	multi		domain	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
2403553	2	73	gly	receptor	249:256	arg1	the N-linked oligosaccharides	receptor			the N-linked oligosaccharides	Fterm		receptor			During our studies on the structures of the N-linked oligosaccharides of the receptor, we discovered that the receptor contains O-linked oligosaccharides.
2403553	2	49	gly	contains	291:298	arg1	the receptor AND O-linked oligosaccharides	the receptor			O-linked oligosaccharides	Fterm		receptor			During our studies on the structures of the N-linked oligosaccharides of the receptor, we discovered that the receptor contains O-linked oligosaccharides.
1731338	7	36	gly	galactoglycoprotein	1273:1291	arg1	125I-labeled galactoglycoprotein	125I-labeled galactoglycoprotein				PUBTATOR		125I-labeled galactoglycoprotein	6693		Further support of the relatedness of these molecules was obtained by immunoprecipitation of 125I-labeled galactoglycoprotein by monoclonal anti-CD43 antibodies.
2387072	3	60	gly	attached	861:868	arg1	asparagine AND the N-acetylglucosamine			asparagine	the N-acetylglucosamine					asparagine	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	3	85	gly	glycopeptides	692:704	arg2	The CF derived glycopeptides			The CF derived glycopeptides						glycopeptides	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
1533633	11	23	gly	nonglycosylated	1656:1670	arg1	the nonglycosylated, misfolded alpha-subunit	the nonglycosylated, misfolded alpha-subunit				OGER		subunit	P06865		The properties of the nonglycosylated, misfolded alpha-subunit were similar to some mutant alpha-subunits in Tay-Sachs disease patients.
24103369	8	49	gly	sialylated	1306:1315	arg1	the sialylated and fucosylated glycoforms				the sialylated and fucosylated glycoforms						Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	52	gly	fucosylated	1321:1331	arg1	the sialylated and fucosylated glycoforms				the sialylated and fucosylated glycoforms						Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
15869464	0	50	part_of	osteopontin	55:65	arg1	Post-translationally modified residues	osteopontin		Post-translationally modified residues		PUBTATOR	Site	osteopontin	6696	residues	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
10207177	1	109	part_of	regions	359:365	arg1	other proteins	proteins		regions		Fterm		proteins			Most cell surface molecules are glycoproteins consisting of linear arrays of globular domains containing stretches of amino acid sequence with similarities to regions in other proteins.
7776966	0	83	part_of	sites	22:26	arg1	the follicle-stimulating hormone (FSH) receptor	follicle-stimulating hormone (FSH) receptor		sites		PUBTATOR	Site	follicle-stimulating hormone (FSH) receptor	2492	sites	Identification of the sites of N-linked glycosylation on the follicle-stimulating hormone (FSH) receptor and assessment of their role in FSH receptor function.
18514042	5	1	gly	heterogeneity	874:886	arg1	the assigned glycopeptides			the assigned glycopeptides	the assigned glycopeptides		Site			glycopeptides	Mass spectrometric carbohydrate heterogeneity in the assigned glycopeptides was analyzed by an additional LC/MS.
18514042	5	13	gly	glycopeptides	904:916	arg2	the assigned glycopeptides			the assigned glycopeptides						glycopeptides	Mass spectrometric carbohydrate heterogeneity in the assigned glycopeptides was analyzed by an additional LC/MS.
21317871	4	23	part_of	GluRs	647:651	arg1	unconstrained lower clamshell lobes	GluRs		unconstrained lower clamshell lobes		OGER	Site	GluRs	Q5JPH6	lobes	GluA3 features a zipped-open dimer interface with unconstrained lower clamshell lobes, reminiscent of metabotropic GluRs (mGluRs).
2033371	8	10	gly	oligosaccharide	1615:1629	arg1	CD43	CD43			oligosaccharide	PUBTATOR		CD43	6693		Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
7681597	10	13	gly	glycosylated	1390:1401	arg1	three consecutive glycosylated Ser/Thr residues			three consecutive glycosylated Ser/Thr residues						residues	The structure consisting of three consecutive glycosylated Ser/Thr residues may be essential for Tn antigenicity in the light of previous results for ovine submaxillary mucin.
16766521	7	18	part_of	protein	1502:1508	arg1	a novel hydrophobic receptor domain	protein		a novel hydrophobic receptor domain		Fterm	Site	protein		domain	Taken together, our results identify a novel hydrophobic receptor domain in the family of the heptahelical G protein-coupled receptors and the first pseudo signal peptide of a eukaryotic membrane protein.
16766521	7	18	part_of	protein	1502:1508	arg1	the first pseudo signal peptide	protein		the first pseudo signal peptide		Fterm	Site	protein		peptide	Taken together, our results identify a novel hydrophobic receptor domain in the family of the heptahelical G protein-coupled receptors and the first pseudo signal peptide of a eukaryotic membrane protein.
16766521	7	44	part_of	receptor	1363:1370	arg1	a novel hydrophobic receptor domain	receptor		a novel hydrophobic receptor domain		Fterm	Site	receptor		domain	Taken together, our results identify a novel hydrophobic receptor domain in the family of the heptahelical G protein-coupled receptors and the first pseudo signal peptide of a eukaryotic membrane protein.
15084671	5	39	gly	glycosylation	684:696	arg2	33 glycosylation sites			33 glycosylation sites						sites	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	5	21	gly	carrying	616:623	arg1	asparagine residues AND glycan moieties by (18)O			asparagine residues	glycan moieties by (18)O					asparagine residues	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
27966990	8	48	gly	N-glycosylation	1484:1498	arg2	N-glycosylation site occupancy			N-glycosylation site occupancy						site	The data presented here provide direct evidence for site-specific, heterogeneous N-glycosylation and N-glycosylation site occupancy on VEGFR-2.
7599134	2	0	gly	attached	378:385	arg1	asparagines 96, 135, 155, and 192 AND four N-linked oligosaccharides			asparagines 96, 135, 155, and 192	four N-linked oligosaccharides					asparagines 96, 135, 155, and 192	The alpha-ATIII isoform has four N-linked oligosaccharides attached to asparagines 96, 135, 155, and 192.
7599134	2	9	gly	has	343:345	arg1	The alpha-ATIII isoform AND four N-linked oligosaccharides	The alpha-ATIII isoform			four N-linked oligosaccharides	PUBTATOR		ATIII isoform	462		The alpha-ATIII isoform has four N-linked oligosaccharides attached to asparagines 96, 135, 155, and 192.
18787108	3	38	part_of	adiponectin	549:559	arg1	its globular C1q domain	adiponectin		its globular C1q domain		PUBTATOR	Site	adiponectin	11450	domain	Of all the CTRP paralogs, CTRP9 shows the highest degree of amino acid identity to adiponectin in its globular C1q domain.
18787108	3	80	part_of	C1q	577:579	arg1	its globular C1q domain	C1q		its globular C1q domain		OGER	Site	C1q		domain	Of all the CTRP paralogs, CTRP9 shows the highest degree of amino acid identity to adiponectin in its globular C1q domain.
10074346	0	33	part_of	fibrin	62:67	arg1	fragments D and double-D	fibrin		fragments D and double-D		Fterm	Site	fibrin		fragments	Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide.
18780401	8	41	gly	glycoproteins	1207:1219	arg1	The glycoproteins	The glycoproteins				Fterm		glycoproteins			The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
9449027	5	80	gly	nonfucosylated	1290:1303	arg1	nonfucosylated, mono- and biantennary N-linked structures				nonfucosylated, mono- and biantennary N-linked structures						In the carbohydrate moiety, alpha-subunit from normal pregnancy hCG contained nonfucosylated, mono- and biantennary N-linked structures (49.3 and 36.7%, means); fucosylated biantennary and triantennary oligosaccharides were also identified (7.3 and 6.9%).
9449027	5	139	gly	fucosylated	1373:1383	arg1	fucosylated biantennary and triantennary oligosaccharides				fucosylated biantennary and triantennary oligosaccharides						In the carbohydrate moiety, alpha-subunit from normal pregnancy hCG contained nonfucosylated, mono- and biantennary N-linked structures (49.3 and 36.7%, means); fucosylated biantennary and triantennary oligosaccharides were also identified (7.3 and 6.9%).
9449027	5	22	gly	contained	1280:1288	arg1	alpha-subunit AND nonfucosylated, mono- and biantennary N-linked structures	alpha-subunit			nonfucosylated, mono- and biantennary N-linked structures	Fterm		alpha-subunit			In the carbohydrate moiety, alpha-subunit from normal pregnancy hCG contained nonfucosylated, mono- and biantennary N-linked structures (49.3 and 36.7%, means); fucosylated biantennary and triantennary oligosaccharides were also identified (7.3 and 6.9%).
8243461	2	29	gly	chains	474:479	arg1	these peptides			these peptides	these peptides		Site			peptides	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	2	71	gly	peptides	490:497	arg1	the O-linked oligosaccharide chains			peptides	the O-linked oligosaccharide chains					peptides	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	2	106	gly	glycopeptides	308:320	arg2	protease-digested glycopeptides			protease-digested glycopeptides						glycopeptides	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
19196183	4	42	gly	glycopeptides	501:513	arg2	glycopeptides			glycopeptides						glycopeptides	For the enrichment of glycopeptides, capture methods with hydrophilic affinity (HA) and hydrazide chemistry (HC) were used complementarily.
8702538	8	84	part_of	motifs	1291:1296	arg1	the first or second Ig domains	motifs		the first or second Ig domains						domains	Site-directed mutagenesis of similar NC(T/S) motifs in the first or second Ig domains of the I-type lectins myelin-associated glycoprotein, and sialoadhesin did not disrupt their ability to mediate sialic acid binding.
14658030	3	59	gly	glycosylated	1004:1015	arg1	consensus sequences			consensus sequences						sequences	Several recent reports have established that mass spectrometric techniques such as matrix-assisted laser desorption/ionization or electrospray ionization mass spectrometry (MALDI-TOF or ESI-MS, respectively) with or without preceding HPLC and in combination with PNGase F treatment are suited to analyze whether consensus sequences for N-glycosylation are glycosylated or not.
9169007	6	51	gly	variants	782:789	arg1	Heparin-agarose chromatography	antithrombin variants			Heparin-agarose chromatography	PUBTATOR		antithrombin variants	462		Heparin-agarose chromatography of the four antithrombin variants revealed that Gln 96, Gln 135, and Gln 192 variants still displayed the two functional heparin-affinity forms previously observed with the wild-type inhibitor, whereas the Gln 155 variant showed only a single functional high heparin affinity form.
20006580	1	5	gly	N-glycosylation	171:185	arg2	one or two N-glycosylation consensus sites			one or two N-glycosylation consensus sites						sites	Within the first external loop of mouse and human TRESK subunits one or two N-glycosylation consensus sites were identified, respectively.
2113054	6	5	gly	glycosylation	1171:1183	arg1	sCD4	sCD4				PUBTATOR		sCD4	499358		The role of glycosylation in the expression of sCD4 was investigated by mutagenesis of the constructs to remove each of the two N-linked glycosylation sites in turn and both together.
2113054	6	39	gly	glycosylation	1296:1308	arg2	the two N-linked glycosylation sites			the two N-linked glycosylation sites						sites	The role of glycosylation in the expression of sCD4 was investigated by mutagenesis of the constructs to remove each of the two N-linked glycosylation sites in turn and both together.
20473317	2	44	part_of	RET	349:351	arg1	two N-terminal cadherin-like domains	RET		two N-terminal cadherin-like domains		PUBTATOR	Site	RET	5979	domains	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
18929574	5	20	part_of	epitope	788:794	arg1	CD8beta	CD8beta		epitope		PUBTATOR	Site	CD8beta	12526	epitope	The YTS156.7 epitope on CD8beta was identified and implies that residues in the CDR1 and CDR2-equivalent loops of CD8beta are occluded upon binding to class I pMHC.
18929574	5	60	part_of	residues	839:846	arg1	CDR1	CDR1		residues		PUBTATOR	AminoAcid	CDR1	P51861	residues in	The YTS156.7 epitope on CD8beta was identified and implies that residues in the CDR1 and CDR2-equivalent loops of CD8beta are occluded upon binding to class I pMHC.
17652170	3	39	part_of	receptor	506:513	arg1	the largest cytokine receptor fragment	receptor		the largest cytokine receptor fragment		Fterm	Site	receptor		fragment	The structure is, to date, the largest cytokine receptor fragment determined by x-ray crystallography.
16445295	6	43	gly	unglycosylated	984:997	arg1	an unglycosylated variant	an unglycosylated variant				Fterm		variant			Asn219 was also found in an unglycosylated variant.
14693913	6	60	gly	occupied	1100:1107	arg2	these sites			these sites						sites	Using hBSSL as a platform to study Pichia's O-glycosylation capabilities, we found that nearly all of these sites were occupied by mannose-containing O-glycans, whose structures, after beta-elimination and purification, were assigned by (1)H NMR and, in some cases, by linkage-specific exoglycosidases and methylation analysis.
17956937	8	26	part_of	PSA	1864:1866	arg1	the N-glycosylation site	PSA		the N-glycosylation site		PUBTATOR	Site	PSA	354	site	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
23039992	4	21	part_of	OPG	624:626	arg1	the monomeric cytokine-binding region	OPG		the monomeric cytokine-binding region		PUBTATOR	Site	OPG	4982	region	Complementary biochemical and functional studies reveal that the monomeric cytokine-binding region of OPG binds RANKL with ∼500-fold higher affinity than RANK and inhibits RANKL-stimulated osteoclastogenesis ∼150 times more effectively, in part because the binding cleft of RANKL makes unique contacts with OPG.
12144777	1	21	gly	glycoprotein	125:136	arg1	Human renal dipeptidase	Human renal dipeptidase				PUBTATOR		renal dipeptidase	1800		Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics.
12144777	1	21	gly	glycoprotein	125:136	arg1	a membrane-bound glycoprotein	a membrane-bound glycoprotein				Fterm		glycoprotein			Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics.
9295302	8	74	gly	modified	1378:1385	arg3	Asn1006 AND N-linked oligosaccharides			Asn1006	N-linked oligosaccharides					Asn1006	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	8	74	gly	modified	1378:1385	arg3	the only sites AND N-linked oligosaccharides			the only sites	N-linked oligosaccharides					sites	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	8	74	gly	modified	1378:1385	arg3	Asn23 AND N-linked oligosaccharides			Asn19 and Asn23	N-linked oligosaccharides					Asn19 and Asn23	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
22629392	5	6	gly	Thr	1007:1009	arg1	O-GlcNAcylations			Thr 305 and Thr 312	O-GlcNAcylations					Thr 305 and Thr 312	Further studies utilizing mass spectrometry and mutagenesis approaches showed that O-GlcNAcylations at Thr 305 and Thr 312 inhibited Akt phosphorylation at Thr 308 via disrupting the interaction between Akt and PDK1.
22629392	5	15	gly	Thr	1019:1021	arg1	O-GlcNAcylations			Thr 305 and Thr 312	O-GlcNAcylations					Thr 305 and Thr 312	Further studies utilizing mass spectrometry and mutagenesis approaches showed that O-GlcNAcylations at Thr 305 and Thr 312 inhibited Akt phosphorylation at Thr 308 via disrupting the interaction between Akt and PDK1.
3934016	3	8	gly	nonglycosylated	573:587	arg1	angiotensinogen	angiotensinogen				PUBTATOR		angiotensinogen	183		35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	3	14	gly	glycosylated	556:567	arg1	angiotensinogen	angiotensinogen				PUBTATOR		angiotensinogen	183		35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
15504740	8	15	gly	glycosylation	1496:1508	arg2	asparagine-linked glycosylation sites			asparagine-linked glycosylation sites						sites	The data show that Asn-365 and Asn-392 are extracellular and that the introduction of asparagine-linked glycosylation sites at His-72, Ala-81, Tyr-414, and Tyr-423 leads to an increase in molecular mass consistent with an extracellular apposition.
1908233	5	2	gly	Thr-O-glycosylation	865:883	arg1	O-glycosylated proteins	O-glycosylated proteins				Fterm		proteins			This motif predicts the site(s) of Pro- associated Thr-O-glycosylation in O-glycosylated proteins, although it is clear that there are also other forms of Thr-O-glycosylation not associated with Pro.
1908233	5	29	gly	O-glycosylated	888:901	arg1	O-glycosylated proteins	O-glycosylated proteins				Fterm		proteins			This motif predicts the site(s) of Pro- associated Thr-O-glycosylation in O-glycosylated proteins, although it is clear that there are also other forms of Thr-O-glycosylation not associated with Pro.
18491227	8	40	gly	E-cadherin	1305:1314	arg1	N-glycans	E-cadherin			N-glycans	PUBTATOR		E-cadherin	999		Furthermore, we found that N-glycans of M4 E-cadherin were modified in immature high mannose type, suggesting that it could not depart to Golgi apparatus.
18787108	6	57	gly	glycosylated	995:1006	arg1	hydroxylated and glycosylated lysines			hydroxylated and glycosylated lysines						lysines	CTRP9 is a secreted glycoprotein with multiple post-translational modifications in its collagen domain that include hydroxylated prolines and hydroxylated and glycosylated lysines.
18787108	6	69	gly	glycoprotein	856:867	arg1	a secreted glycoprotein	a secreted glycoprotein				Fterm		glycoprotein			CTRP9 is a secreted glycoprotein with multiple post-translational modifications in its collagen domain that include hydroxylated prolines and hydroxylated and glycosylated lysines.
18787108	6	69	gly	glycoprotein	856:867	arg1	CTRP9	CTRP9				PUBTATOR		CTRP9	239126		CTRP9 is a secreted glycoprotein with multiple post-translational modifications in its collagen domain that include hydroxylated prolines and hydroxylated and glycosylated lysines.
10201933	6	71	gly	glycosylation	933:945	arg2	the five potential N-linked glycosylation sites			the five potential N-linked glycosylation sites						sites	The RGD (Arg-Gly-Asp) cell attachment sequence and the five potential N-linked glycosylation sites were located on the membrane-anchoring form.
8329384	1	0	part_of	EGF	295:297	arg1	the N-terminal EGF domains	N-terminal EGF		the N-terminal EGF domains		OGER	Site	N-terminal EGF	P01133	domains	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	1	12	part_of	Cys-X-X-Gly-Gly-Thr/Ser-Cys	249:275	arg1	several coagulation/fibrinolytic proteins	proteins		Cys-X-X-Gly-Gly-Thr/Ser-Cys		Fterm	AminoAcid	proteins		Cys	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	1	22	part_of	proteins	343:350	arg1	the N-terminal EGF domains	proteins		the N-terminal EGF domains		Fterm	Site	proteins		domains	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	1	76	part_of	N-terminal	284:293	arg1	the N-terminal EGF domains	N-terminal EGF		the N-terminal EGF domains		OGER	Site	N-terminal EGF	P01133	domains	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
2243102	0	50	gly	glycoproteins	55:67	arg1	human lysosomal membrane glycoproteins	glycoproteins			The polylactosaminoglycans	Fterm		glycoproteins			The polylactosaminoglycans of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
3524673	1	49	part_of	factor	109:114	arg1	The complete amino acid sequence	von Willebrand factor		The complete amino acid sequence		PUBTATOR	Site	von Willebrand factor	7450	sequence	The complete amino acid sequence of human von Willebrand factor (vWF) is presented.
11805077	1	15	gly	carbohydrates	292:304	arg1	glycoproteins	glycoproteins			carbohydrates	Fterm		glycoproteins			We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	1	50	gly	glycoproteins	309:321	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
8329384	0	26	part_of	IX	165:166	arg1	serine 61	factor IX		serine 61		OGER	SpecificSite	factor IX	P00740	serine 61	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
25187573	12	53	gly	glycosylation	2036:2048	arg2	These glycosylation sites			These glycosylation sites						sites	These glycosylation sites were focused in the central STP-rich region, giving the domain a negative charge.
19508227	1	2	gly	N-glycosylation	242:256	arg2	all four potential N-glycosylation sites			all four potential N-glycosylation sites						sites	We showed that Tspan-1, a tetraspanin overexpressed in many human cancers, harbours oligosaccharides at all four potential N-glycosylation sites.
19864504	3	48	gly	enzyme	464:469	arg1	N-linked oligosaccharide-mediated delivery	enzyme			N-linked oligosaccharide-mediated delivery	Fterm		enzyme			This therapy depends on N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells.
23302862	0	29	part_of	site	40:43	arg1	the insulin receptor	insulin receptor		site		PUBTATOR	Site	insulin receptor	3630	site	How insulin engages its primary binding site on the insulin receptor.
25374123	7	60	gly	glycopeptides	1094:1106	arg2	glycopeptides			glycopeptides						glycopeptides	In HCD mode, oxonium ions were used for recognizing glycopeptides and y ions for sequencing the peptide backbone.
11544325	7	19	gly	glycosylation	1198:1210	arg1	hMD-2	hMD-2		Asn(26) and Asn(114)		PUBTATOR		hMD-2	23643	Asn(26) and Asn(114)	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	114			Asn(26) and Asn(114)						Asn(26) and Asn(114)	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	26			Asn(26) and Asn(114)						Asn(26) and Asn(114)	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	Asn			Asn(26) and Asn(114)						Asn(26) and Asn(114)	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	114	hMD-2		Asn(26) and Asn(114)		PUBTATOR		hMD-2	23643	Asn(26) and Asn(114)	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	26	hMD-2		Asn(26) and Asn(114)		PUBTATOR		hMD-2	23643	Asn(26) and Asn(114)	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	Asn	hMD-2		Asn(26) and Asn(114)		PUBTATOR		hMD-2	23643	Asn(26) and Asn(114)	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	26			Asn(26) and Asn(114)						Asn(26) and Asn(114)	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	Asn			Asn(26) and Asn(114)						Asn(26) and Asn(114)	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	Asn			Asn(26) and Asn(114)						Asn(26) and Asn(114)	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
15093539	1	28	part_of	receptor	199:206	arg1	the extracellular domain	epidermal growth factor receptor 2		the extracellular domain		PUBTATOR	Site	epidermal growth factor receptor 2	2064	domain	We have determined the 3.2 A X-ray crystal structure of the extracellular domain of the human epidermal growth factor receptor 2 (ErbB2 or HER2) in a complex with the antigen binding fragment of pertuzumab, an anti-ErbB2 monoclonal antibody also known as 2C4 or Omnitarg.
14749323	7	48	gly	deglycosylation	1232:1246	arg1	Asp-39			Asp-39						Asp-39	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14693913	3	51	gly	N-glycosylation	445:459	arg2	Asn187			Asn187						Asn187	hBSSL has one N-glycosylation site at Asn187, which was 38-40% occupied with a Man(10)GlcNAc(2) structure defined previously in Pichia as the oligosaccharide-lipid form of Man(9)GlcNAc(2) trimmed of the middle-arm terminal alpha 1,2-Man and elongated with Man alpha 1,2Man alpha 1,6-disaccharide attached to the lower-arm core alpha 1,3-Man (Trimble et al. [1991], J. Biol.
14693913	3	51	gly	N-glycosylation	445:459	arg2	one N-glycosylation site			one N-glycosylation site						site	hBSSL has one N-glycosylation site at Asn187, which was 38-40% occupied with a Man(10)GlcNAc(2) structure defined previously in Pichia as the oligosaccharide-lipid form of Man(9)GlcNAc(2) trimmed of the middle-arm terminal alpha 1,2-Man and elongated with Man alpha 1,2Man alpha 1,6-disaccharide attached to the lower-arm core alpha 1,3-Man (Trimble et al. [1991], J. Biol.
9334252	1	1	gly	urine	168:172	arg1	RNase 2	RNase 2			urine	PUBTATOR		RNase 2	6036		C2-alpha-Mannosyltryptophan was discovered in RNase 2 from human urine, representing a novel way of attaching carbohydrate to a protein.
18536718	3	32	part_of	site	471:474	arg1	C5	C5		site		PUBTATOR	Site	C5	727	site	However, in contrast to C3, the convertase cleavage site in C5 was ordered and the C345C domain flexibly attached to the core of C5.
8627329	2	35	gly	O-glycosylated	204:217	arg1	An O-glycosylated peptide			An O-glycosylated peptide						peptide	An O-glycosylated peptide connects the ligand-binding domain of NTR to its transmembrane helix.
3497398	11	5	part_of	protein	1698:1704	arg1	This protein sequence	protein		This protein sequence		Fterm	Site	protein		sequence	This protein sequence agrees completely with that deduced from the cDNA sequence reported by Lopez et al. [Lopez, J.A., Chung, D.W., Fujikawa, K., Hagen, F.S., Papayannopoulou, T. & Roth, G.J. (1987) Proc.
11788899	7	22	part_of	WNT8B	910:914	arg1	Gly230	WNT8B		Gly230 and Arg284		PUBTATOR	AminoAcid	WNT8B	7479	Gly230 and Arg284	Gly230 and Arg284 of WNT8B were conserved in WNT8A.
2642896	8	52	gly	glycosylated	990:1001	arg1	Both sites			Both sites						sites	Both sites were considered to be glycosylated with carbohydrate chains of Mr 3,000, since two smaller proteins with Mr 23,000 and 20,000 were found during deglycosylation of the purified enzyme (Mr 26,000) with N-glycanase.
2642896	8	81	gly	deglycosylation	1112:1126	arg1	the purified enzyme	the purified enzyme				Fterm		enzyme			Both sites were considered to be glycosylated with carbohydrate chains of Mr 3,000, since two smaller proteins with Mr 23,000 and 20,000 were found during deglycosylation of the purified enzyme (Mr 26,000) with N-glycanase.
3524673	7	36	gly	containing	557:566	arg1	2050 amino acid residues AND 10 Thr/Ser-linked oligosaccharide chains			2050 amino acid residues	10 Thr/Ser-linked oligosaccharide chains					residues	The protein is composed of 2050 amino acid residues containing 12 Asn-linked and 10 Thr/Ser-linked oligosaccharide chains.
11904304	3	0	part_of	Thr-58	677:682	arg1	c-Myc	c-Myc		Thr-58		PUBTATOR	SpecificSite	c-Myc	4609	Thr-58	One antibody specifically reacts with the Thr-58-glycosylated form of c-Myc, and the other reacts only with unmodified Thr-58 in c-Myc.
10894551	4	40	gly	glycosylated	532:543	arg1	the glycosylated dimerized hormone-binding domain	ANP receptor		domain		OGER		ANP receptor	P01160	domain	Here we present the crystal structure of the glycosylated dimerized hormone-binding domain of the ANP receptor at 2.0-A resolution.
15869464	6	22	part_of	CKII	1390:1393	arg1	the motif	CKII		the motif		PUBTATOR	Site	CKII	1457	motif	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	63	part_of	motif	1366:1370	arg1	positioned	motif		positioned						position	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	102	part_of	CKII	1262:1265	arg1	the target sequence	CKII		the target sequence		PUBTATOR	Site	CKII	1457	sequence	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
19864504	10	34	gly	released	1454:1461	arg1	the three glycosylation sites AND the N-glycans			the three glycosylation sites	the N-glycans					sites	Notably, roughly one-third of the N-glycans released from the three glycosylation sites were fucosylated.
19864504	10	47	gly	fucosylated	1503:1513	arg1	the N-glycans				the N-glycans						Notably, roughly one-third of the N-glycans released from the three glycosylation sites were fucosylated.
19864504	10	83	gly	glycosylation	1478:1490	arg2	the three glycosylation sites			the three glycosylation sites						sites	Notably, roughly one-third of the N-glycans released from the three glycosylation sites were fucosylated.
9169007	5	76	gly	glycosylation	621:633	arg2	the four Asn residue sites			the four Asn residue sites						Asn residue sites	To determine the source of the glycosylation heterogeneity responsible for these different heparin-affinity forms, each of the four Asn residue sites of glycosylation, residues 96, 135, 155, and 192, was mutated to Gln to block glycosylation at these sites.
9169007	5	54	gly	glycosylation	696:708	arg2	these sites			sites						sites	To determine the source of the glycosylation heterogeneity responsible for these different heparin-affinity forms, each of the four Asn residue sites of glycosylation, residues 96, 135, 155, and 192, was mutated to Gln to block glycosylation at these sites.
14658030	0	82	gly	N-glycosylation	18:32	arg2	N-glycosylation sites	NCAM		sites		PUBTATOR		NCAM	17967	sites	Identification of N-glycosylation sites of the murine neural cell adhesion molecule NCAM by MALDI-TOF and MALDI-FTICR mass spectrometry.
2243102	5	51	gly	glycopeptides	747:759	arg2	isolated glycopeptides			isolated glycopeptides						glycopeptides	The poly-N-acetyllactosaminyl structures of isolated glycopeptides were confirmed by the susceptibility of their released oligosaccharides to endo-beta-galactosidase.
24967714	1	15	gly	glycoprotein	212:223	arg1	the HIV-1 glycoprotein gp120	the HIV-1 glycoprotein gp120				Fterm		glycoprotein			N-linked glycans covering the surface of the HIV-1 glycoprotein gp120 are of major importance for the correct folding of this glycoprotein.
24967714	1	80	gly	glycoprotein	287:298	arg1	this glycoprotein	this glycoprotein				Fterm		glycoprotein			N-linked glycans covering the surface of the HIV-1 glycoprotein gp120 are of major importance for the correct folding of this glycoprotein.
16732286	0	27	part_of	receptor	31:38	arg1	the Tie2 receptor ectodomain	Tie2 receptor		the Tie2 receptor ectodomain		PUBTATOR	Site	Tie2 receptor	7010	ectodomain	Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex.
16732286	0	31	part_of	Tie2	26:29	arg1	the Tie2 receptor ectodomain	Tie2 receptor		the Tie2 receptor ectodomain		PUBTATOR	Site	Tie2 receptor	7010	ectodomain	Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex.
3356193	7	78	gly	sialylated	1009:1018	arg1	an identical Gal beta 1----3GalNAc core				an identical Gal beta 1----3GalNAc core						The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
1740433	8	71	gly	glycosylation	1178:1190	arg2	a NSS tripeptide			a NSS tripeptide						tripeptide	The C-SAA octapeptide specifies the first two residues of a NSS tripeptide, the only potential N-linked glycosylation site in the molecule.
1740433	8	71	gly	glycosylation	1178:1190	arg2	the only potential N-linked glycosylation site			the only potential N-linked glycosylation site						site	The C-SAA octapeptide specifies the first two residues of a NSS tripeptide, the only potential N-linked glycosylation site in the molecule.
2808371	1	6	gly	possesses	174:182	arg1	a cytoplasmic protein AND a protein-saccharide modification structure	a cytoplasmic protein			a protein-saccharide modification structure	Fterm		protein			Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	1	6	gly	possesses	174:182	arg1	a cytoplasmic protein AND an O-N-acetyl-D-glucosamine (GlcNAc) moiety	a cytoplasmic protein			an O-N-acetyl-D-glucosamine (GlcNAc) moiety	Fterm		protein			Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	1	6	gly	possesses	174:182	arg1	Erythrocyte protein 4.1 AND a protein-saccharide modification structure	Erythrocyte protein 4.1			a protein-saccharide modification structure	PUBTATOR		protein 4.1	281753		Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	1	6	gly	possesses	174:182	arg1	Erythrocyte protein 4.1 AND an O-N-acetyl-D-glucosamine (GlcNAc) moiety	Erythrocyte protein 4.1			an O-N-acetyl-D-glucosamine (GlcNAc) moiety	PUBTATOR		protein 4.1	281753		Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
21932778	9	20	gly	occupied	1683:1690	arg2	the potential N-glycosylation sites			the potential N-glycosylation sites						sites	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	9	45	gly	glycans	1714:1720	arg1	glypican-1	glypican-1			glycans	PUBTATOR		glypican-1	2817		In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	9	72	gly	N-glycosylation	1632:1646	arg2	the potential N-glycosylation sites			the potential N-glycosylation sites						sites	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
10889209	0	43	gly	Glycosylation	0:12	arg2	Asn119	GIRK1		Asn119		PUBTATOR		GIRK1	3760	Asn119	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
14749323	10	96	gly	glycosylation	1816:1828	arg1	individual sites	OAT1		sites		PUBTATOR		OAT1	9356	sites	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	10	96	gly	glycosylation	1816:1828	arg2	individual sites	OAT1		sites		PUBTATOR		OAT1	9356	sites	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	10	96	gly	glycosylation	1816:1828	arg2	individual sites			sites						sites	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
18729387	11	102	gly	occupied	1785:1792	arg2	The first Ig domains			The first Ig domains						domains	The first Ig domains were occupied by Man-5-9.
19088065	6	94	gly	N-glycosylation	668:682	arg1	this protein	this protein				Fterm		protein			Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
20624874	6	11	part_of	pADAMTS13	945:953	arg1	Cleavage sites	pADAMTS13		Cleavage sites		Cterm	Site	pADAMTS13	11093	sites	Cleavage sites of the purified pADAMTS13 by three proteases were identified; thrombin cleaved the four peptidyl bonds between Arg257-Ala258, Arg459-Ser460, Arg888-Thr889 and Arg1176-Arg1177, plasmin cleaved the three peptidyl bonds between Arg257-Ala258, Arg888-Thr889 and Arg1176-Arg1177, and elastase cleaved the two peptidyl bonds between Ile380-Ala381 and Thr874-Ser875.
1388166	7	4	gly	Asn-linked	1450:1459	arg1	sulfated Asn-linked oligosaccharides			Asn	sulfated Asn-linked oligosaccharides					Asn	Chinese hamster ovary (CHO) cells do not contain detectable levels of either transferase and rTFPI expressed in CHO cells does not contain sulfated Asn-linked oligosaccharides.
25802287	8	70	gly	deglycosylated	1269:1282	arg1	the deglycosylated peptide			the deglycosylated peptide						peptide	Furthermore, the deglycosylated peptide can be sequenced efficiently in a simple collision-induced dissociation-MS experiment.
20484118	4	6	part_of	PLN	697:699	arg1	the site	PLN		the site		PUBTATOR	Site	PLN	64672	site	Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation.
20484118	4	6	part_of	PLN	697:699	arg1	Ser	PLN		Ser(16)		PUBTATOR	SpecificSite	PLN	64672	Ser(16)	Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation.
18795891	3	6	part_of	tetraspanin	539:549	arg1	tetraspanin microdomains	tetraspanin		tetraspanin microdomains		Fterm	Site	tetraspanin		microdomains	However, our understanding of how tetraspanin microdomains regulate platelets is hindered by the fact that only four of the 33 mammalian tetraspanins have been identified in platelets.
7106126	5	39	gly	sialoglycoproteins	910:927	arg1	the MN and Ss erythrocyte membrane sialoglycoproteins	the MN and Ss erythrocyte membrane sialoglycoproteins				Fterm		sialoglycoproteins			In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
14718370	10	38	part_of	MUC5AC	1642:1647	arg1	the Cys subdomains	MUC5AC		the Cys subdomains		PUBTATOR	AminoAcid	MUC5AC	P98088	Cys subdomains	Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs.
14718370	10	49	part_of	MUC5B	1653:1657	arg1	the Cys subdomains	MUC5B		the Cys subdomains		PUBTATOR	AminoAcid	MUC5B	Q9HC84	Cys subdomains	Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs.
14718370	10	68	part_of	motifs	1703:1708	arg1	MUC5B	MUC5B		motifs		PUBTATOR	Site	MUC5B	Q9HC84	motifs	Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs.
14718370	10	68	part_of	motifs	1703:1708	arg1	MUC5AC	MUC5AC		motifs		PUBTATOR	Site	MUC5AC	P98088	motifs	Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs.
14718370	10	68	part_of	motifs	1703:1708	arg1	the Cys subdomains	motifs		the Cys subdomains						Cys subdomains	Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs.
7776966	7	102	gly	glycosylation	1056:1068	arg2	the actual sites	FSHR		sites		PUBTATOR		FSHR	2492	sites	Therefore, further experiments, done in the context of the full-length receptor, were performed to determine the actual sites of glycosylation in the FSHR as well as to elucidate their role in the functions of the FSHR.
15504740	5	69	gly	glycosylation	975:987	arg2	the five predicted endogenous asparagine-linked glycosylation sites			the five predicted endogenous asparagine-linked glycosylation sites						sites	We deleted the five predicted endogenous asparagine-linked glycosylation sites (Asn-Xaa-(Ser/Thr)) at Asn-22, Asn-365, Asn-392, Asn-478, and Asn-487 to map the extracellular topology.
15504740	5	80	gly	sites	989:993	arg1	Ser/Thr			Ser/Thr						Ser/Thr	We deleted the five predicted endogenous asparagine-linked glycosylation sites (Asn-Xaa-(Ser/Thr)) at Asn-22, Asn-365, Asn-392, Asn-478, and Asn-487 to map the extracellular topology.
15504740	5	80	gly	sites	989:993	arg1	Asn-Xaa-			Asn-Xaa-						Asn	We deleted the five predicted endogenous asparagine-linked glycosylation sites (Asn-Xaa-(Ser/Thr)) at Asn-22, Asn-365, Asn-392, Asn-478, and Asn-487 to map the extracellular topology.
16368742	0	76	gly	Glycosylation	0:12	arg1	the osmoresponsive transient receptor potential channel TRPV4	the osmoresponsive transient receptor potential channel TRPV4				PUBTATOR		TRPV4	59341		Glycosylation of the osmoresponsive transient receptor potential channel TRPV4 on Asn-651 influences membrane trafficking.
11741940	4	2	part_of	proteins	824:831	arg1	homologous domains	proteins		homologous domains		Fterm	Site	proteins		domains	Numbering sFRP-1 cysteines sequentially from the N terminus, the five disulfide linkages in the Fz domain are 1-5, 2-4, 3-8, 6-10, and 7-9, consistent with the disulfide pattern determined for homologous domains of several other proteins.
11741940	4	112	part_of	sFRP-1	605:610	arg1	sFRP-1 cysteines	Numbering sFRP-1		sFRP-1 cysteines		PUBTATOR	AminoAcid	Numbering sFRP-1	6422	cysteines	Numbering sFRP-1 cysteines sequentially from the N terminus, the five disulfide linkages in the Fz domain are 1-5, 2-4, 3-8, 6-10, and 7-9, consistent with the disulfide pattern determined for homologous domains of several other proteins.
2793860	7	5	gly	O-glycosylated	1095:1108	arg1	the protein	the protein				Fterm		protein			The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	7	10	gly	nonglycosylated	1117:1131	arg1	the protein	the protein				Fterm		protein			The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
10066782	6	54	part_of	motifs	947:952	arg1	known Ig superfamily domains	motifs		known Ig superfamily domains						domains	The disulfides Cys102-Cys113 and Cys146-Cys157 are consistent with known cytokine-binding domain motifs, and Cys28-Cys77 with known Ig superfamily domains.
30127001	2	27	gly	domain	344:349	arg1	a novel O-linked hexose modification			domain	a novel O-linked hexose modification					domain	A recent structural analysis suggested that a novel O-linked hexose modification on serine 435 of the mammalian NOTCH1 core ligand-binding domain lies at the interface with its ligands.
30127001	2	32	gly	modification	273:284	arg1	serine 435			serine 435	serine 435		SpecificSite			serine 435	A recent structural analysis suggested that a novel O-linked hexose modification on serine 435 of the mammalian NOTCH1 core ligand-binding domain lies at the interface with its ligands.
30127001	2	74	gly	modification	273:284	arg1	the mammalian NOTCH1 core ligand-binding domain AND a novel O-linked hexose modification			the mammalian NOTCH1 core ligand-binding domain	a novel O-linked hexose modification					domain	A recent structural analysis suggested that a novel O-linked hexose modification on serine 435 of the mammalian NOTCH1 core ligand-binding domain lies at the interface with its ligands.
9030779	0	65	part_of	sphingomyelinase	71:86	arg1	the N-glycosylation sites	acid sphingomyelinase		the N-glycosylation sites		PUBTATOR	Site	acid sphingomyelinase	6609	sites	Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis.
25187573	11	29	gly	O-glycosylation	1970:1984	arg2	168 sites			168 sites						sites	The density of glycosylation was shown to be high: 168 sites of O-glycosylation, predominately sialylated, were identified.
25187573	11	108	gly	sialylated	2001:2010	arg1	168 sites			168 sites						sites	The density of glycosylation was shown to be high: 168 sites of O-glycosylation, predominately sialylated, were identified.
2361960	3	39	part_of	IL-5	522:525	arg1	human IL-5 cDNA sequence	IL-5		human IL-5 cDNA sequence		PUBTATOR	Site	IL-5	3567	sequence	After digestion with API, we could identify all the peptides which were expected from human IL-5 cDNA sequence.
19864504	0	73	gly	A	91:91	arg1	N-linked oligosaccharides	arylsulfatase A			N-linked oligosaccharides	PUBTATOR		arylsulfatase A	410		Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A produced in different cell lines.
15454184	5	21	gly	glycosylated	711:722	arg1	both N-glycosylation sites			both N-glycosylation sites						sites	Using mass spectrometric peptide/glycopeptide mapping and precursor-ion scanning, we found that both N-glycosylation sites were partially glycosylated.
15454184	5	56	gly	N-glycosylation	674:688	arg2	both N-glycosylation sites			both N-glycosylation sites						sites	Using mass spectrometric peptide/glycopeptide mapping and precursor-ion scanning, we found that both N-glycosylation sites were partially glycosylated.
15454184	5	76	gly	peptide/glycopeptide	598:617	arg2	mass spectrometric peptide/glycopeptide mapping			mass spectrometric peptide/glycopeptide mapping						peptide/glycopeptide	Using mass spectrometric peptide/glycopeptide mapping and precursor-ion scanning, we found that both N-glycosylation sites were partially glycosylated.
21669976	7	25	gly	glycoforms	1272:1281	arg1	the different KCNE1 glycoforms	the different KCNE1 glycoforms				PUBTATOR		KCNE1	3753		The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
7744025	1	75	gly	protein	351:357	arg1	one repeat	protein			one repeat	Fterm		protein			A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
17548821	3	36	part_of	Monomeric	544:552	arg1	Monomeric fragment	Monomeric		Monomeric fragment		Cterm	Site	Monomeric		fragment	Monomeric fragment exhibited a suboptimal level of signaling activity and artificial oligomerization resulted in a 10-fold increase in activity, indicating the critical importance of higher-order multimerization in physiological reelin.
19159218	5	84	gly	N-glycosites	906:917	arg2	many N-glycosites			many N-glycosites						N-glycosites	Thus many N-glycosites could not be localized if only trypsin was used to digest proteins.
16492764	3	26	part_of	GCSF-R	588:593	arg1	the cytokine receptor homologous domain	GCSF		the cytokine receptor homologous domain		PUBTATOR	Site	GCSF	12985	domain	The conformation of the complex is quite different from that between human GCSF and the cytokine receptor homologous domain of mouse GCSF-R, but similar to that of the IL-6/gp130 signaling complex.
8798614	8	32	gly	glycosylation	1532:1544	arg2	Asn18			Asn18						Asn18	These data suggest that the MAC inhibitory function of CD59 is entirely provided by residues exposed at the surface of the core polypeptide and that this core structure is not influenced by glycosylation at Asn18.
18420026	0	40	gly	N-glycosylation	55:69	arg2	a single N-glycosylation site			a single N-glycosylation site						site	Nectin-like molecule 1 is a glycoprotein with a single N-glycosylation site at N290KS which influences its adhesion activity.
18420026	0	60	gly	glycoprotein	28:39	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Nectin-like molecule 1 is a glycoprotein with a single N-glycosylation site at N290KS which influences its adhesion activity.
18420026	0	60	gly	glycoprotein	28:39	arg1	Nectin-like molecule 1	Nectin-like molecule 1				PUBTATOR		Nectin-like molecule 1	57863		Nectin-like molecule 1 is a glycoprotein with a single N-glycosylation site at N290KS which influences its adhesion activity.
30659065	10	52	gly	N-glycosylation	1818:1832	arg1	N92			N92						N92	In digests of the sera from a subset of donors, we detected an unmodified peptide containing a proline residue at position 93; this substitution would strongly disfavor N-glycosylation at N92.
7654718	4	66	part_of	C-tail	696:701	arg1	the purified C-tail fragment	C-tail		the purified C-tail fragment		Cterm	Site	C-tail		fragment	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	4	91	part_of	enzyme	770:775	arg1	residues 528-712	enzyme		residues 528-712		Fterm	SpecificSite	enzyme		residues 528-712	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
22601780	1	65	gly	glycoprotein	133:144	arg1	Developmental endothelial cell locus-1 (Del-1) glycoprotein	Developmental endothelial cell locus-1 (Del-1) glycoprotein				Fterm		glycoprotein			Developmental endothelial cell locus-1 (Del-1) glycoprotein is secreted by endothelial cells and a subset of macrophages.
8477709	1	9	part_of	erythropoietin	199:212	arg1	Ser126	erythropoietin		Ser126		PUBTATOR	AminoAcid	erythropoietin	2056	Ser126	The native structures of the Asn-linked oligosaccharides and the O-glycans at Ser126 of human erythropoietin expressed from recombinant BHK cells have been elucidated.
8407981	2	26	gly	glycosylated	215:226	arg1	cytochrome P-450	cytochrome P-450(arom)				PUBTATOR		cytochrome P-450(arom)	55010		It was found that cytochrome P-450(arom) purified from human placenta microsomes is glycosylated, and the sugar chain was cleaved with endoglycosidase H (Endo H).
3935432	6	19	gly	O-linked	867:874	arg1	the IL-2 protein AND Carbohydrates	IL-2 protein		threonine-3	Carbohydrates	PUBTATOR		IL-2 protein	3558	threonine-3	Carbohydrates are O-linked to the IL-2 protein via threonine-3 of the polypeptide chain.
26467158	9	36	gly	GlcNAc	1556:1561	arg1	BACE1	BACE1			GlcNAc	PUBTATOR		BACE1	23821		These mutations almost cancelled the enhanced BACE1 degradation seen in Mgat3(-/-) MEFs, indicating that bisecting GlcNAc on BACE1 indeed regulates its degradation.
468798	0	0	gly	gonadotropin	81:92	arg1	the O-glycosidic carbohydrate units	chorionic gonadotropin			the O-glycosidic carbohydrate units	OGER		chorionic gonadotropin			Structure and location of the O-glycosidic carbohydrate units of human chorionic gonadotropin.
24161696	9	1	gly	Kv3.1b	1722:1727	arg1	N-glycans	Kv3.1b			N-glycans	Cterm		Kv3.1b			GENERAL SIGNIFICANCE: Our study demonstrates that N-glycans of Kv3.1b contain information regarding the association, clustering, and distribution of Kv3.1b in the cell membrane, and furthermore that decreased occupancy caused by congenital disorders of glycosylation may alter the biological activity of Kv3.1b.
24884609	8	19	gly	N-glycosylation	1202:1216	arg2	A fifth N-glycosylation site			A fifth N-glycosylation site						site	A fifth N-glycosylation site was discovered at N274 with the rare nonconsensus NVV motif.
2493268	1	36	gly	O-glycosylated	128:141	arg1	The 5-oxoproline N-terminal chain	chain		residue		OGER		chain		residue	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	1	36	gly	O-glycosylated	128:141	arg1	the 5th amino acid residue			residue						residue	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	1	36	gly	O-glycosylated	128:141	arg1	the 5th amino acid residue	chain		residue		OGER		chain		residue	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
15532026	9	82	gly	glycosylation	1577:1589	arg2	the used glycosylation site			the used glycosylation site						site	These data suggest that the loss of the used glycosylation site in the gamma subunit may affect the intracellular localization of GNPTAG and the overall efficiency of M6P formation.
3202829	3	65	gly	glycoprotein	387:398	arg1	a glycoprotein 128 amino acids long	a glycoprotein 128 amino acids long				Fterm		glycoprotein			It is a glycoprotein 128 amino acids long, differing from human pancreatic RNase in the presence of an additional threonine residue at the C-terminus.
11531339	6	36	part_of	IgE	996:998	arg1	the IgE binding site	IgE		the IgE binding site		OGER	Site	IgE	P01854	site	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
22809326	11	38	gly	glycosylated	1313:1324	arg1	the glycosylated luminal regions			the glycosylated luminal regions						regions	Computational models of the glycosylated luminal regions of LAMP-1 and LAMP-2 indicate that the proteins adopt a compact conformation in close proximity to the lysosomal membrane.
10531064	2	9	part_of	TfR	364:366	arg1	the dimeric ectodomain	TfR		the dimeric ectodomain		PUBTATOR	Site	TfR	7037	ectodomain	The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit.
19017259	7	89	gly	glycoprotein	1251:1262	arg1	a partially phosphorylated glycoprotein	a partially phosphorylated glycoprotein				Fterm		glycoprotein			f-pTFPI showed a partially phosphorylated glycoprotein comprising a total of 276 amino acids by peptide mapping.
2498325	11	66	gly	sialylated	1689:1698	arg1	multiply sialylated apoE	multiply sialylated apoE				PUBTATOR		apoE	348		The transfected wild-type cells secreted multiply sialylated apoE.
15536627	1	2	gly	Asn630	395:400	arg1	the carbohydrate profiles			Asn432 and Asn630	the carbohydrate profiles					Asn432 and Asn630	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	1	11	gly	Asn432	384:389	arg1	the carbohydrate profiles			Asn432 and Asn630	the carbohydrate profiles					Asn432 and Asn630	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	1	49	gly	carbohydrate	359:370	arg2	Asn432			Asn432 and Asn630						Asn432 and Asn630	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
17331201	8	45	part_of	regions	1559:1565	arg1	Cbln2	Cbln2		regions		PUBTATOR	Site	Cbln2	147381	regions	These results indicate that like Cbln1, Cbln2 and Cbln4 may also serve as transneuronal regulators of synaptic functions in various brain regions.
17331201	8	45	part_of	regions	1559:1565	arg1	Cbln4	Cbln4		regions		PUBTATOR	Site	Cbln4	140689	regions	These results indicate that like Cbln1, Cbln2 and Cbln4 may also serve as transneuronal regulators of synaptic functions in various brain regions.
16321355	7	35	gly	sialylated	1245:1254	arg1	sialylated tetraantennary oligosaccharide				sialylated tetraantennary oligosaccharide						A small amount of sialylated tetraantennary oligosaccharide was detected.
16877748	6	35	gly	trisialylated	1149:1161	arg1	trisialylated complex-type N-glycans				trisialylated complex-type N-glycans						Ion-exchange chromatography and matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) of the released N-glycans showed that sICAM-1 mostly carried di- and trisialylated complex-type N-glycans with or without one fucose.
16877748	6	18	gly	carried	1133:1139	arg1	sICAM-1 AND trisialylated complex-type N-glycans	sICAM-1			trisialylated complex-type N-glycans	Cterm		sICAM-1	3383		Ion-exchange chromatography and matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) of the released N-glycans showed that sICAM-1 mostly carried di- and trisialylated complex-type N-glycans with or without one fucose.
16877748	6	18	gly	carried	1133:1139	arg1	sICAM-1 AND di-	sICAM-1			di-	Cterm		sICAM-1	3383		Ion-exchange chromatography and matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) of the released N-glycans showed that sICAM-1 mostly carried di- and trisialylated complex-type N-glycans with or without one fucose.
26117840	3	58	part_of	E-selectin	562:571	arg1	the extracellular E-selectin region	E-selectin		the extracellular E-selectin region		PUBTATOR	Site	E-selectin	6401	region	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
18491227	0	38	part_of	E-cadherin	56:65	arg1	extracellular domain	E-cadherin		extracellular domain		PUBTATOR	Site	E-cadherin	999	domain	Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD.
20188224	10	76	gly	glycosylation	1499:1511	arg2	the sites			the sites						sites	The method developed was applied to progranulin (PGRN) to characterize the structures of the released glycans and to identify the sites of glycosylation.
30659065	5	29	gly	occupancy	1225:1233	arg2	site occupancy			site occupancy						site	Here we employ a nLC-MS/MS method using stepped-energy higher energy collisional dissociation to characterize the N-glycan repertoire and site occupancy of circulating serum antibodies.
16877748	10	42	gly	trisialylated	1819:1831	arg1	mostly di- and trisialylated complex-type N-glycans				mostly di- and trisialylated complex-type N-glycans						These results show that the N-glycans that enhance the MIP-2-inducing activity of mouse sICAM-1 are mostly di- and trisialylated complex-type N-glycans including a small fraction carrying more sialic acid residues than antennae and that the nine N-glycosylation sites of mouse sICAM-1 are all glycosylated.
16877748	10	42	gly	trisialylated	1819:1831	arg1	the N-glycans				the N-glycans						These results show that the N-glycans that enhance the MIP-2-inducing activity of mouse sICAM-1 are mostly di- and trisialylated complex-type N-glycans including a small fraction carrying more sialic acid residues than antennae and that the nine N-glycosylation sites of mouse sICAM-1 are all glycosylated.
16877748	10	31	gly	glycosylated	1997:2008	arg1	the nine N-glycosylation sites	sICAM-1		sites		Cterm		sICAM-1	3383	sites	These results show that the N-glycans that enhance the MIP-2-inducing activity of mouse sICAM-1 are mostly di- and trisialylated complex-type N-glycans including a small fraction carrying more sialic acid residues than antennae and that the nine N-glycosylation sites of mouse sICAM-1 are all glycosylated.
16877748	10	67	gly	N-glycosylation	1950:1964	arg1	mouse sICAM-1	sICAM-1		sites		Cterm		sICAM-1	3383	sites	These results show that the N-glycans that enhance the MIP-2-inducing activity of mouse sICAM-1 are mostly di- and trisialylated complex-type N-glycans including a small fraction carrying more sialic acid residues than antennae and that the nine N-glycosylation sites of mouse sICAM-1 are all glycosylated.
1997323	8	21	gly	Asn-linked	965:974	arg1	the Asn-linked GlcNAc			Asn	the Asn-linked GlcNAc					Asn	All glycans possessed a common, trimannosyl-N,N'-diacetylchitobiose core with or without one L-fucose alpha-1,6-linked to the Asn-linked GlcNAc.
17360426	2	16	part_of	receptor	365:372	arg1	the ligand-binding region	receptor		the ligand-binding region		Fterm	Site	receptor		region	We determined the crystal structure of the entire extracellular region of the group II receptor and that of the ligand-binding region of the group III receptor.
17360426	2	18	part_of	receptor	301:308	arg1	the entire extracellular region	receptor		the entire extracellular region		Fterm	Site	receptor		region	We determined the crystal structure of the entire extracellular region of the group II receptor and that of the ligand-binding region of the group III receptor.
22967898	2	10	gly	N-glycosylation	249:263	arg2	two predicted N-glycosylation sites			two predicted N-glycosylation sites						sites	Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not.
22967898	2	17	gly	glycosylated	324:335	arg1	cathepsin V	cathepsin V				PUBTATOR		cathepsin V	1515		Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not.
22848655	4	70	part_of	kinase	638:643	arg1	the intracellular kinase domains	kinase		the intracellular kinase domains		Fterm	Site	kinase		domains	The binding of MSP α/β heterodimer to the extracellular region of RON receptor induces receptor dimerization and activation by autophosphorylation of the intracellular kinase domains.
22848655	4	95	part_of	receptor	540:547	arg1	the extracellular region	RON receptor		the extracellular region		OGER	Site	RON receptor	Q04912	region	The binding of MSP α/β heterodimer to the extracellular region of RON receptor induces receptor dimerization and activation by autophosphorylation of the intracellular kinase domains.
15331613	7	12	part_of	site	1515:1518	arg1	the NGC core protein	protein		site		Fterm	Site	protein		site	As the first step in investigating the CS glycosylation mechanism using Neuro 2a cells, we determined the CS attachment site as Ser-123 on the NGC core protein by site-directed mutagenesis.
18676855	7	36	part_of	glycoprotein	1275:1286	arg1	predicted glycosylation sites	glycoprotein		predicted glycosylation sites		Fterm	Site	glycoprotein		sites	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
8639592	8	87	gly	structures	1501:1510	arg1	r-hTFPI	hTFPI			structures	OGER		hTFPI	P10646		All the N-linked structures in r-hTFPI were complex-type carbohydrate chains with one fucose residue attached to the reducing-end GlcNAc and consisted of bi-, tri-, and tetraantennary carbohydrate chains in the ratio 1.9:1.3:1.0.
12944413	5	40	gly	sialylated	821:830	arg1	sialylated N-glycans				sialylated N-glycans						However, defects in sialylated N-glycans did not alter surface expression of the SERT protein.
17157876	4	92	part_of	transthyretin	938:950	arg1	an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain	transthyretin		an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain		OGER	Site	transthyretin	P02766	domain	The structural analysis reveals that CPN1 has a pear-like shape, consisting of a 319 residue N-terminal catalytic domain and an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain, more resembling CPD-2 than CPM.
17157876	4	96	part_of	TT	953:954	arg1	an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain	TT		an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain		Cterm	Site	TT	P02766	domain	The structural analysis reveals that CPN1 has a pear-like shape, consisting of a 319 residue N-terminal catalytic domain and an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain, more resembling CPD-2 than CPM.
21980294	9	37	part_of	C-terminal	1364:1373	arg1	the gD C-terminal region	gD C		the gD C-terminal region		PUBTATOR	Site	gD C	8034	region	Furthermore, the structure of the complex supports a model in which gD-receptor binding triggers HSV entry through receptor-mediated displacement of the gD C-terminal region.
21980294	9	68	part_of	gD	1361:1362	arg1	the gD C-terminal region	gD C		the gD C-terminal region		PUBTATOR	Site	gD C	8034	region	Furthermore, the structure of the complex supports a model in which gD-receptor binding triggers HSV entry through receptor-mediated displacement of the gD C-terminal region.
19358553	2	33	gly	glycopeptides	419:431	arg2	widely different glycopeptides			widely different glycopeptides						glycopeptides	Thus, a systematic study of widely different glycopeptides was performed to determine the relationship between the relative abundances of the individual glycoforms and the MALDI-TOF MS signal strength.
11544325	4	47	part_of	MD-2	628:631	arg1	two potential glycosylation sites	MD-2		two potential glycosylation sites		PUBTATOR	Site	MD-2	23643	sites	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	47	part_of	MD-2	628:631	arg1	Asn(26)	MD-2		Asn(26) and Asn(114)		PUBTATOR	SpecificSite	MD-2	23643	Asn(26) and Asn(114)	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
24841998	10	13	gly	glycoprotein	1535:1546	arg1	a specific glycoprotein	a specific glycoprotein				Fterm		glycoprotein			Analysis showed that the changes often concerned one or two, but not all, N-glycosylation sites in a specific glycoprotein.
24841998	10	47	gly	one	1474:1476	arg1	N-glycosylation sites			N-glycosylation sites						sites	Analysis showed that the changes often concerned one or two, but not all, N-glycosylation sites in a specific glycoprotein.
24841998	10	48	gly	N-glycosylation	1499:1513	arg2	N-glycosylation sites			N-glycosylation sites						sites	Analysis showed that the changes often concerned one or two, but not all, N-glycosylation sites in a specific glycoprotein.
12154198	2	37	part_of	found	328:332	arg1	the type I insulin-like growth factor receptor AND domains	the type I insulin-like growth factor receptor		domains		Fterm	Site	receptor		domains	The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor.
20696930	5	43	part_of	epitope	587:593	arg1	HER2	HER2		epitope		PUBTATOR	Site	HER2	2064	epitope	Zher2 binds to a conformational epitope on HER2 that is distant from those recognized by the therapeutic antibodies trastuzumab and pertuzumab.
21264968	7	105	part_of	MUC5AC	2418:2423	arg1	the consecutive Thr residues	MUC5AC		the consecutive Thr residues		PUBTATOR	AminoAcid	MUC5AC	4586	Thr residues	Such conformational impact on the underlying peptides was proved to be remarkable in the glycosylation at the consecutive Thr residues of MUC5AC.
8163535	0	73	part_of	site	50:53	arg1	syndecan-1	syndecan-1		site		PUBTATOR	Site	syndecan-1	20969	site	Core protein structure and sequence determine the site and presence of heparan sulfate and chondroitin sulfate on syndecan-1.
7689829	8	11	gly	N-glycosylation	1069:1083	arg2	a single N-glycosylation site			a single N-glycosylation site						site	There is a single N-glycosylation site in the mouse GM2 activator protein sequence (Asn151-Phe-Thr) which differs in its location from the single site reported in the human GM2 activator protein sequence (Asn63-Val-Thr).
7689829	8	22	gly	site	1085:1088	arg1	the mouse GM2 activator protein sequence			site	the mouse GM2 activator protein sequence					site	There is a single N-glycosylation site in the mouse GM2 activator protein sequence (Asn151-Phe-Thr) which differs in its location from the single site reported in the human GM2 activator protein sequence (Asn63-Val-Thr).
28668641	0	25	gly	Glycosylation	0:12	arg1	SERPINA12	SERPINA12				PUBTATOR		SERPINA12	145264		Glycosylation of human vaspin (SERPINA12) and its impact on serpin activity, heparin binding and thermal stability.
28668641	0	25	gly	Glycosylation	0:12	arg1	human vaspin	human vaspin				PUBTATOR		vaspin	145264		Glycosylation of human vaspin (SERPINA12) and its impact on serpin activity, heparin binding and thermal stability.
2056274	6	84	part_of	contains	1087:1094	arg1	This inserted region AND a potential site			site						site	This inserted region is rich in serine and threonine residues that may serve as sites of O-linked glycosylation, and contains a potential site of N-linked glycosylation and a potential site of chondroitin sulphate attachment.
19153605	9	33	gly	C-mannosylation	1064:1078	arg1	the TSR				the TSR						We further showed that mindin recognizes lipopolysaccharide (LPS) through its TSR domain, and obtained evidence that C-mannosylation of the TSR influences LPS binding.
25765764	6	21	part_of	LRIG1-LRR-1Ig	923:935	arg1	The FLAG-tagged LRIG1-LRR-1Ig fragment	FLAG-tagged LRIG1		The FLAG-tagged LRIG1-LRR-1Ig fragment		PUBTATOR	Site	FLAG-tagged LRIG1	26018	fragment	The FLAG-tagged LRIG1-LRR-1Ig fragment binds weakly to colon cancer cells regardless of the presence of EGFRs.
25765764	6	24	part_of	FLAG-tagged	911:921	arg1	The FLAG-tagged LRIG1-LRR-1Ig fragment	FLAG-tagged LRIG1		The FLAG-tagged LRIG1-LRR-1Ig fragment		PUBTATOR	Site	FLAG-tagged LRIG1	26018	fragment	The FLAG-tagged LRIG1-LRR-1Ig fragment binds weakly to colon cancer cells regardless of the presence of EGFRs.
27238017	4	39	part_of	contains	593:600	arg1	NPC1 AND three distinct lumenal domains	NPC1		three distinct lumenal domains		PUBTATOR	Site	NPC1	4864	domains	NPC1 contains 13 transmembrane segments (TMs) and three distinct lumenal domains A (also designated NTD), C, and I. TMs 2-13 exhibit a typical resistance-nodulation-cell division fold, among which TMs 3-7 constitute the sterol-sensing domain conserved in several proteins involved in cholesterol metabolism and signaling.
9245713	0	19	gly	glycoprotein	104:115	arg1	a novel palmitoylated surface glycoprotein	a novel palmitoylated surface glycoprotein				Fterm		glycoprotein			Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
19571171	5	46	part_of	addressin	1038:1046	arg1	a sulfated peripheral lymph node addressin epitope	addressin		a sulfated peripheral lymph node addressin epitope		Fterm	Site	addressin		epitope	The N196 and N410 glycans differentially affect sulfation of two different substrates: cells that express an enzyme lacking the N410 glycan are able to sulfate the sialyl Lewis X substrate, but produce reduced levels of a sulfated peripheral lymph node addressin epitope and cells that express an enzyme lacking the N196 glycan are able to produce a sulfated peripheral lymph node addressin epitope, but are impaired in their ability to sulfate sialyl Lewis X.
19571171	5	57	part_of	addressin	1166:1174	arg1	a sulfated peripheral lymph node addressin epitope	addressin		a sulfated peripheral lymph node addressin epitope		Fterm	Site	addressin		epitope	The N196 and N410 glycans differentially affect sulfation of two different substrates: cells that express an enzyme lacking the N410 glycan are able to sulfate the sialyl Lewis X substrate, but produce reduced levels of a sulfated peripheral lymph node addressin epitope and cells that express an enzyme lacking the N196 glycan are able to produce a sulfated peripheral lymph node addressin epitope, but are impaired in their ability to sulfate sialyl Lewis X.
6333684	4	3	part_of	interleukin	590:600	arg1	The entire primary sequence	interleukin 2		The entire primary sequence		PUBTATOR	Site	interleukin 2	3558	sequence	The entire primary sequence of interleukin 2, including the location of the intramolecular disulfide bridge, was determined by a combination of peptide mapping and protein sequencing.
15628971	5	6	gly	attachment	859:868	arg2	a single N-glycan AND the C-terminal region			the C-terminal region	a single N-glycan					region	We found that (i) treatment of recombinant C4ST-1 with peptide N-glycosidase F caused a marked decrease in activity, (ii) production of the active form of C4ST-1 by COS-7 cells transfected with cDNA of C4ST-1 was inhibited by tunicamycin, (iii) deletion of the N-glycosylation site located at the C-terminal region of C4ST-1 abolished activity, (iv) attachment of a single N-glycan at the C-terminal region supported production of the active form of C4ST-1, but the resulting recombinant enzyme was much more unstable at 37 degrees C than the control recombinant protein, and (v) truncation of C-terminal region up to the N-glycosylation site at the C-terminal region resulted in total loss of activity.
15628971	5	38	gly	N-glycosylation	1131:1145	arg2	the C-terminal region			the C-terminal region						region	We found that (i) treatment of recombinant C4ST-1 with peptide N-glycosidase F caused a marked decrease in activity, (ii) production of the active form of C4ST-1 by COS-7 cells transfected with cDNA of C4ST-1 was inhibited by tunicamycin, (iii) deletion of the N-glycosylation site located at the C-terminal region of C4ST-1 abolished activity, (iv) attachment of a single N-glycan at the C-terminal region supported production of the active form of C4ST-1, but the resulting recombinant enzyme was much more unstable at 37 degrees C than the control recombinant protein, and (v) truncation of C-terminal region up to the N-glycosylation site at the C-terminal region resulted in total loss of activity.
15628971	5	38	gly	N-glycosylation	1131:1145	arg2	the N-glycosylation site			the N-glycosylation site						site	We found that (i) treatment of recombinant C4ST-1 with peptide N-glycosidase F caused a marked decrease in activity, (ii) production of the active form of C4ST-1 by COS-7 cells transfected with cDNA of C4ST-1 was inhibited by tunicamycin, (iii) deletion of the N-glycosylation site located at the C-terminal region of C4ST-1 abolished activity, (iv) attachment of a single N-glycan at the C-terminal region supported production of the active form of C4ST-1, but the resulting recombinant enzyme was much more unstable at 37 degrees C than the control recombinant protein, and (v) truncation of C-terminal region up to the N-glycosylation site at the C-terminal region resulted in total loss of activity.
15628971	5	48	gly	N-glycosylation	770:784	arg2	the N-glycosylation site			the N-glycosylation site						site	We found that (i) treatment of recombinant C4ST-1 with peptide N-glycosidase F caused a marked decrease in activity, (ii) production of the active form of C4ST-1 by COS-7 cells transfected with cDNA of C4ST-1 was inhibited by tunicamycin, (iii) deletion of the N-glycosylation site located at the C-terminal region of C4ST-1 abolished activity, (iv) attachment of a single N-glycan at the C-terminal region supported production of the active form of C4ST-1, but the resulting recombinant enzyme was much more unstable at 37 degrees C than the control recombinant protein, and (v) truncation of C-terminal region up to the N-glycosylation site at the C-terminal region resulted in total loss of activity.
2110822	0	51	gly	asparagine-linked	19:35	arg1	asparagine-linked sugar chains			asparagine	asparagine-linked sugar chains					asparagine	Characteristics of asparagine-linked sugar chains of sphingolipid activator protein 1 purified from normal human liver and GM1 gangliosidosis (type 1) liver.
2110822	0	58	gly	protein	76:82	arg1	asparagine-linked sugar chains	activator protein 1			asparagine-linked sugar chains	PUBTATOR		activator protein 1	5660		Characteristics of asparagine-linked sugar chains of sphingolipid activator protein 1 purified from normal human liver and GM1 gangliosidosis (type 1) liver.
2403553	1	62	gly	oligosaccharides	88:103	arg1	the human transferrin receptor	transferrin receptor			oligosaccharides	PUBTATOR		transferrin receptor	7018		We have investigated the oligosaccharides in the human transferrin receptor from three different cell lines.
22171320	2	36	part_of	glycoproteins	394:406	arg1	glycosylation sites	glycoproteins		glycosylation sites		Fterm	Site	glycoproteins		sites	Previous proteomic studies have identified more than 2800 urinary proteins but analyses aimed at unraveling glycan structures and glycosylation sites of urinary glycoproteins are lacking.
20622017	1	12	gly	glycoprotein	130:141	arg1	The cell surface glycoprotein γ-glutamyl transpeptidase	The cell surface glycoprotein γ-glutamyl transpeptidase				Fterm		glycoprotein			The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
22588082	2	8	part_of	contain	333:339	arg1	>40 human proteins AND the TSR consensus sequence	>40 human proteins		the TSR consensus sequence		Fterm	Site	proteins		sequence	The fucose transfer is catalysed by the protein O-fucosyltransferase 2 (POFUT2) and >40 human proteins contain the TSR consensus sequence for POFUT2-dependent fucosylation.
11738084	3	48	gly	released	344:351	arg1	the protein AND The oligosaccharide	the protein			The oligosaccharide	Fterm		protein			The oligosaccharide was released from the protein using anhydrous hydrazine, and its structure was investigated using neuraminidase and a reagent array analysis method, which is based on the use of specific exoglycosidases.
3458201	0	57	part_of	alpha	36:40	arg1	Amino acid sequence	alpha 1B-glycoprotein		Amino acid sequence		PUBTATOR	Site	alpha 1B-glycoprotein	1	sequence	Amino acid sequence of human plasma alpha 1B-glycoprotein: homology to the immunoglobulin supergene family.
29741879	9	32	gly	glycopeptides	1878:1890	arg2	glycopeptides			glycopeptides						glycopeptides	This analysis revealed an extensive number of glycopeptides hidden in the global and enriched in IMAC-based phosphopeptide-enriched proteomic data, information which would have remained unknown from the original study otherwise.
15869464	9	1	part_of	containing	1786:1795	arg1	the regions AND the RGD (Arg-Gly-Asp) integrin-binding sequence	the regions		the RGD (Arg-Gly-Asp) integrin-binding sequence						sequence	The phosphorylations are arranged in clusters of three to five phosphoresidues and the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence are devoid of phosphorylations.
3463996	4	8	part_of	B	815:815	arg1	procathepsin B sequences	procathepsin B		procathepsin B sequences		Cterm	Site	procathepsin B	1508	sequences	A comparison of procathepsin B sequences from three species (human, mouse, and rat) reveals that the homology between the propeptides is relatively conserved with a minimum of 68% sequence identity.
3463996	4	56	part_of	procathepsin	802:813	arg1	procathepsin B sequences	procathepsin B		procathepsin B sequences		Cterm	Site	procathepsin B	1508	sequences	A comparison of procathepsin B sequences from three species (human, mouse, and rat) reveals that the homology between the propeptides is relatively conserved with a minimum of 68% sequence identity.
8489250	2	9	gly	N-glycosylation	353:367	arg2	six potential N-glycosylation sites			six potential N-glycosylation sites						sites	Peptide peptides containing six potential N-glycosylation sites were analyzed to determine that Asn residues 9, 34, 63, 73, 96, and 116 were utilized.
8489250	2	24	gly	utilized	452:459	arg2	Asn residues 9, 34, 63, 73, 96, and 116			Asn residues 9, 34, 63, 73, 96, and 116						Asn residues 9, 34, 63, 73, 96, and 116	Peptide peptides containing six potential N-glycosylation sites were analyzed to determine that Asn residues 9, 34, 63, 73, 96, and 116 were utilized.
8344280	12	73	gly	proteins	2032:2039	arg1	complex oligosaccharide chains	proteins			complex oligosaccharide chains	Fterm		proteins			No evidence was obtained for the presence of secreted proteins with complex oligosaccharide chains, irrespective of the cell-culture conditions used or the harvesting time, for infected cells with recombinant baculovirus constructs.
29345911	6	24	part_of	convertase	830:839	arg1	convertase cleavage site	convertase		convertase cleavage site		Fterm	Site	convertase		site	To obtain more insight into the role of some of its post-translational modifications, we designed a mutant GPC3, sGPC3m, without its GPI anchor, convertase cleavage site, and glycosaminoglycan chains.
29345911	6	41	part_of	GPI	818:820	arg1	convertase cleavage site	GPI		convertase cleavage site		OGER	Site	GPI	P06744	site	To obtain more insight into the role of some of its post-translational modifications, we designed a mutant GPC3, sGPC3m, without its GPI anchor, convertase cleavage site, and glycosaminoglycan chains.
17924658	0	74	part_of	gamma-glutamyltranspeptidase	106:133	arg1	glycosylation sites	gamma-glutamyltranspeptidase		glycosylation sites		PUBTATOR	Site	gamma-glutamyltranspeptidase	102724197	sites	Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human gamma-glutamyltranspeptidase.
26536155	0	54	part_of	Pronase	168:174	arg1	Pronase Treated Glycopeptides	Pronase		Pronase Treated Glycopeptides		Fterm	Site	Pronase		Glycopeptides	Site-Specific Protein N- and O-Glycosylation Analysis by a C18-Porous Graphitized Carbon-Liquid Chromatography-Electrospray Ionization Mass Spectrometry Approach Using Pronase Treated Glycopeptides.
26536155	0	89	part_of	Treated	176:182	arg1	Pronase Treated Glycopeptides	Treated		Pronase Treated Glycopeptides		Cterm	Site	Treated		Glycopeptides	Site-Specific Protein N- and O-Glycosylation Analysis by a C18-Porous Graphitized Carbon-Liquid Chromatography-Electrospray Ionization Mass Spectrometry Approach Using Pronase Treated Glycopeptides.
19951703	2	30	gly	glycosylated	239:250	arg1	a glycosylated luminal domain			a glycosylated luminal domain						domain	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
22902367	4	4	part_of	Necl-5	752:757	arg1	natively glycosylated full ectodomains	Necl-5		natively glycosylated full ectodomains		OGER	Site	Necl-5	P15151	ectodomains	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	4	part_of	Necl-5	752:757	arg1	adhesive fragments	Necl-5		adhesive fragments		OGER	Site	Necl-5	P15151	fragments	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	56	part_of	nectins	740:746	arg1	natively glycosylated full ectodomains	nectins 		natively glycosylated full ectodomains		PUBTATOR	Site	nectins 	5818	ectodomains	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	56	part_of	nectins	740:746	arg1	adhesive fragments	nectins 		adhesive fragments		PUBTATOR	Site	nectins 	5818	fragments	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
17117926	3	2	gly	Asn311	404:409	arg1	glycans			Asn114, Asn120, Asn311 and Asn325	glycans					Asn114, Asn120, Asn311 and Asn325	We found that Wnt-5a is modified with palmitate at Cys104 and glycans at Asn114, Asn120, Asn311 and Asn325.
17117926	3	44	gly	Asn325	415:420	arg1	glycans			Asn114, Asn120, Asn311 and Asn325	glycans					Asn114, Asn120, Asn311 and Asn325	We found that Wnt-5a is modified with palmitate at Cys104 and glycans at Asn114, Asn120, Asn311 and Asn325.
17117926	3	51	gly	Asn120	396:401	arg1	glycans			Asn114, Asn120, Asn311 and Asn325	glycans					Asn114, Asn120, Asn311 and Asn325	We found that Wnt-5a is modified with palmitate at Cys104 and glycans at Asn114, Asn120, Asn311 and Asn325.
7613477	3	27	gly	glycopeptides	885:897	arg2	three additional glycopeptides			three additional glycopeptides						glycopeptides	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	3	109	gly	glycopeptide	830:841	arg2	a di-O-linked glycopeptide			a di-O-linked glycopeptide						glycopeptide	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	3	117	gly	glycopeptides	793:805	arg1	LCAT	LCAT		glycopeptides		PUBTATOR		LCAT	3931	glycopeptides	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
9535843	7	34	gly	glycosylation	1062:1074	arg2	ten separate glycosylation sites			ten separate glycosylation sites						sites	After removal of this site and insertion of ten separate glycosylation sites, we defined two additional extracellular loops between H4 and H5, and H6 and H7.
15003450	4	40	part_of	domain	642:647	arg1	the active site	domain		the active site						site	The structure is a homodimer with each monomer containing a (beta/alpha)8 domain with the active site and an antiparallel beta domain.
15003450	4	50	part_of	domain	589:594	arg1	the active site	domain		the active site						site	The structure is a homodimer with each monomer containing a (beta/alpha)8 domain with the active site and an antiparallel beta domain.
29226084	3	84	gly	N-glycosylation	444:458	arg2	N12			N12						N12	In this study, we investigated the post-translational modification of GPR61 by N-glycosylation at an identified consensus N-glycosylation site (N12) and the impact of this modification upon the subcellular expression of the protein.
29226084	3	84	gly	N-glycosylation	444:458	arg2	an identified consensus N-glycosylation site			an identified consensus N-glycosylation site						site	In this study, we investigated the post-translational modification of GPR61 by N-glycosylation at an identified consensus N-glycosylation site (N12) and the impact of this modification upon the subcellular expression of the protein.
29226084	3	55	gly	N-glycosylation	401:415	arg2	N12			N12						N12	In this study, we investigated the post-translational modification of GPR61 by N-glycosylation at an identified consensus N-glycosylation site (N12) and the impact of this modification upon the subcellular expression of the protein.
29226084	3	55	gly	N-glycosylation	401:415	arg2	an identified consensus N-glycosylation site			site						site	In this study, we investigated the post-translational modification of GPR61 by N-glycosylation at an identified consensus N-glycosylation site (N12) and the impact of this modification upon the subcellular expression of the protein.
23234360	0	74	gly	glycoproteins	102:114	arg1	human cerebrospinal fluid glycoproteins	glycoproteins			glycan structures	Fterm		glycoproteins			LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	0	41	gly	O-glycosylation	29:43	arg1	human cerebrospinal fluid glycoproteins	glycoproteins		sites		Fterm		glycoproteins		sites	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
7592613	6	56	gly	sialylated	1145:1154	arg1	lacNAc				lacNAc						It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
19196183	7	10	gly	glycopeptides	976:988	arg2	glycopeptides			glycopeptides						glycopeptides	In brief, in terms of selectivity for glycopeptides, HC is superior to HA (92.9% vs 51.3%); however, based on the number of glycosites identified, HA outweighs HC (265 vs 159).
19196183	7	66	gly	glycosites	1062:1071	arg2	glycosites			glycosites						glycosites	In brief, in terms of selectivity for glycopeptides, HC is superior to HA (92.9% vs 51.3%); however, based on the number of glycosites identified, HA outweighs HC (265 vs 159).
12545205	3	88	gly	glycosylated	393:404	arg1	a heavily glycosylated protein	a heavily glycosylated protein				Fterm		protein			N-cadherin is a heavily glycosylated protein.
12545205	3	88	gly	glycosylated	393:404	arg1	N-cadherin	N-cadherin				PUBTATOR		N-cadherin	1000		N-cadherin is a heavily glycosylated protein.
19678840	4	66	part_of	GCPIII	800:805	arg1	the human GCPIII ectodomain	GCPIII		the human GCPIII ectodomain		PUBTATOR	Site	GCPIII	219595	ectodomain	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
7535613	11	82	gly	glycosylation	1610:1622	arg2	The PSA glycosylation site			site, Asn 61						site, Asn 61	The PSA glycosylation site, Asn 61, is fully accessible to the solvent and is enclosed in a positive region of the isopotential map.
21757702	5	68	part_of	EGF	764:766	arg1	a novel, non-traditional consensus site	EGF 9		a novel, non-traditional consensus site		OGER	Site	EGF 9	P01133	site	O-Glucose is also found at a novel, non-traditional consensus site at EGF 9.
17286803	4	19	gly	glycosylated	519:530	arg2	asparagine residues 71 and 85	CLN3		asparagine residues 71 and 85		OGER		CLN3	Q13286	asparagine residues 71 and 85	Mutational analysis revealed that in COS7 cells, CLN3 is glycosylated at asparagine residues 71 and 85.
17286803	4	19	gly	glycosylated	519:530	arg2	85	CLN3		asparagine residues 71 and 85		OGER		CLN3	Q13286	asparagine residues 71 and 85	Mutational analysis revealed that in COS7 cells, CLN3 is glycosylated at asparagine residues 71 and 85.
17286803	4	19	gly	glycosylated	519:530	arg2	85			asparagine residues 71 and 85						asparagine residues 71 and 85	Mutational analysis revealed that in COS7 cells, CLN3 is glycosylated at asparagine residues 71 and 85.
22173220	6	43	gly	Glycosylation	712:724	arg2	the first five sites			the first five sites						sites	Glycosylation at the first five sites was confirmed by tandem mass spectrometry.
16321355	2	48	gly	glycosylation	270:282	arg1	CP	CP				PUBTATOR		CP	1356		In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	2	48	gly	glycosylation	270:282	arg1	human ceruloplasmin	human ceruloplasmin				PUBTATOR		ceruloplasmin	1356		In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
24190431	2	30	part_of	vimentin	336:343	arg1	vimentin epitopes	vimentin		vimentin epitopes		PUBTATOR	Site	vimentin	7431	epitopes	We show how citrullinated aggrecan and vimentin epitopes bind to HLA-DRB1*04:01/04.
3521732	0	58	gly	contains	64:71	arg1	a serine protease AND four tandem repeats	a serine protease			four tandem repeats	Fterm		protease			Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats.
3651384	6	43	part_of	SGP-2	822:826	arg1	The derived SGP-2 sequence	SGP-2		The derived SGP-2 sequence		PUBTATOR	Site	SGP-2	24854	sequence	The derived SGP-2 sequence has a molecular weight of 51,379 and contains six potential N-glycosylation sites.
3651384	6	63	part_of	contains	874:881	arg1	The derived SGP-2 sequence AND six potential N-glycosylation sites	The derived SGP-2 sequence		six potential N-glycosylation sites						sites	The derived SGP-2 sequence has a molecular weight of 51,379 and contains six potential N-glycosylation sites.
11805077	4	39	gly	residue	552:558	arg1	the sulfated N-linked oligosaccharide			residue in	the sulfated N-linked oligosaccharide					residue in	Sulfated monosaccharide residue in the sulfated N-linked oligosaccharide was determined by exoglycosidase digestion followed by sugar mapping by LC/MS.
8436110	1	14	gly	glycoproteins	217:229	arg1	The carbohydrate chains	glycoproteins			The carbohydrate chains	Fterm		glycoproteins			The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
9153399	8	45	gly	ICAM-2	1268:1273	arg1	N-linked glycans	ICAM-2			N-linked glycans	PUBTATOR		ICAM-2	3384		A bend between domains 1 and 2 of ICAM-2 and a tripod-like arrangement of N-linked glycans in the membrane-proximal region of domain 2 may be important for presenting the recognition surface to LFA-1.
7541354	1	40	gly	present	117:123	arg1	human plasma vitronectin AND N-linked oligosaccharides	human plasma vitronectin			N-linked oligosaccharides	PUBTATOR		vitronectin	7448		The structures of N-linked oligosaccharides present on human plasma vitronectin were elucidated.
6816276	4	50	gly	located	529:535	arg1	the mu chain constant region AND high-mannose			the mu chain constant region	high-mannose					region	Three complex-type and two high-mannose oligosaccharides are located in the mu chain constant region.
6816276	4	50	gly	located	529:535	arg2	the mu chain constant region AND complex-type			the mu chain constant region	complex-type					region	Three complex-type and two high-mannose oligosaccharides are located in the mu chain constant region.
26192331	1	40	gly	polysialylation	169:183	arg1	surface-localized glycoproteins	surface-localized glycoproteins				Fterm		glycoproteins			Sialyltransferases of the mammalian ST8Sia family catalyze oligo- and polysialylation of surface-localized glycoproteins and glycolipids through transfer of sialic acids from CMP-sialic acid to the nonreducing ends of sialic acid acceptors.
26192331	1	43	gly	glycoproteins	206:218	arg1	surface-localized glycoproteins	glycoproteins			oligo-	Fterm		glycoproteins			Sialyltransferases of the mammalian ST8Sia family catalyze oligo- and polysialylation of surface-localized glycoproteins and glycolipids through transfer of sialic acids from CMP-sialic acid to the nonreducing ends of sialic acid acceptors.
26192331	1	43	gly	glycoproteins	206:218	arg1	surface-localized glycoproteins	glycoproteins			polysialylation	Fterm		glycoproteins			Sialyltransferases of the mammalian ST8Sia family catalyze oligo- and polysialylation of surface-localized glycoproteins and glycolipids through transfer of sialic acids from CMP-sialic acid to the nonreducing ends of sialic acid acceptors.
1898343	1	0	part_of	containing	106:115	arg1	Human pancreatic elastase 1 AND two potential N-glycosylation sites	Human pancreatic elastase 1		two potential N-glycosylation sites		PUBTATOR	Site	Human pancreatic elastase 1	1990	sites	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	0	part_of	containing	106:115	arg1	a glycoprotein AND two potential N-glycosylation sites	a glycoprotein		two potential N-glycosylation sites		Fterm	Site	glycoprotein		sites	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
2514791	4	23	part_of	t-PA	1495:1498	arg1	Asn-448	t-PA		Asn-448		PUBTATOR	SpecificSite	t-PA	5327	Asn-448	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
12839991	3	14	part_of	NgR	488:490	arg1	soluble fragments	NgR		soluble fragments		OGER	Site	NgR	Q9BZR6	fragments	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	3	29	part_of	Nogo	474:477	arg1	soluble fragments	Nogo		soluble fragments		OGER	Site	Nogo	Q9NQC3	fragments	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	3	53	part_of	MAG	480:482	arg1	soluble fragments	MAG		soluble fragments		OGER	Site	MAG	P20916	fragments	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
20622017	12	32	gly	glycoprotein	1657:1668	arg1	a human glycoprotein	a human glycoprotein				Fterm		glycoprotein			This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	12	38	gly	glycopeptides	1632:1644	arg2	individual glycopeptides	glycoprotein		glycopeptides		Fterm		glycoprotein		glycopeptides	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
17956937	3	48	gly	PSA	610:612	arg1	the glycan profiles	PSA			the glycan profiles	PUBTATOR		PSA	354		In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	3	73	gly	PSA	558:560	arg1	free and complexed forms	PSA			free and complexed forms	PUBTATOR		PSA	354		In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	3	93	gly	glycopeptides	645:657	arg2	the glycopeptides			the glycopeptides						glycopeptides	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
12604466	2	35	gly	glycosylation	326:338	arg2	glycosylation sites			glycosylation sites						sites	In the present study, we investigate glycosylation sites in NBCe1.
22023369	4	15	gly	fucosylation	669:680	arg1	the receptor binding site			site	the Fc N-glycans					site	However, fucosylation of the Fc N-glycans inhibits this interaction, because of steric hindrance, and furthermore, negatively affects the dynamics of the receptor binding site.
15117952	0	43	part_of	receptor	62:69	arg1	hormone-bound atrial natriuretic peptide receptor extracellular domain	receptor		hormone-bound atrial natriuretic peptide receptor extracellular domain		Fterm	Site	receptor		domain	Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: rotation mechanism for transmembrane signal transduction.
9722584	7	7	gly	N-glycosylation	1062:1076	arg2	two putative N-glycosylation sites			two putative N-glycosylation sites						sites	The human homolog of porcine NTPPHase described here contains 10 cysteine residues and two putative N-glycosylation sites.
26496195	4	43	gly	repeats	605:611	arg1	the extracellular domain			the extracellular domain	the extracellular domain		Site			domain	We show that wsnp is a null allele of Protein O-glucosyltransferase 1 (Poglut1), which encodes an enzyme previously shown to add O-glucose to EGF repeats in the extracellular domain of Drosophila and mammalian Notch, but the role of POGLUT1 in mammalian gastrulation has not been investigated.
20511397	8	28	part_of	apoE	1456:1459	arg1	the C terminus	apoE		the C terminus		PUBTATOR	Site	apoE	348	terminus	Given the importance of the C terminus of apoE in regulating apoE solubility, stability, and lipid binding, these results may have important implications for our understanding of apoE biochemistry.
24721674	11	19	gly	composition	2233:2243	arg1	sequence			sequence						peptides sequence	Totally 811 N-glycosylation sites from 567 proteins were identified and 177 intact glycopeptides with both glycan composition and peptides sequence were characterized, which provided a solution for site-specific N-glycosylation characterization of membrane.
24721674	11	100	gly	N-glycosylation	2131:2145	arg2	811 N-glycosylation sites			811 N-glycosylation sites						sites	Totally 811 N-glycosylation sites from 567 proteins were identified and 177 intact glycopeptides with both glycan composition and peptides sequence were characterized, which provided a solution for site-specific N-glycosylation characterization of membrane.
24721674	11	112	gly	glycopeptides	2202:2214	arg2	177 intact glycopeptides			glycopeptides	glycan composition					glycopeptides	Totally 811 N-glycosylation sites from 567 proteins were identified and 177 intact glycopeptides with both glycan composition and peptides sequence were characterized, which provided a solution for site-specific N-glycosylation characterization of membrane.
10712595	7	47	gly	glycosylation	1185:1197	arg2	this glycosylation site			this glycosylation site						site	Furthermore, the invariant third-position Ser137 at this glycosylation site of mammalian and chicken antithrombins is substituted by Thr in the salmon, a replacement that has been shown to induce full glycosylation in human antithrombin.
10712595	7	59	gly	glycosylation	1329:1341	arg1	human antithrombin	human antithrombin				PUBTATOR		antithrombin	462		Furthermore, the invariant third-position Ser137 at this glycosylation site of mammalian and chicken antithrombins is substituted by Thr in the salmon, a replacement that has been shown to induce full glycosylation in human antithrombin.
25561468	8	17	part_of	NTF	1238:1240	arg1	the NTF RESP18 homology domain	NTF RESP18		the NTF RESP18 homology domain		PUBTATOR	Site	NTF RESP18	389075	domain	The signal for SG sorting is located within the NTF RESP18 homology domain (RESP18-HD), whereas soluble NTF is retained in the endoplasmic reticulum.
25561468	8	57	part_of	RESP18	1242:1247	arg1	the NTF RESP18 homology domain	NTF RESP18		the NTF RESP18 homology domain		PUBTATOR	Site	NTF RESP18	389075	domain	The signal for SG sorting is located within the NTF RESP18 homology domain (RESP18-HD), whereas soluble NTF is retained in the endoplasmic reticulum.
19017797	3	29	part_of	FMS	621:623	arg1	the major ligand-binding domain	FMS		the major ligand-binding domain		OGER	Site	FMS	P07333	domain	The ligand binding mode of FMS is surprisingly different from KIT, another class III RTK, in which the major ligand-binding domain of FMS, D2, uses the CD and EF loops, but not the beta-sheet on the opposite side of the Ig domain as in KIT, to bind ligand.
10200178	3	32	gly	glycosylated	745:756	arg1	the glycosylated peptide spanning Asn-197			the glycosylated peptide spanning Asn-197						Asn-197	The identification of the glycosylated peptide spanning Asn-197 was not reported.
9767079	3	50	gly	glycosylated	545:556	arg1	glycosylated RFC	glycosylated RFC				PUBTATOR		RFC	6573		At 3 microg/ml tunicamycin, the nearly complete loss of glycosylated RFC was accompanied by a approximately 25% decreased rate of methotrexate uptake.
11710528	2	36	part_of	hTR	379:381	arg1	The radiolabeled hTR glycopeptides	hTR		The radiolabeled hTR glycopeptides		PUBTATOR	Site	hTR	P25116	glycopeptides	The radiolabeled hTR glycopeptides were prepared and fractionated by a lectin chromatography of Concanavalin A-Sepharose.
18308854	0	51	gly	protein	79:85	arg1	three N-linked carbohydrate chains	protein			three N-linked carbohydrate chains	Fterm		protein			Topological assessment of oatp1a1: a 12-transmembrane domain integral membrane protein with three N-linked carbohydrate chains.
3202829	5	69	gly	glycosylated	716:727	arg1	the three Asn-Xaa-Ser/Thr sequences			the three Asn-Xaa-Ser/Thr sequences						sequences	Each of the three Asn-Xaa-Ser/Thr sequences (Asn-34, Asn-76, Asn-88) is glycosylated with a complex-type oligosaccharide chain.
11544325	4	40	gly	sites	596:600	arg1	two potential glycosylation sites			two potential glycosylation sites						sites	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	9	gly	glycosylation	582:594	arg1	MD-2	MD-2		Asn(26) and Asn(114)		PUBTATOR		MD-2	23643	Asn(26) and Asn(114)	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	9	gly	glycosylation	582:594	arg2	Asn(114)			Asn(26) and Asn(114)						Asn(26) and Asn(114)	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	9	gly	glycosylation	582:594	arg2	Asn(114)	MD-2		Asn(26) and Asn(114)		PUBTATOR		MD-2	23643	Asn(26) and Asn(114)	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	9	gly	glycosylation	582:594	arg2	two potential glycosylation sites	MD-2		sites		PUBTATOR		MD-2	23643	sites	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	40	gly	sites	596:600	arg1	Asn(26)			Asn(26) and Asn(114)						Asn(26) and Asn(114)	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
15173186	0	93	gly	glycosylation	14:26	arg2	Four N-linked glycosylation sites			Four N-linked glycosylation sites						sites	Four N-linked glycosylation sites in human toll-like receptor 2 cooperate to direct efficient biosynthesis and secretion.
7642555	2	4	gly	modified	337:344	arg1	c-Myc AND O-linked N-acetylglucosamine	c-Myc			O-linked N-acetylglucosamine	PUBTATOR		c-Myc	4609		Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	2	4	gly	modified	337:344	arg1	c-Myc AND O-GlcNAc	c-Myc			O-GlcNAc	PUBTATOR		c-Myc	4609		Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7841792	1	60	part_of	containing	303:312	arg1	peptides AND individual glycosylation sites	peptides		individual glycosylation sites						sites	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
8336134	6	34	gly	N-glycosylation	1001:1015	arg2	The two N-glycosylation sites			The two N-glycosylation sites						sites	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	6	49	gly	occupied	1081:1088	arg2	the polypeptide			the polypeptide						polypeptide	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	6	49	gly	occupied	1081:1088	arg2	The two N-glycosylation sites			The two N-glycosylation sites						sites	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	6	34	gly	N-glycosylation	1001:1015	arg1	the polypeptide			polypeptide						polypeptide	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
1694179	0	45	gly	glycosylated	22:33	arg2	asparagine 329	Beta protein C		asparagine 329		Cterm		Beta protein C		asparagine 329	Beta protein C is not glycosylated at asparagine 329.
9767079	7	33	gly	N-glycosylation	1274:1288	arg1	human RFC	human RFC				PUBTATOR		RFC	6573		Collectively, our results demonstrate that N-glycosylation of human RFC plays no significant role in either transport function or membrane targeting.
11912203	5	63	gly	glycosylated	658:669	arg1	the adiponectin isoforms	the adiponectin isoforms				PUBTATOR		adiponectin isoforms	9370		Carbohydrate detection revealed that six of the adiponectin isoforms are glycosylated.
14764083	2	68	gly	glycosylation	232:244	arg1	LF	LF				PUBTATOR		LF	3131		To elucidate the role of N-linked glycosylation in protection of LF against proteolysis, we compared the tryptic susceptibility of human LF (hLF) variants from human milk, expressed in human 293(S) cells or in the milk of transgenic mice and cows.
6203908	7	70	part_of	subunit	660:666	arg1	Cys-447	subunit		Cys-447		OGER	SpecificSite	subunit	2	Cys-447	Cys-447 probably forms an interchain bridge with Cys-447 from another subunit.
1823160	4	67	gly	linked	883:888	arg2	a sialic acid AND the 6-position			the 6-position	a sialic acid					position	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
27314333	11	55	gly	N-glycosylation	1736:1750	arg1	Rspo1	Rspo1				PUBTATOR		Rspo1	284654		Our findings provide evidence for the critical role of N-glycosylation in the biogenesis of Rspo1.
10861392	0	77	gly	glycosylation	38:50	arg1	a recombinant fusion protein	a recombinant fusion protein				Fterm		protein			Metabolic shifts do not influence the glycosylation patterns of a recombinant fusion protein expressed in BHK cells.
8942648	9	0	part_of	position	1168:1175	arg1	TPO 1-246	TPO 1-246		position		PUBTATOR	Site	TPO 1-246	256987	position,	The glycosylation map indicates the position, occupancy, and structures of the N- and O-glycans in TPO 1-246.
17157876	3	10	part_of	CPN1	676:679	arg1	the recombinant C-terminally truncated catalytic domain	CPN1		the recombinant C-terminally truncated catalytic domain		PUBTATOR	Site	CPN1	1369	domain	We have prepared and crystallized the recombinant C-terminally truncated catalytic domain of human CPN1, and have determined and refined its 2.1 A crystal structure.
3484330	2	18	part_of	protein	510:516	arg1	the amino-terminal sequence	protein		the amino-terminal sequence		Fterm	Site	protein		sequence	cDNA clones were isolated by use of antibodies specific for the intact proteoglycan and antibodies against a peptide synthesized on the basis of the amino-terminal sequence of the core protein.
7106126	0	52	gly	sialoglycoprotein	34:50	arg1	sialoglycoprotein D	sialoglycoprotein D				PUBTATOR		sialoglycoprotein D	2995		N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
18533687	5	86	gly	glycosylation	797:809	arg1	RXFP1	RXFP1				PUBTATOR		RXFP1	59350		We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
12927778	1	6	gly	glycoproteins	107:119	arg1	Membrane glycoproteins	Membrane glycoproteins				Fterm		glycoproteins			Membrane glycoproteins of neural cells play crucial roles in axon guidance, synaptogenesis, and neuronal transmission.
7514386	0	21	gly	asparagine-linked	69:85	arg1	the asparagine-linked sugar chain			asparagine	the asparagine-linked sugar chain					asparagine	Structural study on the glycosyl-phosphatidylinositol anchor and the asparagine-linked sugar chain of a soluble form of CD59 in human urine.
7514386	0	31	gly	form	112:115	arg1	the asparagine-linked sugar chain	form of CD59			the asparagine-linked sugar chain	PUBTATOR		form of CD59	966		Structural study on the glycosyl-phosphatidylinositol anchor and the asparagine-linked sugar chain of a soluble form of CD59 in human urine.
9169007	11	8	part_of	heparin-binding	2142:2156	arg1	the putative heparin-binding site	heparin		the putative heparin-binding site		Fterm	Site	heparin		site	These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin.
9169007	11	105	part_of	site	2158:2161	arg1	antithrombin	antithrombin		site		PUBTATOR	Site	antithrombin	462	site	These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin.
11372680	3	40	part_of	sequence	492:499	arg1	a poly (A) tail	sequence		a poly (A) tail						tail	The cDNA contains 100 nucleotides 5' of a translation initiation codon and an open reading frame of 1344 nucleotides followed by a 163 nucleotide 3' untranslated sequence with a poly (A) tail.
1150658	4	23	gly	attached	849:856	arg3	Oligosaccharide side chains AND residues 52 and 78			residues 52 and 78	Oligosaccharide side chains					residues 52 and 78	Oligosaccharide side chains are attached at residues 52 and 78.
10441114	9	64	part_of	endostatin-related	1497:1514	arg1	immunoreactive endostatin-related C-terminal fragments	endostatin		immunoreactive endostatin-related C-terminal fragments		PUBTATOR	Site	endostatin	80781	fragments	Furthermore, immunoreactive endostatin-related C-terminal fragments of human collagen XV are found in the hemofiltrate.
10207177	0	33	gly	glycoproteins	68:80	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Oligosaccharide analysis and molecular modeling of soluble forms of glycoproteins belonging to the Ly-6, scavenger receptor, and immunoglobulin superfamilies expressed in Chinese hamster ovary cells.
18065761	7	34	part_of	TSPN-1	1334:1339	arg1	the TSPN-1 domain	TSPN-1		the TSPN-1 domain		Cterm	Site	TSPN-1		domain	The formation of cis and trans dimers of the TSPN-1 domain with relatively short segments of heparin further enhances the ability of TSP-1 to participate in high affinity binding to glycosaminoglycans.
11953431	5	44	part_of	amidotransferase	740:755	arg1	the class I glutamine amidotransferase domains	amidotransferase		the class I glutamine amidotransferase domains		Fterm	Site	amidotransferase		domains	The topology is very similar to that of the class I glutamine amidotransferase domains, with the only major differences consisting of extensions in four loops and at the C terminus.
7525874	11	47	gly	glycosylation	1274:1286	arg2	Asn29			Asn29 and Asn56						Asn29 and Asn56	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
11326277	10	22	part_of	have	1375:1378	arg1	T1r3 AND an extra amino-terminal glycosylation site	T1r3		an extra amino-terminal glycosylation site		PUBTATOR	Site	T1r3	83771	site	According to models of its structure, T1r3 from non-tasters is predicted to have an extra amino-terminal glycosylation site that, if used, would interfere with dimerization.
8942641	11	98	gly	glycosylated	1927:1938	arg1	the 140 and 150 kDa receptors	the 140 and 150 kDa receptors				Fterm		receptors			The results indicate the 140 and 150 kDa receptors are differentially glycosylated forms of the same polypeptide chain.
21757702	5	52	gly	found	712:716	arg1	a novel, non-traditional consensus site AND O-Glucose			a novel, non-traditional consensus site	O-Glucose					site	O-Glucose is also found at a novel, non-traditional consensus site at EGF 9.
3458201	1	17	gly	1B-glycoprotein	171:185	arg1	alpha 1B-glycoprotein	alpha 1B-glycoprotein				PUBTATOR		alpha 1B-glycoprotein	1		The complete amino acid sequence has been determined for alpha 1B-glycoprotein (alpha 1B), a protein of unknown function present in human plasma.
3458201	1	17	gly	1B-glycoprotein	171:185	arg1	alpha 1B	alpha 1B				PUBTATOR		alpha 1B	1		The complete amino acid sequence has been determined for alpha 1B-glycoprotein (alpha 1B), a protein of unknown function present in human plasma.
3458201	1	17	gly	1B-glycoprotein	171:185	arg1	a protein	a protein				Fterm		protein			The complete amino acid sequence has been determined for alpha 1B-glycoprotein (alpha 1B), a protein of unknown function present in human plasma.
18676855	3	26	gly	epitope	687:693	arg1	a hemagglutinin epitope tag				a hemagglutinin epitope tag						To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
12859190	5	16	gly	carries	592:598	arg1	the first tryptophan AND a C-linked hexosyl residue			the first tryptophan	a C-linked hexosyl residue					tryptophan	Here we report that the first tryptophan in the motif of the recombinant extracellular domain of EPOR (sEPOR) expressed in HEK-EBNA cells carries a C-linked hexosyl residue.
27314333	4	52	part_of	TSR1	847:850	arg1	TSR1 domain	TSR1		TSR1 domain		PUBTATOR	Site	TSR1	55720	domain	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
2390069	4	4	gly	non-fucosylated	726:740	arg1	two disialylated and non-fucosylated biantennary glycans				two disialylated and non-fucosylated biantennary glycans						Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	4	7	gly	released	636:643	arg1	human leucocyte lactotransferrin AND oligosaccharide alditols	human leucocyte lactotransferrin			oligosaccharide alditols	PUBTATOR		lactotransferrin	4057		Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	4	16	gly	disialylated	709:720	arg1	two disialylated and non-fucosylated biantennary glycans				two disialylated and non-fucosylated biantennary glycans						Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
18533687	11	83	gly	N-glycosylation	1774:1788	arg1	the receptor	the receptor				Fterm		receptor			Hence, as is the case for other LGR family members, N-glycosylation is essential for the transport of the receptor to the cell surface.
18586680	8	44	part_of	caspase-3	1343:1351	arg1	a novel caspase-3 cleavage site	caspase-3		a novel caspase-3 cleavage site		PUBTATOR	Site	caspase-3	836	site	These studies support the identification of O-GlcNAcase as a caspase-3 substrate with a novel caspase-3 cleavage site and provide insight about O-GlcNAcase regulation during apoptosis.
20427285	9	29	part_of	Gla	1268:1270	arg1	ZPI Gla domains	ZPI Gla		ZPI Gla domains		PUBTATOR	Site	ZPI Gla	51156	domains	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
20427285	9	73	part_of	ZPI	1264:1266	arg1	ZPI Gla domains	ZPI Gla		ZPI Gla domains		PUBTATOR	Site	ZPI Gla	51156	domains	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
11502179	1	29	gly	histidine	307:315	arg1	a 10-residue histidine tag			histidine	a 10-residue histidine tag					histidine	The amino-terminal ectodomain of the human TSH receptor has been expressed at the surface of CHO cells as a glycosylphosphatidylinositol-anchored molecule containing a 10-residue histidine tag close to its C terminus.
11502179	1	68	gly	containing	283:292	arg1	the human TSH receptor AND a 10-residue histidine tag	TSH receptor		ectodomain	a 10-residue histidine tag	PUBTATOR		TSH receptor	7253	ectodomain	The amino-terminal ectodomain of the human TSH receptor has been expressed at the surface of CHO cells as a glycosylphosphatidylinositol-anchored molecule containing a 10-residue histidine tag close to its C terminus.
2387072	0	21	part_of	residues	19:26	arg1	a secreted glycoprotein	glycoprotein		residues		Fterm	Site	glycoprotein		residues	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	0	21	part_of	residues	19:26	arg1	membrane glycoproteins	glycoproteins		residues		Fterm	Site	glycoproteins		residues	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
25092234	7	4	part_of	hFXI	994:997	arg1	hFXI glycopeptides	hFXI		hFXI glycopeptides		PUBTATOR	Site	hFXI	2160	glycopeptides	Analysis of hFXI glycopeptides by LC-MS/MS enabled site-specific glycan profiling and occupancy.
11703926	4	21	part_of	ephrin-B2	557:565	arg1	the extracellular domain	ephrin-B2		the extracellular domain		PUBTATOR	Site	ephrin-B2	13642	domain	We have determined the structure of the extracellular domain of mouse ephrin-B2.
9852066	3	64	part_of	CGA-derived	558:568	arg1	large CGA-derived fragments	CGA		large CGA-derived fragments		PUBTATOR	Site	CGA	1113	fragments	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
19690161	3	41	gly	sites	503:507	arg1	the glycans			sites	the glycans					sites	Here we describe heterogeneity in the composition of the glycans of the two N-linked sites of vIL-6.
9013598	0	29	part_of	sites	41:45	arg1	human testis angiotensin-converting enzyme	angiotensin-converting enzyme		sites		PUBTATOR	Site	angiotensin-converting enzyme	1636	sites	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
6776528	3	35	part_of	chain	393:397	arg1	the 511 alpha chain constant region	chain		the 511 alpha chain constant region		OGER	Site	chain		region	Comparison of the 511 alpha chain constant region with that of other mouse and human heavy chains shows that sequence divain.
9054441	0	0	part_of	plasminogen	75:85	arg1	Ser-248	plasminogen 2		Ser-248		OGER	SpecificSite	plasminogen 2	P00747	Ser-248	Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2.
15616124	4	68	gly	FVII	541:544	arg1	one and two N-glycans	FVII			one and two N-glycans	Cterm		FVII	2155		Pulse-chase labeled intracellular FVII migrated as two bands corresponding to FVII with one and two N-glycans, respectively.
17980170	2	0	gly	glycosylated	356:367	arg1	NAAA	NAAA				PUBTATOR		NAAA	27163		Previously, we suggested that NAAA is glycosylated and proteolytically cleaved.
9578468	6	33	gly	sialylated	952:961	arg1	at least two sialylated O-glycosylated variants	at least two sialylated O-glycosylated variants				Fterm		variants			It is O-glycosylated at Thr71, resulting in at least two sialylated O-glycosylated variants.
9578468	6	55	gly	O-glycosylated	901:914	arg2	Thr71			Thr71						Thr71	It is O-glycosylated at Thr71, resulting in at least two sialylated O-glycosylated variants.
9578468	6	72	gly	O-glycosylated	963:976	arg1	at least two sialylated O-glycosylated variants	at least two sialylated O-glycosylated variants				Fterm		variants			It is O-glycosylated at Thr71, resulting in at least two sialylated O-glycosylated variants.
26013384	6	28	gly	O-glycopeptide	797:810	arg2	O-glycopeptide profiles			O-glycopeptide profiles						O-glycopeptide	Peptide mapping analysis for each peak fraction using Asp-N and Glu-C shows differences in O-glycopeptide profiles at Ser126.
25265424	4	9	gly	fucosylation	561:572	arg1	the proteins	the proteins				Fterm		proteins			Our exoglycosidase-assisted LC-MS/MS analysis confirms the high degree of fucosylation of some of the proteins but shows that microheterogeneity is protein- and site-specific.
26811476	7	23	part_of	glycoproteins	1285:1297	arg1	the sequence	glycoproteins		the sequence		Fterm	Site	glycoproteins		sequence	This arrangement is required for filament formation and is directed by an ordered ZP-N/ZP-C linker that is not observed in ZP2 but is conserved in the sequence of deafness/Crohn's disease-associated homopolymeric glycoproteins α-tectorin (TECTA) and glycoprotein 2 (GP2).
12878160	9	48	part_of	VIPL	1153:1156	arg1	the cytoplasmic tail	VIPL		the cytoplasmic tail		PUBTATOR	Site	VIPL	81562	tail	Like VIP36, the cytoplasmic tail of VIPL terminates in the sequence KRFY, a motif characteristic for proteins recycling between the ER and ERGIC/cis-Golgi.
12527193	8	61	part_of	have	1162:1165	arg1	Mouse and human CRB3 AND identical intracellular domains	CRB3		domains		PUBTATOR	Site	CRB3	92359	domains	Mouse and human CRB3 have identical intracellular domains but divergent extracellular domains except for a conserved N-glycosylation site.
23209641	4	53	part_of	adiponectin	818:828	arg1	the galactosylhydroxylysine residues	adiponectin		the galactosylhydroxylysine residues		PUBTATOR	Site	adiponectin	Q15848	residues	In cells that totally lack LH3 enzyme, the galactosylhydroxylysine residues of adiponectin were not glucosylated to glucosylgalactosylhydroxylysine residues and the formation of high and middle molecular weight adiponectin oligomers was impaired.
10441114	0	43	gly	glycosylated	6:17	arg1	human plasma endostatin	human plasma endostatin				PUBTATOR		endostatin	80781		Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
1885588	1	11	gly	glycoprotein	209:220	arg1	N-linked glycoprotein processing	N-linked glycoprotein processing				Fterm		glycoprotein			We have analyzed the functional domain structure of rat mammary glucosidase I, an enzyme involved in N-linked glycoprotein processing, using biochemical and immunological approaches.
7512967	0	63	gly	O-glycosylation	0:14	arg1	hinge region			hinge region						region	O-glycosylation in hinge region of mouse immunoglobulin G2b.
2514791	5	7	gly	glycoprotein	1623:1634	arg1	the t-PA glycoprotein	the t-PA glycoprotein				PUBTATOR		t-PA glycoprotein	5327		These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	5	75	gly	oligosaccharides	1764:1779	arg1	a common polypeptide			a common polypeptide	a common polypeptide		Site			polypeptide	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
16877748	0	27	part_of	molecule-1	86:95	arg1	N-glycosylation sites	intercellular adhesion molecule-1		N-glycosylation sites		PUBTATOR	Site	intercellular adhesion molecule-1	15894	sites	N-glycan structures and N-glycosylation sites of mouse soluble intercellular adhesion molecule-1 revealed by MALDI-TOF and FTICR mass spectrometry.
20881961	2	36	part_of	plexin	383:388	arg1	the plexin ectodomain	plexin		the plexin ectodomain		Fterm	Site	plexin		ectodomain	The binding of soluble or membrane-anchored semaphorins to the membrane-distal region of the plexin ectodomain activates plexin's intrinsic GTPase-activating protein (GAP) at the cytoplasmic region, ultimately modulating cellular adhesion behaviour.
26598643	11	12	gly	O-glycosylation	1775:1789	arg2	11 novel O-glycosylation sites			11 novel O-glycosylation sites						sites	Strikingly, also 11 novel O-glycosylation sites and regions were identified.
6725284	8	2	gly	glycopeptide	1219:1230	arg2	the desialyzed resulting glycopeptide fraction			the desialyzed resulting glycopeptide fraction						glycopeptide	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
32363391	6	9	gly	O-glycosylation	1107:1121	arg2	the site			the site						site	Even though O-glycosylation has been predicted on the spike protein of SARS-CoV-2, this is the first report of experimental data for both the site of O-glycosylation and identity of the O-glycans attached on the subunit S1.
32363391	6	46	gly	O-glycosylation	969:983	arg1	the spike protein	the spike protein				Fterm		protein			Even though O-glycosylation has been predicted on the spike protein of SARS-CoV-2, this is the first report of experimental data for both the site of O-glycosylation and identity of the O-glycans attached on the subunit S1.
19022411	8	49	part_of	GAPDH	1362:1366	arg1	Thr227	GAPDH		Thr227		PUBTATOR	AminoAcid	GAPDH	2597	Thr227	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
19022411	8	49	part_of	GAPDH	1362:1366	arg1	the major GAPDH O-GlcNAcylation site	GAPDH		the major GAPDH O-GlcNAcylation site		PUBTATOR	Site	GAPDH	2597	site	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
22448645	0	64	gly	glycosylation	50:62	arg1	the human serotonin 5-HT₇a receptor	the human serotonin 5-HT₇a receptor				Cterm		5-HT₇a			Biochemical and pharmacological study of N-linked glycosylation of the human serotonin 5-HT₇a receptor.
23269669	6	16	gly	glycosylation	1148:1160	arg1	GC-C	GC-C		sites		PUBTATOR		GC-C	2984	sites	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
15173186	12	23	gly	glycosylation	1863:1875	arg2	Toll-like receptor 2 glycosylation sites			Toll-like receptor 2 glycosylation sites						sites	The remaining Toll-like receptor 2 glycosylation sites also contribute to efficient protein secretion, albeit to a lesser degree.
10821832	3	46	gly	glycosylated	864:875	arg1	glycosylated domains			glycosylated domains						domains	These results were further confirmed by expression of NPC1 and identification of glycosylated domains that are located in the lumen of the endoplasmic reticulum.
7688323	0	37	gly	O-glycosylation	19:33	arg2	an O-glycosylation site			an O-glycosylation site						site	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.
1577715	10	73	gly	asparagine-linked	1781:1797	arg1	these asparagine-linked oligosaccharides			asparagine	these asparagine-linked oligosaccharides					asparagine	Occurrence of these asparagine-linked oligosaccharides with blood group A and B structures suggest that the repeated use of factor VIII/vWF pooled concentrate for the treatment of hemophiliacs could result in the production of antibodies against vWF with a different blood group from that of the patient, and this development may be pathogenic.
11150294	7	69	part_of	MUPP1	1181:1185	arg1	MUPP1 PDZ domains	MUPP1		MUPP1 PDZ domains		OGER	Site	MUPP1	O75970	domains	Moreover, 5-HT(2A) and 5-HT(2B), sharing the C-terminal EX(V/I)SXV sequence with 5-HT(2C) receptors, also bind MUPP1 PDZ domains in vitro.
11706042	3	12	gly	glycosylation	525:537	arg2	9 N-linked glycosylation sites			9 N-linked glycosylation sites						sites	We demonstrate that MD-2 contains 2 N-glycosylated sites at positions Asn(26) and Asn(114), whereas the amino-terminal ectodomain of human TLR4 contains 9 N-linked glycosylation sites.
11706042	3	41	gly	N-glycosylated	397:410	arg1	2 N-glycosylated sites			2 N-glycosylated sites						sites	We demonstrate that MD-2 contains 2 N-glycosylated sites at positions Asn(26) and Asn(114), whereas the amino-terminal ectodomain of human TLR4 contains 9 N-linked glycosylation sites.
11706042	3	85	gly	positions	421:429	arg1	Asn(114)			positions Asn(26) and Asn(114)						positions Asn(26) and Asn(114)	We demonstrate that MD-2 contains 2 N-glycosylated sites at positions Asn(26) and Asn(114), whereas the amino-terminal ectodomain of human TLR4 contains 9 N-linked glycosylation sites.
11706042	3	85	gly	positions	421:429	arg1	Asn(26)			positions Asn(26) and Asn(114)						positions Asn(26) and Asn(114)	We demonstrate that MD-2 contains 2 N-glycosylated sites at positions Asn(26) and Asn(114), whereas the amino-terminal ectodomain of human TLR4 contains 9 N-linked glycosylation sites.
11706042	3	85	gly	positions	421:429	arg1	Asn(26)			positions Asn(26) and Asn(114)						positions Asn(26) and Asn(114)	We demonstrate that MD-2 contains 2 N-glycosylated sites at positions Asn(26) and Asn(114), whereas the amino-terminal ectodomain of human TLR4 contains 9 N-linked glycosylation sites.
21053369	0	79	gly	glycosylation	66:78	arg2	glycosylation sites			glycosylation sites						sites	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
19690161	2	71	gly	glycosylation	342:354	arg1	huIL-6 (1)	huIL-6 (1)				PUBTATOR		IL-6	3569		Our previous work showed that N-linked glycosylation was required for optimal function of vIL6 but not huIL-6 (1).
19556306	7	26	gly	TLR4	1167:1170	arg1	high mannose type	TLR4			high mannose type	PUBTATOR		TLR4	7099		alpha-Mannosidase II inhibitor blocked the processing N-glycans to complex type, but TLR4 with high mannose type appeared on the cell surface, suggesting that TLR4 is destined to locate on the cell surface before processing N-glycans from a high mannose type to a complex type.
16445295	10	54	part_of	contains	1373:1380	arg1	TAFI AND eight cysteine residues	TAFI		eight cysteine residues		PUBTATOR	AminoAcid	TAFI	1361	cysteine residues	TAFI contains eight cysteine residues, of which two, Cys69 and Cys383, are not involved in disulfides and contain free sulfhydryl groups.
20944746	5	24	part_of	domain	881:886	arg1	a single immunoglobulin-like domain	domain		a single immunoglobulin-like domain						domain	The pre-Tα chain comprised a single immunoglobulin-like domain that is structurally distinct from the constant (C) domain of the TCR α-chain; nevertheless, the mode of association between pre-Tα and TCRβ mirrored that mediated by the Cα-Cβ domains of the αβTCR.
20944746	5	72	part_of	α-chain	899:905	arg1	the constant (C) domain	TCR α-		the constant (C) domain		PUBTATOR	Site	TCR α-	28755	domain	The pre-Tα chain comprised a single immunoglobulin-like domain that is structurally distinct from the constant (C) domain of the TCR α-chain; nevertheless, the mode of association between pre-Tα and TCRβ mirrored that mediated by the Cα-Cβ domains of the αβTCR.
20944746	5	76	part_of	αβTCR	1021:1025	arg1	the Cα-Cβ domains	TCR		the Cα-Cβ domains		PUBTATOR	Site	TCR	6962	domains	The pre-Tα chain comprised a single immunoglobulin-like domain that is structurally distinct from the constant (C) domain of the TCR α-chain; nevertheless, the mode of association between pre-Tα and TCRβ mirrored that mediated by the Cα-Cβ domains of the αβTCR.
16368742	5	83	part_of	TRPV4	974:978	arg1	Residue N651	TRPV4		Residue N651		PUBTATOR	SpecificSite	TRPV4	59341	N651	Residue N651 of TRPV4 is immediately adjacent to the pore-forming loop.
12590919	3	18	gly	glycosylated	480:491	arg2	Asn(48)			Asn(48) and Asn(57)						Asn(48) and Asn(57)	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	3	18	gly	glycosylated	480:491	arg1	hENT2	hENT2		Asn(48) and Asn(57)		PUBTATOR		hENT2	3177	Asn(48) and Asn(57)	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	3	18	gly	glycosylated	480:491	arg1	hENT2	hENT2		Asn(48) and Asn(57)		PUBTATOR		hENT2	3177	Asn(48) and Asn(57)	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
21264968	6	74	part_of	MUC4	2024:2027	arg1	Thr10	MUC4		Thr10		PUBTATOR	AminoAcid	MUC4	4585	Thr10	The solution structures determined by NMR spectroscopic studies elicited that the preferential introduction of α-GalNAc at Thr10 of MUC4 stabilizes specifically a β-like extended backbone structure at this area, whereas other synthetic models with a single α-GalNAc residue at Thr1, Thr6, or Thr15 did not exhibit any converged three-dimensional structure at the proximal peptide moiety.
14693913	3	79	part_of	has	437:439	arg1	hBSSL AND one N-glycosylation site	hBSSL		one N-glycosylation site		PUBTATOR	Site	hBSSL	1056	site	hBSSL has one N-glycosylation site at Asn187, which was 38-40% occupied with a Man(10)GlcNAc(2) structure defined previously in Pichia as the oligosaccharide-lipid form of Man(9)GlcNAc(2) trimmed of the middle-arm terminal alpha 1,2-Man and elongated with Man alpha 1,2Man alpha 1,6-disaccharide attached to the lower-arm core alpha 1,3-Man (Trimble et al. [1991], J. Biol.
10092871	9	34	gly	glycosylation	1512:1524	arg2	the two potential glycosylation sites			the two potential glycosylation sites						sites	We also show that, of the two potential glycosylation sites in the MMP-1 sequence, only Asn120 is used.
10092871	9	66	gly	used	1570:1573	arg2	only Asn120			only Asn120						Asn120	We also show that, of the two potential glycosylation sites in the MMP-1 sequence, only Asn120 is used.
22601780	5	58	part_of	EGF	583:585	arg1	its 3 EGF domains	3 EGF		its 3 EGF domains		OGER	Site	3 EGF	P01133	domains	We report the crystal structure of its 3 EGF domains.
1737041	2	24	gly	sites	481:485	arg1	two N-linked carbohydrate side chains			sites	two N-linked carbohydrate side chains					sites	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	2	21	gly	contains	395:402	arg1	Human GM-CSF AND two N-linked carbohydrate side chains	Human GM-CSF			two N-linked carbohydrate side chains	PUBTATOR		Human GM-CSF	1437		Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
7535613	11	62	part_of	PSA	1606:1608	arg1	The PSA glycosylation site	PSA		site, Asn 61		PUBTATOR	SpecificSite	PSA	P07288	site, Asn 61	The PSA glycosylation site, Asn 61, is fully accessible to the solvent and is enclosed in a positive region of the isopotential map.
3264725	3	66	part_of	VIIa	727:730	arg1	the amino acid sequence	factor VIIa		the amino acid sequence		Cterm	Site	factor VIIa		sequence	In the present study, the amino acid sequence and posttranslational modifications of recombinant factor VIIa as purified from the culture medium of a transfected baby hamster kidney cell line have been compared to human plasma factor VIIa.
21138434	0	20	part_of	subunit	75:81	arg1	N-glycosylated residues	subunit		N-glycosylated residues		Fterm	Site	subunit		residues	The identification of N-glycosylated residues of the human 5-HT3B receptor subunit: importance for cell membrane expression.
12610629	0	47	part_of	HER2	41:44	arg1	the extracellular region	HER2		the extracellular region		PUBTATOR	Site	HER2	2064	region	Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab.
23661698	5	50	gly	deglycosylated	651:664	arg1	deglycosylated ephrin-A1	deglycosylated ephrin-A1				PUBTATOR		ephrin-A1	1942		We found that deglycosylated ephrin-A1 does not efficiently induce EphA2 receptor internalization and degradation, and does not activate the downstream signaling pathways involved in cell migration and proliferation.
3458201	6	13	part_of	1B	782:783	arg1	several domains	alpha 1B		several domains		PUBTATOR	Site	alpha 1B	1	domains	However, several domains of alpha 1B, especially the third, show statistically significant homology to variable regions of certain immunoglobulin light and heavy chains.
23001782	11	20	part_of	hSHBG	1946:1950	arg1	a prerequisite	hSHBG		a prerequisite		PUBTATOR	Site	hSHBG	6462	prerequisite	To date, this work represents the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans.
6171497	3	38	gly	attached	493:500	arg2	Carbohydrate side chains AND two positions			two positions	Carbohydrate side chains					positions	Carbohydrate side chains are attached in two positions.
10712595	6	53	gly	glycosylated	1104:1115	arg2	Asn135	antithrombin		Asn135		PUBTATOR		antithrombin	462	Asn135	The high heparin binding affinity of the salmon inhibitor, Kd of 2.2 and 48 nM at I = 0.15 and 0.3, respectively, is very similar to that of the minor human isoform beta-antithrombin, which is not glycosylated at Asn135.
9425112	7	33	gly	glycosylated	1113:1124	arg2	Asn-72			Asn-72						Asn-72	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
9425112	7	46	gly	N-glycosylation	1074:1088	arg2	potential N-glycosylation sites			potential N-glycosylation sites						sites	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
2498325	12	32	gly	glycosylation	1825:1837	arg1	apoE	apoE				PUBTATOR		apoE	P02649		The transfected ldlD cells also secreted high levels of apoE even in the absence of glycosylation, which confirms that glycosylation is not essential for secretion of apoE.
11098061	8	11	part_of	cysteines	1245:1253	arg1	gp130	gp130		cysteines		PUBTATOR	AminoAcid	gp130	P40189	cysteines	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	16	part_of	gp130	1285:1289	arg1	the NH2-terminal domain	gp130		the NH2-terminal domain		PUBTATOR	Site	gp130	P40189	domain	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
18691975	4	51	part_of	ICAM-5	682:687	arg1	the N-terminal two domains	ICAM-5		the N-terminal two domains		PUBTATOR	Site	ICAM-5	Q9UMF0	domains	We describe the crystal structure of an engineered high-affinity I domain from the integrin alpha(L)beta(2) (LFA-1) alpha subunit in complex with the N-terminal two domains of ICAM-5, an adhesion molecule expressed in telencephalic neurons.
18691975	4	54	part_of	subunit	628:634	arg1	an engineered high-affinity I domain	subunit		an engineered high-affinity I domain		Fterm	Site	subunit		domain	We describe the crystal structure of an engineered high-affinity I domain from the integrin alpha(L)beta(2) (LFA-1) alpha subunit in complex with the N-terminal two domains of ICAM-5, an adhesion molecule expressed in telencephalic neurons.
3651384	0	61	gly	glycoprotein	47:58	arg1	sulfated glycoprotein 2	sulfated glycoprotein 2				PUBTATOR		sulfated glycoprotein 2	24854		Biosynthesis and molecular cloning of sulfated glycoprotein 2 secreted by rat Sertoli cells.
17322565	2	42	gly	glycosylation	516:528	arg1	EL	EL				PUBTATOR		EL	9388		The current study demonstrates that mutagenesis of either Asn-116 to threonine (Thr) or Thr-118 to Ala also disrupted the glycosylation of EL and enhanced catalytic activity toward synthetic substrates by 3-fold versus wild-type EL.
8486673	5	34	gly	attached	787:794	arg2	Asn-128 AND one oligosaccharide chain			Asn-128	one oligosaccharide chain					Asn-128	FAB-MS, electrospray-mass spectrometry, and linkage analysis demonstrated that each monomer of rat CRP contained one oligosaccharide chain, predominantly a disialylated biantennary structure, attached to Asn-128.
8486673	5	71	gly	disialylated	751:762	arg1	a disialylated biantennary structure				a disialylated biantennary structure						FAB-MS, electrospray-mass spectrometry, and linkage analysis demonstrated that each monomer of rat CRP contained one oligosaccharide chain, predominantly a disialylated biantennary structure, attached to Asn-128.
8486673	5	69	gly	contained	698:706	arg1	rat CRP AND one oligosaccharide chain	rat CRP			one oligosaccharide chain	PUBTATOR		CRP	25419		FAB-MS, electrospray-mass spectrometry, and linkage analysis demonstrated that each monomer of rat CRP contained one oligosaccharide chain, predominantly a disialylated biantennary structure, attached to Asn-128.
24058541	0	28	gly	N-glycosylation	12:26	arg1	lysosomal protein CLN5	lysosomal protein CLN5				OGER		protein CLN5	O75503		The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.
12297050	1	30	part_of	receptor	203:210	arg1	the EGF receptor (EGFR) extracellular region	EGF receptor		the EGF receptor (EGFR) extracellular region		PUBTATOR	Site	EGF receptor	1956	region	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
15173186	12	22	part_of	Toll-like	1842:1850	arg1	Toll-like receptor 2 glycosylation sites	Toll-like receptor 2		Toll-like receptor 2 glycosylation sites		PUBTATOR	Site	Toll-like receptor 2	7097	sites	The remaining Toll-like receptor 2 glycosylation sites also contribute to efficient protein secretion, albeit to a lesser degree.
15173186	12	81	part_of	receptor	1852:1859	arg1	Toll-like receptor 2 glycosylation sites	Toll-like receptor 2		Toll-like receptor 2 glycosylation sites		PUBTATOR	Site	Toll-like receptor 2	7097	sites	The remaining Toll-like receptor 2 glycosylation sites also contribute to efficient protein secretion, albeit to a lesser degree.
22387313	3	26	part_of	containing	497:506	arg1	DPP10 AND eight predicted N-glycosylation sites	DPP10		eight predicted N-glycosylation sites		PUBTATOR	Site	DPP10	57628	sites	DPP10 is a glycoprotein containing eight predicted N-glycosylation sites in the extracellular domain.
22387313	3	26	part_of	containing	497:506	arg1	a glycoprotein AND eight predicted N-glycosylation sites	a glycoprotein		eight predicted N-glycosylation sites		Fterm	Site	glycoprotein		sites	DPP10 is a glycoprotein containing eight predicted N-glycosylation sites in the extracellular domain.
8486673	4	46	gly	CRP	452:454	arg1	the oligosaccharide chain	CRP			the oligosaccharide chain	PUBTATOR		CRP	25419		In this study, the nature of the oligosaccharide chain of rat CRP was investigated by fast atom bombardment-mass spectrometry (FAB-MS), and general features of its biosynthetic pathway were also analyzed.
21053369	7	94	gly	glycopeptides	1208:1220	arg2	target glycopeptides			target glycopeptides						glycopeptides	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
16203964	0	36	part_of	ErbB4	28:32	arg1	The extracellular region	ErbB4		The extracellular region		PUBTATOR	Site	ErbB4	2066	region	The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand.
3410849	2	22	gly	glycopeptide	119:130	arg2	a glycopeptide			a glycopeptide						glycopeptide	Nephritogenoside is a glycopeptide with the ability to induce chronic progressive glomerulonephritis (end stage kidney) in homologous animals, by a single footpad injection.
10769135	3	32	gly	sugars	535:540	arg1	the glycon (-1, -2, -3) sites			the glycon (-1, -2, -3) sites	the glycon (-1, -2, -3) sites		Site			sites	The preferred binding/cleavage mode occurs when a maltose residue serves as the leaving group (aglycone sites +1 and +2) and there are three sugars in the glycon (-1, -2, -3) sites.
20188224	1	6	part_of	granulin	159:166	arg1	the granulin domain	granulin		the granulin domain		PUBTATOR	Site	granulin	2896	domain	PGRN is a modular protein with 7 1/2 repeats of the granulin domain separated by short spacer sequences.
27314333	6	14	gly	N-glycosylation	1013:1027	arg2	the N-glycosylation site			the N-glycosylation site						site	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
21752865	3	59	gly	glycosylated	714:725	arg1	BRI2	BRI2				PUBTATOR		BRI2	9445		Its apparent molecular mass (42-44 kDa) is significantly higher than that predicted by the number and composition of amino acids (30 kDa) suggesting that BRI2 is glycosylated.
15628971	7	0	gly	microheterogeneity	1564:1581	arg1	N-linked oligosaccharides				N-linked oligosaccharides						In addition, the N-linked oligosaccharide at the C-terminal region appears to affect the glycosylation pattern of recombinant C4ST; a broad protein band of the wildtype protein resulting from microheterogeneity of N-linked oligosaccharides disappeared and four discrete protein bands with different numbers of N-linked oligosaccharides appeared when the N-linked oligosaccharide at the C-terminal region was deleted.
15628971	7	66	gly	region	1432:1437	arg1	the N-linked oligosaccharide			region	the N-linked oligosaccharide					region	In addition, the N-linked oligosaccharide at the C-terminal region appears to affect the glycosylation pattern of recombinant C4ST; a broad protein band of the wildtype protein resulting from microheterogeneity of N-linked oligosaccharides disappeared and four discrete protein bands with different numbers of N-linked oligosaccharides appeared when the N-linked oligosaccharide at the C-terminal region was deleted.
15628971	7	83	gly	glycosylation	1461:1473	arg1	recombinant C4ST	recombinant C4ST				PUBTATOR		C4ST	314694		In addition, the N-linked oligosaccharide at the C-terminal region appears to affect the glycosylation pattern of recombinant C4ST; a broad protein band of the wildtype protein resulting from microheterogeneity of N-linked oligosaccharides disappeared and four discrete protein bands with different numbers of N-linked oligosaccharides appeared when the N-linked oligosaccharide at the C-terminal region was deleted.
15628971	7	104	gly	region	1769:1774	arg1	the N-linked oligosaccharide			region	the N-linked oligosaccharide					region	In addition, the N-linked oligosaccharide at the C-terminal region appears to affect the glycosylation pattern of recombinant C4ST; a broad protein band of the wildtype protein resulting from microheterogeneity of N-linked oligosaccharides disappeared and four discrete protein bands with different numbers of N-linked oligosaccharides appeared when the N-linked oligosaccharide at the C-terminal region was deleted.
14749323	5	1	gly	glycosylation	734:746	arg2	putative glycosylation sites			putative glycosylation sites						sites	In the present study, we investigated the effect of disrupting putative glycosylation sites in mOAT1 as well as its human counterpart, hOAT1, by mutating asparagine to glutamine and assessing mutant transporters in HeLa cells.
24076154	3	15	gly	glycosylated	607:618	arg1	The recombinant rat and monkey enzymes	The recombinant rat and monkey enzymes				Fterm		enzymes			The recombinant rat and monkey enzymes expressed in Sf9 insect cells (IAP-Ic) were found to be glycosylated and active.
19506079	7	14	part_of	CaMKIV	952:957	arg1	the active site	CaMKIV		the active site		PUBTATOR	Site	CaMKIV	814	site	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
26791533	2	31	part_of	present	320:326	arg2	seminal plasma glycoproteins AND Epitopes	seminal plasma glycoproteins		Epitopes		Fterm		glycoproteins			Epitopes such as Lewis x and y are known to be present on seminal plasma glycoproteins, which can modulate the maternal immune response.
21056543	6	7	gly	Thr20	1101:1105	arg1	NeuAcGalGalNAc			Thr20	NeuAcGalGalNAc					Thr20	Furthermore, we have provided experimental evidence that PCI in both individuals is O-glycosylated on Thr20 with a core type 1 O-glycan, which is mostly NeuAcGalGalNAc.
21056543	6	7	gly	Thr20	1101:1105	arg1	a core type 1 O-glycan			Thr20	a core type 1 O-glycan					Thr20	Furthermore, we have provided experimental evidence that PCI in both individuals is O-glycosylated on Thr20 with a core type 1 O-glycan, which is mostly NeuAcGalGalNAc.
21056543	6	15	gly	O-glycosylated	1083:1096	arg1	PCI			Thr20	PCI					Thr20	Furthermore, we have provided experimental evidence that PCI in both individuals is O-glycosylated on Thr20 with a core type 1 O-glycan, which is mostly NeuAcGalGalNAc.
21056543	6	15	gly	O-glycosylated	1083:1096	arg1	Thr20			Thr20						Thr20	Furthermore, we have provided experimental evidence that PCI in both individuals is O-glycosylated on Thr20 with a core type 1 O-glycan, which is mostly NeuAcGalGalNAc.
21056543	6	15	gly	O-glycosylated	1083:1096	arg1	Thr20			Thr20	PCI					Thr20	Furthermore, we have provided experimental evidence that PCI in both individuals is O-glycosylated on Thr20 with a core type 1 O-glycan, which is mostly NeuAcGalGalNAc.
24509848	11	42	gly	presence	1630:1637	arg2	that site AND glycan moieties			that site	glycan moieties					site	The presence of glycan moieties at that site may help to lock the collagen-binding domain in the inactive state and prevent unwarranted signaling by receptor dimers.
10715549	7	40	gly	N-glycosylation	1344:1358	arg1	Asn	CGbeta		Asn(13)		PUBTATOR	SpecificSite	CGbeta	1082	Asn(13)	Both CGbeta wild-type (WT) and CGbeta lacking N-glycosylation at Asn(13) (CGbeta-N13) showed aggregates in lysate.
10715549	7	40	gly	N-glycosylation	1344:1358	arg1	13	CGbeta		Asn(13)		PUBTATOR	SpecificSite	CGbeta	1082	Asn(13)	Both CGbeta wild-type (WT) and CGbeta lacking N-glycosylation at Asn(13) (CGbeta-N13) showed aggregates in lysate.
10715549	7	40	gly	N-glycosylation	1344:1358	arg2	Asn	CGbeta		Asn(13)		PUBTATOR	SpecificSite	CGbeta	1082	Asn(13)	Both CGbeta wild-type (WT) and CGbeta lacking N-glycosylation at Asn(13) (CGbeta-N13) showed aggregates in lysate.
10715549	7	40	gly	N-glycosylation	1344:1358	arg2	CGbeta-N13	CGbeta		N13		PUBTATOR	SpecificSite	CGbeta	1082	N13	Both CGbeta wild-type (WT) and CGbeta lacking N-glycosylation at Asn(13) (CGbeta-N13) showed aggregates in lysate.
10715549	7	40	gly	N-glycosylation	1344:1358	arg2	13	CGbeta		Asn(13)		PUBTATOR	SpecificSite	CGbeta	1082	Asn(13)	Both CGbeta wild-type (WT) and CGbeta lacking N-glycosylation at Asn(13) (CGbeta-N13) showed aggregates in lysate.
10715549	7	40	gly	N-glycosylation	1344:1358	arg1	13			Asn(13)						Asn(13)	Both CGbeta wild-type (WT) and CGbeta lacking N-glycosylation at Asn(13) (CGbeta-N13) showed aggregates in lysate.
10715549	7	40	gly	N-glycosylation	1344:1358	arg2	Asn			Asn(13)						Asn(13)	Both CGbeta wild-type (WT) and CGbeta lacking N-glycosylation at Asn(13) (CGbeta-N13) showed aggregates in lysate.
10715549	7	40	gly	N-glycosylation	1344:1358	arg2	13			Asn(13)						Asn(13)	Both CGbeta wild-type (WT) and CGbeta lacking N-glycosylation at Asn(13) (CGbeta-N13) showed aggregates in lysate.
10715549	7	40	gly	N-glycosylation	1344:1358	arg2	Asn			Asn(13)						Asn(13)	Both CGbeta wild-type (WT) and CGbeta lacking N-glycosylation at Asn(13) (CGbeta-N13) showed aggregates in lysate.
10715549	7	40	gly	N-glycosylation	1344:1358	arg2	13			Asn(13)						Asn(13)	Both CGbeta wild-type (WT) and CGbeta lacking N-glycosylation at Asn(13) (CGbeta-N13) showed aggregates in lysate.
10715549	7	40	gly	N-glycosylation	1344:1358	arg2	13			Asn(13)						Asn(13)	Both CGbeta wild-type (WT) and CGbeta lacking N-glycosylation at Asn(13) (CGbeta-N13) showed aggregates in lysate.
25568315	1	71	part_of	contains	186:193	arg1	The extracellular loop 3 AND 4 highly conserved cysteines	extracellular loop 3 (EL-3		cysteines		PUBTATOR	AminoAcid	extracellular loop 3 (EL-3	6710	cysteines	The extracellular loop 3 (EL-3) of SLC4 Na(+)-coupled transporters contains 4 highly conserved cysteines and multiple N-glycosylation consensus sites.
25568315	1	71	part_of	contains	186:193	arg1	The extracellular loop 3 AND multiple N-glycosylation consensus sites	extracellular loop 3 (EL-3		sites		PUBTATOR	Site	extracellular loop 3 (EL-3	6710	sites	The extracellular loop 3 (EL-3) of SLC4 Na(+)-coupled transporters contains 4 highly conserved cysteines and multiple N-glycosylation consensus sites.
17591618	5	61	gly	disialylated	942:953	arg1	diantennary disialylated glycans				diantennary disialylated glycans						This mass difference is consistent with CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites.
17591618	5	79	gly	glycosylation	913:925	arg1	eight sites			sites						sites	This mass difference is consistent with CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites.
15616124	10	37	gly	N-glycosylation	1561:1575	arg1	a non-modified protein	a non-modified protein				Fterm		protein			This is the first documentation of posttranslational N-glycosylation of a non-modified protein in mammalian cells with an intact N-glycosylation machinery.
24342833	4	17	gly	Type-β-catenin	725:738	arg1	potential O-GlcNAc sites	-catenin			potential O-GlcNAc sites	PUBTATOR		-catenin	1499		METHOD: Missense mutations were introduced to potential O-GlcNAc sites of pEGFP-C2-N-Terminal- or pEGFP-C2-Wild Type-β-catenin by site-directed mutagenesis.
2642896	1	83	part_of	synthetase	139:148	arg1	The amino acid sequence	synthetase		The amino acid sequence		Fterm	Site	synthetase		sequence	The amino acid sequence of rat brain prostaglandin D synthetase (Urade, Y., Fujimoto, N., and Hayaishi, O. (1985) J. Biol.
16186819	2	12	part_of	THBS2	308:312	arg1	the glycosylated signature domain	THBS2		the glycosylated signature domain		PUBTATOR	Site	THBS2	7058	domain	Here, we describe the 2.6-A-resolution crystal structure of the glycosylated signature domain of human THBS2, which includes three epidermal growth factor-like modules, 13 aspartate-rich repeats and a lectin-like module.
1740433	9	31	gly	glycosylated	1273:1284	arg1	these sites			these sites						sites	Studies indicate that approximately 50% of these sites are glycosylated, thereby giving rise to two size classes, 14 and 19 kDa, of C-SAA in vivo.
19139490	3	48	gly	glycoproteins	460:472	arg1	CF glycoproteins	CF glycoproteins				Fterm		glycoproteins			However, current techniques are unable to reveal CF glycoproteins precisely on a large scale.
26271046	11	76	gly	N-glycans	1912:1920	arg1	GluA2	GluA2			N-glycans	PUBTATOR		GluA2	2891		Thus, our data suggested that site-specific N-glycans on GluA2 regulate the intracellular trafficking and cell surface expression of AMPAR.
28668641	1	3	part_of	glycoprotein	128:139	arg1	three predicted glycosylation sites	glycoprotein		three predicted glycosylation sites		Fterm	Site	glycoprotein		sites	Vaspin is a glycoprotein with three predicted glycosylation sites at asparagine residues located in proximity to the reactive center loop and close to domains that play important roles in conformational changes underlying serpin function.
1708771	11	4	gly	glycosylated	1637:1648	arg1	Asn120			Asn120						Asn120	Sequence determination of isolated peptides suggested that Asn120 is glycosylated, Asn65 and Asn109 glycosylated in some molecules but not in others, and Asn72 not glycosylated.
12654314	9	80	gly	attached	1537:1544	arg1	Asn-363 AND Only two high-mannose type oligosaccharides			Asn-363	Only two high-mannose type oligosaccharides					Asn-363	Only two high-mannose type oligosaccharides were attached to Asn-363.
23139753	3	39	part_of	WFDC	349:352	arg1	a conserved WFDC domain	WFDC		a conserved WFDC domain		Cterm	Site	WFDC		domain	A WFDC protein has a conserved WFDC domain of 50 amino acids with eight conserved cystine residue.
23139753	3	30	part_of	has	333:335	arg1	A WFDC protein AND a conserved WFDC domain	A WFDC protein		a conserved WFDC domain		Fterm	Site	protein		domain	A WFDC protein has a conserved WFDC domain of 50 amino acids with eight conserved cystine residue.
3667593	0	43	gly	interferon-beta	46:60	arg1	the carbohydrate moiety	interferon-beta			the carbohydrate moiety	PUBTATOR		interferon-beta	3456		Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line.
10704524	8	82	gly	sialylated	1419:1428	arg1	unique phosphorylated and sialylated structures				unique phosphorylated and sialylated structures						Approximately 54% of the hybrid oligosaccharide were phosphorylated and one-third of these structures were further sialylated, the latter representing unique phosphorylated and sialylated structures.
26271046	10	7	gly	epitope	1768:1774	arg1	N-glycan				N-glycan						The HNK-1 epitope on N-glycan at the N413 of GluA2 was also involved in the cell surface expression of GluA1.
26271046	10	63	gly	N413	1795:1798	arg1	The HNK-1 epitope			N413	The HNK-1 epitope					N413	The HNK-1 epitope on N-glycan at the N413 of GluA2 was also involved in the cell surface expression of GluA1.
18657508	3	1	part_of	CD47	513:516	arg1	The unusual and convoluted interacting face	CD47		The unusual and convoluted interacting face		PUBTATOR	Site	CD47	961	face	The unusual and convoluted interacting face of CD47, comprising the N terminus and loops at the end of the domain, intercalates with the corresponding regions in SIRPalpha.
18657508	3	21	part_of	regions	617:623	arg1	SIRPalpha	SIRPalpha		regions		PUBTATOR	Site	SIRPalpha	140885	regions	The unusual and convoluted interacting face of CD47, comprising the N terminus and loops at the end of the domain, intercalates with the corresponding regions in SIRPalpha.
8702538	6	81	part_of	CD22	1059:1062	arg1	the first immunoglobulin domain	CD22		the first immunoglobulin domain		PUBTATOR	Site	CD22	933	domain	We show that mutation of a single potential N-linked glycosylation site in the first immunoglobulin domain of CD22 completely abrogates ligand recognition.
2498325	8	70	gly	N-glycosylation	1261:1275	arg2	position 194			position 194,						position 194,	Apolipoprotein E(Thr194----Asn,Gly196----Ser), which introduces a potential site for N-glycosylation at position 194, was secreted with a higher apparent molecular weight than native, O-glycosylated apoE.
12603841	8	24	gly	domain	1388:1393	arg1	the two conserved ligand-binding domain glycans				the two conserved ligand-binding domain glycans						We therefore report that the two conserved ligand-binding domain glycans do not play any major role in receptor-ligand interactions, do not impart a stabilizing effect on the ligand-binding domain, and are not critical for the formation and surface localization of homomeric GluR-D AMPA receptors in HEK293 cells.
3463996	5	65	part_of	sequences	1014:1022	arg1	the propeptide	sequences		the propeptide						propeptide	In particular, two conserved sequences in the propeptide that may be functionally significant include a potential glycosylation site and the presence of a single cysteine at position 59.
19931471	3	43	part_of	TLR2-TLR6-diacylated	343:362	arg1	TLR2-TLR6-diacylated lipopeptide	TLR6		TLR2-TLR6-diacylated lipopeptide		PUBTATOR	Site	TLR6	10333	lipopeptide	We have determined the crystal structures of TLR2-TLR6-diacylated lipopeptide, TLR2-lipoteichoic acid, and TLR2-PE-DTPA complexes.
22660477	5	13	part_of	GBR2	551:554	arg1	the GBR2 ectodomain	GBR2		the GBR2 ectodomain		Cterm	Site	GBR2		ectodomain	Here we demonstrate that the GBR2 ectodomain directly interacts with the GBR1 ectodomain to increase agonist affinity by selectively stabilizing the agonist-bound conformation of GBR1.
10988252	1	67	part_of	having	194:199	arg1	a transmembrane glycoprotein AND 11 potential N-glycosylation sites	a transmembrane glycoprotein		11 potential N-glycosylation sites		Fterm	Site	glycoprotein		sites	The human epidermal growth factor receptor (EGFR) is a transmembrane glycoprotein having 11 potential N-glycosylation sites in its extracellular domain.
10988252	1	67	part_of	having	194:199	arg1	The human epidermal growth factor receptor AND 11 potential N-glycosylation sites	The human epidermal growth factor receptor		11 potential N-glycosylation sites		PUBTATOR	Site	epidermal growth factor receptor	1956	sites	The human epidermal growth factor receptor (EGFR) is a transmembrane glycoprotein having 11 potential N-glycosylation sites in its extracellular domain.
1517205	2	31	gly	factor	504:509	arg1	a tetrasaccharide O-fucosidically	factor IX			a tetrasaccharide O-fucosidically	OGER		factor IX	P00740		We now have evidence of another modification in the first EGF-like domain of human factor IX, which proved to be a tetrasaccharide O-fucosidically linked to Ser-61.
1517205	2	74	gly	linked	568:573	arg2	Ser-61 AND a tetrasaccharide O-fucosidically			Ser-61	a tetrasaccharide O-fucosidically					Ser-61	We now have evidence of another modification in the first EGF-like domain of human factor IX, which proved to be a tetrasaccharide O-fucosidically linked to Ser-61.
24121512	4	9	part_of	AE1	955:957	arg1	the cytosolic domain	AE1		the cytosolic domain		PUBTATOR	Site	AE1	6521	domain	Introduction of single and double mutations at the equivalent arginine (Arg(283)) and at an interacting glutamate (Glu(85)) in the cytosolic domain of human AE1 (cdAE1) had no effect on the cell surface expression or the transport activity of AE1 expressed in HEK-293 cells.
24721674	3	52	gly	N-glycosylation	796:810	arg2	protein N-glycosylation sites			protein N-glycosylation sites						sites	In this study, a systematic approach was developed which combined: an integrated hydrophilic interaction chromatography solid phase interaction (HILIC SPE) for simultaneous detergent removal and glycopeptide enrichment, and mass spectrometric identification of both protein N-glycosylation sites and site-specific glycan composition.
24721674	3	71	gly	glycopeptide	717:728	arg2	glycopeptide enrichment			glycopeptide enrichment						glycopeptide	In this study, a systematic approach was developed which combined: an integrated hydrophilic interaction chromatography solid phase interaction (HILIC SPE) for simultaneous detergent removal and glycopeptide enrichment, and mass spectrometric identification of both protein N-glycosylation sites and site-specific glycan composition.
2476841	8	18	gly	contain	1221:1227	arg1	This Mr 27,000 protein AND one N-linked oligosaccharide residue	This Mr 27,000 protein			one N-linked oligosaccharide residue	Fterm		protein			This Mr 27,000 protein was found to contain one N-linked oligosaccharide residue by endoglycosidase-F treatment.
18467335	0	14	part_of	inhibitor	42:50	arg1	the N terminus	protein C inhibitor		the N terminus		OGER	Site	protein C inhibitor	P05154	terminus	N-glycans and the N terminus of protein C inhibitor affect the cofactor-enhanced rates of thrombin inhibition.
22363519	5	6	gly	receptor	866:873	arg1	the complex crystal structure	receptor			the complex crystal structure	Fterm		receptor			Based on the complex crystal structure of the decoy receptor with MD2, we first designed single amino acid substitutions in the decoy receptor, and obtained three variants showing a binding affinity (K(D)) one-order of magnitude higher than the wild-type decoy receptor.
21467029	6	9	part_of	COX	764:766	arg1	the COX site	COX		the COX site		OGER	Site	COX		site	Heme binds tightly only to the peroxidase site of E(cat), whereas substrates, as well as certain inhibitors (e.g. celecoxib), bind the COX site of E(cat).
21467029	6	57	part_of	peroxidase	660:669	arg1	the peroxidase site	peroxidase		the peroxidase site		Fterm	Site	peroxidase		site	Heme binds tightly only to the peroxidase site of E(cat), whereas substrates, as well as certain inhibitors (e.g. celecoxib), bind the COX site of E(cat).
17503783	4	38	part_of	EGF-like	920:927	arg1	this unique EGF-like domain	EGF		this unique EGF-like domain		OGER	Site	EGF	P01133	domain	The structure shows that the fold of this unique EGF-like domain is intact in four alternative splice-variants, whereas the catalytic domain is likely to be unfolded.
16964247	3	7	gly	Ser	540:542	arg1	O-GlcNAcylation			Ser 149	O-GlcNAcylation					Ser 149	Accordingly, O-GlcNAcylation at Ser 149 stabilizes p53 by blocking ubiquitin-dependent proteolysis.
9295302	9	87	gly	N-Glycosylation	1419:1433	arg1	Asn23			Asn19 and Asn23						Asn19 and Asn23	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
16445295	7	61	gly	attached	1108:1115	arg1	Asn22 AND the glycan			Asn22	the glycan					Asn22	Four of the glycans, Asn51, Asn63, Asn86, and Asn219 displayed microheterogeneity, while the glycan attached to Asn22 appeared to be homogeneous.
23894062	8	56	part_of	SOST	1039:1042	arg1	a SOST peptide	SOST		a SOST peptide		PUBTATOR	Site	SOST	50964	peptide	We showed a SOST peptide (SOST-S146, with homology to a bacterial glycotransferase peptide) binds to a NOG peptide (NOG-N54), which contains a N-glycosylation site.
23894062	8	94	part_of	NOG	1130:1132	arg1	NOG-N54	NOG		NOG-N54		PUBTATOR	SpecificSite	NOG	9241	N54	We showed a SOST peptide (SOST-S146, with homology to a bacterial glycotransferase peptide) binds to a NOG peptide (NOG-N54), which contains a N-glycosylation site.
23894062	8	94	part_of	NOG	1130:1132	arg1	a NOG peptide	NOG		a NOG peptide		PUBTATOR	Site	NOG	9241	peptide	We showed a SOST peptide (SOST-S146, with homology to a bacterial glycotransferase peptide) binds to a NOG peptide (NOG-N54), which contains a N-glycosylation site.
23894062	8	68	part_of	contains	1159:1166	arg1	a NOG peptide AND a N-glycosylation site	NOG		site		PUBTATOR	Site	NOG	9241	site	We showed a SOST peptide (SOST-S146, with homology to a bacterial glycotransferase peptide) binds to a NOG peptide (NOG-N54), which contains a N-glycosylation site.
22718755	8	49	part_of	ALK1	1148:1151	arg1	the extracellular domains	ALK1		the extracellular domains		PUBTATOR	Site	ALK1	94	domains	We also report the crystal structure of a fully assembled ternary complex of BMP9 with the extracellular domains of ALK1 and ActRIIB.
22718755	8	52	part_of	ActRIIB	1157:1163	arg1	the extracellular domains	ActRIIB		the extracellular domains		PUBTATOR	Site	ActRIIB	93	domains	We also report the crystal structure of a fully assembled ternary complex of BMP9 with the extracellular domains of ALK1 and ActRIIB.
7505568	6	12	gly	glycosylated	566:577	arg1	all MAG glycosylated sequons			all MAG glycosylated sequons							Furthermore, preliminary data indicate that all MAG glycosylated sequons might bear the L2/HNK-1 epitope.
7505568	6	1	gly	bear	593:596	arg1	all MAG glycosylated sequons AND the L2/HNK-1 epitope			all MAG glycosylated sequons	the L2/HNK-1 epitope						Furthermore, preliminary data indicate that all MAG glycosylated sequons might bear the L2/HNK-1 epitope.
16234806	2	5	gly	glycoprotein	258:269	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			We show that Cbln1 is a glycoprotein secreted from cerebellar granule cells that is essential for three processes in cerebellar Purkinje cells: the matching and maintenance of pre- and postsynaptic elements at parallel fiber-Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses.
16234806	2	5	gly	glycoprotein	258:269	arg1	Cbln1	Cbln1				PUBTATOR		Cbln1	12404		We show that Cbln1 is a glycoprotein secreted from cerebellar granule cells that is essential for three processes in cerebellar Purkinje cells: the matching and maintenance of pre- and postsynaptic elements at parallel fiber-Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses.
21569239	3	9	part_of	found	518:522	arg2	amphiF-spondin AND The FS domain	amphiF-spondin		The FS domain		Fterm	Site	amphiF-spondin	10418	domain	The FS domain is found in F-spondins, mindins, M-spondin and amphiF-spondin.
21569239	3	9	part_of	found	518:522	arg2	M-spondin AND The FS domain	M-spondin		The FS domain		PUBTATOR	Site	M-spondin	10417	domain	The FS domain is found in F-spondins, mindins, M-spondin and amphiF-spondin.
28252640	3	68	part_of	BoNT/A1	606:612	arg1	Arg 1294	BoNT		residues, Arg 1156 and Arg 1294		Cterm	SpecificSite	BoNT		residues, Arg 1156 and Arg 1294	Notably, two BoNT/A1 residues, Arg 1156 and Arg 1294, that are crucial for the interaction with SV2, are not conserved among subtypes.
28252640	3	68	part_of	BoNT/A1	606:612	arg1	two BoNT/A1 residues	BoNT		residues, Arg 1156 and Arg 1294		Cterm	SpecificSite	BoNT		residues, Arg 1156 and Arg 1294	Notably, two BoNT/A1 residues, Arg 1156 and Arg 1294, that are crucial for the interaction with SV2, are not conserved among subtypes.
28252640	3	68	part_of	BoNT/A1	606:612	arg1	two BoNT/A1 residues	BoNT		residues, Arg 1156 and Arg 1294		Cterm	SpecificSite	BoNT		residues, Arg 1156 and Arg 1294	Notably, two BoNT/A1 residues, Arg 1156 and Arg 1294, that are crucial for the interaction with SV2, are not conserved among subtypes.
21932778	5	75	gly	glycosylation	732:744	arg1	glypican-1	glypican-1				PUBTATOR		glypican-1	2817		Experiments using the drug tunicamycin to inhibit the N-linked glycosylation of glypican-1 showed that secretion of anchorless glypican-1 was reduced and that the protein did not accumulate inside the cells.
23592772	8	48	gly	subunit	1200:1206	arg1	O-GlcNAcylated	NF-κB p65 subunit			O-GlcNAcylated	PUBTATOR		NF-κB p65 subunit	5970		The NF-κB p65 subunit and upstream kinases IKKα/IKKβ were O-GlcNAcylated in PDAC.
23661698	8	6	part_of	EphA2	1196:1200	arg1	two residues	EphA2		two residues		PUBTATOR	Site	EphA2	1969	residues	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
23661698	8	6	part_of	EphA2	1196:1200	arg1	Asp-78	EphA2		Asp-78 and Lys-136		PUBTATOR	SpecificSite	EphA2	1969	Asp-78 and Lys-136	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
8068684	1	88	gly	glycosylation	241:253	arg1	asparagines 75, 370, and 410			asparagines 75, 370, and 410						asparagines 75, 370, and 410	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8670172	9	96	part_of	Asn-18	1358:1363	arg1	CD59u	CD59u		Asn-18		PUBTATOR	SpecificSite	CD59u	966	Asn-18	The N-linked carbohydrate side chain of CD59u (at Asn-18) also displayed considerable heterogeneity.
29666272	1	27	gly	Asn-linked	127:136	arg1	Asn-linked oligosaccharides			Asn	Asn-linked oligosaccharides					Asn	Asn-linked oligosaccharides are extensively modified during transit through the secretory pathway, first by trimming of the nascent glycan chains and subsequently by initiating and extending multiple oligosaccharide branches from the trimannosyl glycan core.
2511201	11	34	gly	Xyl-Glc-Ser	1856:1866	arg1	a Xyl-Glc-Ser structure			Ser	a Xyl-Glc-Ser structure					Ser	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	48	gly	Xyl2-Glc-Ser	1837:1848	arg1	a Xyl-Glc-Ser structure			Ser	a Xyl-Glc-Ser structure					Ser	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	58	gly	structure	1868:1876	arg1	human factors VII	VII			structure	Cterm		VII			In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	58	gly	structure	1868:1876	arg1	the first epidermal growth factor-like domains			the first epidermal growth factor-like domains	the first epidermal growth factor-like domains		Site			domains	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	58	gly	structure	1868:1876	arg1	protein Z	protein Z			structure	Cterm		protein Z			In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2813359	5	17	gly	contains	850:857	arg1	EPO-bi AND the biantennary complex type	EPO-bi			the biantennary complex type	PUBTATOR		EPO	2056		However, structural analyses of their N-linked sugar chains revealed that EPO-bi contains the biantennary complex type as the major sugar chain, while EPO-tetra and the standard EPO contain the tetraantennary complex type as the major sugar chain.
2813359	5	17	gly	contains	850:857	arg1	EPO-bi AND the major sugar chain	EPO-bi			the major sugar chain	PUBTATOR		EPO	2056		However, structural analyses of their N-linked sugar chains revealed that EPO-bi contains the biantennary complex type as the major sugar chain, while EPO-tetra and the standard EPO contain the tetraantennary complex type as the major sugar chain.
2813359	5	45	gly	contain	951:957	arg1	the standard EPO AND the major sugar chain	EPO			the major sugar chain	PUBTATOR		EPO	2056		However, structural analyses of their N-linked sugar chains revealed that EPO-bi contains the biantennary complex type as the major sugar chain, while EPO-tetra and the standard EPO contain the tetraantennary complex type as the major sugar chain.
2813359	5	45	gly	contain	951:957	arg1	the standard EPO AND the tetraantennary complex type	EPO			the tetraantennary complex type	PUBTATOR		EPO	2056		However, structural analyses of their N-linked sugar chains revealed that EPO-bi contains the biantennary complex type as the major sugar chain, while EPO-tetra and the standard EPO contain the tetraantennary complex type as the major sugar chain.
11983428	3	12	gly	glycosylation	634:646	arg2	the sites			the sites						sites	We have defined the transmembrane topology of STIM1 by determining the sites of N-linked glycosylation.
24766575	0	28	gly	glycopeptide	23:34	arg2	Efficient and accurate glycopeptide identification			Efficient and accurate glycopeptide identification						glycopeptide	Efficient and accurate glycopeptide identification pipeline for high-throughput site-specific N-glycosylation analysis.
18214858	1	30	gly	fucosylated	213:223	arg1	fucosylated haptoglobin	fucosylated haptoglobin				PUBTATOR		haptoglobin	3240		It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
8486673	7	51	part_of	precursor	1025:1033	arg1	a cleavable signal sequence	precursor		a cleavable signal sequence		Fterm	Site	precursor		sequence	The results revealed that each monomer of rat CRP was synthesized individually as a single-chain precursor with a cleavable signal sequence.
8702840	7	25	gly	sites	1071:1075	arg1	Thr19			Thr19	Thr19		AminoAcid			Thr19 and Ser34	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	25	gly	sites	1071:1075	arg1	Ser34			Ser34	Ser34		AminoAcid			Thr19 and Ser34	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	25	gly	sites	1071:1075	arg1	Ser48			Ser48	Ser48		AminoAcid			Ser34 and Ser48	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
15628971	1	82	part_of	position	183:190	arg1	chondroitin	chondroitin		position		Fterm	Site	chondroitin		position 4	C4ST-1 (chondroitin 4-sulphotransferase-1) transfers sulphate to position 4 of N-acetylgalactosamine in chondroitin.
11258925	2	19	gly	glycoprotein	176:187	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
17322565	7	34	gly	Glycosylation	1167:1179	arg2	this site			this site						site	Glycosylation at this site suppressed the LPL hydrolysis of synthetic substrates, LDL, HDL2, and HDL3 but had little effect on HL activity.
10677208	3	76	gly	N-glycosylation	652:666	arg2	an N-glycosylation site			an N-glycosylation site						site	CR3 contains an N-glycosylation site, which is conserved in all forms of LTBP known to date.
27349982	2	3	part_of	ASM	369:371	arg1	the ASM polypeptide	ASM		the ASM polypeptide		PUBTATOR	Site	ASM	6609	polypeptide	While other lysosomal sphingolipid hydrolases require a saposin activator protein for full activity, the ASM polypeptide incorporates a built-in N-terminal saposin domain and does not require an external activator protein.
18214858	3	37	gly	haptoglobin	600:610	arg1	site-specific N-glycan structures	haptoglobin			site-specific N-glycan structures	PUBTATOR		haptoglobin	3240		In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
11439087	6	4	gly	N-glycosylation	927:941	arg2	four putative N-glycosylation sites			four putative N-glycosylation sites						sites	BST-1 contains four putative N-glycosylation sites.
1904059	9	114	gly	observed	1249:1256	arg1	plasma factor VII AND the three glycan structures	plasma factor VII			the three glycan structures	OGER		factor VII	P08709		Approximately equal amounts of the three glycan structures were observed in plasma factor VII, whereas in recombinant factor VII the glucose and the glucose-(xylose)2 structures predominated.
11533490	2	14	part_of	receptor	417:424	arg1	the extracellular domain	NP receptor		the extracellular domain		PUBTATOR	Site	NP receptor	4883	domain	We report the hormone-binding thermodynamics and crystal structures at 2.9 and 2.0 angstroms, respectively, of the extracellular domain of the unliganded human NP receptor (NPR-C) and its complex with CNP, a 22-amino acid NP.
12435857	9	15	gly	glycosylation	1876:1888	arg1	misfolded THTR-1 protein	misfolded THTR-1 protein				PUBTATOR		THTR-1 protein	10560		CONCLUSIONS: Taken collectively, these results suggest that the G172D mutation presumably misfolded THTR-1 protein that fails to undergo a complete glycosylation, is retained in the Golgi-ER compartment and thereby cannot be targeted to the plasma membrane.
17157876	2	85	part_of	CPN1	563:566	arg1	a 48 to 55 kDa catalytic (CPN1) domain	CPN1		a 48 to 55 kDa catalytic (CPN1) domain		PUBTATOR	Site	CPN1	1369	domain	Normally, CPN circulates in blood plasma as a hetero-tetramer consisting of two 83 kDa (CPN2) domains each flanked by a 48 to 55 kDa catalytic (CPN1) domain.
8172892	6	50	gly	alpha-D4	993:1000	arg1	Component sugar and sialic acid analyses	AP alpha			Component sugar and sialic acid analyses	PUBTATOR		AP alpha	2028		Component sugar and sialic acid analyses of AP alpha-D4 and AP alpha-D5 revealed that they contained 1 mol each of N-acetyl-D-galactosamine (GalNAc), D-galactose (Gal), and sialic acid.
8172892	6	95	gly	alpha-D5	1009:1016	arg1	Component sugar and sialic acid analyses	AP alpha			Component sugar and sialic acid analyses	PUBTATOR		AP alpha	2028		Component sugar and sialic acid analyses of AP alpha-D4 and AP alpha-D5 revealed that they contained 1 mol each of N-acetyl-D-galactosamine (GalNAc), D-galactose (Gal), and sialic acid.
8243461	8	17	gly	residues	1695:1702	arg1	factor X	factor X			residues	OGER		factor X	P00742		It appears that carbohydrate residues in factor X play an important role in the activation of the zymogen.
8617200	6	3	part_of	LTBP-1	1028:1033	arg1	The N-terminal region	LTBP-1		The N-terminal region		PUBTATOR	Site	LTBP-1	4052	region	The N-terminal region of LTBP-1 consisting of the first 400 amino acids was found to associate covalently with the ECM.
20427285	10	21	part_of	has	1371:1373	arg1	ZPI AND P1 tyrosine	ZPI		P1 tyrosine		PUBTATOR	AminoAcid	ZPI	51156	tyrosine	To understand why ZPI has P1 tyrosine, we examined a P1 Arg variant.
7538124	1	34	part_of	Keratin	87:93	arg1	Keratin polypeptides 8 and 18 (K8/18)	Keratin		Keratin polypeptides 8 and 18 (K8/18)		Cterm	Site	Keratin		polypeptides	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
29932112	6	25	gly	N-glycosylation	862:876	arg2	the only N-glycosylation site	Panx2		site		PUBTATOR		Panx2	56666	site	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	6	25	gly	N-glycosylation	862:876	arg2	N86	Panx2		N86		PUBTATOR		Panx2	56666	N86	Our results showed that N86 is the only N-glycosylation site of Panx2.
479158	16	60	gly	glycosylated	1386:1397	arg1	the glycosylated threonine			the glycosylated threonine						threonine	The amino acid sequence around the glycosylated threonine was found to be NH2-Ala.
28334865	1	87	gly	proteins	320:327	arg1	epidermal growth factor-like repeats	proteins			epidermal growth factor-like repeats	Fterm		proteins			Protein O-fucosyltransferase-1 (POFUT1), which transfers fucose residues to acceptor sites on serine and threonine residues of epidermal growth factor-like repeats of recipient proteins, is essential for Notch signal transduction in mammals.
22588082	1	12	gly	found	155:159	arg1	serine/threonine residues AND Protein O-fucosylation			serine/threonine residues	Protein O-fucosylation					residues	Protein O-fucosylation is a post-translational modification found on serine/threonine residues of thrombospondin type 1 repeats (TSR).
10441114	0	47	part_of	endostatin	41:50	arg1	circulating endostatin-related fragments	endostatin		circulating endostatin-related fragments		PUBTATOR	Site	endostatin	80781	fragments	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	0	74	part_of	endostatin-related	68:85	arg1	circulating endostatin-related fragments	endostatin		circulating endostatin-related fragments		PUBTATOR	Site	endostatin	80781	fragments	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
8631363	9	64	gly	glycosylated	1387:1398	arg1	the glycosylated peptides			the glycosylated peptides						peptides	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	9	62	gly	0-glycosylation	1551:1565	arg2	the 0-glycosylation site	tumor necrosis factor-alpha		site		PUBTATOR		tumor necrosis factor-alpha	7124	site	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	9	62	gly	0-glycosylation	1551:1565	arg2	Ser 4	tumor necrosis factor-alpha		Ser 4		PUBTATOR		tumor necrosis factor-alpha	7124	Ser 4	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
1737041	4	33	gly	factor	881:886	arg1	native or carbohydrate-deficient forms	factor			native or carbohydrate-deficient forms	Fterm		factor			Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
26563299	6	2	part_of	IL-15	881:885	arg1	IL-15 Asn79	IL-15		IL-15 Asn79		PUBTATOR	AminoAcid	IL-15	3600	Asn79	IL-15 Asn79 and sIL-15Rα Asn107 carried the same repertoire of biosynthetically-related N-glycans covering mostly α1-6-core-fucosylated and β-GlcNAc-terminating complex-type structures.
26563299	6	93	part_of	sIL-15Rα	897:904	arg1	sIL-15Rα Asn107	sIL		sIL-15Rα Asn107		OGER	AminoAcid	sIL	Q15468	Asn107	IL-15 Asn79 and sIL-15Rα Asn107 carried the same repertoire of biosynthetically-related N-glycans covering mostly α1-6-core-fucosylated and β-GlcNAc-terminating complex-type structures.
2573604	0	66	gly	glycosylation	9:21	arg1	rat renal gamma-glutamyltranspeptidase	rat renal gamma-glutamyltranspeptidase				PUBTATOR		gamma-glutamyltranspeptidase	116568		O-linked glycosylation of rat renal gamma-glutamyltranspeptidase adjacent to its membrane anchor domain.
15173186	6	83	gly	glycosylation	906:918	arg2	N-linked glycosylation consensus sites			N-linked glycosylation consensus sites						sites	Additionally, all Toll-like receptors contain N-linked glycosylation consensus sites, and Toll-like receptor 4 requires glycosylation for function.
1908233	5	5	part_of	Thr-O-glycosylation	865:883	arg1	O-glycosylated proteins	proteins		Thr-O-glycosylation		Fterm	AminoAcid	proteins		Thr	This motif predicts the site(s) of Pro- associated Thr-O-glycosylation in O-glycosylated proteins, although it is clear that there are also other forms of Thr-O-glycosylation not associated with Pro.
19951703	3	40	gly	N-glycosylation	318:332	arg1	human UGT1A9	human UGT1A9				PUBTATOR		UGT1A9	54600		In the present study, we investigated the role of N-glycosylation in the function of human UGT1A9.
26598643	1	69	gly	glycoproteins	166:178	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Site-specific glycosylation analysis is key to investigate structure-function relationships of glycoproteins, e.g. in the context of antigenicity and disease progression.
9689040	1	12	part_of	fibrinogen-420	142:155	arg1	a recombinant alphaEC domain	fibrinogen		a recombinant alphaEC domain		PUBTATOR	Site	fibrinogen	2244	domain	The crystal structure of a recombinant alphaEC domain from human fibrinogen-420 has been determined at a resolution of 2.1 A.
8069634	13	102	gly	lectin	2235:2240	arg1	the carbohydrate recognition domain	lectin			the carbohydrate recognition domain	Fterm		lectin			Our structure shows a large complementary surface area between the oligosaccharide and the lectin, in contrast with the recently determined structure of a complex between the carbohydrate recognition domain of a C-type mammalian lectin and an oligomannoside, where only the non-reducing terminal mannose residue interacts with the lectin.
25759508	7	7	gly	O-glycosylation	1035:1049	arg2	potential O-glycosylation sites			potential O-glycosylation sites						sites	The O-glycosylation site was further confirmed by the recombinant production of mutant IgG3 in which potential O-glycosylation sites had been knocked out.
25759508	7	34	gly	O-glycosylation	928:942	arg2	The O-glycosylation site			The O-glycosylation site						site	The O-glycosylation site was further confirmed by the recombinant production of mutant IgG3 in which potential O-glycosylation sites had been knocked out.
17643119	5	0	part_of	residues	858:865	arg1	the nonchannel homolog acetylcholine-binding proteins	proteins		residues		Fterm	AminoAcid	proteins		residues in	The two hydrophilic core residues are highly conserved in nAChRs, but correspond to hydrophobic residues in the nonchannel homolog acetylcholine-binding proteins.
3661998	2	41	gly	glycopeptides	326:338	arg2	glycopeptides			glycopeptides	carbohydrate chains					glycopeptides	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
24721674	9	9	gly	glycopeptide	1867:1878	arg2	intact glycopeptide enrichment			intact glycopeptide enrichment						glycopeptide	It is comprised of an integrated hydrophilic interaction chromatography solid phase extraction for the simultaneous detergent removal and intact glycopeptide enrichment.
28279966	0	14	part_of	K1491-R1492	41:51	arg1	Von Willebrand Factor	Plasmin Cleaves Von Willebrand Factor		K1491-R1492		PUBTATOR	SiteSequence	Plasmin Cleaves Von Willebrand Factor	5340	K1491-R1492	Plasmin Cleaves Von Willebrand Factor at K1491-R1492 in the A1-A2 Linker Region in a Shear- and Glycan-Dependent Manner In Vitro.
28279966	0	23	part_of	Factor	31:36	arg1	the A1-A2 Linker Region	Plasmin Cleaves Von Willebrand Factor		the A1-A2 Linker Region		PUBTATOR		Plasmin Cleaves Von Willebrand Factor	5340		Plasmin Cleaves Von Willebrand Factor at K1491-R1492 in the A1-A2 Linker Region in a Shear- and Glycan-Dependent Manner In Vitro.
25187573	4	49	part_of	lubricin	879:886	arg1	the STP-rich domain	lubricin		the STP-rich domain		PUBTATOR	Site	lubricin	10216	domain	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	4	106	part_of	STP-rich	845:852	arg1	the STP-rich domain	STP		the STP-rich domain		OGER	Site	STP	P50225	domain	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
26271046	4	8	gly	GluA2	817:821	arg1	N-glycans	GluA2			N-glycans	PUBTATOR		GluA2	2891		However, evidence that the HNK-1 epitope on N-glycans of GluA2 directly affects these phenomena is lacking.
26271046	4	16	gly	epitope	793:799	arg1	N-glycans				N-glycans						However, evidence that the HNK-1 epitope on N-glycans of GluA2 directly affects these phenomena is lacking.
12925531	2	31	part_of	COX	300:302	arg1	the COX active site	COX		the COX active site		OGER	Site	COX		site	Several modes of inhibitor binding in the COX active site have been described including ion pairing of carboxylic acid containing inhibitors with Arg-120 of COX-1 and COX-2 and insertion of arylsulfonamides and sulfones into the COX-2 side pocket.
10814696	1	66	gly	A	393:393	arg1	the carbohydrate component	arylsulfatase A			the carbohydrate component	PUBTATOR		arylsulfatase A	410		It has been shown that the concentration of arylsulfatase A increases in the body fluids of patients with some forms of cancer, and the carbohydrate component of arylsulfatase A synthesized in tumor tissues and transformed cells undergoes increased sialylation, phosphorylation and sulfation.
9748270	5	76	gly	N-glycosylated	625:638	arg1	the N-glycosylated extracellular domain			the N-glycosylated extracellular domain						domain	The globular intracellular domain was disulfide-linked, and the N-glycosylated extracellular domain of three 120-kDa polypeptides was triple-helical at physiological temperatures.
9748270	5	76	gly	N-glycosylated	625:638	arg1	three 120-kDa polypeptides			three 120-kDa polypeptides						polypeptides	The globular intracellular domain was disulfide-linked, and the N-glycosylated extracellular domain of three 120-kDa polypeptides was triple-helical at physiological temperatures.
30899004	4	5	gly	N-glycosites	780:791	arg2	1,545 N-glycosites			1,545 N-glycosites						N-glycosites	Here we show that N-glycoproteome site-specific microheterogeneity can be captured via large-scale glycopeptide profiling methods enabled by activated ion electron transfer dissociation (AI-ETD), ultimately characterizing 1,545 N-glycosites (>5,600 unique N-glycopeptides) from mouse brain tissue.
30899004	4	5	gly	N-glycosites	780:791	arg2	>5,600 unique N-glycopeptides			>5,600 unique N-glycopeptides						N-glycopeptides	Here we show that N-glycoproteome site-specific microheterogeneity can be captured via large-scale glycopeptide profiling methods enabled by activated ion electron transfer dissociation (AI-ETD), ultimately characterizing 1,545 N-glycosites (>5,600 unique N-glycopeptides) from mouse brain tissue.
30899004	4	40	gly	glycopeptide	651:662	arg2	large-scale glycopeptide profiling methods			large-scale glycopeptide profiling methods						glycopeptide	Here we show that N-glycoproteome site-specific microheterogeneity can be captured via large-scale glycopeptide profiling methods enabled by activated ion electron transfer dissociation (AI-ETD), ultimately characterizing 1,545 N-glycosites (>5,600 unique N-glycopeptides) from mouse brain tissue.
30899004	4	45	gly	N-glycopeptides	808:822	arg2	1,545 N-glycosites			1,545 N-glycosites						N-glycosites	Here we show that N-glycoproteome site-specific microheterogeneity can be captured via large-scale glycopeptide profiling methods enabled by activated ion electron transfer dissociation (AI-ETD), ultimately characterizing 1,545 N-glycosites (>5,600 unique N-glycopeptides) from mouse brain tissue.
30899004	4	45	gly	N-glycopeptides	808:822	arg2	>5,600 unique N-glycopeptides			>5,600 unique N-glycopeptides						N-glycopeptides	Here we show that N-glycoproteome site-specific microheterogeneity can be captured via large-scale glycopeptide profiling methods enabled by activated ion electron transfer dissociation (AI-ETD), ultimately characterizing 1,545 N-glycosites (>5,600 unique N-glycopeptides) from mouse brain tissue.
7505568	4	29	gly	glycosylated	398:409	arg2	Asn106			Asn106						Asn106	Of the 9 MAG sequons 7 were glycosylated and 1 was partially glycosylated at Asn106.
10419520	7	61	part_of	S2P	1074:1076	arg1	S2P face the cytosol	S2P		S2P face the cytosol		PUBTATOR	Site	S2P	51360	face	Both the NH(2) and COOH termini of S2P face the cytosol.
11788899	4	4	gly	glycosylation	616:628	arg2	two N-linked glycosylation sites			two N-linked glycosylation sites						sites	WNT8B gene of about 23-kb in size consisted of six exons, and encoded a 351-amino-acid polypeptide with the N-terminal signal peptide and two N-linked glycosylation sites.
20856818	7	100	part_of	glycoprotein	1091:1102	arg1	a C-terminal globular domain	glycoprotein		a C-terminal globular domain		Fterm	Site	glycoprotein		domain	Otolin is a secreted glycoprotein of ∼70 kDa, with a C-terminal globular domain that is homologous to the immune complement C1q, and contains extensive posttranslational modifications including hydroxylated prolines and glycosylated lysines.
20856818	7	53	part_of	contains	1203:1210	arg1	a C-terminal globular domain AND glycosylated lysines	a C-terminal globular domain		glycosylated lysines						lysines	Otolin is a secreted glycoprotein of ∼70 kDa, with a C-terminal globular domain that is homologous to the immune complement C1q, and contains extensive posttranslational modifications including hydroxylated prolines and glycosylated lysines.
20856818	7	53	part_of	contains	1203:1210	arg1	a C-terminal globular domain AND hydroxylated prolines	a C-terminal globular domain		hydroxylated prolines						prolines	Otolin is a secreted glycoprotein of ∼70 kDa, with a C-terminal globular domain that is homologous to the immune complement C1q, and contains extensive posttranslational modifications including hydroxylated prolines and glycosylated lysines.
3191509	6	44	gly	epitope	1070:1076	arg1	mucin-carried O-glycans			epitope	mucin-carried O-glycans					epitope	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
17105447	8	1	gly	N-glycosylation	1175:1189	arg2	six N-glycosylation sites			six N-glycosylation sites						sites	The presence of six N-glycosylation sites was validated by progressive peptide-N-glycosidase F deglycosylation.
3665919	0	42	gly	glycoproteins	67:79	arg1	bronchial mucus glycoproteins	bronchial mucus glycoproteins				Fterm		glycoproteins			Structure of sialyl-oligosaccharides isolated from bronchial mucus glycoproteins of patients (blood group O) suffering from cystic fibrosis.
23662732	6	3	gly	N-glycoproteins	1241:1255	arg1	N-glycoproteins	N-glycoproteins				Fterm		N-glycoproteins			The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	6	10	gly	O-glycoproteins	1289:1303	arg1	O-glycoproteins	O-glycoproteins				Fterm		O-glycoproteins			The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
29932112	1	1	gly	glycoproteins	147:159	arg1	channel-forming glycoproteins	channel-forming glycoproteins				Fterm		glycoproteins			Pannexins (Panx1, 2, 3) are channel-forming glycoproteins expressed in mammalian tissues.
29932112	1	1	gly	glycoproteins	147:159	arg1	Pannexins	Pannexins				PUBTATOR		Pannexins (Panx1	24145		Pannexins (Panx1, 2, 3) are channel-forming glycoproteins expressed in mammalian tissues.
3949763	4	25	gly	glycosylation	395:407	arg2	the sites			the sites						sites	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
26207632	4	14	part_of	Obif	714:717	arg1	the Obif extracellular domain	Obif		the Obif extracellular domain		OGER	Site	Obif	Q8R138	domain	RESULTS: First, we found that O-glycosylation of the Obif protein occurs at serine residue 36 in the Obif extracellular domain.
19690161	7	38	gly	glycosylation	1036:1048	arg2	the Asn-89 site	protein		Asn-89 site		Fterm		protein		Asn-89 site	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	7	38	gly	glycosylation	1036:1048	arg1	the Asn-89 site	protein		Asn-89 site		Fterm		protein		Asn-89 site	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	7	38	gly	glycosylation	1036:1048	arg2	the Asn-89 site	vIL		Asn-89 site		OGER		vIL	P09327	Asn-89 site	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	7	38	gly	glycosylation	1036:1048	arg1	the Asn-89 site	vIL		Asn-89 site		OGER		vIL	P09327	Asn-89 site	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	7	38	gly	glycosylation	1036:1048	arg1	the Asn-89 site			Asn-89 site						Asn-89 site	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
7044414	1	32	part_of	alpha-lactalbumin	105:121	arg1	The amino acid sequence	alpha-lactalbumin		The amino acid sequence		PUBTATOR	Site	alpha-lactalbumin	24528	sequence	The amino acid sequence of rat alpha-lactalbumin has been determined.
2493268	3	27	gly	bears	537:541	arg1	a threonine AND the single carbohydrate chain			a threonine	the single carbohydrate chain					threonine	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
8344278	2	44	part_of	precursor	421:429	arg1	separate domains	precursor		separate domains		Fterm	Site	precursor		domains	These saposins, together with saposin B, are small glycoproteins, derived from separate domains of a single precursor, prosaposin, and are required for the lysosomal hydrolysis of various sphingolipids.
9169007	9	58	gly	glycosylation	1604:1616	arg2	the mutated glycosylation site			the mutated glycosylation site						site	The extent of heparin-affinity enhancement was correlated with the distance of the mutated glycosylation site to the putative heparin-binding site in the X-ray structure of antithrombin.
1472036	2	9	part_of	receptor	375:382	arg1	the soluble extracellular domain	insulin receptor		the soluble extracellular domain		PUBTATOR	Site	insulin receptor	3643	domain	We have digested the soluble extracellular domain of the insulin receptor with succinylated trypsin, partially separated the resulting peptides, and sequenced a number of fractions.
20406422	2	76	gly	N-glycosylation	428:442	arg1	CLN7	CLN7		N371 and N376		PUBTATOR		CLN7	256471	N371 and N376	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	76	gly	N-glycosylation	428:442	arg2	N371			N371 and N376						N371 and N376	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	76	gly	N-glycosylation	428:442	arg1	CLN7	CLN7		sites		PUBTATOR		CLN7	256471	sites	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	76	gly	N-glycosylation	428:442	arg2	N371	CLN7		N371 and N376		PUBTATOR		CLN7	256471	N371 and N376	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
16274239	3	10	gly	glycosylated	509:520	arg2	N			N(579)						N(579)	To characterize the subpopulation of receptors not glycosylated at N(579), we established a 32D cell line expressing a point mutant of the EGFR (N579Q), which cannot be glycosylated at this position.
16274239	3	10	gly	glycosylated	509:520	arg1	receptors	receptors		N(579)		Fterm		receptors		N(579)	To characterize the subpopulation of receptors not glycosylated at N(579), we established a 32D cell line expressing a point mutant of the EGFR (N579Q), which cannot be glycosylated at this position.
16274239	3	10	gly	glycosylated	509:520	arg1	receptors	receptors		N(579)		Fterm		receptors		N(579)	To characterize the subpopulation of receptors not glycosylated at N(579), we established a 32D cell line expressing a point mutant of the EGFR (N579Q), which cannot be glycosylated at this position.
16274239	3	24	gly	glycosylated	627:638	arg2	this position	EGFR (N579Q)		position		PUBTATOR		EGFR (N579Q)	13649	position	To characterize the subpopulation of receptors not glycosylated at N(579), we established a 32D cell line expressing a point mutant of the EGFR (N579Q), which cannot be glycosylated at this position.
18795891	10	62	part_of	tetraspanin	1535:1545	arg1	tetraspanin microdomains	tetraspanin		tetraspanin microdomains		Fterm	Site	tetraspanin		microdomains	Finally, Tspan9 was shown to be a component of tetraspanin microdomains that included the collagen receptor GPVI (glycoprotein VI) and integrin alpha6beta1, but not the von Willebrand receptor GPIbalpha or the integrins alphaIIbbeta3 or alpha2beta1.
22826440	9	69	gly	proteins	1858:1865	arg1	O-GlcNAc-6-phosphate	proteins			O-GlcNAc-6-phosphate	Fterm		proteins			Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
11356966	10	18	part_of	has	1133:1135	arg1	PiT-2 AND 12 transmembrane domains	PiT-2		12 transmembrane domains		PUBTATOR	Site	PiT-2	6575	domains	A model in which PiT-2 has 12 transmembrane domains and extracellular N- and C-terminal extremities is proposed.
7512967	0	40	part_of	G2b	56:58	arg1	hinge region	immunoglobulin G2b		hinge region		Cterm	Site	immunoglobulin G2b		region	O-glycosylation in hinge region of mouse immunoglobulin G2b.
10531415	0	46	gly	glycosylation	9:21	arg1	D1	D1				Cterm		D1			N-linked glycosylation is required for plasma membrane localization of D5, but not D1, dopamine receptors in transfected mammalian cells.
10531415	0	46	gly	glycosylation	9:21	arg1	dopamine receptors	dopamine receptors				Fterm		receptors			N-linked glycosylation is required for plasma membrane localization of D5, but not D1, dopamine receptors in transfected mammalian cells.
23527852	1	10	gly	glycoprotein	175:186	arg1	Apolipoprotein-CIII	Apolipoprotein-CIII				PUBTATOR		Apolipoprotein-CIII	345		Apolipoprotein-CIII (apoCIII) is an abundant blood glycoprotein associated with lipoprotein particles.
23527852	1	10	gly	glycoprotein	175:186	arg1	an abundant blood glycoprotein	an abundant blood glycoprotein				Fterm		glycoprotein			Apolipoprotein-CIII (apoCIII) is an abundant blood glycoprotein associated with lipoprotein particles.
1904059	13	97	gly	serine	1830:1835	arg1	the carbohydrate moiety			serine 52	the carbohydrate moiety					serine 52	In order to assess whether the carbohydrate moiety at serine 52 contributes to the biological activity of factor VII, we have constructed a site-specific mutant of recombinant factor VII in which serine 52 has been replaced with an alanine residue.
12659834	5	59	gly	Asn15	1093:1097	arg1	the two particular N-linked glycans			Asn15 and Asn123	the two particular N-linked glycans					Asn15 and Asn123	It has been demonstrated that the two particular N-linked glycans at Asn15 and Asn123 interfered with the B-cell response to the HBV-derived pre-S1S2, resulting in low titers of pre-S1S2-neutralizing antibodies.
12659834	5	70	gly	Asn123	1103:1108	arg1	the two particular N-linked glycans			Asn15 and Asn123	the two particular N-linked glycans					Asn15 and Asn123	It has been demonstrated that the two particular N-linked glycans at Asn15 and Asn123 interfered with the B-cell response to the HBV-derived pre-S1S2, resulting in low titers of pre-S1S2-neutralizing antibodies.
15616124	2	83	gly	N-glycosylation	312:326	arg1	FVII	FVII				Cterm		FVII	2155		In the present study, however, we demonstrate posttranslational N-glycosylation of recombinant human coagulation factor VII (FVII) in CHO-K1 and 293A cells.
15616124	2	83	gly	N-glycosylation	312:326	arg1	recombinant human coagulation factor VII	recombinant human coagulation factor VII				PUBTATOR		coagulation factor VII	2155		In the present study, however, we demonstrate posttranslational N-glycosylation of recombinant human coagulation factor VII (FVII) in CHO-K1 and 293A cells.
7654718	1	49	part_of	positions	103:111	arg1	C-tail	C-tail		positions		Cterm	Site	C-tail		positions	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
3264725	9	2	gly	VIIa	1858:1861	arg1	the overall carbohydrate compositions	factor VIIa			the overall carbohydrate compositions	Cterm		factor VIIa			Besides minor differences in the sialic acid and fucose contents, the overall carbohydrate compositions were nearly identical in recombinant factor VIIa and human plasma factor VIIa.
3264725	9	75	gly	VIIa	1829:1832	arg1	the overall carbohydrate compositions	factor VIIa			the overall carbohydrate compositions	Cterm		factor VIIa			Besides minor differences in the sialic acid and fucose contents, the overall carbohydrate compositions were nearly identical in recombinant factor VIIa and human plasma factor VIIa.
1577715	5	99	gly	glycoprotein	767:778	arg1	The glycoprotein	The glycoprotein				Fterm		glycoprotein			The glycoprotein was shown to be unique in its great diversity of oligosaccharide structures.
16040958	1	9	gly	glycosylated	414:425	arg1	its amino-terminal heavily glycosylated nonserpin region			its amino-terminal heavily glycosylated nonserpin region						region	The C1 inhibitor (C1INH), a plasma complement regulatory protein, prevents endotoxin shock, at least partially via the direct interaction of its amino-terminal heavily glycosylated nonserpin region with gram-negative bacterial lipopolysaccharide (LPS).
8142896	2	1	gly	carried	348:354	arg1	The protein AND N-linked carbohydrate	The protein			N-linked carbohydrate	Fterm		protein			The protein carried N-linked carbohydrate and showed a heterogeneity on denaturing polyacrylamide gels.
10704524	6	37	gly	sialylated	1086:1095	arg1	the complex oligosaccharides				the complex oligosaccharides						Approximately 80% of the complex oligo-saccharides had a core-region fucose and 50% of the complex oligosaccharides were sialylated exclusively with alpha-2,3-linked sialic acid residues.
20505120	4	34	part_of	EphA2	476:480	arg1	the complete EphA2 ectodomain	EphA2		the complete EphA2 ectodomain		PUBTATOR	Site	EphA2	1969	ectodomain	Here we present high-resolution structures of the complete EphA2 ectodomain and complexes with ephrin-A1 and A5 as the base unit of an Eph cluster.
2513186	9	79	gly	attached	1541:1548	arg1	Asn448 AND Oligosaccharides			Asn448	Oligosaccharides					Asn448	Oligosaccharides attached to Asn448 are almost completely substituted by (alpha 2-3)- or (alpha 2-6)-linked sialic acid residues and carry the majority of sulfate groups present.
10842180	0	40	gly	N-glycosylated	13:26	arg1	Doppel	Doppel				PUBTATOR		Doppel	26434		Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein.
10842180	0	40	gly	N-glycosylated	13:26	arg1	an N-glycosylated, glycosylphosphatidylinositol-anchored protein	an N-glycosylated, glycosylphosphatidylinositol-anchored protein				Fterm		protein			Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein.
10712595	8	41	gly	glycosylation	1464:1476	arg2	a glycosylation site			a glycosylation site						site	Thus a rapidly reacting pool of antithrombin may have evolved in two different ways: absence of a glycosylation site in lower vertebrates vs. incomplete glycosylation of a part of the circulating antithrombin in higher vertebrates.
16537470	3	69	part_of	tail	670:673	arg1	a shorter fatty acyl chain	chain		tail		OGER	Site	chain	12479	tail	For GalA-GSL, a shorter fatty acyl chain, an absence of the 4-OH on the sphingosine tail and a 6'-COOH group on the galactose moiety account for its observed antigenic potency.
16537470	3	86	part_of	chain	621:625	arg1	the sphingosine tail	chain		the sphingosine tail		OGER	Site	chain	12479	tail	For GalA-GSL, a shorter fatty acyl chain, an absence of the 4-OH on the sphingosine tail and a 6'-COOH group on the galactose moiety account for its observed antigenic potency.
21525977	3	21	part_of	NPC1L1	440:445	arg1	the N-terminal domain	NPC1L1		the N-terminal domain		PUBTATOR	Site	NPC1L1	29881	domain	PRINCIPAL FINDINGS: Here we present the 2.8 Å crystal structure of the N-terminal domain (NTD) of NPC1L1 in the absence of cholesterol.
23829323	3	4	gly	N-glycopeptide	684:697	arg2	direct N-glycopeptide analysis			direct N-glycopeptide analysis						N-glycopeptide	However, successful implementation of direct N-glycopeptide analysis by tandem mass spectrometry remains a challenge.
19880749	3	45	part_of	ADAMTS13	455:462	arg1	an exosite-containing human ADAMTS13 fragment	ADAMTS13		an exosite-containing human ADAMTS13 fragment		PUBTATOR	Site	ADAMTS13	11093	fragment	Here, we determined 2 crystal structures of ADAMTS13-DTCS (residues 287-685), an exosite-containing human ADAMTS13 fragment, at 2.6-A and 2.8-A resolution.
19413349	7	36	gly	deglycosylation	1213:1227	arg1	wild-type or mutant melanopsin	wild-type or mutant melanopsin				PUBTATOR		melanopsin	192223		Further in vitro O-linked deglycosylation of wild-type or mutant melanopsin with O-glycosidase and neuraminidase converted the 55 kDa band to a 49 kDa band.
22902367	4	11	gly	glycosylated	676:687	arg1	natively glycosylated full ectodomains	Necl-5		ectodomains		OGER		Necl-5	P15151	ectodomains	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	11	gly	glycosylated	676:687	arg1	natively glycosylated full ectodomains	nectins 		ectodomains		PUBTATOR		nectins 	5818	ectodomains	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
16263699	4	9	gly	N-glycosylation	630:644	arg2	N-glycosylation sites	proteins		sites		Fterm		proteins		sites	Here we report the analysis of N-glycosylation sites of human platelet proteins.
25374123	6	49	gly	N-glycopeptides	905:919	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	The sequences of N-glycopeptides were identified from the mass spectra by high-energy C-trap dissociation (HCD) and collision-induced dissociation (CID).
16335952	6	62	gly	N-glycoproteins	1311:1325	arg1	303 nonredundant N-glycoproteins	303 nonredundant N-glycoproteins				Fterm		N-glycoproteins			Using stringent criteria, a total of 2053 different N-glycopeptides were confidently identified, covering 303 nonredundant N-glycoproteins.
16335952	6	71	gly	N-glycopeptides	1240:1254	arg2	2053 different N-glycopeptides			2053 different N-glycopeptides						N-glycopeptides	Using stringent criteria, a total of 2053 different N-glycopeptides were confidently identified, covering 303 nonredundant N-glycoproteins.
16622833	4	58	part_of	A1PI	623:626	arg1	The single cysteine residue	A1PI		The single cysteine residue		PUBTATOR	AminoAcid	A1PI	5265	cysteine residue	The single cysteine residue of A1PI formed a disulfide bridge with free cysteine.
25327667	0	54	gly	glycosylation	33:45	arg1	prostate specific antigen	prostate specific antigen				PUBTATOR		prostate specific antigen	354		Glycoproteomics: identifying the glycosylation of prostate specific antigen at normal and high isoelectric points by LC-MS/MS.
1544894	7	69	gly	has	1145:1147	arg1	the first EGF domain AND O-linked fucose	factor VII		domain	O-linked fucose	OGER		factor VII	P08709	domain	It has been recently reported that the first EGF domain of human factor VII has O-linked fucose at the equivalent position (Ser-60) (Bjoern, S., Foster, D. C., Thim, L., Wiberg, F. C., Christensen, M., Komiyama, Y., Pedersen, A. H., and Kisiel, W. (1991) J. Biol.
24417605	5	56	gly	sialylated	667:676	arg1	the N-glycans				the N-glycans						Most of the N-glycans (∼90%) from HDL glycoproteins were sialylated with one or two neuraminic acids (Neu5Ac).
24417605	5	59	gly	glycoproteins	648:660	arg1	the N-glycans	HDL glycoproteins			the N-glycans	OGER		HDL glycoproteins	Q9UNE0		Most of the N-glycans (∼90%) from HDL glycoproteins were sialylated with one or two neuraminic acids (Neu5Ac).
6203908	4	24	part_of	contain	209:215	arg1	The identical subunits AND 1451 amino acid residues	The identical subunits		1451 amino acid residues		OGER	Site	subunits	2	residues	The identical subunits contain 1451 amino acid residues.
9450956	10	53	gly	C-glycosylation	1286:1300	arg1	recombinant human interleukin 12	recombinant human interleukin 12				OGER		interleukin 12			Two of these proteins were analyzed protein chemically, which showed partial C-glycosylation of recombinant human interleukin 12.
30459171	0	8	gly	glycopeptides	71:83	arg2	O-linked glycopeptides			O-linked glycopeptides						glycopeptides	Mapping the O-glycoproteome using site-specific extraction of O-linked glycopeptides (EXoO).
7744025	3	43	gly	glycosylated	649:660	arg1	The glycosylated peptides			The glycosylated peptides						peptides	The glycosylated peptides were isolated by ultrafiltration, purified by reverse-phase HPLC and further analysed by liquid secondary ion mass spectrometry (LSIMS).
28973932	1	10	part_of	cdh	263:265	arg1	their extracellular cdh (EC) domains	cdh		their extracellular cdh (EC) domains		OGER	Site	cdh	Q8NE62	domains	The cadherin (cdh) superfamily of adhesion molecules carry O-linked mannose (O-Man) glycans at highly conserved sites localized to specific β-strands of their extracellular cdh (EC) domains.
28973932	1	28	part_of	EC	268:269	arg1	their extracellular cdh (EC) domains	EC		their extracellular cdh (EC) domains		Cterm	Site	EC	Q8NE62	domains	The cadherin (cdh) superfamily of adhesion molecules carry O-linked mannose (O-Man) glycans at highly conserved sites localized to specific β-strands of their extracellular cdh (EC) domains.
1150658	3	21	part_of	subunit	245:251	arg1	The amino acid sequence	subunit		The amino acid sequence		Fterm	Site	subunit		sequence	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
22333914	5	2	part_of	overall	1073:1079	arg1	the overall GAIN domain	l GAIN		the overall GAIN domain		PUBTATOR	Site	l GAIN	23218	domain	Functionally, the GAIN domain is both necessary and sufficient for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyse peptide bond hydrolysis.
22333914	5	10	part_of	GAIN	1081:1084	arg1	the overall GAIN domain	l GAIN		the overall GAIN domain		PUBTATOR	Site	l GAIN	23218	domain	Functionally, the GAIN domain is both necessary and sufficient for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyse peptide bond hydrolysis.
29581294	5	47	gly	occupied	741:748	arg2	the copper-binding site			the copper-binding site						site	Unexpectedly, the copper-binding site of hLOXL2 is occupied by zinc, which blocks LTQ generation and the enzymatic activity of hLOXL2 in our in vitro assay.
7654718	7	37	gly	glycosylation	1157:1169	arg2	glycosylation sites			glycosylation sites						sites	Edman degradation of C-tail fragment and its pronase subfragment suggest a number of glycosylation sites which are flanked by a consensus motif of PVPP.
1694115	6	41	gly	glycosylation	978:990	arg1	alpha-fetoprotein	alpha-fetoprotein				PUBTATOR		alpha-fetoprotein	174		However, because the presence of different glycoforms has been reported in alpha-fetoprotein preparations, both from human sources and from other species, it was important to establish the type and extent of glycosylation of alpha-fetoprotein prepared by our method.
17715132	3	18	gly	N-glycosylated	480:493	arg1	Pannexin1	Pannexin1				PUBTATOR		Pannexin1	24145		We show here that Pannexin1 forms a hexameric channel and reaches the cell surface but, unlike connexins, is N-glycosylated.
1456441	1	6	gly	N-glycosylation	211:225	arg2	N-glycosylation site			N-glycosylation site						site	This report describes the N-glycosylation site mapping of human serotransferrin (h-STF).
21300292	2	16	part_of	N-cadherin	368:377	arg1	E- and N-cadherin ectodomains	N-cadherin		E- and N-cadherin ectodomains		PUBTATOR	Site	N-cadherin	12558	ectodomains	We show that a molecular layer seen in crystal structures of E- and N-cadherin ectodomains reported here and in a previous C-cadherin structure corresponds to the extracellular architecture of adherens junctions.
25092234	8	58	gly	glycosylated	1114:1125	arg1	N335			N335						N335	It was evidenced that N335 was not glycosylated and that N72 and N108 were fully occupied, whereas N432 and N473 were occupied at about 92 and 95%, respectively.
25092234	8	7	gly	occupied	1160:1167	arg2	N72			N72 and N108						N72 and N108	It was evidenced that N335 was not glycosylated and that N72 and N108 were fully occupied, whereas N432 and N473 were occupied at about 92 and 95%, respectively.
25092234	8	65	gly	occupied	1197:1204	arg2	N432			N432 and N473						N432 and N473	It was evidenced that N335 was not glycosylated and that N72 and N108 were fully occupied, whereas N432 and N473 were occupied at about 92 and 95%, respectively.
24692546	3	6	gly	glycosylated	516:527	arg1	fully glycosylated FSH	fully glycosylated FSH				OGER		FSH			The model predicts that FSHR binds Asnα(52)-deglycosylated FSH at a 3-fold higher capacity than fully glycosylated FSH.
24692546	3	14	gly	-deglycosylated	457:471	arg1	Asnα(52)-deglycosylated FSH	Asnα(52)-deglycosylated FSH				OGER		FSH			The model predicts that FSHR binds Asnα(52)-deglycosylated FSH at a 3-fold higher capacity than fully glycosylated FSH.
16212939	5	4	gly	N-glycosylation	956:970	arg2	an additional N-glycosylation site			an additional N-glycosylation site						site	In contrast, the mutant containing an additional N-glycosylation site on the N-terminal 24 amino acids of hIL-1beta (Gln15Asn) secreted twice as much rhG-CSF into culture media as wild type hIL-1beta.
10878002	7	42	part_of	contains	852:859	arg1	Properdin AND 20 tryptophans	Properdin		20 tryptophans		PUBTATOR	AminoAcid	Properdin	5199	tryptophans	Properdin contains 20 tryptophans of which 17 are part of a WXXW motif.
14529283	6	75	part_of	NTPDase6	1412:1419	arg1	the amino acid sequence	NTPDase6		the amino acid sequence		PUBTATOR	Site	NTPDase6	955	sequence	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
16740002	4	11	gly	N-glycosylated	652:665	arg1	formerly N-glycosylated peptides			formerly N-glycosylated peptides						peptides	In this approach, glycoproteins were coupled onto a hydrazide resin, the proteins were then digested and formerly N-glycosylated peptides were selectively released with the enzyme PNGase F and analyzed by LC-MS/MS.
16740002	4	17	gly	glycoproteins	556:568	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			In this approach, glycoproteins were coupled onto a hydrazide resin, the proteins were then digested and formerly N-glycosylated peptides were selectively released with the enzyme PNGase F and analyzed by LC-MS/MS.
16040958	2	26	gly	glycosylation	650:662	arg2	the three N-linked glycosylation sites			the three N-linked glycosylation sites						sites	To further characterize the potential LPS-binding site(s) within the amino-terminal domain, mutations were introduced into C1INH at the three N-linked glycosylation sites and at the four positively charged amino acid residues.
18491227	2	36	gly	N-glycosylation	336:350	arg2	four potential N-glycosylation sites			four potential N-glycosylation sites						sites	In a previous study, we demonstrated that all of four potential N-glycosylation sites in E-cadherin are occupied by N-glycans in human breast carcinoma cells in vivo and the elimination of N-glycan at Asn-633 dramatically affected E-cadherin expression and made it degraded.
18491227	2	55	gly	occupied	376:383	arg2	four potential N-glycosylation sites			four potential N-glycosylation sites						sites	In a previous study, we demonstrated that all of four potential N-glycosylation sites in E-cadherin are occupied by N-glycans in human breast carcinoma cells in vivo and the elimination of N-glycan at Asn-633 dramatically affected E-cadherin expression and made it degraded.
20188224	12	21	part_of	granulin	1759:1766	arg1	granulin domains	granulin		granulin domains		PUBTATOR	Site	granulin	2896	domains	Two of the observed glycosylation sites occur within granulin domains, which may have important implications for understanding the structural basis of PGRN action.
10066782	0	17	part_of	receptor	106:113	arg1	the extracellular domain	interleukin-6 receptor		the extracellular domain		PUBTATOR	Site	interleukin-6 receptor	3570	domain	Disulfide bond structure and N-glycosylation sites of the extracellular domain of the human interleukin-6 receptor.
16622833	5	66	gly	acids	733:737	arg1	glycosylation site N107			glycosylation site N107	glycosylation site N107		SpecificSite			site N107	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	5	74	gly	antennae	707:714	arg1	glycosylation site N107			glycosylation site N107	glycosylation site N107		SpecificSite			site N107	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	5	29	gly	glycosylation	742:754	arg2	glycosylation site N107			site N107						site N107	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
10207177	4	91	gly	attached	1034:1041	arg1	individual proteins AND oligosaccharides	individual proteins			oligosaccharides	Fterm		proteins			While we found no evidence for superfamily-specific modifications of the glycans, marked differences were seen in the types of oligosaccharides attached to individual proteins within a given superfamily.
2511201	9	20	gly	glycopeptide	1567:1578	arg2	Bovine protein Z glycopeptide			Bovine protein Z glycopeptide						glycopeptide	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
15869464	3	61	gly	glycosylation	664:676	arg1	native human OPN	native human OPN				PUBTATOR		OPN	6696		Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of native human OPN.
17591618	9	26	gly	glycosylation	1435:1447	arg2	the glycosylation sites			the glycosylation sites						sites	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	9	35	gly	sites	1449:1453	arg1	site-specific N-glycan identification			sites	site-specific N-glycan identification					sites	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
2363690	3	7	gly	galactose	438:446	arg1	the Man(alpha 1----6) arm			the Man(alpha 1----6) arm	the Man(alpha 1----6) arm						The IgG2 and some IgG3 proteins analysed exhibit a predominance of oligosaccharide moieties having galactose on the Man(alpha 1----3) arm rather than the Man(alpha 1----6) arm; it was previously held that galactosylation of the Man(alpha 1----6) arm is preferred, as observed for IgG1, IgG4 and polyclonal IgG.
2363690	3	7	gly	galactose	438:446	arg1	the Man(alpha 1----3) arm			the Man(alpha 1----3) arm	the Man(alpha 1----3) arm						The IgG2 and some IgG3 proteins analysed exhibit a predominance of oligosaccharide moieties having galactose on the Man(alpha 1----3) arm rather than the Man(alpha 1----6) arm; it was previously held that galactosylation of the Man(alpha 1----6) arm is preferred, as observed for IgG1, IgG4 and polyclonal IgG.
2108149	2	85	gly	glycosylation	401:413	arg1	the IgGs	the IgGs				Cterm		IgGs			The glycosylation patterns of the IgGs of the parental and fused cells were studied.
21327254	6	9	gly	Tau	1162:1164	arg1	the microtubule-associated repeats	Tau			the microtubule-associated repeats	Cterm		Tau			Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	57	gly	proline-rich	1077:1088	arg1	the microtubule-associated repeats			proline	the microtubule-associated repeats					proline	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
1577715	0	32	gly	factor	83:88	arg1	the asparagine-linked oligosaccharide chains	von Willebrand factor			the asparagine-linked oligosaccharide chains	PUBTATOR		von Willebrand factor	7450		Structures of the asparagine-linked oligosaccharide chains of human von Willebrand factor.
1577715	0	100	gly	asparagine-linked	18:34	arg1	the asparagine-linked oligosaccharide chains			asparagine	the asparagine-linked oligosaccharide chains					asparagine	Structures of the asparagine-linked oligosaccharide chains of human von Willebrand factor.
1456441	5	88	gly	glycosylation	832:844	arg2	the glycosylation sites			the glycosylation sites						sites	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
2033371	2	41	gly	CD43	459:462	arg1	O-glycans	CD43			O-glycans	PUBTATOR		CD43	6693		Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	2	77	gly	CD43	329:332	arg1	the 70 to 80 O-linked carbohydrate chains	CD43			the 70 to 80 O-linked carbohydrate chains	PUBTATOR		CD43	6693		Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
10397151	9	3	gly	occupied	1175:1182	arg2	both potential N-linked glycosylation sites			both potential N-linked glycosylation sites						sites	Furthermore, both potential N-linked glycosylation sites are occupied.
10397151	9	113	gly	glycosylation	1151:1163	arg2	both potential N-linked glycosylation sites			both potential N-linked glycosylation sites						sites	Furthermore, both potential N-linked glycosylation sites are occupied.
24884609	6	1	gly	N-glycoforms	998:1009	arg1	ITIH4 N-glycoforms	ITIH4 N-glycoforms				PUBTATOR		ITIH4	3700		Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
24884609	6	11	gly	glycopeptides	903:915	arg2	ITIH4 trypsin-GluC glycopeptides			ITIH4 trypsin-GluC glycopeptides						glycopeptides	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
6833285	11	47	gly	linked	1262:1267	arg2	the Ser residue AND the carbohydrate unit			the Ser residue	the carbohydrate unit					Ser residue	Thereby, the carbohydrate unit which is linked to the Ser residue located in the first beta-turn appears to be directed away from the protein.
6684483	0	2	gly	globulin	68:75	arg1	the carbohydrate moiety	sex hormone-binding globulin			the carbohydrate moiety	PUBTATOR		sex hormone-binding globulin	6462		Study of the carbohydrate moiety of human serum sex hormone-binding globulin.
23756652	3	23	gly	domain	438:443	arg1	the complex structure			domain	the complex structure					domain	Here we report the complex structure of the LGR4 extracellular domain (ECD) with the RSPO1 N-terminal fragment (RSPO1-2F) containing two adjacent furin-like cysteine-rich domains (FU-CRDs).
7538124	9	69	gly	glycosylation	1493:1505	arg2	K18 glycosylation sites			K18 glycosylation sites						sites	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	9	1	gly	glycosylation	1608:1620	arg1	other intermediate filament proteins	proteins		sites		Fterm		proteins		sites	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
28089369	7	6	part_of	Notch1	1116:1121	arg1	the Notch1 extracellular domain	Notch1		the Notch1 extracellular domain		PUBTATOR	Site	Notch1	18128	domain	Combined, these results suggest that Fringe modifications "mark" different regions in the Notch1 extracellular domain for activation or inhibition.
28089369	7	36	part_of	regions	1101:1107	arg1	the Notch1 extracellular domain	regions		the Notch1 extracellular domain						domain	Combined, these results suggest that Fringe modifications "mark" different regions in the Notch1 extracellular domain for activation or inhibition.
18775496	0	27	gly	agrin	25:29	arg1	O-fucosylation	agrin			O-fucosylation	PUBTATOR		agrin	O00468		O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors.
18775496	0	38	gly	O-fucosylation	0:13	arg1	muscle agrin	muscle agrin				PUBTATOR		agrin	O00468		O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors.
16894147	0	55	part_of	receptor	39:46	arg1	The first three domains	insulin receptor		The first three domains		PUBTATOR	Site	insulin receptor	3643	domains	The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.
16894147	0	56	part_of	receptor	106:113	arg1	the regions	receptor		the regions		Fterm	Site	receptor		regions	The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.
22750213	6	56	gly	glycosylation	877:889	arg1	mouse PRiMA	mouse PRiMA				PUBTATOR		PRiMA	170952		Abolishing glycosylation on mouse PRiMA appeared not to affect its assembly with AChE(T), the enzymatic properties of AChE, and the membrane trafficking of PRiMA-linked AChE tetramers.
21500857	7	51	gly	found	878:882	arg2	Thr-310 AND O-GlcNAc-P			Thr-310	O-GlcNAc-P					Thr-310	O-GlcNAc or O-GlcNAc-P, but not phosphorylation alone, was found at Thr-310.
21500857	7	51	gly	found	878:882	arg2	Thr-310 AND O-GlcNAc			Thr-310	O-GlcNAc					Thr-310	O-GlcNAc or O-GlcNAc-P, but not phosphorylation alone, was found at Thr-310.
2001369	5	13	gly	glycopeptides	781:793	arg2	Tryptic glycopeptides			Tryptic glycopeptides						glycopeptides	Tryptic glycopeptides containing either of the sites were purified by reversed-phase HPLC, and their oligosaccharides were released enzymatically.
19805286	0	70	part_of	anhydrase	81:89	arg1	the catalytic domain	carbonic anhydrase IX		the catalytic domain		PUBTATOR	Site	carbonic anhydrase IX	768	domain	Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX.
12297050	2	12	part_of	EGFR	406:409	arg1	the EGFR extracellular region	EGFR		the EGFR extracellular region		PUBTATOR	Site	EGFR	1956	region	In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution.
12297050	2	19	part_of	EGF	394:396	arg1	the EGFR extracellular region	EGF		the EGFR extracellular region		PUBTATOR	Site	EGF	1950	region	In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution.
17082223	1	67	gly	glycosylation	185:197	arg1	the bile salt export pump [Bsep	the bile salt export pump [Bsep				OGER		bile salt export pump	O70127		The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	67	gly	glycosylation	185:197	arg1	protein stability	protein stability				Fterm		protein			The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
9425062	8	11	gly	oligosaccharides	1085:1100	arg1	Thr637			Thr637	Thr637		AminoAcid			Thr612, Ser619, Thr621, and Thr637	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	11	gly	oligosaccharides	1085:1100	arg1	Ser619			Ser619	Ser619		AminoAcid			Thr612, Ser619, Thr621, and Thr637	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	11	gly	oligosaccharides	1085:1100	arg1	Thr612			Thr612	Thr612		AminoAcid			Thr612, Ser619, Thr621, and Thr637	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	11	gly	oligosaccharides	1085:1100	arg1	Thr621			Thr621	Thr621		AminoAcid			Thr612, Ser619, Thr621, and Thr637	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
15863501	3	76	part_of	sPLA	512:515	arg1	C-terminal domains	sPLA(2)-III		C-terminal domains		PUBTATOR	Site	sPLA(2)-III	50487	domains	In several if not all cell types, the N- and C-terminal domains of sPLA(2)-III were proteolytically removed, leading to the production of the form containing only the sPLA(2) domain, which could be further N-glycosylated at two consensus sites.
26510530	6	5	gly	glycopeptide	915:926	arg2	The glycopeptide ion abundances			The glycopeptide ion abundances						glycopeptide	The glycopeptide ion abundances were normalized to the respective protein abundances to separate protein glycosylation from protein expression.
11439087	8	49	part_of	sBST-1	1133:1138	arg1	N1-N4	sBST-1		N1-N4		Cterm	SiteSequence	sBST-1	683	N1-N4	Site-directed mutagenesis was performed to generate sBST-1 mutants (N1-N4), each preserving a single N-glycosylation site.
3693371	6	22	part_of	region	1004:1009	arg1	the hyaluronic acid binding region	region		the hyaluronic acid binding region						region	The COOH-terminal two-thirds of rat chondrosarcoma link protein, starting at residue 105, has 41.3% identity with a similar region in the hyaluronic acid binding region.
19864504	7	27	gly	sites	1086:1090	arg1	the glycans			sites	the glycans					sites	The susceptibility for trimming is different for the glycans at the three N-glycosylation sites.
19864504	7	77	gly	N-glycosylation	1070:1084	arg2	the three N-glycosylation sites			the three N-glycosylation sites						sites	The susceptibility for trimming is different for the glycans at the three N-glycosylation sites.
1457416	0	15	gly	A-chain	41:47	arg1	O-glycans	A-chain			O-glycans	Fterm		A-chain			Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	0	15	gly	A-chain	41:47	arg1	N-	A-chain			N-	Fterm		A-chain			Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	0	28	gly	2HS-glycoprotein	71:86	arg1	2HS-glycoprotein	2HS-glycoprotein				PUBTATOR		alpha 2HS-glycoprotein	197		Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
25939779	3	32	gly	glycopeptides	656:668	arg2	glycopeptides			glycopeptides						glycopeptides	Here we present the first crystal structures of complexes of GalNAc-T2 with glycopeptides that together with enhanced sampling molecular dynamics simulations demonstrate a cooperative mechanism by which the lectin domain enables free acceptor sites binding of glycopeptides into the catalytic domain.
25939779	3	49	gly	glycopeptides	472:484	arg2	glycopeptides			glycopeptides						glycopeptides	Here we present the first crystal structures of complexes of GalNAc-T2 with glycopeptides that together with enhanced sampling molecular dynamics simulations demonstrate a cooperative mechanism by which the lectin domain enables free acceptor sites binding of glycopeptides into the catalytic domain.
17643119	0	52	part_of	alpha1	55:60	arg1	the extracellular domain	nAChR alpha1		the extracellular domain		PUBTATOR	Site	nAChR alpha1	11441	domain	Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 A resolution.
7599134	4	71	part_of	ATIII	648:652	arg1	the normal human ATIII cDNA sequence	ATIII		the normal human ATIII cDNA sequence		PUBTATOR	Site	ATIII	462	sequence	Two isoforms are also produced when the normal human ATIII cDNA sequence is expressed in baculovirus-infected insect cells, and the recombinant beta' isoform similarly binds heparin with higher affinity than the recombinant alpha' isoform.
17196528	1	20	part_of	NGF	253:255	arg1	a "high-affinity" NGF binding site	NGF		a "high-affinity" NGF binding site		OGER	Site	NGF	P01138	site	Nerve growth factor engages two structurally distinct transmembrane receptors, TrkA and p75, which have been proposed to create a "high-affinity" NGF binding site through formation of a ternary TrkA/NGF/p75 complex.
21241660	1	33	part_of	immunoreceptor	126:139	arg1	an immunoreceptor tyrosine-based inhibitory motif	receptor		an immunoreceptor tyrosine-based inhibitory motif		Fterm	Site	receptor		motif	PILRα is an immune inhibitory receptor possessing an immunoreceptor tyrosine-based inhibitory motif (ITIM) in its cytoplasmic domain enabling it to deliver inhibitory signals.
21241660	1	0	part_of	possessing	112:121	arg1	PILRα AND an immunoreceptor tyrosine-based inhibitory motif	PILRα		an immunoreceptor tyrosine-based inhibitory motif		PUBTATOR	Site	PILRα 	231805	motif	PILRα is an immune inhibitory receptor possessing an immunoreceptor tyrosine-based inhibitory motif (ITIM) in its cytoplasmic domain enabling it to deliver inhibitory signals.
21241660	1	0	part_of	possessing	112:121	arg1	an immune inhibitory receptor AND an immunoreceptor tyrosine-based inhibitory motif	an immune inhibitory receptor		an immunoreceptor tyrosine-based inhibitory motif		Fterm	Site	receptor		motif	PILRα is an immune inhibitory receptor possessing an immunoreceptor tyrosine-based inhibitory motif (ITIM) in its cytoplasmic domain enabling it to deliver inhibitory signals.
2390069	3	22	gly	lactotransferrin	442:457	arg1	the glycans	lactotransferrin			the glycans	PUBTATOR		lactotransferrin	4057		A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	3	29	gly	lactotransferrin	355:370	arg1	the molar carbohydrate compositions	lactotransferrin			the molar carbohydrate compositions	PUBTATOR		lactotransferrin	4057		A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	3	44	gly	lactotransferrin	387:402	arg1	the molar carbohydrate compositions	lactotransferrin			the molar carbohydrate compositions	PUBTATOR		lactotransferrin	4057		A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
26235030	1	12	gly	leucine-rich	84:95	arg1	Fibronectin leucine-rich repeat			leucine	Fibronectin leucine-rich repeat					leucine	Fibronectin leucine-rich repeat transmembrane proteins (FLRTs) are cell-adhesion molecules with emerging functions in cortical development and synapse formation.
19153605	8	21	part_of	mindin	886:891	arg1	The mindin FS domain	mindin FS		The mindin FS domain		PUBTATOR	Site	mindin FS	10417	domain	The mindin FS domain therefore represents a new integrin ligand.
19153605	8	50	part_of	FS	893:894	arg1	The mindin FS domain	mindin FS		The mindin FS domain		PUBTATOR	Site	mindin FS	10417	domain	The mindin FS domain therefore represents a new integrin ligand.
14764083	6	63	part_of	containing	1011:1020	arg1	rhLF AND Thr130	rhLF		Thr130 and Cys404		OGER	AminoAcid	rhLF	P02788	Thr130 and Cys404	J. 312, 107-114] is restricted to rhLF containing the Thr130 and Cys404.
21689651	0	6	gly	glycosylated	58:69	arg1	glycosylated transmembrane proteins	glycosylated transmembrane proteins				Fterm		proteins			The cataract-associated protein TMEM114, and TMEM235, are glycosylated transmembrane proteins that are distinct from claudin family members.
21689651	0	6	gly	glycosylated	58:69	arg1	TMEM235	TMEM235				OGER		TMEM235	A6NFC5		The cataract-associated protein TMEM114, and TMEM235, are glycosylated transmembrane proteins that are distinct from claudin family members.
21689651	0	6	gly	glycosylated	58:69	arg1	The cataract-associated protein TMEM114	The cataract-associated protein TMEM114				PUBTATOR		TMEM114	B3SHH9		The cataract-associated protein TMEM114, and TMEM235, are glycosylated transmembrane proteins that are distinct from claudin family members.
21264968	5	4	gly	Thr3	1870:1873	arg1	four α-GalNAc residues			residues at Thr2, Thr3, Thr7, and Thr8	four α-GalNAc residues					residues at Thr2, Thr3, Thr7, and Thr8	On the contrary, O-glycosylation of naked MUC5AC peptide occurred predominantly at consecutive Thr residues and led to MUC5AC with four α-GalNAc residues at Thr2, Thr3, Thr7, and Thr8.
21264968	5	9	gly	Thr2	1864:1867	arg1	four α-GalNAc residues			residues at Thr2, Thr3, Thr7, and Thr8	four α-GalNAc residues					residues at Thr2, Thr3, Thr7, and Thr8	On the contrary, O-glycosylation of naked MUC5AC peptide occurred predominantly at consecutive Thr residues and led to MUC5AC with four α-GalNAc residues at Thr2, Thr3, Thr7, and Thr8.
21264968	5	18	gly	Thr7	1876:1879	arg1	four α-GalNAc residues			residues at Thr2, Thr3, Thr7, and Thr8	four α-GalNAc residues					residues at Thr2, Thr3, Thr7, and Thr8	On the contrary, O-glycosylation of naked MUC5AC peptide occurred predominantly at consecutive Thr residues and led to MUC5AC with four α-GalNAc residues at Thr2, Thr3, Thr7, and Thr8.
21264968	5	31	gly	Thr8	1886:1889	arg1	four α-GalNAc residues			residues at Thr2, Thr3, Thr7, and Thr8	four α-GalNAc residues					residues at Thr2, Thr3, Thr7, and Thr8	On the contrary, O-glycosylation of naked MUC5AC peptide occurred predominantly at consecutive Thr residues and led to MUC5AC with four α-GalNAc residues at Thr2, Thr3, Thr7, and Thr8.
21264968	5	64	gly	O-glycosylation	1724:1738	arg2	consecutive Thr residues			consecutive Thr residues						Thr residues	On the contrary, O-glycosylation of naked MUC5AC peptide occurred predominantly at consecutive Thr residues and led to MUC5AC with four α-GalNAc residues at Thr2, Thr3, Thr7, and Thr8.
21264968	5	64	gly	O-glycosylation	1724:1738	arg1	naked MUC5AC peptide			naked MUC5AC peptide						peptide	On the contrary, O-glycosylation of naked MUC5AC peptide occurred predominantly at consecutive Thr residues and led to MUC5AC with four α-GalNAc residues at Thr2, Thr3, Thr7, and Thr8.
21264968	5	95	gly	MUC5AC	1826:1831	arg1	four α-GalNAc residues	MUC5AC			four α-GalNAc residues	PUBTATOR		MUC5AC	4586		On the contrary, O-glycosylation of naked MUC5AC peptide occurred predominantly at consecutive Thr residues and led to MUC5AC with four α-GalNAc residues at Thr2, Thr3, Thr7, and Thr8.
25153361	3	64	gly	N-glycosylation	605:619	arg2	>4 N-glycosylation sequons			>4 N-glycosylation sequons							We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	4	gly	glycoproteins	587:599	arg1	>4 N-glycosylation sequons	glycoproteins				Fterm		glycoproteins			We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	71	gly	glycopeptides	560:572	arg1	complex glycoproteins	glycoproteins		glycopeptides		Fterm		glycoproteins		glycopeptides	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	71	gly	glycopeptides	560:572	arg1	>4 N-glycosylation sequons			glycopeptides						glycopeptides	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	71	gly	glycopeptides	560:572	arg1	>4 N-glycosylation sequons	glycoproteins				Fterm		glycoproteins			We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
1544894	10	25	gly	fucosylation	1527:1538	arg1	EGF domains			EGF domains							These observations raise the possibility that O-linked fucosylation and beta-hydroxylation of EGF domains are mutually exclusive post-translational modifications.
1544894	10	33	gly	domains	1570:1576	arg1	beta-hydroxylation				beta-hydroxylation						These observations raise the possibility that O-linked fucosylation and beta-hydroxylation of EGF domains are mutually exclusive post-translational modifications.
1544894	10	33	gly	domains	1570:1576	arg1	O-linked fucosylation				O-linked fucosylation						These observations raise the possibility that O-linked fucosylation and beta-hydroxylation of EGF domains are mutually exclusive post-translational modifications.
1544894	10	33	gly	domains	1570:1576	arg1	mutually exclusive post-translational modifications				mutually exclusive post-translational modifications						These observations raise the possibility that O-linked fucosylation and beta-hydroxylation of EGF domains are mutually exclusive post-translational modifications.
9767079	1	45	gly	N-glycosylation	153:167	arg1	folate carrier	folate carrier				PUBTATOR		reduced folate carrier	6573		The role of N-glycosylation in reduced folate carrier (RFC) transport and membrane targeting was examined in transport-deficient K562 (K500E) cells transfected with human RFC cDNAs.
9767079	1	45	gly	N-glycosylation	153:167	arg1	RFC	RFC				PUBTATOR		RFC	6573		The role of N-glycosylation in reduced folate carrier (RFC) transport and membrane targeting was examined in transport-deficient K562 (K500E) cells transfected with human RFC cDNAs.
7776966	10	106	gly	Asn174	1575:1580	arg1	carbohydrate			Asn174	carbohydrate					Asn174	Binding assays demonstrate that these two N-linked FSHR carbohydrates are redundant in function since carbohydrate at either Asn174 or Asn276 allows the receptor to be expressed on the cell surface and to bind FSH with normal affinity.
7776966	10	111	gly	Asn276	1585:1590	arg1	carbohydrate			Asn276	carbohydrate					Asn276	Binding assays demonstrate that these two N-linked FSHR carbohydrates are redundant in function since carbohydrate at either Asn174 or Asn276 allows the receptor to be expressed on the cell surface and to bind FSH with normal affinity.
7679920	6	5	gly	fucosylated	1356:1366	arg1	the fucosylated and non-fucosylated triantennary sugar chains				the fucosylated and non-fucosylated triantennary sugar chains						Thus, the fucosylated and non-fucosylated triantennary sugar chains were newly identified in human AFP.
7679920	6	31	gly	non-fucosylated	1372:1386	arg1	the fucosylated and non-fucosylated triantennary sugar chains				the fucosylated and non-fucosylated triantennary sugar chains						Thus, the fucosylated and non-fucosylated triantennary sugar chains were newly identified in human AFP.
18065761	8	11	part_of	TSPN-1	1524:1529	arg1	TSPN-1 domains	TSPN-1		TSPN-1 domains		Cterm	Site	TSPN-1		domains	Dimer formation may also involve TSPN-1 domains from two separate TSP-1 molecules.
24374484	4	43	part_of	enzyme	793:798	arg1	the entire extracellular domain	enzyme		the entire extracellular domain		Fterm	Site	enzyme		domain	In this article, we report the expression, purification, and the crystallographic structure of the entire extracellular domain of this enzyme.
20044576	1	17	gly	glycoprotein	130:141	arg1	a receptor	receptor			Alpha-dystroglycan	Fterm		receptor			Alpha-dystroglycan (alpha-DG) is a cell-surface glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains and certain arenaviruses.
20044576	1	17	gly	glycoprotein	130:141	arg1	a cell-surface glycoprotein	glycoprotein			Alpha-dystroglycan	Fterm		glycoprotein			Alpha-dystroglycan (alpha-DG) is a cell-surface glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains and certain arenaviruses.
18559974	1	43	part_of	fibrinolysis	149:160	arg1	a pro-metallocarboxypeptidase	Thrombin-activatable fibrinolysis inhibitor		a pro-metallocarboxypeptidase		PUBTATOR	AminoAcid	Thrombin-activatable fibrinolysis inhibitor	1361	pro	Thrombin-activatable fibrinolysis inhibitor (TAFI) is a pro-metallocarboxypeptidase that can be proteolytically activated (TAFIa).
18559974	1	47	part_of	Thrombin-activatable	128:147	arg1	a pro-metallocarboxypeptidase	Thrombin-activatable fibrinolysis inhibitor		a pro-metallocarboxypeptidase		PUBTATOR	AminoAcid	Thrombin-activatable fibrinolysis inhibitor	1361	pro	Thrombin-activatable fibrinolysis inhibitor (TAFI) is a pro-metallocarboxypeptidase that can be proteolytically activated (TAFIa).
16083266	4	69	gly	glycopeptides	1778:1790	arg2	glycopeptides			glycopeptides						glycopeptides	Furthermore, additional positively charged arginine and lysine residues in the Lys-C fragments enhance the sensitivity of the post-translationally modified phospho- and glycopeptides by at least 10-fold relative to tryptic fragments.
1059087	2	5	gly	attached	361:368	arg1	asparagine AND one more complex unit			asparagine	one more complex unit					asparagine	Fifteen oligosaccharides are linked to threonine/serine residues via O-glycosidic bonds, and one more complex unit is attached to asparagine.
1059087	2	17	gly	linked	272:277	arg2	threonine/serine residues AND Fifteen oligosaccharides			threonine/serine residues	Fifteen oligosaccharides					residues	Fifteen oligosaccharides are linked to threonine/serine residues via O-glycosidic bonds, and one more complex unit is attached to asparagine.
10207176	7	45	gly	C-mannosylated	955:968	arg1	a C-mannosylated protein	a C-mannosylated protein				Fterm		protein			This is only the second report on a C-mannosylated protein.
2513186	4	55	gly	glycosylation	717:729	arg2	individual glycosylation sites			individual glycosylation sites						sites	Glycopeptides comprising individual glycosylation sites were identified by N-terminal amino acid sequencing.
2226832	1	25	part_of	CAP37	208:212	arg1	the amino acid sequence	CAP37		the amino acid sequence		PUBTATOR	Site	CAP37	566	sequence	We report the amino acid sequence of CAP37, a human neutrophil granule protein with antibacterial and monocyte-specific chemotactic activity.
9757569	0	10	part_of	residue	32:38	arg1	ovine angiotensinogen	angiotensinogen		residue		PUBTATOR	AminoAcid	angiotensinogen	183	residue at position 14	Effects of glycosylation of the residue at position 14 in ovine angiotensinogen on the human renin reaction.
14970177	0	42	gly	glycosylation	9:21	arg1	Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6	Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6				OGER		interleukin 6	P05231		N-linked glycosylation is required for optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6.
3038148	2	69	part_of	enzyme	328:333	arg1	The active site	enzyme		The active site		Fterm	Site	enzyme		site	The active site of this kallikrein-related enzyme is thus made up of the same catalytic triad (Asp, Ser, and His) found in all known serine proteases.
22576872	0	89	part_of	protein	134:140	arg1	endogenous fragments	amyloid precursor protein		endogenous fragments		OGER	Site	amyloid precursor protein	P05067	fragments	An online nano-LC-ESI-FTICR-MS method for comprehensive characterization of endogenous fragments from amyloid β and amyloid precursor protein in human and cat cerebrospinal fluid.
14749323	6	60	gly	glycosylated	1022:1033	arg1	Asp-39			Asp-39						Asp-39	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	6	60	gly	glycosylated	1022:1033	arg1	the corresponding site			the corresponding site						site	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	6	72	gly	glycosylated	960:971	arg1	the putative glycosylation site Asp-39			the putative glycosylation site Asp-39						site Asp-39	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	6	43	gly	glycosylation	917:929	arg2	Asp-39			site Asp-39						site Asp-39	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
8942648	0	85	gly	mapping	38:44	arg1	recombinant human thrombopoietin	recombinant human thrombopoietin				PUBTATOR		thrombopoietin	7066		Peptide, disulfide, and glycosylation mapping of recombinant human thrombopoietin from ser1 to Arg246.
23527852	7	13	gly	fucosylated	981:991	arg1	more complex glycan moieties				more complex glycan moieties						These were characterized by more complex glycan moieties that are fucosylated instead of sialylated.
16474139	4	87	gly	glycosylated	836:847	arg1	The M protein	The M protein				OGER		M protein	P54296		The M protein plays a crucial role in coronavirus assembly and is glycosylated in all coronaviruses, either by N-linked or by O-linked oligosaccharides.
17591618	12	19	gly	non-fucosylated	1873:1887	arg1	triantennary trisialylated fucosylated and non-fucosylated structures				triantennary trisialylated fucosylated and non-fucosylated structures						Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	12	32	gly	trisialylated	1843:1855	arg1	triantennary trisialylated fucosylated and non-fucosylated structures				triantennary trisialylated fucosylated and non-fucosylated structures						Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	12	36	gly	monosialylated	1803:1816	arg1	Diantennary monosialylated glycans				Diantennary monosialylated glycans						Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	12	93	gly	fucosylated	1857:1867	arg1	triantennary trisialylated fucosylated and non-fucosylated structures				triantennary trisialylated fucosylated and non-fucosylated structures						Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
10731668	6	65	gly	glycosylation	967:979	arg1	32			Asn(32 )						Asn(32 )	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
10731668	6	65	gly	glycosylation	967:979	arg2	Asn			Asn(32 )						Asn(32 )	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
10731668	6	65	gly	glycosylation	967:979	arg1	Asn			Asn(32 )						Asn(32 )	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
10731668	6	65	gly	glycosylation	967:979	arg2	Asn			Asn(32 )						Asn(32 )	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
10731668	6	65	gly	glycosylation	967:979	arg1	Asn			Asn(32 )						Asn(32 )	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
10731668	6	65	gly	glycosylation	967:979	arg1	Asn			Asn(32 )						Asn(32 )	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
1556128	7	56	part_of	HB-EGF	1055:1060	arg1	the mature HB-EGF polypeptide	HB-EGF		the mature HB-EGF polypeptide		PUBTATOR	Site	HB-EGF	1839	polypeptide	Microsequencing of tryptic fragments indicated that the mature HB-EGF polypeptide can contain at least 86 of the 208 amino acids predicted by nucleotide sequence to be the HB-EGF precursor molecule.
16815919	7	70	part_of	PLAP	1283:1286	arg1	the calcium-binding site	PLAP		the calcium-binding site		PUBTATOR	Site	PLAP	250	site	The use of the flexible and polarizable force-field TCPEp (topological and classical polarization effects for proteins) predicts that calcium or strontium has similar interaction energies at the calcium-binding site of PLAP.
12799386	9	43	part_of	ZP1	1130:1132	arg1	The C termini	ZP1		The C termini		PUBTATOR	Site	ZP1	22786	termini	The C termini of ZP1, ZP2, and ZP3 lie upstream of a dibasic motif, which is part of, but distinct from, a proprotein convertase cleavage site.
12799386	9	55	part_of	proprotein	1220:1229	arg1	, a proprotein convertase cleavage site	protein		, a proprotein convertase cleavage site		Fterm	Site	protein		site	The C termini of ZP1, ZP2, and ZP3 lie upstream of a dibasic motif, which is part of, but distinct from, a proprotein convertase cleavage site.
12799386	9	59	part_of	ZP2	1135:1137	arg1	The C termini	ZP2		The C termini		PUBTATOR	Site	ZP2	22787	termini	The C termini of ZP1, ZP2, and ZP3 lie upstream of a dibasic motif, which is part of, but distinct from, a proprotein convertase cleavage site.
12799386	9	70	part_of	ZP3	1144:1146	arg1	The C termini	ZP3		The C termini		PUBTATOR	Site	ZP3	22788	termini	The C termini of ZP1, ZP2, and ZP3 lie upstream of a dibasic motif, which is part of, but distinct from, a proprotein convertase cleavage site.
3521732	4	26	gly	asparagine-linked	526:542	arg1	Five asparagine-linked carbohydrate attachment sites			asparagine	Five asparagine-linked carbohydrate attachment sites					asparagine	Five asparagine-linked carbohydrate attachment sites were identified.
24884609	9	6	gly	contained	1294:1302	arg1	Site N274 AND high-mannose N-linked glycans	ITIH4		N274	high-mannose N-linked glycans	PUBTATOR	SpecificSite	ITIH4	3700	N274	Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4.
23376777	8	23	gly	Deglycosylated	1486:1499	arg1	KCC4	KCC4				PUBTATOR		KCC4	20499		Deglycosylated forms of KCC4 also demonstrated decreased tumor formation and lung colonization in mouse xenografts.
28279966	9	49	part_of	VWF	1435:1437	arg1	the VWF A1-A2 linker region	VWF		the VWF A1-A2 linker region		PUBTATOR	Site	VWF	7450	region	Rather under shear stress conditions, or in the presence of denaturants, such as urea or ristocetin, plasmin cleaves the K1491-R1492 peptide bond within the VWF A1-A2 linker region.
24884609	3	41	gly	glycosylation	443:455	arg1	recombinant and serum-derived ITIH4	recombinant and serum-derived ITIH4				PUBTATOR		ITIH4	3700		In this study, we aimed to characterize glycosylation of recombinant and serum-derived ITIH4 using analytical mass spectrometry.
9118998	5	38	gly	glycosylations	933:946	arg1	mFA1	mFA1				PUBTATOR		mFA1	13386		Three N-linked glycosylations were localized in mFA1 (Asn77, Asn142 and Asn151), two of which (Asn142 and Asn151) were in the unusual Asn-Xaa-Cys motif.
9118998	5	69	gly	localized	953:961	arg1	the unusual Asn-Xaa-Cys motif			the unusual Asn-Xaa-Cys motif						Cys motif	Three N-linked glycosylations were localized in mFA1 (Asn77, Asn142 and Asn151), two of which (Asn142 and Asn151) were in the unusual Asn-Xaa-Cys motif.
9118998	5	31	gly	motif	1064:1068	arg1	Asn151			Asn142 and Asn151						Asn142 and Asn151	Three N-linked glycosylations were localized in mFA1 (Asn77, Asn142 and Asn151), two of which (Asn142 and Asn151) were in the unusual Asn-Xaa-Cys motif.
9118998	5	69	gly	localized	953:961	arg1	Asn142			Asn77, Asn142 and Asn151						Asn77, Asn142 and Asn151	Three N-linked glycosylations were localized in mFA1 (Asn77, Asn142 and Asn151), two of which (Asn142 and Asn151) were in the unusual Asn-Xaa-Cys motif.
9118998	5	69	gly	localized	953:961	arg1	Asn77			Asn77, Asn142 and Asn151						Asn77, Asn142 and Asn151	Three N-linked glycosylations were localized in mFA1 (Asn77, Asn142 and Asn151), two of which (Asn142 and Asn151) were in the unusual Asn-Xaa-Cys motif.
9118998	5	69	gly	localized	953:961	arg1	Asn77			Asn77, Asn142 and Asn151						Asn77, Asn142 and Asn151	Three N-linked glycosylations were localized in mFA1 (Asn77, Asn142 and Asn151), two of which (Asn142 and Asn151) were in the unusual Asn-Xaa-Cys motif.
11912203	7	49	gly	glycosylated	921:932	arg1	These four lysines			These four lysines						lysines	These four lysines were found to be hydroxylated and subsequently glycosylated.
24058541	4	24	gly	N-glycosylation	483:497	arg2	the N-glycosylation consensus sites			the N-glycosylation consensus sites						sites	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	4	55	gly	utilized	576:583	arg2	all eight putative N-glycosylation sites			all eight putative N-glycosylation sites						sites	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	4	59	gly	N-glycosylation	550:564	arg2	all eight putative N-glycosylation sites			all eight putative N-glycosylation sites						sites	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
27314333	6	43	part_of	N137	1080:1083	arg1	Rspo1	Rspo1		N137		PUBTATOR	SpecificSite	Rspo1	284654	N137	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
8404899	6	12	part_of	have	881:884	arg1	The purified variants AND amino-acid composition	The purified variants		amino-acid composition		Fterm	Site	variants		position	The purified variants have an identical molecular mass and amino-acid composition.
9572875	2	32	gly	nonglycosylated	386:400	arg1	Glycosylated and nonglycosylated recombinant human IGFBP-6	Glycosylated and nonglycosylated recombinant human IGFBP-6				PUBTATOR		IGFBP-6	3489		Glycosylated and nonglycosylated recombinant human IGFBP-6, expressed in Chinese hamster ovary cells and Escherichia coli, respectively, were purified using IGF-II affinity chromatography and reverse-phase medium-pressure chromatography.
3555489	0	41	part_of	enkephalinase	49:61	arg1	amino acid sequence	enkephalinase		amino acid sequence		PUBTATOR	Site	enkephalinase	24590	sequence	Molecular cloning and amino acid sequence of rat enkephalinase.
17591618	3	44	gly	glycosylation	437:449	arg1	CFH	CFH				PUBTATOR		CFH	P08603		In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	3	53	gly	CFH	463:465	arg1	a complete site-specific N-glycan characterization	CFH			a complete site-specific N-glycan characterization	PUBTATOR		CFH	P08603		In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
2033371	9	93	gly	GalNAcOH	1987:1994	arg1	CD43	CD43			GalNAcOH	PUBTATOR		CD43	6693		Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
8615697	9	69	gly	contain	1354:1360	arg1	Five sites AND high mannose type units			Five sites	high mannose type units					sites	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
1898343	6	38	gly	linked	1045:1050	arg1	residues AND lactosamine antennae			residues	lactosamine antennae					residues	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
28207759	4	33	gly	PLC	774:776	arg1	9	Shire PLC			9	PUBTATOR		Shire PLC	3339		Two recombinant GBA preparations with distinct N-linked glycans are registered in Europe for treatment of type I GD: imiglucerase (Genzyme), contains predominantly Man(3) glycans, and velaglucerase (Shire PLC) Man(9) glycans.
28207759	4	33	gly	PLC	774:776	arg1	velaglucerase (Shire PLC) Man	Shire PLC			velaglucerase (Shire PLC) Man	PUBTATOR		Shire PLC	3339		Two recombinant GBA preparations with distinct N-linked glycans are registered in Europe for treatment of type I GD: imiglucerase (Genzyme), contains predominantly Man(3) glycans, and velaglucerase (Shire PLC) Man(9) glycans.
28207759	4	93	gly	Shire	768:772	arg1	9	Shire PLC			9	PUBTATOR		Shire PLC	3339		Two recombinant GBA preparations with distinct N-linked glycans are registered in Europe for treatment of type I GD: imiglucerase (Genzyme), contains predominantly Man(3) glycans, and velaglucerase (Shire PLC) Man(9) glycans.
28207759	4	93	gly	Shire	768:772	arg1	velaglucerase (Shire PLC) Man	Shire PLC			velaglucerase (Shire PLC) Man	PUBTATOR		Shire PLC	3339		Two recombinant GBA preparations with distinct N-linked glycans are registered in Europe for treatment of type I GD: imiglucerase (Genzyme), contains predominantly Man(3) glycans, and velaglucerase (Shire PLC) Man(9) glycans.
28207759	4	53	gly	contains	710:717	arg1	Genzyme AND Man(3) glycans	Genzyme			Man(3) glycans	Fterm		Genzyme	2629		Two recombinant GBA preparations with distinct N-linked glycans are registered in Europe for treatment of type I GD: imiglucerase (Genzyme), contains predominantly Man(3) glycans, and velaglucerase (Shire PLC) Man(9) glycans.
28207759	4	53	gly	contains	710:717	arg1	imiglucerase AND Man(3) glycans	imiglucerase			Man(3) glycans	PUBTATOR		GD: imiglucerase	2629		Two recombinant GBA preparations with distinct N-linked glycans are registered in Europe for treatment of type I GD: imiglucerase (Genzyme), contains predominantly Man(3) glycans, and velaglucerase (Shire PLC) Man(9) glycans.
16342937	15	13	gly	numerous	2483:2490	arg1	potential O-glycosylation sites			potential O-glycosylation sites						sites	In comparison, potential O-glycosylation sites are numerous (59-83 Ser/Thr residues), but only two regions were observed to carry O-glycans in rat ZP3.
16342937	15	13	gly	numerous	2483:2490	arg1	59-83 Ser/Thr residues			59-83 Ser/Thr residues						residues	In comparison, potential O-glycosylation sites are numerous (59-83 Ser/Thr residues), but only two regions were observed to carry O-glycans in rat ZP3.
16342937	15	65	gly	O-glycosylation	2457:2471	arg2	potential O-glycosylation sites			potential O-glycosylation sites						sites	In comparison, potential O-glycosylation sites are numerous (59-83 Ser/Thr residues), but only two regions were observed to carry O-glycans in rat ZP3.
16342937	15	65	gly	O-glycosylation	2457:2471	arg2	59-83 Ser/Thr residues			59-83 Ser/Thr residues						residues	In comparison, potential O-glycosylation sites are numerous (59-83 Ser/Thr residues), but only two regions were observed to carry O-glycans in rat ZP3.
10756055	2	28	gly	glycosylation	365:377	arg2	the N-linked glycosylation sites			the N-linked glycosylation sites						sites	Here we report on the unexpected observation that the removal of the N-linked glycosylation sites in CXCR4 potentially allows the protein to serve as a universal coreceptor for both X4 and R5 laboratory-adapted and primary HIV-1 strains.
15696168	3	24	part_of	Fab	393:395	arg1	the Fab fragment	Fab		the Fab fragment		PUBTATOR	Site	Fab	2187	fragment	Here we present the crystal structure of a soluble form of CD28 in complex with the Fab fragment of a mitogenic antibody.
11595658	1	16	gly	N-glycosylation	178:192	arg2	five potential N-glycosylation sites			five potential N-glycosylation sites						sites	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	gly	sites	194:198	arg1	five potential N-glycosylation sites			five potential N-glycosylation sites						sites	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N98			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N90			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N45			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N78			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N90			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N45			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N78			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N45			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N78			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N78			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	gly	sites	194:198	arg1	N98			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	gly	sites	194:198	arg1	N78			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	gly	sites	194:198	arg1	N38			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	gly	sites	194:198	arg1	N90			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	gly	sites	194:198	arg1	N78			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	gly	sites	194:198	arg1	N38			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	gly	sites	194:198	arg1	N90			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	gly	sites	194:198	arg1	N38			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	gly	sites	194:198	arg1	N90			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	gly	sites	194:198	arg1	N90			N38, N45, N78, N90, and N98						N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
8962717	6	27	gly	fucosylated	1004:1014	arg1	tetra-antennary oligosaccharides				tetra-antennary oligosaccharides						The data were consistent with the complex chains being trisialylated tetra-antennary oligosaccharides fucosylated on the reducing terminal GlcNAc.
8962717	6	32	gly	trisialylated	957:969	arg1	the complex chains				the complex chains						The data were consistent with the complex chains being trisialylated tetra-antennary oligosaccharides fucosylated on the reducing terminal GlcNAc.
15173186	9	2	part_of	located	1363:1369	arg2	other human Toll-like receptors AND consensus glycosylation sites	other human Toll-like receptors		consensus glycosylation sites		Fterm	Site	receptors		sites	We have also analyzed where consensus glycosylation sites are located in the extracellular domains of other human Toll-like receptors.
15173186	9	85	part_of	receptors	1425:1433	arg1	the extracellular domains	receptors		the extracellular domains		Fterm	Site	receptors		domains	We have also analyzed where consensus glycosylation sites are located in the extracellular domains of other human Toll-like receptors.
2108149	5	12	gly	possessed	848:856	arg1	IgGs AND oligosaccharide units	IgGs			oligosaccharide units	Cterm		IgGs			IgGs from both parental lines possessed oligosaccharide units displaying microheterogeneity based upon a common symmetrical biantennary structure terminating in beta-GlcNAc.
1731338	5	52	gly	galactoglycoprotein	897:915	arg1	galactoglycoprotein molecules	galactoglycoprotein molecules				PUBTATOR		galactoglycoprotein	6693		C-terminal analysis revealed multiple C-terminal residues, suggesting that galactoglycoprotein molecules are of varying lengths.
6966283	3	0	part_of	protein	232:238	arg1	3 separate asparaginyl residues	protein		3 separate asparaginyl residues		Fterm	Site	protein		residues	Human alpha 1-protease inhibitor has three oligosaccharide side chains attached to 3 separate asparaginyl residues of the protein by N-glycosyl linkages.
10029548	1	64	part_of	transferrin	216:226	arg1	the N-lobe	transferrin		the N-lobe		PUBTATOR	Site	transferrin	7018	N-lobe	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
15458386	6	11	gly	glycosylated	789:800	arg1	these sites			these sites						sites	Mutations of the five potential N-glycosylation sites individually and in combination showed that these sites were all glycosylated and deficient glycosylation decreased the enzyme activity.
15458386	6	47	gly	N-glycosylation	702:716	arg2	the five potential N-glycosylation sites			the five potential N-glycosylation sites						sites	Mutations of the five potential N-glycosylation sites individually and in combination showed that these sites were all glycosylated and deficient glycosylation decreased the enzyme activity.
19946266	4	17	part_of	channel	758:764	arg1	the ion channel domain	channel		the ion channel domain		Fterm	Site	channel		domain	The receptor harbours an overall axis of two-fold symmetry with the extracellular domains organized as pairs of local dimers and with the ion channel domain exhibiting four-fold symmetry.
8130392	4	106	gly	N-glycosylation	655:669	arg2	four N-glycosylation sites			four N-glycosylation sites						sites	Protein C is a heavily post-translationally modified serine protease with four N-glycosylation sites.
28089369	1	9	gly	Notch	300:304	arg1	epidermal growth factor-like (EGF) repeats	Notch			epidermal growth factor-like (EGF) repeats	PUBTATOR		Notch	31293		Fringe proteins are β3-N-acetylglucosaminyltransferases that modulate Notch activity by modifying O-fucose residues on epidermal growth factor-like (EGF) repeats of Notch.
16321355	4	62	part_of	peptides	646:653	arg1	the glycopeptides	peptides		the glycopeptides						glycopeptides	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
25153361	6	5	gly	glycopeptides	980:992	arg2	glycopeptides the most abundant ions			glycopeptides the most abundant ions						glycopeptides	The online enrichment renders glycopeptides the most abundant ions detected, thereby facilitating the generation of high-quality data-dependent tandem mass spectra.
25374123	3	58	part_of	vitronectin	511:521	arg1	the site-specific N-glycopeptides	vitronectin		the site-specific N-glycopeptides		PUBTATOR	Site	vitronectin	7448	N-glycopeptides	Here, we systematically analyzed the site-specific N-glycopeptides of vitronectin in human plasma by tandem mass spectrometry combined with immunoprecipitation and hydrophilic interaction liquid chromatography (HILIC) enrichment.
23302862	6	11	part_of	insulin	1249:1255	arg1	insulin B-chain residues	insulin		insulin B-chain residues		PUBTATOR	Site	insulin	P01308	residues	Contact between insulin and L1 is restricted to insulin B-chain residues.
3353370	8	111	gly	leucine-rich	1676:1687	arg1	the leucine-rich tandem repeats			leucine	the leucine-rich tandem repeats					leucine	The leucine-rich sequence in the beta chain of GPIb is flanked on both sides by amino acid sequences that are similar to those flanking the leucine-rich tandem repeats of the alpha chain of GPIb and leucine-rich alpha 2-glycoprotein.
8053566	1	29	gly	glycopeptides	295:307	arg2	glycopeptides			glycopeptides						glycopeptides	A rapid and sensitive method for sequencing oligosaccharides has been developed, using matrix-assisted laser desorption mass spectrometry to monitor the digestion of glycopeptides by specific exoglycosidases.
9334252	9	39	gly	glycoproteins	1658:1670	arg1	recombinant glycoproteins	recombinant glycoproteins				Fterm		glycoproteins			These results not only form the basis for further studies on the biochemical aspects of C-mannosylation but also have implications for the choice of cells for production of recombinant glycoproteins.
21244856	2	22	gly	N-glycosylation	459:473	arg1	multiple asparagines			multiple asparagines						asparagines	It is presumed that all 19 mammalian Wnt family members contain two types of post-translational modification: the covalent attachment of fatty acids at two distinct positions, and the N-glycosylation of multiple asparagines.
21244856	2	29	gly	N-glycosylation	459:473	arg1	two distinct positions			positions,						positions,	It is presumed that all 19 mammalian Wnt family members contain two types of post-translational modification: the covalent attachment of fatty acids at two distinct positions, and the N-glycosylation of multiple asparagines.
8202534	0	43	gly	invariant	38:46	arg1	Human serum amyloid P component	invariant			Human serum amyloid P component	Fterm		invariant			Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
2775232	4	0	part_of	receptors	970:978	arg1	the conservative positions	receptors		the conservative positions		Fterm	Site	receptors		positions	Given the extensive structural similarity among the two-chain alpha-subunits of Arg-Gly-Asp adhesion receptors and the conservative positions of cysteine residues in their amino acid sequences, the intrachain and interchain disulphide-bond pattern found here in GPIIb will most probably be conserved in all two-chain alpha-subunits of these receptors.
2775232	4	8	part_of	sequences	1052:1060	arg1	the conservative positions	sequences		the conservative positions						positions	Given the extensive structural similarity among the two-chain alpha-subunits of Arg-Gly-Asp adhesion receptors and the conservative positions of cysteine residues in their amino acid sequences, the intrachain and interchain disulphide-bond pattern found here in GPIIb will most probably be conserved in all two-chain alpha-subunits of these receptors.
2775232	4	8	part_of	sequences	1052:1060	arg1	the two-chain alpha-subunits	subunits		sequences		OGER	Site	subunits	3674	sequences	Given the extensive structural similarity among the two-chain alpha-subunits of Arg-Gly-Asp adhesion receptors and the conservative positions of cysteine residues in their amino acid sequences, the intrachain and interchain disulphide-bond pattern found here in GPIIb will most probably be conserved in all two-chain alpha-subunits of these receptors.
2775232	4	90	part_of	alpha-subunits	931:944	arg1	their amino acid sequences	subunits		their amino acid sequences		OGER	Site	subunits	3674	sequences	Given the extensive structural similarity among the two-chain alpha-subunits of Arg-Gly-Asp adhesion receptors and the conservative positions of cysteine residues in their amino acid sequences, the intrachain and interchain disulphide-bond pattern found here in GPIIb will most probably be conserved in all two-chain alpha-subunits of these receptors.
21308849	5	24	part_of	NgR2	819:822	arg1	the stalk regions	NgR2		the stalk regions		PUBTATOR	Site	NgR2	349667	regions	We also present the crystal structure of the LRR and part of the stalk regions of NgR2 and compare it to the previously reported NgR1 structure with respect to the distinct signaling properties of the two receptor isoforms.
1533633	8	18	gly	glycosylation	1250:1262	arg2	all three glycosylation sites			all three glycosylation sites						sites	The unglycosylated alpha-subunit, resulting from genetic alteration of all three glycosylation sites or synthesis of the wild-type protein in the presence of tunicamycin, was catalytically inactive.
1533633	8	61	gly	unglycosylated	1173:1186	arg1	The unglycosylated alpha-subunit	The unglycosylated alpha-subunit				OGER		subunit	P06865		The unglycosylated alpha-subunit, resulting from genetic alteration of all three glycosylation sites or synthesis of the wild-type protein in the presence of tunicamycin, was catalytically inactive.
22511793	6	27	gly	N-glycosylation	1049:1063	arg2	potential N-glycosylation sites			potential N-glycosylation sites						sites	By differential membrane extraction and sequential mutagenesis of potential N-glycosylation sites, we identified TMEM106B as a type 2 integral membrane protein with a highly glycosylated luminal domain.
22511793	6	47	gly	glycosylated	1147:1158	arg1	a highly glycosylated luminal domain			a highly glycosylated luminal domain						domain	By differential membrane extraction and sequential mutagenesis of potential N-glycosylation sites, we identified TMEM106B as a type 2 integral membrane protein with a highly glycosylated luminal domain.
2387072	2	40	gly	glycopeptides	427:439	arg2	the membrane glycopeptides			the membrane glycopeptides						glycopeptides	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	2	49	gly	attached	566:573	arg1	asparagine AND N-acetylglucosamine			asparagine	N-acetylglucosamine					asparagine	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
24058541	9	22	part_of	CLN5	1318:1321	arg1	various N-glycosylation sites	CLN5		various N-glycosylation sites		PUBTATOR	Site	CLN5	O75503	sites	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
8407981	7	18	part_of	protein	1096:1102	arg1	modified Asn-180 residue	protein		modified Asn-180 residue		Fterm	SpecificSite	protein		Asn-180 residue	The core glycosylation did not occur when the Asn-12 residue was mutated, whereas the mutant protein with modified Asn-180 residue was glycosylated.
2049076	14	51	gly	O-glycosylated	2248:2261	arg1	the only O-glycosylated human IFN-alpha protein	the only O-glycosylated human IFN-alpha protein				PUBTATOR		IFN-alpha protein	3440		As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.
9535843	2	53	part_of	proteins	358:365	arg1	the amino acid sequence	proteins		the amino acid sequence		Fterm	Site	proteins		sequence	Kyte-Doolittle analysis of the amino acid sequence of Trp proteins identifies seven hydrophobic regions (H1-H7) with potential of forming transmembrane segments.
6619126	12	17	gly	linked	1853:1858	arg1	about 2-3 Ser and/or Thr residues AND The saccharides			about 2-3 Ser and/or Thr residues	The saccharides					Ser	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	12	17	gly	linked	1853:1858	arg1	about 2-3 Ser and/or Thr residues AND The saccharides			about 2-3 Ser and/or Thr residues	The saccharides					Thr residues	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	12	133	gly	glycoprotein	1913:1924	arg1	the donor LG glycoprotein	the donor LG glycoprotein				Fterm		glycoprotein			The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
8344278	1	15	gly	A	242:242	arg1	the oligosaccharide moieties	saposin A			the oligosaccharide moieties	Cterm		saposin A			We have determined and compared the structures of the oligosaccharide moieties of saposin A, C and D purified from the spleen of a patient with Gaucher disease.
10207177	10	0	gly	glycoproteins	2117:2129	arg1	the native cell surface glycoproteins	the native cell surface glycoproteins				Fterm		glycoproteins			The models also indicated that sugars are likely to play a role in the packing of the native cell surface glycoproteins and to limit nonspecific protein-protein interactions.
23001782	4	5	part_of	sites	684:688	arg1	intact hSHBG	hSHBG		sites		PUBTATOR	Site	hSHBG	6462	sites	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	91	part_of	hSHBG	832:836	arg1	glycosylation sites	hSHBG		glycosylation sites		PUBTATOR	Site	hSHBG	6462	sites	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
16362042	7	62	part_of	Gas6	991:994	arg1	Only the minor Gas6 binding site	Gas6		Only the minor Gas6 binding site		PUBTATOR	Site	Gas6	2621	site	Only the minor Gas6 binding site is highly conserved in the other Axl family receptors, Sky/Tyro3 and Mer.
9228058	7	36	part_of	FasL	1238:1241	arg1	Tyr-218	FasL		Tyr-218		PUBTATOR	SpecificSite	FasL	356	Tyr-218	Although the cytotoxic activity of mutant Y218D was unaltered, mutant Y218R was inactive, correlating with the prediction that Tyr-218 of FasL interacts with a cluster of three basic amino acid side chains of Fas.
7663166	4	66	part_of	OSF-2	599:603	arg1	a C-terminal synthetic OSF-2 peptide	OSF-2		a C-terminal synthetic OSF-2 peptide		PUBTATOR	Site	OSF-2	50706	peptide	Western blotting analysis employing polyclonal antiserum raised against a C-terminal synthetic OSF-2 peptide detected a protein of approximately 90-kDa as early as 2 days after infection of Sf9 cells with the recombinant virus.
3877053	7	92	part_of	XII	889:891	arg1	the predicted amino acid sequence	factor XII		the predicted amino acid sequence		OGER	Site	factor XII	P00748	sequence	Within the predicted amino acid sequence of factor XII, we have identified three peptide bonds that are cleaved by kallikrein during the formation of beta-factor XIIa.
7309709	1	19	gly	asparagine-linked	108:124	arg1	three asparagine-linked sugar chains			asparagine	three asparagine-linked sugar chains					asparagine	Human prothrombin contains three asparagine-linked sugar chains in one molecule.
7309709	1	17	gly	contains	93:100	arg1	Human prothrombin AND three asparagine-linked sugar chains	Human prothrombin			three asparagine-linked sugar chains	PUBTATOR		Human prothrombin	2147		Human prothrombin contains three asparagine-linked sugar chains in one molecule.
1997323	14	1	gly	tetrasialylated	1711:1725	arg1	several tetrasialylated diantennary glycans				several tetrasialylated diantennary glycans						A further preparation, obtained from the most anionic DEAE-cellulose fraction (peak V) or rTf contained several tetrasialylated diantennary glycans whose precise structures remain to be established in future studies.
1997323	14	70	gly	contained	1693:1701	arg1	rTf AND several tetrasialylated diantennary glycans	rTf			several tetrasialylated diantennary glycans	Cterm		rTf	24825		A further preparation, obtained from the most anionic DEAE-cellulose fraction (peak V) or rTf contained several tetrasialylated diantennary glycans whose precise structures remain to be established in future studies.
8142896	3	12	gly	receptor	585:592	arg1	the carbohydrate moieties	receptor			the carbohydrate moieties	Fterm		receptor			We investigated the utilization of the potential sites for N-linked glycosylation and the structure of the carbohydrate moieties of this soluble receptor.
27922006	6	28	gly	glycosylation	795:807	arg1	tryptophan C-mannosylation				tryptophan C-mannosylation						Two post-translational modifications were identified-N-linked glycosylation at the dimerization interface and tryptophan C-mannosylation proximal to the ganglioside binding site-that appear to have regulatory functions.
27922006	6	61	gly	tryptophan	843:852	arg1	tryptophan C-mannosylation			tryptophan	tryptophan C-mannosylation					tryptophan	Two post-translational modifications were identified-N-linked glycosylation at the dimerization interface and tryptophan C-mannosylation proximal to the ganglioside binding site-that appear to have regulatory functions.
21550978	4	80	gly	glycosylation	762:774	arg1	hPAR(1)	hPAR(1)				PUBTATOR		hPAR(1)	2149		We have analyzed the role of N-linked glycosylation in regulating proteinase activation/disarming and cell global expression of hPAR(1).
9030779	6	8	gly	N-glycosylation	801:815	arg2	the two C-terminal N-glycosylation sites			the two C-terminal N-glycosylation sites						sites	However, removal of the two C-terminal N-glycosylation sites inhibits the formation of mature enzyme.
20534510	4	41	part_of	PDGFRbeta	674:682	arg1	the first three Ig domains	PDGFRbeta		the first three Ig domains		PUBTATOR	Site	PDGFRbeta	5159	domains	We also present the structure of the complex between PDGF-B and the first three Ig domains of PDGFRbeta, showing that two PDGF-B protomers clamp PDGFRbeta at their dimerization seam.
17018531	5	36	gly	utilized	952:959	arg2	Asn-116			Asn-116						Asn-116	Mass spectrometric analysis revealed that of the three potential N-linked glycosylation sites present in the mature protein, Asn-19 is not utilized; Asn-39 is linked to an endoglycosidase H (Endo H)-sensitive oligosaccharide, and Asn-116 is variably utilized, either being unmodified or linked to Endo H-sensitive or Endo H-resistant oligosaccharides.
17018531	5	58	gly	utilized	841:848	arg2	Asn-19			Asn-19						Asn-19	Mass spectrometric analysis revealed that of the three potential N-linked glycosylation sites present in the mature protein, Asn-19 is not utilized; Asn-39 is linked to an endoglycosidase H (Endo H)-sensitive oligosaccharide, and Asn-116 is variably utilized, either being unmodified or linked to Endo H-sensitive or Endo H-resistant oligosaccharides.
17018531	5	92	gly	glycosylation	776:788	arg2	the three potential N-linked glycosylation sites			the three potential N-linked glycosylation sites						sites	Mass spectrometric analysis revealed that of the three potential N-linked glycosylation sites present in the mature protein, Asn-19 is not utilized; Asn-39 is linked to an endoglycosidase H (Endo H)-sensitive oligosaccharide, and Asn-116 is variably utilized, either being unmodified or linked to Endo H-sensitive or Endo H-resistant oligosaccharides.
7538124	4	53	part_of	K18	638:640	arg1	K18 Ser	K18		K18 Ser		PUBTATOR	AminoAcid	K18	3875	Ser and Thr	For this, we generated a panel of K18 Ser and Thr-->Ala mutants at potential glycosylation sites followed by expression in a baculovirus-insect cell system.
8243461	5	30	gly	glycopeptides	1228:1240	arg2	the glycopeptides			the glycopeptides						glycopeptides	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	5	75	gly	deglycosylation	1205:1219	arg1	the glycopeptides			the glycopeptides						glycopeptides	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
20406422	3	38	gly	non-glycosylated	487:502	arg1	Both partially and non-glycosylated CLN7	Both partially and non-glycosylated CLN7				PUBTATOR		CLN7	256471		Both partially and non-glycosylated CLN7 were correctly transported to lysosomes.
9597769	1	9	gly	glycopeptides	169:181	arg2	glycopeptides			glycopeptides						glycopeptides	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides was evaluated using quadrupole time-of-flight (QTOF) technology in the MS/MS mode.
17715132	0	42	gly	glycosylation	29:41	arg2	a glycosylation site			a glycosylation site						site	Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane.
16014566	6	89	gly	glycosylation	1277:1289	arg2	N92			N92						N92	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	6	89	gly	glycosylation	1277:1289	arg1	human GPVI	GPVI		N92		PUBTATOR		GPVI	51206	N92	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	6	89	gly	glycosylation	1277:1289	arg1	human GPVI	GPVI		N92		PUBTATOR		GPVI	51206	N92	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16212939	6	78	gly	N-glycosylation	1132:1146	arg1	the secretion enhancer peptide			the secretion enhancer peptide						peptide	These results show that N-glycosylation of the secretion enhancer peptide plays an important role in increasing the secretion efficiency of the downstream target proteins.
1517205	4	51	gly	peptides	916:923	arg1	sialic acid analysis			peptides	sialic acid analysis					peptides	Data on the component sugar analysis after pyridylamination (PA) and sialic acid analysis of the isolated peptides indicated that they contained 1 mol each of galactose (Gal), fucose (Fuc), N-acetylglucosamine (GlcNAc), and N-acetylneuraminic acid (NeuAc), in addition to Glc and Xyl.
20693656	1	40	part_of	phosphatase	206:216	arg1	the functional sites	phosphatase		the functional sites		Fterm	Site	phosphatase		sites	In order to gain deeper insights into the functional sites of human placental alkaline phosphatase, the structures of the enzyme with the putative regulators L-Phe, pNPP and 5'-AMP [Llinas et al. (2005), J. Mol.
23376777	4	3	gly	glycosylation	670:682	arg2	N-linked glycosylation sites			N-linked glycosylation sites						sites	We showed that triple (N312/331/344/Q) and quadruple (N312/331/344/360/Q) mutations of N-linked glycosylation sites disrupt the N-linked glycosylation of KCC4, resulting in the accumulation of KCC4, predominantly in the endoplasmic reticulum (ER) and not at the cell surface.
23376777	4	69	gly	glycosylation	711:723	arg1	KCC4	KCC4				PUBTATOR		KCC4	20499		We showed that triple (N312/331/344/Q) and quadruple (N312/331/344/360/Q) mutations of N-linked glycosylation sites disrupt the N-linked glycosylation of KCC4, resulting in the accumulation of KCC4, predominantly in the endoplasmic reticulum (ER) and not at the cell surface.
7263706	0	35	part_of	gamma-subunit	31:43	arg1	The amino acid sequence	gamma-subunit		The amino acid sequence		Fterm	Site	gamma-subunit		sequence	The amino acid sequence of the gamma-subunit of mouse submaxillary gland 7 S nerve growth factor.
12731887	1	5	gly	glycoprotein	203:214	arg1	2- (eIF2-) associated glycoprotein p67	2- (eIF2-) associated glycoprotein p67				Fterm		glycoprotein			Eukaryotic initiation factor 2- (eIF2-) associated glycoprotein p67 blocks eIF2alpha phosphorylation by kinases, and its N-terminal 1-97 amino acid segment can induce efficient translation.
16847056	2	63	gly	linked	258:263	arg1	beta1 AND sialic acid residues	beta1			sialic acid residues	Cterm		beta1			We have shown that sialic acid residues linked to Nav alpha and beta1 subunits alter channel gating.
10715549	0	36	gly	N-glycosylation	11:25	arg2	13			Asn(13)						Asn(13)	Additional N-glycosylation at Asn(13) rescues the human LHbeta-subunit from disulfide-linked aggregation.
10715549	0	36	gly	N-glycosylation	11:25	arg1	Asn			Asn(13)						Asn(13)	Additional N-glycosylation at Asn(13) rescues the human LHbeta-subunit from disulfide-linked aggregation.
10715549	0	36	gly	N-glycosylation	11:25	arg2	Asn			Asn(13)						Asn(13)	Additional N-glycosylation at Asn(13) rescues the human LHbeta-subunit from disulfide-linked aggregation.
10715549	0	36	gly	N-glycosylation	11:25	arg1	Asn			Asn(13)						Asn(13)	Additional N-glycosylation at Asn(13) rescues the human LHbeta-subunit from disulfide-linked aggregation.
10715549	0	36	gly	N-glycosylation	11:25	arg2	Asn			Asn(13)						Asn(13)	Additional N-glycosylation at Asn(13) rescues the human LHbeta-subunit from disulfide-linked aggregation.
10715549	0	36	gly	N-glycosylation	11:25	arg2	Asn			Asn(13)						Asn(13)	Additional N-glycosylation at Asn(13) rescues the human LHbeta-subunit from disulfide-linked aggregation.
1899031	0	53	gly	present	27:33	arg2	asparagine-289 AND Oligosaccharide structures			asparagine-289	Oligosaccharide structures					asparagine-289	Oligosaccharide structures present on asparagine-289 of recombinant human plasminogen expressed in a Chinese hamster ovary cell line.
15657036	5	50	gly	type	603:606	arg1	secreted FGE	FGE			type	PUBTATOR		FGE	285362		Intracellular FGE contains a high mannose type N-glycan, which is processed to the complex type in secreted FGE.
15657036	5	14	gly	contains	530:537	arg1	Intracellular FGE AND a high mannose type N-glycan	Intracellular FGE			a high mannose type N-glycan	PUBTATOR		FGE	285362		Intracellular FGE contains a high mannose type N-glycan, which is processed to the complex type in secreted FGE.
2983222	2	14	part_of	receptor	295:302	arg1	a precursor processing enzyme cleavage site	receptor		a precursor processing enzyme cleavage site		Fterm	Site	receptor		site	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	25	part_of	precursor	321:329	arg1	a precursor processing enzyme cleavage site	precursor		a precursor processing enzyme cleavage site		Fterm	Site	precursor		site	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	23	part_of	containing	386:395	arg1	the receptor alpha-subunit AND a single 23-amino-acid transmembrane sequence	subunit		sequence		OGER	Site	subunit	3643	sequence	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
7574684	0	39	part_of	trkB	46:49	arg1	Extracellular domain	trkB		Extracellular domain		PUBTATOR	Site	trkB	4915	domain	Extracellular domain of neurotrophin receptor trkB: disulfide structure, N-glycosylation sites, and ligand binding.
16203964	3	39	part_of	ErbB4	519:523	arg1	the extracellular region	ErbB4		the extracellular region		PUBTATOR	Site	ErbB4	2066	region	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
17222411	4	9	gly	glycopeptides	514:526	arg2	glycopeptides			glycopeptides						glycopeptides	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	20	gly	glycosylation	716:728	arg2	residue Thr52			residue Thr52						residue Thr52	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	20	gly	glycosylation	716:728	arg2	a glycosylation site			a glycosylation site						site	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
7462199	1	31	gly	asparagine-linked	98:114	arg1	The asparagine-linked sugar chains			asparagine	The asparagine-linked sugar chains					asparagine	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	1	31	gly	asparagine-linked	98:114	arg1	oligosaccharides			asparagine	oligosaccharides					asparagine	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	1	57	gly	globulin	147:154	arg1	The asparagine-linked sugar chains	cold-insoluble globulin			The asparagine-linked sugar chains	PUBTATOR		cold-insoluble globulin	2335		The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	1	57	gly	globulin	147:154	arg1	oligosaccharides	cold-insoluble globulin			oligosaccharides	PUBTATOR		cold-insoluble globulin	2335		The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
18420026	4	30	gly	positions	1132:1140	arg1	positions			positions						positions	Bioinformatics analysis showed there were two putative N-glycosylation sites within human NECL1 at positions N25LS and N290KS and within mouse Necl1 at positions N23LS and N288KS, respectively.
18420026	4	58	gly	N-glycosylation	1088:1102	arg2	two putative N-glycosylation sites			two putative N-glycosylation sites						sites	Bioinformatics analysis showed there were two putative N-glycosylation sites within human NECL1 at positions N25LS and N290KS and within mouse Necl1 at positions N23LS and N288KS, respectively.
18420026	4	71	gly	positions	1185:1193	arg1	positions			positions						positions	Bioinformatics analysis showed there were two putative N-glycosylation sites within human NECL1 at positions N25LS and N290KS and within mouse Necl1 at positions N23LS and N288KS, respectively.
9334252	7	19	part_of	RNase	1156:1160	arg1	Trp-7	RNase 2		Trp-7		PUBTATOR	SpecificSite	RNase 2	6036	Trp-7	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
17286803	9	24	part_of	CLN3	1209:1212	arg1	cytoplasmic tails	CLN3		cytoplasmic tails		OGER	Site	CLN3	Q13286	tails	Alteration of the spacing between the transmembrane domain and the CAAX motif or the substitution of the entire C-terminal domain of CLN3 with cytoplasmic tails of mannose 6-phosphate receptors have demonstrated the importance of the C-terminal domain of proper length and composition for exit of the endoplasmic reticulum.
17286803	9	40	part_of	CLN3	1209:1212	arg1	the entire C-terminal domain	CLN3		the entire C-terminal domain		OGER	Site	CLN3	Q13286	domain	Alteration of the spacing between the transmembrane domain and the CAAX motif or the substitution of the entire C-terminal domain of CLN3 with cytoplasmic tails of mannose 6-phosphate receptors have demonstrated the importance of the C-terminal domain of proper length and composition for exit of the endoplasmic reticulum.
7774715	0	20	gly	isolated	49:56	arg2	recombinant human lactoferrin AND two N-linked glycans	recombinant human lactoferrin			two N-linked glycans	OGER		lactoferrin	P02788		Structural determination of two N-linked glycans isolated from recombinant human lactoferrin expressed in BHK cells.
1457969	0	47	gly	glycosylation	53:65	arg2	individual glycosylation sites			individual glycosylation sites						sites	The asparagine-linked oligosaccharides at individual glycosylation sites in human thyrotrophin.
20427278	5	15	gly	O-glycosylation	678:692	arg1	APP	APP				OGER		APP	P05067		TMEM59 transfection inhibited complex N- and O-glycosylation of APP in cultured cells.
16263699	2	3	gly	glycoprotein	304:315	arg1	glycoprotein VI	glycoprotein VI				Fterm		glycoprotein			They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
21573946	1	14	gly	N-glycosylated	229:242	arg1	EC-SOD	EC-SOD				PUBTATOR		EC-SOD	20657		Extracellular superoxide dismutase (EC-SOD), the major SOD isoenzyme in biological fluids, is known to be N-glycosylated and heterogeneous as was detected in most glycoproteins.
21573946	1	14	gly	N-glycosylated	229:242	arg1	Extracellular superoxide dismutase	Extracellular superoxide dismutase				PUBTATOR		Extracellular superoxide dismutase	20657		Extracellular superoxide dismutase (EC-SOD), the major SOD isoenzyme in biological fluids, is known to be N-glycosylated and heterogeneous as was detected in most glycoproteins.
21573946	1	14	gly	N-glycosylated	229:242	arg1	the major SOD isoenzyme	the major SOD isoenzyme				PUBTATOR		SOD isoenzyme	6649		Extracellular superoxide dismutase (EC-SOD), the major SOD isoenzyme in biological fluids, is known to be N-glycosylated and heterogeneous as was detected in most glycoproteins.
21573946	1	58	gly	glycoproteins	286:298	arg1	most glycoproteins	most glycoproteins				Fterm		glycoproteins			Extracellular superoxide dismutase (EC-SOD), the major SOD isoenzyme in biological fluids, is known to be N-glycosylated and heterogeneous as was detected in most glycoproteins.
18533687	8	5	gly	utilized	1341:1348	arg2	the potential N-glycosylation sites			the potential N-glycosylation sites						sites	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	8	9	gly	N-glycosylation	1305:1319	arg1	RXFP1	RXFP1		sites		PUBTATOR		RXFP1	59350	sites	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
8323280	9	35	part_of	rhLT	1949:1952	arg1	the lectin-like domain	rhLT		the lectin-like domain		Cterm	Site	rhLT		domain	These results indicate that the lectin-like domain of rhLT is exposed on its desialylation.
18642129	12	16	part_of	position	1702:1709	arg1	the light chain	chain		position		OGER	SpecificSite	chain	P08709	position Ser(60) and Ser(52)	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
7642555	6	17	gly	s	607:607	arg1	c-Myc	c-Myc			s	PUBTATOR		c-Myc	4609		In this paper, we identified the O-GlcNAc attachment site(s) on c-Myc.
24279413	4	57	gly	attached	819:826	arg1	their glycosylation sites AND N-linked glycans			their glycosylation sites	N-linked glycans					sites	This paper introduces a computational framework for identifying intact N-linked glycopeptides, i.e. glycopeptides with N-linked glycans attached to their glycosylation sites, in complex proteome samples.
24279413	4	59	gly	glycopeptides	763:775	arg2	intact N-linked glycopeptides			intact N-linked glycopeptides						glycopeptides	This paper introduces a computational framework for identifying intact N-linked glycopeptides, i.e. glycopeptides with N-linked glycans attached to their glycosylation sites, in complex proteome samples.
24279413	4	63	gly	glycosylation	837:849	arg2	their glycosylation sites			their glycosylation sites						sites	This paper introduces a computational framework for identifying intact N-linked glycopeptides, i.e. glycopeptides with N-linked glycans attached to their glycosylation sites, in complex proteome samples.
24279413	4	13	gly	glycopeptides	783:795	arg2	glycopeptides			glycopeptides	N-linked glycans					glycopeptides	This paper introduces a computational framework for identifying intact N-linked glycopeptides, i.e. glycopeptides with N-linked glycans attached to their glycosylation sites, in complex proteome samples.
19159218	8	7	gly	N-glycosites	1363:1374	arg2	622 N-glycosites			622 N-glycosites						N-glycosites	Use of trypsin alone resulted in identification of 622 N-glycosites, while using pepsin and thermolysin resulted in identification of 317 additional N-glycosites.
19159218	8	16	gly	N-glycosites	1457:1468	arg2	317 additional N-glycosites			317 additional N-glycosites						N-glycosites	Use of trypsin alone resulted in identification of 622 N-glycosites, while using pepsin and thermolysin resulted in identification of 317 additional N-glycosites.
3427055	5	35	part_of	Gla	833:835	arg1	the gamma-carboxyglutamic acid (Gla) domain	Gla		the gamma-carboxyglutamic acid (Gla) domain		OGER	Site	Gla	P06280	domain	This region, although neither gamma-carboxylated nor homologous, resembles the gamma-carboxyglutamic acid (Gla) domain of vitamin K dependent proteins of the blood clotting system in charge density, size of negatively charged clusters, and linkage to the rest of the molecule by a cysteine-rich domain.
3427055	5	58	part_of	proteins	868:875	arg1	the gamma-carboxyglutamic acid (Gla) domain	proteins		the gamma-carboxyglutamic acid (Gla) domain		Fterm	Site	proteins		domain	This region, although neither gamma-carboxylated nor homologous, resembles the gamma-carboxyglutamic acid (Gla) domain of vitamin K dependent proteins of the blood clotting system in charge density, size of negatively charged clusters, and linkage to the rest of the molecule by a cysteine-rich domain.
16859706	0	19	part_of	TPST1	6:10	arg1	Human TPST1 transmembrane domain	TPST1		Human TPST1 transmembrane domain		PUBTATOR	Site	TPST1	8460	domain	Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment.
22678432	2	0	gly	glycopeptides	345:357	arg2	glycopeptides			glycopeptides						glycopeptides	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
16321355	6	9	gly	sialylated	1137:1146	arg1	a sialylated biantennary or triantennary oligosaccharide				a sialylated biantennary or triantennary oligosaccharide						Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	6	41	gly	N-glycosylation	1053:1067	arg2	the seven potential N-glycosylation sites			the seven potential N-glycosylation sites						sites	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	6	69	gly	four	1076:1079	arg1	Asn743			Asn119, Asn339, Asn378, and Asn743						Asn119, Asn339, Asn378, and Asn743	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	6	69	gly	four	1076:1079	arg1	Asn339			Asn119, Asn339, Asn378, and Asn743						Asn119, Asn339, Asn378, and Asn743	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	6	69	gly	four	1076:1079	arg1	Asn339			Asn119, Asn339, Asn378, and Asn743						Asn119, Asn339, Asn378, and Asn743	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
23592772	2	47	gly	glutamine	395:403	arg1	greatly increased glucose and glutamine uptake			glutamine	greatly increased glucose and glutamine uptake					glutamine	This necessitates greatly increased glucose and glutamine uptake, both of which enter the hexosamine biosynthetic pathway (HBP).
26467158	8	41	gly	sites	1359:1363	arg1	two N-glycosylation sites			two N-glycosylation sites						sites	Point mutations at two N-glycosylation sites (Asn(153) and Asn(223)) abolish the bisecting GlcNAc modification on BACE1.
26467158	8	43	gly	N-glycosylation	1343:1357	arg2	two N-glycosylation sites			two N-glycosylation sites						sites	Point mutations at two N-glycosylation sites (Asn(153) and Asn(223)) abolish the bisecting GlcNAc modification on BACE1.
26467158	8	76	gly	modification	1418:1429	arg1	BACE1	BACE1			modification	PUBTATOR		BACE1	23821		Point mutations at two N-glycosylation sites (Asn(153) and Asn(223)) abolish the bisecting GlcNAc modification on BACE1.
26467158	8	41	gly	sites	1359:1363	arg1	Asn(153)			Asn(153) and Asn(223)						Asn(153) and Asn(223)	Point mutations at two N-glycosylation sites (Asn(153) and Asn(223)) abolish the bisecting GlcNAc modification on BACE1.
26467158	8	43	gly	N-glycosylation	1343:1357	arg2	Asn(223)			Asn(153) and Asn(223)						Asn(153) and Asn(223)	Point mutations at two N-glycosylation sites (Asn(153) and Asn(223)) abolish the bisecting GlcNAc modification on BACE1.
18036614	4	22	part_of	NtMGAM	772:777	arg1	the NtMGAM active site	NtMGAM		the NtMGAM active site		Cterm	Site	NtMGAM	8972	site	Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings.
7044414	0	20	part_of	alpha-lactalbumin	27:43	arg1	Amino acid sequence	alpha-lactalbumin		Amino acid sequence		PUBTATOR	Site	alpha-lactalbumin	24528	sequence	Amino acid sequence of rat alpha-lactalbumin: a unique alpha-lactalbumin.
12731887	2	22	gly	glycosylation	365:377	arg1	this region			region						region	To investigate whether glycosylation at the serine/threonine clusters at this region is important in protein synthesis, we selected (27)TSST(30) and (60)SGTS(63) clusters for further analysis.
28514451	3	39	part_of	GCGR	606:609	arg1	the GCGR transmembrane domain	structure of the GCGR		the GCGR transmembrane domain		PUBTATOR	Site	structure of the GCGR	2642	domain	The two domains are connected by a 12-residue segment termed the stalk, which adopts a β-strand conformation, instead of forming an α-helix as observed in the previously solved structure of the GCGR transmembrane domain.
9574531	0	43	gly	glycosylation	6:18	arg1	HLA-DRalpha	HLA-DRalpha				OGER		HLA			Novel glycosylation of HLA-DRalpha disrupts antigen presentation without altering endosomal localization.
8962717	0	18	part_of	receptor	98:105	arg1	the extracellular domain	epidermal growth factor receptor		the extracellular domain		PUBTATOR	Site	epidermal growth factor receptor	P00533	domain	Analysis of the glycosylation patterns of the extracellular domain of the epidermal growth factor receptor expressed in Chinese hamster ovary fibroblasts.
18930737	11	24	part_of	PIP	1489:1491	arg1	alpha1-alpha2 domains	PIP		alpha1-alpha2 domains		PUBTATOR	Site	PIP	5304	domains	On the perpendicular interface involving alpha1-alpha2 domains of ZAG and a loop of PIP, another salt bridge is formed.
18930737	11	76	part_of	ZAG	1471:1473	arg1	alpha1-alpha2 domains	ZAG		alpha1-alpha2 domains		PUBTATOR	Site	ZAG	563	domains	On the perpendicular interface involving alpha1-alpha2 domains of ZAG and a loop of PIP, another salt bridge is formed.
12421832	3	49	part_of	basic	520:524	arg1	pro-MBP	eosinophil major basic protein		pro-MBP		PUBTATOR	AminoAcid	eosinophil major basic protein	5553	pro	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	3	52	part_of	eosinophil	503:512	arg1	pro-MBP	eosinophil major basic protein		pro-MBP		PUBTATOR	AminoAcid	eosinophil major basic protein	5553	pro	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	3	104	part_of	major	514:518	arg1	pro-MBP	eosinophil major basic protein		pro-MBP		PUBTATOR	AminoAcid	eosinophil major basic protein	5553	pro	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
22333914	0	20	part_of	novel	2:6	arg1	A novel evolutionarily conserved domain	l		A novel evolutionarily conserved domain		PUBTATOR	Site	l	23218	domain	A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis.
22333914	0	29	part_of	conserved	23:31	arg1	A novel evolutionarily conserved domain	d		A novel evolutionarily conserved domain		PUBTATOR	Site	d	23218	domain	A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis.
19159218	4	11	gly	N-glycosites	814:825	arg2	N-glycosites			N-glycosites						N-glycosites	And the quite big size of glycan groups may block trypsin to access the K, R residues near N-glycosites for digestion, which will result in generation of big glycopeptides.
19159218	4	72	gly	glycopeptides	881:893	arg2	big glycopeptides			big glycopeptides						glycopeptides	And the quite big size of glycan groups may block trypsin to access the K, R residues near N-glycosites for digestion, which will result in generation of big glycopeptides.
21569239	4	55	part_of	F-spondin	629:637	arg1	human F-spondin FS domain	F-spondin		human F-spondin FS domain		PUBTATOR	Site	F-spondin	10418	domain	RESULTS: We present the crystal structure of human F-spondin FS domain at 1.95Å resolution.
19692335	7	25	part_of	disintegrin	1579:1589	arg1	the disintegrin domain	disintegrin		the disintegrin domain		Fterm	Site	disintegrin		domain	The structure, combined with calorimetric experiments, suggests distinct roles of three putative calcium ions bound to ADAM22, with one in the metalloproteinase-like domain being regulatory and two in the disintegrin domain being structural.
19692335	7	37	part_of	metalloproteinase-like	1517:1538	arg1	the metalloproteinase-like domain	metalloproteinase		the metalloproteinase-like domain		Fterm	Site	metalloproteinase		domain	The structure, combined with calorimetric experiments, suggests distinct roles of three putative calcium ions bound to ADAM22, with one in the metalloproteinase-like domain being regulatory and two in the disintegrin domain being structural.
2668275	4	57	gly	utilized	458:465	arg2	the N-glycosylation sites			the N-glycosylation sites						sites	Two of the N-glycosylation sites are utilized and were localized to the asparagine residues 47 and 259.
2668275	4	69	gly	N-glycosylation	432:446	arg2	the N-glycosylation sites			the N-glycosylation sites						sites	Two of the N-glycosylation sites are utilized and were localized to the asparagine residues 47 and 259.
2668275	4	54	gly	residues	504:511	arg1	47			asparagine residues 47 and 259						asparagine residues 47 and 259	Two of the N-glycosylation sites are utilized and were localized to the asparagine residues 47 and 259.
3935432	0	67	gly	interleukin-2	55:67	arg1	the major carbohydrates	interleukin-2			the major carbohydrates	PUBTATOR		interleukin-2	3558		Structures of the major carbohydrates of natural human interleukin-2.
20378933	9	20	gly	N58	1411:1413	arg1	desialylation			N58	desialylation					N58	Furthermore, increased IgA binding was also observed on desialylated FcalphaR after neuraminidase treatment and desialylation of N58 contributed most to the increased IgA binding.
20378933	9	69	gly	desialylation	1394:1406	arg1	N58	IgA		N58		OGER		IgA	P11912	N58	Furthermore, increased IgA binding was also observed on desialylated FcalphaR after neuraminidase treatment and desialylation of N58 contributed most to the increased IgA binding.
6587378	0	1	gly	2-glycoprotein	50:63	arg1	human plasma beta 2-glycoprotein I	human plasma beta 2-glycoprotein I				OGER		beta 2-glycoprotein I	P02749		Complete amino acid sequence of human plasma beta 2-glycoprotein I.
24085305	11	61	gly	glycosylated	1774:1785	arg1	optimally glycosylated LILRA3	optimally glycosylated LILRA3				PUBTATOR		LILRA3	11026		Binding to monocytes was partially blocked by β-lactose, indicating that optimally glycosylated LILRA3 might be critical for ligand binding and function.
16474139	12	31	gly	glycosylated	2100:2111	arg1	the SARS-CoV M protein	the SARS-CoV M protein				OGER		M protein	P54296		Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.
16474139	12	78	gly	O-glycosylated	1985:1998	arg1	the SARS-CoV 3a protein	the SARS-CoV 3a protein				Fterm		protein			Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.
16474139	12	78	gly	O-glycosylated	1985:1998	arg1	an O-glycosylated glycoprotein	an O-glycosylated glycoprotein				Fterm		glycoprotein			Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.
16474139	12	83	gly	glycoprotein	2000:2011	arg1	the SARS-CoV 3a protein	the SARS-CoV 3a protein				Fterm		protein			Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.
16474139	12	83	gly	glycoprotein	2000:2011	arg1	an O-glycosylated glycoprotein	an O-glycosylated glycoprotein				Fterm		glycoprotein			Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.
17989695	3	27	part_of	Nrp2	541:544	arg1	Nrp2 fragments	Nrp2		Nrp2 fragments		PUBTATOR	Site	Nrp2	8828	fragments	We report several crystal structures of Nrp1 and Nrp2 fragments alone and in complex with antibodies that selectively block either semaphorin or vascular endothelial growth factor (VEGF) binding.
1820200	3	15	gly	N-glycosylation	1816:1830	arg2	individual N-glycosylation sites	hCG		sites		PUBTATOR		hCG	93659	sites	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
22576872	7	13	gly	Tyr10	1315:1319	arg1	O-glycans			Tyr10	O-glycans					Tyr10	Further, sialylated core 1 like O-glycans at Tyr10, recently discovered in human Aβ (a previously unknown glycosylation type), were identified also in cat cerebrospinal fluid (CSF).
22576872	7	51	gly	sialylated	1279:1288	arg1	sialylated core 1				sialylated core 1						Further, sialylated core 1 like O-glycans at Tyr10, recently discovered in human Aβ (a previously unknown glycosylation type), were identified also in cat cerebrospinal fluid (CSF).
22226965	4	7	part_of	PPARγ	641:645	arg1	the threonine 54 of the N-terminal AF-1 domain	PPARγ 		the threonine 54 of the N-terminal AF-1 domain		PUBTATOR	Site	PPARγ 	19016	domain	Mass spectrometric analysis and mutant studies revealed that the threonine 54 of the N-terminal AF-1 domain of PPARγ is the major O-GlcNAc site.
22226965	4	50	part_of	AF-1	626:629	arg1	the threonine 54 of the N-terminal AF-1 domain	AF-1		the threonine 54 of the N-terminal AF-1 domain		OGER	Site	AF-1	P38484	domain	Mass spectrometric analysis and mutant studies revealed that the threonine 54 of the N-terminal AF-1 domain of PPARγ is the major O-GlcNAc site.
8349699	3	99	gly	Glycosylation	349:361	arg1	PGH synthase-1	PGH synthase-1		Asn410		PUBTATOR		PGH synthase-1	19224	Asn410	Glycosylation of PGH synthase-1 at Asn410 and at either Asn68 or Asn144 was required for expression of both the cyclooxygenase and the peroxidase activities of the enzyme.
8349699	3	99	gly	Glycosylation	349:361	arg1	PGH synthase-1	PGH synthase-1		Asn144		PUBTATOR		PGH synthase-1	19224	Asn144	Glycosylation of PGH synthase-1 at Asn410 and at either Asn68 or Asn144 was required for expression of both the cyclooxygenase and the peroxidase activities of the enzyme.
8349699	3	99	gly	Glycosylation	349:361	arg2	Asn68	PGH synthase-1		Asn68		PUBTATOR		PGH synthase-1	19224	Asn68	Glycosylation of PGH synthase-1 at Asn410 and at either Asn68 or Asn144 was required for expression of both the cyclooxygenase and the peroxidase activities of the enzyme.
12768205	2	13	part_of	IgA1	369:372	arg1	the Fc region	IgA1 (Fcalpha)		the Fc region		PUBTATOR	Site	IgA1 (Fcalpha)	P01876	region	Here we present crystal structures of human FcalphaRI alone and in a complex with the Fc region of IgA1 (Fcalpha).
22660477	7	23	part_of	subunits	868:875	arg1	GBR1 residues	subunits		GBR1 residues		Fterm	Site	subunits		residues	We also identify specific heterodimer contacts from both subunits, and GBR1 residues involved in ligand recognition.
2793860	8	18	gly	O-glycosylated	1279:1292	arg1	O-glycosylated human IL-2	O-glycosylated human IL-2				PUBTATOR		IL-2	P60568		Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
7774715	6	38	gly	glycoprotein	787:798	arg1	the recombinant glycoprotein	the recombinant glycoprotein				Fterm		glycoprotein			In regard to its glycan moiety, the recombinant glycoprotein is close to native lactoferrins from milk or leucocytes but shows specific structural features which should be taken into account prior to in vivo and in vitro biological studies.
16201406	4	2	gly	found	819:823	arg2	natural hLF AND complex-type glycans	natural hLF			complex-type glycans	PUBTATOR		hLF	3131		Even though rhLF contains oligomannose- and hybrid-type N-linked glycans next to complex-type glycans, which are the only glycans found on natural hLF, the structures are identical within the experimental error (r.m.s. deviation of only 0.28 A for the main-chain atoms).
16201406	4	2	gly	found	819:823	arg2	natural hLF AND the only glycans	natural hLF			the only glycans	PUBTATOR		hLF	3131		Even though rhLF contains oligomannose- and hybrid-type N-linked glycans next to complex-type glycans, which are the only glycans found on natural hLF, the structures are identical within the experimental error (r.m.s. deviation of only 0.28 A for the main-chain atoms).
16201406	4	19	gly	contains	706:713	arg1	rhLF AND oligomannose- and hybrid-type N-linked glycans	rhLF			oligomannose- and hybrid-type N-linked glycans	OGER		rhLF	P02788		Even though rhLF contains oligomannose- and hybrid-type N-linked glycans next to complex-type glycans, which are the only glycans found on natural hLF, the structures are identical within the experimental error (r.m.s. deviation of only 0.28 A for the main-chain atoms).
17139081	0	41	gly	glycosylated	37:48	arg1	the defective enzyme	the defective enzyme				Fterm		enzyme			Structural comparison of differently glycosylated forms of acid-beta-glucosidase, the defective enzyme in Gaucher disease.
17139081	0	41	gly	glycosylated	37:48	arg1	acid-beta-glucosidase	acid-beta-glucosidase				PUBTATOR		acid-beta-glucosidase	2629		Structural comparison of differently glycosylated forms of acid-beta-glucosidase, the defective enzyme in Gaucher disease.
19556306	0	61	part_of	receptor	44:51	arg1	Cys(88)	Toll-like receptor 4		Cys(88)		PUBTATOR	SpecificSite	Toll-like receptor 4	7099	Cys(88)	Mutational analysis of Cys(88) of Toll-like receptor 4 highlights the critical role of MD-2 in cell surface receptor expression.
11788899	4	64	part_of	WNT8B	465:469	arg1	a 351-amino-acid polypeptide	WNT8B		a 351-amino-acid polypeptide		PUBTATOR	Site	WNT8B	7479	polypeptide	WNT8B gene of about 23-kb in size consisted of six exons, and encoded a 351-amino-acid polypeptide with the N-terminal signal peptide and two N-linked glycosylation sites.
11788899	4	86	part_of	351-amino-acid	537:550	arg1	a 351-amino-acid polypeptide	351-amino-acid		a 351-amino-acid polypeptide		Cterm	Site	351-amino-acid		polypeptide	WNT8B gene of about 23-kb in size consisted of six exons, and encoded a 351-amino-acid polypeptide with the N-terminal signal peptide and two N-linked glycosylation sites.
11258925	10	6	gly	non-glycosylated	1587:1602	arg1	a non-glycosylated tryptic peptide			a non-glycosylated tryptic peptide						peptide	Finally, a non-glycosylated tryptic peptide was observed containing the Asn 592.
11741940	1	101	part_of	contains	239:246	arg1	Secreted Frizzled-related protein-1 AND an N-terminal domain	Secreted Frizzled-related protein-1		domain		PUBTATOR	Site	Secreted Frizzled-related protein-1	6422	domain	Secreted Frizzled-related protein-1 (sFRP-1), a soluble protein that binds to Wnts and modulates Wnt signaling, contains an N-terminal domain homologous to the putative Wnt-binding site of Frizzled (Fz domain) and a C-terminal heparin-binding domain with weak homology to netrin.
11741940	1	101	part_of	contains	239:246	arg1	a soluble protein AND an N-terminal domain	protein		domain		Fterm	Site	protein		domain	Secreted Frizzled-related protein-1 (sFRP-1), a soluble protein that binds to Wnts and modulates Wnt signaling, contains an N-terminal domain homologous to the putative Wnt-binding site of Frizzled (Fz domain) and a C-terminal heparin-binding domain with weak homology to netrin.
11741940	1	101	part_of	contains	239:246	arg1	sFRP-1 AND an N-terminal domain	sFRP-1		domain		PUBTATOR	Site	sFRP-1	6422	domain	Secreted Frizzled-related protein-1 (sFRP-1), a soluble protein that binds to Wnts and modulates Wnt signaling, contains an N-terminal domain homologous to the putative Wnt-binding site of Frizzled (Fz domain) and a C-terminal heparin-binding domain with weak homology to netrin.
20622017	6	63	gly	observed	883:890	arg1	a single site AND Up to 15 different glycans			a single site	Up to 15 different glycans					site	Up to 15 different glycans were observed at a single site, with site-specific variation in glycan composition.
6776528	1	10	part_of	chain	145:149	arg1	The complete amino acid sequence	chain		The complete amino acid sequence		OGER	Site	chain		sequence	The complete amino acid sequence of the 432-residue heavy (alpha) chain of mouse myeloma MOPC 511 has been determined.
2141278	5	6	part_of	plasmin-cleavage	1348:1363	arg1	the other plasmin-cleavage fragments	plasmin		the other plasmin-cleavage fragments		Fterm	Site	plasmin		fragments	As measured by equilibrium dialysis, native alpha 2, like the other plasmin-cleavage fragments, did not retain the ability of intact C1-s to bind Ca2+.
19690161	7	29	part_of	vIL-6	1072:1076	arg1	the Asn-89 site	vIL		the Asn-89 site		OGER	SpecificSite	vIL	P09327	Asn-89 site	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
10764840	6	19	part_of	Epo-RPMI	979:986	arg1	the amino acid sequence	Epo		the amino acid sequence		PUBTATOR	Site	Epo	2056	sequence	As expected, the amino acid sequence of the Epo-RPMI conformed to that of uHuEpo.
22171320	12	70	gly	O-glycosylation	2083:2097	arg2	40 of 57 putative O-glycosylation sites			40 of 57 putative O-glycosylation sites						sites	The combination of CID and electron capture dissociation techniques allowed for the exact identification of Ser/Thr attachment site(s) for 40 of 57 putative O-glycosylation sites.
25456591	3	3	gly	O-glycopeptides	738:752	arg2	the corresponding intact O-glycopeptides			the corresponding intact O-glycopeptides						O-glycopeptides	From the same sample concurrently prepared without β-elimination, the corresponding intact O-glycopeptides were mapped by accurate precursor ion mass using an in-house glycan database majorly composed of GalNAc (mucin-type) core and the retention-time shift (ΔRt).
1281977	2	57	gly	glycopeptides	223:235	arg2	asparagine-linked glycopeptides			asparagine-linked glycopeptides						glycopeptides	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
22023369	0	13	gly	defucosylation	68:81	arg1	their Fc glycans				their Fc glycans						Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans.
7107587	9	25	part_of	fibrinogen	996:1005	arg1	fibrinogen glycopeptides	fibrinogen		fibrinogen glycopeptides		PUBTATOR	Site	fibrinogen	2244	glycopeptides	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
14769026	8	74	gly	N-glycosylation	1214:1228	arg2	The potential N-glycosylation sequons			The potential N-glycosylation sequons							The potential N-glycosylation sequons in NL1 at Asn 109, Asn 303, Asn 343, and Asn 547 are shown occupied by carbohydrate.
14769026	8	44	gly	occupied	1297:1304	arg2	Asn 547			Asn 109, Asn 303, Asn 343, and Asn 547						Asn 109, Asn 303, Asn 343, and Asn 547	The potential N-glycosylation sequons in NL1 at Asn 109, Asn 303, Asn 343, and Asn 547 are shown occupied by carbohydrate.
14769026	8	44	gly	occupied	1297:1304	arg2	Asn 109			Asn 109, Asn 303, Asn 343, and Asn 547						Asn 109, Asn 303, Asn 343, and Asn 547	The potential N-glycosylation sequons in NL1 at Asn 109, Asn 303, Asn 343, and Asn 547 are shown occupied by carbohydrate.
14769026	8	44	gly	occupied	1297:1304	arg2	Asn 343			Asn 109, Asn 303, Asn 343, and Asn 547						Asn 109, Asn 303, Asn 343, and Asn 547	The potential N-glycosylation sequons in NL1 at Asn 109, Asn 303, Asn 343, and Asn 547 are shown occupied by carbohydrate.
14769026	8	44	gly	occupied	1297:1304	arg2	Asn 109			Asn 109, Asn 303, Asn 343, and Asn 547						Asn 109, Asn 303, Asn 343, and Asn 547	The potential N-glycosylation sequons in NL1 at Asn 109, Asn 303, Asn 343, and Asn 547 are shown occupied by carbohydrate.
14769026	8	44	gly	occupied	1297:1304	arg2	Asn 343			Asn 109, Asn 303, Asn 343, and Asn 547						Asn 109, Asn 303, Asn 343, and Asn 547	The potential N-glycosylation sequons in NL1 at Asn 109, Asn 303, Asn 343, and Asn 547 are shown occupied by carbohydrate.
14769026	8	44	gly	occupied	1297:1304	arg2	Asn 343			Asn 109, Asn 303, Asn 343, and Asn 547						Asn 109, Asn 303, Asn 343, and Asn 547	The potential N-glycosylation sequons in NL1 at Asn 109, Asn 303, Asn 343, and Asn 547 are shown occupied by carbohydrate.
1482348	0	41	gly	O-glycosylated	38:51	arg1	O-glycosylated oligosaccharide				O-glycosylated oligosaccharide						Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on the alpha chain.
25700513	4	32	part_of	Delta/Serrate/Lag-2	455:473	arg1	DLL4 Delta/Serrate/Lag-2 (DSL) domain	Lag-2		DLL4 Delta/Serrate/Lag-2 (DSL) domain		OGER	Site	Lag-2	P22749	domain	Notch1 epidermal growth factor-like repeats 11 and 12 interact with the DLL4 Delta/Serrate/Lag-2 (DSL) domain and module at the N-terminus of Notch ligands (MNNL) domains, respectively.
25700513	4	35	part_of	DLL4	450:453	arg1	DLL4 Delta/Serrate/Lag-2 (DSL) domain	DLL4		DLL4 Delta/Serrate/Lag-2 (DSL) domain		OGER	Site	DLL4	Q9NR61	domain	Notch1 epidermal growth factor-like repeats 11 and 12 interact with the DLL4 Delta/Serrate/Lag-2 (DSL) domain and module at the N-terminus of Notch ligands (MNNL) domains, respectively.
25700513	4	37	part_of	DSL	476:478	arg1	DLL4 Delta/Serrate/Lag-2 (DSL) domain	DSL		DLL4 Delta/Serrate/Lag-2 (DSL) domain		Cterm	Site	DSL	P22749	domain	Notch1 epidermal growth factor-like repeats 11 and 12 interact with the DLL4 Delta/Serrate/Lag-2 (DSL) domain and module at the N-terminus of Notch ligands (MNNL) domains, respectively.
11390601	1	41	part_of	sites	360:364	arg1	its gp120 subunit	gp120 subunit		sites		PUBTATOR	Site	gp120 subunit	155971	sites	The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) is extensively glycosylated, containing approximately 23 asparagine (N)-linked glycosylation sites on its gp120 subunit.
8489250	2	34	part_of	Peptide	311:317	arg1	Peptide peptides	Peptide		Peptide peptides		OGER	Site	Peptide		peptides	Peptide peptides containing six potential N-glycosylation sites were analyzed to determine that Asn residues 9, 34, 63, 73, 96, and 116 were utilized.
8489250	2	4	part_of	containing	328:337	arg1	Peptide peptides AND six potential N-glycosylation sites	Peptide peptides		six potential N-glycosylation sites						sites	Peptide peptides containing six potential N-glycosylation sites were analyzed to determine that Asn residues 9, 34, 63, 73, 96, and 116 were utilized.
24530628	8	8	gly	glycopeptides	1300:1312	arg2	glycopeptides			glycopeptides						glycopeptides	Our enrichment method is capable of isolating glycopeptides from complex peptide mixtures such as crude serum.
21606496	4	38	part_of	2B4	509:511	arg1	the extracellular domain	2B4		the extracellular domain		PUBTATOR	Site	2B4	51744	domain	Using a recombinant fusion protein of the extracellular domain of 2B4, we demonstrate that N-linked glycosylation of 2B4 is essential for the binding to its ligand CD48.
21768335	4	23	gly	glycosylated	676:687	arg1	a glycosylated Fcγ receptor	a glycosylated Fcγ receptor				Cterm		Fcγ			In this study, the crystal structures of a glycosylated Fcγ receptor complexed with either afucosylated or fucosylated Fc were determined allowing a detailed, molecular understanding of the regulatory role of Fc-oligosaccharide core fucosylation in improving ADCC.
12151713	2	22	part_of	lactoferrin	269:279	arg1	The human lactoferrin coding sequence	lactoferrin		The human lactoferrin coding sequence		OGER	Site	lactoferrin	P02788	sequence	The human lactoferrin coding sequence was inserted into the pUC18 plasmid under control of the wheat glutenin promoter.
2275556	4	5	part_of	cathepsin	847:855	arg1	cathepsin L mRNA sequences	cathepsin L mRNA		cathepsin L mRNA sequences		PUBTATOR	Site	cathepsin L mRNA	13039	sequences	Although cathepsin L message levels were elevated 20-fold in the transformed fibroblasts, normal and transformed cells displayed similar cathepsin L genomic DNA digest patterns and gene copy numbers, and cathepsin L mRNA sequences appeared identical by RNase protection analysis.
2275556	4	24	part_of	mRNA	859:862	arg1	cathepsin L mRNA sequences	cathepsin L mRNA		cathepsin L mRNA sequences		PUBTATOR	Site	cathepsin L mRNA	13039	sequences	Although cathepsin L message levels were elevated 20-fold in the transformed fibroblasts, normal and transformed cells displayed similar cathepsin L genomic DNA digest patterns and gene copy numbers, and cathepsin L mRNA sequences appeared identical by RNase protection analysis.
2275556	4	99	part_of	L	857:857	arg1	cathepsin L mRNA sequences	cathepsin L mRNA		cathepsin L mRNA sequences		PUBTATOR	Site	cathepsin L mRNA	13039	sequences	Although cathepsin L message levels were elevated 20-fold in the transformed fibroblasts, normal and transformed cells displayed similar cathepsin L genomic DNA digest patterns and gene copy numbers, and cathepsin L mRNA sequences appeared identical by RNase protection analysis.
15003450	6	35	gly	glycoproteins	854:866	arg1	glycoproteins	glycoproteins			galactose	Fterm		glycoproteins			To understand how the enzyme cleaves galactose from glycoproteins and glycolipids, we also determined the structure of the complex of alpha-GAL with its catalytic product.
12927778	0	57	gly	glycoprotein	71:82	arg1	an oligomannosidic glycoprotein	an oligomannosidic glycoprotein				Fterm		glycoprotein			Characterization of nucleotide pyrophosphatase-5 as an oligomannosidic glycoprotein in rat brain.
9023546	0	33	part_of	EGF	109:111	arg1	EGF domains	EGF		EGF domains		OGER	Site	EGF	P01133	domains	Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains.
19196183	10	9	gly	glycoproteins	1381:1393	arg1	the glycoproteins	the glycoproteins				Fterm		glycoproteins			Among the glycoproteins identified, alpha-fetoprotein, CD44 and laminin have been reported to be implicated in HCC and its metastasis.
11371615	6	14	part_of	Sp1	901:903	arg1	the second activation domain	Sp1		the second activation domain		OGER	Site	Sp1	Q8N907	domain	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	25	part_of	Sp1	1071:1073	arg1	Sp1 activation domain	Sp1		Sp1 activation domain		OGER	Site	Sp1	Q8N907	domain	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
8636209	9	31	part_of	gamma	1147:1151	arg1	the TM domain	CD3 gamma		the TM domain		PUBTATOR	Site	CD3 gamma	917	domain	Site-directed mutagenesis of the acidic amino acid in the TM domain of CD3 gamma demonstrated that this residue is involved in TCR assembly probably by binding to Ti beta.
3877053	9	109	part_of	region	1355:1360	arg1	factor XII	factor XII		region		OGER	Site	factor XII	P00748	region	As the type II region of fibronectin contains a collagen-binding site, the homologous region in factor XII may be responsible for the binding of factor XII to collagen.
3877053	9	110	part_of	fibronectin	1294:1304	arg1	the type II region	fibronectin		the type II region		PUBTATOR	Site	fibronectin	2335	region	As the type II region of fibronectin contains a collagen-binding site, the homologous region in factor XII may be responsible for the binding of factor XII to collagen.
3877053	9	72	part_of	contains	1306:1313	arg1	the type II region AND a collagen-binding site	the type II region		a collagen-binding site						site	As the type II region of fibronectin contains a collagen-binding site, the homologous region in factor XII may be responsible for the binding of factor XII to collagen.
20959806	3	24	gly	serine112	516:524	arg1	O-GlcNAc			serine112	O-GlcNAc					serine112	We show that by suppressing O-phosphorylation-mediated degradation, O-GlcNAc at serine112 stabilizes Snail1 and thus increases its repressor function, which in turn attenuates E-cadherin mRNA expression.
8193552	1	11	gly	N-deglycosylated	297:312	arg1	the enzymically N-deglycosylated beta-subunit	the enzymically N-deglycosylated beta-subunit				OGER		subunit	P0DN86		The disialylated poly-(N-acetyllactosamine)-containing O-linked oligosaccharide alditols, released by alkaline borohydride treatment of the enzymically N-deglycosylated beta-subunit of equine chorionic gonadotropin, were purified by fast protein liquid chromatography (FPLC) on Mono Q and analysed by fast ion bombardment mass spectrometry (FAB-MS) and 1H-NMR spectroscopy.
8193552	1	24	gly	disialylated	149:160	arg1	The disialylated poly-(N-acetyllactosamine)-containing O-linked oligosaccharide alditols				The disialylated poly-(N-acetyllactosamine)-containing O-linked oligosaccharide alditols						The disialylated poly-(N-acetyllactosamine)-containing O-linked oligosaccharide alditols, released by alkaline borohydride treatment of the enzymically N-deglycosylated beta-subunit of equine chorionic gonadotropin, were purified by fast protein liquid chromatography (FPLC) on Mono Q and analysed by fast ion bombardment mass spectrometry (FAB-MS) and 1H-NMR spectroscopy.
22848655	8	6	part_of	Sema	1139:1142	arg1	RON Sema domain	RON Sema		RON Sema domain		OGER	Site	RON Sema	Q04912	domain	RON Sema domain adopts a seven-bladed β-propeller fold, followed by disulfide bond rich, cysteine-knot PSI motif.
22848655	8	61	part_of	RON	1135:1137	arg1	RON Sema domain	RON Sema		RON Sema domain		OGER	Site	RON Sema	Q04912	domain	RON Sema domain adopts a seven-bladed β-propeller fold, followed by disulfide bond rich, cysteine-knot PSI motif.
22902367	1	5	gly	glycoproteins	107:119	arg1	immunoglobulin superfamily glycoproteins	immunoglobulin superfamily glycoproteins				Fterm		glycoproteins			Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues.
23234360	6	4	gly	glycoproteins	1237:1249	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	6	20	gly	glycans	1202:1208	arg1	glycoproteins	glycoproteins			glycans	Fterm		glycoproteins			The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	6	43	gly	glycosylation	1214:1226	arg2	glycosylation sites			glycosylation sites						sites	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
8130392	7	6	gly	Asn-linked	986:995	arg1	The Asn-linked oligosaccharides			Asn	The Asn-linked oligosaccharides					Asn	The Asn-linked oligosaccharides of rHPC were released by N-glycanase and separated into 25 fractions by high-pH anion-exchange chromatography.
8130392	7	58	gly	rHPC	1017:1020	arg1	The Asn-linked oligosaccharides	rHPC			The Asn-linked oligosaccharides	OGER		rHPC	P52873		The Asn-linked oligosaccharides of rHPC were released by N-glycanase and separated into 25 fractions by high-pH anion-exchange chromatography.
8390218	2	91	gly	residue	717:723	arg1	a fucose residue			a fucose residue	a fucose residue		AminoAcid			residue at	We found that the LCA-reactive species of AAT from patients with HCC carried both the biantennary sugar chain with a fucose residue at the innermost N-acetylglucosamine residue, Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc-PA, and the biantennary chain without a fucose residue, Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4GlcNAc-PA, at a ratio of about 1:0.6.
6776528	2	51	part_of	chain	231:235	arg1	The variable region	chain		The variable region		OGER	Site	chain	P11912	region	The variable region of the alpha chain of IgA 511, a phosphocholine-binding protein, is highly homologous to that of the other phosphocholine-binding immunoglobulins.
27922006	1	1	gly	glycoprotein	94:105	arg1	Myelin-associated glycoprotein	Myelin-associated glycoprotein				PUBTATOR		Myelin-associated glycoprotein	4099		Myelin-associated glycoprotein (MAG) is a myelin-expressed cell-adhesion and bi-directional signalling molecule.
27922006	1	1	gly	glycoprotein	94:105	arg1	MAG	MAG				PUBTATOR		MAG	4099		Myelin-associated glycoprotein (MAG) is a myelin-expressed cell-adhesion and bi-directional signalling molecule.
29671580	4	11	gly	modified	830:837	arg1	glycosites AND triantennary sialylated N-glycans			glycosites	triantennary sialylated N-glycans					glycosites	Specifically, 3/4 of glycosites were modified by biantennary N-glycans and 1/3 of glycosites were modified by triantennary sialylated N-glycans.
29671580	4	14	gly	glycosites	814:823	arg2	glycosites			glycosites						glycosites	Specifically, 3/4 of glycosites were modified by biantennary N-glycans and 1/3 of glycosites were modified by triantennary sialylated N-glycans.
29671580	4	34	gly	sialylated	855:864	arg1	triantennary sialylated N-glycans				triantennary sialylated N-glycans						Specifically, 3/4 of glycosites were modified by biantennary N-glycans and 1/3 of glycosites were modified by triantennary sialylated N-glycans.
29671580	4	45	gly	glycosites	753:762	arg2	glycosites			glycosites						glycosites	Specifically, 3/4 of glycosites were modified by biantennary N-glycans and 1/3 of glycosites were modified by triantennary sialylated N-glycans.
29671580	4	50	gly	modified	769:776	arg1	glycosites AND biantennary N-glycans			glycosites	biantennary N-glycans					glycosites	Specifically, 3/4 of glycosites were modified by biantennary N-glycans and 1/3 of glycosites were modified by triantennary sialylated N-glycans.
16754968	2	0	part_of	region	544:549	arg1	position	region		position						position	A minor improvement in resolution has resulted in improved electron-density maps, which have given a clearer indication of the position and stabilization of the key residues Tyr15, Phe79, Tyr347, His349, Ile350 and Tyr403 in the elbow region between domain 1 and domain 4 of the dimer-related molecule.
25265424	0	64	gly	glycoproteins	63:75	arg1	liver-secreted glycoproteins	liver-secreted glycoproteins				Fterm		glycoproteins			Protein and site specificity of fucosylation in liver-secreted glycoproteins.
11733580	0	13	part_of	receptor	87:94	arg1	the NH2-terminal domain	CC chemokine receptor 5		the NH2-terminal domain		PUBTATOR	Site	CC chemokine receptor 5	1234	domain	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	0	27	part_of	tyrosines	34:42	arg1	CC chemokine receptor 5	CC chemokine receptor 5		tyrosines		PUBTATOR	AminoAcid	CC chemokine receptor 5	1234	tyrosines	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
10386995	4	1	gly	sites	727:731	arg1	synapsin I	synapsin I			sites	PUBTATOR		synapsin I	24949		The seven O-GlcNAcylation sites (Ser55, Thr56, Thr87, Ser516, Thr524, Thr562, and Ser576) in synapsin I are clustered around its five phosphorylation sites in domains B and D.
18036614	5	23	gly	contains	1016:1023	arg1	the NtMGAM active site AND two primary sugar subsites			the NtMGAM active site	two primary sugar subsites					site	These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship.
21053369	2	84	gly	glycosylated	326:337	arg1	a heterodimeric receptor	a heterodimeric receptor				Fterm		receptor			It signals through a heterodimeric receptor consisting of IL-23r, which is heavily glycosylated.
14693913	10	32	gly	glycoproteins	2022:2034	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			This is the first report of the synthesis of beta-Man- and phosphate-containing O-linked constituents on glycoproteins synthesized by P. pastoris.
16445295	5	14	gly	utilized	827:834	arg2	all five potential N-glycosylation sites			all five potential N-glycosylation sites						sites	The analyses revealed that all five potential N-glycosylation sites were utilized including Asn22, Asn51, Asn63, Asn86 (located in the activation peptide), and Asn219 (located in the catalytic domain).
16445295	5	56	gly	N-glycosylation	800:814	arg2	all five potential N-glycosylation sites			all five potential N-glycosylation sites						sites	The analyses revealed that all five potential N-glycosylation sites were utilized including Asn22, Asn51, Asn63, Asn86 (located in the activation peptide), and Asn219 (located in the catalytic domain).
21752865	5	65	gly	N-glycosylated	1011:1024	arg1	BRI2	BRI2				PUBTATOR		BRI2	9445		Given that N-glycosylation is considered essential for protein folding, processing and trafficking, we examined whether BRI2 is N-glycosylated.
6320120	3	54	gly	used	438:441	arg2	inserted fragments			inserted fragments						fragments	Purified inserted fragments were used as a hybridisation probe against chromosomal "Southern blots" to show that at least twelve rat IFN-alpha-related sequences are present in the genome.
1456441	9	23	gly	N-glycosylation	1336:1350	arg2	the two N-glycosylation sites	h-STF		sites		Cterm		h-STF	7018	sites	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	9	71	gly	h-STF	1361:1365	arg1	Asn611			Asn413 and Asn611						Asn413 and Asn611	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
26598643	3	79	gly	glycoproteins	445:457	arg1	many human blood plasma glycoproteins	many human blood plasma glycoproteins				Fterm		glycoproteins			In consequence, despite their clinical and biopharmaceutical importance, many human blood plasma glycoproteins have not been characterized comprehensively with respect to their O-glycosylation.
26783088	4	61	part_of	SMPDL3a	622:628	arg1	the binuclear site	SMPDL3a		the binuclear site		PUBTATOR	Site	SMPDL3a	10924	site	We show that the binuclear site of SMPDL3a is occupied by two Zn(2+) ions and that excess Zn(2+) leads to inhibition of enzyme activity through binding to additional sites.
19358553	4	30	gly	sialoglycopeptides	1028:1045	arg1	fetuin	fetuin		sialoglycopeptides		Fterm		fetuin		sialoglycopeptides	Similarly, precise quantitation was observed for various forms of N-glycans (free, permethylated, and fluorescence-labeled) using MS. In addition, three different sialoglycopeptides from fetuin were site-specifically profiled, and good correlation between peak intensities and relative abundances was found with only a minor loss of sialic acids (r = 0.9664, n = 5).
2209609	9	66	gly	glycosylation	1521:1533	arg2	each glycosylation site			each glycosylation site						site	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	9	75	gly	released	1502:1509	arg1	each glycosylation site AND oligosaccharide structures			each glycosylation site	oligosaccharide structures					site	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
11683872	3	23	gly	glycosylated	528:539	arg1	VR1	VR1				PUBTATOR		VR1	7442		VR1 was found to be glycosylated in both cell types.
8286855	2	8	part_of	site	556:559	arg1	GpA	GpA		site		PUBTATOR	Site	GpA	2993	site	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	15	part_of	sites	319:323	arg1	GpA	GpA		sites		PUBTATOR	Site	GpA	2993	sites	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	19	part_of	GpA	375:377	arg1	the extracellular domain	GpA		the extracellular domain		PUBTATOR	Site	GpA	2993	domain	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
23242014	10	16	gly	glycosylated	1509:1520	arg1	Thr385			Thr385						Thr385	Based on our data, Thr385 is probably glycosylated as well.
10929010	3	13	gly	transferrin	528:538	arg1	the N-glycan structures	transferrin			the N-glycan structures	PUBTATOR		transferrin	7018		Consequently, the N-glycan structures of transferrin in the culture medium were determined using three-dimensional high performance liquid chromatography.
7599134	5	57	part_of	ATIII	868:872	arg1	the ATIII N-glycosylation sites	ATIII		the ATIII N-glycosylation sites		PUBTATOR	Site	ATIII	462	sites	Consensus sequences (CSs) of the ATIII N-glycosylation sites are N-X-S for 135 and N-X-T for 96, 155, and 192.
15807535	0	41	gly	glycosylation	9:21	arg1	the human ABC transporter ABCG2	ABCG2		asparagine 596		PUBTATOR		ABCG2	9429	asparagine 596	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	0	73	gly	glycosylation	9:21	arg1	asparagine 596			asparagine 596						asparagine 596	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	0	73	gly	glycosylation	9:21	arg1	asparagine 596	ABCG2		asparagine 596		PUBTATOR		ABCG2	9429	asparagine 596	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
11258925	3	28	gly	glycosylation	348:360	arg2	the glycosylation site analysis	COX-2		site		PUBTATOR		COX-2	4513	site	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
12122212	7	38	gly	glycosylation	1154:1166	arg1	CD21	CD21				PUBTATOR		CD21	1380		We present evidence that the V-shaped conformation is induced by deglycosylation of the protein, and that physiologic glycosylation of CD21 would result in a more extended conformation, perhaps with additional epitopes for C3d binding.
12122212	7	52	gly	deglycosylation	1101:1115	arg1	the protein	the protein				Fterm		protein			We present evidence that the V-shaped conformation is induced by deglycosylation of the protein, and that physiologic glycosylation of CD21 would result in a more extended conformation, perhaps with additional epitopes for C3d binding.
16014566	0	77	gly	glycoprotein	68:79	arg1	platelet glycoprotein VI	platelet glycoprotein VI				PUBTATOR		platelet glycoprotein VI	51206		The influence of N-linked glycosylation on the function of platelet glycoprotein VI.
16014566	0	93	gly	glycosylation	26:38	arg1	platelet glycoprotein VI	platelet glycoprotein VI				PUBTATOR		platelet glycoprotein VI	51206		The influence of N-linked glycosylation on the function of platelet glycoprotein VI.
30392906	8	9	gly	glycosylation	960:972	arg1	Asn50			Asn50						Asn50	Our results demonstrate that glycosylation of Asn50 is essential for its function as a receptor of ConA.
12408961	1	25	gly	glycoprotein	206:217	arg1	a secreted glycoprotein	a secreted glycoprotein				Fterm		glycoprotein			The cellular repressor of E1A-stimulated genes, CREG, is a secreted glycoprotein that enhances differentiation of pluripotent stem cells.
7505568	0	6	gly	glycoprotein	70:81	arg1	human myelin-associated glycoprotein	human myelin-associated glycoprotein				PUBTATOR		myelin-associated glycoprotein	4099		Identification of the glycosylated sequons of human myelin-associated glycoprotein.
7505568	0	15	gly	glycosylated	22:33	arg1	the glycosylated sequons			the glycosylated sequons							Identification of the glycosylated sequons of human myelin-associated glycoprotein.
9677334	11	70	part_of	TPO	1513:1515	arg1	the Arg10 and Arg17 residues	TPO		the Arg10 and Arg17 residues		PUBTATOR	AminoAcid	TPO	7066	Arg10 and Arg17 residues	Moreover we found that the Arg10 and Arg17 residues of TPO seem to be specific determinants for TPO/c-Mpl recognition.
9136890	13	2	gly	Asn	1676:1678	arg1	the oliosaccharide			Asn 727	the oliosaccharide					Asn 727	Previous studies indicated that the oliosaccharide at Asn 727 was high-mannose type [Hayes, G. R., et al. (1995) Glycobiology 5, 227-232].
9136890	13	2	gly	Asn	1676:1678	arg1	high-mannose type [Hayes			Asn 727	high-mannose type [Hayes					Asn 727	Previous studies indicated that the oliosaccharide at Asn 727 was high-mannose type [Hayes, G. R., et al. (1995) Glycobiology 5, 227-232].
19252480	9	61	part_of	residues	1481:1488	arg1	MD-2	MD-2		residues		OGER	AminoAcid	MD-2	Q9Y6Y9	residues in	This structural shift allows phosphate groups of LPS to contribute to receptor multimerization by forming ionic interactions with a cluster of positively charged residues in TLR4 and MD-2.
19252480	9	61	part_of	residues	1481:1488	arg1	TLR4	TLR4		residues		OGER	AminoAcid	TLR4	O00206	residues in	This structural shift allows phosphate groups of LPS to contribute to receptor multimerization by forming ionic interactions with a cluster of positively charged residues in TLR4 and MD-2.
2001369	9	52	gly	attached	1472:1479	arg1	Asn-300 AND the oligosaccharides			Asn-300	the oligosaccharides					Asn-300	Two different hybrid structures were found to account for 34% of the oligosaccharides attached to Asn-300.
12911312	1	24	gly	glycoprotein	227:238	arg1	Rat selenoprotein P	Rat selenoprotein P				PUBTATOR		Rat selenoprotein P	29360		Rat selenoprotein P is an extracellular glycoprotein of 366 amino acid residues that is rich in cysteine and selenocysteine.
12911312	1	24	gly	glycoprotein	227:238	arg1	an extracellular glycoprotein	an extracellular glycoprotein				Fterm		glycoprotein			Rat selenoprotein P is an extracellular glycoprotein of 366 amino acid residues that is rich in cysteine and selenocysteine.
2971663	5	43	gly	structures	1277:1286	arg1	leukosialin	leukosialin			structures	PUBTATOR		leukosialin	P16150		Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
20877282	4	48	part_of	PLXNB1	868:873	arg1	semaphorin ectodomains	PLXNB1		semaphorin ectodomains		OGER	Site	PLXNB1	O43157	ectodomains	Here we present crystal structures of cognate complexes of the semaphorin-binding regions of plexins B1 and A2 with semaphorin ectodomains (human PLXNB1(1-2)-SEMA4D(ecto) and murine PlxnA2(1-4)-Sema6A(ecto)), plus unliganded structures of PlxnA2(1-4) and Sema6A(ecto).
20877282	4	51	part_of	semaphorin	838:847	arg1	semaphorin ectodomains	semaphorin		semaphorin ectodomains		Fterm	Site	semaphorin		ectodomains	Here we present crystal structures of cognate complexes of the semaphorin-binding regions of plexins B1 and A2 with semaphorin ectodomains (human PLXNB1(1-2)-SEMA4D(ecto) and murine PlxnA2(1-4)-Sema6A(ecto)), plus unliganded structures of PlxnA2(1-4) and Sema6A(ecto).
20877282	4	54	part_of	PlxnA2	904:909	arg1	semaphorin ectodomains	PlxnA2		semaphorin ectodomains		OGER	Site	PlxnA2	O75051	ectodomains	Here we present crystal structures of cognate complexes of the semaphorin-binding regions of plexins B1 and A2 with semaphorin ectodomains (human PLXNB1(1-2)-SEMA4D(ecto) and murine PlxnA2(1-4)-Sema6A(ecto)), plus unliganded structures of PlxnA2(1-4) and Sema6A(ecto).
20877282	4	88	part_of	semaphorin-binding	785:802	arg1	the semaphorin-binding regions	semaphorin		the semaphorin-binding regions		Fterm	Site	semaphorin		regions	Here we present crystal structures of cognate complexes of the semaphorin-binding regions of plexins B1 and A2 with semaphorin ectodomains (human PLXNB1(1-2)-SEMA4D(ecto) and murine PlxnA2(1-4)-Sema6A(ecto)), plus unliganded structures of PlxnA2(1-4) and Sema6A(ecto).
17643119	2	51	part_of	subunit	357:363	arg1	a nAChR subunit extracellular domain	nAChR subunit		a nAChR subunit extracellular domain		PUBTATOR	Site	nAChR subunit	11441	domain	This structure is the first atomic-resolution view of a nAChR subunit extracellular domain, revealing receptor-specific features such as the main immunogenic region (MIR), the signature Cys-loop and the N-linked carbohydrate chain.
17643119	2	54	part_of	nAChR	351:355	arg1	a nAChR subunit extracellular domain	nAChR subunit		a nAChR subunit extracellular domain		PUBTATOR	Site	nAChR subunit	11441	domain	This structure is the first atomic-resolution view of a nAChR subunit extracellular domain, revealing receptor-specific features such as the main immunogenic region (MIR), the signature Cys-loop and the N-linked carbohydrate chain.
1456441	0	84	gly	N-glycosylation	0:14	arg2	N-glycosylation site mapping			N-glycosylation site mapping						site	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
23376777	7	59	gly	deglycosylated	1413:1426	arg1	KCC4	KCC4				PUBTATOR		KCC4	20499		Under hypotonic stress conditions, the ability to adapt to changes in intracellular chloride ion concentrations and RVD (regulatory volume decrease) activities were less efficient in cells containing the deglycosylated form of KCC4 that were not expressed at the cell surface.
17925379	0	75	gly	glycoproteins	30:42	arg1	Pannexin 1	Pannexin 1				PUBTATOR		Pannexin 1	24145		Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins.
17925379	0	75	gly	glycoproteins	30:42	arg1	pannexin 3	pannexin 3				PUBTATOR		pannexin 3	116337		Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins.
17925379	0	75	gly	glycoproteins	30:42	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins.
30459171	4	10	gly	glycosylation	661:673	arg2	O-linked glycosylation sites			O-linked glycosylation sites						sites	This large-scale localization of O-linked glycosylation sites demonstrated that EXoO is an effective method for defining the site-specific O-linked glycoproteome in different types of sample.
8053566	7	11	gly	nonfucosylated	1466:1479	arg1	4.4% nonfucosylated mannose (Man4) oligosaccharide				4.4% nonfucosylated mannose (Man4) oligosaccharide						The Asn78 site also contained 4.4% nonfucosylated mannose (Man4) oligosaccharide.
8053566	7	2	gly	contained	1451:1459	arg1	The Asn78 site AND 4.4% nonfucosylated mannose (Man4) oligosaccharide			The Asn78 site	4.4% nonfucosylated mannose (Man4) oligosaccharide					Asn78 site	The Asn78 site also contained 4.4% nonfucosylated mannose (Man4) oligosaccharide.
8286855	1	61	part_of	contains	184:191	arg1	The human red blood cell sialoglycoprotein AND a 'mucin-like' extensively O-glycosylated extracellular domain	The human red blood cell sialoglycoprotein		a 'mucin-like' extensively O-glycosylated extracellular domain		Fterm	Site	sialoglycoprotein		domain	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	1	61	part_of	contains	184:191	arg1	glycophorin A AND a 'mucin-like' extensively O-glycosylated extracellular domain	glycophorin A		a 'mucin-like' extensively O-glycosylated extracellular domain		PUBTATOR	Site	glycophorin A	2993	domain	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
24977290	7	38	part_of	ADAMTS13	1204:1211	arg1	the TSR domains	ADAMTS13		the TSR domains		PUBTATOR	Site	ADAMTS13	Q76LX8	domains	Moreover, six putative O-fucosylated sites were identified in the TSR domains of plasma ADAMTS13 by performing searches of the tandem mass spectrometry (MS/MS) data for loss of hexose (162 Da), deoxyhexose (146 Da), or hexose deoxyhexose(308 Da).
1904059	11	37	gly	fucosylation	1621:1632	arg1	serine 60			serine 60						serine 60	Carbohydrate and mass spectrometry analyses indicated that the fucosylation of serine 60 was virtually quantitative.
1904059	11	94	gly	serine	1637:1642	arg1	the fucosylation			serine 60	the fucosylation					serine 60	Carbohydrate and mass spectrometry analyses indicated that the fucosylation of serine 60 was virtually quantitative.
7776966	14	7	gly	Asn174	2301:2306	arg1	a carbohydrate			Asn174	a carbohydrate					Asn174	Our results demonstrate that while N-linked carbohydrates on the FSH receptor are not required directly for the binding of hormone, a carbohydrate at either Asn174 or Asn276 is required for the efficient folding of the nascent receptor protein into a conformation that allows high affinity binding of hormone.
7776966	14	21	gly	Asn276	2311:2316	arg1	a carbohydrate			Asn276	a carbohydrate					Asn276	Our results demonstrate that while N-linked carbohydrates on the FSH receptor are not required directly for the binding of hormone, a carbohydrate at either Asn174 or Asn276 is required for the efficient folding of the nascent receptor protein into a conformation that allows high affinity binding of hormone.
7776966	14	32	gly	carbohydrates	2188:2200	arg1	the FSH receptor	FSH receptor			carbohydrates	PUBTATOR		FSH receptor	2492		Our results demonstrate that while N-linked carbohydrates on the FSH receptor are not required directly for the binding of hormone, a carbohydrate at either Asn174 or Asn276 is required for the efficient folding of the nascent receptor protein into a conformation that allows high affinity binding of hormone.
10089882	0	33	part_of	CCR5	44:47	arg1	the amino terminus	CCR5		the amino terminus		OGER	Site	CCR5	P51681	terminus	Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry.
12171601	2	47	part_of	N-terminus	394:403	arg1	Asn(30)-->Ala	N-terminus [hPAR(2		Asn(30)-->Ala		OGER	AminoAcid	N-terminus [hPAR(2	P55085	Ala	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
2498325	7	85	gly	glycosylation	1122:1134	arg1	apoE	apoE				PUBTATOR		apoE	348		Apolipoprotein E(Thr194----Ala) was secreted exclusively as the asialo isoform, confirming that Thr194 is the site of carbohydrate attachment in these cells and indicating that glycosylation of apoE is not essential for secretion.
1904059	17	150	gly	linked	2641:2646	arg1	serine 52 AND the carbohydrate moiety			serine 52	the carbohydrate moiety					serine 52	These results indicate that the carbohydrate moiety O-glycosidically linked to serine 52 does not appear to be involved either in the interaction of factor VIIa with tissue factor, or the expression of its proteolytic activity toward factor X or factor IX following complex formation with tissue factor.
7925474	2	16	gly	glycosylation	247:259	arg1	fetal antigen 1	fetal antigen 1				PUBTATOR		fetal antigen 1	8788		The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	2	16	gly	glycosylation	247:259	arg1	FA1	FA1				PUBTATOR		FA1	8788		The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
24365146	6	2	part_of	Pro-156	1013:1019	arg1	p22	p22		Pro-156		PUBTATOR	SpecificSite	p22	11261	Pro-156	Superoxide production by unglycosylated Nox1 is largely dependent on p22(phox), which is abrogated by glutamine substitution for Pro-156 in p22(phox), a mutation leading to a defective interaction with the Nox1-activating protein Noxo1.
8507662	1	34	part_of	protein	140:146	arg1	The amino-acid sequence	protein		The amino-acid sequence		Fterm	Site	protein		sequence	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
15738388	4	55	part_of	cystatins	602:610	arg1	two topologically equivalent subdomains	cystatins		two topologically equivalent subdomains		OGER	Site	cystatins	P01036	subdomains	Human latexin consists of two topologically equivalent subdomains, reminiscent of cystatins, consisting of an alpha-helix enveloped by a curved beta-sheet.
11390601	3	93	gly	glycosylation	718:730	arg2	the glycosylation sites			the glycosylation sites						sites	Of the glycosylation sites that were evaluated, those proximal to the V1/V2 loops (N135, N141, N156, N160) and the V3 loops (N301) of gp120 were functionally critical.
11390601	3	22	gly	loops	787:791	arg1	N160			N135, N141, N156, N160						N135, N141, N156, N160	Of the glycosylation sites that were evaluated, those proximal to the V1/V2 loops (N135, N141, N156, N160) and the V3 loops (N301) of gp120 were functionally critical.
22344443	4	1	part_of	receptor	683:690	arg1	the transmembrane region	receptor		the transmembrane region		Fterm	Site	receptor		region	Access is gained by ligands entering laterally between helices I and VII within the transmembrane region of the receptor.
11279095	7	5	part_of	terminus	1365:1372	arg1	the cysteine			cysteine						cysteine	By using the same enzyme preparation and performing mass spectrometric analysis, we found that the first cysteine in sialylmotif L and the cysteine in sialylmotif S form a disulfide bridge, whereas the second cysteine in sialylmotif L and the cysteine at the COOH terminus form a second disulfide bridge.
19508227	0	14	gly	Glycosylation	0:12	arg1	tetraspanin Tspan-1	Tspan-1		sites		PUBTATOR		Tspan-1	10103	sites	Glycosylation of tetraspanin Tspan-1 at four distinct sites promotes its transition through the endoplasmic reticulum.
3038148	4	24	part_of	contains	604:611	arg1	The complete amino acid sequence AND 235 residues	The complete amino acid sequence		235 residues						residues	The complete amino acid sequence thus contains 235 residues corresponding to a molecular weight of 25,658, more in agreement with previously reported molecular weights.
3038148	4	24	part_of	contains	604:611	arg1	The complete amino acid sequence AND The complete amino acid sequence	The complete amino acid sequence		The complete amino acid sequence						sequence	The complete amino acid sequence thus contains 235 residues corresponding to a molecular weight of 25,658, more in agreement with previously reported molecular weights.
11738084	6	11	gly	glycosylated	804:815	arg1	glycosylated albumin variants	glycosylated albumin variants				OGER		albumin variants	P02768		The structure is principally the same as that of glycans bound to two other types of glycosylated albumin variants.
2059624	0	41	gly	Asparagine-linked	0:16	arg1	Asparagine-linked oligosaccharide processing			Asparagine	Asparagine-linked oligosaccharide processing					Asparagine	Asparagine-linked oligosaccharide processing in lepidopteran insect cells.
3497198	0	88	gly	glycosylation	14:26	arg1	H-2K	H-2K				PUBTATOR		H-2K	14972		Site specific glycosylation patterns of H-2K: effects of allelic polymorphism and mitogenic stimulation.
19880749	7	9	part_of	VWF-binding	957:967	arg1	3 VWF-binding exosites	3 VWF		3 VWF-binding exosites		PUBTATOR	Site	3 VWF	7450	exosites	We identified 3 VWF-binding exosites on the linearly aligned discontinuous surfaces of the D, C(A), and S domains traversing the W-shaped molecule.
1323463	5	3	gly	sequences	998:1006	arg1	The Lewis(y) and blood-group-A determinants				The Lewis(y) and blood-group-A determinants						The Lewis(y) and blood-group-A determinants of these sequences have not been found previously in the acidic oligosaccharides of bovine submaxillary-gland mucin, although they have recently been characterised in the neutral chains of bovine submaxillary-gland mucin.
1323463	5	18	gly	mucin	1099:1103	arg1	the acidic oligosaccharides	mucin			the acidic oligosaccharides	PUBTATOR		mucin	281333		The Lewis(y) and blood-group-A determinants of these sequences have not been found previously in the acidic oligosaccharides of bovine submaxillary-gland mucin, although they have recently been characterised in the neutral chains of bovine submaxillary-gland mucin.
23829323	5	55	gly	sequences	1119:1127	arg1	peptide-glycan pairs			sequences	peptide-glycan pairs					sequences	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	5	73	gly	N-glycopeptides	1038:1052	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
10712595	9	2	gly	have	1629:1632	arg1	Salmon antithrombin AND three complex oligosaccharide side chains	Salmon antithrombin			three complex oligosaccharide side chains	PUBTATOR		antithrombin	462		Salmon antithrombin appears to have three complex oligosaccharide side chains containing sialic acid terminally linked alpha(2-3) to galactose, while trace amounts of Galbeta(1-4)GlcNAc suggest microheterogeneity due to partial loss of sialic acid.
24161696	5	33	part_of	Kv3.1b	992:997	arg1	both N-glycosylation sites	Kv3.1b		both N-glycosylation sites		Cterm	Site	Kv3.1b		sites	RESULTS: Microscopy images revealed that occupancy of both N-glycosylation sites of Kv3.1b had relatively similar amounts of Kv3.1b in the outgrowth and cell body while vacancy of one or both sites led to increased accumulation of Kv3.1b in the cell body.
30659065	1	17	gly	glycoproteins	166:178	arg1	critical glycoproteins	critical glycoproteins				Fterm		glycoproteins			Antibodies are critical glycoproteins that bridge the innate and adaptive immune systems to provide protection against infection.
3521732	7	0	part_of	precursor	904:912	arg1	a signal peptide	precursor		a signal peptide		Fterm	Site	precursor		peptide	Analysis of the cDNA indicated that human plasma prekallikrein is synthesized as a precursor with a signal peptide of 19 amino acids.
2108149	3	66	gly	glycopeptides	614:626	arg2	fluoresceinated glycopeptides			fluoresceinated glycopeptides						glycopeptides	Pronase digestion of the purified heavy chains and subsequent end labeling with fluorescein isothiocyanate produced fluoresceinated glycopeptides which were detected and purified by polyacrylamide gel electrophoresis.
6118137	6	2	gly	located	486:492	arg1	Asn-74 AND Three N-linked amino sugars			Asn-23, Asn-74 and Asn-98	Three N-linked amino sugars					Asn-23, Asn-74 and Asn-98	Three N-linked amino sugars were located at Asn-23, Asn-74 and Asn-98.
6118137	6	2	gly	located	486:492	arg1	Asn-23 AND Three N-linked amino sugars			Asn-23, Asn-74 and Asn-98	Three N-linked amino sugars					Asn-23, Asn-74 and Asn-98	Three N-linked amino sugars were located at Asn-23, Asn-74 and Asn-98.
6118137	6	2	gly	located	486:492	arg1	Asn-23 AND Three N-linked amino sugars			Asn-23, Asn-74 and Asn-98	Three N-linked amino sugars					Asn-23, Asn-74 and Asn-98	Three N-linked amino sugars were located at Asn-23, Asn-74 and Asn-98.
28753425	4	28	part_of	rhodopsin	685:693	arg1	rhodopsin C-terminal tail residues T336 and S338	rhodopsin		rhodopsin C-terminal tail residues T336 and S338		PUBTATOR	Site	rhodopsin	6010	residues	Phosphorylation was detected at rhodopsin C-terminal tail residues T336 and S338.
7781780	1	27	gly	glycosylation	425:437	arg2	this glycosylation site			this glycosylation site						site	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	7	gly	glycosylation	234:246	arg1	recombinant human erythropoietin	erythropoietin		Asn-24		PUBTATOR		erythropoietin	2056	Asn-24	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	7	gly	glycosylation	234:246	arg1	recombinant human erythropoietin	erythropoietin		site		PUBTATOR		erythropoietin	2056	site	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
9705299	3	48	gly	glycosylation	486:498	arg2	three potential asparagine (N)-linked glycosylation sites			three potential asparagine (N)-linked glycosylation sites						sites	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
1482348	2	33	gly	O-glycosylated	284:297	arg1	O-glycosylated oligosaccharide				O-glycosylated oligosaccharide						N-acetylgalactosamine (GalNAc) in the alpha chain suggested the presence of O-glycosylated oligosaccharide.
1567356	0	6	part_of	glycoprotein	63:74	arg1	the five glycosylation sites	glycoprotein		the five glycosylation sites		Fterm	Site	glycoprotein		sites	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
12927778	8	38	gly	glycoprotein	1140:1151	arg1	a neural oligomannosidic glycoprotein	a neural oligomannosidic glycoprotein				Fterm		glycoprotein			These data, therefore, suggest that NPP-5 is a neural oligomannosidic glycoprotein that may participate in neural cell communications.
12927778	8	38	gly	glycoprotein	1140:1151	arg1	NPP-5	NPP-5				PUBTATOR		NPP-5	316249		These data, therefore, suggest that NPP-5 is a neural oligomannosidic glycoprotein that may participate in neural cell communications.
17558413	2	13	part_of	sites	259:263	arg1	proteins	proteins		sites		Fterm	Site	proteins		sites	We describe a subtractive strategy to determine the sites of tyrosine O-sulfation in proteins.
17558413	2	39	part_of	proteins	292:299	arg1	the sites	proteins		the sites		Fterm	Site	proteins		sites	We describe a subtractive strategy to determine the sites of tyrosine O-sulfation in proteins.
7774715	3	6	gly	lactoferrin	380:390	arg1	Two N-linked glycans	lactoferrin			Two N-linked glycans	OGER		lactoferrin	P02788		Two N-linked glycans from purified recombinant lactoferrin were released by hydrazinolysis and analyzed by 400-MHz 1H-NMR spectroscopy.
8053566	4	37	gly	glycopeptide	974:985	arg2	each glycopeptide			each glycopeptide						glycopeptide	The oligosaccharide composition of the glycoforms was inferred from the observed mass shifts following digestion by peptide-N-glycosidase F. Composition and sequence were then elucidated by digestion with specific exoglycosidases, using a total of 200 pmol of each glycopeptide.
7780197	0	43	part_of	receptor	53:60	arg1	The critical glycosylation site	transferrin receptor		The critical glycosylation site		PUBTATOR	Site	transferrin receptor	7037	site	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
10878002	6	23	gly	C-mannosylation	755:769	arg1	human properdin	human properdin				PUBTATOR		properdin	5199		We studied the C-mannosylation pattern of human properdin by mass spectrometry and Edman degradation.
10878002	6	29	gly	properdin	788:796	arg1	the C-mannosylation pattern	properdin			the C-mannosylation pattern	PUBTATOR		properdin	5199		We studied the C-mannosylation pattern of human properdin by mass spectrometry and Edman degradation.
29391424	6	41	gly	glycopeptide	877:888	arg2	O-linked glycopeptide spectra			O-linked glycopeptide spectra						glycopeptide	Thus, a single tool was developed that collectively allows the (i) elucidation of N- and O-linked glycopeptide spectra, (ii) matching glycopeptides to known protein sequences, and (iii) high-throughput, batch-wise analysis of large-scale glycoproteomics data sets.
29391424	6	59	gly	glycopeptides	913:925	arg2	glycopeptides			glycopeptides						glycopeptides	Thus, a single tool was developed that collectively allows the (i) elucidation of N- and O-linked glycopeptide spectra, (ii) matching glycopeptides to known protein sequences, and (iii) high-throughput, batch-wise analysis of large-scale glycoproteomics data sets.
7686446	3	6	gly	AFP	697:699	arg1	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	AFP			Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	PUBTATOR		AFP	174		Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	6	gly	AFP	697:699	arg1	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	AFP			Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	PUBTATOR		AFP	174		Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	6	gly	AFP	697:699	arg1	the whole sugar chain structures	AFP			the whole sugar chain structures	PUBTATOR		AFP	174		Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	6	gly	AFP	697:699	arg1	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta	AFP			Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta	PUBTATOR		AFP	174		Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
1463457	5	20	gly	N-glycosylation	909:923	arg2	13 potential N-glycosylation sites			13 potential N-glycosylation sites						sites	The predicted sequence has 552 amino acids with a leader peptide of 36 amino acids and contains 13 potential N-glycosylation sites, of which it is likely that 10 are used.
15657036	7	48	part_of	containing	758:767	arg1	a calcium-binding protein AND an N-terminal (residues 86-168) and a C-terminal (residues 178-374) protease-resistant domain	a calcium-binding protein		an N-terminal (residues 86-168) and a C-terminal (residues 178-374) protease-resistant domain		Fterm	Site	protein		domain	FGE is a calcium-binding protein containing an N-terminal (residues 86-168) and a C-terminal (residues 178-374) protease-resistant domain.
15657036	7	48	part_of	containing	758:767	arg1	FGE AND an N-terminal (residues 86-168) and a C-terminal (residues 178-374) protease-resistant domain	FGE		an N-terminal (residues 86-168) and a C-terminal (residues 178-374) protease-resistant domain		PUBTATOR	Site	FGE	285362	domain	FGE is a calcium-binding protein containing an N-terminal (residues 86-168) and a C-terminal (residues 178-374) protease-resistant domain.
17525160	3	89	gly	glycosylation	342:354	arg2	Asn-15			Asn-15						Asn-15	Part of this increased mass is due to N-linked glycosylation at Asn-15.
23661698	7	17	part_of	site	1007:1010	arg1	ephrin-A1	ephrin-A1		site		PUBTATOR	Site	ephrin-A1	1942	site	Mutations in the glycosylation site on ephrin-A1 result in protein aggregation and mislocalization.
23001782	1	72	gly	glycoprotein	195:206	arg1	Human sex hormone binding globulin	Human sex hormone binding globulin				PUBTATOR		Human sex hormone binding globulin	6462		Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	72	gly	glycoprotein	195:206	arg1	a serum glycoprotein	a serum glycoprotein				Fterm		glycoprotein			Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23236605	4	40	gly	contains	724:731	arg1	human AIM AND no N-glycan	human AIM			no N-glycan	OGER		AIM	Q07108		Although human AIM contains no N-glycan, attachment of N-glycans increased AIM secretion.
20188224	11	54	gly	Glycosylation	1514:1526	arg1	four out of five potential PGRN N-glycosylation consensus sites			four out of five potential PGRN N-glycosylation consensus sites						sites	Glycosylation of four out of five potential PGRN N-glycosylation consensus sites was demonstrated (the final one remains undetermined), with one of the four observed to be partially occupied.
20188224	11	63	gly	N-glycosylation	1563:1577	arg2	four out of five potential PGRN N-glycosylation consensus sites			four out of five potential PGRN N-glycosylation consensus sites						sites	Glycosylation of four out of five potential PGRN N-glycosylation consensus sites was demonstrated (the final one remains undetermined), with one of the four observed to be partially occupied.
2403553	0	69	gly	contains	27:34	arg1	Human transferrin receptor AND O-linked oligosaccharides	Human transferrin receptor			O-linked oligosaccharides	PUBTATOR		transferrin receptor	7018		Human transferrin receptor contains O-linked oligosaccharides.
21712440	5	22	gly	glycosylated	1253:1264	arg2	Tyr10			Tyr10						Tyr10	Unexpectedly, we also identified a series of 27 glycopeptides, the Aβ1-X series, where X was 20 (DAEFRHDSGYEVHHQKLVFF), 19, 18, 17, 16, and 15, which were all uniquely glycosylated on Tyr10.
21712440	5	46	gly	glycopeptides	1133:1145	arg2	27 glycopeptides			27 glycopeptides						glycopeptides	Unexpectedly, we also identified a series of 27 glycopeptides, the Aβ1-X series, where X was 20 (DAEFRHDSGYEVHHQKLVFF), 19, 18, 17, 16, and 15, which were all uniquely glycosylated on Tyr10.
11706042	3	10	part_of	TLR4	500:503	arg1	the amino-terminal ectodomain	TLR4		the amino-terminal ectodomain		PUBTATOR	Site	TLR4	7099	ectodomain	We demonstrate that MD-2 contains 2 N-glycosylated sites at positions Asn(26) and Asn(114), whereas the amino-terminal ectodomain of human TLR4 contains 9 N-linked glycosylation sites.
11706042	3	65	part_of	contains	386:393	arg1	MD-2 AND 2 N-glycosylated sites	MD-2		2 N-glycosylated sites		OGER	Site	MD-2	Q9Y6Y9	sites	We demonstrate that MD-2 contains 2 N-glycosylated sites at positions Asn(26) and Asn(114), whereas the amino-terminal ectodomain of human TLR4 contains 9 N-linked glycosylation sites.
11706042	3	51	part_of	contains	505:512	arg1	human TLR4 AND 9 N-linked glycosylation sites	human TLR4		9 N-linked glycosylation sites		PUBTATOR	Site	TLR4	7099	sites	We demonstrate that MD-2 contains 2 N-glycosylated sites at positions Asn(26) and Asn(114), whereas the amino-terminal ectodomain of human TLR4 contains 9 N-linked glycosylation sites.
24134926	1	74	gly	present	193:199	arg2	ECM AND a glycosaminoglycan	ECM			a glycosaminoglycan	OGER		ECM	Q13201		Hyaluronan (HA) is a glycosaminoglycan composed by repeating units of D-glucuronic acid (GlcUA) and N-acetylglucosamine (GlcNAc) that is ubiquitously present in the extracellular matrix (ECM) where it has a critical role in the physiology and pathology of several mammalian tissues.
10024660	4	44	gly	present	711:717	arg1	BSSL AND esterified N- glycans	BSSL			esterified N- glycans	PUBTATOR		BSSL	P19835		The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10715549	4	8	gly	attached	1037:1044	arg2	the Asn(13) AND N-linked oligosaccharides			the Asn(13)	N-linked oligosaccharides					Asn(13)	No aggregation was seen when N-linked oligosaccharides were attached to the Asn(13) of LHbeta.
2550193	5	6	gly	EPO	610:612	arg1	The two major N-linked oligosaccharides	Namalwa EPO			The two major N-linked oligosaccharides	PUBTATOR		Namalwa EPO	2056		The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
28011641	1	53	gly	fucosylated	140:150	arg1	fucosylated glycan ligands				fucosylated glycan ligands						Selectin interactions with fucosylated glycan ligands mediate leukocyte rolling in the vasculature under shear forces.
10704524	4	47	gly	structures	552:561	arg1	the secreted enzyme	enzyme			structures	Fterm		enzyme			Characterization of the N-linked oligosaccharide structures on the secreted enzyme overexpressed in Chinese hamster ovary cells revealed highly heterogeneous structures consisting of complex (approximately 53%), hybrid (approximately 12%), and high mannose-type (approximately 33%) oligosaccharides.
23829323	2	23	gly	glycopeptides	473:485	arg2	glycopeptides			glycopeptides						glycopeptides	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
16332679	1	77	gly	O-glycosylation	171:185	arg1	Sp1	Sp1				OGER		Sp1	P08047		O-glycosylation and phosphorylation of Sp1 are thought to modulate the expression of a number of genes in normal and diabetic state.
26146185	2	1	part_of	receptor	324:331	arg1	the N-terminal immunoglobulin superfamily (IgSF) domain	receptor		the N-terminal immunoglobulin superfamily (IgSF) domain		Fterm	Site	receptor		domain	The membrane proximal domain of CD6 binds the N-terminal immunoglobulin superfamily (IgSF) domain of another cell surface receptor, CD166, which also engages in homophilic interactions.
26146185	2	41	part_of	CD6	234:236	arg1	The membrane proximal domain	CD6		The membrane proximal domain		PUBTATOR	Site	CD6	923	domain	The membrane proximal domain of CD6 binds the N-terminal immunoglobulin superfamily (IgSF) domain of another cell surface receptor, CD166, which also engages in homophilic interactions.
8407880	4	37	gly	glycosylation	725:737	arg2	the two glycosylation sites			the two glycosylation sites						sites	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
10383441	7	47	gly	residues	1358:1365	arg1	lysosomal enzymes	enzymes			residues	Fterm		enzymes			Tyr54 and Ser190 are widely separated from each other and from Asn106 on the surface of DNase I, indicating that residues present over a broad area influence the interaction with UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, which is responsible for the formation of mannose 6-phosphate residues on lysosomal enzymes.
22750213	5	14	gly	glycosylation	837:849	arg2	the N-linked glycosylation site	PRiMA		site		PUBTATOR		PRiMA	170952	site	By using site-directed mutagenesis, the asparagine-43 was identified to be the N-linked glycosylation site of PRiMA.
22750213	5	14	gly	glycosylation	837:849	arg2	the asparagine-43	PRiMA		asparagine-43		PUBTATOR		PRiMA	170952	asparagine-43	By using site-directed mutagenesis, the asparagine-43 was identified to be the N-linked glycosylation site of PRiMA.
8357534	2	22	gly	occupied	323:330	arg1	two N-glycosylation sites			two N-glycosylation sites						sites	Elastase has two N-glycosylation sites occupied (Asn-45 and Asn-144), whereas cathepsin G has only one (Asn-64).
8357534	2	45	gly	N-glycosylation	301:315	arg2	two N-glycosylation sites			two N-glycosylation sites						sites	Elastase has two N-glycosylation sites occupied (Asn-45 and Asn-144), whereas cathepsin G has only one (Asn-64).
8357534	2	22	gly	occupied	323:330	arg1	Asn-144			Asn-45 and Asn-144						Asn-45 and Asn-144	Elastase has two N-glycosylation sites occupied (Asn-45 and Asn-144), whereas cathepsin G has only one (Asn-64).
8357534	2	45	gly	N-glycosylation	301:315	arg2	Asn-45			Asn-45 and Asn-144						Asn-45 and Asn-144	Elastase has two N-glycosylation sites occupied (Asn-45 and Asn-144), whereas cathepsin G has only one (Asn-64).
27966990	7	21	gly	glycopeptides	1116:1128	arg2	glycopeptides			glycopeptides						glycopeptides	MS/MS analyses of glycopeptides and deamidated, deglycosylated (PNGase F-treated) peptides from ectopically expressed VEGFR-2 in porcine aortic endothelial (PAE) cells identified N-glycans at the majority of the 17 potential N-glycosylation sites on VEGFR-2 in a site-specific manner.
27966990	7	38	gly	N-glycosylation	1323:1337	arg2	the 17 potential N-glycosylation sites			the 17 potential N-glycosylation sites						sites	MS/MS analyses of glycopeptides and deamidated, deglycosylated (PNGase F-treated) peptides from ectopically expressed VEGFR-2 in porcine aortic endothelial (PAE) cells identified N-glycans at the majority of the 17 potential N-glycosylation sites on VEGFR-2 in a site-specific manner.
27966990	7	25	gly	deglycosylated	1146:1159	arg1	deamidated, deglycosylated (PNGase F-treated) peptides	PNGase		peptides		PUBTATOR		PNGase	59007	peptides	MS/MS analyses of glycopeptides and deamidated, deglycosylated (PNGase F-treated) peptides from ectopically expressed VEGFR-2 in porcine aortic endothelial (PAE) cells identified N-glycans at the majority of the 17 potential N-glycosylation sites on VEGFR-2 in a site-specific manner.
21053369	4	37	gly	occupancy	605:613	arg2	each site			each site						site	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	75	gly	glycosylation	419:431	arg1	rhIL-23r	rhIL-23r				OGER		rhIL-23r	Q5VWK5		In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	75	gly	glycosylation	419:431	arg1	soluble recombinant human IL-23r	soluble recombinant human IL-23r				PUBTATOR		IL-23r	149233		In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	18	gly	glycosylation	560:572	arg2	glycosylation sites			sites	attached oligosaccharides					sites	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
10201933	1	19	gly	glycoprotein	210:221	arg1	an 80-kDa glycosylphosphatidylinositol (GPI)-anchored membrane glycoprotein	an 80-kDa glycosylphosphatidylinositol (GPI)-anchored membrane glycoprotein				Fterm		glycoprotein			CDw108, also known as the John-Milton-Hagen human blood group Ag, is an 80-kDa glycosylphosphatidylinositol (GPI)-anchored membrane glycoprotein that is preferentially expressed on activated lymphocytes and E.
10201933	1	19	gly	glycoprotein	210:221	arg1	CDw108	CDw108				PUBTATOR		CDw108	8482		CDw108, also known as the John-Milton-Hagen human blood group Ag, is an 80-kDa glycosylphosphatidylinositol (GPI)-anchored membrane glycoprotein that is preferentially expressed on activated lymphocytes and E.
24841998	0	45	gly	N-glycopeptide	25:38	arg2	sialylated N-glycopeptide levels			sialylated N-glycopeptide levels						N-glycopeptide	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
19285951	1	37	gly	glycoprotein	128:139	arg1	a plasma protein	a plasma protein				Fterm		protein			Histidine-rich glycoprotein (HRG) is a plasma protein implicated in the innate immune system.
19285951	1	37	gly	glycoprotein	128:139	arg1	HRG	HRG				PUBTATOR		HRG	3273		Histidine-rich glycoprotein (HRG) is a plasma protein implicated in the innate immune system.
20739279	6	22	part_of	Ig1	821:823	arg1	the corresponding SynCAM 1 Ig1 domain	SynCAM 1 Ig1		the corresponding SynCAM 1 Ig1 domain		PUBTATOR	Site	SynCAM 1 Ig1	23705	domain	Structural modeling of the corresponding SynCAM 1 Ig1 domain indicates that its glycosylation sites Asn(70)/Asn(104) flank the binding interface of this domain.
20739279	6	30	part_of	SynCAM	812:817	arg1	the corresponding SynCAM 1 Ig1 domain	SynCAM 1 Ig1		the corresponding SynCAM 1 Ig1 domain		PUBTATOR	Site	SynCAM 1 Ig1	23705	domain	Structural modeling of the corresponding SynCAM 1 Ig1 domain indicates that its glycosylation sites Asn(70)/Asn(104) flank the binding interface of this domain.
25456591	0	48	gly	O-glycosylation	26:40	arg2	protein O-glycosylation site			protein O-glycosylation site						site	Identification of protein O-glycosylation site and corresponding glycans using liquid chromatography-tandem mass spectrometry via mapping accurate mass and retention time shift.
9343410	4	8	gly	glycosylation	899:911	arg2	this glycosylation site			this glycosylation site						site	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	4	12	gly	contain	790:796	arg1	this 97-amino-acid domain AND a dominant O-GlcNAc residue	Sp1		domain	a dominant O-GlcNAc residue	OGER		Sp1	Q8N907	domain	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
15863501	9	48	gly	N-glycosylation	1604:1618	arg1	sPLA(2)-III	sPLA(2)-III				PUBTATOR		sPLA(2)-III	50487		Taken together, these results reveal unique cell type-specific processing and N-glycosylation of sPLA(2)-III and the potential role of this enzyme in cancer development by stimulating tumor cell growth and angiogenesis.
15863501	9	48	gly	N-glycosylation	1604:1618	arg1	this enzyme	this enzyme				Fterm		enzyme			Taken together, these results reveal unique cell type-specific processing and N-glycosylation of sPLA(2)-III and the potential role of this enzyme in cancer development by stimulating tumor cell growth and angiogenesis.
14718370	10	72	gly	C-mannosylated	1663:1676	arg1	the Cys subdomains	MUC5B		Cys subdomains		PUBTATOR		MUC5B	Q9HC84	Cys subdomains	Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs.
14718370	10	72	gly	C-mannosylated	1663:1676	arg1	the Cys subdomains	MUC5AC		Cys subdomains		PUBTATOR		MUC5AC	P98088	Cys subdomains	Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs.
8942641	6	104	gly	glycoprotein	1019:1030	arg1	The receptor	The receptor				Fterm		receptor			The receptor is a glycoprotein; treatment of RINm5f or alpha TC-6 cells with tunicamycin reduces the 140 and 150 kDa species to a single approximately 137 kDa protein.
8942641	6	104	gly	glycoprotein	1019:1030	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			The receptor is a glycoprotein; treatment of RINm5f or alpha TC-6 cells with tunicamycin reduces the 140 and 150 kDa species to a single approximately 137 kDa protein.
7686446	0	57	gly	alpha-fetoprotein	33:49	arg1	Sugar chains	alpha-fetoprotein			Sugar chains	PUBTATOR		alpha-fetoprotein	174		Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	0	121	gly	glycoproteins	96:108	arg1	glycoproteins	glycoproteins			N-linked sugar chains	Fterm		glycoproteins			Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
20489211	0	55	part_of	gp130	46:50	arg1	the entire ectodomain	gp130		the entire ectodomain		PUBTATOR	Site	gp130	3572	ectodomain	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
2108149	0	37	part_of	G	34:34	arg1	The polypeptide	immunoglobulin G		The polypeptide		Cterm	Site	immunoglobulin G		polypeptide	The polypeptide of immunoglobulin G influences its galactosylation in vivo.
16622833	2	67	part_of	A1PI	270:273	arg1	The three N-glycosylation sites	A1PI		The three N-glycosylation sites		PUBTATOR	Site	A1PI	5265	sites	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
9336835	8	122	gly	glycosylation	1247:1259	arg2	six N-linked glycosylation sites			six N-linked glycosylation sites						sites	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
22766194	7	19	gly	N-glycosylated	1402:1415	arg1	the three consensus sites	CD10		sites		PUBTATOR		CD10	4311	sites	All of the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10 were confirmed to be N-glycosylated.
12144777	6	8	part_of	urease	1096:1101	arg1	the catalytic domain	urease		the catalytic domain		Fterm	Site	urease		domain	The barrel and active-site architectures utilizing catalytic metal ions exhibit unexpected similarities to those of the murine adenosine deaminase and the catalytic domain of the bacterial urease.
8068684	6	4	gly	utilized	1162:1169	arg2	Asn 75			Asn 75						Asn 75	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	6	4	gly	utilized	1162:1169	arg2	only the first N-glycosylation site			only the first N-glycosylation site						site	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	6	87	gly	N-glycosylation	1129:1143	arg2	Asn 75			Asn 75						Asn 75	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	6	87	gly	N-glycosylation	1129:1143	arg2	only the first N-glycosylation site			only the first N-glycosylation site						site	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
17715132	6	17	gly	glycosylation	788:800	arg1	Pannexin1	Pannexin1				PUBTATOR		Pannexin1	24145		The glycosylation of Pannexin1 at its extracellular surface makes it unlikely that two oligomers could dock to form an intercellular channel.
25759508	0	41	gly	O-Glycosylation	13:27	arg1	Human Immunoglobulin G3	Human Immunoglobulin G3				PUBTATOR		Human Immunoglobulin G3	3502		Hinge-Region O-Glycosylation of Human Immunoglobulin G3 (IgG3).
25759508	0	41	gly	O-Glycosylation	13:27	arg1	IgG3	IgG3				PUBTATOR		IgG3	P01860		Hinge-Region O-Glycosylation of Human Immunoglobulin G3 (IgG3).
12654314	5	16	gly	possessed	957:965	arg1	Asn-166 AND one high-mannose-type oligosaccharide			Asn-166	one high-mannose-type oligosaccharide					Asn-166	Asn-166 possessed 20 monosialylated and nonsialylated, and fucosylated and nonfucosylated complex- and hybrid-type oligosaccharides and one high-mannose-type oligosaccharide.
12654314	5	16	gly	possessed	957:965	arg1	Asn-166 AND hybrid-type oligosaccharides			Asn-166	hybrid-type oligosaccharides					Asn-166	Asn-166 possessed 20 monosialylated and nonsialylated, and fucosylated and nonfucosylated complex- and hybrid-type oligosaccharides and one high-mannose-type oligosaccharide.
11912203	6	44	part_of	adiponectin	795:805	arg1	the collagenous domain	adiponectin		the collagenous domain		PUBTATOR	Site	adiponectin	9370	domain	The glycosylation sites were mapped to several lysines (residues 68, 71, 80, and 104) located in the collagenous domain of adiponectin, each having the surrounding motif of GXKGE(D).
11904304	3	46	gly	Thr-58-glycosylated	600:618	arg1	the Thr-58-glycosylated form	form of c-Myc				PUBTATOR		form of c-Myc	4609		One antibody specifically reacts with the Thr-58-glycosylated form of c-Myc, and the other reacts only with unmodified Thr-58 in c-Myc.
29992770	9	31	part_of	haptoglobin	1267:1277	arg1	N-glycopeptides	haptoglobin		N-glycopeptides		Fterm	Site	haptoglobin	3240	N-glycopeptides	N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls.
29992770	9	59	part_of	transferrin	1284:1294	arg1	N-glycopeptides	transferrin		N-glycopeptides		Fterm	Site	transferrin	7018	N-glycopeptides	N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls.
7014218	5	53	gly	glycopeptide	634:645	arg2	The glycopeptide C3			The glycopeptide C3						glycopeptide	The glycopeptide C3 contains 77 amino acids corresponding to a molecular weight of 8653.
20188224	9	36	gly	attached	1330:1337	arg3	N-glycan AND particular sites			particular sites	N-glycan					sites	In addition, glycopeptides were produced using in-solution pronase digestion to identify species of N-glycan attached at particular sites.
20188224	9	53	gly	glycopeptides	1234:1246	arg2	glycopeptides			glycopeptides						glycopeptides	In addition, glycopeptides were produced using in-solution pronase digestion to identify species of N-glycan attached at particular sites.
8033893	7	69	gly	O-glycosylation	1032:1046	arg1	rat platelet factor 4	rat platelet factor 4				OGER		platelet factor 4	P06765		Overall consideration of these data led to identification of the higher-molecular-mass protein as a glycosylated form of rat platelet factor 4 with O-glycosylation at the second N-terminal amino acid, while the structure of the oligosaccharide core was established by mass spectrometry and sugar differentiation with lectins.
8033893	7	76	gly	glycosylated	984:995	arg1	rat platelet factor 4	rat platelet factor 4				OGER		platelet factor 4	P06765		Overall consideration of these data led to identification of the higher-molecular-mass protein as a glycosylated form of rat platelet factor 4 with O-glycosylation at the second N-terminal amino acid, while the structure of the oligosaccharide core was established by mass spectrometry and sugar differentiation with lectins.
3422739	4	55	gly	serine	714:719	arg1	a candidate serine glycosaminoglycan-acceptor site			serine	a candidate serine glycosaminoglycan-acceptor site					serine	Ii does not have multiple candidate glycosaminoglycan-attachment sites, and we used site-directed mutagenesis to replace a candidate serine glycosaminoglycan-acceptor site with alanine at position 201 in the murine Ii protein.
3422739	4	43	gly	have	593:596	arg1	Ii AND multiple candidate glycosaminoglycan-attachment sites	Ii			multiple candidate glycosaminoglycan-attachment sites	Cterm		Ii			Ii does not have multiple candidate glycosaminoglycan-attachment sites, and we used site-directed mutagenesis to replace a candidate serine glycosaminoglycan-acceptor site with alanine at position 201 in the murine Ii protein.
1512232	9	72	gly	glycosylation	1645:1657	arg2	The other glycosylation sites			The other glycosylation sites						sites	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1898343	3	21	gly	glycoprotein	304:315	arg1	glycoprotein	glycoprotein				Fterm		glycoprotein			In order to study its glycosylation, glycoprotein isolated from post-mortem pancreas tissue of 75 donors was digested with trypsin.
15901639	9	20	part_of	CEACAM10	1194:1201	arg1	the CEACAM10 binding region	CEACAM10		the CEACAM10 binding region		PUBTATOR	Site	CEACAM10	26366	region	A cytochemical study illustrated the presence of the CEACAM10 binding region on the entire surface of mouse sperm.
7929098	5	18	gly	glycosylated	796:807	arg1	eight potential sites			eight potential sites						sites	Sequence analysis also revealed eight potential sites for N-glycosylation, six of which were found to be glycosylated (Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538), indicating that they are extracellular.
7929098	5	71	gly	glycosylated	796:807	arg1	Asn424			Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538						Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538	Sequence analysis also revealed eight potential sites for N-glycosylation, six of which were found to be glycosylated (Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538), indicating that they are extracellular.
7929098	5	71	gly	glycosylated	796:807	arg1	Asn538			Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538						Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538	Sequence analysis also revealed eight potential sites for N-glycosylation, six of which were found to be glycosylated (Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538), indicating that they are extracellular.
7929098	5	71	gly	glycosylated	796:807	arg1	Asn339			Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538						Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538	Sequence analysis also revealed eight potential sites for N-glycosylation, six of which were found to be glycosylated (Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538), indicating that they are extracellular.
7929098	5	71	gly	glycosylated	796:807	arg1	Asn320			Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538						Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538	Sequence analysis also revealed eight potential sites for N-glycosylation, six of which were found to be glycosylated (Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538), indicating that they are extracellular.
7929098	5	71	gly	glycosylated	796:807	arg1	Asn538			Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538						Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538	Sequence analysis also revealed eight potential sites for N-glycosylation, six of which were found to be glycosylated (Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538), indicating that they are extracellular.
7929098	5	71	gly	glycosylated	796:807	arg1	Asn339			Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538						Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538	Sequence analysis also revealed eight potential sites for N-glycosylation, six of which were found to be glycosylated (Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538), indicating that they are extracellular.
7929098	5	71	gly	glycosylated	796:807	arg1	Asn320			Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538						Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538	Sequence analysis also revealed eight potential sites for N-glycosylation, six of which were found to be glycosylated (Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538), indicating that they are extracellular.
7929098	5	71	gly	glycosylated	796:807	arg1	Asn339			Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538						Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538	Sequence analysis also revealed eight potential sites for N-glycosylation, six of which were found to be glycosylated (Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538), indicating that they are extracellular.
7929098	5	71	gly	glycosylated	796:807	arg1	Asn320			Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538						Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538	Sequence analysis also revealed eight potential sites for N-glycosylation, six of which were found to be glycosylated (Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538), indicating that they are extracellular.
7929098	5	71	gly	glycosylated	796:807	arg1	Asn320			Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538						Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538	Sequence analysis also revealed eight potential sites for N-glycosylation, six of which were found to be glycosylated (Asn190, Asn259, Asn320, Asn339, Asn424, and Asn538), indicating that they are extracellular.
21264968	3	40	gly	O-glycosylation	1193:1207	arg2	multiple and potential O-glycosylation sites			multiple and potential O-glycosylation sites						sites	An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly).
21264968	3	104	gly	sites	1209:1213	arg1	the tandem repeats			sites	the tandem repeats					sites	An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly).
21264968	3	84	gly	glycoproteins	1252:1264	arg1	human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly)	mucin glycoproteins		Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly		PUBTATOR		mucin glycoproteins	100508689	Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly	An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly).
21264968	3	84	gly	glycoproteins	1252:1264	arg1	MUC5AC	MUC5AC		Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly		PUBTATOR		MUC5AC	4586	Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly	An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly).
21264968	3	84	gly	glycoproteins	1252:1264	arg1	MUC4	MUC4		Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly		PUBTATOR		MUC4	4585	Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly	An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly).
21264968	3	128	gly	glycoproteins	1252:1264	arg1	the tandem repeats	mucin glycoproteins		Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly	the tandem repeats	PUBTATOR		mucin glycoproteins	100508689	Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly	An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly).
21264968	3	84	gly	glycoproteins	1252:1264	arg1	human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly)	mucin glycoproteins		Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp		PUBTATOR		mucin glycoproteins	100508689	Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp	An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly).
21264968	3	84	gly	glycoproteins	1252:1264	arg1	MUC5AC	MUC5AC		Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp		PUBTATOR		MUC5AC	4586	Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp	An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly).
21264968	3	84	gly	glycoproteins	1252:1264	arg1	MUC4	MUC4		Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp		PUBTATOR		MUC4	4585	Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp	An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly).
21264968	3	128	gly	glycoproteins	1252:1264	arg1	the tandem repeats	mucin glycoproteins		Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp	the tandem repeats	PUBTATOR		mucin glycoproteins	100508689	Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp	An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly).
21264968	3	128	gly	glycoproteins	1252:1264	arg1	the tandem repeats	mucin glycoproteins			the tandem repeats	PUBTATOR		mucin glycoproteins	100508689		An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly).
27966990	2	3	part_of	VEGFR-2	290:296	arg1	The extracellular domain	VEGFR-2		The extracellular domain		PUBTATOR	Site	VEGFR-2	P35968	domain	The extracellular domain of VEGFR-2 is composed of seven immunoglobulin-like domains, each with multiple potential N-glycosylation sites (sequons).
22267737	6	20	part_of	contain	811:817	arg1	C8β AND three homologous subdomains	C8β		three homologous subdomains		PUBTATOR	Site	C8β 	732	subdomains	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	6	20	part_of	contain	811:817	arg1	C6 AND three homologous subdomains	C6, C8α,		subdomains		PUBTATOR	Site	C6, C8α,	731	subdomains	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
12799386	10	44	part_of	sites	1327:1331	arg1	ZP1	ZP1		sites		PUBTATOR	Site	ZP1	22786	sites	The zona proteins are highly glycosylated and 4/4 potential N-linkage sites on ZP1, 6/6 on ZP2, and 5/6 on ZP3 are occupied.
12799386	10	44	part_of	sites	1327:1331	arg1	ZP3	ZP3		sites		PUBTATOR	Site	ZP3	22788	sites	The zona proteins are highly glycosylated and 4/4 potential N-linkage sites on ZP1, 6/6 on ZP2, and 5/6 on ZP3 are occupied.
12799386	10	44	part_of	sites	1327:1331	arg1	6/6 on ZP2	ZP2		sites		PUBTATOR	Site	ZP2	22787	sites	The zona proteins are highly glycosylated and 4/4 potential N-linkage sites on ZP1, 6/6 on ZP2, and 5/6 on ZP3 are occupied.
7776966	12	45	gly	nonglycosylated	1952:1966	arg1	the resulting nonglycosylated FSHR	the resulting nonglycosylated FSHR				PUBTATOR		FSHR	2492		Similarly, when cells expressing the wild type FSHR were treated with tunicamycin to prevent N-linked glycosylation, the resulting nonglycosylated FSHR was not able to bind FSH.
17293352	12	58	gly	glycopeptides	2036:2048	arg2	glycopeptides			glycopeptides						glycopeptides	Using HPLC-mass spectrometry of glycopeptides, information was generated with respect to the site-specific location of the various glycans.
15385547	6	26	part_of	contain	974:980	arg1	the transmembrane regions AND the catalytic residues	the transmembrane regions		the catalytic residues						residues	The hydrophilic loops joining the transmembrane regions, which contain the catalytic residues, are facing the exoplasm.
14764083	9	65	gly	glycosylation	1291:1303	arg2	Asn281			Asn281						Asn281	This difference is due to glycosylation at Asn281 in bLF-A.
16476442	4	16	part_of	sACE	715:718	arg1	the N domain	ACE		the N domain		PUBTATOR	Site	ACE	1636	domain	Previously we determined the structure of testis ACE (C domain); here we present the crystal structure of the N domain of sACE (both in the presence and absence of the antihypertensive drug lisinopril) in order to aid the understanding of how these two domains differ in specificity and function.
26013384	8	53	part_of	Ser126	1023:1028	arg1	fully O-glycosylated rHu-EPO	EPO		Ser126		PUBTATOR	AminoAcid	EPO	2056	Ser126	It is concluded that the variant peak is non-O-glycosylated rHu-EPO and the main peak is fully O-glycosylated rHu-EPO at Ser126.
11533490	4	7	part_of	dimer	736:740	arg1	the membrane-proximal domains	dimer		the membrane-proximal domains		Fterm	Site	dimer		domains	Hormone binding induces a 20 angstrom closure between the membrane-proximal domains of the dimer.
1421757	1	40	part_of	containing	134:143	arg1	a glycoprotein AND three N-linked and one O-linked glycosylation sites	a glycoprotein		three N-linked and one O-linked glycosylation sites		Fterm	Site	glycoprotein		sites	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	1	40	part_of	containing	134:143	arg1	The human transferrin receptor AND three N-linked and one O-linked glycosylation sites	The human transferrin receptor		three N-linked and one O-linked glycosylation sites		PUBTATOR	Site	transferrin receptor	7018	sites	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
18227435	5	36	gly	O-glycosylated	873:886	arg1	(3) P17	3) P17		Thr10		PUBTATOR		3) P17	653820	Thr10	Our findings are as follows: (1) the N-terminal amino acid of P16 and P17 is pyroglutamic acid; (2) the Ser residue at the sixth position of P16 is phosphorylated; (3) P17 is O-glycosylated at Thr10; and (4) the C-terminal amino acid of P16 and P17 is truncated.
2386787	1	3	gly	Asn289-linked	164:176	arg1	the Asn289-linked oligosaccharide structures			Asn289	the Asn289-linked oligosaccharide structures					Asn289	A comparison has been made between the Asn289-linked oligosaccharide structures of human plasma plasminogen and a recombinant human plasminogen, expressed in lepidopteran insect (Spodoptera frugiperda) cells, after infection of these cells with a recombinant baculovirus containing the entire human plasminogen cDNA.
2386787	1	11	gly	plasminogen	221:231	arg1	the Asn289-linked oligosaccharide structures	plasminogen			the Asn289-linked oligosaccharide structures	OGER		plasminogen	P00747		A comparison has been made between the Asn289-linked oligosaccharide structures of human plasma plasminogen and a recombinant human plasminogen, expressed in lepidopteran insect (Spodoptera frugiperda) cells, after infection of these cells with a recombinant baculovirus containing the entire human plasminogen cDNA.
2386787	1	45	gly	plasminogen	257:267	arg1	the Asn289-linked oligosaccharide structures	plasminogen			the Asn289-linked oligosaccharide structures	OGER		plasminogen	P00747		A comparison has been made between the Asn289-linked oligosaccharide structures of human plasma plasminogen and a recombinant human plasminogen, expressed in lepidopteran insect (Spodoptera frugiperda) cells, after infection of these cells with a recombinant baculovirus containing the entire human plasminogen cDNA.
3524673	0	37	part_of	factor	44:49	arg1	Amino acid sequence	von Willebrand factor		Amino acid sequence		PUBTATOR	Site	von Willebrand factor	7450	sequence	Amino acid sequence of human von Willebrand factor.
12970363	10	5	gly	glycosylation	1397:1409	arg2	the e2 glycosylation site			the e2 glycosylation site						site	Elimination of the e2 glycosylation site, missing in the monoglycosylated TRPC3, was sufficient to convert the tightly receptor-regulated TRPC6 into a constitutively active channel, displaying functional characteristics of TRPC3.
12970363	10	21	gly	monoglycosylated	1432:1447	arg1	the monoglycosylated TRPC3	the monoglycosylated TRPC3				PUBTATOR		TRPC3	7222		Elimination of the e2 glycosylation site, missing in the monoglycosylated TRPC3, was sufficient to convert the tightly receptor-regulated TRPC6 into a constitutively active channel, displaying functional characteristics of TRPC3.
1457416	8	85	gly	HS-glycoprotein	1656:1670	arg1	alpha 2 HS-glycoprotein	alpha 2 HS-glycoprotein				PUBTATOR		alpha 2 HS-glycoprotein	197		On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	8	11	gly	possess	1685:1691	arg1	the A-chain AND two biantennary N-glycans	the A-chain			two biantennary N-glycans	Fterm		A-chain			On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	8	11	gly	possess	1685:1691	arg1	the A-chain AND two O-linked trisaccharides	the A-chain			two O-linked trisaccharides	Fterm		A-chain			On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
11983428	1	35	gly	glycoprotein	241:252	arg1	a cell surface transmembrane glycoprotein	a cell surface transmembrane glycoprotein				Fterm		glycoprotein			Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	1	35	gly	glycoprotein	241:252	arg1	Stromal interaction molecule 1	Stromal interaction molecule 1				PUBTATOR		Stromal interaction molecule 1	6786		Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
18596036	0	25	part_of	MASP-1/3	55:62	arg1	the CUB1-EGF-CUB2 domain	MASP-1/3		the CUB1-EGF-CUB2 domain		PUBTATOR	Site	MASP-1/3	5648	domain	Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins.
18596036	0	36	part_of	CUB1-EGF-CUB2	25:37	arg1	the CUB1-EGF-CUB2 domain	EGF		the CUB1-EGF-CUB2 domain		OGER	Site	EGF	P01133	domain	Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins.
3123586	2	27	part_of	apoC-III	194:201	arg1	The apoC-III polypeptide	apoC-III		The apoC-III polypeptide		PUBTATOR	Site	apoC-III	345	polypeptide	The apoC-III polypeptide contains a carbohydrate chain containing galactosamine, galactose, and sialic acid attached in O-linkage to a threonine residue at position 74.
19671700	10	72	gly	mannosylated	1606:1617	arg1	mannosylated Trp residues			mannosylated Trp residues						Trp residues	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
16342937	14	15	gly	N-glycosylation	2276:2290	arg2	nearly all potential N-glycosylation sites			nearly all potential N-glycosylation sites						sites	Last, nearly all potential N-glycosylation sites are occupied in the rat zonae glycoproteins (three of three for ZP1, six or seven of seven for ZP2, and four or five of six for ZP3).
16342937	14	37	gly	occupied	2302:2309	arg2	nearly all potential N-glycosylation sites			nearly all potential N-glycosylation sites						sites	Last, nearly all potential N-glycosylation sites are occupied in the rat zonae glycoproteins (three of three for ZP1, six or seven of seven for ZP2, and four or five of six for ZP3).
16342937	14	102	gly	glycoproteins	2328:2340	arg1	the rat zonae glycoproteins	the rat zonae glycoproteins				Fterm		glycoproteins			Last, nearly all potential N-glycosylation sites are occupied in the rat zonae glycoproteins (three of three for ZP1, six or seven of seven for ZP2, and four or five of six for ZP3).
1709161	6	53	part_of	BP-4	724:727	arg1	The prepeptide sequences	BP-4 and -5		The prepeptide sequences		PUBTATOR	Site	BP-4 and -5	Q13323	sequences	The prepeptide sequences of BP-4 and -5 contain 27 and 21, the mature proteins 213 and 237 amino acids, respectively (Mr = 22,610 and 25,980).
1709161	6	94	part_of	-5	733:734	arg1	The prepeptide sequences	BP-4 and -5		The prepeptide sequences		PUBTATOR	Site	BP-4 and -5	Q13323	sequences	The prepeptide sequences of BP-4 and -5 contain 27 and 21, the mature proteins 213 and 237 amino acids, respectively (Mr = 22,610 and 25,980).
28252640	0	32	part_of	SV2C	117:120	arg1	the luminal domain	SV2C		the luminal domain		PUBTATOR	Site	SV2C	9900	domain	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	0	44	part_of	BoNT/A2	25:31	arg1	the BoNT/A2 receptor-binding domain	structure of the BoNT		the BoNT/A2 receptor-binding domain		Cterm	Site	structure of the BoNT		domain	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
16037490	8	61	gly	glycopeptide	1824:1835	arg2	the enriched glycopeptide			the enriched glycopeptide						glycopeptide	The results also demonstrated that the enriched glycopeptide provides resources for site-specific analysis of oligosaccharides in glycoproteomics.
10894551	7	53	part_of	ANP-binding	1020:1030	arg1	the ANP-binding site	ANP		the ANP-binding site		OGER	Site	ANP	P01160	site	From affinity labelling and mutagenesis studies, the ANP-binding site maps to the side of the dimer crevice and extends to near the dimer interface.
1900431	0	18	part_of	factor	101:106	arg1	the epidermal growth factor domain	factor		the epidermal growth factor domain		Fterm	Site	factor		domain	Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
8636209	8	53	gly	glycosylation	1015:1027	arg1	TCR assembly	TCR assembly				PUBTATOR		TCR	6962		In contrast, treatment of T cells with tunicamycin suggested that N-linked glycosylation of CD3 delta is required for TCR assembly.
8636209	8	53	gly	glycosylation	1015:1027	arg1	CD3 delta	CD3 delta				PUBTATOR		CD3 delta	915		In contrast, treatment of T cells with tunicamycin suggested that N-linked glycosylation of CD3 delta is required for TCR assembly.
7460900	0	40	gly	casein	55:60	arg1	the sugar part	casein			the sugar part	Fterm		casein			Localisation and importance of the sugar part of human casein.
18642129	7	11	gly	sialylated	1136:1145	arg1	triantennary sialylated glycans				triantennary sialylated glycans						LC-ESIMS/MS analysis revealed that both light chain and heavy chain were N-glycosylated mainly by A2S2 but also by triantennary sialylated glycans.
18642129	7	20	gly	N-glycosylated	1081:1094	arg1	heavy chain	chain				OGER		chain	P08709		LC-ESIMS/MS analysis revealed that both light chain and heavy chain were N-glycosylated mainly by A2S2 but also by triantennary sialylated glycans.
18795891	10	44	gly	glycoprotein	1602:1613	arg1	the collagen receptor GPVI (glycoprotein VI) and integrin alpha6beta1, but not the von Willebrand receptor GPIbalpha	the collagen receptor GPVI (glycoprotein VI) and integrin alpha6beta1, but not the von Willebrand receptor GPIbalpha				PUBTATOR		glycoprotein VI	51206		Finally, Tspan9 was shown to be a component of tetraspanin microdomains that included the collagen receptor GPVI (glycoprotein VI) and integrin alpha6beta1, but not the von Willebrand receptor GPIbalpha or the integrins alphaIIbbeta3 or alpha2beta1.
8323280	4	93	gly	fucosylated	1109:1119	arg1	a fucosylated mannose core				a fucosylated mannose core						After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
21757702	4	36	part_of	EGF	593:595	arg1	the site	EGF		the site		OGER	Site	EGF	P01133	site	For instance, although most sites are modified at high stoichiometries, the site at EGF 27 is only partially glucosylated, and the occupancy of the site at EGF 4 varies with cell type.
21757702	4	60	part_of	EGF	665:667	arg1	the site	EGF 4		the site		OGER	Site	EGF 4	P01133	site	For instance, although most sites are modified at high stoichiometries, the site at EGF 27 is only partially glucosylated, and the occupancy of the site at EGF 4 varies with cell type.
11258925	0	38	gly	glycosylation	24:36	arg2	the glycosylation sites			the glycosylation sites						sites	Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry.
23269669	1	7	part_of	Guanylyl	189:196	arg1	a multidomain	Guanylyl cyclase C		a multidomain		PUBTATOR	Site	Guanylyl cyclase C	2984	multidomain	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
23269669	1	59	part_of	cyclase	198:204	arg1	a multidomain	Guanylyl cyclase C		a multidomain		PUBTATOR	Site	Guanylyl cyclase C	2984	multidomain	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
21264968	4	27	gly	glycosylated	1611:1622	arg1	densely glycosylated MUC4	densely glycosylated MUC4				PUBTATOR		MUC4	4585		In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	44	gly	Thr1	1665:1668	arg1	six α-GalNAc residues			residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	six α-GalNAc residues					residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	98	gly	O-glycosylation	1413:1427	arg1	naked MUC4 peptide			naked MUC4 peptide						peptide	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	98	gly	O-glycosylation	1413:1427	arg1	Thr10			Thr10						Thr10	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	127	gly	containing	1629:1638	arg1	densely glycosylated MUC4 AND six α-GalNAc residues	densely glycosylated MUC4		Thr15	six α-GalNAc residues	PUBTATOR	AminoAcid	MUC4	4585	residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
20356844	0	3	part_of	N-terminal	96:105	arg1	sucrase-isomaltase N-terminal domains	sucrase-isomaltase N-terminal		sucrase-isomaltase N-terminal domains		PUBTATOR	Site	sucrase-isomaltase N-terminal	6476	domains	Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
20356844	0	49	part_of	sucrase-isomaltase	77:94	arg1	sucrase-isomaltase N-terminal domains	sucrase-isomaltase N-terminal		sucrase-isomaltase N-terminal domains		PUBTATOR	Site	sucrase-isomaltase N-terminal	6476	domains	Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
18642129	11	45	gly	difucosylated	1589:1601	arg1	triantennary difucosylated structures				triantennary difucosylated structures						Glycan sequencing using different glycanases led to the identification of triantennary difucosylated structures.
3191509	2	2	gly	glycoproteins	280:292	arg1	smaller-sized glycoproteins	smaller-sized glycoproteins				Fterm		glycoproteins			phenol and separated from the bulk of smaller-sized glycoproteins by exclusion on Sephacryl S400.
8416919	0	62	gly	kallidinogenase	102:116	arg1	GalNAc-containing N-linked oligosaccharides	kallidinogenase			GalNAc-containing N-linked oligosaccharides	Fterm		kallidinogenase			Structural elucidation of a variety of GalNAc-containing N-linked oligosaccharides from human urinary kallidinogenase.
1451807	1	0	gly	O-glycosylation	65:79	arg2	Thr7			Thr7						Thr7	Variable O-glycosylation at Thr7, proteolytic processing, and allelic variation.
10731668	4	35	gly	glycosylation	671:683	arg2	this atypical glycosylation site			this atypical glycosylation site						site	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
19838169	2	4	gly	glycoproteins	168:180	arg1	Sialylated glycoproteins	Sialylated glycoproteins				Fterm		glycoproteins			Sialylated glycoproteins were selectively periodate-oxidized, captured on hydrazide beads, trypsinized and released by acid hydrolysis of sialic acid glycosidic bonds.
22664871	3	9	part_of	N-terminal	489:498	arg1	the N-terminal fragment	N-terminal		the N-terminal fragment		Cterm	Site	N-terminal		fragment	In this article, we report the 2.7-Å crystal structure of human RANKL trimer in complex with the N-terminal fragment of human OPG containing four cysteine-rich TNFR homologous domains (OPG-CRD).
22664871	3	44	part_of	OPG	518:520	arg1	the N-terminal fragment	OPG		the N-terminal fragment		PUBTATOR	Site	OPG	4982	fragment	In this article, we report the 2.7-Å crystal structure of human RANKL trimer in complex with the N-terminal fragment of human OPG containing four cysteine-rich TNFR homologous domains (OPG-CRD).
22664871	3	12	part_of	containing	522:531	arg1	human OPG AND four cysteine-rich TNFR homologous domains	human OPG		four cysteine-rich TNFR homologous domains		PUBTATOR	Site	OPG	4982	domains	In this article, we report the 2.7-Å crystal structure of human RANKL trimer in complex with the N-terminal fragment of human OPG containing four cysteine-rich TNFR homologous domains (OPG-CRD).
24342833	3	35	part_of	β-catenin	489:497	arg1	identified sites	-catenin		identified sites		PUBTATOR	Site	-catenin	1499	sites	OBJECTIVE: The objectives of this investigation were to identify the putative O-GlcNAc sites of β-catenin and the relevance of identified sites in the regulation of β-catenin's localization and transcriptional activity.
7535613	12	79	part_of	serine	1800:1805	arg1	trypsin	trypsin		serine		Fterm	AminoAcid	trypsin		serine	The bottom of the substrate specificity pocket, residue S1, is a serine (Ser 189) as in chymotrypsin, rather than aspartate (Asp 189) as in tonin, kallikrein, and trypsin.
7535613	12	79	part_of	serine	1800:1805	arg1	kallikrein	kallikrein		serine		PUBTATOR	AminoAcid	kallikrein	9622	serine	The bottom of the substrate specificity pocket, residue S1, is a serine (Ser 189) as in chymotrypsin, rather than aspartate (Asp 189) as in tonin, kallikrein, and trypsin.
7535613	12	79	part_of	serine	1800:1805	arg1	chymotrypsin	chymotrypsin		serine		Fterm	AminoAcid	chymotrypsin		serine	The bottom of the substrate specificity pocket, residue S1, is a serine (Ser 189) as in chymotrypsin, rather than aspartate (Asp 189) as in tonin, kallikrein, and trypsin.
30659065	4	60	part_of	have	838:841	arg1	IgGs AND a single N-glycosylation site	IgGs		a single N-glycosylation site		Cterm	Site	IgGs		site	Although IgGs usually have a single N-glycosylation site and are well studied, other antibody isotypes, e.g. IgA and IgM, that are the first responders in certain diseases, have two to five sites/monomer of antibody, and little is known about their N-glycosylation.
25908590	4	42	part_of	IL1RAPL1	729:736	arg1	The first immunoglobulin-like (Ig) domain	IL1RAPL1		The first immunoglobulin-like (Ig) domain		PUBTATOR	Site	IL1RAPL1	11141	domain	The first immunoglobulin-like (Ig) domain of IL1RAPL1 directly recognizes the first splice insert, which is critical for binding to IL1RAPL1.
8172892	4	82	part_of	AP	645:646	arg1	residues 157-165	AP alpha		residues 157-165		PUBTATOR	SpecificSite	AP alpha	2028	residues 157-165	A nonapeptide (AP alpha-D4, residues 157-165) and an undecapeptide (AP alpha-D5, 166-176) derived from AP alpha contained Thr-159 and Thr-169, neither of which could be identified using a gas-phase protein sequencer.
8172892	4	71	part_of	contained	742:750	arg1	AP alpha-D5, 166-176 AND Thr-159	AP alpha		Thr-159 and Thr-169		PUBTATOR	SpecificSite	AP alpha	2028	Thr-159 and Thr-169	A nonapeptide (AP alpha-D4, residues 157-165) and an undecapeptide (AP alpha-D5, 166-176) derived from AP alpha contained Thr-159 and Thr-169, neither of which could be identified using a gas-phase protein sequencer.
16321355	0	33	gly	N-glycosylation	14:28	arg1	human plasma ceruloplasmin	human plasma ceruloplasmin				PUBTATOR		ceruloplasmin	1356		Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry.
15350125	0	39	part_of	transporter	137:147	arg1	the extracellular binding domains	apical sodium-dependent bile acid transporter		the extracellular binding domains		PUBTATOR	Site	apical sodium-dependent bile acid transporter	6555	domains	Topology scanning and putative three-dimensional structure of the extracellular binding domains of the apical sodium-dependent bile acid transporter (SLC10A2).
21676880	4	19	gly	glycosylation	811:823	arg1	the post-translational site			the post-translational site						site	Mutations that ablate the co-translational site concomitantly reduce glycosylation at the post-translational site, resulting in unglycosylated KCNE1 subunits that cannot reach the cell surface with their cognate K(+) channel.
21676880	4	34	gly	unglycosylated	870:883	arg1	unglycosylated KCNE1 subunits	unglycosylated KCNE1 subunits				PUBTATOR		KCNE1 subunits	3753		Mutations that ablate the co-translational site concomitantly reduce glycosylation at the post-translational site, resulting in unglycosylated KCNE1 subunits that cannot reach the cell surface with their cognate K(+) channel.
1991473	2	0	gly	N-glycosylated	268:281	arg1	hLH beta	hLH beta		Asn30		PUBTATOR		hLH beta	3972	Asn30	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	2	11	gly	N-glycosylated	219:232	arg2	Asn52			Asn52 and Asn78						Asn52 and Asn78	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	2	11	gly	N-glycosylated	219:232	arg1	hLH alpha	hLH alpha		Asn52 and Asn78		PUBTATOR		hLH alpha	1081	Asn52 and Asn78	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	2	11	gly	N-glycosylated	219:232	arg1	hLH alpha	hLH alpha		Asn52 and Asn78		PUBTATOR		hLH alpha	1081	Asn52 and Asn78	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
20944746	9	2	part_of	β-chain	1781:1787	arg1	both the V and C domains	TCR β-chain		both the V and C domains		PUBTATOR	Site	TCR β-chain	6962	domains	Accordingly, we provide a mechanism of pre-TCR self-association that allows the pre-Tα chain to simultaneously 'sample' the correct folding of both the V and C domains of any TCR β-chain, regardless of its ultimate specificity, which represents a critical checkpoint in T-cell development.
108268	0	31	gly	chain	44:48	arg1	the oligosaccharide	J chain			the oligosaccharide	PUBTATOR		J chain	3512		Structure of the oligosaccharide of human J chain.
21148085	2	7	part_of	proteins	311:318	arg1	C-terminal propeptides	proteins		C-terminal propeptides		Fterm	Site	proteins		propeptides	VEGFR-3 ligands VEGF-C and VEGF-D are produced as precursor proteins with long N- and C-terminal propeptides and show enhanced VEGFR-2 and VEGFR-3 binding on proteolytic removal of the propeptides.
8286855	9	66	part_of	GpA	1315:1317	arg1	the extracellular domain	GpA		the extracellular domain		PUBTATOR	Site	GpA	2993	domain	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
7654718	2	25	part_of	BAL	438:440	arg1	the C-tail fragment	BAL		the C-tail fragment		OGER	Site	BAL	P19835	fragment	A large-scale purification method has been devised to purify the C-tail fragment from human milk BAL.
7654718	2	38	part_of	C-tail	406:411	arg1	the C-tail fragment	C-tail		the C-tail fragment		Cterm	Site	C-tail		fragment	A large-scale purification method has been devised to purify the C-tail fragment from human milk BAL.
1993171	10	3	gly	used	1315:1318	arg2	the potential N-glycosylation sites			the potential N-glycosylation sites						sites	Sequence analysis of the peptides containing the third and fifth cysteines of human IL-4 also demonstrated that only one of the potential N-glycosylation sites is used by C127 mammary tumor cells.
1993171	10	46	gly	N-glycosylation	1290:1304	arg2	the potential N-glycosylation sites			the potential N-glycosylation sites						sites	Sequence analysis of the peptides containing the third and fifth cysteines of human IL-4 also demonstrated that only one of the potential N-glycosylation sites is used by C127 mammary tumor cells.
16107205	3	21	gly	glycosylation	708:720	arg1	Asn-243			Asn-243						Asn-243	Human DNase X, ectopically expressed in HeLa S3 cells, is located in the ER (endoplasmic reticulum) and is modified by an N-linked glycosylation at Asn-243.
18308854	7	5	gly	utilized	1434:1441	arg2	the potential glycosylation site			the potential glycosylation site						site	These studies revealed that oatp1a1 is a 12-transmembrane-domain protein in which the second and fifth extracellular loops are glycosylated at asparagines 124, 135, and 492, whereas the potential glycosylation site at asparagine 62 is not utilized, consistent with its position in a transmembrane domain.
18308854	7	5	gly	utilized	1434:1441	arg2	asparagine 62			asparagine 62						asparagine 62	These studies revealed that oatp1a1 is a 12-transmembrane-domain protein in which the second and fifth extracellular loops are glycosylated at asparagines 124, 135, and 492, whereas the potential glycosylation site at asparagine 62 is not utilized, consistent with its position in a transmembrane domain.
18308854	7	58	gly	glycosylation	1391:1403	arg2	the potential glycosylation site			the potential glycosylation site						site	These studies revealed that oatp1a1 is a 12-transmembrane-domain protein in which the second and fifth extracellular loops are glycosylated at asparagines 124, 135, and 492, whereas the potential glycosylation site at asparagine 62 is not utilized, consistent with its position in a transmembrane domain.
18308854	7	58	gly	glycosylation	1391:1403	arg2	asparagine 62			asparagine 62						asparagine 62	These studies revealed that oatp1a1 is a 12-transmembrane-domain protein in which the second and fifth extracellular loops are glycosylated at asparagines 124, 135, and 492, whereas the potential glycosylation site at asparagine 62 is not utilized, consistent with its position in a transmembrane domain.
18308854	7	69	gly	glycosylated	1322:1333	arg2	asparagines 124, 135, and 492	protein		asparagines 124, 135, and 492		Fterm		protein		asparagines 124, 135, and 492	These studies revealed that oatp1a1 is a 12-transmembrane-domain protein in which the second and fifth extracellular loops are glycosylated at asparagines 124, 135, and 492, whereas the potential glycosylation site at asparagine 62 is not utilized, consistent with its position in a transmembrane domain.
3356193	6	72	gly	fucosylated	830:840	arg1	the porcine N-glycan				the porcine N-glycan						In addition, the porcine N-glycan is fucosylated to about 80% in alpha 1----6 linkage to the GlcNAc-1 residue.
26496195	10	70	gly	proteins	1683:1690	arg1	the EGF repeats	proteins			the EGF repeats	Fterm		proteins			Mutations in human POGLUT1 cause Dowling-Degos Disease, POGLUT1 is overexpressed in a variety of tumor cells, and mutations in the EGF repeats of human CRUMBS proteins are associated with human congenital nephrosis, retinitis pigmentosa and retinal degeneration, suggesting that O-glucosylation of CRUMBS proteins has broad roles in human health.
10712595	0	8	gly	has	20:22	arg1	Salmon antithrombin AND only three carbohydrate side chains	Salmon antithrombin			only three carbohydrate side chains	PUBTATOR		antithrombin	462		Salmon antithrombin has only three carbohydrate side chains, and shows functional similarities to human beta-antithrombin.
1388166	8	31	part_of	contains	1484:1491	arg1	TFPI AND the sequence Pro-Phe-Lys, 9 residues	TFPI		the sequence Pro-Phe-Lys, 9 residues		PUBTATOR	Site	TFPI	7035	residues	TFPI contains the sequence Pro-Phe-Lys, 9 residues N-terminal to the glycosylation site at position 228; this tripeptide may act as the recognition sequence for the GalNAc-transferase.
8798614	0	70	gly	glycosylation	34:46	arg2	potential sites			potential sites						sites	Elimination of potential sites of glycosylation fails to abrogate complement regulatory function of cell surface CD59.
23345538	6	6	gly	glycosylation	1246:1258	arg2	118 glycosylation sites			118 glycosylation sites						sites	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	6	11	gly	glycopeptide	1158:1169	arg2	Direct glycopeptide analysis			Direct glycopeptide analysis						glycopeptide	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	6	1	gly	glycopeptides	1207:1219	arg1	59 proteins	proteins		sites		Fterm		proteins		sites	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	6	1	gly	glycopeptides	1207:1219	arg2	131 glycopeptides	proteins		glycopeptides		Fterm		proteins		glycopeptides	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
11741940	6	81	part_of	sFRP-1	1131:1136	arg1	an NTR-type domain	sFRP-1		domain		PUBTATOR	Site	sFRP-1	6422	domain	This latter set of assignments provides experimental verification of one of the disulfide patterns proposed for netrin (NTR) modules and thereby supports the prediction that the C-terminal heparin-binding domain of sFRP-1 is an NTR-type domain.
16877748	8	56	part_of	sICAM-1	1437:1443	arg1	The N-glycosylation sites	sICAM-1		The N-glycosylation sites		Cterm	Site	sICAM-1	3383	sites	The N-glycosylation sites of mouse sICAM-1 were analyzed by MALDI-Fourier transform ion cyclotron resonance (FTICR)-MS and nanoLC-ESI-FTICR-MS of tryptic digests of mouse sICAM-1 expressed in the Lec1 mutant of CHO cells.
7309709	5	26	gly	prothrombin	645:655	arg1	the asparagine-linked sugar chains	prothrombin			the asparagine-linked sugar chains	PUBTATOR		prothrombin	2147		By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	5	30	gly	asparagine-linked	605:621	arg1	the asparagine-linked sugar chains			asparagine	the asparagine-linked sugar chains					asparagine	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
21757702	0	47	part_of	sites	82:86	arg1	mouse Notch1	Notch1		sites		PUBTATOR	Site	Notch1	18128	sites	O-glucose trisaccharide is present at high but variable stoichiometry at multiple sites on mouse Notch1.
9153399	6	9	part_of	residue	1035:1041	arg1	fibronectin	fibronectin		residue		PUBTATOR	AminoAcid	fibronectin	2335	aspartic acid residue	The glutamic acid residue at position 37 is critical for LFA-1 binding and is proposed to coordinate the Mg2+ ion in the I domain; this Glu 37 is surrounded by a relatively flat recognition surface and lies in a beta-strand, whereas the critical aspartic acid residue in VCAM-1 and fibronectin lie in protruding loops.
9153399	6	9	part_of	residue	1035:1041	arg1	VCAM-1	VCAM-1		residue		PUBTATOR	AminoAcid	VCAM-1	7412	aspartic acid residue	The glutamic acid residue at position 37 is critical for LFA-1 binding and is proposed to coordinate the Mg2+ ion in the I domain; this Glu 37 is surrounded by a relatively flat recognition surface and lies in a beta-strand, whereas the critical aspartic acid residue in VCAM-1 and fibronectin lie in protruding loops.
10878002	4	24	gly	C-Mannosylation	555:569	arg1	human RNase 2	human RNase 2				PUBTATOR		RNase 2	6036		C-Mannosylation was first found in human RNase 2 and interleukin-12.
10878002	4	24	gly	C-Mannosylation	555:569	arg1	interleukin-12	interleukin-12				OGER		interleukin-12			C-Mannosylation was first found in human RNase 2 and interleukin-12.
10878002	4	36	gly	found	581:585	arg2	human RNase 2 AND C-Mannosylation	human RNase 2			C-Mannosylation	PUBTATOR		RNase 2	6036		C-Mannosylation was first found in human RNase 2 and interleukin-12.
10878002	4	36	gly	found	581:585	arg2	interleukin-12 AND C-Mannosylation	interleukin-12			C-Mannosylation	OGER		interleukin-12			C-Mannosylation was first found in human RNase 2 and interleukin-12.
3264725	8	51	gly	glycosylated	1667:1678	arg1	asparagine residue 145			asparagine residue 145						asparagine residue 145	In the recombinant factor VIIa, asparagine residue 322 was fully glycosylated whereas asparagine residue 145 was only partially (approximately 66%) glycosylated.
3264725	8	62	gly	glycosylated	1584:1595	arg1	asparagine residue 322	factor VIIa		asparagine residue 322		Cterm		factor VIIa		asparagine residue 322	In the recombinant factor VIIa, asparagine residue 322 was fully glycosylated whereas asparagine residue 145 was only partially (approximately 66%) glycosylated.
3264725	8	62	gly	glycosylated	1584:1595	arg2	asparagine residue 322	factor VIIa		asparagine residue 322		Cterm		factor VIIa		asparagine residue 322	In the recombinant factor VIIa, asparagine residue 322 was fully glycosylated whereas asparagine residue 145 was only partially (approximately 66%) glycosylated.
3264725	8	62	gly	glycosylated	1584:1595	arg2	asparagine residue 322			asparagine residue 322						asparagine residue 322	In the recombinant factor VIIa, asparagine residue 322 was fully glycosylated whereas asparagine residue 145 was only partially (approximately 66%) glycosylated.
2040275	1	12	gly	glycosylation	265:277	arg2	a single asparagine glycosylation site			a single asparagine glycosylation site						site	1H-NMR spectroscopy has been used to study the conformation and dynamics of the isolated tailpiece from human serum immunoglobulin M, a 22-residue peptide containing a single asparagine glycosylation site.
12171601	4	87	gly	glycosylation	929:941	arg2	both glycosylation sequons			both glycosylation sequons							FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
23050552	3	16	part_of	contain	346:352	arg1	The beta and gamma subunits AND one N-glycosylation site	The beta and gamma subunits		one N-glycosylation site		Fterm	Site	subunits		site	The beta and gamma subunits each contain one N-glycosylation site, each of which is occupied by a biantennary N-glycan.
8223648	7	39	gly	contain	746:752	arg1	protein AND only the core oligosaccharide	protein			only the core oligosaccharide	Fterm		protein			265, 9290-9295], the insect cell produced protein which was demonstrated by lectin blot, mass spectroscopy and HPLC analysis to contain only the core oligosaccharide.
22128166	5	25	part_of	TIM	767:769	arg1	a catalytic TIM barrel domain	TIM		a catalytic TIM barrel domain		OGER	Site	TIM	P60174	domain	Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2.
25485983	4	30	part_of	antithrombin	637:648	arg1	this defective glycosylation site	antithrombin		this defective glycosylation site		PUBTATOR	Site	antithrombin	462	site	We evaluated the effect of the aromatic sequon in this defective glycosylation site of antithrombin, despite of being located in a loop between the helix D and the strand 2A.
7694285	7	5	gly	glycosylation	1089:1101	arg2	three putative glycosylation sites			three putative glycosylation sites						sites	The polypeptide has three putative glycosylation sites and one hydrophobic domain at the C terminus.
8407981	0	51	gly	glycosylation	5:17	arg1	cytochrome P-450	cytochrome P-450(arom)				PUBTATOR		cytochrome P-450(arom)	55010		Core glycosylation of cytochrome P-450(arom).
7525874	0	27	gly	protein	38:44	arg1	Carbohydrate structures	beta-trace protein			Carbohydrate structures	PUBTATOR		beta-trace protein	5730		Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.
3542030	6	55	part_of	terminus	776:783	arg1	an additional leucine	terminus		an additional leucine						leucine	24, 815] have an additional leucine at the amino terminus, making a total of 373 residues in the chain.
9334252	4	18	part_of	Trp-7	688:692	arg1	The enzyme	enzyme		Trp-7		Fterm	SpecificSite	enzyme		Trp-7	The enzyme was C-mannosylated at Trp-7, showing that the modification occurs intracellularly, before secretion of the protein.
3651384	1	44	gly	glycoprotein	102:113	arg1	SGP-2	SGP-2				PUBTATOR		2 (SGP-2	24854		Sulfated glycoprotein 2 (SGP-2) is the major protein secreted by rat Sertoli cells.
3651384	1	44	gly	glycoprotein	102:113	arg1	the major protein	the major protein				Fterm		protein			Sulfated glycoprotein 2 (SGP-2) is the major protein secreted by rat Sertoli cells.
3651384	1	44	gly	glycoprotein	102:113	arg1	Sulfated glycoprotein 2	Sulfated glycoprotein 2				PUBTATOR		Sulfated glycoprotein 2	24854		Sulfated glycoprotein 2 (SGP-2) is the major protein secreted by rat Sertoli cells.
20188224	11	66	part_of	PGRN	1558:1561	arg1	four out of five potential PGRN N-glycosylation consensus sites	PGRN		four out of five potential PGRN N-glycosylation consensus sites		PUBTATOR	Site	PGRN	2896	sites	Glycosylation of four out of five potential PGRN N-glycosylation consensus sites was demonstrated (the final one remains undetermined), with one of the four observed to be partially occupied.
1569071	8	76	gly	desialylated	1587:1598	arg1	the desialylated precursors	the desialylated precursors				Fterm		precursors			When the desialylated precursors of IGF-II were treated with O-glycosidase, but not when treated with N-glycosidase, the Mr values were reduced further to about 10,000.
20879038	5	77	gly	proline-rich	764:775	arg1	basic proline-rich protein 2			proline	basic proline-rich protein 2					proline	Through the salivary peptidome characterization of 20 different subjects from Control, Diabetic, and Head and Neck Cancer groups, it was possible to identify the following species: (i) N-glycosylation sites: two in basic proline-rich protein 2 (bPRP2), one in bPRP3 and one in bPRP4; (ii) O-glycosylation sites: two in bPRP2 and one in aPRP; (iii) other terminal monosaccharide sites: six in bPRP1, two in bPRP2 and two in bPRP3; (iv) other modifications such as N-terminal pyro-Glu (two in bPRP1, six in bPRP2, eight in bPRP3 and nine in bPRP4); (v) phosphorylation in serine, three in bPRP1, one in bPRP2, one in bPRP3 and one in aPRP1; (vi) bPRP1 (allele S, allele M and variant CP5) and bPRP4 (allele M).
20879038	5	77	gly	proline-rich	764:775	arg1	bPRP2			proline	bPRP2					proline	Through the salivary peptidome characterization of 20 different subjects from Control, Diabetic, and Head and Neck Cancer groups, it was possible to identify the following species: (i) N-glycosylation sites: two in basic proline-rich protein 2 (bPRP2), one in bPRP3 and one in bPRP4; (ii) O-glycosylation sites: two in bPRP2 and one in aPRP; (iii) other terminal monosaccharide sites: six in bPRP1, two in bPRP2 and two in bPRP3; (iv) other modifications such as N-terminal pyro-Glu (two in bPRP1, six in bPRP2, eight in bPRP3 and nine in bPRP4); (v) phosphorylation in serine, three in bPRP1, one in bPRP2, one in bPRP3 and one in aPRP1; (vi) bPRP1 (allele S, allele M and variant CP5) and bPRP4 (allele M).
20879038	5	77	gly	proline-rich	764:775	arg1	one			proline	one					proline	Through the salivary peptidome characterization of 20 different subjects from Control, Diabetic, and Head and Neck Cancer groups, it was possible to identify the following species: (i) N-glycosylation sites: two in basic proline-rich protein 2 (bPRP2), one in bPRP3 and one in bPRP4; (ii) O-glycosylation sites: two in bPRP2 and one in aPRP; (iii) other terminal monosaccharide sites: six in bPRP1, two in bPRP2 and two in bPRP3; (iv) other modifications such as N-terminal pyro-Glu (two in bPRP1, six in bPRP2, eight in bPRP3 and nine in bPRP4); (v) phosphorylation in serine, three in bPRP1, one in bPRP2, one in bPRP3 and one in aPRP1; (vi) bPRP1 (allele S, allele M and variant CP5) and bPRP4 (allele M).
19413349	6	27	gly	glycosylation	1078:1090	arg2	the two extracellular N-linked glycosylation sites			the two extracellular N-linked glycosylation sites						sites	Likewise, mutation of the two extracellular N-linked glycosylation sites gave a melanopsin size comparable to that of PNGase F or tunicamycin treatment (55 kDa).
28327546	7	51	gly	glycosylation	806:818	arg1	N582			N582						N582	Selected mutations also lead to partial glycosylation of N582, suggesting that rapid folding of local conformation prevents glycosylation of this site in wild-type FVIII.
28327546	7	60	gly	glycosylation	890:902	arg1	wild-type FVIII	FVIII		site		PUBTATOR		FVIII	2157	site	Selected mutations also lead to partial glycosylation of N582, suggesting that rapid folding of local conformation prevents glycosylation of this site in wild-type FVIII.
11067851	8	1	gly	carry	1113:1117	arg1	Thr-489 AND the O-linked disaccharide			Ser-377, Thr-432, and Thr-489	the O-linked disaccharide					Ser-377, Thr-432, and Thr-489	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	8	1	gly	carry	1113:1117	arg1	Ser-377 AND the O-linked disaccharide			Ser-377, Thr-432, and Thr-489	the O-linked disaccharide					Ser-377, Thr-432, and Thr-489	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	8	1	gly	carry	1113:1117	arg1	Ser-377 AND the O-linked disaccharide			Ser-377, Thr-432, and Thr-489	the O-linked disaccharide					Ser-377, Thr-432, and Thr-489	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
479158	5	26	gly	glycopeptides	293:305	arg2	glycopeptides			glycopeptides						glycopeptides	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
28489325	1	40	gly	N-glycosylation	258:272	arg2	seven N-glycosylation sites			seven N-glycosylation sites						sites	L-Selectin, a cell-adhesion receptor on the surface of most leukocytes, contains seven N-glycosylation sites.
12214108	3	9	part_of	protein	414:420	arg1	residue 183	protein		residue 183		Fterm	SpecificSite	protein		residue 183	One pathogenic mutation, Thr to Ala at residue 183 of the human prion protein, blocks addition of the first glycan to the Asp residue 181.
10386995	5	8	gly	sites	935:939	arg1	synapsin I	synapsin I			sites	PUBTATOR		synapsin I	24949		The proximity of phosphorylation sites to O-GlcNAcylation sites in the regulatory domains of synapsin I suggests that O-GlcNAcylation may modulate phosphorylation and indirectly affect synapsin I interactions.
10386995	5	8	gly	sites	935:939	arg1	the regulatory domains			the regulatory domains	the regulatory domains		Site			domains	The proximity of phosphorylation sites to O-GlcNAcylation sites in the regulatory domains of synapsin I suggests that O-GlcNAcylation may modulate phosphorylation and indirectly affect synapsin I interactions.
7096333	0	0	gly	ceruloplasmin	81:93	arg1	the carbohydrate chains	ceruloplasmin			the carbohydrate chains	PUBTATOR		ceruloplasmin	1356		The structures and microheterogeneity of the carbohydrate chains of human plasma ceruloplasmin.
7096333	0	8	gly	microheterogeneity	19:36	arg1	the carbohydrate chains				the carbohydrate chains						The structures and microheterogeneity of the carbohydrate chains of human plasma ceruloplasmin.
6689265	0	5	gly	protein	84:90	arg1	the O-glycan chain	vitamin-D binding protein			the O-glycan chain	PUBTATOR		vitamin-D binding protein	2638		Isolation and characterization of the O-glycan chain of the human vitamin-D binding protein.
16740002	0	8	gly	glycoprotein	60:71	arg1	glycoprotein capture	glycoprotein capture				Fterm		glycoprotein			Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
16740002	0	40	gly	glycoproteins	27:39	arg1	N-linked glycoproteins	N-linked glycoproteins				Fterm		glycoproteins			Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
2023947	3	49	gly	attached	502:509	arg2	threonine AND a single monosaccharide			threonine	a single monosaccharide					threonine	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	49	gly	attached	502:509	arg2	a single monosaccharide AND the peptide			the peptide	a single monosaccharide					peptide	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	49	gly	attached	502:509	arg2	threonine AND An unusual carbohydrate-protein linkage			threonine	An unusual carbohydrate-protein linkage					threonine	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	49	gly	attached	502:509	arg2	An unusual carbohydrate-protein linkage AND the peptide			the peptide	An unusual carbohydrate-protein linkage					peptide	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	49	gly	attached	502:509	arg2	threonine AND fucose			threonine	fucose					threonine	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	49	gly	attached	502:509	arg2	fucose AND the peptide			the peptide	fucose					peptide	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
12847106	0	35	gly	O-glycosylated	15:28	arg1	Plakoglobin	Plakoglobin				Fterm		Plakoglobin			Plakoglobin is O-glycosylated close to the N-terminal destruction box.
12839991	7	1	part_of	NgR	1131:1133	arg1	NgR surface residues	NgR		NgR surface residues		OGER	Site	NgR	Q9BZR6	residues	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
22826440	1	27	gly	found	184:188	arg1	the neuronal protein AP180 AND Phosphorylated O-GlcNAc	the neuronal protein AP180			Phosphorylated O-GlcNAc	PUBTATOR		AP180	65178		Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
28775322	2	60	gly	glycosylate	369:379	arg1	serine residues			serine residues						serine residues	Protein O-glucosyltransferase 1 shows specificity for folded EGF-like domains, it can only glycosylate serine residues in the C1XSXPC2 motif, and it possesses an uncommon dual donor substrate specificity.
12768205	6	32	part_of	FcalphaRI-binding	820:836	arg1	The FcalphaRI-binding site	FcalphaRI		The FcalphaRI-binding site		PUBTATOR	Site	FcalphaRI	2204	site	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	6	49	part_of	site	838:841	arg1	IgA1	IgA1		site		PUBTATOR	Site	IgA1	P01876	site	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
8130392	9	55	gly	Asn-linked	1521:1530	arg1	the Asn-linked oligosaccharides			Asn	the Asn-linked oligosaccharides					Asn	The structure of the major neutral oligosaccharide in rHPC was determined to be: [formula: see text] Two representatives of the sialylated oligosaccharides in rHPC are: [formula: see text] and [formula: see text] Thus, many of the Asn-linked oligosaccharides in rHPC were found to terminate in GalNAc beta (1-->4)GlcNAc beta (1-->.)
8130392	9	68	gly	oligosaccharides	1429:1444	arg1	rHPC are	rHPC			oligosaccharides	OGER		rHPC	P52873		The structure of the major neutral oligosaccharide in rHPC was determined to be: [formula: see text] Two representatives of the sialylated oligosaccharides in rHPC are: [formula: see text] and [formula: see text] Thus, many of the Asn-linked oligosaccharides in rHPC were found to terminate in GalNAc beta (1-->4)GlcNAc beta (1-->.)
8130392	9	86	gly	oligosaccharides	1532:1547	arg1	rHPC	rHPC			oligosaccharides	OGER		rHPC	P52873		The structure of the major neutral oligosaccharide in rHPC was determined to be: [formula: see text] Two representatives of the sialylated oligosaccharides in rHPC are: [formula: see text] and [formula: see text] Thus, many of the Asn-linked oligosaccharides in rHPC were found to terminate in GalNAc beta (1-->4)GlcNAc beta (1-->.)
8130392	9	96	gly	sialylated	1418:1427	arg1	the sialylated oligosaccharides				the sialylated oligosaccharides						The structure of the major neutral oligosaccharide in rHPC was determined to be: [formula: see text] Two representatives of the sialylated oligosaccharides in rHPC are: [formula: see text] and [formula: see text] Thus, many of the Asn-linked oligosaccharides in rHPC were found to terminate in GalNAc beta (1-->4)GlcNAc beta (1-->.)
8130392	9	128	gly	oligosaccharide	1325:1339	arg1	rHPC	rHPC			oligosaccharide	OGER		rHPC	P52873		The structure of the major neutral oligosaccharide in rHPC was determined to be: [formula: see text] Two representatives of the sialylated oligosaccharides in rHPC are: [formula: see text] and [formula: see text] Thus, many of the Asn-linked oligosaccharides in rHPC were found to terminate in GalNAc beta (1-->4)GlcNAc beta (1-->.)
17534424	0	116	gly	glycoprotein	32:43	arg1	a late endosomal glycoprotein	a late endosomal glycoprotein				Fterm		glycoprotein			Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains.
17534424	0	116	gly	glycoprotein	32:43	arg1	Human ClC-6	Human ClC-6				PUBTATOR		ClC-6	1185		Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains.
7727388	0	91	gly	glycosylation	27:39	arg1	the human natriuretic peptide receptor-C homodimer	natriuretic peptide receptor-C homodimer		sites		PUBTATOR		natriuretic peptide receptor-C homodimer	4883	sites	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
19343721	1	75	gly	macro-heterogeneity	256:274	arg1	plasma-derived hPC	plasma-derived hPC				OGER		hPC	P11498		We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
15863501	3	7	gly	N-glycosylated	651:664	arg2	two consensus sites			two consensus sites						sites	In several if not all cell types, the N- and C-terminal domains of sPLA(2)-III were proteolytically removed, leading to the production of the form containing only the sPLA(2) domain, which could be further N-glycosylated at two consensus sites.
7654718	6	44	gly	glycosylated	1058:1069	arg1	less than one serine residue			less than one serine residue						serine residue	beta-Elimination reaction revealed that nine threonine residues and less than one serine residue were glycosylated.
7654718	6	44	gly	glycosylated	1058:1069	arg1	nine threonine residues			nine threonine residues						threonine residues	beta-Elimination reaction revealed that nine threonine residues and less than one serine residue were glycosylated.
9933650	0	81	gly	interleukin-1	52:64	arg1	novel carbohydrate binding activity	interleukin-1			novel carbohydrate binding activity	PUBTATOR		interleukin-1	3552		Detection of novel carbohydrate binding activity of interleukin-1.
24125761	3	34	gly	glycosylation	341:353	arg1	AADAC enzyme activity	AADAC enzyme				PUBTATOR		AADAC enzyme	13		In the present study, we investigated the effect of glycosylation on AADAC enzyme activity.
18952059	3	36	gly	unglycosylated	302:315	arg1	unglycosylated IZUMO	unglycosylated IZUMO				PUBTATOR		IZUMO	73456		In the present paper, we produced transgenic mouse lines expressing unglycosylated IZUMO (N204Q-IZUMO) in Izumo1 -/- background.
18952059	3	36	gly	unglycosylated	302:315	arg1	N204Q-IZUMO	N204Q-IZUMO				PUBTATOR		-IZUMO	73456		In the present paper, we produced transgenic mouse lines expressing unglycosylated IZUMO (N204Q-IZUMO) in Izumo1 -/- background.
20044576	3	12	part_of	alpha-DG	609:616	arg1	the mucin-like domain	DG,		the mucin-like domain		PUBTATOR	Site	DG,	1605	domain	Using mass spectrometry- and nuclear magnetic resonance (NMR)-based structural analyses, we identified a phosphorylated O-mannosyl glycan on the mucin-like domain of recombinant alpha-DG, which was required for laminin binding.
30392906	4	11	part_of	MPZL1	545:549	arg1	the extracellular domain	MPZL1		the extracellular domain		PUBTATOR	Site	MPZL1	9019	domain	To elucidate the functional basis, we have determined the crystal structure of the extracellular domain of MPZL1 at 2.7 Å resolution.
19467646	9	18	part_of	BDNF	1197:1200	arg1	the glycosylated pro-form	BDNF		the glycosylated pro-form		PUBTATOR	AminoAcid	BDNF	627	pro	Treatment with N-glycanase and plasmin reduced the size of the higher molecular weight bands, confirming the glycosylated pro-form of BDNF.
7512967	6	27	gly	O-glycosylated	922:935	arg2	Thr-221A			Thr-221A						Thr	It was revealed that approximately 40% of the heavy chain of the mouse IgG2b are O-glycosylated at Thr-221A in the hinge region, predominantly with a tetrasaccharide composed of GalNAc, Gal, and two N-glycolylneuraminic acid residues.
11706042	2	29	gly	TLR4	355:358	arg1	N-linked carbohydrates	TLR4			N-linked carbohydrates	PUBTATOR		TLR4	7099		Because each of these proteins is glycosylated, we have examined the functional role of N-linked carbohydrates of both MD-2 and TLR4.
11706042	2	32	gly	MD-2	346:349	arg1	N-linked carbohydrates	MD-2			N-linked carbohydrates	OGER		MD-2	Q9Y6Y9		Because each of these proteins is glycosylated, we have examined the functional role of N-linked carbohydrates of both MD-2 and TLR4.
11706042	2	45	gly	glycosylated	261:272	arg1	these proteins	these proteins				Fterm		proteins			Because each of these proteins is glycosylated, we have examined the functional role of N-linked carbohydrates of both MD-2 and TLR4.
1323463	1	38	gly	released	186:193	arg1	bovine submaxillary-gland mucin AND The acidic oligosaccharide alditols	bovine submaxillary-gland mucin			The acidic oligosaccharide alditols	PUBTATOR		mucin	281333		The acidic oligosaccharide alditols released from bovine submaxillary-gland mucin by Carlson degradation were investigated by a combination of liquid secondary-ion mass spectrometry, methylation analysis and 1H-NMR.
24977290	9	59	part_of	ADAMTS13	1627:1634	arg1	the TSR1 and TSR4 domains	ADAMTS13		the TSR1 and TSR4 domains		PUBTATOR	Site	ADAMTS13	Q76LX8	domains	In addition to putative O-fucosylation and N-linked glycosylation, two putative C-mannosylation sites were identified within the TSR1 and TSR4 domains of ADAMTS13.
24977290	9	104	part_of	TSR1	1602:1605	arg1	the TSR1 and TSR4 domains	TSR1		the TSR1 and TSR4 domains		OGER	Site	TSR1	Q2NL82	domains	In addition to putative O-fucosylation and N-linked glycosylation, two putative C-mannosylation sites were identified within the TSR1 and TSR4 domains of ADAMTS13.
23050552	5	32	part_of	fibrinogen	551:560	arg1	proteinase K-generated fibrinogen glycopeptides	K-generated fibrinogen		proteinase K-generated fibrinogen glycopeptides		PUBTATOR	Site	K-generated fibrinogen	2244	glycopeptides	Here, we make use of tryptic- and proteinase K-generated fibrinogen glycopeptides for the detailed analysis of the protein's O-glycosylation by combining information obtained from both one- and two-dimensional nanoLC-ESI-ion trap (IT)-MS approaches.
23050552	5	35	part_of	K-generated	539:549	arg1	proteinase K-generated fibrinogen glycopeptides	K-generated fibrinogen		proteinase K-generated fibrinogen glycopeptides		PUBTATOR	Site	K-generated fibrinogen	2244	glycopeptides	Here, we make use of tryptic- and proteinase K-generated fibrinogen glycopeptides for the detailed analysis of the protein's O-glycosylation by combining information obtained from both one- and two-dimensional nanoLC-ESI-ion trap (IT)-MS approaches.
24884609	6	60	part_of	trypsin-GluC	890:901	arg1	ITIH4 trypsin-GluC glycopeptides	GluC		ITIH4 trypsin-GluC glycopeptides		PUBTATOR	Site	GluC	57733	glycopeptides	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
24884609	6	67	part_of	ITIH4	884:888	arg1	ITIH4 trypsin-GluC glycopeptides	ITIH4		ITIH4 trypsin-GluC glycopeptides		PUBTATOR	Site	ITIH4	3700	glycopeptides	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
19952283	1	30	gly	glycoprotein	107:118	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Neuroplastin (Np) is a glycoprotein belonging to the immunoglobulin superfamily of cell adhesion molecules (CAMs) and existing in two isoforms, Np55 and Np65, named according to their molecular weights.
19952283	1	30	gly	glycoprotein	107:118	arg1	Neuroplastin	Neuroplastin				OGER		Neuroplastin	P97546		Neuroplastin (Np) is a glycoprotein belonging to the immunoglobulin superfamily of cell adhesion molecules (CAMs) and existing in two isoforms, Np55 and Np65, named according to their molecular weights.
20951142	2	72	part_of	extracellular	364:376	arg1	extracellular amino-terminal domains	r		extracellular amino-terminal domains		PUBTATOR	Site	r	2900	domains	The selective assembly of iGluRs into AMPA, kainate, and N-methyl-d-aspartic acid (NMDA) receptor subtypes is regulated by their extracellular amino-terminal domains (ATDs).
15054092	5	40	gly	glycosylation	715:727	arg1	the G5/G8 heterodimer	the G5/G8 heterodimer				Fterm		heterodimer			N-Linked glycosylation of G8 was required for efficient trafficking of the G5/G8 heterodimer, but mutations that abolished glycosylation of G5 did not prevent trafficking of the heterodimer.
15054092	5	40	gly	glycosylation	715:727	arg1	G8	G8				Cterm		G8	Q9H221		N-Linked glycosylation of G8 was required for efficient trafficking of the G5/G8 heterodimer, but mutations that abolished glycosylation of G5 did not prevent trafficking of the heterodimer.
15054092	5	43	gly	glycosylation	829:841	arg1	G5	G5				Cterm		G5	Q9H222		N-Linked glycosylation of G8 was required for efficient trafficking of the G5/G8 heterodimer, but mutations that abolished glycosylation of G5 did not prevent trafficking of the heterodimer.
8702538	6	67	gly	glycosylation	1002:1014	arg2	a single potential N-linked glycosylation site			a single potential N-linked glycosylation site						site	We show that mutation of a single potential N-linked glycosylation site in the first immunoglobulin domain of CD22 completely abrogates ligand recognition.
23050552	3	61	gly	occupied	397:404	arg2	one N-glycosylation site			one N-glycosylation site						site	The beta and gamma subunits each contain one N-glycosylation site, each of which is occupied by a biantennary N-glycan.
23050552	3	71	gly	N-glycosylation	358:372	arg2	one N-glycosylation site			one N-glycosylation site						site	The beta and gamma subunits each contain one N-glycosylation site, each of which is occupied by a biantennary N-glycan.
19167329	5	4	part_of	protein	866:872	arg1	the N-terminal signal sequence	protein		the N-terminal signal sequence		Fterm	Site	protein		sequence	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
16877748	10	63	part_of	sICAM-1	1981:1987	arg1	the nine N-glycosylation sites	sICAM-1		the nine N-glycosylation sites		Cterm	Site	sICAM-1	3383	sites	These results show that the N-glycans that enhance the MIP-2-inducing activity of mouse sICAM-1 are mostly di- and trisialylated complex-type N-glycans including a small fraction carrying more sialic acid residues than antennae and that the nine N-glycosylation sites of mouse sICAM-1 are all glycosylated.
3542030	11	14	part_of	receptors	1461:1469	arg1	the cDNA-derived sequences	receptors		the cDNA-derived sequences		Fterm	Site	receptors		sequences	The protein shows no homology either with the cDNA-derived sequences of the estrogen and glucocorticoid receptors found by others to be homologous with each other or with any other protein sequence in the 1986 data base.
20739279	0	45	gly	N-glycosylation	0:14	arg1	synaptic cell adhesion molecule	synaptic cell adhesion molecule				PUBTATOR		synaptic cell adhesion molecule	23705		N-glycosylation at the SynCAM (synaptic cell adhesion molecule) immunoglobulin interface modulates synaptic adhesion.
11320094	0	72	gly	glycosylation	150:162	arg2	N-linked glycosylation sites			N-linked glycosylation sites						sites	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
27384988	8	17	gly	Concanavalin	809:820	arg1	a carbohydrate binding lectin protein	Concanavalin A			a carbohydrate binding lectin protein	Cterm		Concanavalin A			RpS3 bound to Concanavalin A, a carbohydrate binding lectin protein, while treatment with peptide-N-glycosidase F shifted the secreted rpS3 to a lower molecular weight band.
25265424	6	70	gly	glycopeptides	1064:1076	arg2	select glycopeptides			select glycopeptides						glycopeptides	Core fucosylation is detectable in only trace amounts in haptoglobin but with confidence on hemopexin and complement factor H, where core fucosylation of the bi-antennary glycans on select glycopeptides reaches 15-20% intensity.
25265424	6	85	gly	fucosylation	1013:1024	arg1	select glycopeptides			glycopeptides	select glycopeptides		Site			glycopeptides	Core fucosylation is detectable in only trace amounts in haptoglobin but with confidence on hemopexin and complement factor H, where core fucosylation of the bi-antennary glycans on select glycopeptides reaches 15-20% intensity.
25265424	6	85	gly	fucosylation	1013:1024	arg1	select glycopeptides			glycopeptides	the bi-antennary glycans					glycopeptides	Core fucosylation is detectable in only trace amounts in haptoglobin but with confidence on hemopexin and complement factor H, where core fucosylation of the bi-antennary glycans on select glycopeptides reaches 15-20% intensity.
8507662	4	2	gly	glycosylated	636:647	arg1	Asn-70			Ser-8, Thr-9, Ser-46 and Asn-70						Ser-8, Thr-9, Ser-46 and Asn-70	Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated.
8507662	4	2	gly	glycosylated	636:647	arg1	Ser-46			Ser-8, Thr-9, Ser-46 and Asn-70						Ser-8, Thr-9, Ser-46 and Asn-70	Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated.
8507662	4	2	gly	glycosylated	636:647	arg1	Thr-9			Ser-8, Thr-9, Ser-46 and Asn-70						Ser-8, Thr-9, Ser-46 and Asn-70	Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated.
8507662	4	2	gly	glycosylated	636:647	arg1	Ser-46			Ser-8, Thr-9, Ser-46 and Asn-70						Ser-8, Thr-9, Ser-46 and Asn-70	Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated.
8507662	4	2	gly	glycosylated	636:647	arg1	Thr-9			Ser-8, Thr-9, Ser-46 and Asn-70						Ser-8, Thr-9, Ser-46 and Asn-70	Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated.
8507662	4	2	gly	glycosylated	636:647	arg1	Thr-9			Ser-8, Thr-9, Ser-46 and Asn-70						Ser-8, Thr-9, Ser-46 and Asn-70	Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated.
23167757	4	11	part_of	contains	689:696	arg1	PDIA2 AND three predicted N-linked glycosylation sites	PDIA2		three predicted N-linked glycosylation sites		PUBTATOR	Site	PDIA2	64714	sites	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
22809326	14	61	gly	glycoprotein	1761:1772	arg1	the lysosomal glycoprotein coat	the lysosomal glycoprotein coat				Fterm		glycoprotein			Insights into the structure of the lysosomal glycoprotein coat were obtained by computational models of the LAMP-1 and LAMP-2 luminal regions.
28011641	2	19	part_of	Ca2+	372:375	arg1	the Ca2+ coordination site	Ca2		the Ca2+ coordination site		OGER	Site	Ca2	P00918	site	Crystal structures of P- and E-selectin suggest a two-state model in which ligand binding to the lectin domain closes loop 83-89 around the Ca2+ coordination site, enabling Glu-88 to engage Ca2+ and fucose.
9705299	5	22	gly	glycosylation	912:924	arg2	all three potential N-linked glycosylation sites			all three potential N-linked glycosylation sites						sites	We therefore characterized mutant G6Pases lacking one, two, or all three potential N-linked glycosylation sites.
24995978	5	31	gly	serine	834:839	arg1	the key O-GlcNAcylated serine residues			serine residues	the key O-GlcNAcylated serine residues					serine residues	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
29689099	5	64	gly	glycosylation	1059:1071	arg2	critical N-linked glycosylation sites			critical N-linked glycosylation sites						sites	Both of the monomeric gp120 immunogens (MN- and A244-rgp120) in the AIDSVAX B/E vaccine used in the RV144 trial were enriched for glycans containing high levels of sialic acid, and lacked critical N-linked glycosylation sites required for binding by several families of bN-mAbs.
25765764	2	46	part_of	LRIG1	333:337	arg1	The two LRIG1 domains	LRIG1		The two LRIG1 domains		PUBTATOR	Site	LRIG1	26018	domains	The two LRIG1 domains crystallised so that we have been able to determine the three-dimensional structures at 2.3Å resolution.
3542030	1	9	part_of	protein	129:135	arg1	The amino acid sequence	sex steroid binding protein		The amino acid sequence		PUBTATOR	Site	sex steroid binding protein	6462	sequence	The amino acid sequence of the sex steroid binding protein (SBP) from human plasma has been determined.
26536155	5	15	gly	glycoproteins	1218:1230	arg1	Pronase treated glycoproteins	Pronase treated glycoproteins				Fterm		glycoproteins			Here, we describe a universal workflow for site-specific N- and O-glycopeptide analysis of Pronase treated glycoproteins with integrated, sequential C18 reverse phase and porous graphitized carbon-LC-ESI-QTOF-MS/MS employing a combination of lower- and enhanced-energy collision-induced dissociation.
26536155	5	55	gly	O-glycopeptide	1175:1188	arg2	O-glycopeptide analysis			O-glycopeptide analysis						O-glycopeptide	Here, we describe a universal workflow for site-specific N- and O-glycopeptide analysis of Pronase treated glycoproteins with integrated, sequential C18 reverse phase and porous graphitized carbon-LC-ESI-QTOF-MS/MS employing a combination of lower- and enhanced-energy collision-induced dissociation.
7727388	3	39	gly	glycosylation	429:441	arg1	this receptor	receptor		sites		Fterm		receptor		sites	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
17534424	3	74	gly	N-glycosylated	1099:1112	arg1	the three sites			the three sites						sites	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	84	gly	K	912:912	arg1	Three asparagine residues			Three asparagine residues						asparagine residues	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	19	gly	N-glycosylated	766:779	arg1	human ClC-6	ClC-6		region		PUBTATOR		ClC-6	1185	region	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	84	gly	K	912:912	arg1	N422			N410, N422 and N432						N410, N422 and N432	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	84	gly	K	912:912	arg1	N410			N410, N422 and N432						N410, N422 and N432	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	84	gly	K	912:912	arg1	N410			N410, N422 and N432						N410, N422 and N432	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
10878002	0	13	gly	C-mannosylated	59:72	arg1	Properdin	Properdin				PUBTATOR		Properdin	5199		Properdin, the positive regulator of complement, is highly C-mannosylated.
12888562	8	43	gly	glycosylated	1500:1511	arg1	the Cys399			the Cys399						Cys399	Neither the Cys399 nor Asn443 mutants were fully glycosylated, and both were retained in the endoplasmic reticulum.
12731887	3	9	part_of	residues	667:674	arg1	full-length p67	p67		residues		PUBTATOR	AminoAcid	p67	64370	residues in	By site-directed mutagenesis, (27)TSST(30) and (60)SGTS(63) clusters were substituted with (27)AAGA(30) and (60)AGAA(63) amino acid residues in full-length p67, and their EGFP fusions were constitutively expressed in rat tumor hepatoma cells (KRC-7).
12906826	2	7	part_of	DPP-IV	318:323	arg1	the ectodomain	DPP-IV		the ectodomain		PUBTATOR	Site	DPP-IV	1803	ectodomain	We expressed and purified the ectodomain of human DPP-IV in Pichia pastoris and determined the X-ray structure at 2.1 A resolution.
27294781	0	39	gly	glycosylation	9:21	arg1	SV2	SV2				PUBTATOR		SV2	9900		N-linked glycosylation of SV2 is required for binding and uptake of botulinum neurotoxin A. Botulinum neurotoxin serotype A1 (BoNT/A1), a licensed drug widely used for medical and cosmetic applications, exerts its action by invading motoneurons.
27294781	0	39	gly	glycosylation	9:21	arg1	botulinum neurotoxin	botulinum neurotoxin				Fterm		neurotoxin A			N-linked glycosylation of SV2 is required for binding and uptake of botulinum neurotoxin A. Botulinum neurotoxin serotype A1 (BoNT/A1), a licensed drug widely used for medical and cosmetic applications, exerts its action by invading motoneurons.
1883960	4	18	gly	O-glycosylated	1037:1050	arg1	25-kD O-glycosylated IL-6	25-kD O-glycosylated IL-6				PUBTATOR		IL-6	3569		Amino acid sequencing revealed that the major amino terminus in the fibroblast-derived 23- to 25-kD O-glycosylated IL-6 was at Ala28 whereas the major amino terminus in the 28- to 30-kD N- and O-glycosylated IL-6 was at Val30, suggesting that targeting of newly synthesized IL-6 polypeptides into the two different processing pathways in fibroblasts may be keyed to differences in the signal peptide cleavage site.
1883960	4	89	gly	O-glycosylated	1130:1143	arg1	the 28- to 30-kD N- and O-glycosylated IL-6	the 28- to 30-kD N- and O-glycosylated IL-6				PUBTATOR		IL-6	3569		Amino acid sequencing revealed that the major amino terminus in the fibroblast-derived 23- to 25-kD O-glycosylated IL-6 was at Ala28 whereas the major amino terminus in the 28- to 30-kD N- and O-glycosylated IL-6 was at Val30, suggesting that targeting of newly synthesized IL-6 polypeptides into the two different processing pathways in fibroblasts may be keyed to differences in the signal peptide cleavage site.
11152692	10	10	part_of	asporin	1116:1122	arg1	The deduced amino acid sequence	asporin		The deduced amino acid sequence		PUBTATOR	Site	asporin	54829	sequence	The deduced amino acid sequence of asporin was confirmed by mass spectrometry of the isolated protein resulting in 84% sequence coverage.
21138434	0	37	gly	N-glycosylated	22:35	arg1	N-glycosylated residues	subunit		residues		Fterm		subunit		residues	The identification of N-glycosylated residues of the human 5-HT3B receptor subunit: importance for cell membrane expression.
17980170	12	52	gly	N-glycosylation	1495:1509	arg2	actual N-glycosylation sites			actual N-glycosylation sites						sites	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	52	gly	N-glycosylation	1495:1509	arg2	Asn-333			Asn-37, Asn-107, Asn-309, and Asn-333						Asn-37, Asn-107, Asn-309, and Asn-333	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	52	gly	N-glycosylation	1495:1509	arg2	Asn-37			Asn-37, Asn-107, Asn-309, and Asn-333						Asn-37, Asn-107, Asn-309, and Asn-333	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	52	gly	N-glycosylation	1495:1509	arg2	Asn-309			Asn-37, Asn-107, Asn-309, and Asn-333						Asn-37, Asn-107, Asn-309, and Asn-333	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	52	gly	N-glycosylation	1495:1509	arg2	Asn-37			Asn-37, Asn-107, Asn-309, and Asn-333						Asn-37, Asn-107, Asn-309, and Asn-333	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	52	gly	N-glycosylation	1495:1509	arg2	Asn-309			Asn-37, Asn-107, Asn-309, and Asn-333						Asn-37, Asn-107, Asn-309, and Asn-333	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	52	gly	N-glycosylation	1495:1509	arg2	Asn-309			Asn-37, Asn-107, Asn-309, and Asn-333						Asn-37, Asn-107, Asn-309, and Asn-333	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
25187573	5	7	gly	glycosylated	1013:1024	arg1	adjacent threonine residues			adjacent threonine residues						threonine residues	This showed that adjacent threonine residues within the central STP-rich region could be simultaneously and/or individually glycosylated.
20145116	6	20	part_of	VEGFR-2	840:846	arg1	the VEGFR-2 high-affinity-binding site	VEGFR		the VEGFR-2 high-affinity-binding site		PUBTATOR	Site	VEGFR	3791	site	Here we present the crystal structure of VEGF-C bound to the VEGFR-2 high-affinity-binding site, which consists of immunoglobulin homology domains D2 and D3.
18093522	6	44	part_of	sites	826:830	arg1	neurexin-1 beta	neurexin-1 beta		sites		OGER	Site	neurexin-1 beta	P58400	sites	Alternatively spliced sites in neurexin-1 beta and in neuroligin-1 are positioned nearby the binding interface, explaining how they regulate the interaction.
18093522	6	44	part_of	sites	826:830	arg1	neuroligin-1	neuroligin-1		sites		PUBTATOR	Site	neuroligin-1	22871	sites	Alternatively spliced sites in neurexin-1 beta and in neuroligin-1 are positioned nearby the binding interface, explaining how they regulate the interaction.
7620335	2	73	gly	glycosylation	518:530	arg2	a glycosylation site			a glycosylation site						site	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	2	78	gly	glycopeptides	486:498	arg2	X. Four glycopeptides			X. Four glycopeptides						glycopeptides	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
22688517	7	49	gly	glycopeptides	1434:1446	arg2	glycopeptides			glycopeptides						glycopeptides	In addition, manual annotation of multistage MS data utilizing diagnostic ions, which were found to be particularly useful in defining the structure of glycopeptides and glycans was addressed for proper spectra interpretation.
8672508	5	3	part_of	gp210	972:976	arg1	the cytoplasmic domain	gp210		the cytoplasmic domain		PUBTATOR	Site	gp210	23225	domain	Mutant and wild-type fusion proteins containing the cytoplasmic domain of gp210 were phosphorylated in vitro and their phosphopeptide maps compared to that of mitotic gp210.
8672508	5	4	part_of	containing	935:944	arg1	Mutant and wild-type fusion proteins AND the cytoplasmic domain	Mutant and wild-type fusion proteins		the cytoplasmic domain		Fterm	Site	proteins		domain	Mutant and wild-type fusion proteins containing the cytoplasmic domain of gp210 were phosphorylated in vitro and their phosphopeptide maps compared to that of mitotic gp210.
12589760	0	11	part_of	CLIP	63:66	arg1	a human CLIP peptide	CLIP		a human CLIP peptide		PUBTATOR	Site	CLIP	6249	peptide	Crystal structure of MHC class II I-Ab in complex with a human CLIP peptide: prediction of an I-Ab peptide-binding motif.
20622017	10	69	gly	glycosylation	1305:1317	arg2	Two glycosylation sites			Two glycosylation sites						sites	Two glycosylation sites on renal GGT were modified exclusively by neutral glycans.
20622017	10	92	gly	modified	1343:1350	arg1	Two glycosylation sites AND neutral glycans			Two glycosylation sites	neutral glycans					sites	Two glycosylation sites on renal GGT were modified exclusively by neutral glycans.
8344278	6	19	gly	glycosylation	1187:1199	arg1	each saposin	each saposin				Fterm		saposin			The possible reasons for the unique glycosylation of each saposin is discussed.
22579623	2	33	part_of	Fab	412:414	arg1	three neutralizing Fab fragments	Fab		three neutralizing Fab fragments		PUBTATOR	Site	Fab	2187	fragments	We report the crystal structure of human TLR3 ectodomain (TLR3ecd) in a quaternary complex with three neutralizing Fab fragments.
22579623	2	58	part_of	TLR3	338:341	arg1	human TLR3 ectodomain	TLR3		human TLR3 ectodomain		PUBTATOR	Site	TLR3	7098	ectodomain	We report the crystal structure of human TLR3 ectodomain (TLR3ecd) in a quaternary complex with three neutralizing Fab fragments.
23319596	6	34	gly	Asn-644	1045:1051	arg1	N-linked glycans			Asn-455 and Asn-644	N-linked glycans					Asn-455 and Asn-644	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	6	66	gly	Asn-455	1033:1039	arg1	N-linked glycans			Asn-455 and Asn-644	N-linked glycans					Asn-455 and Asn-644	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
3356193	9	71	gly	disialylated	1183:1194	arg1	Mono- and disialylated forms				Mono- and disialylated forms						Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
25153361	2	51	gly	nonglycosylated	254:268	arg1	nonglycosylated peptides			nonglycosylated peptides						peptides	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	2	84	gly	glycoproteins	474:486	arg1	complex glycoproteins	complex glycoproteins				Fterm		glycoproteins			As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
8672508	4	36	gly	glycoprotein	731:742	arg1	Pore membrane glycoprotein gp210	Pore membrane glycoprotein gp210				Fterm		glycoprotein			Pore membrane glycoprotein gp210, that has a cytoplasmic, carboxyl-terminal domain facing the pore, was not phosphorylated in interphase but specifically phosphorylated in mitosis.
8999954	2	6	gly	modified	280:287	arg1	eukaryotic RNA polymerase II AND Ser(Thr)-O-linked N-acetylglucosamine moieties	eukaryotic RNA polymerase II			Ser(Thr)-O-linked N-acetylglucosamine moieties	OGER		RNA polymerase II			Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	2	6	gly	modified	280:287	arg3	eukaryotic RNA polymerase II AND O-GlcNAc	eukaryotic RNA polymerase II			O-GlcNAc	OGER		RNA polymerase II			Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	2	6	gly	modified	280:287	arg1	Many transcription factors AND Ser(Thr)-O-linked N-acetylglucosamine moieties	Many transcription factors			Ser(Thr)-O-linked N-acetylglucosamine moieties	Fterm		factors			Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	2	6	gly	modified	280:287	arg1	Many transcription factors AND O-GlcNAc	Many transcription factors			O-GlcNAc	Fterm		factors			Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	2	9	gly	Ser	292:294	arg1	O-GlcNAc			Ser	O-GlcNAc					Ser	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	2	9	gly	Ser	292:294	arg1	Ser(Thr)-O-linked N-acetylglucosamine moieties			Ser	Ser(Thr)-O-linked N-acetylglucosamine moieties					Ser	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
24342833	0	44	gly	glycosylated	22:33	arg2	Serine 23	-catenin		Serine 23		PUBTATOR		-catenin	1499	Serine 23	β-catenin is O-GlcNAc glycosylated at Serine 23: implications for β-catenin's subcellular localization and transactivator function.
21768335	5	5	gly	receptor	1023:1030	arg1	glycans	receptor			glycans	Fterm		receptor			The structures reveal a unique type of interface consisting of carbohydrate-carbohydrate interactions between glycans of the receptor and the afucosylated Fc.
11696579	0	35	part_of	Akt	107:109	arg1	the Akt site	Akt		the Akt site		PUBTATOR	Site	Akt	207	site	Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site.
24706782	8	76	gly	sialylated	1119:1128	arg1	sialylated human-type oligosaccharides				sialylated human-type oligosaccharides						Moreover, extensive in planta glycoengineering allowed the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM.
2842863	7	16	part_of	contained	1026:1034	arg1	Each domain AND internal amino acid sequences	Each domain		internal amino acid sequences						sequences	Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges.
21932778	9	58	part_of	sites	1648:1652	arg1	glypican-1	glypican-1		sites		PUBTATOR	Site	glypican-1	2817	sites	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
11595658	3	28	gly	nonglycosylated	320:334	arg1	The nonglycosylated receptor	The nonglycosylated receptor				Fterm		receptor			The nonglycosylated receptor did not bind the radioligand and had a decreased cAMP stimulation potency in response to CRF.
19017259	4	18	gly	structures	784:793	arg1	rTFPI	rTFPI			structures	PUBTATOR		rTFPI	29436		Sugar chain structures in rTFPI expressed in Chinese hamster ovary (CHO) cells have been reported previously, but those of plasma TFPI have not been.
24884609	7	52	gly	N-glycosylation	1156:1170	arg2	N-glycosylation sites			N-glycosylation sites						sites	While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ.
24884609	7	79	gly	occupancy	1143:1151	arg2	N-glycosylation sites			N-glycosylation sites						sites	While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ.
24103369	1	16	gly	glycoproteins	147:159	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The site-specific characterization of N-glycans in glycoproteins with the potential of clinical application is important.
9524075	3	61	gly	glycosylation	396:408	arg2	the only glycosylation site			the only glycosylation site						site	HEK 293-cells which do not express cathepsin S were transfected with cDNA of either wild type human procathepsin S or a mutant procathepsin S in which Asn of the only glycosylation site in the proregion was replaced by Gln.
17018531	2	28	gly	glycoprotein	340:351	arg1	a soluble lysosomal glycoprotein	a soluble lysosomal glycoprotein				Fterm		glycoprotein			One form of the disease is caused by a deficiency in NPC2, a soluble lysosomal glycoprotein that binds cholesterol.
17018531	2	28	gly	glycoprotein	340:351	arg1	NPC2	NPC2				OGER		NPC2	Q9Z0J0		One form of the disease is caused by a deficiency in NPC2, a soluble lysosomal glycoprotein that binds cholesterol.
8846222	4	23	part_of	beta-chain	502:511	arg1	the N-terminal threonine	chain		the N-terminal threonine		OGER	AminoAcid	chain	P20933	threonine	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	4	23	part_of	beta-chain	502:511	arg1	The catalytically essential residue	chain		The catalytically essential residue		OGER	Site	chain	P20933	residue	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
17040911	1	14	gly	glycosylated	174:185	arg1	a highly glycosylated, secreted zinc metalloprotease	a highly glycosylated, secreted zinc metalloprotease				Fterm		metalloprotease			The meprin A homo-oligomer is a highly glycosylated, secreted zinc metalloprotease of the astacin family and metzincin superfamily.
23234360	4	34	gly	attached	968:975	arg2	one to four Ser/Thr residues AND predominantly core-1-like HexHexNAc-O- structure			one to four Ser/Thr residues	predominantly core-1-like HexHexNAc-O- structure					residues	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	39	gly	glycosylation	861:873	arg2	the glycosylation site			the glycosylation site						site	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	56	gly	glycopeptides	890:902	arg2	the glycopeptides			the glycopeptides						glycopeptides	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	39	gly	glycosylation	861:873	arg2	the glycopeptides			glycopeptides						glycopeptides	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
19690161	4	58	part_of	vIL-6	538:542	arg1	The Asn-89 site	vIL		The Asn-89 site		OGER	SpecificSite	vIL	P09327	Asn-89 site	The Asn-89 site of vIL-6, found to be required for optimal cytokine function, is composed of complex glycans.
23345538	8	60	gly	glycopeptides	1474:1486	arg2	predominantly high-intensity, multiply charged glycopeptides			predominantly high-intensity, multiply charged glycopeptides						glycopeptides	The former detected predominantly high-intensity, multiply charged glycopeptides, whereas the latter preferentially selected precursors with complex/hybrid glycans for fragmentation.
26195816	4	23	part_of	Fab	540:542	arg1	a Fab fragment	Fab		a Fab fragment		PUBTATOR	Site	Fab	2187	fragment	Crystallization required enzymatic removal of N-linked glycans and complex formation with a Fab fragment from a tool antibody.
8130392	13	23	gly	Asn-linked	1890:1899	arg1	the Asn-linked oligosaccharides			Asn	the Asn-linked oligosaccharides					Asn	Biochem., 16D, 151] observed in the Asn-linked oligosaccharides of rHPC derived from human kidney 293 cells, we propose to label the GalNAc beta-(1-->4)[Fuc alpha (1-->3)]GlcNAc beta (1-->.)
8130392	13	38	gly	rHPC	1921:1924	arg1	the Asn-linked oligosaccharides	rHPC			the Asn-linked oligosaccharides	OGER		rHPC	P52873		Biochem., 16D, 151] observed in the Asn-linked oligosaccharides of rHPC derived from human kidney 293 cells, we propose to label the GalNAc beta-(1-->4)[Fuc alpha (1-->3)]GlcNAc beta (1-->.)
18547526	0	0	part_of	7TM	77:79	arg1	a 7TM receptor-attached lectin-like domain	7TM		a 7TM receptor-attached lectin-like domain		Cterm	Site	7TM		domain	Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL: a 7TM receptor-attached lectin-like domain.
18547526	0	11	part_of	receptor-attached	81:97	arg1	a 7TM receptor-attached lectin-like domain	receptor		a 7TM receptor-attached lectin-like domain		Fterm	Site	receptor		domain	Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL: a 7TM receptor-attached lectin-like domain.
8026573	2	16	gly	glycoprotein	283:294	arg1	an intact glycoprotein	an intact glycoprotein				Fterm		glycoprotein			The structure assessment of an intact glycoprotein in solution requires an extensive assignment of the carbohydrate NMR resonances.
9875849	3	28	part_of	receptor	429:436	arg1	the antibody-binding domains	IgE receptor		the antibody-binding domains		OGER	Site	IgE receptor	P01854	domains	We have solved the X-ray crystal structure of the antibody-binding domains of the human IgE receptor at 2.4 A resolution.
2403553	9	19	gly	contains	1159:1166	arg1	The receptor AND at least one O-linked oligosaccharide	The receptor			at least one O-linked oligosaccharide	Fterm		receptor			The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
8286855	6	34	gly	O-glycosylation	842:856	arg2	All 16 O-glycosylation sites			All 16 O-glycosylation sites						sites	All 16 O-glycosylation sites are explained on the basis of four motifs.
18250328	8	35	part_of	residues	1118:1125	arg1	NL3	NL3		residues		OGER	Site	NL3	Q9NZ94	residues	Finally, sequence comparisons of NL isoforms allow for mapping the location of residues of previously identified mutations in NL3 and NL4 found in patients with autism spectrum disorders.
18250328	8	65	part_of	NL3	1165:1167	arg1	residues	NL3		residues		OGER	Site	NL3	Q9NZ94	residues	Finally, sequence comparisons of NL isoforms allow for mapping the location of residues of previously identified mutations in NL3 and NL4 found in patients with autism spectrum disorders.
12527193	9	62	gly	glycosylation	1367:1379	arg2	the conserved N linked glycosylation site			the conserved N linked glycosylation site						site	CRB3 is localized to the apical surface and tight junctions but the conserved N linked glycosylation site does not appear to be necessary for CRB3 apical targeting.
9748270	2	5	part_of	XVII	143:146	arg1	The cDNA sequence	XVII		The cDNA sequence		Cterm	Site	XVII		sequence	The cDNA sequence of human collagen XVII predicts an unusual type II transmembrane protein, but a biochemical characterization of this structure has not been accomplished yet.
18203274	9	46	gly	glycoprotein	1261:1272	arg1	the important human plasma glycoprotein BChE	the important human plasma glycoprotein BChE				Fterm		glycoprotein			This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
2275556	5	44	part_of	cathepsin	1043:1051	arg1	(ii) cathepsin L polypeptides	cathepsin L		(ii) cathepsin L polypeptides		PUBTATOR	Site	cathepsin L	13039	polypeptides	These findings indicate that (i) cathepsin L is synthesized from the same gene in normal and transformed cells and (ii) cathepsin L polypeptides made by these cells are translated with the same primary sequence.
2275556	5	110	part_of	L	1053:1053	arg1	(ii) cathepsin L polypeptides	cathepsin L		(ii) cathepsin L polypeptides		PUBTATOR	Site	cathepsin L	13039	polypeptides	These findings indicate that (i) cathepsin L is synthesized from the same gene in normal and transformed cells and (ii) cathepsin L polypeptides made by these cells are translated with the same primary sequence.
30582698	5	32	gly	MGL	680:682	arg1	this glycan specificity	MGL			this glycan specificity	PUBTATOR		MGL	10462		Even though this glycan specificity of MGL is well described, there is a lack of understanding of the actual glycoproteins that bind MGL.
30582698	5	59	gly	glycoproteins	750:762	arg1	the actual glycoproteins	the actual glycoproteins				Fterm		glycoproteins			Even though this glycan specificity of MGL is well described, there is a lack of understanding of the actual glycoproteins that bind MGL.
21264968	7	89	gly	glycosylation	2369:2381	arg2	the consecutive Thr residues	MUC5AC		Thr residues		PUBTATOR		MUC5AC	4586	Thr residues	Such conformational impact on the underlying peptides was proved to be remarkable in the glycosylation at the consecutive Thr residues of MUC5AC.
21264968	7	89	gly	glycosylation	2369:2381	arg1	the consecutive Thr residues	MUC5AC		Thr residues		PUBTATOR		MUC5AC	4586	Thr residues	Such conformational impact on the underlying peptides was proved to be remarkable in the glycosylation at the consecutive Thr residues of MUC5AC.
21264968	7	89	gly	glycosylation	2369:2381	arg1	the consecutive Thr residues			Thr residues						Thr residues	Such conformational impact on the underlying peptides was proved to be remarkable in the glycosylation at the consecutive Thr residues of MUC5AC.
9524075	9	36	gly	non-glycosylated	1048:1063	arg1	the glycosylated and non-glycosylated procathepsin S	the glycosylated and non-glycosylated procathepsin S				Cterm		the glycosylated and non-glycosylated procathepsin S	1520		A reuptake of the glycosylated and non-glycosylated procathepsin S by HEK 293-cells could be observed.
9524075	9	55	gly	glycosylated	1031:1042	arg1	the glycosylated and non-glycosylated procathepsin S	the glycosylated and non-glycosylated procathepsin S				Cterm		the glycosylated and non-glycosylated procathepsin S	1520		A reuptake of the glycosylated and non-glycosylated procathepsin S by HEK 293-cells could be observed.
22613618	2	63	gly	glycosylated	223:234	arg1	a heavily glycosylated membrane protein	a heavily glycosylated membrane protein				Fterm		protein			Kv1.3 is a heavily glycosylated membrane protein.
1997323	1	9	gly	trisialylated	137:149	arg1	trisialylated diantennary glycan				trisialylated diantennary glycan						Determination of glycan primary structures and characterization of a new type of trisialylated diantennary glycan.
18420026	0	105	part_of	glycoprotein	28:39	arg1	a single N-glycosylation site	glycoprotein		a single N-glycosylation site		Fterm	Site	glycoprotein		site	Nectin-like molecule 1 is a glycoprotein with a single N-glycosylation site at N290KS which influences its adhesion activity.
3123586	5	31	gly	glycosylated	754:765	arg1	the mutant apoC-III polypeptide			the mutant apoC-III polypeptide						polypeptide	As a result of this amino acid replacement, the mutant apoC-III polypeptide is not glycosylated.
19139490	7	37	gly	glycopeptide	1084:1095	arg2	CF glycopeptide			CF glycopeptide						glycopeptide	Over 100 CF glycoproteins and CF sites were identified, and over 10,000 mass spectra of CF glycopeptide were found.
19139490	7	72	gly	glycoproteins	1005:1017	arg1	Over 100 CF glycoproteins	Over 100 CF glycoproteins				Fterm		glycoproteins			Over 100 CF glycoproteins and CF sites were identified, and over 10,000 mass spectra of CF glycopeptide were found.
8798614	5	54	part_of	CD59	993:996	arg1	the CD59 polypeptide	CD59		the CD59 polypeptide		PUBTATOR	Site	CD59	966	polypeptide	In this study, we specifically examined how deletion or transposition of the site of N-linked glycosylation in the CD59 polypeptide affects its MAC inhibitory function.
11356966	6	12	gly	glycosylation	647:659	arg1	asparagine 81			asparagine 81						asparagine 81	Evidence was obtained for glycosylation of asparagine 81.
24121512	5	82	part_of	AE1	1109:1111	arg1	the membrane domain	AE1		the membrane domain		PUBTATOR	Site	AE1	6521	domain	In addition, the membrane domain of AE1 (mdAE1) efficiently mediated anion transport.
19656770	8	46	gly	glycoproteins	1561:1573	arg1	the identified N-linked glycoproteins	the identified N-linked glycoproteins				Fterm		glycoproteins			Several of the identified N-linked glycoproteins, including aquaporin-1 and beta-sarcoglycan, were found in validation experiments to change in overall abundance as the myoblasts differentiate toward myotubes.
2943741	2	81	gly	glycopeptides	415:427	arg2	glycopeptides			glycopeptides						glycopeptides	Leukosialin was isolated by specific immunoprecipitation from cells which were metabolically labeled with [3H]glucosamine, and glycopeptides were isolated after Pronase digestion.
29226084	6	0	gly	N-glycosylation	1199:1213	arg1	GPR61	GPR61				OGER		GPR61	Q9BZJ8		These results demonstrate that GPR61 is subject to N-glycosylation but suggest this is not a prerequisite for cell surface expression, although N-glycosylation of other proteins may be important for cell membrane expression of GPR61.
29226084	6	0	gly	N-glycosylation	1199:1213	arg1	other proteins	other proteins				Fterm		proteins			These results demonstrate that GPR61 is subject to N-glycosylation but suggest this is not a prerequisite for cell surface expression, although N-glycosylation of other proteins may be important for cell membrane expression of GPR61.
15687489	6	6	part_of	enzyme	832:837	arg1	the DUF323 domain	formylglycine-generating enzyme		domain		PUBTATOR	Site	formylglycine-generating enzyme	285362	domain	Both proteins belong to a large family of pro- and eukaryotic proteins containing the DUF323 domain, a formylglycine-generating enzyme domain of unknown three-dimensional structure.
15687489	6	33	part_of	formylglycine-generating	807:830	arg1	the DUF323 domain	formylglycine-generating enzyme		domain		PUBTATOR	Site	formylglycine-generating enzyme	285362	domain	Both proteins belong to a large family of pro- and eukaryotic proteins containing the DUF323 domain, a formylglycine-generating enzyme domain of unknown three-dimensional structure.
15687489	6	9	part_of	containing	775:784	arg1	pro- and eukaryotic proteins AND the DUF323 domain	proteins		domain		Fterm	Site	proteins		domain	Both proteins belong to a large family of pro- and eukaryotic proteins containing the DUF323 domain, a formylglycine-generating enzyme domain of unknown three-dimensional structure.
20489211	3	70	part_of	fibronectin	629:639	arg1	D4-D6	fibronectin		D4-D6		PUBTATOR	SiteSequence	fibronectin	2335	D4-D6	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	3	70	part_of	fibronectin	629:639	arg1	the membrane-proximal fibronectin type III domains	fibronectin		the membrane-proximal fibronectin type III domains		PUBTATOR	Site	fibronectin	2335	domains	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
24161696	5	12	gly	occupancy	949:957	arg2	both N-glycosylation sites			both N-glycosylation sites						sites	RESULTS: Microscopy images revealed that occupancy of both N-glycosylation sites of Kv3.1b had relatively similar amounts of Kv3.1b in the outgrowth and cell body while vacancy of one or both sites led to increased accumulation of Kv3.1b in the cell body.
24161696	5	88	gly	N-glycosylation	967:981	arg2	both N-glycosylation sites	Kv3.1b		sites		Cterm		Kv3.1b		sites	RESULTS: Microscopy images revealed that occupancy of both N-glycosylation sites of Kv3.1b had relatively similar amounts of Kv3.1b in the outgrowth and cell body while vacancy of one or both sites led to increased accumulation of Kv3.1b in the cell body.
15152093	0	22	part_of	sites	38:42	arg1	glutamate carboxypeptidase II	glutamate carboxypeptidase II		sites		PUBTATOR	Site	glutamate carboxypeptidase II	2346	sites	Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity.
2108149	1	74	gly	possessing	327:336	arg1	different IgGs AND structurally distinct CH2-linked oligosaccharide moieties	different IgGs			structurally distinct CH2-linked oligosaccharide moieties	Cterm		IgGs			To examine the nature of the factors influencing the galactosylation pattern of the heavy chain of murine immunoglobulin G (IgG), cell fusion was performed between a myeloma (P3x63Ag8) and a hybridoma (Sp2HL/Bu) cell line which secrete different IgGs possessing structurally distinct CH2-linked oligosaccharide moieties.
24530628	3	18	gly	glycopeptide	388:399	arg2	efficient glycopeptide enrichment			efficient glycopeptide enrichment						glycopeptide	Here, we establish a versatile method for efficient glycopeptide enrichment to acquire reliable mass spectra.
24090084	8	23	gly	N-glycopeptide	1271:1284	arg2	N-glycopeptide			N-glycopeptide						N-glycopeptide	The assignment of glycan compositions to peptide sequences was achieved by searching the N-glycopeptide HCD MS/MS spectra against the glycopeptide-centric concatenated databases employing the N-glycan modification database.
15102839	5	57	part_of	Asn	1120:1122	arg1	the murine enzyme	enzyme		Asn		Fterm	SpecificSite	enzyme		Asn(515)	A Man(6)GlcNAc(2) oligosaccharide attached to Asn(515) in the murine enzyme was found to extend into the active site of an adjoining protein unit in the crystal lattice in a presumed enzyme-product complex.
7240157	8	65	gly	glycopeptide	1314:1325	arg2	a glycopeptide mixture			a glycopeptide mixture						glycopeptide	It is thus noteworthy that this spectral technique allows elucidation of structures of very closely related carbohydrate chains in a glycopeptide mixture.
2573604	9	18	gly	O-glycosylation	1707:1721	arg1	the Thr28-Thr29-Ser30 sequence			sequence						sequence	The papain-sensitivity of the oligosaccharide from the larger subunit is consistent with O-glycosylation at the Thr28-Thr29-Ser30 sequence.
9530955	0	57	gly	glycoprotein	57:68	arg1	epitectin	epitectin				Fterm		epitectin			Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	0	57	gly	glycoprotein	57:68	arg1	the MUC1 mucin-type glycoprotein	the MUC1 mucin-type glycoprotein				Fterm		glycoprotein			Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
16263699	8	50	gly	glycosylation	1240:1252	arg2	70 different glycosylation sites			70 different glycosylation sites						sites	Using both methods in combination with nano-LC-ESI-MS/MS analysis 70 different glycosylation sites within 41 different proteins were identified.
7541354	2	34	gly	released	192:199	arg1	the vitronectin AND Oligosaccharides	the vitronectin			Oligosaccharides	PUBTATOR		vitronectin	7448		Oligosaccharides were released from the vitronectin by N-glycosidase F digestion and tagged with 2-aminopyridine; the pyridylamino-oligosaccharides were then fractionated by anion-exchange and reverse-phase HPLC.
3163150	0	26	part_of	kallikrein--amino	14:30	arg1	Human urinary kallikrein--amino acid sequence	kallikrein		Human urinary kallikrein--amino acid sequence		PUBTATOR	Site	kallikrein	9622	sequence	Human urinary kallikrein--amino acid sequence and carbohydrate attachment sites.
10429212	1	26	gly	N-glycosylation	142:156	arg2	the natural N-glycosylation site			the natural N-glycosylation site						site	We have used the natural N-glycosylation site in the N-tail of cig30, a eukaryotic polytopic membrane protein, as a marker for N-tail translocation across the microsomal membrane.
9153399	5	35	part_of	ICAM-2	767:772	arg1	the extracellular region	ICAM-2		the extracellular region		PUBTATOR	Site	ICAM-2	3384	region	Here we present the crystal structure of the extracellular region of ICAM-2.
25187573	5	67	part_of	STP-rich	953:960	arg1	the central STP-rich region	STP		the central STP-rich region		OGER	Site	STP	P50225	region	This showed that adjacent threonine residues within the central STP-rich region could be simultaneously and/or individually glycosylated.
2226832	0	31	part_of	CAP37	23:27	arg1	Amino acid sequence	CAP37		Amino acid sequence		PUBTATOR	Site	CAP37	566	sequence	Amino acid sequence of CAP37, a human neutrophil granule-derived antibacterial and monocyte-specific chemotactic glycoprotein structurally similar to neutrophil elastase.
8981093	4	63	gly	EPO	988:990	arg1	sialic acid content	EPO			sialic acid content	PUBTATOR		EPO	2056		On the other hand, an inverse relationship between the in vitro bioactivity and sialic acid content of EPO was observed.
16452088	8	63	gly	modified	1384:1391	arg3	proteins AND O-GlcNAc	proteins			O-GlcNAc	Fterm		proteins			Bassoon and Piccolo, proteins critical to synapse assembly and vesicle docking, were extensively modified by O-GlcNAc.
16452088	8	63	gly	modified	1384:1391	arg1	Piccolo AND O-GlcNAc	Piccolo			O-GlcNAc	Cterm		Piccolo			Bassoon and Piccolo, proteins critical to synapse assembly and vesicle docking, were extensively modified by O-GlcNAc.
9395518	3	12	gly	glycoprotein	504:515	arg1	a 30-kDa plasma membrane glycoprotein	a 30-kDa plasma membrane glycoprotein				Fterm		glycoprotein			It codes for a 30-kDa plasma membrane glycoprotein with five putative transmembrane domains.
9539702	7	29	part_of	ICAM-1	1300:1305	arg1	previously described I set domains	ICAM-1		previously described I set domains		OGER	Site	ICAM-1	P05362	domains	A subdivision of the intermediate (I) set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set.
9539702	7	29	part_of	ICAM-1	1300:1305	arg1	domain 1	ICAM-1		domain 1		OGER	Site	ICAM-1	P05362	domain	A subdivision of the intermediate (I) set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set.
9539702	7	36	part_of	ICAM-2	1391:1396	arg1	domain 2	ICAM-2		domain 2		OGER	Site	ICAM-2	P13598	domain	A subdivision of the intermediate (I) set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set.
9539702	7	38	part_of	molecule-1	1426:1435	arg1	domain 2	cell adhesion molecule-1		domain 2		OGER	Site	cell adhesion molecule-1	Q9BY67	domain	A subdivision of the intermediate (I) set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set.
9539702	7	72	part_of	ICAM-1	1383:1388	arg1	domain 2	ICAM-1		domain 2		OGER	Site	ICAM-1	P05362	domain	A subdivision of the intermediate (I) set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set.
9013598	6	13	gly	unglycosylated	1184:1197	arg1	six glycosylated and one unglycosylated Asn			six glycosylated and one unglycosylated Asn						Asn	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
9013598	6	56	gly	glycosylated	1163:1174	arg1	six glycosylated and one unglycosylated Asn			six glycosylated and one unglycosylated Asn						Asn	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
1569071	9	16	gly	unglycosylated	1800:1813	arg1	precursor IGF-II	precursor IGF-II				PUBTATOR		IGF-II	P01344		This was the Mr value that would be predicted for an unglycosylated form of precursor IGF-II that had a carboxyl-terminal end at or near Lys88.
23050552	8	46	gly	fibrinogen	1086:1095	arg1	The previously reported N-glycan attachment sites	fibrinogen			The previously reported N-glycan attachment sites	PUBTATOR		fibrinogen	2244		The previously reported N-glycan attachment sites of human fibrinogen could be confirmed.
9295302	9	29	part_of	has	1511:1513	arg1	MRP AND an extracytosolic NH2 terminus	MRP		an extracytosolic NH2 terminus		PUBTATOR	Site	MRP	4363	terminus	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
25765764	7	2	part_of	LRIG1-3Ig	1067:1075	arg1	the LRIG1-3Ig domains	LRIG1		the LRIG1-3Ig domains		PUBTATOR	Site	LRIG1	26018	domains	Similarly, neither the soluble LRIG1-LRR nor the LRIG1-3Ig domains nor the full-length LRIG1 co-expressed in HEK293 cells inhibited ligand-stimulated activation of cell-surface EGFR.
22809326	11	2	part_of	LAMP-2	1356:1361	arg1	the glycosylated luminal regions	LAMP-2		the glycosylated luminal regions		PUBTATOR	Site	LAMP-2	P13473	regions	Computational models of the glycosylated luminal regions of LAMP-1 and LAMP-2 indicate that the proteins adopt a compact conformation in close proximity to the lysosomal membrane.
22809326	11	6	part_of	LAMP-1	1345:1350	arg1	the glycosylated luminal regions	LAMP-1		the glycosylated luminal regions		PUBTATOR	Site	LAMP-1	3916	regions	Computational models of the glycosylated luminal regions of LAMP-1 and LAMP-2 indicate that the proteins adopt a compact conformation in close proximity to the lysosomal membrane.
21550978	5	22	part_of	hPAR	932:935	arg1	the N terminus	hPAR(1)		the N terminus		PUBTATOR	Site	hPAR(1)	2149	terminus	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21676880	0	43	gly	N-glycosylation	19:33	arg1	type I transmembrane KCNE1 peptides			type I transmembrane KCNE1 peptides						peptides	Post-translational N-glycosylation of type I transmembrane KCNE1 peptides: implications for membrane protein biogenesis and disease.
1991473	6	53	gly	sulphated/sialylated	955:974	arg1	a sulphated/sialylated structure				a sulphated/sialylated structure						The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	15	gly	attached	776:783	arg1	hLH alpha AND The oligosaccharides	hLH alpha		Asn52	The oligosaccharides	PUBTATOR		hLH alpha	1081	Asn52	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	15	gly	attached	776:783	arg1	hLH beta AND The oligosaccharides	hLH beta		Asn52	The oligosaccharides	PUBTATOR		hLH beta	3972	Asn52	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	15	gly	attached	776:783	arg1	Asn30 AND The oligosaccharides	hLH alpha		Asn30	The oligosaccharides	PUBTATOR		hLH alpha	1081	Asn30	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	15	gly	attached	776:783	arg1	hLH beta AND The oligosaccharides	hLH beta		Asn30	The oligosaccharides	PUBTATOR		hLH beta	3972	Asn30	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
11069170	6	35	part_of	domains	850:856	arg1	the dimer	dimer		domains		Fterm		dimer			Movements of the four domains in the dimer are likely to affect the separation of the transmembrane and intracellular regions, and thereby activate the receptor.
7679920	5	7	gly	fucosylated	1134:1144	arg1	a fucosylated triantennary sugar chain				a fucosylated triantennary sugar chain						The Con A-nonreactive and LCA-nonreactive species contained a fucosylated triantennary sugar chain as a major component, and two minor components: a triantennary sugar chain and a biantennary sugar chain with a bisecting-N-acetylglucosamine residue at the trimannosyl core.
12925274	3	21	part_of	containing	470:479	arg1	a secreted 65 kDa form AND the full semaphorin domain	a secreted 65 kDa form		the full semaphorin domain		PUBTATOR	Site	form of Semaphorin-3A	10371	domain	We report the crystal structure of a secreted 65 kDa form of Semaphorin-3A (Sema3A), containing the full semaphorin domain.
108268	4	29	gly	glycopeptides	658:670	arg2	iodinated glycopeptides			iodinated glycopeptides						glycopeptides	The preparation and utilization of iodinated glycopeptides for sequence analysis is presented.
15379548	2	5	gly	glycoproteins	285:297	arg1	three glycoproteins	three glycoproteins				Fterm		glycoproteins			The mouse zona pellucida is composed of three glycoproteins (ZP1, ZP2, ZP3).
10386995	6	36	gly	presence	1132:1139	arg2	Ser576 AND an O-GlcNAc			sites Thr562 and Ser576	an O-GlcNAc					sites Thr562 and Ser576	With use of synthetic peptides, however, the presence of an O-GlcNAc at sites Thr562 and Ser576 resulted in only a 66% increase in the Km of calcium/calmodulin-dependent protein kinase II phosphorylation of site Ser566 with no effect on its Vmax.
10386995	6	36	gly	presence	1132:1139	arg1	Thr562 AND an O-GlcNAc			sites Thr562 and Ser576	an O-GlcNAc					sites Thr562 and Ser576	With use of synthetic peptides, however, the presence of an O-GlcNAc at sites Thr562 and Ser576 resulted in only a 66% increase in the Km of calcium/calmodulin-dependent protein kinase II phosphorylation of site Ser566 with no effect on its Vmax.
10386995	6	36	gly	presence	1132:1139	arg1	Thr562 AND an O-GlcNAc			sites Thr562 and Ser576	an O-GlcNAc					sites Thr562 and Ser576	With use of synthetic peptides, however, the presence of an O-GlcNAc at sites Thr562 and Ser576 resulted in only a 66% increase in the Km of calcium/calmodulin-dependent protein kinase II phosphorylation of site Ser566 with no effect on its Vmax.
15823095	12	62	part_of	Lag1	1711:1714	arg1	the conserved Lag1 motif	Lag1		the conserved Lag1 motif		OGER	Site	Lag1	P13236	motif	From these data we propose topology for the conserved Lag1 motif in Lass family members, namely that the N-terminal region faces the luminal side and the C-terminal region the cytosolic side of the endoplasmic reticulum membrane.
1457969	2	72	gly	glycosylated	414:425	arg2	Asn 23	hTSH beta		Asn 23		PUBTATOR		hTSH beta	7252	Asn 23	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	72	gly	glycosylated	414:425	arg1	its subunits	subunits		Asn 23		Fterm		subunits		Asn 23	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	85	gly	glycosylated	364:375	arg2	Asn 52			Asn 52 and Asn 78						Asn 52 and Asn 78	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	85	gly	glycosylated	364:375	arg1	hTSH alpha	hTSH alpha		Asn 52 and Asn 78		PUBTATOR		hTSH alpha	1081	Asn 52 and Asn 78	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	85	gly	glycosylated	364:375	arg1	its subunits	subunits		Asn 52 and Asn 78		Fterm		subunits		Asn 52 and Asn 78	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	85	gly	glycosylated	364:375	arg1	hTSH alpha	hTSH alpha		Asn 52 and Asn 78		PUBTATOR		hTSH alpha	1081	Asn 52 and Asn 78	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	85	gly	glycosylated	364:375	arg1	its subunits	subunits		Asn 52 and Asn 78		Fterm		subunits		Asn 52 and Asn 78	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
20427278	7	66	gly	N-glycosylation	980:994	arg1	the prion protein	the prion protein				Fterm		protein			Moreover, TMEM59 inhibited the complex N-glycosylation of the prion protein, suggesting a more general modulation of Golgi glycosylation reactions.
9030779	2	63	gly	sphingomyelinase	379:394	arg1	the six potential N-linked oligosaccharide chains	acid sphingomyelinase			the six potential N-linked oligosaccharide chains	PUBTATOR		acid sphingomyelinase	6609		We have determined the influence of the six potential N-linked oligosaccharide chains of human acid sphingomyelinase (ASM) on catalytic activity, targeting, and processing of the enzyme.
17548821	0	30	part_of	receptor-binding	15:30	arg1	a receptor-binding fragment	receptor		a receptor-binding fragment		Fterm	Site	receptor		fragment	Structure of a receptor-binding fragment of reelin and mutational analysis reveal a recognition mechanism similar to endocytic receptors.
17548821	0	47	part_of	reelin	44:49	arg1	a receptor-binding fragment	reelin		a receptor-binding fragment		PUBTATOR	Site	reelin	5649	fragment	Structure of a receptor-binding fragment of reelin and mutational analysis reveal a recognition mechanism similar to endocytic receptors.
11152678	2	20	gly	N-glycosylated	434:447	arg1	a 32-kDa precursor	precursor		site		Fterm		precursor		site	Metabolic labeling, immunoprecipitation, and SDS-polyacrylamide gel electrophoresis reveal that pro-BDNF is generated as a 32-kDa precursor that is N-glycosylated and glycosulfated on a site, within the pro-domain.
11152678	2	20	gly	N-glycosylated	434:447	arg1	pro-BDNF	BDNF		site		PUBTATOR	AminoAcid	BDNF	627	site	Metabolic labeling, immunoprecipitation, and SDS-polyacrylamide gel electrophoresis reveal that pro-BDNF is generated as a 32-kDa precursor that is N-glycosylated and glycosulfated on a site, within the pro-domain.
11152678	2	20	gly	N-glycosylated	434:447	arg1	a site			site						site	Metabolic labeling, immunoprecipitation, and SDS-polyacrylamide gel electrophoresis reveal that pro-BDNF is generated as a 32-kDa precursor that is N-glycosylated and glycosulfated on a site, within the pro-domain.
11152678	2	20	gly	N-glycosylated	434:447	arg1	a 32-kDa precursor	precursor		pro		Fterm		precursor		pro	Metabolic labeling, immunoprecipitation, and SDS-polyacrylamide gel electrophoresis reveal that pro-BDNF is generated as a 32-kDa precursor that is N-glycosylated and glycosulfated on a site, within the pro-domain.
11152678	2	20	gly	N-glycosylated	434:447	arg1	pro-BDNF	BDNF		pro		PUBTATOR	AminoAcid	BDNF	627	pro	Metabolic labeling, immunoprecipitation, and SDS-polyacrylamide gel electrophoresis reveal that pro-BDNF is generated as a 32-kDa precursor that is N-glycosylated and glycosulfated on a site, within the pro-domain.
11152678	2	20	gly	N-glycosylated	434:447	arg1	a site	precursor		site		Fterm		precursor		site	Metabolic labeling, immunoprecipitation, and SDS-polyacrylamide gel electrophoresis reveal that pro-BDNF is generated as a 32-kDa precursor that is N-glycosylated and glycosulfated on a site, within the pro-domain.
11152678	2	20	gly	N-glycosylated	434:447	arg1	a site	BDNF		site		PUBTATOR	AminoAcid	BDNF	627	site	Metabolic labeling, immunoprecipitation, and SDS-polyacrylamide gel electrophoresis reveal that pro-BDNF is generated as a 32-kDa precursor that is N-glycosylated and glycosulfated on a site, within the pro-domain.
12545205	0	97	gly	N-cadherin	25:34	arg1	Carbohydrate moieties	N-cadherin			Carbohydrate moieties	PUBTATOR		N-cadherin	1000		Carbohydrate moieties of N-cadherin from human melanoma cell lines.
7679920	4	44	gly	residue	1063:1069	arg1	a focus residue			a focus residue	a focus residue		AminoAcid			residue at	The Con A-nonreactive and LCA-reactive species contained a biantennary sugar chain both with a bisecting-N-acetylglucosamine residue at the trimannosyl core and with a focus residue at the innermost N-acetylglucosamine residue.
24121512	3	45	part_of	NBCe1	619:623	arg1	the cytosolic domain	NBCe1		the cytosolic domain		OGER	Site	NBCe1	Q9Y6R1	domain	Mutation of a conserved arginine residue (R298S) in the cytosolic domain of NBCe1 (SLC4A4) is linked to proximal renal tubular acidosis and results in impaired transport function, suggesting that the cytosolic domain plays a role in substrate permeation.
20489211	4	22	part_of	receptor	780:787	arg1	the complete ectodomain	receptor		the complete ectodomain		Fterm	Site	receptor		ectodomain	This represents the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor.
19141282	3	9	gly	unglycosylated	454:467	arg1	unglycosylated IL-7Ralpha	unglycosylated IL-7Ralpha				PUBTATOR		IL-7Ralpha	3575		IL-7 binds glycosylated IL-7Ralpha 300-fold more tightly than unglycosylated IL-7Ralpha, and the enhanced affinity is attributed primarily to an accelerated on rate.
19141282	3	31	gly	glycosylated	403:414	arg1	glycosylated IL-7Ralpha	glycosylated IL-7Ralpha				PUBTATOR		IL-7Ralpha	3575		IL-7 binds glycosylated IL-7Ralpha 300-fold more tightly than unglycosylated IL-7Ralpha, and the enhanced affinity is attributed primarily to an accelerated on rate.
2059624	1	95	part_of	plasminogen	182:192	arg1	asparagine-289	plasminogen		asparagine-289		OGER	SpecificSite	plasminogen	P00747	asparagine-289	Temporal dependence of the nature of the oligosaccharides assembled on asparagine-289 of recombinant human plasminogen produced in baculovirus vector infected Spodoptera frugiperda (IPLB-SF-21AE) cells.
22160680	1	7	gly	attached	175:182	arg2	a maltosaccharide chain AND Tyr195			Tyr195	a maltosaccharide chain					Tyr195	Glycogenin initiates the synthesis of a maltosaccharide chain covalently attached to itself on Tyr195 via a stepwise glucosylation reaction, priming glycogen synthesis.
19237744	2	63	gly	glycosylated	174:185	arg1	a glycosylated 75 kDa preproprotein	a glycosylated 75 kDa preproprotein				Fterm		preproprotein			It is synthesized as a glycosylated 75 kDa preproprotein which is further processed into 28 and 40 kDa fragments.
26598643	10	68	gly	O-glycosylation	1632:1646	arg2	31 O-glycosylation sites			31 O-glycosylation sites						sites	Overall, 31 O-glycosylation sites and regions belonging to 22 proteins were identified, the majority being acute-phase proteins.
23269669	5	15	gly	glycosylation	902:914	arg1	human GC-C	human GC-C				PUBTATOR		GC-C	2984		When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
23269669	5	50	gly	glycosylation	1026:1038	arg2	the 10 predicted glycosylation sites			the 10 predicted glycosylation sites						sites	When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
19563754	0	30	part_of	NPC1	34:37	arg1	N-terminal domain	NPC1		N-terminal domain		PUBTATOR	Site	NPC1	O15118	domain	Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol.
1731338	1	57	part_of	galactoglycoprotein	146:164	arg1	The amino acid sequence	galactoglycoprotein		The amino acid sequence		PUBTATOR	Site	galactoglycoprotein	6693	sequence	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
21053369	5	52	gly	glycopeptides	859:871	arg2	glycopeptides			glycopeptides						glycopeptides	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
1708771	9	21	gly	glycosylation	1513:1525	arg2	four potential N-linked glycosylation sites			four potential N-linked glycosylation sites						sites	There are four potential N-linked glycosylation sites.
10861210	7	81	gly	glycoprotein	1137:1148	arg1	the glycoprotein	the glycoprotein				Fterm		form of the glycoprotein			The complex form of the N555 mutant could be biotinylated showing that this form of the glycoprotein was at the cell surface.
1374031	2	13	gly	subunit	246:252	arg1	The N-linked carbohydrate chains	subunit			The N-linked carbohydrate chains	OGER		subunit	P0DN86		The N-linked carbohydrate chains of the beta subunit of human chorionic gonadotropin (hCG-beta) isolated from the culture fluid of the choriocarcinoma cell line BeWo were released enzymatically by peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F. Subsequently, the O-linked oligosaccharides were split off from the N-deglycosylated protein by mild alkaline borohydride treatment.
1374031	2	98	gly	N-deglycosylated	527:542	arg1	the N-deglycosylated protein	the N-deglycosylated protein				Fterm		protein			The N-linked carbohydrate chains of the beta subunit of human chorionic gonadotropin (hCG-beta) isolated from the culture fluid of the choriocarcinoma cell line BeWo were released enzymatically by peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F. Subsequently, the O-linked oligosaccharides were split off from the N-deglycosylated protein by mild alkaline borohydride treatment.
2963625	5	40	gly	H	720:720	arg1	the seventh homologous repeat unit	factor H			the seventh homologous repeat unit	PUBTATOR		factor H	3075		A tyrosine/histidine polymorphism was observed within the seventh homologous repeat unit of factor H.
17395588	5	14	part_of	punctin-1	851:859	arg1	tryptic peptides	punctin-1		tryptic peptides		PUBTATOR	Site	punctin-1	92949	peptides	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	28	part_of	TSR3	898:901	arg1	the appropriate peptides	TSR3		the appropriate peptides		PUBTATOR	Site	TSR3	115939	peptides	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	31	part_of	TSR2	892:895	arg1	the appropriate peptides	TSR2		the appropriate peptides		PUBTATOR	Site	TSR2	90121	peptides	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
19692335	8	0	part_of	metalloproteinase-like	1620:1641	arg1	The metalloproteinase-like domain	metalloproteinase		The metalloproteinase-like domain		Fterm	Site	metalloproteinase		domain	The metalloproteinase-like domain contacts the rest of ADAM22 with discontinuous, hydrophilic, and poorly complemented interactions, suggesting the possibility of modular movement of ADAM22 and other ADAMs.
12034704	3	10	part_of	C	870:870	arg1	the phospholipid binding domain	protein C		the phospholipid binding domain		OGER	Site	protein C	P02810	domain	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
28668641	1	8	gly	glycosylation	162:174	arg2	asparagine residues			asparagine residues						asparagine residues	Vaspin is a glycoprotein with three predicted glycosylation sites at asparagine residues located in proximity to the reactive center loop and close to domains that play important roles in conformational changes underlying serpin function.
28668641	1	8	gly	glycosylation	162:174	arg2	three predicted glycosylation sites			three predicted glycosylation sites						sites	Vaspin is a glycoprotein with three predicted glycosylation sites at asparagine residues located in proximity to the reactive center loop and close to domains that play important roles in conformational changes underlying serpin function.
28668641	1	34	gly	glycoprotein	128:139	arg1	Vaspin	Vaspin				PUBTATOR		Vaspin	145264		Vaspin is a glycoprotein with three predicted glycosylation sites at asparagine residues located in proximity to the reactive center loop and close to domains that play important roles in conformational changes underlying serpin function.
28668641	1	34	gly	glycoprotein	128:139	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Vaspin is a glycoprotein with three predicted glycosylation sites at asparagine residues located in proximity to the reactive center loop and close to domains that play important roles in conformational changes underlying serpin function.
14718370	0	31	gly	MUC5AC	19:24	arg1	C-Mannosylation	MUC5AC			C-Mannosylation	PUBTATOR		MUC5AC	P98088		C-Mannosylation of MUC5AC and MUC5B Cys subdomains.
14718370	0	35	gly	MUC5B	30:34	arg1	C-Mannosylation	MUC5B			C-Mannosylation	PUBTATOR		MUC5B	Q9HC84		C-Mannosylation of MUC5AC and MUC5B Cys subdomains.
11683872	2	41	gly	glycosylation	321:333	arg1	VR1	VR1				PUBTATOR		structure of VR1	7442		Here we describe its biochemical properties and assess the subcellular localization, the glycosylation state and the quaternary structure of VR1 expressed in HEK293 cells and in the DRG-derived cell line F-11 (N18TG2 mouse neuroblastoma x rat dorsal root ganglia, hybridoma).
2573604	2	130	part_of	gamma-glutamyltranspeptidase	354:381	arg1	the primary sequence	gamma-glutamyltranspeptidase		the primary sequence		PUBTATOR	Site	gamma-glutamyltranspeptidase	116568	sequence	No such domain is evident in the primary sequence of rat renal gamma-glutamyltranspeptidase.
22848655	5	16	part_of	dimerization	715:726	arg1	the ligand recognition and dimerization domains	dimerization		the ligand recognition and dimerization domains		Fterm	Site	dimerization		domains	The ectodomain of RON, containing the ligand recognition and dimerization domains, is composed of a semaphorin (Sema), Plexins-Semaphorins-Integrins domain (PSI), and four Immunoglobulins-Plexins-Transcription factor (IPT) domains.
22848655	5	63	part_of	IPT	872:874	arg1	four Immunoglobulins-Plexins-Transcription factor (IPT) domains	IPT		four Immunoglobulins-Plexins-Transcription factor (IPT) domains		OGER	Site	IPT	Q9H3H1	domains	The ectodomain of RON, containing the ligand recognition and dimerization domains, is composed of a semaphorin (Sema), Plexins-Semaphorins-Integrins domain (PSI), and four Immunoglobulins-Plexins-Transcription factor (IPT) domains.
22848655	5	71	part_of	RON	672:674	arg1	The ectodomain	RON		The ectodomain		OGER	Site	RON	Q04912	ectodomain	The ectodomain of RON, containing the ligand recognition and dimerization domains, is composed of a semaphorin (Sema), Plexins-Semaphorins-Integrins domain (PSI), and four Immunoglobulins-Plexins-Transcription factor (IPT) domains.
22848655	5	47	part_of	containing	677:686	arg1	RON AND the ligand recognition and dimerization domains	RON		the ligand recognition and dimerization domains		OGER	Site	RON	Q04912	domains	The ectodomain of RON, containing the ligand recognition and dimerization domains, is composed of a semaphorin (Sema), Plexins-Semaphorins-Integrins domain (PSI), and four Immunoglobulins-Plexins-Transcription factor (IPT) domains.
25053408	4	69	part_of	PCFT	682:685	arg1	the PCFT substrate binding domain	PCFT		the PCFT substrate binding domain		PUBTATOR	Site	PCFT	113235	domain	By structural homology to other solute carriers, TMD2 may form part of the PCFT substrate binding domain.
29095159	1	26	gly	glycoprotein	284:295	arg1	myelin-associated glycoprotein	myelin-associated glycoprotein				OGER		myelin-associated glycoprotein	P20916		The Nogo Receptor (NgR) is a glycophosphatidylinositol-anchored cell-surface protein and is a receptor for three myelin-associated inhibitors of regeneration: myelin-associated glycoprotein, Nogo66 and oligodendrocyte myelin glycoprotein.
29095159	1	57	gly	glycoprotein	332:343	arg1	oligodendrocyte myelin glycoprotein	oligodendrocyte myelin glycoprotein				PUBTATOR		oligodendrocyte myelin glycoprotein	4974		The Nogo Receptor (NgR) is a glycophosphatidylinositol-anchored cell-surface protein and is a receptor for three myelin-associated inhibitors of regeneration: myelin-associated glycoprotein, Nogo66 and oligodendrocyte myelin glycoprotein.
24018687	3	54	gly	N-glycosylation	742:756	arg2	a conserved N-glycosylation site			a conserved N-glycosylation site						site	Site-directed mutational analysis of the consensus N-glycosylation sites of the DDRs revealed that mutations of asparagine 213 of DDR2 and asparagine 211 of DDR1, a conserved N-glycosylation site among vertebrate DDRs, inhibited the generation of the high-molecular-mass isoform.
24018687	3	57	gly	N-glycosylation	618:632	arg2	the consensus N-glycosylation sites			the consensus N-glycosylation sites						sites	Site-directed mutational analysis of the consensus N-glycosylation sites of the DDRs revealed that mutations of asparagine 213 of DDR2 and asparagine 211 of DDR1, a conserved N-glycosylation site among vertebrate DDRs, inhibited the generation of the high-molecular-mass isoform.
20540760	4	53	part_of	contains	495:502	arg1	PRCP AND a novel helical structural domain	PRCP		domain		PUBTATOR	Site	PRCP	5547	domain	PRCP contains an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad and a novel helical structural domain that caps the active site.
1544894	0	5	part_of	XII	81:83	arg1	the first epidermal growth factor domain	factor XII		the first epidermal growth factor domain		OGER	Site	factor XII	P00748	domain	O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system.
1544894	0	28	part_of	C.	101:102	arg1	protein C. Epidermal growth factor (EGF) domains	protein C		protein C. Epidermal growth factor (EGF) domains		OGER	Site	protein C	P02810	domains	O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system.
1544894	0	30	part_of	protein	93:99	arg1	protein C. Epidermal growth factor (EGF) domains	protein C		protein C. Epidermal growth factor (EGF) domains		OGER	Site	protein C	P02810	domains	O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system.
1544894	0	47	part_of	factor	121:126	arg1	protein C. Epidermal growth factor (EGF) domains	factor		protein C. Epidermal growth factor (EGF) domains		Fterm	Site	factor		domains	O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system.
1544894	0	60	part_of	found	146:150	arg2	many proteins AND the first epidermal growth factor domain	many proteins		the first epidermal growth factor domain		Fterm	Site	proteins		domain	O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system.
1544894	0	60	part_of	found	146:150	arg2	many proteins AND protein C. Epidermal growth factor (EGF) domains	many proteins		protein C. Epidermal growth factor (EGF) domains		Fterm	Site	proteins		domains	O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system.
1544894	0	61	part_of	factor	57:62	arg1	the first epidermal growth factor domain	factor		the first epidermal growth factor domain		Fterm	Site	factor		domain	O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system.
10207176	6	9	gly	C-mannosylated	895:908	arg1	nonrecombinant IL-12	nonrecombinant IL-12				OGER		IL-12			This shows that nonrecombinant IL-12 is potentially C-mannosylated as well.
7654718	5	33	part_of	C-tail	818:823	arg1	the C-tail fragment	C-tail		the C-tail fragment		Cterm	Site	C-tail		fragment	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
14749323	4	67	gly	glycosylation	629:641	arg1	mOAT1 function	mOAT1 function				PUBTATOR		mOAT1	18399		274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
25700513	5	2	part_of	residues	585:592	arg1	Notch1	Notch1		residues		PUBTATOR	AminoAcid	Notch1	4851	Threonine and serine residues	Threonine and serine residues on Notch1 are functionalized with O-fucose and O-glucose, which act as surrogate amino acids by making specific, and essential, contacts to residues on DLL4.
10677208	6	44	gly	modified	1157:1164	arg1	the peptide AND hybrid and complex sugars			the peptide	hybrid and complex sugars					peptide	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
8757293	9	29	part_of	PR3	1477:1479	arg1	The linear antigenic sites	PR3		The linear antigenic sites		PUBTATOR	Site	PR3	5657	sites	The linear antigenic sites of PR3 reported to react with Wegener's granulomatosis autoantibodies occur in regions of the three-dimensional structure that may implicate the inactive pro-form of the enzyme in the pathogenesis of the disease.
18657508	2	28	part_of	alpha	447:451	arg1	the N-terminal ligand-binding domain	signal regulatory protein alpha		the N-terminal ligand-binding domain		PUBTATOR	Site	signal regulatory protein alpha	140885	domain	We describe the high-resolution X-ray crystallographic structures of the immunoglobulin superfamily domain of CD47 alone and in complex with the N-terminal ligand-binding domain of signal regulatory protein alpha (SIRPalpha).
18657508	2	38	part_of	CD47	350:353	arg1	the immunoglobulin superfamily domain	CD47		the immunoglobulin superfamily domain		PUBTATOR	Site	CD47	961	domain	We describe the high-resolution X-ray crystallographic structures of the immunoglobulin superfamily domain of CD47 alone and in complex with the N-terminal ligand-binding domain of signal regulatory protein alpha (SIRPalpha).
486087	8	13	part_of	has	857:859	arg1	The A-chain AND a threonine residue	The A-chain		a threonine residue		Fterm	SpecificSite	A-chain		threonine residue at position	The A-chain has a threonine residue at position A-39, which is located between two Gly-X-Y triplets.
15102839	5	48	gly	attached	1108:1115	arg1	Asn(515) AND A Man(6)GlcNAc(2) oligosaccharide			Asn(515)	A Man(6)GlcNAc(2) oligosaccharide					Asn(515)	A Man(6)GlcNAc(2) oligosaccharide attached to Asn(515) in the murine enzyme was found to extend into the active site of an adjoining protein unit in the crystal lattice in a presumed enzyme-product complex.
18547526	3	5	part_of	found	436:440	arg2	other metazoan transmembrane proteins AND RBL domains	other metazoan transmembrane proteins		RBL domains		Fterm	Site	proteins		domains	RBL domains, first isolated from the eggs of marine species, are also found in the ectodomains of other metazoan transmembrane proteins, including a recently discovered coreceptor of the neuronal axon guidance molecule SLT-1/Slit.
18547526	3	55	part_of	proteins	493:500	arg1	the ectodomains	proteins		the ectodomains		Fterm	Site	proteins		ectodomains	RBL domains, first isolated from the eggs of marine species, are also found in the ectodomains of other metazoan transmembrane proteins, including a recently discovered coreceptor of the neuronal axon guidance molecule SLT-1/Slit.
3550808	1	18	part_of	elastase	101:108	arg1	The complete amino acid sequence	neutrophil elastase		The complete amino acid sequence		PUBTATOR	Site	neutrophil elastase	1991	sequence	The complete amino acid sequence of human neutrophil elastase has been determined.
14754895	3	47	part_of	ACE2	587:590	arg1	the ACE2 extracellular domains	ACE2		the ACE2 extracellular domains		OGER	Site	ACE2	Q9BYF1	domains	To gain further insights into this enzyme, the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains were solved to 2.2- and 3.0-A resolution, respectively.
25500532	6	12	part_of	receptor	706:713	arg1	the IL-18 receptor second domain	IL-18 receptor		the IL-18 receptor second domain		PUBTATOR	Site	IL-18 receptor	3606	domain	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	6	14	part_of	IL-18	700:704	arg1	the IL-18 receptor second domain	IL-18 receptor		the IL-18 receptor second domain		PUBTATOR	Site	IL-18 receptor	3606	domain	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
24841998	7	90	gly	N-glycosylation	1110:1124	arg2	total 27 N-glycosylation sites			total 27 N-glycosylation sites						sites	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
18214858	2	46	part_of	has	404:406	arg1	an acute phase protein AND four potential N-glycosylation sites	an acute phase protein		four potential N-glycosylation sites		Fterm	Site	protein		sites	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	2	46	part_of	has	404:406	arg1	Haptoglobin AND four potential N-glycosylation sites	Haptoglobin		four potential N-glycosylation sites		PUBTATOR	Site	Haptoglobin	3240	sites	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
3342889	4	6	part_of	cathepsin	499:507	arg1	the propeptide	cathepsin H		the propeptide		PUBTATOR	Site	cathepsin H	1512	propeptide	The glycosylated mini chain is a proteolytic fragment of the propeptide of cathepsin H. Human cathepsin L has 217 amino acid residues and an Mr of 23720.
3342889	4	44	part_of	has	530:532	arg1	Human cathepsin L AND 217 amino acid residues	Human cathepsin L		217 amino acid residues		PUBTATOR	Site	cathepsin L	1514	residues	The glycosylated mini chain is a proteolytic fragment of the propeptide of cathepsin H. Human cathepsin L has 217 amino acid residues and an Mr of 23720.
10029548	7	67	gly	glycosylation	1087:1099	arg1	hTF/2N	hTF		Ser-32		OGER		hTF	P02787	Ser-32	Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N.
8026573	5	4	part_of	protein	790:796	arg1	the protein C alpha-H alpha region	protein C alpha-H		the protein C alpha-H alpha region		OGER	Site	protein C alpha-H	P02810	region	Most carbohydrate 1H-13C correlations appear in a distinct region between the aromatic region and the protein C alpha-H alpha region.
8026573	5	55	part_of	C	798:798	arg1	the protein C alpha-H alpha region	protein C alpha-H		the protein C alpha-H alpha region		OGER	Site	protein C alpha-H	P02810	region	Most carbohydrate 1H-13C correlations appear in a distinct region between the aromatic region and the protein C alpha-H alpha region.
8026573	5	58	part_of	alpha-H	800:806	arg1	the protein C alpha-H alpha region	protein C alpha-H		the protein C alpha-H alpha region		OGER	Site	protein C alpha-H	P02810	region	Most carbohydrate 1H-13C correlations appear in a distinct region between the aromatic region and the protein C alpha-H alpha region.
27384988	0	42	gly	glycosylated	75:86	arg1	Ribosomal protein S3	Ribosomal protein S3				PUBTATOR		Ribosomal protein S3	6188		Ribosomal protein S3 (rpS3) secreted from various cancer cells is N-linked glycosylated.
27384988	0	42	gly	glycosylated	75:86	arg1	rpS3	rpS3				PUBTATOR		rpS3	6188		Ribosomal protein S3 (rpS3) secreted from various cancer cells is N-linked glycosylated.
21757702	2	16	gly	sites	297:301	arg1	mouse Notch1 (mN1) using the consensus sequence C(1)XSXPC(2)			mouse Notch1 (mN1) using the consensus sequence C(1)XSXPC(2)	mouse Notch1 (mN1) using the consensus sequence C(1)XSXPC(2)		SpecificSite			sequence C(1)	Here we examine the occupancy of the predicted O-glucose sites on mouse Notch1 (mN1) using the consensus sequence C(1)XSXPC(2).
18930737	6	41	gly	N-glycosylation	858:872	arg2	Asn77			Asn77						Asn77	The amino acid sequence of PIP contains one potential N-glycosylation site at Asn77, and the same is found glycosylated with four sugar residues.
18930737	6	41	gly	N-glycosylation	858:872	arg2	one potential N-glycosylation site			one potential N-glycosylation site						site	The amino acid sequence of PIP contains one potential N-glycosylation site at Asn77, and the same is found glycosylated with four sugar residues.
17960739	4	61	gly	conversion	565:574	arg1	Asn			Asn						Asn	After immunoprecipitation, CD9P-1 was subjected to enzymatic PNGase F cleavage of N-glycans, resulting in Asn to Asp conversion and increase in 1 mass unit.
22448645	8	65	gly	N-glycosylation	1285:1299	arg1	the 5-HT(7) receptor	the 5-HT(7) receptor				Fterm		receptor			We conclude that N-glycosylation is not important for cell surface expression of the 5-HT(7) receptor.
17255936	3	16	part_of	KIT	488:490	arg1	the extracellular ligand-binding domains	KIT		the extracellular ligand-binding domains		PUBTATOR	Site	KIT	3815	domains	We report a 2.5 A crystal structure of the functional core of SCF bound to the extracellular ligand-binding domains of KIT.
19088065	12	35	gly	sialylation	1587:1597	arg1	KLK6	KLK6				Cterm		KLK6			Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	12	85	gly	KLK6	1602:1605	arg1	the extensive and almost exclusive sialylation	KLK6			the extensive and almost exclusive sialylation	Cterm		KLK6			Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
17563389	5	60	gly	nonglycosylated	1021:1035	arg1	nonglycosylated NK1R	nonglycosylated NK1R				PUBTATOR		NK1R	6869		All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
1991473	0	31	part_of	lutropin	95:102	arg1	individual glycosylation sites	lutropin		individual glycosylation sites		Fterm	Site	lutropin		sites	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
26467158	7	14	part_of	BACE1-derived	1239:1251	arg1	BACE1-derived glycopeptides	BACE1		BACE1-derived glycopeptides		PUBTATOR	Site	BACE1	23821	glycopeptides	We purified BACE1 from Neuro2A cells and performed LC/ESI/MS analysis for BACE1-derived glycopeptides and mapped bisecting GlcNAc-modified sites on BACE1.
15728350	2	3	part_of	ICAM-3	317:322	arg1	the ICAM-3 N-terminal domain	structure of the ICAM-3 N-terminal		the ICAM-3 N-terminal domain		PUBTATOR	Site	structure of the ICAM-3 N-terminal	3385	domain	We report a 1.65-A-resolution crystal structure of the ICAM-3 N-terminal domain (D1) in complex with the inserted domain, the ligand-binding domain of alphaLbeta2.
15728350	2	5	part_of	N-terminal	324:333	arg1	the ICAM-3 N-terminal domain	structure of the ICAM-3 N-terminal		the ICAM-3 N-terminal domain		PUBTATOR	Site	structure of the ICAM-3 N-terminal	3385	domain	We report a 1.65-A-resolution crystal structure of the ICAM-3 N-terminal domain (D1) in complex with the inserted domain, the ligand-binding domain of alphaLbeta2.
2387072	5	1	gly	glycopeptides	1486:1498	arg2	the peripheral membrane glycopeptides			the peripheral membrane glycopeptides						glycopeptides	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	5	44	gly	glycoprotein	1218:1229	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	5	44	gly	glycoprotein	1218:1229	arg1	fibronectin	fibronectin				PUBTATOR		fibronectin	2335		Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
9343410	7	58	gly	domain	1315:1320	arg1	a signal				a signal						We propose the hypothesis that the removal of O-GlcNAc from an interaction domain can be a signal for protein association.
9343410	7	58	gly	domain	1315:1320	arg1	the removal				the removal						We propose the hypothesis that the removal of O-GlcNAc from an interaction domain can be a signal for protein association.
14764083	9	9	part_of	Asn281	1308:1313	arg1	bLF-A	bLF		Asn281		Cterm	AminoAcid	bLF	3131	Asn281	This difference is due to glycosylation at Asn281 in bLF-A.
24977290	10	88	gly	glycosylation	1676:1688	arg2	several glycosylation sites			several glycosylation sites						sites	CONCLUSIONS: Our data identify several glycosylation sites on plasma derived ADAMTS13.
7008791	0	7	gly	glycopeptides	46:58	arg2	the three glycopeptides			the three glycopeptides						glycopeptides	Amino acid sequence and location of the three glycopeptides in the Fc region of human immunoglobulin D.
1457969	8	18	gly	hTSH	1609:1612	arg1	the N-glycans	hTSH			the N-glycans	OGER		hTSH			Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
11733580	2	6	gly	O-glycosylated	375:388	arg1	the NH2 terminus	CCR5		terminus		PUBTATOR		CCR5	1234	terminus	We provide evidence that CCR5 is O-glycosylated on serine 6 in the NH2 terminus.
11733580	2	6	gly	O-glycosylated	375:388	arg1	serine 6	CCR5		serine 6		PUBTATOR		CCR5	1234	serine 6	We provide evidence that CCR5 is O-glycosylated on serine 6 in the NH2 terminus.
8034632	1	45	part_of	Mucin	112:116	arg1	Mucin glycopeptides	Mucin		Mucin glycopeptides		PUBTATOR	Site	Mucin	100508689	glycopeptides	Mucin glycopeptides were prepared from the sputum of a patient suffering from cystic fibrosis.
32366695	2	36	gly	glycoprotein	295:306	arg1	the spike (S) glycoprotein	the spike (S) glycoprotein				Fterm		glycoprotein			Vaccine development is focused on the principal target of the humoral immune response, the spike (S) glycoprotein, which mediates cell entry and membrane fusion.
12654314	4	53	gly	N-glycosylation	926:940	arg2	the N-glycosylation sites			the N-glycosylation sites						sites	The oligosaccharide side chains of monoclonal IgM 12A1 were characterized at each of the N-glycosylation sites.
16037490	5	7	gly	glycopeptide	1263:1274	arg2	the glycopeptide			the glycopeptide						glycopeptide	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16037490	5	79	gly	O-glycosylation	1103:1117	arg2	a new O-glycosylation site			a new O-glycosylation site						site	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16803907	3	62	part_of	CD48	565:568	arg1	the receptor-binding domain	CD48		the receptor-binding domain		PUBTATOR	Site	CD48	245962	domain	Structures of CD2 and CD244 have been solved previously, and we now present the structure of the receptor-binding domain of rat CD48.
24090084	5	50	gly	N-glycopeptides	877:891	arg2	the former N-glycopeptides			the former N-glycopeptides						N-glycopeptides	The first set of aliquots were treated with peptide-N-glycosidase F (PNGase F) to remove N-glycans and the former N-glycopeptides analyzed by nano-RPLC-MS/MS (pH 2.7) and identified by Mascot database search.
9169007	7	5	part_of	antithrombin	1124:1135	arg1	Asn 155	antithrombin		Asn 155		PUBTATOR	SpecificSite	antithrombin	462	Asn 155	These results demonstrate that heterogeneous glycosylation of Asn 155 of recombinant antithrombin is responsible for generating the low heparin affinity glycoform.
9295302	7	47	gly	utilized	1143:1150	arg2	the sequon			the sequon						sequon	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	7	47	gly	utilized	1143:1150	arg2	Asn354			Asn354						Asn354	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	7	93	gly	N-glycosylation	1187:1201	arg2	approximate sites			approximate sites						sites	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
17286803	3	61	gly	glycosylation	351:363	arg1	CLN3	CLN3				OGER		CLN3	Q13286		We now examined the role of glycosylation and the C-terminal CAAX motif in lysosomal transport of CLN3 in non-neuronal and neuronal cells.
12927778	2	34	gly	glycoproteins	253:265	arg1	membrane glycoproteins	membrane glycoproteins				Fterm		glycoproteins			We have here characterized membrane glycoproteins containing terminal alpha-mannose residues in rat brain membranes.
12927778	2	3	gly	containing	267:276	arg1	membrane glycoproteins AND terminal alpha-mannose residues	membrane glycoproteins			terminal alpha-mannose residues	Fterm		glycoproteins			We have here characterized membrane glycoproteins containing terminal alpha-mannose residues in rat brain membranes.
25374123	9	4	part_of	vitronectin	1352:1362	arg1	12 N-glycopeptides	vitronectin		12 N-glycopeptides		PUBTATOR	Site	vitronectin	7448	N-glycopeptides	As a result, a total of 17 site-specific N-glycopeptides were completely identified in all of the three N-glycosylation sites of vitronectin in human plasma, including 12 N-glycopeptides first reported.
25374123	9	4	part_of	vitronectin	1352:1362	arg1	the three N-glycosylation sites	vitronectin		the three N-glycosylation sites		PUBTATOR	Site	vitronectin	7448	sites	As a result, a total of 17 site-specific N-glycopeptides were completely identified in all of the three N-glycosylation sites of vitronectin in human plasma, including 12 N-glycopeptides first reported.
18533687	9	19	gly	glycosylation	1534:1546	arg2	glycosylation sites			glycosylation sites						sites	However, combinations of glycosylation sites were required for cell surface expression and cAMP signaling.
15173186	5	11	gly	leucine-rich	696:707	arg1	leucine-rich repeats			leucine	leucine-rich repeats					leucine	Toll-like receptors have leucine-rich repeats in their extracellular domains and are thus believed to adopt solenoid structures, similar to that found in platelet glycoprotein Ib.
15173186	5	31	gly	glycoprotein	834:845	arg1	platelet glycoprotein Ib	platelet glycoprotein Ib				Fterm		glycoprotein			Toll-like receptors have leucine-rich repeats in their extracellular domains and are thus believed to adopt solenoid structures, similar to that found in platelet glycoprotein Ib.
15173186	5	45	gly	repeats	709:715	arg1	their extracellular domains			their extracellular domains	their extracellular domains		Site			domains	Toll-like receptors have leucine-rich repeats in their extracellular domains and are thus believed to adopt solenoid structures, similar to that found in platelet glycoprotein Ib.
15173186	5	56	gly	have	691:694	arg1	Toll-like receptors AND leucine-rich repeats	Toll-like receptors			leucine-rich repeats	Fterm		receptors			Toll-like receptors have leucine-rich repeats in their extracellular domains and are thus believed to adopt solenoid structures, similar to that found in platelet glycoprotein Ib.
24058541	3	43	gly	N-glycosylation	318:332	arg2	eight potential N-glycosylation sites			eight potential N-glycosylation sites						sites	CLN5 has eight potential N-glycosylation sites based on the Asn-X-Thr/Ser consensus sequence.
7505568	0	30	part_of	glycoprotein	70:81	arg1	the glycosylated sequons	myelin-associated glycoprotein		the glycosylated sequons		PUBTATOR		myelin-associated glycoprotein	4099		Identification of the glycosylated sequons of human myelin-associated glycoprotein.
11258925	6	5	gly	glycopeptides	1076:1088	arg2	potential glycopeptides			potential glycopeptides						glycopeptides	The MALDI MS analysis of a tryptic digest of the protein showed a number of potential glycopeptides.
21757702	2	82	part_of	Notch1	312:317	arg1	mouse Notch1 (mN1) using the consensus sequence C(1)XSXPC(2)	Notch1		mouse Notch1 (mN1) using the consensus sequence C(1)XSXPC(2)		PUBTATOR	SpecificSite	Notch1	18128	sequence C(1)	Here we examine the occupancy of the predicted O-glucose sites on mouse Notch1 (mN1) using the consensus sequence C(1)XSXPC(2).
17614963	1	38	gly	glycoprotein	120:131	arg1	young age-related urinary glycoprotein	young age-related urinary glycoprotein				Fterm		glycoprotein			Ugl-Y (young age-related urinary glycoprotein) is an age-specific protein that we have previously identified in urine from healthy subjects under 18 years of age.
19088065	0	38	gly	N-glycosylation	13:27	arg1	kallikrein 6	kallikrein 6				Fterm		kallikrein 6			Differential N-glycosylation of kallikrein 6 derived from ovarian cancer cells or the central nervous system.
8615697	13	118	gly	glycopeptide	2351:2362	arg2	the purified glycopeptide population			the purified glycopeptide population						glycopeptide	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
21757702	11	17	part_of	Notch	1533:1537	arg1	the Abruptex region	Notch		the Abruptex region		PUBTATOR	Site	Notch	18128	region	Interestingly, elimination of the site in EGF 28, found in the Abruptex region of Notch, does significantly reduce activity.
10889209	5	53	part_of	GIRK1	729:733	arg1	GIRK1 membrane-spanning domain 1	GIRK1		GIRK1 membrane-spanning domain 1		PUBTATOR	Site	GIRK1	3760	domain	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	5	67	part_of	GIRK4	846:850	arg1	GIRK4 membrane-spanning domain 1	GIRK4		GIRK4 membrane-spanning domain 1		PUBTATOR	Site	GIRK4	3762	domain	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
25456591	4	19	gly	glycopeptide	917:928	arg2	glycopeptide			glycopeptide						glycopeptide	Each glycopeptide assignment was verified by the detection of glycan-specific fragments using collision-induced dissociation (CID) to estimate False Discovery Rate (FDR).
21317871	2	39	part_of	domain	386:391	arg1	AMPARs	AMPARs		domain		PUBTATOR	Site	AMPARs	2891	domain	The distal, N-terminal domain (NTD) has allosteric potential in NMDA-type iGluRs, which has not been ascribed to the analogous domain in AMPA receptors (AMPARs).
21317871	2	39	part_of	domain	386:391	arg1	AMPA receptors	receptors		domain		Fterm	Site	receptors		domain	The distal, N-terminal domain (NTD) has allosteric potential in NMDA-type iGluRs, which has not been ascribed to the analogous domain in AMPA receptors (AMPARs).
26536155	3	91	gly	glycopeptides	698:710	arg2	glycopeptides			glycopeptides						glycopeptides	The use of unspecific proteases such as Pronase can largely overcome this problem by generating glycopeptides with a small peptide portion.
16834341	6	27	part_of	hFSH	872:875	arg1	Asn7	hFSH		Asn7		OGER	AminoAcid	hFSH		Asn7	For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms.
1904059	3	15	gly	linked	412:417	arg2	serine 52 AND Xyl2-Glc			serine 52	Xyl2-Glc					serine 52	Earlier studies demonstrated a novel disaccharide (Xyl-Glc) or trisaccharide (Xyl2-Glc) O-glycosidically linked to serine 52 in human plasma factor VII (Nishimura, H., Kawabata, S., Kisiel, W., Hase, S., Ikenaka, T., Shimonishi, Y., and Iwanaga, S. (1989) J. Biol.
1904059	3	15	gly	linked	412:417	arg2	serine 52 AND a novel disaccharide			serine 52	a novel disaccharide					serine 52	Earlier studies demonstrated a novel disaccharide (Xyl-Glc) or trisaccharide (Xyl2-Glc) O-glycosidically linked to serine 52 in human plasma factor VII (Nishimura, H., Kawabata, S., Kisiel, W., Hase, S., Ikenaka, T., Shimonishi, Y., and Iwanaga, S. (1989) J. Biol.
1904059	3	15	gly	linked	412:417	arg2	serine 52 AND Xyl-Glc			serine 52	Xyl-Glc					serine 52	Earlier studies demonstrated a novel disaccharide (Xyl-Glc) or trisaccharide (Xyl2-Glc) O-glycosidically linked to serine 52 in human plasma factor VII (Nishimura, H., Kawabata, S., Kisiel, W., Hase, S., Ikenaka, T., Shimonishi, Y., and Iwanaga, S. (1989) J. Biol.
2808371	5	36	part_of	contain	1030:1036	arg1	Multiple protein 4.1 isoforms AND this sequence	Multiple protein 4.1 isoforms		this sequence		PUBTATOR	Site	protein 4.1 isoforms	281753	sequence	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
11741940	11	110	part_of	protein	1932:1938	arg1	Phe	protein		Asp(41) and Phe(50)		Fterm	SpecificSite	protein		Asp(41) and Phe(50)	The predominant N terminus was Ser(31), although minor amounts of the protein with Asp(41) and Phe(50) as the N termini were observed.
11741940	11	110	part_of	protein	1932:1938	arg1	Asp(41)	protein		Asp(41) and Phe(50)		Fterm	SpecificSite	protein		Asp(41) and Phe(50)	The predominant N terminus was Ser(31), although minor amounts of the protein with Asp(41) and Phe(50) as the N termini were observed.
11741940	11	110	part_of	protein	1932:1938	arg1	Asp(41)	protein		Asp(41) and Phe(50)		Fterm	SpecificSite	protein		Asp(41) and Phe(50)	The predominant N terminus was Ser(31), although minor amounts of the protein with Asp(41) and Phe(50) as the N termini were observed.
12063277	6	33	gly	used	862:865	arg2	N629			N629						N629	In contrast, N629 is not used for glycosylation, but mutation of this site (N629Q) causes a protein trafficking defect, which results in its intracellular retention.
22171320	3	95	gly	found	518:522	arg2	asparagine (N-linked) or serine/threonine (O-linked) residues AND glycan structures			asparagine (N-linked) or serine/threonine (O-linked) residues	glycan structures					asparagine	Glycoproteomic characterization remains difficult because of the complexity of glycan structures found mainly on asparagine (N-linked) or serine/threonine (O-linked) residues.
9334252	7	4	gly	C-mannosylated	1311:1324	arg1	C-mannosylated proteins				C-mannosylated proteins						The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	7	14	gly	C-mannosylation	1122:1136	arg1	Trp-7			Trp-7						Trp-7	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
16740002	5	47	part_of	N-glycoproteins	944:958	arg1	84 formerly N-glycosylated peptides	N-glycoproteins		84 formerly N-glycosylated peptides		Fterm	Site	N-glycoproteins		peptides	Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
26536155	1	2	gly	O-glycopeptides	222:236	arg2	O-glycopeptides			O-glycopeptides						O-glycopeptides	The analysis of N- and O-glycopeptides remains challenging due to the microheterogeneity (different glycoforms attached to one glycosylation site) and macroheterogeneity (site occupancy) of the glycoprotein.
26536155	1	13	gly	macroheterogeneity	350:367	arg1	the glycoprotein	the glycoprotein				Fterm		glycoprotein			The analysis of N- and O-glycopeptides remains challenging due to the microheterogeneity (different glycoforms attached to one glycosylation site) and macroheterogeneity (site occupancy) of the glycoprotein.
26536155	1	30	gly	glycosylation	326:338	arg2	one glycosylation site			one glycosylation site						site	The analysis of N- and O-glycopeptides remains challenging due to the microheterogeneity (different glycoforms attached to one glycosylation site) and macroheterogeneity (site occupancy) of the glycoprotein.
26536155	1	50	gly	glycoprotein	393:404	arg1	the glycoprotein	the glycoprotein				Fterm		glycoprotein			The analysis of N- and O-glycopeptides remains challenging due to the microheterogeneity (different glycoforms attached to one glycosylation site) and macroheterogeneity (site occupancy) of the glycoprotein.
26536155	1	75	gly	microheterogeneity	269:286	arg1	the glycoprotein	the glycoprotein				Fterm		glycoprotein			The analysis of N- and O-glycopeptides remains challenging due to the microheterogeneity (different glycoforms attached to one glycosylation site) and macroheterogeneity (site occupancy) of the glycoprotein.
18676855	9	55	gly	used	1655:1658	arg2	the extracellular regions			the extracellular regions						regions	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
3497198	4	73	gly	monosialylated	728:741	arg1	monosialylated chains				monosialylated chains						Asn176 of both H-2Kk and H-2Kb contained the same ratio (2.8 to 1) of bi- to monosialylated chains.
24977290	10	10	part_of	sites	1690:1694	arg1	plasma derived ADAMTS13	ADAMTS13		sites		PUBTATOR	Site	ADAMTS13	Q76LX8	sites	CONCLUSIONS: Our data identify several glycosylation sites on plasma derived ADAMTS13.
14529283	7	45	part_of	residues	1448:1455	arg1	the soluble NTPDase6	NTPDase6		residues		PUBTATOR	AminoAcid	NTPDase6	955	cysteine residues	Four of the five cysteine residues in the soluble NTPDase6 are highly conserved among all the NTPDases, while the fifth residue is not.
11080501	7	65	gly	glycosylated	1479:1490	arg1	Asn175			Asn175						sites, Asn175	Of the three potential N-linked glycosylation sites, Asn175 was not glycosylated, whereas Asn88 was completely glycosylated, and Asn51 was partially glycosylated.
11080501	7	71	gly	glycosylation	1443:1455	arg2	the three potential N-linked glycosylation sites			the three potential N-linked glycosylation sites						sites, Asn175	Of the three potential N-linked glycosylation sites, Asn175 was not glycosylated, whereas Asn88 was completely glycosylated, and Asn51 was partially glycosylated.
11080501	7	78	gly	glycosylated	1560:1571	arg1	Asn51			Asn51						Asn51	Of the three potential N-linked glycosylation sites, Asn175 was not glycosylated, whereas Asn88 was completely glycosylated, and Asn51 was partially glycosylated.
11080501	7	97	gly	glycosylated	1522:1533	arg1	Asn88			Asn88						Asn88	Of the three potential N-linked glycosylation sites, Asn175 was not glycosylated, whereas Asn88 was completely glycosylated, and Asn51 was partially glycosylated.
3200844	11	46	gly	glycoprotein	1571:1582	arg1	the 62-kDa nuclear pore glycoprotein	the 62-kDa nuclear pore glycoprotein				Fterm		glycoprotein			The partial sequence of the 62-kDa nuclear pore glycoprotein shows little similarity to other characterized proteins and elucidates structural features of a member of the family of nuclear pore glycoproteins.
3200844	11	77	gly	glycoproteins	1717:1729	arg1	nuclear pore glycoproteins	nuclear pore glycoproteins				Fterm		glycoproteins			The partial sequence of the 62-kDa nuclear pore glycoprotein shows little similarity to other characterized proteins and elucidates structural features of a member of the family of nuclear pore glycoproteins.
8323280	0	102	gly	lymphotoxin	52:62	arg1	N-linked sugar chain structure	lymphotoxin			N-linked sugar chain structure	Fterm		lymphotoxin			N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
7686446	6	32	gly	AFP	1803:1805	arg1	fucosylation	AFP			fucosylation	PUBTATOR		AFP	174		Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	6	50	gly	AFP	1676:1678	arg1	Fucosylation	AFP			Fucosylation	PUBTATOR		AFP	174		Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	6	92	gly	fucosylation	1787:1798	arg1	AFP	AFP				PUBTATOR		AFP	174		Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	6	106	gly	Fucosylation	1660:1671	arg1	AFP	AFP				PUBTATOR		AFP	174		Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
23527852	8	58	gly	glycosylation	1062:1074	arg2	the glycosylation site			the glycosylation site						site	To confirm the glycan moiety and localize the glycosylation site, top-down ESI-FTICR-MS/MS and bottom-up LC-ion trap MS/MS were used.
19153605	0	27	part_of	F-spondin	17:25	arg1	the F-spondin domain	structure of the F-spondin		the F-spondin domain		PUBTATOR	Site	structure of the F-spondin	10418	domain	Structure of the F-spondin domain of mindin, an integrin ligand and pattern recognition molecule.
19153605	0	43	part_of	mindin	37:42	arg1	the F-spondin domain	mindin		the F-spondin domain		PUBTATOR	Site	mindin	10417	domain	Structure of the F-spondin domain of mindin, an integrin ligand and pattern recognition molecule.
8702538	10	0	part_of	position	1684:1691	arg1	the CD22 and CD33 glycoproteins	CD33 glycoproteins		position		PUBTATOR	Site	CD33 glycoproteins	945	position	These observations suggest that a single N-linked glycosylation site located at a similar position in the CD22 and CD33 glycoproteins is critical for regulating ligand recognition by both receptors.
2493268	0	46	gly	glycosylated	37:48	arg1	human pancreatic stone protein	human pancreatic stone protein				OGER		pancreatic stone protein	P05451		N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein.
12218058	4	47	gly	glycosylation	886:898	arg2	all glycosylation sites			all glycosylation sites						sites	Recombinant BMP-1 molecules lacking all glycosylation sites or the three CUB-specific sites were not secreted.
9136890	4	69	gly	found	549:553	arg2	the native TfR AND the oligosaccharides	the native TfR			the oligosaccharides	PUBTATOR		TfR	7037		Human TfR isolated from placentae was used to characterize the structure of the oligosaccharides found in the native TfR.
12654314	7	63	gly	attached	1321:1328	arg2	Asn-378 AND Twelve hybrid-type oligosaccharides			Asn-378	Twelve hybrid-type oligosaccharides					Asn-378	Twelve hybrid-type oligosaccharides were attached to Asn-378, three of which had terminal sialic acids.
12654314	7	35	gly	had	1357:1359	arg1	Asn-378 AND terminal sialic acids			Asn-378	terminal sialic acids					Asn-378	Twelve hybrid-type oligosaccharides were attached to Asn-378, three of which had terminal sialic acids.
15687489	7	42	gly	glycosylated	911:922	arg1	the glycosylated human pFGE	the glycosylated human pFGE				PUBTATOR		pFGE	25870		We have crystallized the glycosylated human pFGE and determined its crystal structure at a resolution of 1.86 A.
16740002	6	43	gly	glycoproteins	974:986	arg1	16 glycoproteins	16 glycoproteins				Fterm		glycoproteins			Of these, 16 glycoproteins have not been reported previously in saliva.
8639592	0	97	gly	inhibitor	92:100	arg1	carbohydrate structure	tissue factor pathway inhibitor			carbohydrate structure	PUBTATOR		tissue factor pathway inhibitor	7035		Amino acid sequence and carbohydrate structure of a recombinant human tissue factor pathway inhibitor expressed in Chinese hamster ovary cells: one N-and two O-linked carbohydrate chains are located between Kunitz domains 2 and 3 and one N-linked carbohydrate chain is in Kunitz domain 2.
10889209	4	55	gly	glycosylated	655:666	arg2	Asn			Asn(119)						Asn(119)	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	4	55	gly	glycosylated	655:666	arg1	GIRK1	GIRK1		Asn(119)		PUBTATOR		GIRK1	3760	Asn(119)	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	4	55	gly	glycosylated	655:666	arg1	GIRK1	GIRK1		Asn(119)		PUBTATOR		GIRK1	3760	Asn(119)	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	4	68	gly	glycosylated	703:714	arg2	Asn			Asn(132)						Asn(132)	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	4	68	gly	glycosylated	703:714	arg1	GIRK4	GIRK4		Asn(132)		PUBTATOR		GIRK4	3762	Asn(132)	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	4	68	gly	glycosylated	703:714	arg1	GIRK4	GIRK4		Asn(132)		PUBTATOR		GIRK4	3762	Asn(132)	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10756055	2	57	part_of	sites	379:383	arg1	CXCR4	CXCR4		sites		PUBTATOR	Site	CXCR4	7852	sites	Here we report on the unexpected observation that the removal of the N-linked glycosylation sites in CXCR4 potentially allows the protein to serve as a universal coreceptor for both X4 and R5 laboratory-adapted and primary HIV-1 strains.
23756652	5	31	part_of	RSPO1	735:739	arg1	Both the FU-CRD1 and FU-CRD2 domains	RSPO1		Both the FU-CRD1 and FU-CRD2 domains		PUBTATOR	Site	RSPO1	284654	domains	Both the FU-CRD1 and FU-CRD2 domains of RSPO1 contribute to LGR4 interaction, and binding and cellular assays identified critical RSPO1 residues for its biological activities.
23756652	5	32	part_of	RSPO1	825:829	arg1	critical RSPO1 residues	RSPO1		critical RSPO1 residues		PUBTATOR	Site	RSPO1	284654	residues	Both the FU-CRD1 and FU-CRD2 domains of RSPO1 contribute to LGR4 interaction, and binding and cellular assays identified critical RSPO1 residues for its biological activities.
25802287	11	44	gly	glycopeptide	1711:1722	arg2	A detailed glycopeptide characterization			A detailed glycopeptide characterization						glycopeptide	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25458834	0	11	gly	O-glycosylated	61:74	arg1	O-glycosylated podoplanin	O-glycosylated podoplanin				OGER		podoplanin	Q86YL7		A platform of C-type lectin-like receptor CLEC-2 for binding O-glycosylated podoplanin and nonglycosylated rhodocytin.
25458834	0	23	gly	nonglycosylated	91:105	arg1	nonglycosylated rhodocytin	nonglycosylated rhodocytin				Fterm		rhodocytin			A platform of C-type lectin-like receptor CLEC-2 for binding O-glycosylated podoplanin and nonglycosylated rhodocytin.
9628725	5	32	part_of	beta-chain	905:914	arg1	the beta-chain domain	beta-chain		the beta-chain domain		Fterm	Site	beta-chain		domain	Additionally, we have found that the beta-chain domain, like its gamma-chain counterpart, binds calcium.
18984734	9	22	part_of	sites	1317:1321	arg1	erythrocyte proteins	proteins		sites		Fterm	Site	proteins		sites	CONCLUSIONS: GlcNAcylation is differentially regulated at individual sites on erythrocyte proteins in response to glycemic status.
3264725	2	70	gly	N-glycosylated	587:600	arg1	2 N-glycosylated asparagine residues			2 N-glycosylated asparagine residues						asparagine residues	Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues.
25092234	2	90	gly	N-glycosylation	306:320	arg2	N473			N473						N432 , N473	Its deficiency results in bleeding diathesis referred to as hemophilia C. hFXI bears five N-glycosylation consensus sites per monomer, N72 , N108 , N335 on the heavy chain and N432 , N473 on the light chain.
25092234	2	90	gly	N-glycosylation	306:320	arg2	five N-glycosylation consensus sites			five N-glycosylation consensus sites						sites	Its deficiency results in bleeding diathesis referred to as hemophilia C. hFXI bears five N-glycosylation consensus sites per monomer, N72 , N108 , N335 on the heavy chain and N432 , N473 on the light chain.
25092234	2	90	gly	N-glycosylation	306:320	arg2	N335			N72 , N108 , N335						N72 , N108 , N335	Its deficiency results in bleeding diathesis referred to as hemophilia C. hFXI bears five N-glycosylation consensus sites per monomer, N72 , N108 , N335 on the heavy chain and N432 , N473 on the light chain.
11588155	1	79	gly	B100	279:282	arg1	The carbohydrate composition	apolipoprotein (apo) B100			The carbohydrate composition	PUBTATOR		apolipoprotein (apo) B100	338		The carbohydrate composition of apolipoprotein (apo) B100, particularly its degree of sialylation, may contribute to the atherogenic properties of low-density lipoprotein (LDL).
25802287	10	73	gly	deglycosylated	1619:1632	arg1	all five deglycosylated peptides			all five deglycosylated peptides						peptides	By scanning the treated spots with low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS, we observed all five deglycosylated peptides, including the one originating from the secretory chain.
23027977	5	22	part_of	Enpp1	628:632	arg1	the extracellular region	Enpp1		the extracellular region		PUBTATOR	Site	Enpp1	18605	region	Here, we report the crystal structures of the extracellular region of mouse Enpp1 in complex with four different nucleotide monophosphates, at resolutions of 2.7-3.2 Å.
16263699	6	55	gly	glycosylated	973:984	arg1	glycosylated proteins	glycosylated proteins				Fterm		proteins			Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
14760718	9	64	gly	N-glycosylation	1291:1305	arg2	86 N-glycosylation sites			86 N-glycosylation sites						sites	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
3458201	5	16	part_of	has	714:716	arg1	alpha 1B AND a unique amino acid sequence	alpha 1B		a unique amino acid sequence		PUBTATOR	Site	alpha 1B	1	sequence	alpha 1B has a unique amino acid sequence.
10419520	9	39	gly	glycosylated	1223:1234	arg1	the long hydrophilic sequences			the long hydrophilic sequences						sequences	All three of the long hydrophilic sequences of S2P can be glycosylated, indicating that they all project into the lumen.
24841998	11	88	gly	N-glycopeptides	1697:1711	arg2	intact sialylated N-glycopeptides			intact sialylated N-glycopeptides						N-glycopeptides	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	11	102	gly	sialylated	1686:1695	arg1	intact sialylated N-glycopeptides			intact sialylated N-glycopeptides						N-glycopeptides	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
17015441	1	47	gly	glycosylation	118:130	arg1	mouse TRPM8	mouse TRPM8				PUBTATOR		TRPM8	Q7Z2W7		We have investigated the glycosylation, disulfide bonding, and subunit structure of mouse TRPM8.
1381905	5	13	gly	deglycosylated	839:852	arg1	a deglycosylated C-terminal peptide			a deglycosylated C-terminal peptide						peptide	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	5	77	gly	deglycosylated	813:826	arg1	the deglycosylated SCF	the deglycosylated SCF				OGER		SCF	P21583		Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1468573	1	7	gly	urokinase	220:228	arg1	enzymically released N-linked carbohydrate chains	urokinase			enzymically released N-linked carbohydrate chains	Fterm		urokinase			Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	14	gly	oligosaccharides	332:347	arg1	the only N-glycosylation site			the only N-glycosylation site	the only N-glycosylation site		Site			site	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	35	gly	N-glycosylation	361:375	arg2	the only N-glycosylation site			the only N-glycosylation site						site	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
12654314	8	1	gly	attached	1425:1432	arg2	Asn-331 AND Eleven hybrid-type oligosaccharides			Asn-331	Eleven hybrid-type oligosaccharides					Asn-331	Eleven hybrid-type oligosaccharides were attached to Asn-331, seven of which had terminal sialic acids.
12654314	8	9	gly	had	1461:1463	arg1	Asn-331 AND terminal sialic acids			Asn-331	terminal sialic acids					Asn-331	Eleven hybrid-type oligosaccharides were attached to Asn-331, seven of which had terminal sialic acids.
8216207	0	17	gly	site	63:66	arg1	soluble recombinant human thrombomodulin	thrombomodulin			site	PUBTATOR		thrombomodulin	7056		Identification of the predominant glycosaminoglycan-attachment site in soluble recombinant human thrombomodulin: potential regulation of functionality by glycosyltransferase competition for serine474.
3497398	0	87	gly	glycoprotein	85:96	arg1	platelet membrane glycoprotein Ib	platelet membrane glycoprotein Ib				Fterm		glycoprotein			Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib.
20036257	8	60	part_of	proNGF	1055:1060	arg1	the pro regions	NGF		the pro regions		OGER	AminoAcid	NGF	P01138	pro regions	In the proNGF-p75NTR complex, the pro regions of proNGF are mostly disordered and two hairpin loops (loop 2) at the top of the NGF dimer have undergone conformational changes in comparison with mature NT structures, suggesting possible interactions with the propeptide.
20624874	7	29	gly	glycoproteins	1608:1620	arg1	other plasma glycoproteins	other plasma glycoproteins				Fterm		glycoproteins			Lectin blot analysis indicated the presence of non-reducing terminal α2-6 and α2-3-linked sialic acid residues with penultimate β-galactose residues on the N- and O-linked sugar chains of pADAMTS13, suggesting that pADAMTS13 is cleared from the circulation via the hepatic asialoglycoprotein receptor like other plasma glycoproteins.
20624874	7	36	gly	asialoglycoprotein	1562:1579	arg1	the hepatic asialoglycoprotein receptor	the hepatic asialoglycoprotein receptor				Fterm		asialoglycoprotein			Lectin blot analysis indicated the presence of non-reducing terminal α2-6 and α2-3-linked sialic acid residues with penultimate β-galactose residues on the N- and O-linked sugar chains of pADAMTS13, suggesting that pADAMTS13 is cleared from the circulation via the hepatic asialoglycoprotein receptor like other plasma glycoproteins.
20624874	7	51	gly	pADAMTS13	1477:1485	arg1	O-linked sugar chains	pADAMTS13			O-linked sugar chains	Cterm		pADAMTS13	11093		Lectin blot analysis indicated the presence of non-reducing terminal α2-6 and α2-3-linked sialic acid residues with penultimate β-galactose residues on the N- and O-linked sugar chains of pADAMTS13, suggesting that pADAMTS13 is cleared from the circulation via the hepatic asialoglycoprotein receptor like other plasma glycoproteins.
20624874	7	51	gly	pADAMTS13	1477:1485	arg1	N-	pADAMTS13			N-	Cterm		pADAMTS13	11093		Lectin blot analysis indicated the presence of non-reducing terminal α2-6 and α2-3-linked sialic acid residues with penultimate β-galactose residues on the N- and O-linked sugar chains of pADAMTS13, suggesting that pADAMTS13 is cleared from the circulation via the hepatic asialoglycoprotein receptor like other plasma glycoproteins.
2059624	2	43	part_of	r-HPg	502:506	arg1	Asn289	r-HPg		Asn289		Cterm	AminoAcid	r-HPg	P00747	Asn289	Previous studies from this laboratory have established that lepidopteran insect cells possess the glycosylation machinery needed to assemble N-linked complex-type oligosaccharides on Asn289 of recombinant human plasminogen (r-HPg).
2528451	0	0	part_of	P40	66:68	arg1	Complete amino acid sequence	T-cell growth factor P40		Complete amino acid sequence		PUBTATOR	Site	T-cell growth factor P40	16198	sequence	Complete amino acid sequence of a new murine T-cell growth factor P40.
9336835	6	11	gly	glycopeptides	1067:1079	arg2	tryptic glycopeptides			tryptic glycopeptides						glycopeptides	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning was used to selectively identify and preparatively fractionate tryptic glycopeptides.
23050552	7	62	gly	O-glycopeptides	910:924	arg2	the generated O-glycopeptides			the generated O-glycopeptides						O-glycopeptides	MS3 spectra of the generated O-glycopeptides showed cleavages of the peptide backbone and provided essential information on the peptide sequence.
10413465	5	26	part_of	apoE2	1166:1170	arg1	the O-glycosylation site	apoE2		the O-glycosylation site		PUBTATOR	Site	apoE2	348	site	This analysis showed that a mutation in the O-glycosylation site of apoE2 (Thr194-Ala) did not affect the SDS-stable binding of apoE to Abeta.
16037490	4	17	part_of	isoform	1052:1058	arg1	Asn1007	isoform		Asn1007		Fterm	AminoAcid	isoform		Asn1007 and Asn2108	There was a remarkable site-specific difference in fucosylation between these isoforms; Asn1244 selectively escaped the global fucosylation of cellular FN, whereas only Asn1007 and Asn2108 of the plasma isoform underwent modification.
8349699	1	93	gly	N-glycosylated	258:271	arg1	Asn410			Asn68, Asn144, and Asn410						Asn68, Asn144, and Asn410	Using site-directed mutagenesis, we have determined that Asn68, Asn144, and Asn410 of ovine prostaglandin endoperoxide (PGH) synthase-1 are N-glycosylated.
8349699	1	93	gly	N-glycosylated	258:271	arg1	Asn68			Asn68, Asn144, and Asn410						Asn68, Asn144, and Asn410	Using site-directed mutagenesis, we have determined that Asn68, Asn144, and Asn410 of ovine prostaglandin endoperoxide (PGH) synthase-1 are N-glycosylated.
8349699	1	93	gly	N-glycosylated	258:271	arg1	Asn68			Asn68, Asn144, and Asn410						Asn68, Asn144, and Asn410	Using site-directed mutagenesis, we have determined that Asn68, Asn144, and Asn410 of ovine prostaglandin endoperoxide (PGH) synthase-1 are N-glycosylated.
23236605	2	20	gly	N-glycosylation	369:383	arg2	N-glycosylation sites			N-glycosylation sites						sites	Inactivation of N-glycosylation sites revealed that mouse AIM contains two N-glycans in the first and second scavenger receptor cysteine-rich domains, and that depletion of N-glycans decreased AIM secretion from producing cells.
23236605	2	42	gly	N-glycans	428:436	arg1	the first and second scavenger receptor cysteine-rich domains			the first and second scavenger receptor cysteine-rich domains	the first and second scavenger receptor cysteine-rich domains		Site			domains	Inactivation of N-glycosylation sites revealed that mouse AIM contains two N-glycans in the first and second scavenger receptor cysteine-rich domains, and that depletion of N-glycans decreased AIM secretion from producing cells.
23236605	2	34	gly	contains	415:422	arg1	mouse AIM AND two N-glycans	mouse AIM			two N-glycans	OGER		AIM	Q07108		Inactivation of N-glycosylation sites revealed that mouse AIM contains two N-glycans in the first and second scavenger receptor cysteine-rich domains, and that depletion of N-glycans decreased AIM secretion from producing cells.
11710528	7	15	gly	hTR	956:958	arg1	the high mannose-type oligosaccharides	hTR			the high mannose-type oligosaccharides	PUBTATOR		hTR	P25116		Our results demonstrate that the high mannose-type oligosaccharides of hTR ranged in size from Man5-R to Man9-R with cell-type specific patterns.
25187573	2	84	gly	glycosylation	355:367	arg1	lubricin	lubricin				PUBTATOR		lubricin	10216		Thus, a site-specific investigation of the glycosylation of lubricin was undertaken, in order to further understand the pathological mechanisms involved in these diseases.
11080501	1	26	gly	glycoprotein	204:215	arg1	a cell surface glycoprotein	a cell surface glycoprotein				Fterm		glycoprotein			The GA733-2 antigen is a cell surface glycoprotein highly expressed on most human gastrointestinal carcinoma and at a lower level on most normal epithelia.
17015441	4	25	gly	glycoproteins	625:637	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Unmodified TRPM8 migrates with an apparent mass of 129 kDa and can be glycosylated in Chinese hamster ovary cells to give glycoproteins with apparent masses of 136 and 147 kDa.
17015441	4	29	gly	glycosylated	573:584	arg1	Unmodified TRPM8	Unmodified TRPM8				PUBTATOR		Unmodified TRPM8	Q7Z2W7		Unmodified TRPM8 migrates with an apparent mass of 129 kDa and can be glycosylated in Chinese hamster ovary cells to give glycoproteins with apparent masses of 136 and 147 kDa.
26846330	2	32	gly	glycosylated	430:441	arg1	all seven possible sites			all seven possible sites						sites	We have determined the crystal structure of glycosylated NPC1 luminal domain C and find all seven possible sites are glycosylated.
12646248	4	37	part_of	protease	576:583	arg1	a serine protease domain	protease		a serine protease domain		Fterm	Site	protease		domain	The molecule consists of a unique eight-bladed beta-propeller domain in the N-terminal region and a serine protease domain in the C-terminal region.
12646248	4	19	part_of	domain	585:590	arg1	the C-terminal region			region						region	The molecule consists of a unique eight-bladed beta-propeller domain in the N-terminal region and a serine protease domain in the C-terminal region.
12646248	4	36	part_of	domain	531:536	arg1	the C-terminal region			region						region	The molecule consists of a unique eight-bladed beta-propeller domain in the N-terminal region and a serine protease domain in the C-terminal region.
3345749	3	77	gly	glycopeptides	422:434	arg1	Carbohydrate chains			glycopeptides	Carbohydrate chains					glycopeptides	Carbohydrate chains of respiratory-mucus glycopeptides from a patient (blood group O) suffering from bronchiectasis with a Kartagener's syndrome have been released by alkaline borohydride treatment.
21805521	8	109	part_of	huDKK1	1558:1563	arg1	the huDKK1 N-terminal domain	huDKK1		the huDKK1 N-terminal domain		Cterm	Site	huDKK1	22943	domain	The five disulfide bonds within the huDKK1 N-terminal domain are unique to the DKK family proteins; there are no exact matches in disulfide positioning when compared to other known disulfide clusters.
16847056	3	75	part_of	beta2	411:415	arg1	Pro5	beta2		Pro5		Cterm	AminoAcid	beta2		Pro5	To determine whether beta2-linked sialic acids similarly impact Nav gating, we co-expressed beta2 with Nav1.5 or Nav1.2 in Pro5 (complete sialylation) and in Lec2 (essentially no sialylation) cells.
1472036	3	24	part_of	containing	675:684	arg1	the peptide AND Cys524	the peptide		Cys524						Cys524	The peptides containing Cys435 and Cys468 appeared in the same fraction, indicating that these two form a disulfide bond, and in another fraction we found the sequence of the peptide containing Cys524.
1472036	3	3	part_of	containing	505:514	arg1	The peptides AND Cys468			Cys435 and Cys468						Cys435 and Cys468	The peptides containing Cys435 and Cys468 appeared in the same fraction, indicating that these two form a disulfide bond, and in another fraction we found the sequence of the peptide containing Cys524.
8053566	6	45	part_of	TIMP	1286:1289	arg1	Both TIMP glycosylation sites	Both TIMP		Both TIMP glycosylation sites		PUBTATOR	Site	Both TIMP	7076	sites	Both TIMP glycosylation sites exhibited extensive heterogeneity comprising mainly fucosylated complex oligosaccharides, but in different proportions.
6118137	2	7	gly	glycoprotein	147:158	arg1	the Thy-1 membrane glycoprotein	the Thy-1 membrane glycoprotein				OGER		Thy-1 membrane glycoprotein	P01830		The full sequence of the Thy-1 membrane glycoprotein of rat brain is reported.
23829323	7	41	gly	glycopeptides	1398:1410	arg2	glycopeptides			glycopeptides						glycopeptides	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	7	49	gly	glycoprotein	1317:1328	arg1	a human glycoprotein standard	a human glycoprotein standard				Fterm		glycoprotein			We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	7	49	gly	glycoprotein	1317:1328	arg1	haptoglobin	haptoglobin				PUBTATOR		haptoglobin	3240		We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
15961631	0	20	part_of	receptor	37:44	arg1	human toll-like receptor 3 (TLR3) ectodomain	toll-like receptor 3		human toll-like receptor 3 (TLR3) ectodomain		PUBTATOR	Site	toll-like receptor 3	7098	ectodomain	Crystal structure of human toll-like receptor 3 (TLR3) ectodomain.
20427285	5	53	part_of	ZPI	672:674	arg1	four ZPI contact residues	ZPI		four ZPI contact residues		PUBTATOR	Site	ZPI	51156	residues	Mutation of four ZPI contact residues eliminated PZ binding and membrane-dependent PZ acceleration of fXa inhibition.
8163535	5	8	part_of	protein	867:873	arg1	The extracellular domain	protein		The extracellular domain		Fterm	Site	protein		domain	The extracellular domain of the syndecan-1 core protein contains five Ser-Gly sites, three clustered near its N terminus and two adjacent to the transmembrane domain near its C terminus.
8163535	5	25	part_of	contains	875:882	arg1	The extracellular domain AND five Ser-Gly sites	protein		sites		Fterm	Site	protein		sites	The extracellular domain of the syndecan-1 core protein contains five Ser-Gly sites, three clustered near its N terminus and two adjacent to the transmembrane domain near its C terminus.
22171320	14	37	gly	glycoproteins	2243:2255	arg1	human urinary glycoproteins	human urinary glycoproteins				Fterm		glycoproteins			This is the first study of human urinary glycoproteins where "intact" glycopeptides were studied, i.e. the presence of glycans and their attachment sites were proven without doubt.
22171320	14	124	gly	glycopeptides	2272:2284	arg2	"intact" glycopeptides			"intact" glycopeptides						glycopeptides	This is the first study of human urinary glycoproteins where "intact" glycopeptides were studied, i.e. the presence of glycans and their attachment sites were proven without doubt.
16622833	8	22	gly	Fucosylation	1416:1427	arg1	diantennary structures				diantennary structures						Fucosylation of diantennary structures was marginal and of the core alpha1,6 type.
12590919	4	5	gly	N-glycosylation	680:694	arg1	hENT2	hENT2				PUBTATOR		hENT2	3177		Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
19196183	3	28	gly	N-glycosylation	395:409	arg2	N-glycosylation sites			N-glycosylation sites						sites	Here, we report the analysis of N-glycosylation sites on secreted proteins of human hepatocellular carcinoma cells.
12911312	0	51	gly	N-	37:38	arg1	sites			sites						sites	Mass spectrometric identification of N- and O-glycosylation sites of full-length rat selenoprotein P and determination of selenide-sulfide and disulfide linkages in the shortest isoform.
12911312	0	63	gly	O-glycosylation	44:58	arg1	full-length rat selenoprotein P	full-length rat selenoprotein P				PUBTATOR		selenoprotein P	29360		Mass spectrometric identification of N- and O-glycosylation sites of full-length rat selenoprotein P and determination of selenide-sulfide and disulfide linkages in the shortest isoform.
7541354	7	36	gly	oligosaccharides	1175:1190	arg1	human vitronectin	vitronectin			oligosaccharides	PUBTATOR		vitronectin	7448		The possibility that several binding activities of vitronectin can be ascribed to its glycan moiety was discussed, based on the specific features of the N-linked oligosaccharides on human vitronectin revealed here.
24530628	2	28	gly	glycopeptides	257:269	arg2	glycopeptides			glycopeptides						glycopeptides	A limitation of this technique is the difficulty in acquiring reliable mass spectra for glycopeptides, mainly due to their high heterogeneity and poor hydrophobicity.
29465778	5	8	part_of	HOXA1	614:618	arg1	domains	HOXA1		domains		PUBTATOR	Site	HOXA1	3198	domains	Here, we confirm OGT as a HOXA1 interactor, we characterise which domains of HOXA1 and OGT are required for the interaction, and we provide evidence that OGT post-translationally modifies HOXA1.
29465778	5	9	part_of	OGT	624:626	arg1	domains	OGT		domains		PUBTATOR	Site	OGT	8473	domains	Here, we confirm OGT as a HOXA1 interactor, we characterise which domains of HOXA1 and OGT are required for the interaction, and we provide evidence that OGT post-translationally modifies HOXA1.
9013598	0	42	gly	glycosylation	27:39	arg2	N-linked glycosylation sites			N-linked glycosylation sites						sites	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
8384526	0	23	gly	glycoproteins	83:95	arg1	glycoproteins	glycoproteins			small oligosaccharides	Fterm		glycoproteins			An improved approach to the analysis of the structure of small oligosaccharides of glycoproteins: application to the O-linked oligosaccharides from human glycophorin A. Treatment of purified human glycophorin A with alkaline borohydride cleaved the oligosaccharide side chains to yield alditol derivatives that were separated by gel filtration into three mixtures of low molecular weight compounds.
3555489	2	2	part_of	possesses	305:313	arg1	The enzyme AND a single transmembrane spanning domain	The enzyme		a single transmembrane spanning domain		Fterm	Site	enzyme		domain	The enzyme possesses a single transmembrane spanning domain near the N-terminal of the molecule but lacks a signal sequence.
19864504	9	35	gly	ASA	1267:1269	arg1	the highest mannose-6-phosphate content	ASA			the highest mannose-6-phosphate content	OGER		ASA	P15289		CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	9	35	gly	ASA	1267:1269	arg1	the most preserved N-glycan structures	ASA			the most preserved N-glycan structures	OGER		ASA	P15289		CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
22967898	4	33	gly	N-glycosylated	471:484	arg2	292			Asn(221) and Asn(292)						Asn(221) and Asn(292)	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg2	Asn			Asn(221) and Asn(292)						Asn(221) and Asn(292)	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg2	Asn			Asn(221) and Asn(292)						Asn(221) and Asn(292)	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg1	cathepsin V	cathepsin V		Asn(221) and Asn(292)		PUBTATOR		cathepsin V	1515	Asn(221) and Asn(292)	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg2	Asn			Asn(221) and Asn(292)						Asn(221) and Asn(292)	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg2	Asn			Asn(221) and Asn(292)						Asn(221) and Asn(292)	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg1	cathepsin V	cathepsin V		Asn(221) and Asn(292)		PUBTATOR		cathepsin V	1515	Asn(221) and Asn(292)	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg2	Asn			Asn(221) and Asn(292)						Asn(221) and Asn(292)	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg1	cathepsin V	cathepsin V		Asn(221) and Asn(292)		PUBTATOR		cathepsin V	1515	Asn(221) and Asn(292)	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg1	cathepsin V	cathepsin V		Asn(221) and Asn(292)		PUBTATOR		cathepsin V	1515	Asn(221) and Asn(292)	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
25419660	6	51	part_of	proteins	1136:1143	arg1	a collagenous domain	proteins		a collagenous domain		Fterm	Site	proteins		domain	Our results confirm that LH3 is the only enzyme capable of glucosylating the galactosylhydroxylysine residues in proteins with a collagenous domain.
25419660	6	72	part_of	residues	1124:1131	arg1	proteins	proteins		residues		Fterm	AminoAcid	proteins		residues in	Our results confirm that LH3 is the only enzyme capable of glucosylating the galactosylhydroxylysine residues in proteins with a collagenous domain.
7654718	0	20	part_of	lipase	65:70	arg1	lipase C-tail fragment	bile salt-activated lipase C-tail		lipase C-tail fragment		PUBTATOR	Site	bile salt-activated lipase C-tail	P19835	fragment	Isolation and characterization of human milk bile salt-activated lipase C-tail fragment.
7654718	0	67	part_of	C-tail	72:77	arg1	lipase C-tail fragment	bile salt-activated lipase C-tail		lipase C-tail fragment		PUBTATOR	Site	bile salt-activated lipase C-tail	P19835	fragment	Isolation and characterization of human milk bile salt-activated lipase C-tail fragment.
9233787	2	32	part_of	follistatin-like	272:287	arg1	a follistatin-like (FS) domain	follistatin		a follistatin-like (FS) domain		OGER	Site	follistatin	P19883	domain	Apart from an acidic N-terminal segment, BM-40 consists of a follistatin-like (FS) domain and an EF-hand calcium-binding (EC) domain.
8243461	1	79	gly	glycosylated	245:256	arg1	a heavily glycosylated activation peptide			a heavily glycosylated activation peptide						peptide	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
7592613	7	0	gly	fucosylated	1365:1375	arg1	fucosylated lacdiNAc				fucosylated lacdiNAc						Oligosaccharides with fucosylated lacdiNAc antennae have previously been shown to potently block selectin-mediated adhesions and may perform the same function in glycodelin.
6192908	0	12	gly	alpha-fetoprotein	15:31	arg1	Sugar chain	alpha-fetoprotein			Sugar chain	PUBTATOR		alpha-fetoprotein	174		Sugar chain of alpha-fetoprotein produced in human yolk sac tumor.
2023947	5	32	gly	fucose-threonine	861:876	arg1	the fucose-threonine bond			threonine	the fucose-threonine bond					threonine	This type of modification is normally not detected without mass spectrometry because the fucose-threonine bond is hydrolyzed under standard acidic conditions of the amino acid analysis and Edman sequencing.
26467158	7	62	gly	sites	1304:1308	arg1	BACE1	BACE1			sites	PUBTATOR		BACE1	23821		We purified BACE1 from Neuro2A cells and performed LC/ESI/MS analysis for BACE1-derived glycopeptides and mapped bisecting GlcNAc-modified sites on BACE1.
26467158	7	66	gly	glycopeptides	1253:1265	arg2	BACE1-derived glycopeptides			BACE1-derived glycopeptides						glycopeptides	We purified BACE1 from Neuro2A cells and performed LC/ESI/MS analysis for BACE1-derived glycopeptides and mapped bisecting GlcNAc-modified sites on BACE1.
1991473	0	76	gly	glycosylation	66:78	arg2	individual glycosylation sites	lutropin		sites		Fterm		lutropin		sites	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
28489325	2	12	gly	glycosylation	503:515	arg2	the three glycosylation sites			the three glycosylation sites						sites	In order to obtain the crystal structure of human L-selectin, we expressed a shortened version of L-selectin comprising the C-type lectin and EGF-like domains (termed LE) and systematically analysed mutations of the three glycosylation sites (Asn22, Asn66 and Asn139) in order to reduce macroheterogeneity.
28489325	2	52	gly	sites	517:521	arg1	the three glycosylation sites			the three glycosylation sites						sites	In order to obtain the crystal structure of human L-selectin, we expressed a shortened version of L-selectin comprising the C-type lectin and EGF-like domains (termed LE) and systematically analysed mutations of the three glycosylation sites (Asn22, Asn66 and Asn139) in order to reduce macroheterogeneity.
28489325	2	12	gly	glycosylation	503:515	arg2	Asn139			Asn22, Asn66 and Asn139						Asn22, Asn66 and Asn139	In order to obtain the crystal structure of human L-selectin, we expressed a shortened version of L-selectin comprising the C-type lectin and EGF-like domains (termed LE) and systematically analysed mutations of the three glycosylation sites (Asn22, Asn66 and Asn139) in order to reduce macroheterogeneity.
28489325	2	52	gly	sites	517:521	arg1	Asn66			Asn22, Asn66 and Asn139						Asn22, Asn66 and Asn139	In order to obtain the crystal structure of human L-selectin, we expressed a shortened version of L-selectin comprising the C-type lectin and EGF-like domains (termed LE) and systematically analysed mutations of the three glycosylation sites (Asn22, Asn66 and Asn139) in order to reduce macroheterogeneity.
26510530	4	36	gly	glycopeptides	712:724	arg2	64 glycopeptides			64 glycopeptides						glycopeptides	A total of 64 glycopeptides and 15 peptides were monitored for IgG, IgA, and IgM in a 20 min ultra high performance (UP)LC gradient.
11710528	4	4	gly	glycopeptides	643:655	arg2	The Con A-III glycopeptides			The Con A-III glycopeptides						glycopeptides	The Con A-III glycopeptides were treated with Endo H.
3949763	2	10	gly	glycoprotein	251:262	arg1	this important glycoprotein	this important glycoprotein				Fterm		glycoprotein			Because of its extreme scarcity, very little information is available regarding structural features of this important glycoprotein.
24884609	1	70	gly	glycoprotein	167:178	arg1	Inter-alpha-trypsin inhibitor heavy chain H4	Inter-alpha-trypsin inhibitor heavy chain H4				PUBTATOR		Inter-alpha-trypsin inhibitor heavy chain H4	3700		Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	1	70	gly	glycoprotein	167:178	arg1	a 120 kDa acute-phase glycoprotein	a 120 kDa acute-phase glycoprotein				Fterm		glycoprotein			Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
8344946	3	57	gly	linked	651:656	arg2	threonine AND single N-acetylglucosamine monosaccharides			threonine	single N-acetylglucosamine monosaccharides					threonine residues	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	3	57	gly	linked	651:656	arg1	serine AND single N-acetylglucosamine monosaccharides			serine	single N-acetylglucosamine monosaccharides					serine	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	3	74	gly	serine	661:666	arg1	residues			residues						threonine residues	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
17157876	1	91	gly	glycoprotein	208:219	arg1	Human carboxypeptidase N (CPN)	Human carboxypeptidase N (CPN)				PUBTATOR		CPN	1369		Human carboxypeptidase N (CPN), a member of the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, is an extracellular glycoprotein synthesized in the liver and secreted into the blood, where it controls the activity of vasoactive peptide hormones, growth factors and cytokines by specifically removing C-terminal basic residues.
17157876	1	91	gly	glycoprotein	208:219	arg1	an extracellular glycoprotein	an extracellular glycoprotein				Fterm		glycoprotein			Human carboxypeptidase N (CPN), a member of the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, is an extracellular glycoprotein synthesized in the liver and secreted into the blood, where it controls the activity of vasoactive peptide hormones, growth factors and cytokines by specifically removing C-terminal basic residues.
24365146	0	30	gly	glycosylation	9:21	arg1	the superoxide-producing NADPH oxidase Nox1	the superoxide-producing NADPH oxidase Nox1				PUBTATOR		Nox1	27035		N-Linked glycosylation of the superoxide-producing NADPH oxidase Nox1.
17395588	6	99	part_of	TSR1	1118:1121	arg1	the relevant peptide	TSR1		the relevant peptide		PUBTATOR	Site	TSR1	55720	peptide	Although mass spectral analysis did not unambiguously identify the relevant peptide from TSR1, metabolic labeling of cells expressing TSR1 and the cysteine-rich module led to incorporation of [(3)H]fucose into this construct.
7620335	7	47	gly	glycosylation	1209:1221	arg2	both N-linked glycosylation sites			both N-linked glycosylation sites						sites	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	7	80	gly	isolated	1181:1188	arg1	both N-linked glycosylation sites AND Six neutral and twelve monosialyl oligosaccharides			both N-linked glycosylation sites	Six neutral and twelve monosialyl oligosaccharides					sites	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
28327546	3	82	part_of	FVIII	388:392	arg1	N582	FVIII		N582		PUBTATOR	SpecificSite	FVIII	2157	N582	Here we characterize how hemophilia mutations near the unused N-glycosylation site of the A2 domain (N582) of FVIII affect protein conformation and intracellular trafficking.
28327546	3	82	part_of	FVIII	388:392	arg1	the A2 domain	FVIII		the A2 domain		PUBTATOR	Site	FVIII	2157	domain	Here we characterize how hemophilia mutations near the unused N-glycosylation site of the A2 domain (N582) of FVIII affect protein conformation and intracellular trafficking.
29932112	4	17	gly	N-glycosylation	547:561	arg2	the predicted N-glycosylation site	Panx2		site		PUBTATOR		Panx2	56666	site	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
18787108	0	15	gly	glycoprotein	63:74	arg1	a novel secreted glycoprotein	a novel secreted glycoprotein				Fterm		glycoprotein			Identification and characterization of CTRP9, a novel secreted glycoprotein, from adipose tissue that reduces serum glucose in mice and forms heterotrimers with adiponectin.
18787108	0	15	gly	glycoprotein	63:74	arg1	CTRP9	CTRP9				PUBTATOR		CTRP9	239126		Identification and characterization of CTRP9, a novel secreted glycoprotein, from adipose tissue that reduces serum glucose in mice and forms heterotrimers with adiponectin.
9852066	0	49	part_of	A	64:64	arg1	Phosphorylation and O-glycosylation sites	chromogranin A		Phosphorylation and O-glycosylation sites		PUBTATOR	Site	chromogranin A	1113	sites	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9233787	1	9	gly	glycoprotein	166:177	arg1	an anti-adhesive secreted glycoprotein	an anti-adhesive secreted glycoprotein				Fterm		glycoprotein			BM-40 (also known as SPARC or osteonectin) is an anti-adhesive secreted glycoprotein involved in tissue remodelling.
9233787	1	9	gly	glycoprotein	166:177	arg1	BM-40	BM-40				OGER		BM-40	P09486		BM-40 (also known as SPARC or osteonectin) is an anti-adhesive secreted glycoprotein involved in tissue remodelling.
22451694	0	26	part_of	α5β1	21:24	arg1	α5β1 integrin ectodomain	structure of α5		α5β1 integrin ectodomain		Cterm	Site	structure of α5		ectodomain	Crystal structure of α5β1 integrin ectodomain: atomic details of the fibronectin receptor.
7451505	1	27	gly	glycoproteins	166:178	arg1	human plasma glycoproteins	glycoproteins			the triantennary complex type sugar chains	Fterm		glycoproteins			Structural characteristics of the triantennary complex type sugar chains of human plasma glycoproteins.
23001782	9	81	gly	heterogeneity	1608:1620	arg1	the isoforms	the isoforms				Fterm		isoforms			Electrophoretic analysis of intact hSHBG revealed size and charge heterogeneity of the isoforms circulating in blood serum.
11595658	1	42	part_of	contains	154:161	arg1	The corticotropin-releasing factor (CRF) receptor type 1 AND five potential N-glycosylation sites	The corticotropin-releasing factor (CRF) receptor type 1		five potential N-glycosylation sites		PUBTATOR	Site	corticotropin-releasing factor (CRF) receptor type 1	1394	sites	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	CRFR1 AND five potential N-glycosylation sites	CRFR1		five potential N-glycosylation sites		PUBTATOR	Site	CRFR1	1394	sites	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	The corticotropin-releasing factor (CRF) receptor type 1 AND N98	corticotropin-releasing factor (CRF) receptor type 1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	corticotropin-releasing factor (CRF) receptor type 1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	The corticotropin-releasing factor (CRF) receptor type 1 AND N90	corticotropin-releasing factor (CRF) receptor type 1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	corticotropin-releasing factor (CRF) receptor type 1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	The corticotropin-releasing factor (CRF) receptor type 1 AND N45	corticotropin-releasing factor (CRF) receptor type 1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	corticotropin-releasing factor (CRF) receptor type 1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	The corticotropin-releasing factor (CRF) receptor type 1 AND N78	corticotropin-releasing factor (CRF) receptor type 1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	corticotropin-releasing factor (CRF) receptor type 1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	The corticotropin-releasing factor (CRF) receptor type 1 AND N90	corticotropin-releasing factor (CRF) receptor type 1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	corticotropin-releasing factor (CRF) receptor type 1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	The corticotropin-releasing factor (CRF) receptor type 1 AND N45	corticotropin-releasing factor (CRF) receptor type 1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	corticotropin-releasing factor (CRF) receptor type 1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	The corticotropin-releasing factor (CRF) receptor type 1 AND N78	corticotropin-releasing factor (CRF) receptor type 1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	corticotropin-releasing factor (CRF) receptor type 1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	The corticotropin-releasing factor (CRF) receptor type 1 AND N45	corticotropin-releasing factor (CRF) receptor type 1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	corticotropin-releasing factor (CRF) receptor type 1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	The corticotropin-releasing factor (CRF) receptor type 1 AND N78	corticotropin-releasing factor (CRF) receptor type 1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	corticotropin-releasing factor (CRF) receptor type 1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	The corticotropin-releasing factor (CRF) receptor type 1 AND N78	corticotropin-releasing factor (CRF) receptor type 1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	corticotropin-releasing factor (CRF) receptor type 1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	CRFR1 AND N98	CRFR1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	CRFR1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	CRFR1 AND N90	CRFR1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	CRFR1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	CRFR1 AND N45	CRFR1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	CRFR1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	CRFR1 AND N78	CRFR1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	CRFR1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	CRFR1 AND N90	CRFR1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	CRFR1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	CRFR1 AND N45	CRFR1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	CRFR1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	CRFR1 AND N78	CRFR1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	CRFR1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	CRFR1 AND N45	CRFR1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	CRFR1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	CRFR1 AND N78	CRFR1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	CRFR1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	part_of	contains	154:161	arg1	CRFR1 AND N78	CRFR1		N38, N45, N78, N90, and N98		PUBTATOR	SpecificSite	CRFR1	1394	N38, N45, N78, N90, and N98	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
18340083	10	66	gly	N-glycosylation	1365:1379	arg1	GPIHBP1	GPIHBP1				PUBTATOR		GPIHBP1	68453		These studies demonstrate that N-glycosylation of GPIHBP1 is important for the trafficking of GPIHBP1 to the cell surface.
10092871	7	48	gly	2,3-sialylated	1154:1167	arg1	alpha 2,3-sialylated complex-type diantennary glycans				alpha 2,3-sialylated complex-type diantennary glycans						MMP-1 derived from fibroblasts was found to carry mainly alpha 2,3-sialylated complex-type diantennary glycans.
10092871	7	73	gly	carry	1135:1139	arg1	MMP-1 AND alpha 2,3-sialylated complex-type diantennary glycans	MMP-1			alpha 2,3-sialylated complex-type diantennary glycans	PUBTATOR		MMP-1	4312		MMP-1 derived from fibroblasts was found to carry mainly alpha 2,3-sialylated complex-type diantennary glycans.
9572875	7	38	gly	nonglycosylated	1296:1310	arg1	nonglycosylated IGFBP-6	nonglycosylated IGFBP-6				PUBTATOR		IGFBP-6	3489		Glycosylated IGFBP-6 exhibited greater resistance to proteolysis by chymotrypsin and trypsin than nonglycosylated IGFBP-6.
24098488	1	59	gly	serine	331:336	arg1	residues			residues						serine and threonine residues	O-linked β-N-acetylglucosamine (O-GlcNAc) is an important post-translational modification (PTM) consisting of a single N-acetylglucosamine moiety attached via an O-β-glycosidic linkage to serine and threonine residues.
3524673	9	0	part_of	factor	792:797	arg1	The sequence	von Willebrand factor		The sequence		PUBTATOR	Site	von Willebrand factor	7450	sequence	The sequence of von Willebrand factor includes several regions bearing evidence of internal gene duplication of ancestral sequences.
8286855	2	2	gly	Ser	496:498	arg1	residues			residues						Ser and Thr residues	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	29	gly	O-glycosylated	481:494	arg1	O-glycosylated Ser			O-glycosylated Ser						Ser and Thr residues	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	68	gly	N-glycosylation	540:554	arg2	the single N-glycosylation site			the single N-glycosylation site						site	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	38	gly	O-glycosylation	328:342	arg1	the extracellular domain	GpA		domain		PUBTATOR		GpA	2993	domain	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	38	gly	O-glycosylation	328:342	arg2	the single N-glycosylation site	GpA		site		PUBTATOR		GpA	2993	site	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	38	gly	O-glycosylation	328:342	arg2	the sites	GpA		sites		PUBTATOR		GpA	2993	sites	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
2129367	5	69	part_of	IX	639:640	arg1	Ser-53	factor IX		Ser-53		OGER	SpecificSite	factor IX	P00740	Ser-53	The same results were also obtained for a pentapeptide containing Ser-53 of factor IX and protein Z. Component sugar analysis revealed that the peptide contained 1 mol of glucose and 2 mol of xylose.
14693913	0	56	gly	glycosylation	36:48	arg1	recombinant human bile salt-stimulated lipase	recombinant human bile salt-stimulated lipase				OGER		bile salt-stimulated lipase	P19835		Characterization of N- and O-linked glycosylation of recombinant human bile salt-stimulated lipase secreted by Pichia pastoris.
25153361	1	44	part_of	contain	114:120	arg1	A glycoprotein AND several sites	A glycoprotein		several sites		Fterm	Site	glycoprotein		sites	A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
20145116	3	69	part_of	receptor	512:519	arg1	the intracellular tyrosine kinase domain	receptor		the intracellular tyrosine kinase domain		Fterm	Site	receptor		domain	Dimerization initiates transmembrane signaling, which activates the intracellular tyrosine kinase domain of the receptor.
27434672	3	28	part_of	CaSR	502:505	arg1	the entire extracellular domain	CaSR		the entire extracellular domain		OGER	Site	CaSR	P41180	domain	Here, we present the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations.
15687489	5	28	part_of	FGE	633:635	arg1	the FGE recognition motif	FGE		the FGE recognition motif		PUBTATOR	Site	FGE	285362	motif	pFGE binds a sulfatase-derived peptide bearing the FGE recognition motif, but it lacks formylglycine-generating activity.
11544325	0	30	gly	glycosylations	9:22	arg2	26			Asn(26) and Asn(114)						Asn(26) and Asn(114)	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg2	114			Asn(26) and Asn(114)						Asn(26) and Asn(114)	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg1	human MD-2	MD-2		Asn(26) and Asn(114)		PUBTATOR		MD-2	23643	Asn(26) and Asn(114)	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg2	Asn			Asn(26) and Asn(114)						Asn(26) and Asn(114)	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg2	114			Asn(26) and Asn(114)						Asn(26) and Asn(114)	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg1	human MD-2	MD-2		Asn(26) and Asn(114)		PUBTATOR		MD-2	23643	Asn(26) and Asn(114)	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg2	Asn			Asn(26) and Asn(114)						Asn(26) and Asn(114)	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg1	human MD-2	MD-2		Asn(26) and Asn(114)		PUBTATOR		MD-2	23643	Asn(26) and Asn(114)	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg2	Asn			Asn(26) and Asn(114)						Asn(26) and Asn(114)	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg2	Asn	MD-2		Asn(26) and Asn(114)		PUBTATOR		MD-2	23643	Asn(26) and Asn(114)	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
27313224	0	76	gly	N559-glycan	17:27	arg1	the synaptic vesicle glycoprotein 2C	synaptic vesicle glycoprotein 2C			N559-glycan	PUBTATOR		synaptic vesicle glycoprotein 2C	22987		Only the complex N559-glycan in the synaptic vesicle glycoprotein 2C mediates high affinity binding to botulinum neurotoxin serotype A1.
27313224	0	82	gly	glycoprotein	53:64	arg1	the synaptic vesicle glycoprotein 2C	the synaptic vesicle glycoprotein 2C				PUBTATOR		synaptic vesicle glycoprotein 2C	22987		Only the complex N559-glycan in the synaptic vesicle glycoprotein 2C mediates high affinity binding to botulinum neurotoxin serotype A1.
7106126	1	22	part_of	sequence	119:126	arg1	a minor human erythrocyte membrane sialoglycoprotein	sialoglycoprotein		sequence		Fterm	Site	sialoglycoprotein		sequence	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	1	43	part_of	sialoglycoprotein	207:223	arg1	the N-terminal tryptic glycopeptide	sialoglycoprotein		the N-terminal tryptic glycopeptide		Fterm	Site	sialoglycoprotein		glycopeptide	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	1	43	part_of	sialoglycoprotein	207:223	arg1	The amino acid sequence	sialoglycoprotein		The amino acid sequence		Fterm	Site	sialoglycoprotein		sequence	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
9933650	6	49	part_of	IL-1-dependent	910:923	arg1	D10-G4	IL-1		D10-G4		PUBTATOR	SiteSequence	IL-1	3552	D10-G4	The oligosaccharides in fraction AR also inhibited the growth of an IL-1-dependent cell line, D10-G4.
19038966	4	42	part_of	Ca2+-binding	778:789	arg1	an octahedrally coordinated Ca2+-binding site	Ca2		an octahedrally coordinated Ca2+-binding site		OGER	Site	Ca2	P00918	site	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
1823160	3	51	gly	glycoprotein	596:607	arg1	the latter glycoprotein	the latter glycoprotein				Fterm		glycoprotein			In the latter glycoprotein we have identified a novel structure as the major oligosaccharide attached to Asn-184 and Asn-448.
1823160	3	4	gly	attached	675:682	arg1	Asn-448 AND the major oligosaccharide			Asn-184 and Asn-448	the major oligosaccharide					Asn-184 and Asn-448	In the latter glycoprotein we have identified a novel structure as the major oligosaccharide attached to Asn-184 and Asn-448.
1823160	8	9	gly	glycoproteins	1414:1426	arg1	natural and recombinant glycoproteins	natural and recombinant glycoproteins				Fterm		glycoproteins			This study demonstrates the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins.
3886654	2	72	part_of	XIIa	424:427	arg1	the previously determined sequence	factor XIIa		the previously determined sequence		Cterm	Site	factor XIIa		sequence	Combining this sequence with the previously determined sequence of beta-factor XIIa (Fujikawa, K., and McMullen, B. A. (1983) J. Biol.
15869464	8	34	gly	occupied	1663:1670	arg2	two potential sites			two potential sites						sites	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Five threonine residues			Five threonine residues						threonine residues	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	gly	O-glycosylated	1534:1547	arg1	Thr131			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	gly	O-glycosylated	1534:1547	arg1	Thr136			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	gly	O-glycosylated	1534:1547	arg1	Thr122			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr118			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr131			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr136			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr122			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	gly	O-glycosylated	1534:1547	arg1	Thr136			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	gly	O-glycosylated	1534:1547	arg1	Thr122			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr118			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr131			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr136			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr122			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	gly	O-glycosylated	1534:1547	arg1	Thr122			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr118			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr131			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr136			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr122			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr118			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr131			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr136			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr122			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr118			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr131			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr136			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr122			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr131			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr136			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr122			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr136			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr122			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr122			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr127			Thr118, Thr122, Thr127, Thr131 and Thr136						Thr118, Thr122, Thr127, Thr131 and Thr136	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	96	gly	N-glycosylation	1621:1635	arg1	Asn63			Asn63 and Asn90						Asn63 and Asn90	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
24334224	4	20	gly	glycosylation	898:910	arg2	Thr134			Thr134						Thr134	Our results demonstrated that Thr134, the equivalent O-linked glycosylation site found on endogenous human G-CSF, is the only site modified with a single mannose, allowing glycoengineered P. pastoris to be used as a viable production platform for therapeutic rhG-CSF.
24334224	4	20	gly	glycosylation	898:910	arg2	the equivalent O-linked glycosylation site			the equivalent O-linked glycosylation site						site	Our results demonstrated that Thr134, the equivalent O-linked glycosylation site found on endogenous human G-CSF, is the only site modified with a single mannose, allowing glycoengineered P. pastoris to be used as a viable production platform for therapeutic rhG-CSF.
6966283	11	11	gly	inhibitor	1125:1133	arg1	The sialic acid	alpha 1-protease inhibitor			The sialic acid	PUBTATOR		alpha 1-protease inhibitor	5265		The sialic acid of human alpha 1-protease inhibitor was determined to be N-acetylneuraminic acid.
6966283	11	11	gly	inhibitor	1125:1133	arg1	N-acetylneuraminic acid	alpha 1-protease inhibitor			N-acetylneuraminic acid	PUBTATOR		alpha 1-protease inhibitor	5265		The sialic acid of human alpha 1-protease inhibitor was determined to be N-acetylneuraminic acid.
23027977	0	58	gly	glycoprotein	45:56	arg1	Crystal structure	Crystal structure				PUBTATOR		structure of Enpp1	5167		Crystal structure of Enpp1, an extracellular glycoprotein involved in bone mineralization and insulin signaling.
23027977	0	58	gly	glycoprotein	45:56	arg1	an extracellular glycoprotein	an extracellular glycoprotein				Fterm		glycoprotein			Crystal structure of Enpp1, an extracellular glycoprotein involved in bone mineralization and insulin signaling.
21182469	6	17	part_of	ABCC11	843:848	arg1	Gly180	ABCC11		Gly180		PUBTATOR	AminoAcid	ABCC11	85320	Gly180	On the other hand, the wild type (Gly180) of ABCC11 is associated with wet-type earwax, axillary osmidrosis, colostrum secretion from the mammary gland, and the potential susceptibility of breast cancer.
2403553	14	111	gly	oligosaccharides	2227:2242	arg1	the receptors	receptors			oligosaccharides	Fterm		receptors			Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	14	34	gly	contains	2096:2103	arg1	the human transferrin receptor AND O-linked oligosaccharides	the human transferrin receptor			O-linked oligosaccharides	PUBTATOR		transferrin receptor	7018		Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2775174	9	35	gly	N-glycosylation	1118:1132	arg1	Asn-15	subunit		Asn-15		OGER		subunit	P20933	Asn-15	N-Terminal sequence analysis of each subunit revealed a frayed N-terminus of the 24 kDa subunit and an apparent N-glycosylation of Asn-15 in the same subunit.
2775174	9	35	gly	N-glycosylation	1118:1132	arg1	the same subunit	subunit				OGER		subunit	P20933		N-Terminal sequence analysis of each subunit revealed a frayed N-terminus of the 24 kDa subunit and an apparent N-glycosylation of Asn-15 in the same subunit.
2775174	9	35	gly	N-glycosylation	1118:1132	arg1	the same subunit	subunit		Asn-15		OGER		subunit	P20933	Asn-15	N-Terminal sequence analysis of each subunit revealed a frayed N-terminus of the 24 kDa subunit and an apparent N-glycosylation of Asn-15 in the same subunit.
16407218	5	4	part_of	Asn-846	930:936	arg1	alpha2M	alpha2M		Asn-846		PUBTATOR	SpecificSite	alpha2M	2	Asn-846	We investigated the mechanism of formation of complexes between alpha2M and MBL and concluded that they form by the direct binding of oligomannose glycans Man(5-7) occupying Asn-846 on alpha2M to the lectin domains (carbohydrate recognition domains) of MBL.
16407218	5	40	part_of	lectin	956:961	arg1	the lectin domains	lectin		the lectin domains		Fterm	Site	lectin		domains	We investigated the mechanism of formation of complexes between alpha2M and MBL and concluded that they form by the direct binding of oligomannose glycans Man(5-7) occupying Asn-846 on alpha2M to the lectin domains (carbohydrate recognition domains) of MBL.
16407218	5	66	part_of	MBL	1009:1011	arg1	the lectin domains	MBL		the lectin domains		PUBTATOR	Site	MBL	4153	domains	We investigated the mechanism of formation of complexes between alpha2M and MBL and concluded that they form by the direct binding of oligomannose glycans Man(5-7) occupying Asn-846 on alpha2M to the lectin domains (carbohydrate recognition domains) of MBL.
8942648	11	6	gly	trisialylated	1601:1613	arg1	trisialylated triantennary structures				trisialylated triantennary structures						The N-glycans are of the complex type with the core-fucosylated disialylated biantennary and trisialylated triantennary structures predominating.
7925474	4	70	part_of	contains	509:516	arg1	FA1 AND up to ten O-glycosylation and N-glycosylation sites	FA1		up to ten O-glycosylation and N-glycosylation sites		PUBTATOR	Site	FA1	8788	sites	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	4	72	part_of	has	451:453	arg1	FA1 AND six well conserved epidermal-growth-factor motifs	FA1		six well conserved epidermal-growth-factor motifs		PUBTATOR	Site	FA1	8788	motifs	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
9539702	1	17	part_of	190-residue	122:132	arg1	a 190-residue fragment	structure of a 190		a 190-residue fragment		OGER	Site	structure of a 190	O95602	fragment	The 3.0-A structure of a 190-residue fragment of intercellular adhesion molecule-1 (ICAM-1, CD54) reveals two tandem Ig-superfamily (IgSF) domains.
9539702	1	20	part_of	molecule-1	169:178	arg1	a 190-residue fragment	intercellular adhesion molecule-1		a 190-residue fragment		OGER	Site	intercellular adhesion molecule-1	P05362	fragment	The 3.0-A structure of a 190-residue fragment of intercellular adhesion molecule-1 (ICAM-1, CD54) reveals two tandem Ig-superfamily (IgSF) domains.
12911312	11	18	part_of	reductase	1331:1339	arg1	the C terminus	thioredoxin reductase		the C terminus		OGER	Site	thioredoxin reductase	P10599	terminus	The finding of a selenide-sulfide bond in the shortest isoform is compatible with a redox function of this pair that might be analogous to the selenol-thiol pair near the C terminus of animal thioredoxin reductase.
19276170	3	54	part_of	COMP	612:615	arg1	the C-terminal domain	COMP		the C-terminal domain		OGER	Site	COMP	P49747	domain	In this study, we determined the structure of a recombinant protein that contains the last epidermal growth factor repeat, the type 3 repeats and the C-terminal domain (CTD) of COMP to 3.15-A resolution limit by X-ray crystallography.
3342257	1	1	gly	linked	113:118	arg1	human kappa-casein AND The carbohydrate chains	human kappa-casein			The carbohydrate chains	OGER		kappa-casein	P07498		The carbohydrate chains linked to human kappa-casein from mature milk were released by alkaline borohydride treatment as reduced oligosaccharides.
3342257	1	1	gly	linked	113:118	arg1	human kappa-casein AND reduced oligosaccharides	human kappa-casein			reduced oligosaccharides	OGER		kappa-casein	P07498		The carbohydrate chains linked to human kappa-casein from mature milk were released by alkaline borohydride treatment as reduced oligosaccharides.
22351761	3	24	part_of	containing	572:581	arg1	a stable α-helical domain AND 14 conserved Cys residues	a stable α-helical domain		14 conserved Cys residues						Cys residues	Glypican core proteins consist of a stable α-helical domain containing 14 conserved Cys residues followed by a glycosaminoglycan attachment domain that becomes exclusively substituted with heparan sulfate (HS) and presumably adopts a random coil conformation.
1567356	11	51	part_of	OMD	1664:1666	arg1	the individual glycosylation sites	OMD		the individual glycosylation sites		OGER	Site	OMD	Q99983	sites	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
10207177	6	27	gly	proteins	1357:1364	arg1	glycan data	proteins			glycan data	Fterm		proteins			These were constructed using the 3D structures of the proteins, glycan data from this study, and an oligosaccharide structural database.
21876145	5	3	part_of	GALC	664:667	arg1	All three domains	GALC		All three domains		PUBTATOR	Site	GALC	2581	domains	All three domains of GALC contribute residues to the substrate-binding pocket, and disease-causing mutations are widely distributed throughout the protein.
1326557	6	153	part_of	RGDS	1457:1460	arg1	an RGDS sequence	RGDS		an RGDS sequence		PUBTATOR	Site	RGDS	29622	sequence	The deduced amino acid sequence revealed a 22-amino acid signal peptide followed by an immunoglobulin domain, tandem repeats characteristic of the hyaluronic acid-binding region of aggregating proteoglycans, and an RGDS sequence.
11168369	6	38	gly	monosialylated	1276:1289	arg1	a monosialylated HexHexNAc structure				a monosialylated HexHexNAc structure						Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	6	60	gly	O-glycosylated	1256:1269	arg1	albumin Kenitra	albumin Kenitra				PUBTATOR		albumin Kenitra	213		Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
10731668	1	18	part_of	receptor	180:187	arg1	The extracellular domain	EGF receptor		The extracellular domain		OGER	Site	EGF receptor	P01133	domain	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
18488039	2	21	gly	glycoproteins	305:317	arg1	Their attachment glycoproteins	Their attachment glycoproteins				Fterm		glycoproteins			Their attachment glycoproteins are essential for the recognition of the cell-surface receptors ephrin-B2 (EFNB2) and ephrin-B3 (EFNB3).
24365146	2	48	gly	glycosylation	219:231	arg1	Asn-162			Asn-162 and Asn-236						Asn-162 and Asn-236	Here we show that human Nox1 undergoes glycosylation at Asn-162 and Asn-236 in the second and third extracellular loops, respectively.
24365146	2	48	gly	glycosylation	219:231	arg1	human Nox1	Nox1		Asn-162 and Asn-236		PUBTATOR		Nox1	27035	Asn-162 and Asn-236	Here we show that human Nox1 undergoes glycosylation at Asn-162 and Asn-236 in the second and third extracellular loops, respectively.
24365146	2	48	gly	glycosylation	219:231	arg1	Asn-236			Asn-162 and Asn-236						Asn-162 and Asn-236	Here we show that human Nox1 undergoes glycosylation at Asn-162 and Asn-236 in the second and third extracellular loops, respectively.
24365146	2	48	gly	glycosylation	219:231	arg2	Asn-162			Asn-162 and Asn-236						Asn-162 and Asn-236	Here we show that human Nox1 undergoes glycosylation at Asn-162 and Asn-236 in the second and third extracellular loops, respectively.
24365146	2	48	gly	glycosylation	219:231	arg1	human Nox1	Nox1		Asn-162 and Asn-236		PUBTATOR		Nox1	27035	Asn-162 and Asn-236	Here we show that human Nox1 undergoes glycosylation at Asn-162 and Asn-236 in the second and third extracellular loops, respectively.
24365146	2	48	gly	glycosylation	219:231	arg1	Asn-236			Asn-162 and Asn-236						Asn-162 and Asn-236	Here we show that human Nox1 undergoes glycosylation at Asn-162 and Asn-236 in the second and third extracellular loops, respectively.
24365146	2	48	gly	glycosylation	219:231	arg2	Asn-162			Asn-162 and Asn-236						Asn-162 and Asn-236	Here we show that human Nox1 undergoes glycosylation at Asn-162 and Asn-236 in the second and third extracellular loops, respectively.
24365146	2	48	gly	glycosylation	219:231	arg1	Asn-236	Nox1		Asn-162 and Asn-236		PUBTATOR		Nox1	27035	Asn-162 and Asn-236	Here we show that human Nox1 undergoes glycosylation at Asn-162 and Asn-236 in the second and third extracellular loops, respectively.
24365146	2	48	gly	glycosylation	219:231	arg2	Asn-162	Nox1		Asn-162 and Asn-236		PUBTATOR		Nox1	27035	Asn-162 and Asn-236	Here we show that human Nox1 undergoes glycosylation at Asn-162 and Asn-236 in the second and third extracellular loops, respectively.
24365146	2	48	gly	glycosylation	219:231	arg2	Asn-162			Asn-162 and Asn-236						Asn-162 and Asn-236	Here we show that human Nox1 undergoes glycosylation at Asn-162 and Asn-236 in the second and third extracellular loops, respectively.
12743029	6	56	part_of	MBP-binding	974:984	arg1	the MBP-binding site	MBP		the MBP-binding site		PUBTATOR	Site	MBP	4155	site	The crystal structure of the MASP-2 CUB1-EGF-CUB2 dimer reveals an elongated structure with a prominent concave surface that is proposed to be the MBP-binding site.
24692546	2	38	part_of	FSHR	254:257	arg1	The FSHR extracellular domains	FSHR		The FSHR extracellular domains		OGER	Site	FSHR	P23945	domains	The FSHR extracellular domains were observed in the crystal structure as a trimer, which enabled us to propose a novel model for the receptor activation mechanism.
15253437	5	32	gly	glycoproteins	1297:1309	arg1	37 glycoproteins	37 glycoproteins				Fterm		glycoproteins			We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	5	42	gly	glycoproteins	1096:1108	arg1	known glycoproteins	known glycoproteins				Fterm		glycoproteins			We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	5	58	gly	glycosylation	1271:1283	arg2	62 glycosylation sites			62 glycosylation sites						sites	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
1900431	3	19	gly	carbohydrate	374:385	arg1	tryptic and chymotryptic peptides			tryptic and chymotryptic peptides						peptides	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1517205	0	16	gly	linked	55:60	arg1	serine 61 AND a tetrasaccharide			serine 61	a tetrasaccharide					serine 61	Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue.
1517205	0	64	gly	has	16:18	arg1	Human factor IX AND a tetrasaccharide	Human factor IX			a tetrasaccharide	OGER		factor IX	P00740		Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue.
24841998	3	36	gly	glycoprotein	489:500	arg1	novel glycoprotein biomarkers	novel glycoprotein biomarkers				Fterm		glycoprotein			Searching for changes in serum protein site-specific glycosylation could reveal novel glycoprotein biomarkers.
19571171	3	22	gly	glycosylation	503:515	arg2	four potential N-linked glycosylation sites			four potential N-linked glycosylation sites						sites	We determined that glycans are added at three of four potential N-linked glycosylation sites: N196, N410, and N428.
19571171	3	66	gly	three	470:474	arg1	N428			N196, N410, and N428						N196, N410, and N428	We determined that glycans are added at three of four potential N-linked glycosylation sites: N196, N410, and N428.
19571171	3	66	gly	three	470:474	arg1	N196			N196, N410, and N428						N196, N410, and N428	We determined that glycans are added at three of four potential N-linked glycosylation sites: N196, N410, and N428.
19571171	3	66	gly	three	470:474	arg1	N196			N196, N410, and N428						N196, N410, and N428	We determined that glycans are added at three of four potential N-linked glycosylation sites: N196, N410, and N428.
27313224	11	19	gly	SV2C-LD4	1839:1846	arg1	the complex N559-glycan	SV2C			the complex N559-glycan	PUBTATOR		SV2C	22987		In conclusion, we show the importance of the complex N559-glycan of SV2C-LD4, adding a third anchor point beside a ganglioside and the SV2C-LD4 peptide, for BoNT/A neuronal cell surface binding and uptake.
19159218	9	32	gly	either	1623:1628	arg1	the corresponding in silico tryptic peptides			the corresponding in silico tryptic peptides						peptides	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	9	90	gly	N-glycosites	1496:1507	arg2	the 317 additional N-glycosites			the 317 additional N-glycosites						N-glycosites	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
2528451	7	57	gly	glycosylation	1160:1172	arg2	four N-linked glycosylation sites			four N-linked glycosylation sites						sites	The protein sequence data reported here predict four N-linked glycosylation sites in the P40 molecule.
19343721	3	29	gly	sialylated	716:725	arg1	The N-glycans				The N-glycans						The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	29	gly	sialylated	716:725	arg1	complex sialylated structures				complex sialylated structures						The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	34	gly	tg-PC	643:647	arg1	The N-glycans	tg-PC			The N-glycans	Cterm		tg-PC	P02810		The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	34	gly	tg-PC	643:647	arg1	complex sialylated structures	tg-PC			complex sialylated structures	Cterm		tg-PC	P02810		The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	39	gly	sialylated	661:670	arg1	The N-glycans				The N-glycans						The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	39	gly	sialylated	661:670	arg1	complex sialylated structures				complex sialylated structures						The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
6587378	3	10	part_of	proline	425:431	arg1	The protein	protein		proline		Fterm	AminoAcid	protein		cysteine and proline	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
6587378	3	32	part_of	cysteine	412:419	arg1	The protein	protein		cysteine		Fterm	AminoAcid	protein		cysteine and proline	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
26620227	3	44	part_of	proSP-B	418:424	arg1	Asn129	SP-B		Asn129		OGER	AminoAcid	SP-B	P07988	Asn129	The SNP causes an altered N-linked glycosylation modification at Asn129 of proSP-B, e.g. the C allele with this glycosylation site but not in the T allele.
16445295	13	74	part_of	TAFI	1844:1847	arg1	the TAFI amino acid sequence	TAFI		the TAFI amino acid sequence		PUBTATOR	Site	TAFI	1361	sequence	LC-MS/MS analyses covering more than 90% of the TAFI amino acid sequence revealed no additional modifications.
27175940	5	43	part_of	p27	987:989	arg1	Ser2	p27		Ser2		PUBTATOR	AminoAcid	p27	3429	Ser2	Cell proliferation was negatively regulated when Ser2 of p27 was replaced with Ala.
23319596	2	22	part_of	oxidase	428:434	arg1	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	lysyl oxidase		the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain		PUBTATOR	Site	lysyl oxidase	4015	domain	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	27	part_of	lysyl	422:426	arg1	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	lysyl oxidase		the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain		PUBTATOR	Site	lysyl oxidase	4015	domain	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	52	part_of	LOX	437:439	arg1	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	LOX		the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain		PUBTATOR	Site	LOX	4015	domain	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
9884403	6	39	gly	glycoprotein	1322:1333	arg1	native human Tamm-Horsfall glycoprotein	native human Tamm-Horsfall glycoprotein				OGER		Tamm-Horsfall glycoprotein	P07911		Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	6	66	gly	Asn208	1223:1228	arg1	the carbohydrate moieties			Asn208	the carbohydrate moieties					Asn208	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
18780401	6	71	part_of	localized	1056:1064	arg1	proteins AND N-glycosylated sites	proteins		N-glycosylated sites		Fterm	Site	proteins		sites	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
8034632	7	9	gly	linkage	914:920	arg1	C-3	C-3			linkage	PUBTATOR		C-3	718		Sialylation may occur on the C-6 of the N-acetylgalactosamine involved in the carbohydrate-peptide linkage or on a terminal galactose residue, either on C-3 or on C-6.
8034632	7	9	gly	linkage	914:920	arg1	C-6	C-6			linkage	PUBTATOR		C-6	729		Sialylation may occur on the C-6 of the N-acetylgalactosamine involved in the carbohydrate-peptide linkage or on a terminal galactose residue, either on C-3 or on C-6.
17117926	0	39	gly	glycosylation	38:50	arg1	Wnt-5a	Wnt-5a				PUBTATOR		Wnt-5a	7474		Post-translational palmitoylation and glycosylation of Wnt-5a are necessary for its signalling.
11741940	7	25	part_of	protein	1470:1476	arg1	the Fz domain	protein		the Fz domain		Fterm	Site	protein		domain	Interestingly, two subsets of sFRPs appear to have alternate disulfide linkage patterns compared with sFRP-1, one of which involves the loss of a disulfide due to deletion of a single cysteine from the NTR module, whereas the remaining cysteine may pair with a new cysteine introduced in the Fz domain of the protein.
24085305	9	36	gly	N-glycosylation	1397:1411	arg2	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites			Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites						Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
27175940	2	8	gly	glycosylation	451:463	arg2	Thr198			Ser2, Ser106, Ser110, Thr157, and Thr198						Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg2	Ser110			Ser2, Ser106, Ser110, Thr157, and Thr198						Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg2	Ser2			Ser2, Ser106, Ser110, Thr157, and Thr198						Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg2	Thr157			Ser2, Ser106, Ser110, Thr157, and Thr198						Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg1	p27	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR		p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg1	p27	p27		sites		PUBTATOR		p27	3429	sites	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg2	Ser110			Ser2, Ser106, Ser110, Thr157, and Thr198						Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg2	Ser2			Ser2, Ser106, Ser110, Thr157, and Thr198						Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg2	Thr157			Ser2, Ser106, Ser110, Thr157, and Thr198						Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg1	p27	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR		p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg2	Ser2			Ser2, Ser106, Ser110, Thr157, and Thr198						Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg2	Thr157			Ser2, Ser106, Ser110, Thr157, and Thr198						Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg1	p27	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR		p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg2	Thr157			Ser2, Ser106, Ser110, Thr157, and Thr198						Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg1	p27	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR		p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	8	gly	glycosylation	451:463	arg1	p27	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR		p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
19349973	0	9	gly	glycoproteins	87:99	arg1	N-linked cell surface glycoproteins	N-linked cell surface glycoproteins				Fterm		glycoproteins			Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.
10531415	6	104	part_of	site	890:893	arg1	the D1 receptor	receptor		site		Fterm	Site	receptor		site	Mutation of a comparable site in the D1 receptor at position N5 had no effect on the delivery of the D1 receptor to the cell surface.
12297050	3	45	part_of	EGFR	473:476	arg1	EGFR domains I-III	EGFR		EGFR domains I-III		PUBTATOR	Site	EGFR	1956	domains	EGFR domains I-III are arranged in a C shape, and EGF is docked between domains I and III.
24058541	5	29	gly	sites	680:684	arg1	certain sites			certain sites						sites	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	29	gly	sites	680:684	arg1	N320			N320						N320	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	58	gly	glycosylation	782:794	arg1	protein folding	protein folding				Fterm		protein			Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	29	gly	sites	680:684	arg1	N252			N179, N252, N304						N179, N252, N304	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	29	gly	sites	680:684	arg1	N179			N179, N252, N304						N179, N252, N304	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	29	gly	sites	680:684	arg1	N179			N179, N252, N304						N179, N252, N304	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
2511201	6	110	gly	glycopeptide	1137:1148	arg2	the glycopeptide			the glycopeptide						glycopeptide	The results indicate that the glycopeptide derived from human factor IX contains 1 mol each of Glc and Xyl.
10386995	0	57	gly	localized	105:113	arg1	domains AND O-linked N-acetylglucosamine residues			domains	O-linked N-acetylglucosamine residues					domains	Glycosylation sites flank phosphorylation sites on synapsin I: O-linked N-acetylglucosamine residues are localized within domains mediating synapsin I interactions.
18214858	2	24	gly	fucosylated	518:528	arg1	fucosylated N-glycans				fucosylated N-glycans						Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	2	72	gly	N-glycosylation	423:437	arg2	four potential N-glycosylation sites			four potential N-glycosylation sites						sites	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
2071582	2	18	part_of	preproenzyme	196:207	arg1	a 226-amino acid catalytic domain	enzyme		a 226-amino acid catalytic domain		Fterm	Site	enzyme		domain	The protein-coding exons reveal a preproenzyme with a 19-amino acid signal peptide, an acidic 2-amino acid propeptide, and a 226-amino acid catalytic domain.
2071582	2	18	part_of	preproenzyme	196:207	arg1	a 19-amino acid signal peptide	enzyme		a 19-amino acid signal peptide		Fterm	Site	enzyme		peptide	The protein-coding exons reveal a preproenzyme with a 19-amino acid signal peptide, an acidic 2-amino acid propeptide, and a 226-amino acid catalytic domain.
2071582	2	18	part_of	preproenzyme	196:207	arg1	an acidic 2-amino acid propeptide	enzyme		an acidic 2-amino acid propeptide		Fterm	Site	enzyme		propeptide	The protein-coding exons reveal a preproenzyme with a 19-amino acid signal peptide, an acidic 2-amino acid propeptide, and a 226-amino acid catalytic domain.
7592613	1	13	gly	glycoprotein	270:281	arg1	Glycodelin	Glycodelin				PUBTATOR		Glycodelin	5047		Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	1	13	gly	glycoprotein	270:281	arg1	a human glycoprotein	a human glycoprotein				Fterm		glycoprotein			Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
8286855	5	48	gly	O-glycosylation	812:826	arg2	potential O-glycosylation sites			potential O-glycosylation sites						sites	We propose that the glycosyltransferases present in erythrocytes recognize specific flanking sequences around potential O-glycosylation sites.
23661698	8	6	gly	EphA2	1196:1200	arg1	the ligand's carbohydrates	EphA2			the ligand's carbohydrates	PUBTATOR		EphA2	1969		Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
18420026	7	26	gly	glycosylation	1694:1706	arg2	the glycosylation site mutation			the glycosylation site mutation						site	Cell aggregation assay further showed there was an increased adhesion activity after the glycosylation site mutation of NECL1 molecule.
22041449	6	17	part_of	G2	1047:1048	arg1	the LN domain	netrin G2		domain and domain		PUBTATOR	Site	netrin G2	Q96CW9	domain and domain	We determined the crystal structure for a fragment comprising the LN domain and domain LE1 of netrin G2 by sulfur single-wavelength anomalous diffraction phasing and refined it to 1.8 Å resolution.
22809326	14	79	part_of	LAMP-2	1835:1840	arg1	the LAMP-1 and LAMP-2 luminal regions	LAMP-2		the LAMP-1 and LAMP-2 luminal regions		PUBTATOR	Site	LAMP-2	P13473	regions	Insights into the structure of the lysosomal glycoprotein coat were obtained by computational models of the LAMP-1 and LAMP-2 luminal regions.
22809326	14	99	part_of	LAMP-1	1824:1829	arg1	the LAMP-1 and LAMP-2 luminal regions	LAMP-1		the LAMP-1 and LAMP-2 luminal regions		PUBTATOR	Site	LAMP-1	3916	regions	Insights into the structure of the lysosomal glycoprotein coat were obtained by computational models of the LAMP-1 and LAMP-2 luminal regions.
15702487	4	12	gly	glycosylation	706:718	arg2	glycosylation sites			glycosylation sites						sites	Glycomics studies most often aim at identifying glycosylation sites, and thus are performed on deglycosylated proteins resulting in loss of site-specific details concerning the glycosylation.
15702487	4	25	gly	deglycosylated	753:766	arg1	deglycosylated proteins	deglycosylated proteins				Fterm		proteins			Glycomics studies most often aim at identifying glycosylation sites, and thus are performed on deglycosylated proteins resulting in loss of site-specific details concerning the glycosylation.
4055801	12	55	part_of	C9	1543:1544	arg1	the C9 polypeptide	C9		the C9 polypeptide		Cterm	Site	C9		polypeptide	Thus, the C9a and C9b segments of the C9 polypeptide are not clearly segregated in poly(C9).
2721499	4	49	part_of	precursor	689:697	arg1	The sequence	precursor		The sequence		Fterm	Site	precursor		sequence	The sequence of the SP-40,40 precursor bears a 77% identity to a rat sulphated glycoprotein-2 (SGP-2) which is the major secreted product of Sertoli cells.
7682553	7	25	part_of	bikunin	1152:1158	arg1	Ser10	bikunin		Ser10		PUBTATOR	AminoAcid	bikunin	259	Ser10	Biochemical and mass spectrometric analysis of the peptides containing the cross-link indicate that it is mediated by a chondroitin-4-sulfate chain that originates from a typical O-glycosidic link to Ser10 of bikunin.
1457969	1	52	part_of	thyrotrophin	192:203	arg1	the three glycosylation sites	thyrotrophin		the three glycosylation sites		Fterm	Site	thyrotrophin		sites	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
20356926	0	43	gly	glycosylation	9:21	arg1	membrane-bound transcription factor CREB-H	membrane-bound transcription factor CREB-H				Fterm		factor			N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H.
11738084	1	6	gly	glycosylated	154:165	arg1	glycosylated variants	glycosylated variants				Fterm		variants			Although human serum albumin is synthesized without carbohydrate, glycosylated variants of the protein can be found.
9030779	4	58	gly	used	628:631	arg2	these sites			these sites						sites	Evidence is presented that five of these sites are used.
11983428	0	42	part_of	contains	97:104	arg1	Stromal interaction molecule 1 AND an extracellular SAM domain	Stromal interaction molecule 1		an extracellular SAM domain		PUBTATOR	Site	Stromal interaction molecule 1	6786	domain	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	0	42	part_of	contains	97:104	arg1	STIM1 AND an extracellular SAM domain	STIM1		an extracellular SAM domain		PUBTATOR	Site	STIM1	6786	domain	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	0	42	part_of	contains	97:104	arg1	a transmembrane protein AND an extracellular SAM domain	a transmembrane protein		an extracellular SAM domain		Fterm	Site	protein		domain	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
8329384	2	29	gly	peptides	437:444	arg1	Carbohydrate composition			peptides	Carbohydrate composition					peptides	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
19592704	5	3	part_of	NCEH	851:854	arg1	the putative N-linked glycosylation sites	NCEH		the putative N-linked glycosylation sites		PUBTATOR	Site	NCEH	57552	sites	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	3	part_of	NCEH	851:854	arg1	Asn	NCEH		Asn(270), Asn(367), and Asn(389)		PUBTATOR	SpecificSite	NCEH	57552	Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	3	part_of	NCEH	851:854	arg1	Asn	NCEH		Asn(270), Asn(367), and Asn(389)		PUBTATOR	SpecificSite	NCEH	57552	Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	3	part_of	NCEH	851:854	arg1	Asn	NCEH		Asn(270), Asn(367), and Asn(389)		PUBTATOR	SpecificSite	NCEH	57552	Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
12956774	8	64	gly	N-glycosylation	1557:1571	arg1	DARC	DARC				PUBTATOR		DARC	2532		We also showed that N-glycosylation of DARC occurred on N16SS and did not influence antibody and chemokine binding.
10756055	3	31	gly	glycoprotein	736:747	arg1	Env	Env				PUBTATOR		Env	100616444		We hypothesize that this alteration unmasks existing common extracellular structures reflecting a conserved three-dimensional similarity of important elements of CXCR4 and CCR5 that are involved in HIV envelope glycoprotein (Env) interaction.
10756055	3	31	gly	glycoprotein	736:747	arg1	HIV envelope glycoprotein	HIV envelope glycoprotein				PUBTATOR		HIV envelope glycoprotein	100616444		We hypothesize that this alteration unmasks existing common extracellular structures reflecting a conserved three-dimensional similarity of important elements of CXCR4 and CCR5 that are involved in HIV envelope glycoprotein (Env) interaction.
3497198	3	50	gly	glycosylation	412:424	arg2	both glycosylation sites			both glycosylation sites						sites	For both glycosylation sites (Asn86 and Asn176) of both antigens, 80% of the structures consisted of mono- and bisialylated biantennary N-linked complex oligosaccharides, with the remaining consisting of smaller (probably high mannose) structures.
3497198	3	66	gly	sites	426:430	arg1	both glycosylation sites			both glycosylation sites						sites	For both glycosylation sites (Asn86 and Asn176) of both antigens, 80% of the structures consisted of mono- and bisialylated biantennary N-linked complex oligosaccharides, with the remaining consisting of smaller (probably high mannose) structures.
3497198	3	96	gly	bisialylated	514:525	arg1	bisialylated biantennary N-linked complex oligosaccharides				bisialylated biantennary N-linked complex oligosaccharides						For both glycosylation sites (Asn86 and Asn176) of both antigens, 80% of the structures consisted of mono- and bisialylated biantennary N-linked complex oligosaccharides, with the remaining consisting of smaller (probably high mannose) structures.
3497198	3	50	gly	glycosylation	412:424	arg2	Asn86			Asn86 and Asn176						Asn86 and Asn176	For both glycosylation sites (Asn86 and Asn176) of both antigens, 80% of the structures consisted of mono- and bisialylated biantennary N-linked complex oligosaccharides, with the remaining consisting of smaller (probably high mannose) structures.
3497198	3	66	gly	sites	426:430	arg1	Asn86			Asn86 and Asn176						Asn86 and Asn176	For both glycosylation sites (Asn86 and Asn176) of both antigens, 80% of the structures consisted of mono- and bisialylated biantennary N-linked complex oligosaccharides, with the remaining consisting of smaller (probably high mannose) structures.
26993603	0	54	part_of	Asn144	24:29	arg1	GP73 N-glycosylation	GP73 N-glycosylation		Asn144		PUBTATOR	AminoAcid	GP73 N-glycosylation	51280	Asn144	GP73 N-glycosylation at Asn144 reduces hepatocellular carcinoma cell motility and invasiveness.
12603841	0	17	part_of	AMPA	64:67	arg1	the AMPA receptor ligand-binding domain	AMPA receptor		the AMPA receptor ligand-binding domain		OGER	Site	AMPA receptor	P19493	domain	Characterization of the functional role of the N-glycans in the AMPA receptor ligand-binding domain.
12603841	0	67	part_of	receptor	69:76	arg1	the AMPA receptor ligand-binding domain	AMPA receptor		the AMPA receptor ligand-binding domain		OGER	Site	AMPA receptor	P19493	domain	Characterization of the functional role of the N-glycans in the AMPA receptor ligand-binding domain.
19671700	10	110	part_of	residues	1623:1630	arg1	TSR1	TSR1		residues		PUBTATOR	AminoAcid	TSR1	Q2NL82	Trp residues	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
9722584	8	14	part_of	NTPPHase	1114:1121	arg1	the NTPPHase region	NTPPHase		the NTPPHase region		Fterm	Site	NTPPHase		region	In the precursor protein the NTPPHase region is immediately preceded by a tetrapeptide conforming to a furin proteinase cleavage consensus sequence.
9722584	8	55	part_of	furin	1188:1192	arg1	a furin proteinase cleavage consensus sequence	furin		a furin proteinase cleavage consensus sequence		OGER	Site	furin	P09958	sequence	In the precursor protein the NTPPHase region is immediately preceded by a tetrapeptide conforming to a furin proteinase cleavage consensus sequence.
6619128	5	5	gly	bear	520:523	arg1	one serine residue AND O-glycosidically linked oligosaccharides			one serine residue	O-glycosidically linked oligosaccharides					serine residue	Three or four threonine residues and one serine residue in the region bear O-glycosidically linked oligosaccharides.
6619128	5	5	gly	bear	520:523	arg1	Three or four threonine residues AND O-glycosidically linked oligosaccharides			Three or four threonine residues	O-glycosidically linked oligosaccharides					threonine residues	Three or four threonine residues and one serine residue in the region bear O-glycosidically linked oligosaccharides.
15702487	1	76	gly	glycoproteins	260:272	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Glycans are oligosaccharides associated with proteins, and are known to confer specific functions and conformations on glycoproteins.
21053369	9	91	gly	glycosylation	1398:1410	arg2	the glycosylation sites			the glycosylation sites						sites	Most of the glycosylation sites were > 95% occupied except Asn250 and Asn6.
10712595	4	17	gly	glycosylation	658:670	arg2	the potential glycosylation site			the potential glycosylation site						site	Hence, in contrast to the vertebrate antithrombins known so far, salmon antithrombin lacks the potential glycosylation site located close to the heparin binding site.
18084303	3	25	part_of	neuroligin-1	447:458	arg1	the mouse neuroligin-1 (NL1) cholinesterase-like domain	neuroligin-1		the mouse neuroligin-1 (NL1) cholinesterase-like domain		PUBTATOR	Site	neuroligin-1	192167	domain	We report a structure of the complex at a resolution of 2.4 A between the mouse neuroligin-1 (NL1) cholinesterase-like domain and the mouse neurexin-1beta (NX1beta) LNS (laminin, neurexin and sex hormone-binding globulin-like) domain.
18084303	3	28	part_of	cholinesterase-like	466:484	arg1	the mouse neuroligin-1 (NL1) cholinesterase-like domain	cholinesterase		the mouse neuroligin-1 (NL1) cholinesterase-like domain		OGER	Site	cholinesterase	P06276	domain	We report a structure of the complex at a resolution of 2.4 A between the mouse neuroligin-1 (NL1) cholinesterase-like domain and the mouse neurexin-1beta (NX1beta) LNS (laminin, neurexin and sex hormone-binding globulin-like) domain.
7776966	13	91	gly	removed	2110:2116	arg1	wild type receptors AND N-linked carbohydrates	wild type receptors			N-linked carbohydrates	Fterm		receptors			In contrast, normal high affinity binding of FSH was maintained when N-linked carbohydrates were enzymatically removed from wild type receptors.
11152692	11	64	part_of	contains	1231:1238	arg1	The protein AND an N-glycosylation site	protein		site		Fterm	Site	protein		site	The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54).
21692750	3	35	gly	non-glycosylated	694:709	arg1	a non-glycosylated C-terminal fragment			a non-glycosylated C-terminal fragment						fragment	DIRC2 is proteolytically processed into a N-glycosylated N-terminal and a non-glycosylated C-terminal fragment respectively.
24365146	6	4	gly	unglycosylated	909:922	arg1	unglycosylated Nox1	unglycosylated Nox1				PUBTATOR		Nox1	27035		Superoxide production by unglycosylated Nox1 is largely dependent on p22(phox), which is abrogated by glutamine substitution for Pro-156 in p22(phox), a mutation leading to a defective interaction with the Nox1-activating protein Noxo1.
18420935	2	30	part_of	TLR3	247:250	arg1	TLR3 ectodomains	TLR3		TLR3 ectodomains		PUBTATOR	Site	TLR3	142980	ectodomains	TLR3 ectodomains (ECDs) dimerize on oligonucleotides of at least 40 to 50 base pairs in length, the minimal length required for signal transduction.
20145116	9	8	part_of	VEGFR-2	1236:1242	arg1	VEGFR-2 subdomains D2 and D3	VEGFR-2		VEGFR-2 subdomains D2 and D3		PUBTATOR	Site	VEGFR-2	3791	subdomains	Our structure shows that two of these loops in VEGF-C bind to VEGFR-2 subdomains D2 and D3, while one interacts primarily with D3.
21733844	8	49	gly	glycosylated	1187:1198	arg1	hAQP10	hAQP10				PUBTATOR		hAQP10	89872		Because only one third of hAQP10 was glycosylated yet the thermostability titration was mono-modal, we suggest that the presence of at least one glycosylated protein within each tetramer is sufficient to convey an enhanced structural stability to the remaining hAQP10 protomers of the tetramer.
21733844	8	63	gly	glycosylated	1295:1306	arg1	at least one glycosylated protein	at least one glycosylated protein				Fterm		protein			Because only one third of hAQP10 was glycosylated yet the thermostability titration was mono-modal, we suggest that the presence of at least one glycosylated protein within each tetramer is sufficient to convey an enhanced structural stability to the remaining hAQP10 protomers of the tetramer.
19805286	6	17	part_of	IX	870:871	arg1	two catalytic domains	CA IX		two catalytic domains		PUBTATOR	Site	CA IX	768	domains	Thus, two catalytic domains of CA IX associate to form a dimer, which is stabilized by the formation of an intermolecular disulfide bond.
12743029	5	20	part_of	CUB1-EGF-CUB2	760:772	arg1	The CUB1-EGF-CUB2 region	EGF		The CUB1-EGF-CUB2 region		PUBTATOR	Site	EGF	1950	region	The CUB1-EGF-CUB2 region mediates homodimerization and binding to MBP.
20511397	1	7	gly	glycoprotein	209:220	arg1	Apolipoprotein E	Apolipoprotein E				PUBTATOR		Apolipoprotein E	348		Apolipoprotein E (apoE) is a 34-kDa glycoprotein secreted from various cells including hepatocytes and macrophages and plays an important role in remnant lipoprotein clearance, immune responses, Alzheimer disease, and atherosclerosis.
20511397	1	7	gly	glycoprotein	209:220	arg1	a 34-kDa glycoprotein	a 34-kDa glycoprotein				Fterm		glycoprotein			Apolipoprotein E (apoE) is a 34-kDa glycoprotein secreted from various cells including hepatocytes and macrophages and plays an important role in remnant lipoprotein clearance, immune responses, Alzheimer disease, and atherosclerosis.
17662946	2	42	part_of	KIT	294:296	arg1	the entire ectodomain	KIT		the entire ectodomain		PUBTATOR	Site	KIT	3815	ectodomain	We describe the crystal structure of the entire ectodomain of KIT before and after SCF stimulation.
19153605	7	35	part_of	FS	798:799	arg1	the FS domain	FS		the FS domain		Cterm	Site	FS	10418	domain	We demonstrated that the FS domain mediates integrin binding and identified the binding site by mutagenesis.
24509848	8	31	part_of	DDR1	1279:1282	arg1	the wild-type DDR1 ectodomain	DDR1		the wild-type DDR1 ectodomain		PUBTATOR	Site	DDR1	Q08345	ectodomain	The N211Q traffics to the cell surface, and its ectodomain displays collagen I binding with an affinity similar to that of the wild-type DDR1 ectodomain.
4077844	6	5	gly	contained	1013:1021	arg1	the beta-chain AND Man6GlcNAc2	the beta-chain			Man6GlcNAc2	Fterm		beta-chain			Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	6	5	gly	contained	1013:1021	arg1	the beta-chain AND Man5GlcNAc2	the beta-chain			Man5GlcNAc2	Fterm		beta-chain			Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	6	20	gly	contained	946:954	arg1	the alpha-chain AND Man9GlcNAc2	the alpha-chain			Man9GlcNAc2	Fterm		alpha-chain			Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	6	20	gly	contained	946:954	arg1	the alpha-chain AND Man8GlcNAc2	the alpha-chain			Man8GlcNAc2	Fterm		alpha-chain			Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
11562499	3	33	gly	glycosylated	539:550	arg1	glycosylated human PEDF	glycosylated human PEDF				PUBTATOR		PEDF	5176		To provide a structural basis for understanding its many biological roles, we have solved the crystal structure of glycosylated human PEDF to 2.85 A.
19167329	0	44	gly	N-glycosylation	38:52	arg1	polypeptides			polypeptides						polypeptides	Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.
29992770	7	51	part_of	N-glycosylation	1046:1060	arg1	19 unique N-glycosylation sites	glycoproteins		19 unique N-glycosylation sites		Fterm	Site	glycoproteins		sites	Thirty-eight tryptic N-glycopeptides are identified, having 19 unique N-glycosylation sites representing 14 glycoproteins.
29992770	7	65	part_of	unique	1039:1044	arg1	19 unique N-glycosylation sites	14		19 unique N-glycosylation sites		Cterm	Site	14		sites	Thirty-eight tryptic N-glycopeptides are identified, having 19 unique N-glycosylation sites representing 14 glycoproteins.
21308849	4	2	part_of	NgR2	731:734	arg1	the isolated LRR region	NgR2		the isolated LRR region		PUBTATOR	Site	NgR2	349667	region	Here, we show that purified recombinant full length NgR1 and NgR2 maintain significantly higher binding affinity for purified MAG as compared to the isolated LRR region of either NgR1 or NgR2.
17040911	4	5	gly	glycosylation	632:644	arg2	the ten potential N-linked glycosylation sites			the ten potential N-linked glycosylation sites						sites	Nine of the ten potential N-linked glycosylation sites (Asn-41, Asn-152, Asn-234, Asn-270, Asn-330, Asn-426, Asn-452, Asn-546, and Asn-553) were found to be glycosylated in recombinant mouse meprin A using chemical and enzymatic deglycosylation methods and electrospray ionization mass spectrometry.
17040911	4	41	gly	glycosylated	754:765	arg1	the ten potential N-linked glycosylation sites			sites						sites	Nine of the ten potential N-linked glycosylation sites (Asn-41, Asn-152, Asn-234, Asn-270, Asn-330, Asn-426, Asn-452, Asn-546, and Asn-553) were found to be glycosylated in recombinant mouse meprin A using chemical and enzymatic deglycosylation methods and electrospray ionization mass spectrometry.
17040911	4	41	gly	glycosylated	754:765	arg1	recombinant mouse meprin A	meprin A		sites		OGER		meprin A		sites	Nine of the ten potential N-linked glycosylation sites (Asn-41, Asn-152, Asn-234, Asn-270, Asn-330, Asn-426, Asn-452, Asn-546, and Asn-553) were found to be glycosylated in recombinant mouse meprin A using chemical and enzymatic deglycosylation methods and electrospray ionization mass spectrometry.
17040911	4	41	gly	glycosylated	754:765	arg1	recombinant mouse meprin A	meprin A		sites		OGER		meprin A		sites	Nine of the ten potential N-linked glycosylation sites (Asn-41, Asn-152, Asn-234, Asn-270, Asn-330, Asn-426, Asn-452, Asn-546, and Asn-553) were found to be glycosylated in recombinant mouse meprin A using chemical and enzymatic deglycosylation methods and electrospray ionization mass spectrometry.
17040911	4	63	gly	Nine	597:600	arg1	Asn-553			Asn-41, Asn-152, Asn-234, Asn-270, Asn-330, Asn-426, Asn-452, Asn-546, and Asn-553						Asn-41, Asn-152, Asn-234, Asn-270, Asn-330, Asn-426, Asn-452, Asn-546, and Asn-553	Nine of the ten potential N-linked glycosylation sites (Asn-41, Asn-152, Asn-234, Asn-270, Asn-330, Asn-426, Asn-452, Asn-546, and Asn-553) were found to be glycosylated in recombinant mouse meprin A using chemical and enzymatic deglycosylation methods and electrospray ionization mass spectrometry.
18988733	3	30	gly	p65	548:550	arg1	O-GlcNAcylation	NFkappaB p65			O-GlcNAcylation	PUBTATOR		NFkappaB p65	4790		In this work, we show that O-GlcNAcylation of NFkappaB p65 decreases binding to IkappaB alpha and increases transcriptional activity under hyperglycemic conditions.
12654314	10	75	part_of	IgM	1675:1677	arg1	individual IgM glycosylation sites	IgM		individual IgM glycosylation sites		OGER	Site	IgM	P01872	sites	These results indicated great complexity in the structure and composition of oligosaccharides attached to individual IgM glycosylation sites.
11567096	0	18	part_of	receptor	116:123	arg1	the N-terminal domain	corticotropin-releasing factor receptor 1		the N-terminal domain		PUBTATOR	Site	corticotropin-releasing factor receptor 1	58959	domain	Functional and protein chemical characterization of the N-terminal domain of the rat corticotropin-releasing factor receptor 1.
10551839	10	6	gly	present	1419:1425	arg2	these proteins AND the thrombospondin type 1 repeats	these proteins			the thrombospondin type 1 repeats	Fterm		proteins			Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
26791533	3	28	gly	glycoproteins	466:478	arg1	seminal plasma glycoproteins	seminal plasma glycoproteins				Fterm		glycoproteins			It is suggested by multiple studies that seminal plasma glycoproteins play, largely undiscovered, important roles in the process of fertilization.
17711303	0	82	gly	N-Glycosylation	0:14	arg1	the human kappa opioid receptor	the human kappa opioid receptor				PUBTATOR		kappa opioid receptor	4986		N-Glycosylation of the human kappa opioid receptor enhances its stability but slows its trafficking along the biosynthesis pathway.
12911312	3	64	part_of	sites	438:442	arg1	the full-length protein	protein		sites		Fterm	Site	protein		sites	Mass spectrometry was used to identify sites of glycosylation on the full-length protein.
8053566	2	22	part_of	has	409:411	arg1	Recombinant human tissue inhibitor AND two glycosylation sites	Recombinant human tissue inhibitor		two glycosylation sites		PUBTATOR	Site	tissue inhibitor of metalloproteinases	7076	sites	Recombinant human tissue inhibitor of metalloproteinases (TIMP), which has two glycosylation sites, has been characterized to illustrate this new approach for obtaining site-specific information.
16212939	4	58	gly	N-glycosylation	700:714	arg2	potential N-glycosylation site			potential N-glycosylation site						site	The mutation of potential N-glycosylation site, by substituting Gln for either Asn7 of N-terminal 24 amino acids of hIL-1beta (Asn7Gln) or Asn84 of IL-1ra (Asn84Gln), resulted in a dramatic reduction of rhG-CSF secretion efficiency.
6587378	5	5	gly	2-glycoprotein	713:726	arg1	beta 2-glycoprotein I	beta 2-glycoprotein I				OGER		beta 2-glycoprotein I	P02749		This suggests that beta 2-glycoprotein I may have evolved by repeated duplications of a gene coding for a 60-amino acid segment of protein.
8349699	10	4	gly	N-glycosylation	1444:1458	arg2	the N-glycosylation sites	PGH synthase-1		sites		PUBTATOR		PGH synthase-1	19224	sites	Assuming that the N-glycosylation sites of PGH synthase-1 are on the luminal side of the endoplasmic reticulum (ER), and that the site of tryptic cleavage of ovine PGH synthase-1 (Arg277) is on the cytoplasmic side of the ER, we propose that both the NH2 and COOH termini of PGH synthase-1 are located in the lumen of the ER and that there are two transmembrane domains located between Asn144 and Arg277 and between Arg277 and Asn410, respectively.
12878160	11	29	gly	glycoproteins	1466:1478	arg1	two glycoproteins	two glycoproteins				Fterm		glycoproteins			Finally, knock-down of VIPL mRNA using siRNA significantly slowed down the secretion of two glycoproteins (M(R) 35 and 250 kDa) to the medium, suggesting that VIPL may also function as an ER export receptor.
17310251	6	55	part_of	protease	890:897	arg1	the serine protease domain	protease		the serine protease domain		Fterm	Site	protease		domain	Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain.
24417605	3	69	gly	glycopeptides	404:416	arg2	glycopeptides			glycopeptides						glycopeptides	N-Glycans, glycopeptides, and gangliosides were extracted and purified followed by analysis with nano-HPLC Chip quadrupole time of flight mass spectrometry and MS/MS.
12654314	6	49	gly	attached	1155:1162	arg2	the site AND Thirteen oligosaccharides			the site	Thirteen oligosaccharides					site	Thirteen oligosaccharides were attached to the site at Asn-401, including six complex-type, four hybrid-type, and three high-mannose-type oligosaccharides.
12654314	6	49	gly	attached	1155:1162	arg2	Thirteen oligosaccharides AND Asn-401			Asn-401	Thirteen oligosaccharides					Asn-401	Thirteen oligosaccharides were attached to the site at Asn-401, including six complex-type, four hybrid-type, and three high-mannose-type oligosaccharides.
18340083	8	26	gly	nonglycosylated	1126:1140	arg1	a nonglycosylated GPIHBP1	a nonglycosylated GPIHBP1				PUBTATOR		GPIHBP1	68453		Consistent with this finding, cells expressing a nonglycosylated GPIHBP1 lack the ability to bind LPL or chylomicrons.
18061361	10	32	gly	N-glycosylation	1718:1732	arg2	the three consensus N-glycosylation sites			the three consensus N-glycosylation sites						sites	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
8910321	3	54	part_of	transglutaminase	437:452	arg1	the entire transglutaminase amino acid sequence	transglutaminase		the entire transglutaminase amino acid sequence		Fterm	Site	transglutaminase		sequence	Fast atom bombardment mapping and automated Edman degradation experiments allowed us to verify that at least 85% of the entire transglutaminase amino acid sequence is identical to that derived from the cDNA of the major androgen-dependent rat prostate protein called DP1.
24766575	2	26	gly	N-glycopeptide	410:423	arg2	high-throughput N-glycopeptide profiling			high-throughput N-glycopeptide profiling						N-glycopeptide	Here we have developed a novel approach for high-throughput N-glycopeptide profiling based on a network-centric algorithm for deciphering glycan fragmentation in mass spectrometry.
15486088	1	48	part_of	proteins	367:374	arg1	Thr	proteins		Thr		Fterm	AminoAcid	proteins		Thr residues	UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases (ppGaNTases) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine from UDP-GalNAc to Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-alpha-1-O-Ser/Thr).
15486088	1	48	part_of	proteins	367:374	arg1	Ser	proteins		Ser		Fterm	AminoAcid	proteins		Ser	UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases (ppGaNTases) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine from UDP-GalNAc to Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-alpha-1-O-Ser/Thr).
15350125	3	44	gly	glycosylated	707:718	arg1	reporter sites			reporter sites						sites	Membrane topology was further evaluated and confirmed by N-glycosylation-scanning mutagenesis, as reporter sites inserted in the putative extracellular loops 1 and 3 were glycosylated.
3191509	4	25	gly	sialylglycoproteins	720:738	arg1	sialylglycoproteins	sialylglycoproteins				Fterm		sialylglycoproteins			The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
8486673	1	56	gly	glycoprotein	131:142	arg1	Rat C-reactive protein	Rat C-reactive protein				PUBTATOR		Rat C-reactive protein	25419		Rat C-reactive protein (CRP) is a pentameric glycoprotein composed of five apparently identical monomers, two of which form a disulfide-linked dimer (Rasosouli, M., Sambasivam, H., Azadi, P., Dell, A., Morris, H. R., Nagpurkar, A., Mookerjea, S., and Murray, R. K. (1992) J. Biol.
8486673	1	56	gly	glycoprotein	131:142	arg1	a pentameric glycoprotein	a pentameric glycoprotein				Fterm		glycoprotein			Rat C-reactive protein (CRP) is a pentameric glycoprotein composed of five apparently identical monomers, two of which form a disulfide-linked dimer (Rasosouli, M., Sambasivam, H., Azadi, P., Dell, A., Morris, H. R., Nagpurkar, A., Mookerjea, S., and Murray, R. K. (1992) J. Biol.
12545205	4	2	gly	carbohydrate	436:447	arg1	this protein	this protein				Fterm		protein			We have analysed the carbohydrate profile of this protein synthesized in human melanoma cell lines: WM35 from the primary tumor site and WM239, WM9, and A375 from different metastatic sites.
12545205	4	21	gly	protein	465:471	arg1	the carbohydrate profile	protein			the carbohydrate profile	Fterm		protein			We have analysed the carbohydrate profile of this protein synthesized in human melanoma cell lines: WM35 from the primary tumor site and WM239, WM9, and A375 from different metastatic sites.
23756652	3	25	part_of	furin-like	521:530	arg1	two adjacent furin-like cysteine-rich domains	furin		two adjacent furin-like cysteine-rich domains		OGER	Site	furin	P09958	domains	Here we report the complex structure of the LGR4 extracellular domain (ECD) with the RSPO1 N-terminal fragment (RSPO1-2F) containing two adjacent furin-like cysteine-rich domains (FU-CRDs).
23756652	3	27	part_of	RSPO1	460:464	arg1	the RSPO1 N-terminal fragment	RSPO1		the RSPO1 N-terminal fragment		PUBTATOR	Site	RSPO1	284654	fragment	Here we report the complex structure of the LGR4 extracellular domain (ECD) with the RSPO1 N-terminal fragment (RSPO1-2F) containing two adjacent furin-like cysteine-rich domains (FU-CRDs).
23756652	3	40	part_of	containing	497:506	arg1	the RSPO1 N-terminal fragment AND two adjacent furin-like cysteine-rich domains	RSPO1		domains		PUBTATOR	Site	RSPO1	284654	domains	Here we report the complex structure of the LGR4 extracellular domain (ECD) with the RSPO1 N-terminal fragment (RSPO1-2F) containing two adjacent furin-like cysteine-rich domains (FU-CRDs).
2110822	6	96	gly	nonsialylated	1727:1739	arg1	the sugar chains				the sugar chains						In contrast to these, the sugar chains of the latter were sialylated and nonsialylated mono- to tetraantennary complex-type sugar chains that were not fully degraded due to a metabolic defect in acid beta-galactosidase activity.
2110822	6	99	gly	sialylated	1712:1721	arg1	the sugar chains				the sugar chains						In contrast to these, the sugar chains of the latter were sialylated and nonsialylated mono- to tetraantennary complex-type sugar chains that were not fully degraded due to a metabolic defect in acid beta-galactosidase activity.
18642129	5	69	part_of	pd-FVII	749:755	arg1	N- and O-glycosylation sites	FVII		N- and O-glycosylation sites		OGER	Site	FVII	P08709	sites	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
6203908	3	26	gly	glycoprotein	124:135	arg1	the tetrameric plasma glycoprotein human alpha 2-macroglobulin	the tetrameric plasma glycoprotein human alpha 2-macroglobulin				Fterm		glycoprotein			The primary structure of the tetrameric plasma glycoprotein human alpha 2-macroglobulin has been determined.
12545205	6	4	part_of	N-cadherin	843:852	arg1	the N-cadherin polypeptides	N-cadherin		the N-cadherin polypeptides		PUBTATOR	Site	N-cadherin	1000	polypeptides	Characterisation of its carbohydrate moieties was carried out by SDS/PAGE electrophoresis and blotting, followed by immunochemical identification of the N-cadherin polypeptides and analysis of their glycans using highly specific digoxigenin or biotin labelled lectins.
29391424	4	2	gly	glycopeptides	538:550	arg2	O-linked glycopeptides			O-linked glycopeptides						glycopeptides	Automated annotation of both N- and O-linked glycopeptides was proven using standard glycoproteins.
29391424	4	20	gly	glycoproteins	578:590	arg1	standard glycoproteins	standard glycoproteins				Fterm		glycoproteins			Automated annotation of both N- and O-linked glycopeptides was proven using standard glycoproteins.
3123586	2	10	gly	attached	298:305	arg2	a threonine residue AND galactosamine			a threonine residue	galactosamine					threonine residue at position 74	The apoC-III polypeptide contains a carbohydrate chain containing galactosamine, galactose, and sialic acid attached in O-linkage to a threonine residue at position 74.
3123586	2	2	gly	contains	215:222	arg1	The apoC-III polypeptide AND a carbohydrate chain			The apoC-III polypeptide	a carbohydrate chain					polypeptide	The apoC-III polypeptide contains a carbohydrate chain containing galactosamine, galactose, and sialic acid attached in O-linkage to a threonine residue at position 74.
17139081	7	45	part_of	enzymes	1185:1191	arg1	the active-site residues	enzymes		the active-site residues		Fterm	Site	enzymes		residues	Comparison of the structure of acid-beta-glucosidase with that of xylanase, a bacterial enzyme from a closely related protein family, demonstrates a close correspondence between the active-site residues of the two enzymes.
9757569	1	11	gly	N-glycosylation	211:225	arg2	a N-glycosylation site			a N-glycosylation site						site	A mutant angiotensinogen, S14N, in which Ser14 of ovine angiotensinogen was replaced by Asn to form a N-glycosylation site, was produced in CHO cells.
20739279	5	10	gly	N-glycan	742:749	arg1	residue			residue	residue		SpecificSite			residue Asn(60)	Through crystallographic analysis of SynCAM 2, we identified within the adhesive interface of its Ig1 domain an N-glycan on residue Asn(60).
20739279	5	68	gly	residue	754:760	arg1	Asn(60)			Asn(60)						residue Asn(60)	Through crystallographic analysis of SynCAM 2, we identified within the adhesive interface of its Ig1 domain an N-glycan on residue Asn(60).
7688323	2	16	gly	sialylated	380:389	arg1	sialylated oligosaccharide chain(s)				sialylated oligosaccharide chain(s)						Recent immunological studies indicate that sialylated oligosaccharide chain(s) are also implicated in expression of the Baka determinant.
21712440	4	14	gly	unglycosylated	819:832	arg1	33 unglycosylated APP/Aβ peptides			33 unglycosylated APP/Aβ peptides						peptides	In addition to 33 unglycosylated APP/Aβ peptides, we identified 37 APP/Aβ glycopeptides with sialylated core 1 like O-glycans attached to Thr(-39, -21, -20, and -13), in a series of APP/AβX-15 glycopeptides, where X was -63, -57, -52, and -45, in relation to Asp1 of the Aβ sequence.
21712440	4	18	gly	glycopeptides	994:1006	arg2	APP/AβX-15 glycopeptides			APP/AβX-15 glycopeptides						glycopeptides	In addition to 33 unglycosylated APP/Aβ peptides, we identified 37 APP/Aβ glycopeptides with sialylated core 1 like O-glycans attached to Thr(-39, -21, -20, and -13), in a series of APP/AβX-15 glycopeptides, where X was -63, -57, -52, and -45, in relation to Asp1 of the Aβ sequence.
21712440	4	82	gly	sialylated	894:903	arg1	sialylated core 1				sialylated core 1						In addition to 33 unglycosylated APP/Aβ peptides, we identified 37 APP/Aβ glycopeptides with sialylated core 1 like O-glycans attached to Thr(-39, -21, -20, and -13), in a series of APP/AβX-15 glycopeptides, where X was -63, -57, -52, and -45, in relation to Asp1 of the Aβ sequence.
21712440	4	90	gly	attached	927:934	arg1	Thr AND O-glycans			Thr	O-glycans					Thr	In addition to 33 unglycosylated APP/Aβ peptides, we identified 37 APP/Aβ glycopeptides with sialylated core 1 like O-glycans attached to Thr(-39, -21, -20, and -13), in a series of APP/AβX-15 glycopeptides, where X was -63, -57, -52, and -45, in relation to Asp1 of the Aβ sequence.
21712440	4	78	gly	glycopeptides	875:887	arg1	sialylated core 1			glycopeptides	sialylated core 1					glycopeptides	In addition to 33 unglycosylated APP/Aβ peptides, we identified 37 APP/Aβ glycopeptides with sialylated core 1 like O-glycans attached to Thr(-39, -21, -20, and -13), in a series of APP/AβX-15 glycopeptides, where X was -63, -57, -52, and -45, in relation to Asp1 of the Aβ sequence.
1456441	10	78	gly	glycopeptides	1438:1450	arg2	The SNA-bound glycopeptides			The SNA-bound glycopeptides						glycopeptides	The SNA-bound glycopeptides were further fractionated by LPHA affinity chromatography.
8639592	11	32	gly	occupied	2109:2116	arg2	the region			the region						region	These results indicated that the region is occupied by a cluster of three bulky and acidic carbohydrate chains.
23302862	4	18	part_of	site	792:795	arg1	the insulin receptor	insulin receptor		site		PUBTATOR	Site	insulin receptor	P01308	site	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
2971663	1	16	gly	sialoglycoprotein	246:262	arg1	the major cell-surface sialoglycoprotein	the major cell-surface sialoglycoprotein				Fterm		sialoglycoprotein			The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2 results in a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein.
17563389	4	66	gly	glycosylation	782:794	arg2	glycosylation sites			glycosylation sites						sites	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
6619128	3	35	gly	present	220:226	arg2	a human IgD myeloma protein AND the oligosaccharides	protein		sites	the oligosaccharides	Fterm		protein		sites	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	3	89	gly	glycosylation	248:260	arg2	the 3 asparagine glycosylation sites	protein		sites		Fterm		protein		sites	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
20877282	3	87	part_of	plexin	569:574	arg1	the plexin ectodomain	plexin		the plexin ectodomain		Fterm	Site	plexin		ectodomain	In the absence of any structural information on the plexin ectodomain or its interaction with semaphorins the extracellular specificity and mechanism controlling plexin signalling has remained unresolved.
11279095	2	1	gly	Polysialylation	190:204	arg1	NCAM	NCAM				PUBTATOR		NCAM	4684		Polysialylation of the neural cell adhesion molecule (NCAM) is catalyzed by two polysialyltransferases, ST8Sia II (STX) and ST8Sia IV (PST), which contain sialylmotifs L and S conserved in all members of the sialyltransferases.
11279095	2	1	gly	Polysialylation	190:204	arg1	the neural cell adhesion molecule	the neural cell adhesion molecule				PUBTATOR		neural cell adhesion molecule	4684		Polysialylation of the neural cell adhesion molecule (NCAM) is catalyzed by two polysialyltransferases, ST8Sia II (STX) and ST8Sia IV (PST), which contain sialylmotifs L and S conserved in all members of the sialyltransferases.
11279095	2	52	gly	molecule	234:241	arg1	Polysialylation	neural cell adhesion molecule			Polysialylation	PUBTATOR		neural cell adhesion molecule	4684		Polysialylation of the neural cell adhesion molecule (NCAM) is catalyzed by two polysialyltransferases, ST8Sia II (STX) and ST8Sia IV (PST), which contain sialylmotifs L and S conserved in all members of the sialyltransferases.
20356926	9	41	gly	glycosylation	1147:1159	arg1	CREB-H	CREB-H				PUBTATOR		CREB-H	84699		Taken together, our findings suggest that N-linked glycosylation is required for full activation of CREB-H through intramembrane proteolysis.
21965667	3	16	part_of	FcγRI	409:413	arg1	all three extracellular Ig-like domains	FcγRI		all three extracellular Ig-like domains		PUBTATOR	Site	FcγRI	2209	domains	Here we report the first crystal structure of an FcγRI with all three extracellular Ig-like domains (designated as D1, D2, and D3).
7776966	7	100	part_of	sites	1047:1051	arg1	the FSHR as well as to elucidate their role in the functions of the FSHR	FSHR		sites		PUBTATOR	Site	FSHR	2492	sites	Therefore, further experiments, done in the context of the full-length receptor, were performed to determine the actual sites of glycosylation in the FSHR as well as to elucidate their role in the functions of the FSHR.
24279413	3	10	gly	glycosylation	662:674	arg2	their corresponding glycosylation sites			their corresponding glycosylation sites						sites	Although computational methods based on mass spectrometric data have proven to be effective in monitoring changes in the glycome, developing such methods for the glycoproteome are challenging, largely due to the inherent complexity in simultaneously studying glycan structures with their corresponding glycosylation sites.
1456441	9	38	part_of	h-STF	1361:1365	arg1	the two N-glycosylation sites	h-STF		the two N-glycosylation sites		Cterm	Site	h-STF	7018	sites	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
30037904	1	37	gly	modified	129:136	arg3	Many intracellular proteins AND O-linked GlcNAc	Many intracellular proteins			O-linked GlcNAc	Fterm		proteins			Many intracellular proteins are reversibly modified by O-linked GlcNAc (O-GlcNAc), a post-translational modification that dynamically regulates fundamental cellular processes in response to diverse environmental cues.
30037904	1	37	gly	modified	129:136	arg3	Many intracellular proteins AND O-GlcNAc	Many intracellular proteins			O-GlcNAc	Fterm		proteins			Many intracellular proteins are reversibly modified by O-linked GlcNAc (O-GlcNAc), a post-translational modification that dynamically regulates fundamental cellular processes in response to diverse environmental cues.
2415652	6	99	gly	beta	1248:1251	arg1	The O-linked oligosaccharides	hCG beta			The O-linked oligosaccharides	PUBTATOR		hCG beta	1082		The O-linked oligosaccharides of standard hCG beta are heterogeneous in size; 13% are of the largest (hexasaccharide) form.
6725284	0	12	gly	galactoglycoprotein	56:74	arg1	galactoglycoprotein	galactoglycoprotein				PUBTATOR		galactoglycoprotein	6693		The structure of the carbohydrate units of human plasma galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy.
22173220	7	22	gly	position	911:918	arg1	a glycan			position 342	a glycan					position 342	Two aspartate residues proposed to interact with flagellin (Asp294 and Asp366) are sterically occluded by a glycan at position 342.
11439087	0	55	gly	N-glycosylation	25:39	arg2	N-glycosylation sites			N-glycosylation sites						sites	Site-directed removal of N-glycosylation sites in BST-1/CD157: effects on molecular and functional heterogeneity.
8885240	1	2	gly	glycosylation	543:555	arg1	the proteolytic processing sites			the proteolytic processing sites						sites	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	1	2	gly	glycosylation	543:555	arg1	the N-linked glycosylation site			the N-linked glycosylation site						site	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	1	10	gly	glycosylation	573:585	arg2	the N-linked glycosylation site			the N-linked glycosylation site						site	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
486087	1	6	part_of	C-chain	224:230	arg1	amino acid residues	C-chain		amino acid residues		Fterm	SpecificSite	C-chain		residues 38--51	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	1	6	part_of	C-chain	224:230	arg1	residues 42--90	C-chain		residues 42--90		Fterm	SpecificSite	C-chain		residues 42--90	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	1	33	part_of	C1q	255:257	arg1	The sequences	C1q		The sequences		PUBTATOR	Site	C1q	712	sequences	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	1	39	part_of	A-chain	188:194	arg1	38--51	A-chain		38--51		Fterm	SpecificSite	A-chain		residues 38--51	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
21402931	3	20	gly	ZP	417:418	arg1	betaglycan	Other ZP			betaglycan	Cterm		Other ZP			Other ZP proteins (namely, betaglycan and endoglin) do not polymerize but serve as important membrane coreceptors for ligands in the transforming growth factor-β (TGF-β) superfamily.
21402931	3	32	gly	Other	411:415	arg1	betaglycan	Other ZP			betaglycan	Cterm		Other ZP			Other ZP proteins (namely, betaglycan and endoglin) do not polymerize but serve as important membrane coreceptors for ligands in the transforming growth factor-β (TGF-β) superfamily.
8130392	6	94	gly	Asn-linked	915:924	arg1	its Asn-linked oligosaccharides			Asn	its Asn-linked oligosaccharides					Asn	In addition, we found that rHPC contains N-acetylgalactosamine (2.6 mol GalNAc/mol rHPC) in its Asn-linked oligosaccharides, while plasma HPC is devoid of GalNAc.
8130392	6	134	gly	contains	851:858	arg1	rHPC AND N-acetylgalactosamine	rHPC			N-acetylgalactosamine	OGER		rHPC	P52873		In addition, we found that rHPC contains N-acetylgalactosamine (2.6 mol GalNAc/mol rHPC) in its Asn-linked oligosaccharides, while plasma HPC is devoid of GalNAc.
8130392	6	134	gly	contains	851:858	arg1	rHPC AND 2.6 mol GalNAc/mol rHPC	rHPC			2.6 mol GalNAc/mol rHPC	OGER		rHPC	P52873		In addition, we found that rHPC contains N-acetylgalactosamine (2.6 mol GalNAc/mol rHPC) in its Asn-linked oligosaccharides, while plasma HPC is devoid of GalNAc.
10944330	4	10	gly	non-glycosylated	595:610	arg1	the non-glycosylated peptide fragment 120-132			the non-glycosylated peptide fragment 120-132						fragment	The antibody shows a high affinity for the glycan N-linked to Asn123, but it also cross-reacts with the non-glycosylated peptide fragment 120-132.
14573609	4	18	gly	glycosylated	578:589	arg1	Heparanase protein	Heparanase protein		Asn residues		PUBTATOR		Heparanase protein	10855	Asn residues	Heparanase protein was glycosylated at six Asn residues in human tumor cell lines.
8130392	4	133	part_of	protease	636:643	arg1	four N-glycosylation sites	protease		four N-glycosylation sites		Fterm	Site	protease		sites	Protein C is a heavily post-translationally modified serine protease with four N-glycosylation sites.
2721499	3	2	part_of	contains	557:564	arg1	The precursor AND six N-linked glycosylation sites	The precursor		six N-linked glycosylation sites		Fterm	Site	precursor		sites	The precursor is preceded by a signal sequence for vectorial export and contains six N-linked glycosylation sites distributed equally between the two chains of the structure.
17322565	1	33	gly	utilized	253:260	arg2	four of five putative N-linked glycosylation sites			four of five putative N-linked glycosylation sites						sites	We previously identified that four of five putative N-linked glycosylation sites of human endothelial lipase (EL) are utilized and suggested that the substitution of asparagine-116 (Asn-116) with alanine (Ala) (N116A) increased the hydrolytic activity of EL.
17322565	1	15	gly	glycosylation	196:208	arg2	four of five putative N-linked glycosylation sites	endothelial lipase		sites		PUBTATOR		endothelial lipase	9388	sites	We previously identified that four of five putative N-linked glycosylation sites of human endothelial lipase (EL) are utilized and suggested that the substitution of asparagine-116 (Asn-116) with alanine (Ala) (N116A) increased the hydrolytic activity of EL.
17322565	1	15	gly	glycosylation	196:208	arg1	EL	EL		sites		PUBTATOR		EL	9388	sites	We previously identified that four of five putative N-linked glycosylation sites of human endothelial lipase (EL) are utilized and suggested that the substitution of asparagine-116 (Asn-116) with alanine (Ala) (N116A) increased the hydrolytic activity of EL.
20534510	6	13	part_of	PDGFRbeta	1300:1308	arg1	the third Ig domain	PDGFRbeta		the third Ig domain		PUBTATOR	Site	PDGFRbeta	5159	domain	A large-scale structural organization and rearrangement is observed for PDGF-B upon receptor binding, in which the PDGF-B L1 loop, disordered in the structure of the free form, adopts a highly specific conformation to form hydrophobic interactions with the third Ig domain of PDGFRbeta.
21569239	2	3	part_of	F-spondin	339:347	arg1	FS domain	F-spondin		domain		PUBTATOR	Site	F-spondin	10418	domain	The reelin_N domain and the F-spondin domain (FS domain) comprise a proteolytic fragment that interacts with the cell membrane and guides the projection of commissural axons to floor plate.
19299457	13	66	gly	glycoprotein	1824:1835	arg1	glycoprotein hormone binding and function	glycoprotein hormone binding and function				Fterm		glycoprotein			These findings expand our present concept of glycoprotein hormone binding and function.
8172892	3	62	gly	contained	487:495	arg1	AP beta AND galactosamine	AP beta			galactosamine	PUBTATOR		AP beta	6051		Amino acid analysis showed that AP alpha, but not AP beta and AP gamma, contained galactosamine in addition to glucosamine, thereby suggesting the presence of an O-linked sugar chain(s) in the molecule of AP alpha.
8172892	3	62	gly	contained	487:495	arg1	AP alpha AND galactosamine	AP alpha			galactosamine	PUBTATOR		AP alpha	2028		Amino acid analysis showed that AP alpha, but not AP beta and AP gamma, contained galactosamine in addition to glucosamine, thereby suggesting the presence of an O-linked sugar chain(s) in the molecule of AP alpha.
30335141	6	26	gly	glycoprotein	1060:1071	arg1	a co-transfected secretory membrane glycoprotein	glycoprotein				Fterm		glycoprotein			In transfected Chinese hamster ovary AP-1 cells, the Leu515Phe mutant protein was correctly targeted to the TGN/post-Golgi vesicles, but its N-linked oligosaccharide maturation as well as that of a co-transfected secretory membrane glycoprotein, vesicular stomatitis virus G (VSVG) glycoprotein, was reduced compared to cells co-expressing SLC9A7 wild-type and VSVG.
30335141	6	91	gly	glycoprotein	1010:1021	arg1	a co-transfected secretory membrane glycoprotein	glycoprotein				Fterm		glycoprotein			In transfected Chinese hamster ovary AP-1 cells, the Leu515Phe mutant protein was correctly targeted to the TGN/post-Golgi vesicles, but its N-linked oligosaccharide maturation as well as that of a co-transfected secretory membrane glycoprotein, vesicular stomatitis virus G (VSVG) glycoprotein, was reduced compared to cells co-expressing SLC9A7 wild-type and VSVG.
10731668	0	31	part_of	receptor	132:139	arg1	the atypical Asn-X-Cys sequence	epidermal growth factor receptor		the atypical Asn-X-Cys sequence		PUBTATOR	Site	epidermal growth factor receptor	1956	sequence	Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.
10988252	4	59	gly	sEGFR	622:626	arg1	the oligosaccharides	EGFR			the oligosaccharides	PUBTATOR		EGFR	1956		After liberation of the oligosaccharides from sEGFR with PNGase F, the glycans were fractionated along different routes, including Concanavalin A affinity chromatography, anion-exchange chromatography, HPLC and high-pH anion-exchange chromatography.
28450392	3	81	gly	NSL3	770:773	arg1	O-GlcNAcylation	NSL3			O-GlcNAcylation	PUBTATOR		NSL3	55683		Here, we demonstrate that OGT1 regulates the activity of the NSL complex by mainly acetylating histone H4 Lys-16, Lys-5, and Lys-8 via O-GlcNAcylation and stabilization of the NSL complex subunit NSL3.
7592613	0	31	gly	glycoprotein	77:88	arg1	a human glycoprotein	a human glycoprotein				Fterm		glycoprotein			Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	0	31	gly	glycoprotein	77:88	arg1	glycodelin	glycodelin				PUBTATOR		glycodelin	5047		Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.
19690161	3	5	part_of	vIL-6	512:516	arg1	the two N-linked sites	vIL		the two N-linked sites		OGER	Site	vIL	P09327	sites	Here we describe heterogeneity in the composition of the glycans of the two N-linked sites of vIL-6.
3484703	5	28	gly	glycosylation	637:649	arg2	position 30			position 30						position 30	Three carbohydrate side chains were found in the heavy chain, all of them N-glycosidically linked to asparagine, which is present in the acceptor sequon Asn-Xaa-Thr (or -Ser); one additional potential glycosylation site devoid of a sugar side chain is found at position 30.
3484703	5	28	gly	glycosylation	637:649	arg2	one additional potential glycosylation site			one additional potential glycosylation site						site	Three carbohydrate side chains were found in the heavy chain, all of them N-glycosidically linked to asparagine, which is present in the acceptor sequon Asn-Xaa-Thr (or -Ser); one additional potential glycosylation site devoid of a sugar side chain is found at position 30.
19088065	9	80	gly	N-glycosylation	1099:1113	arg2	a single N-glycosylation site			a single N-glycosylation site						site	The presence of a single N-glycosylation site on KLK6 was confirmed by site-directed mutagenesis.
1569071	10	57	part_of	IGF-II	1980:1985	arg1	the Ser66-Lys88 endoprotease-generated E domain peptides	IGF-II		the Ser66-Lys88 endoprotease-generated E domain peptides		PUBTATOR	Site	IGF-II	P01344	peptides	When the Ser66-Lys88 endoprotease-generated E domain peptides from pI5.1 and 5.4 high Mr IGF-II were treated with the glycosidases, they had relative mobility changes during sodium dodecyl sulfate-polyacrylamide gel electrophoresis that were similar to those of the intact precursors.
21908432	6	20	part_of	GPIbβ	822:826	arg1	residue Tyr106	GPIbβ,		residue Tyr106		PUBTATOR	AminoAcid	GPIbβ,	2812	residue Tyr106	Central to this interface is residue Tyr106 from GPIbβ, which inserts into a pocket generated by 2 loops (b,c) from GPIX.
25500532	4	4	part_of	receptor	518:525	arg1	the two receptor extracellular domains	receptor		the two receptor extracellular domains		Fterm	Site	receptor	3606	domains	Here, we present a crystal structure of human IL-18 bound to the two receptor extracellular domains.
18308854	3	4	gly	glycosylation	556:568	arg2	oatp1a1's four potential N-linked glycosylation sites			oatp1a1's four potential N-linked glycosylation sites						sites	Which of oatp1a1's four potential N-linked glycosylation sites are actually glycosylated and their influence on transport function have not been investigated in a mammalian system.
16186819	0	30	part_of	thrombospondin-2	56:71	arg1	the calcium-rich signature domain	thrombospondin-2		the calcium-rich signature domain		PUBTATOR	Site	thrombospondin-2	7058	domain	Structure of the calcium-rich signature domain of human thrombospondin-2.
1517205	3	42	part_of	containing	605:614	arg1	Two large peptides AND positions 44-63	Two large peptides		positions 44-63						positions 44	Two large peptides containing Ser-61 (positions 44-63), named hIX-GP1 and hIX-GP2, were first isolated from the lysyl endopeptidase-digest of human factor IX, by reversed-phase high performance liquid chromatography (HPLC).
1517205	3	42	part_of	containing	605:614	arg1	Two large peptides AND Ser-61	Two large peptides		Ser-61						Ser-61	Two large peptides containing Ser-61 (positions 44-63), named hIX-GP1 and hIX-GP2, were first isolated from the lysyl endopeptidase-digest of human factor IX, by reversed-phase high performance liquid chromatography (HPLC).
12610629	5	14	part_of	Herceptin	1008:1016	arg1	the Herceptin antigen-binding fragment	Herceptin		the Herceptin antigen-binding fragment		Fterm	Site	Herceptin		fragment	Here we report crystal structures of the entire extracellular regions of rat HER2 at 2.4 A and human HER2 complexed with the Herceptin antigen-binding fragment (Fab) at 2.5 A.
12610629	5	51	part_of	HER2	960:963	arg1	the entire extracellular regions	HER2		the entire extracellular regions		PUBTATOR	Site	HER2	2064	regions	Here we report crystal structures of the entire extracellular regions of rat HER2 at 2.4 A and human HER2 complexed with the Herceptin antigen-binding fragment (Fab) at 2.5 A.
12839991	5	5	part_of	NgR	924:926	arg1	the biologically active ligand-binding soluble ectodomain	NgR		the biologically active ligand-binding soluble ectodomain		OGER	Site	NgR	Q9BZR6	ectodomain	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
3200844	10	61	gly	glycosylation	1407:1419	arg2	a presumptive glycosylation site			a presumptive glycosylation site						site	Analysis of the residues making up a presumptive glycosylation site suggests that the sequence is unlike any known sites for enzymatic N- or O-linked glycosylation.
15253437	5	10	part_of	sites	1285:1289	arg1	37 glycoproteins	glycoproteins		sites		Fterm	Site	glycoproteins		sites	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
25456591	5	9	gly	glycopeptides	1177:1189	arg2	multiple intact glycopeptides			multiple intact glycopeptides						glycopeptides	Using fetuin as a model, all identified S/T elimination sites were matched to multiple intact glycopeptides with a 31% FDR.
26271046	6	27	gly	N-glycosylation	1052:1066	arg2	potential N-glycosylation sites			potential N-glycosylation sites						sites	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	41	gly	sites	1068:1072	arg1	potential N-glycosylation sites			potential N-glycosylation sites						sites	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	27	gly	N-glycosylation	1052:1066	arg2	N413			N256, N370, N406, and N413						N256, N370, N406, and N413	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	27	gly	N-glycosylation	1052:1066	arg2	N406			N256, N370, N406, and N413						N256, N370, N406, and N413	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	27	gly	N-glycosylation	1052:1066	arg2	N370			N256, N370, N406, and N413						N256, N370, N406, and N413	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	27	gly	N-glycosylation	1052:1066	arg2	N406			N256, N370, N406, and N413						N256, N370, N406, and N413	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	27	gly	N-glycosylation	1052:1066	arg2	N370			N256, N370, N406, and N413						N256, N370, N406, and N413	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	27	gly	N-glycosylation	1052:1066	arg2	N370			N256, N370, N406, and N413						N256, N370, N406, and N413	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	41	gly	sites	1068:1072	arg1	N413			N256, N370, N406, and N413						N256, N370, N406, and N413	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	41	gly	sites	1068:1072	arg1	N370			N256, N370, N406, and N413						N256, N370, N406, and N413	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	41	gly	sites	1068:1072	arg1	N256			N256, N370, N406, and N413						N256, N370, N406, and N413	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	41	gly	sites	1068:1072	arg1	N370			N256, N370, N406, and N413						N256, N370, N406, and N413	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	41	gly	sites	1068:1072	arg1	N256			N256, N370, N406, and N413						N256, N370, N406, and N413	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
26271046	6	41	gly	sites	1068:1072	arg1	N256			N256, N370, N406, and N413						N256, N370, N406, and N413	In the present study, using a series of mutants lacking potential N-glycosylation sites (N256, N370, N406, and N413) within GluA2, we demonstrated that the mutant lacking the N-glycan at N370 strongly suppressed the intracellular trafficking of GluA2 from the endoplasmic reticulum (ER) in HEK293 cells.
15385547	5	32	part_of	contain	766:772	arg1	SPPL2a AND a signal sequence	SPPL2a		a signal sequence		PUBTATOR	Site	Whereas SPPL2a	84888	sequence	Whereas SPPL2a, -2b, and -2c contain a signal sequence, SPP and SPPL3 contain a type I signal anchor sequence for initiation of protein translocation and membrane insertion.
15385547	5	1	part_of	contain	807:813	arg1	SPP AND a type I signal anchor sequence	SPP		a type I signal anchor sequence		PUBTATOR	Site	SPP	81502	sequence	Whereas SPPL2a, -2b, and -2c contain a signal sequence, SPP and SPPL3 contain a type I signal anchor sequence for initiation of protein translocation and membrane insertion.
15385547	5	1	part_of	contain	807:813	arg1	SPPL3 AND a type I signal anchor sequence	SPPL3		a type I signal anchor sequence		PUBTATOR	Site	SPPL3	121665	sequence	Whereas SPPL2a, -2b, and -2c contain a signal sequence, SPP and SPPL3 contain a type I signal anchor sequence for initiation of protein translocation and membrane insertion.
17591618	10	7	part_of	CFH	1561:1563	arg1	the NGSP sequence	CFH		the NGSP sequence		PUBTATOR	Site	CFH	P08603	sequence	The absence of glycosylation at Asn199 of the NGSP sequence of CFH is shown.
10419520	13	74	part_of	S2P	1706:1708	arg1	the active site	S2P		the active site		PUBTATOR	Site	S2P	51360	site	The hydrophobicity of these sequences suggests that the active site of S2P is located within the membrane in an ideal position to cleave its target, a Leu-Cys bond in the first transmembrane helix of SREBPs.
2393398	5	55	gly	glycopeptide	800:811	arg2	the glycopeptide			the glycopeptide						glycopeptide	A combination of these methodologies showed an equimolar ratio of peptide and fucose in the glycopeptide.
14970177	4	16	gly	O-glycosylated	816:829	arg1	hIL-6	hIL-6				OGER		hIL-6	P05231		Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	4	28	gly	N-glycosylated	781:794	arg1	hIL-6	hIL-6		N73		OGER		hIL-6	P05231	N73	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
2040275	1	44	part_of	immunoglobulin	195:208	arg1	a 22-residue peptide	immunoglobulin M		a 22-residue peptide		OGER	Site	immunoglobulin M	P01871	peptide	1H-NMR spectroscopy has been used to study the conformation and dynamics of the isolated tailpiece from human serum immunoglobulin M, a 22-residue peptide containing a single asparagine glycosylation site.
2040275	1	77	part_of	containing	234:243	arg1	human serum immunoglobulin M AND a single asparagine glycosylation site	immunoglobulin M		site		OGER	Site	immunoglobulin M	P01871	site	1H-NMR spectroscopy has been used to study the conformation and dynamics of the isolated tailpiece from human serum immunoglobulin M, a 22-residue peptide containing a single asparagine glycosylation site.
6546754	5	5	part_of	Ba	610:611	arg1	The Ba fragment	Ba		The Ba fragment		Cterm	Site	Ba		fragment	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	5	20	part_of	plasminogen	752:762	arg1	the "kringle" regions	plasminogen		the "kringle" regions		OGER	Site	plasminogen	P00747	regions	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	5	50	part_of	prothrombin	736:746	arg1	the "kringle" regions	prothrombin		the "kringle" regions		OGER	Site	prothrombin	P00734	regions	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	5	48	part_of	contain	635:641	arg1	The Ba fragment AND three regions	The Ba fragment		three regions						regions	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
7681597	3	10	gly	glycopeptides	491:503	arg2	The glycopeptides			The glycopeptides						glycopeptides	The glycopeptides thus obtained were treated with sialidase and beta-galactosidase.
11602603	9	82	part_of	epsilon	1375:1381	arg1	The amino acid sequence	tryptase epsilon		The amino acid sequence		PUBTATOR	Site	tryptase epsilon	64063	sequence	The amino acid sequence of human tryptase epsilon is 38-44% identical to those of human tryptase alpha, tryptase beta I, tryptase beta II, tryptase beta III, transmembrane tryptase/tryptase gamma, marapsin, and Esp-1/testisin.
21240269	4	39	part_of	region	697:702	arg1	the catalytic domain	region		the catalytic domain						domain	They indicate that a loop region in the catalytic domain is a major determinant for the substrate specificity of the Enpp family enzymes.
30867591	4	83	gly	glycoprotein	759:770	arg1	4F2 cell-surface antigen heavy chain (4F2hc; also known as SLC3A2)-a type II membrane glycoprotein	4F2 cell-surface antigen heavy chain (4F2hc; also known as SLC3A2)-a type II membrane glycoprotein				Fterm		glycoprotein			LAT1 forms a heteromeric amino acid transporter complex with 4F2 cell-surface antigen heavy chain (4F2hc; also known as SLC3A2)-a type II membrane glycoprotein that is essential for the stability of LAT1 and for its localization to the plasma membrane8,9.
17715132	9	40	gly	N-glycosylation	1149:1163	arg1	Pannexin1	Pannexin1				PUBTATOR		Pannexin1	24145		We propose that N-glycosylation of Pannexin1 could be a significant mechanism for regulating the trafficking of these membrane proteins to the cell surface in different tissues.
8477709	7	5	gly	attached	1473:1480	arg2	Asn24 AND triantennary oligosaccharides			Asn24	triantennary oligosaccharides					Asn24	Only tetraantennary chains with 0-3 N-acetyllactosamine repeats were detected at Asn38 and Asn83, while almost all of the di- and triantennary oligosaccharides were attached to Asn24.
8477709	7	5	gly	attached	1473:1480	arg2	Asn24 AND di-			Asn24	di-					Asn24	Only tetraantennary chains with 0-3 N-acetyllactosamine repeats were detected at Asn38 and Asn83, while almost all of the di- and triantennary oligosaccharides were attached to Asn24.
8477709	7	14	gly	detected	1377:1384	arg2	Asn83 AND Only tetraantennary chains			Asn38 and Asn83	Only tetraantennary chains					Asn38 and Asn83	Only tetraantennary chains with 0-3 N-acetyllactosamine repeats were detected at Asn38 and Asn83, while almost all of the di- and triantennary oligosaccharides were attached to Asn24.
22399287	10	18	gly	glycosylated	1319:1330	arg1	CNNM2	CNNM2		residue Asn-112		PUBTATOR		CNNM2	54805	residue Asn-112	Mutagenesis screening showed that CNNM2 is glycosylated at residue Asn-112, stabilizing CNNM2 on the plasma membrane.
10531064	0	25	part_of	receptor	57:64	arg1	the ectodomain	transferrin receptor		the ectodomain		PUBTATOR	Site	transferrin receptor	7037	ectodomain	Crystal structure of the ectodomain of human transferrin receptor.
19664639	3	15	part_of	MuSK	509:512	arg1	The ectodomain	MuSK		The ectodomain		PUBTATOR	Site	MuSK	O15146	ectodomain	The ectodomain of MuSK comprises three immunoglobulin-like domains and a cysteine-rich domain (Fz-CRD) related to those in Frizzled proteins, the receptors for Wnts.
12906826	3	23	gly	domain	450:455	arg1	an 8-fold repeat			domain	an 8-fold repeat					domain	The enzyme consists of two domains, the catalytic domain, with an alpha/beta hydrolase fold, and a beta propeller domain with an 8-fold repeat of a four-strand beta sheet motif.
12906826	3	28	gly	domain	514:519	arg1	an 8-fold repeat			domain	an 8-fold repeat					domain	The enzyme consists of two domains, the catalytic domain, with an alpha/beta hydrolase fold, and a beta propeller domain with an 8-fold repeat of a four-strand beta sheet motif.
12906826	3	39	gly	motif	571:575	arg1	an 8-fold repeat			motif	an 8-fold repeat					motif	The enzyme consists of two domains, the catalytic domain, with an alpha/beta hydrolase fold, and a beta propeller domain with an 8-fold repeat of a four-strand beta sheet motif.
28661582	3	13	part_of	tyrosinase-like	543:557	arg1	the typical tyrosinase-like subdomain	tyrosinase		the typical tyrosinase-like subdomain		OGER	Site	tyrosinase	P14679	subdomain	Herein we show that the typical tyrosinase-like subdomain of TYRP1 contains two zinc ions in the active site instead of copper ions as found in tyrosinases, which explains why TYRP1 does not exhibit tyrosinase redox activity.
28661582	3	35	part_of	TYRP1	572:576	arg1	the typical tyrosinase-like subdomain	TYRP1		the typical tyrosinase-like subdomain		OGER	Site	TYRP1	P17643	subdomain	Herein we show that the typical tyrosinase-like subdomain of TYRP1 contains two zinc ions in the active site instead of copper ions as found in tyrosinases, which explains why TYRP1 does not exhibit tyrosinase redox activity.
8344946	5	62	gly	glycopeptides	975:987	arg2	the glycopeptides			the glycopeptides						glycopeptides	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
17157876	7	24	gly	occupied	1630:1637	arg2	equivalent sites			equivalent sites						sites	Three Thr residues at the distal TT edge of CPN1 are O-linked to N-acetyl glucosamine sugars; equivalent sites in the membrane-anchored CPM are occupied by basic residues probably involved in membrane interaction.
17157876	7	72	gly	Thr	1492:1494	arg1	O-linked to N-acetyl glucosamine sugars			Thr residues	O-linked to N-acetyl glucosamine sugars					Thr residues	Three Thr residues at the distal TT edge of CPN1 are O-linked to N-acetyl glucosamine sugars; equivalent sites in the membrane-anchored CPM are occupied by basic residues probably involved in membrane interaction.
17563389	8	50	gly	glycosylation	1502:1514	arg1	NK1R	NK1R				PUBTATOR		NK1R	6869		Therefore, glycosylation of NK1R may stabilize the receptor in the plasma membrane.
8323299	0	39	gly	glycoproteins	94:106	arg1	human lysosomal membrane glycoproteins lamp-1 and lamp-2	human lysosomal membrane glycoproteins lamp-1 and lamp-2				Fterm		glycoproteins			Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	39	gly	glycoproteins	94:106	arg1	lamp-2	lamp-2				PUBTATOR		lamp-2	3920		Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	39	gly	glycoproteins	94:106	arg1	lamp-1	lamp-1				PUBTATOR		lamp-1	3916		Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
2275556	7	109	gly	glycosylation	1427:1439	arg1	mouse cathepsin L	mouse cathepsin L				PUBTATOR		cathepsin L	13039		Site-directed mutagenesis of the mouse liver cDNA and expression in COS monkey cells was used to examine the glycosylation of mouse cathepsin L.
8329384	1	77	gly	attached	200:207	arg2	Thr/Ser residues AND O-Linked fucose			Thr/Ser residues	O-Linked fucose					residues	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
12799386	1	73	gly	glycoproteins	159:171	arg1	three glycoproteins	three glycoproteins				Fterm		glycoproteins			The zona pellucida is an extracellular matrix consisting of three glycoproteins that surrounds mammalian eggs and mediates fertilization.
8033893	0	35	gly	glycosylated	22:33	arg1	platelet factor 4	platelet factor 4				OGER		platelet factor 4	P06765		Rat platelets contain glycosylated and non-glycosylated forms of platelet factor 4.
8033893	0	68	gly	non-glycosylated	39:54	arg1	platelet factor 4	platelet factor 4				OGER		platelet factor 4	P06765		Rat platelets contain glycosylated and non-glycosylated forms of platelet factor 4.
24417605	6	0	gly	found	840:844	arg1	multiple glycoproteins AND a biantennary complex type glycan	multiple glycoproteins			a biantennary complex type glycan	Fterm		glycoproteins			The most abundant N-glycan was a biantennary complex type glycan with two sialic acids (Hexose5HexNAc4Neu5Ac2) and was found in multiple glycoproteins using site-specific glycosylation analysis.
24417605	6	0	gly	found	840:844	arg2	multiple glycoproteins AND The most abundant N-glycan	multiple glycoproteins			The most abundant N-glycan	Fterm		glycoproteins			The most abundant N-glycan was a biantennary complex type glycan with two sialic acids (Hexose5HexNAc4Neu5Ac2) and was found in multiple glycoproteins using site-specific glycosylation analysis.
24417605	6	65	gly	glycoproteins	858:870	arg1	multiple glycoproteins	multiple glycoproteins				Fterm		glycoproteins			The most abundant N-glycan was a biantennary complex type glycan with two sialic acids (Hexose5HexNAc4Neu5Ac2) and was found in multiple glycoproteins using site-specific glycosylation analysis.
3497398	2	1	part_of	von	336:338	arg1	the von Willebrand factor-binding domain	von Willebrand factor		the von Willebrand factor-binding domain		OGER	Site	von Willebrand factor	P04275	domain	This includes the complete sequence of the amino-terminal tryptic fragment of 290 residues comprising the von Willebrand factor-binding domain.
3497398	2	47	part_of	Willebrand	340:349	arg1	the von Willebrand factor-binding domain	von Willebrand factor		the von Willebrand factor-binding domain		OGER	Site	von Willebrand factor	P04275	domain	This includes the complete sequence of the amino-terminal tryptic fragment of 290 residues comprising the von Willebrand factor-binding domain.
3497398	2	96	part_of	factor-binding	351:364	arg1	the von Willebrand factor-binding domain	von Willebrand factor		the von Willebrand factor-binding domain		OGER	Site	von Willebrand factor	P04275	domain	This includes the complete sequence of the amino-terminal tryptic fragment of 290 residues comprising the von Willebrand factor-binding domain.
23269669	8	28	gly	glycosylation	1480:1492	arg2	the same sites			sites						sites	Interaction with VIP36 is dependent on glycosylation at the same sites that allow GC-C to fold and bind ligand.
24018687	0	56	gly	N-glycosylation	30:44	arg2	a conserved N-glycosylation site			a conserved N-glycosylation site						site	Low stability and a conserved N-glycosylation site are associated with regulation of the discoidin domain receptor family by glucose via post-translational N-glycosylation.
12603841	1	15	part_of	subunits	145:152	arg1	The ligand-binding domains	AMPA receptor subunits		The ligand-binding domains		OGER	Site	AMPA receptor subunits	P19493	domains	The ligand-binding domains of AMPA receptor subunits carry two conserved N-glycosylation sites.
12603841	1	49	part_of	carry	154:158	arg1	The ligand-binding domains AND two conserved N-glycosylation sites	AMPA receptor subunits		sites		OGER	Site	AMPA receptor subunits	P19493	sites	The ligand-binding domains of AMPA receptor subunits carry two conserved N-glycosylation sites.
18533687	3	2	part_of	contains	406:413	arg1	RXFP1 AND six putative Asn-linked glycosylation sites	RXFP1		six putative Asn-linked glycosylation sites		PUBTATOR	Site	RXFP1	59350	sites	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
2403553	8	74	gly	released	1072:1079	arg2	peptide AND O-linked oligosaccharides			peptide	O-linked oligosaccharides					peptide	The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
2403553	8	61	gly	contains	1028:1035	arg1	The transferrin receptor AND O-linked oligosaccharides	The transferrin receptor			O-linked oligosaccharides	PUBTATOR		transferrin receptor	7018		The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
10764840	8	2	gly	motif	1285:1289	arg1	a second fucose residue			motif	a second fucose residue					motif	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	18	gly	present	1242:1248	arg2	a sialyl Le(x)motif AND a second fucose residue			motif	a second fucose residue					motif	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
15606899	1	32	part_of	enzyme	323:328	arg1	the C-terminal cytosolic tail	enzyme		the C-terminal cytosolic tail		Fterm	Site	enzyme		tail	Using a yeast two-hybrid system, we screened a human brain cDNA library for possible interacting proteins with the C-terminal cytosolic tail of the beta-secretase beta-amyloid protein converting enzyme (BACE)1.
15606899	1	37	part_of	proteins	225:232	arg1	the C-terminal cytosolic tail	proteins		the C-terminal cytosolic tail		Fterm	Site	proteins		tail	Using a yeast two-hybrid system, we screened a human brain cDNA library for possible interacting proteins with the C-terminal cytosolic tail of the beta-secretase beta-amyloid protein converting enzyme (BACE)1.
9883900	4	33	part_of	IGFBP-5	574:580	arg1	Different fragments	IGFBP-5		Different fragments		PUBTATOR	Site	IGFBP-5	3488	fragments	Different fragments of IGFBP-5 with molecular sizes from 12 to 25 kDa were identified.
8665956	4	41	gly	glycosylated	749:760	arg1	Sg II	Sg II				PUBTATOR		Sg II	6407		To investigate the molecular interaction of Sg with PSA and PCI, we purified Sg II from seminal coagula as a soluble form and found that Sg II is glycosylated with heterogeneous carbohydrate moieties.
26993603	3	7	part_of	GP73	560:563	arg1	three GP73 N-glycosylation sites	GP73		three GP73 N-glycosylation sites		PUBTATOR	Site	GP73	51280	sites	We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398.
26993603	3	7	part_of	GP73	560:563	arg1	Asn144	GP73		Asn109, Asn144 and Asn398		PUBTATOR	AminoAcid	GP73	51280	Asn109, Asn144 and Asn398	We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398.
26993603	3	7	part_of	GP73	560:563	arg1	Asn109	GP73		Asn109, Asn144 and Asn398		PUBTATOR	AminoAcid	GP73	51280	Asn109, Asn144 and Asn398	We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398.
26993603	3	7	part_of	GP73	560:563	arg1	Asn109	GP73		Asn109, Asn144 and Asn398		PUBTATOR	AminoAcid	GP73	51280	Asn109, Asn144 and Asn398	We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398.
1533633	10	7	gly	unglycosylated	1484:1497	arg1	The unglycosylated protein	The unglycosylated protein				Fterm		protein			The unglycosylated protein was trapped in the lumen of the endoplasmic reticulum and was found in a complex with the Ig heavy chain-binding protein, BiP.
22579623	4	5	part_of	sites	697:701	arg1	TLR3ecd at sites	TLR3		sites		PUBTATOR	Site	TLR3	7098	sites	In contrast, Fab12 and Fab1068 bind TLR3ecd at sites distinct from the N- and C-terminal regions that interact with dsRNA and do not inhibit minimal SU formation with short dsRNA.
22579623	4	9	part_of	TLR3ecd	686:692	arg1	TLR3ecd at sites	TLR3		TLR3ecd at sites		PUBTATOR	Site	TLR3	7098	sites	In contrast, Fab12 and Fab1068 bind TLR3ecd at sites distinct from the N- and C-terminal regions that interact with dsRNA and do not inhibit minimal SU formation with short dsRNA.
1517205	7	84	gly	linked	1565:1570	arg1	Ser-61 AND a tetrasaccharide			Ser-61	a tetrasaccharide					Ser-61	Moreover, the data on beta-elimination for N-9 and of the fast atom bombardment mass spectrometric analysis on peptide N-3 suggested the presence of a tetrasaccharide linked to Ser-61.
6267033	4	5	gly	O-glycosylation	465:479	arg2	Thr 45			Thr 45						Thr 45	It bears an O-glycosylation site at Thr 45 and an N-glycosidic linkage at Asn 65.
6267033	4	5	gly	O-glycosylation	465:479	arg2	an O-glycosylation site			an O-glycosylation site						site	It bears an O-glycosylation site at Thr 45 and an N-glycosidic linkage at Asn 65.
6267033	4	5	gly	O-glycosylation	465:479	arg2	Asn 65			Asn 65						Asn 65	It bears an O-glycosylation site at Thr 45 and an N-glycosidic linkage at Asn 65.
32155444	4	4	part_of	furin	542:546	arg1	a furin cleavage site	furin		a furin cleavage site		PUBTATOR	Site	furin	5045	site	We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs.
24018687	5	1	gly	N-glycosylation	1239:1253	arg2	a conserved N-glycosylation site			a conserved N-glycosylation site						site	Due to low stability, the steady-state population of functional DDR proteins in the cell surface depends sensitively on its maturation process via post-translational N-glycosylation, which is controlled by the glucose supply and the presence of a conserved N-glycosylation site.
24018687	5	51	gly	site	1255:1258	arg1	the glucose supply			site	the glucose supply					site	Due to low stability, the steady-state population of functional DDR proteins in the cell surface depends sensitively on its maturation process via post-translational N-glycosylation, which is controlled by the glucose supply and the presence of a conserved N-glycosylation site.
28011641	6	13	part_of	L-selectin	825:834	arg1	the lectin and EGF domains	L-selectin		the lectin and EGF domains		PUBTATOR	Site	L-selectin	6402	domains	Here we report the structure of the lectin and EGF domains of L-selectin bound to a fucose mimetic; that is, a terminal mannose on an N-glycan attached to a symmetry-related molecule.
28011641	6	32	part_of	EGF	810:812	arg1	the lectin and EGF domains	EGF		the lectin and EGF domains		OGER	Site	EGF	P01133	domains	Here we report the structure of the lectin and EGF domains of L-selectin bound to a fucose mimetic; that is, a terminal mannose on an N-glycan attached to a symmetry-related molecule.
8639509	0	72	gly	B-crystallin	62:73	arg1	Dynamic O-GlcNAcylation	alpha B-crystallin			Dynamic O-GlcNAcylation	OGER		alpha B-crystallin	P02511		Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin.
9023546	2	85	part_of	EGF	331:333	arg1	EGF domains	EGF		EGF domains		OGER	Site	EGF	P01133	domains	The enzyme catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in EGF domains.
22601780	11	2	part_of	EGF	1161:1163	arg1	EGF domain sequences	EGF		EGF domain sequences		OGER	Site	EGF	P01133	sequences	A database search for EGF domain sequences shows that this RGD finger is likely an evolutionary insertion and unique to the EGF domain of Del-1 and its homologue milk fat globule-EGF 8.
22601780	11	11	part_of	Del-1	1277:1281	arg1	the EGF domain	Del-1		the EGF domain		PUBTATOR	Site	Del-1	10085	domain	A database search for EGF domain sequences shows that this RGD finger is likely an evolutionary insertion and unique to the EGF domain of Del-1 and its homologue milk fat globule-EGF 8.
22601780	11	28	part_of	EGF	1263:1265	arg1	the EGF domain	EGF		the EGF domain		OGER	Site	EGF	P01133	domain	A database search for EGF domain sequences shows that this RGD finger is likely an evolutionary insertion and unique to the EGF domain of Del-1 and its homologue milk fat globule-EGF 8.
22601780	11	45	part_of	globule-EGF	1310:1320	arg1	the EGF domain	EGF 8		the EGF domain		OGER	Site	EGF 8	P01133	domain	A database search for EGF domain sequences shows that this RGD finger is likely an evolutionary insertion and unique to the EGF domain of Del-1 and its homologue milk fat globule-EGF 8.
25802287	13	13	gly	glycosite	2250:2258	arg2	the glycosite Asn 171			the glycosite Asn 171						glycosite Asn 171	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	74	gly	glycans	2170:2176	arg1	Asn 563			Asn 563	Asn 563		SpecificSite			Asn 563, Asn 402	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	74	gly	glycans	2170:2176	arg1	Asn 402			Asn 402	Asn 402		SpecificSite			Asn 563, Asn 402	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	74	gly	glycans	2170:2176	arg1	the glycosite Asn 171			the glycosite Asn 171	the glycosite Asn 171		SpecificSite			glycosite Asn 171	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	99	gly	glycans	2092:2098	arg1	Asn 395, 332			Asn 395, 332	Asn 395, 332		SpecificSite			Asn 395, 332, 171	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
17889651	3	4	part_of	TLR1	483:486	arg1	the TLR1 and TLR2 ectodomains	TLR1		the TLR1 and TLR2 ectodomains		PUBTATOR	Site	TLR1	7096	ectodomains	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	3	23	part_of	TLR2	492:495	arg1	the TLR1 and TLR2 ectodomains	TLR2		the TLR1 and TLR2 ectodomains		PUBTATOR	Site	TLR2	7097	ectodomains	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
12659834	2	68	gly	used	532:535	arg2	An N-terminus sequence			An N-terminus sequence						sequence	An N-terminus sequence (Ser5-Ala28) of human interleukin 1 beta (hIL-1 beta) was used as synthetic prosequence of recombinant HBV surface antigen (pre-S), secreted from S. cerevisiae.
29019981	5	37	part_of	Ca2+-blocking	900:912	arg1	the luminal Ca2+-blocking site	Ca2		the luminal Ca2+-blocking site		PUBTATOR	Site	Ca2	12349	site	The tightly packed selectivity filter contains multiple ion-binding sites, and the conserved acidic residues form the luminal Ca2+-blocking site that confers luminal pH and Ca2+ modulation on channel conductance.
22664871	6	7	part_of	RANKL	1168:1172	arg1	important interacting residues	RANKL		important interacting residues		PUBTATOR	Site	RANKL	21943	residues	These results, together with a previously reported mouse RANKL/RANK complex structure, reveal that OPG exerts its decoy receptor function by directly blocking the accessibilities of important interacting residues of RANKL for RANK recognition.
12731890	0	57	gly	glycosylation	20:32	arg1	the epidermal growth factor receptor	epidermal growth factor receptor		sites		PUBTATOR		epidermal growth factor receptor	1956	sites	Characterization of glycosylation sites of the epidermal growth factor receptor.
11279095	3	46	part_of	terminus	606:613	arg1	three cysteines	terminus		three cysteines						cysteines	The members of the ST8Sia gene family, including ST8Sia II and ST8Sia IV are unique in having three cysteines in sialylmotif L, one cysteine in sialylmotif S, and one cysteine at the COOH terminus.
11279095	3	46	part_of	terminus	606:613	arg1	one cysteine			cysteine						cysteine	The members of the ST8Sia gene family, including ST8Sia II and ST8Sia IV are unique in having three cysteines in sialylmotif L, one cysteine in sialylmotif S, and one cysteine at the COOH terminus.
10995228	10	9	part_of	region	1314:1319	arg1	mER-beta	mER		region		PUBTATOR	Site	mER	13983	region	The localization of a major O-GlcNAc/O-phosphate site in proximity of the transactivation domain and as part of a PEST region (target sequences for rapid protein degradation) on mER-beta suggests that these modifications may play a role in regulating estrogen receptor beta transactivation and turnover.
24342833	7	40	gly	Serine	1183:1188	arg1	O-GlcNAcylation			Serine 23	O-GlcNAcylation					Serine 23	SIGNIFICANCE: O-GlcNAcylation of Serine 23 is a novel regulatory modification for β-catenin's subcellular localization and transcriptional activity.
1533633	2	3	part_of	sites	313:317	arg1	the alpha-subunit	subunit		sites		OGER	Site	subunit	P06865	sites	We have identified the sites of N-linked glycosylation and oligosaccharide phosphorylation on the alpha-subunit of beta-hexosaminidase and have determined the influence of the oligosaccharides on the folding and transport of the enzyme.
2668275	12	14	gly	contain	1566:1572	arg1	STS AND mannose 6-phosphate residues	STS			mannose 6-phosphate residues	Cterm		STS	412		In spite of its similarity with these two lysosomal sulfatases, STS does not contain mannose 6-phosphate residues and is transported to lysosomes by a mannose 6-phosphate receptor-independent mechanism.
19528533	6	6	part_of	FXa	1348:1350	arg1	the gamma-carboxy-glutamic acid-containing domains	FXa		the gamma-carboxy-glutamic acid-containing domains		PUBTATOR	Site	FXa	2159	domains	As modeled in this study, the gamma-carboxy-glutamic acid-containing domains of PZ and FXa enable them to bind to the same phospholipid surfaces on platelet and other membranes, with optimal proximity for the inhibition of FXa by the complexed ZPI.
22171320	2	104	gly	glycoproteins	394:406	arg1	urinary glycoproteins	glycoproteins			glycan structures	Fterm		glycoproteins			Previous proteomic studies have identified more than 2800 urinary proteins but analyses aimed at unraveling glycan structures and glycosylation sites of urinary glycoproteins are lacking.
22171320	2	113	gly	glycosylation	363:375	arg1	urinary glycoproteins	glycoproteins		sites		Fterm		glycoproteins		sites	Previous proteomic studies have identified more than 2800 urinary proteins but analyses aimed at unraveling glycan structures and glycosylation sites of urinary glycoproteins are lacking.
12438562	1	24	part_of	sites	130:134	arg1	proteins	proteins		sites		Fterm	Site	proteins		sites	Identifying sites of post-translational modifications on proteins is a major challenge in proteomics.
23527852	9	4	gly	fucosylated	1205:1215	arg1	the fucosylated isoforms				the fucosylated isoforms						A large variation in the presence and abundance of the fucosylated isoforms was found in a set of 96 serum samples.
6619128	12	7	gly	sialylated	1506:1515	arg1	the sialylated structures				the sialylated structures						Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
25092234	4	24	gly	A2	740:741	arg1	complex biantennary mono-α2,6-sialylated (A2 S1 , 20%) and bis-α2,6-sialylated structures			A2-S2	complex biantennary mono-α2,6-sialylated (A2 S1 , 20%) and bis-α2,6-sialylated structures					A2-S2	Hydrophilic interaction LC and MS characterization and quantification of the N-glycans showed that the two major forms are complex biantennary mono-α2,6-sialylated (A2 S1 , 20%) and bis-α2,6-sialylated structures (A2 S2 , 66%).
25092234	4	15	gly	mono-α2,6-sialylated	669:688	arg1	A2 S2			A2-S2	complex biantennary mono-α2,6-sialylated (A2 S1 , 20%) and bis-α2,6-sialylated structures					A2-S2	Hydrophilic interaction LC and MS characterization and quantification of the N-glycans showed that the two major forms are complex biantennary mono-α2,6-sialylated (A2 S1 , 20%) and bis-α2,6-sialylated structures (A2 S2 , 66%).
25092234	4	66	gly	bis-α2,6-sialylated	708:726	arg1	A2 S2			A2-S2	complex biantennary mono-α2,6-sialylated (A2 S1 , 20%) and bis-α2,6-sialylated structures					A2-S2	Hydrophilic interaction LC and MS characterization and quantification of the N-glycans showed that the two major forms are complex biantennary mono-α2,6-sialylated (A2 S1 , 20%) and bis-α2,6-sialylated structures (A2 S2 , 66%).
15532026	9	14	part_of	site	1591:1594	arg1	the gamma subunit	subunit		site		OGER	Site	subunit	Q9UJJ9	site	These data suggest that the loss of the used glycosylation site in the gamma subunit may affect the intracellular localization of GNPTAG and the overall efficiency of M6P formation.
22333914	3	16	part_of	overall	698:704	arg1	the overall GAIN domain	l GAIN		the overall GAIN domain		PUBTATOR	Site	l GAIN	23218	domain	Crystal structures of GAIN domains from two distantly related cell-adhesion GPCRs revealed a conserved novel fold in which the GPS motif forms five β-strands that are tightly integrated into the overall GAIN domain.
22333914	3	21	part_of	GAIN	706:709	arg1	the overall GAIN domain	l GAIN		the overall GAIN domain		PUBTATOR	Site	l GAIN	23218	domain	Crystal structures of GAIN domains from two distantly related cell-adhesion GPCRs revealed a conserved novel fold in which the GPS motif forms five β-strands that are tightly integrated into the overall GAIN domain.
22333914	3	44	part_of	GPS	630:632	arg1	the GPS motif	GPS		the GPS motif		OGER	Site	GPS		motif	Crystal structures of GAIN domains from two distantly related cell-adhesion GPCRs revealed a conserved novel fold in which the GPS motif forms five β-strands that are tightly integrated into the overall GAIN domain.
20571061	1	6	gly	N-glycosylation	240:254	arg2	the sites			the sites						sites	Despite increasing importance of protein glycosylation, most of the large-scale glycoproteomics have been limited to profiling the sites of N-glycosylation.
20147294	7	69	gly	glycosylation	906:918	arg1	a signal peptide	ADA2		peptide		PUBTATOR		ADA2	51816	peptide	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
16186819	4	22	part_of	THBS2	533:537	arg1	The THBS2 signature domain	THBS2		The THBS2 signature domain		PUBTATOR	Site	THBS2	7058	domain	The THBS2 signature domain is stabilized by these interactions and by a network of 30 bound Ca(2+) ions and 18 disulfide bonds.
2226832	4	28	gly	glycosylated	480:491	arg2	all three sites			all three sites						sites	Some species of CAP37 are glycosylated at all three sites; some at Asn-114 alone, others at Asn-114 and Asn-110 or Asn-145.
2226832	4	35	gly	sites	506:510	arg1	Asn-145			Asn-145						Asn-145	Some species of CAP37 are glycosylated at all three sites; some at Asn-114 alone, others at Asn-114 and Asn-110 or Asn-145.
25187573	1	2	gly	glycoprotein	186:197	arg1	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin				Fterm		glycoprotein			The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin has previously been observed to contain glycosylation changes related to rheumatoid and osteoarthritis.
28279966	8	16	part_of	Tyr1605-Met1606	1218:1232	arg1	the Tyr1605-Met1606 ADAMTS13 proteolytic site	Tyr1605-Met1606 ADAMTS13		the Tyr1605-Met1606 ADAMTS13 proteolytic site		PUBTATOR	Site	Tyr1605-Met1606 ADAMTS13	11093	site	Although both plasmin and ADAMTS13 cleave VWF in a shear-dependent manner, plasmin does not cleave at the Tyr1605-Met1606 ADAMTS13 proteolytic site in the A2 domain.
28279966	8	41	part_of	ADAMTS13	1234:1241	arg1	the Tyr1605-Met1606 ADAMTS13 proteolytic site	Tyr1605-Met1606 ADAMTS13		the Tyr1605-Met1606 ADAMTS13 proteolytic site		PUBTATOR	Site	Tyr1605-Met1606 ADAMTS13	11093	site	Although both plasmin and ADAMTS13 cleave VWF in a shear-dependent manner, plasmin does not cleave at the Tyr1605-Met1606 ADAMTS13 proteolytic site in the A2 domain.
27462106	2	62	gly	glycoproteins	301:313	arg1	host glycoproteins	host glycoproteins				Fterm		glycoproteins			This dependency exceeds the dependency of host glycoproteins, offering a window for the targeting of ERQC for the development of broad-spectrum antivirals.
23376777	5	65	gly	glycosylation	938:950	arg2	the central two (N331/344/Q) N-linked glycosylation sites			the central two (N331/344/Q) N-linked glycosylation sites						sites	Further investigation indicated that mutations of the central two (N331/344/Q) N-linked glycosylation sites inhibit the membrane trafficking of KCC4.
14711516	6	6	part_of	Thy-1	1015:1019	arg1	asparagine 60	Recombinant Thy-1		asparagine 60		PUBTATOR	SpecificSite	Recombinant Thy-1	P04216	asparagine 60	Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5).
6510521	0	42	part_of	hemopexin	54:62	arg1	the N-terminal region	hemopexin		the N-terminal region		PUBTATOR	Site	hemopexin	3263	region	Amino acid sequence of the N-terminal region of human hemopexin.
18491227	0	34	gly	Unglycosylation	0:14	arg2	Asn-633			Asn-633						Asn-633	Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD.
26791533	5	12	gly	glycoproteins	717:729	arg1	the glycoproteins	the glycoproteins				Fterm		glycoproteins			This analysis provides identification of the glycoproteins, glycosylation sites, glycan compositions, and proposed structures from the original sample.
26791533	5	41	gly	glycosylation	732:744	arg2	glycosylation sites			glycosylation sites						sites	This analysis provides identification of the glycoproteins, glycosylation sites, glycan compositions, and proposed structures from the original sample.
2013294	6	17	gly	Asn77	623:627	arg1	A single N-glycosidic carbohydrate moiety			Asn77	A single N-glycosidic carbohydrate moiety					Asn77	A single N-glycosidic carbohydrate moiety is located at Asn77.
2013294	6	29	gly	located	612:618	arg1	Asn77 AND A single N-glycosidic carbohydrate moiety			Asn77	A single N-glycosidic carbohydrate moiety					Asn77	A single N-glycosidic carbohydrate moiety is located at Asn77.
7240157	2	35	gly	monofucosylated	298:312	arg1	a monofucosylated tetra-antennary glycopeptide fraction				a monofucosylated tetra-antennary glycopeptide fraction						Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	2	45	gly	derived	362:368	arg1	human plasma alpha 1-acid glycoprotein AND a monofucosylated tetra-antennary glycopeptide fraction	human plasma alpha 1-acid glycoprotein			a monofucosylated tetra-antennary glycopeptide fraction	Fterm		glycoprotein			Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	2	57	gly	glycoprotein	401:412	arg1	human plasma alpha 1-acid glycoprotein	human plasma alpha 1-acid glycoprotein				Fterm		glycoprotein			Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
29391424	2	51	gly	glycopeptide	239:250	arg2	intact glycopeptide mass spectra			intact glycopeptide mass spectra						glycopeptide	We present an approach for automated annotation of intact glycopeptide mass spectra.
1904059	1	109	gly	O-glycosylations	61:76	arg2	O-glycosylations at serine residues 52 and 60			O-glycosylations at serine residues 52 and 60						serine residues 52 and 60	Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine.
1904059	1	33	gly	residues	88:95	arg1	60			serine residues 52 and 60						serine residues 52 and 60	Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine.
20450227	10	24	part_of	P2X	1811:1813	arg1	human P2X(7) glycosylation sites	P2X(		human P2X(7) glycosylation sites		PUBTATOR	Site	P2X(	5027	sites	This is the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function.
15331613	1	48	gly	glycosylation	496:508	arg1	NGC	NGC				PUBTATOR		NGC	29873		NGC dramatically changed its structure from a proteoglycan to a nonproteoglycan form with cerebellar development, whereas a small portion of NGC molecules existed in a nonproteoglycan form in the other areas of the mature CNS, suggesting that the CS glycosylation of NGC is developmentally regulated in the whole CNS.
16040958	7	13	gly	Asn	1499:1501	arg1	the N-linked carbohydrate			Asn(3)	the N-linked carbohydrate					Asn(3)	Therefore, the interaction of C1INH with gram-negative bacterial LPS is dependent both on the N-linked carbohydrate at Asn(3) and on the positively charged residues within the amino-terminal domain.
15173186	0	74	part_of	sites	28:32	arg1	human toll-like receptor 2	toll-like receptor 2		sites		PUBTATOR	Site	toll-like receptor 2	7097	sites	Four N-linked glycosylation sites in human toll-like receptor 2 cooperate to direct efficient biosynthesis and secretion.
22041449	3	13	part_of	laminin	509:515	arg1	three laminin epidermal growth factor-like (LE) domains	laminin		three laminin epidermal growth factor-like (LE) domains		OGER	Site	laminin		domains	Netrin G proteins share a common multi-domain architecture comprising a laminin N-terminal (LN) domain followed by three laminin epidermal growth factor-like (LE) domains and a C' region containing a glycosylphosphatidylinositol anchor.
22041449	3	32	part_of	laminin	460:466	arg1	a laminin N-terminal (LN) domain	laminin		a laminin N-terminal (LN) domain		OGER	Site	laminin		domain	Netrin G proteins share a common multi-domain architecture comprising a laminin N-terminal (LN) domain followed by three laminin epidermal growth factor-like (LE) domains and a C' region containing a glycosylphosphatidylinositol anchor.
26598643	14	93	gly	disialylated	2049:2060	arg1	core-1 mucin-type O-glycans				core-1 mucin-type O-glycans						The identified O-glycan compositions most probably correspond to mono- and disialylated core-1 mucin-type O-glycans (T-antigen).
21712440	9	62	gly	sialylated	1687:1696	arg1	sialylated O-glycans				sialylated O-glycans						APP/Aβ sialylated O-glycans, including that of a Tyr residue, the first in a mammalian protein, may modulate APP processing, inhibiting the amyloidogenic pathway associated with AD.
2277032	3	52	part_of	enzyme	572:577	arg1	the 27th residue	enzyme		the 27th residue		Fterm	Site	enzyme		residue	The N-terminal amino acid sequence up to the 27th residue of the enzyme was similar to that of pancreatic deoxyribonuclease I from bovine and other species.
8639592	5	75	gly	O-glycosylated	877:890	arg1	Thr175			Thr175						Thr175	Thr175 was also fully O-glycosylated, but Ser174 was partially O-glycosylated.
8639592	5	100	gly	O-glycosylated	918:931	arg1	Ser174			Ser174						Ser174	Thr175 was also fully O-glycosylated, but Ser174 was partially O-glycosylated.
27175940	4	39	gly	Ser2	796:799	arg1	O-GlcNAcylation			Ser2	O-GlcNAcylation					Ser2	In addition, O-GlcNAcylation at Ser2 suppressed Cyclin/CDK complex-p27 interactions by promoting the nuclear export of p27, thus facilitating cell cycle progression.
7106126	4	25	gly	glycopeptide	668:679	arg2	the glycopeptide			the glycopeptide						glycopeptide	An identical hexapeptide sequence occurring in two regions of the glycopeptide provides evidence that it has developed by an internal gene duplication during evolution.
23959878	5	21	gly	attached	879:886	arg1	N372 AND the N-glycan			N372	the N-glycan					N372	A deglycosylation study showed that enzyme activity was highly correlated with the N-glycan attached to N372.
16037490	1	68	gly	glycopeptides	171:183	arg2	glycopeptides			glycopeptides						glycopeptides	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	1	65	gly	glycoproteins	360:372	arg1	oligosaccharides	glycoproteins			oligosaccharides	Fterm		glycoproteins			Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
22688517	4	16	gly	N-glycosylation	549:563	arg2	N-glycosylation sites			N-glycosylation sites						sites	The present study was aimed at elucidating the N-glycosylation of recombinant human LOX-1 with regard to N-glycan profile and N-glycosylation sites.
22688517	4	43	gly	N-glycosylation	470:484	arg1	recombinant human LOX-1	recombinant human LOX-1				PUBTATOR		LOX-1	4973		The present study was aimed at elucidating the N-glycosylation of recombinant human LOX-1 with regard to N-glycan profile and N-glycosylation sites.
20489211	8	33	part_of	receptors	1330:1338	arg1	the membrane-proximal fibronectin type III domains	receptors		the membrane-proximal fibronectin type III domains		Fterm	Site	receptors		domains	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	8	52	part_of	fibronectin	1280:1290	arg1	the membrane-proximal fibronectin type III domains	fibronectin		the membrane-proximal fibronectin type III domains		PUBTATOR	Site	fibronectin	2335	domains	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
21569239	9	26	part_of	F-spondin	1224:1232	arg1	the F-spondin FS domain	structure of the F-spondin		the F-spondin FS domain		PUBTATOR	Site	structure of the F-spondin	10418	domain	CONCLUSION: The structure of the F-spondin FS domain completes the structural studies of the multiple-domain ECM molecule.
20571061	6	10	gly	glycopeptides	1207:1219	arg2	25 targeted glycopeptides	proteins		glycopeptides		Fterm		proteins		glycopeptides	Versatility of the reverse glycoblotting-assisted MRM assays was demonstrated by quantitative comparison of 25 targeted glycopeptides from 16 proteins between mice with homo and hetero types of diabetes disease model.
11372680	5	66	part_of	ZPI	736:738	arg1	The oligonucleotide and predicted amino acid sequences	ZPI		The oligonucleotide and predicted amino acid sequences		PUBTATOR	Site	ZPI	217847	sequences	The oligonucleotide and predicted amino acid sequences of mouse ZPI are 72% and 81% homologous with those of human ZPI.
22750213	7	6	gly	glycoproteins	1167:1179	arg1	membrane glycoproteins	membrane glycoproteins				Fterm		glycoproteins			This result is contrary to the reports that glycosylation is essential for conformation and trafficking of membrane glycoproteins.
22750213	7	48	gly	glycosylation	1095:1107	arg1	membrane glycoproteins	membrane glycoproteins				Fterm		glycoproteins			This result is contrary to the reports that glycosylation is essential for conformation and trafficking of membrane glycoproteins.
3521732	8	53	part_of	single-chain	1016:1027	arg1	a single-chain polypeptide	chain		a single-chain polypeptide		OGER	Site	chain	3818	polypeptide	The mature form of the protein that circulates in blood is a single-chain polypeptide of 619 amino acids.
1694784	8	24	gly	HC	1098:1099	arg1	the carbohydrate composition	protein HC			the carbohydrate composition	PUBTATOR		protein HC	259		No difference was found between the carbohydrate composition of urinary and plasma protein HC.
26828122	4	13	gly	glycoprotein	953:964	arg1	the hTPPT protein	the hTPPT protein				PUBTATOR		hTPPT protein	80736		Using several approaches including inhibiting de novo N-glycosylation in human colonic epithelial NCM460 cells with tunicamycin as well as enzymatic de-glycosylation, we show that the hTPPT protein is, indeed, a glycoprotein.
26828122	4	13	gly	glycoprotein	953:964	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Using several approaches including inhibiting de novo N-glycosylation in human colonic epithelial NCM460 cells with tunicamycin as well as enzymatic de-glycosylation, we show that the hTPPT protein is, indeed, a glycoprotein.
3202829	1	71	gly	glycopeptides	226:238	arg2	glycopeptides			glycopeptides						glycopeptides	The major secretory ribonuclease (RNase) of human urine (RNase HUA) was isolated and sequenced by automatic Edman degradation and analysis of peptides and glycopeptides.
15616124	11	65	gly	glycoproteins	1782:1794	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Thus, the present study demonstrates that posttranslational N-glycosylation can be a part of the normal processing of glycoproteins.
22664871	5	14	part_of	OPG-CRD	774:780	arg1	the CRD3 domain	OPG		the CRD3 domain		PUBTATOR	Site	OPG	4982	domain	A loop from the CRD3 domain of OPG-CRD inserts into the shallow groove of RANKL, providing the major binding determinant that is further confirmed by affinity measurement and osteoclast differentiation assay.
19139490	5	53	gly	glycopeptides	836:848	arg2	CF glycopeptides			CF glycopeptides						glycopeptides	The rationale for spectrum treatment was innovatively based on computation of the mass distribution in spectra of CF glycopeptides.
7681597	1	47	gly	glycopeptides	251:263	arg2	the glycopeptides			the glycopeptides						glycopeptides	Glycophorin A was digested with glycoprotease (Pasteurella haemolytica) and the digest was fractionated by a combination of high-pressure column chromatographies to produce the glycopeptides GPA-1 to GPA-6.
24308486	6	48	gly	contained	1056:1064	arg1	sites Asn21, Asn49, Asn99, Asn146, and Asn252 AND complex-type glycans			sites Asn21, Asn49, Asn99, Asn146, and Asn252	complex-type glycans					sites Asn21, Asn49, Asn99, Asn146, and Asn252	In all three samples, site Asn275 contained exclusively oligomannosidic structures with between 2 and 9 mannoses, whereas sites Asn21, Asn49, Asn99, Asn146, and Asn252 contained exclusively complex-type glycans.
12297049	2	45	part_of	EGFR	290:293	arg1	both L1 and L2 domains	EGFR		both L1 and L2 domains		PUBTATOR	Site	EGFR	1956	domains	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
18596036	3	13	part_of	MASP-1/3	449:456	arg1	the CUB(1)-EGF-CUB(2) domain	MASP-1/3		the CUB(1)-EGF-CUB(2) domain		PUBTATOR	Site	MASP-1/3	5648	domain	The x-ray structure of the CUB(1)-EGF-CUB(2) domain of human MASP-1/3, responsible for interaction of MASP-1 and -3 with their partner proteins mannan-binding lectin (MBL) and ficolins, was solved to a resolution of 2.3A(.)
18596036	3	42	part_of	-EGF-CUB	421:428	arg1	the CUB(1)-EGF-CUB(2) domain	EGF		the CUB(1)-EGF-CUB(2) domain		OGER	Site	EGF	P01133	domain	The x-ray structure of the CUB(1)-EGF-CUB(2) domain of human MASP-1/3, responsible for interaction of MASP-1 and -3 with their partner proteins mannan-binding lectin (MBL) and ficolins, was solved to a resolution of 2.3A(.)
7306483	4	27	part_of	terminus	500:507	arg1	basic residues	terminus		basic residues						residues at	This region was composed of 39 amino acid residues with a cluster of basic residues at the NH2 terminus and localized positions 308-346 of the H-2Kb molecule.
20068230	9	5	gly	proteins	1509:1516	arg1	O-GlcNAcylation	proteins			O-GlcNAcylation	Fterm		proteins			The data not only illustrate the crosstalk between O-GlcNAcylation and phosphorylation of proteins that are regulators of crucial signaling pathways but also uncover a mechanism for the role of O-GlcNAcylation in regulation of cell division.
16422668	11	43	part_of	Yvo	1629:1631	arg1	the Yvo antigen-binding site	Yvo		the Yvo antigen-binding site		Cterm	Site	Yvo	P01871	site	An atypical serine, arginine and glutamate motif is located in the middle of the Yvo antigen-binding site and displays an overall geometry that mimics the classical serine, histidine and aspartate catalytic triad of serine proteases.
21932778	3	93	gly	N-glycosylation	446:460	arg2	the possible N-glycosylation sites			the possible N-glycosylation sites						sites	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	3	93	gly	N-glycosylation	446:460	arg2	Asn-79			Asn-79 and Asn-116						Asn-79 and Asn-116	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
7460900	4	38	gly	caseinoglycopeptide	685:703	arg2	human caseinoglycopeptide			caseinoglycopeptide	the sugar level					caseinoglycopeptide	A significant microheterogeneity seems to occur at the sugar level of human caseinoglycopeptide, which might thus present differences from one milk to another.
9677337	4	19	gly	linked	735:740	arg2	asparagine residues AND predominantly biantennary structure			asparagine residues	predominantly biantennary structure					asparagine residues at positions 256 and 559	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
9677337	4	13	gly	positions	768:776	arg1	256			asparagine residues at positions 256 and 559						asparagine residues at positions 256 and 559	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
2129367	9	4	gly	-Glc-Ser	1241:1248	arg1	a (Xyl2)-Glc-Ser structure			Ser	a (Xyl2)-Glc-Ser structure					Ser	This is the first report of a (Xyl2)-Glc-Ser structure in glycoproteins to our knowledge.
2129367	9	17	gly	glycoproteins	1263:1275	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			This is the first report of a (Xyl2)-Glc-Ser structure in glycoproteins to our knowledge.
2129367	9	41	gly	structure	1250:1258	arg1	glycoproteins	glycoproteins			structure	Fterm		glycoproteins			This is the first report of a (Xyl2)-Glc-Ser structure in glycoproteins to our knowledge.
12654314	0	14	gly	M	91:91	arg1	the N-linked oligosaccharides	immunoglobulin M			the N-linked oligosaccharides	OGER		immunoglobulin M	P01872		Site-specific characterization of the N-linked oligosaccharides of a murine immunoglobulin M by high-performance liquid chromatography/electrospray mass spectrometry.
7106126	0	45	part_of	D	52:52	arg1	N-terminal amino acid sequence	sialoglycoprotein D		N-terminal amino acid sequence		PUBTATOR	Site	sialoglycoprotein D	2995	sequence	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
8404899	11	72	gly	variants	1815:1822	arg1	sugar	variants			sugar	Fterm		variants			The amount of sugar involved in the O-linked oligosaccharide structure appears to be unchanged in the variants isolated from the pathological pancreatic juice.
19139490	8	26	gly	glycopeptides	1342:1354	arg2	glycopeptides			glycopeptides						glycopeptides	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
7841792	4	51	gly	glycosylated	705:716	arg1	glycosylated PTH-Asn	glycosylated PTH-Asn				PUBTATOR	AminoAcid	PTH	5741		Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	4	18	gly	glycopeptide	653:664	arg1	a mutant human albumin Casebrook	albumin Casebrook		glycopeptide		OGER		albumin Casebrook	P02768	glycopeptide	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
11567096	8	20	gly	glycosylated	1419:1430	arg1	all Asn residues			all Asn residues						Asn residues	Of all putative N-glycosylation sites in positions 32, 38, 45, 78, 90, and 98, all Asn residues except for Asn(32) were glycosylated to a significant extent.
11567096	8	40	gly	N-glycosylation	1315:1329	arg2	all putative N-glycosylation sites			all putative N-glycosylation sites						sites	Of all putative N-glycosylation sites in positions 32, 38, 45, 78, 90, and 98, all Asn residues except for Asn(32) were glycosylated to a significant extent.
24766575	4	0	gly	glycopeptide	920:931	arg2	glycopeptide profiling			glycopeptide profiling						glycopeptide	The results revealed a similar level of glycan microheterogeneity to that of conventional glycomics approach on individual proteins and provided the unique in-depth site-specific information that could only be studied through glycopeptide profiling.
19664639	0	11	part_of	MuSK	92:95	arg1	the frizzled-like cysteine-rich domain	MuSK		the frizzled-like cysteine-rich domain		OGER	Site	MuSK	O15146	domain	Crystal structure of the frizzled-like cysteine-rich domain of the receptor tyrosine kinase MuSK.
3484330	6	4	part_of	protein	978:984	arg1	the core protein sequence	protein		the core protein sequence		Fterm	Site	protein		sequence	A protein data base homology search established the core protein sequence is a unique sequence distinct from published amino acid sequences.
3484330	6	57	part_of	protein	923:929	arg1	a unique sequence	protein		a unique sequence		Fterm	Site	protein		sequence	A protein data base homology search established the core protein sequence is a unique sequence distinct from published amino acid sequences.
19349973	2	7	gly	glycosylation	460:472	arg2	several hundred N-linked glycosylation sites			several hundred N-linked glycosylation sites						sites	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	2	60	gly	glycoproteins	519:531	arg1	cell surface-exposed glycoproteins	cell surface-exposed glycoproteins				Fterm		glycoproteins			We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
12408961	7	27	gly	glycoproteins	1055:1067	arg1	putative secreted glycoproteins	putative secreted glycoproteins				Fterm		glycoproteins			Thus, human and mouse CREG2 are putative secreted glycoproteins and may be novel neuronal extracellular molecules.
23139753	8	6	gly	N-glycosylated	886:899	arg1	HE-4	HE-4				PUBTATOR		HE-4	10406		Moreover, HE-4 is N-glycosylated and highly stable on a wide range of pH and temperature.
23829323	0	51	gly	glycopeptide	80:91	arg2	glycopeptide CID tandem mass spectra			glycopeptide CID tandem mass spectra						glycopeptide	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	0	63	gly	microheterogeneity	40:57	arg1	haptoglobin	haptoglobin				PUBTATOR		haptoglobin	3240		Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	0	104	gly	N-glycosylation	24:38	arg1	haptoglobin	haptoglobin				PUBTATOR		haptoglobin	3240		Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
1323463	0	43	gly	mucin	143:147	arg1	the acidic O-linked carbohydrate chains	mucin			the acidic O-linked carbohydrate chains	PUBTATOR		mucin	281333		Characterisation by mass spectrometry and 1H-NMR of novel hexasaccharides among the acidic O-linked carbohydrate chains of bovine submaxillary mucin.
1908233	1	7	gly	glycopeptides	254:266	arg2	covalently linked glycopeptides			covalently linked glycopeptides						glycopeptides	Here we report the use of automated Edman degradation of covalently linked glycopeptides to identify positively the sites of O- and N-glycosylation.
1908233	1	45	gly	N-glycosylation	311:325	arg2	the sites			the sites						sites	Here we report the use of automated Edman degradation of covalently linked glycopeptides to identify positively the sites of O- and N-glycosylation.
14660577	7	34	gly	glycoprotein	1117:1128	arg1	a monomeric glycoprotein	a monomeric glycoprotein				Fterm		glycoprotein			The structure shows a monomeric glycoprotein with a topology similar to that of other mammalian CA isozymes.
2983222	1	12	part_of	precursor	171:179	arg1	the entire 1,370-amino-acid sequence	precursor		the entire 1,370-amino-acid sequence		Fterm	Site	precursor		sequence	We have deduced the entire 1,370-amino-acid sequence of the human insulin receptor precursor from a single complementary DNA clone.
10677208	5	10	gly	fucosylated	975:985	arg1	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose				the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose						Sf9 cells mainly processed the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose, although hybrid and complex N-glycosylations were also detected.
12944413	9	34	gly	sialylated	1556:1565	arg1	sialylated N-glycans				sialylated N-glycans						We propose that sialylated N-glycans provide a favorable conformation to SERT that allows the transporter to function most efficiently via its protein-protein interactions.
17542669	10	53	gly	glycoprotein	1734:1745	arg1	glycoprotein hormone receptor activation	glycoprotein hormone receptor activation				Fterm		glycoprotein			Furthermore, our structure of the TSHR and its complex with M22 provide foundations for developing new strategies to understand and control both glycoprotein hormone receptor activation and the autoimmune response to the TSHR.
8639592	0	97	part_of	inhibitor	92:100	arg1	Amino acid sequence	tissue factor pathway inhibitor		Amino acid sequence		PUBTATOR	Site	tissue factor pathway inhibitor	7035	sequence	Amino acid sequence and carbohydrate structure of a recombinant human tissue factor pathway inhibitor expressed in Chinese hamster ovary cells: one N-and two O-linked carbohydrate chains are located between Kunitz domains 2 and 3 and one N-linked carbohydrate chain is in Kunitz domain 2.
11226831	9	28	gly	glycopeptides	812:824	arg2	glycopeptides			glycopeptides						glycopeptides	Analyses of glycopeptides identified two additional sites of modification on mER-alpha, at Ser(10) and Thr(50) near the N-terminus.
26828122	3	3	gly	N-glycosylation	576:590	arg2	putative N-glycosylation sites			putative N-glycosylation sites						sites	The hTPPT protein is predicted to have multiple TM domains with a number of putative N-glycosylation sites, but it is not known if the protein is actually glycosylated, and if so at which site, and their role in the functionality of the transporter.
26828122	3	34	gly	glycosylated	646:657	arg1	the protein	the protein				Fterm		protein			The hTPPT protein is predicted to have multiple TM domains with a number of putative N-glycosylation sites, but it is not known if the protein is actually glycosylated, and if so at which site, and their role in the functionality of the transporter.
23209641	5	24	part_of	residues	1179:1186	arg1	adiponectin	adiponectin		residues		PUBTATOR	AminoAcid	adiponectin	Q15848	lysine residues	Circulating adiponectin levels in mutant mice lacking the lysyl hydroxylase activity of LH3 were significantly reduced, which indicates that LH3 is required for complete modification of lysine residues in adiponectin and the loss of some of the glycosylated hydroxylysine residues severely affects the secretion of adiponectin.
15522226	2	47	gly	glycoprotein	243:254	arg1	The WFS1 protein	The WFS1 protein				PUBTATOR		WFS1 protein	22393		The WFS1 protein is a glycoprotein located in the endoplasmic reticulum (ER) membrane but its function is poorly understood.
15522226	2	47	gly	glycoprotein	243:254	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			The WFS1 protein is a glycoprotein located in the endoplasmic reticulum (ER) membrane but its function is poorly understood.
8349699	9	70	gly	Glycosylation	1267:1279	arg1	PGH synthase-2	PGH synthase-2				PUBTATOR		PGH synthase-2	19225		Glycosylation of PGH synthase-2 is necessary for expression of enzyme activity, but glycosylation of PGH synthase-2 at Asn580 per se does not affect activity.
8349699	9	31	gly	glycosylation	1351:1363	arg1	Asn580			Asn580						Asn580	Glycosylation of PGH synthase-2 is necessary for expression of enzyme activity, but glycosylation of PGH synthase-2 at Asn580 per se does not affect activity.
8349699	9	31	gly	glycosylation	1351:1363	arg1	PGH synthase-2	PGH synthase-2		Asn580		PUBTATOR		PGH synthase-2	19225	Asn580	Glycosylation of PGH synthase-2 is necessary for expression of enzyme activity, but glycosylation of PGH synthase-2 at Asn580 per se does not affect activity.
8349699	9	31	gly	glycosylation	1351:1363	arg1	PGH synthase-2	PGH synthase-2		Asn580		PUBTATOR		PGH synthase-2	19225	Asn580	Glycosylation of PGH synthase-2 is necessary for expression of enzyme activity, but glycosylation of PGH synthase-2 at Asn580 per se does not affect activity.
28531887	11	35	gly	N-glycosylation	1425:1439	arg2	the single N-glycosylation site	MT4-MMP		site		PUBTATOR		MT4-MMP	4326	site	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	11	35	gly	N-glycosylation	1425:1439	arg2	Asn318	MT4-MMP		Asn318		PUBTATOR		MT4-MMP	4326	Asn318	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
6587378	1	40	part_of	2-glycoprotein	128:141	arg1	the complete amino acid sequence	beta 2-glycoprotein I		the complete amino acid sequence		OGER	Site	beta 2-glycoprotein I	P02749	sequence	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
29671580	5	19	gly	glycosites	909:918	arg2	two novel atypical glycosites			two novel atypical glycosites						glycosites	In addition, two novel atypical glycosites (with N-X-V motif) were identified and validated from albumin and α-1B-glycoprotein.
29671580	5	30	gly	α-1B-glycoprotein	986:1002	arg1	α-1B-glycoprotein	α-1B-glycoprotein				PUBTATOR		-1B-glycoprotein	1		In addition, two novel atypical glycosites (with N-X-V motif) were identified and validated from albumin and α-1B-glycoprotein.
22040171	2	33	part_of	NAAA	322:325	arg1	the NAAA pro-enzyme	NAAA		the NAAA pro-enzyme		PUBTATOR	AminoAcid	NAAA	27163	pro	We developed a HEK293 cell line stably expressing the NAAA pro-enzyme (zymogen) and a single step chromatographic purification of the protein from the media.
7681597	2	1	gly	glycosylated	382:393	arg1	two serine residues			two serine residues						serine residues	Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure.
7681597	2	20	gly	residues	345:352	arg1	two serine residues			two serine residues						serine residues	Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure.
7681597	2	46	gly	glycosylated	420:431	arg1	two serine residues			two serine residues						serine residues	Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure.
7681597	2	54	gly	glycopeptides	306:318	arg2	the glycopeptides			the glycopeptides						glycopeptides	Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure.
7681597	2	1	gly	glycosylated	382:393	arg1	Ser-14			Ser-14 and Ser-15						Ser-14 and Ser-15	Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure.
7681597	2	20	gly	residues	345:352	arg1	Ser-14			Ser-14 and Ser-15						Ser-14 and Ser-15	Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure.
7681597	2	46	gly	glycosylated	420:431	arg1	Thr-17			Thr-17 and Ser-19						Thr-17 and Ser-19	Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure.
7681597	2	46	gly	glycosylated	420:431	arg1	Ser-14			Ser-14 and Ser-15						Ser-14 and Ser-15	Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure.
2386787	3	18	gly	glycosylation	895:907	arg1	the insect cell expressed recombinant human plasminogen	the insect cell expressed recombinant human plasminogen				OGER		plasminogen	P00747		The glycosylation pattern of the insect cell expressed recombinant human plasminogen showed considerable microheterogeneity, with identifiable high-mannose carbohydrate (Man9GlcNAc2) and truncated high-mannose oligosaccharide (Man5GlcNAc2, Man4GlcNAc2, and Man3GlcNAc2).
20450227	0	70	gly	glycosylation	30:42	arg2	putative N-linked glycosylation sites			putative N-linked glycosylation sites						sites	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
11168369	6	41	part_of	variant	1178:1184	arg1	the four additional cysteine residues	variant		the four additional cysteine residues		Fterm	AminoAcid	variant		cysteine residues	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
10712595	3	110	part_of	antithrombin	473:484	arg1	Asn135	antithrombin		Asn135		PUBTATOR	AminoAcid	antithrombin	462	Asn135	Due to a single nucleotide replacement, Asn135 of the antithrombin in higher vertebrates is substituted by Asp in the salmon homolog.
7686446	5	41	gly	isoform	1527:1533	arg1	the sugar chain structure	AFP isoform			the sugar chain structure	PUBTATOR		AFP isoform	174		In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	5	122	gly	fucosylation	1610:1621	arg1	the proximal N-acetylglucosamine				the proximal N-acetylglucosamine						In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	5	122	gly	fucosylation	1610:1621	arg1	a monosialyl-biantennary sugar chain				a monosialyl-biantennary sugar chain						In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
10551839	5	2	gly	C-mannosylated	760:773	arg1	the first proteins	the first proteins				Fterm		proteins			These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
11983428	4	55	gly	glycosylation	702:714	arg2	two sites			sites						sites	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	4	60	gly	residues	781:788	arg1	N171			asparagine residues N131 and N171						asparagine residues N131 and N171	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	4	60	gly	residues	781:788	arg1	N131			asparagine residues N131 and N171						asparagine residues N131 and N171	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	4	60	gly	residues	781:788	arg1	N131			asparagine residues N131 and N171						asparagine residues N131 and N171	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
21983541	0	21	gly	leucine-rich	78:89	arg1	neuronal leucine-rich repeat protein AMIGO-1			leucine	neuronal leucine-rich repeat protein AMIGO-1					leucine	Crystal structure and role of glycans and dimerization in folding of neuronal leucine-rich repeat protein AMIGO-1.
15532026	0	42	gly	glycosylation	146:158	arg2	a used glycosylation site			a used glycosylation site						site	A novel mutation in UDP-N-acetylglucosamine-1-phosphotransferase gamma subunit (GNPTAG) in two siblings with mucolipidosis type III alters a used glycosylation site.
12788922	0	39	part_of	Ca2+-binding	23:34	arg1	the Ca2+-binding interaction domain	structure of the Ca2		the Ca2+-binding interaction domain		OGER	Site	structure of the Ca2	P00918	domain	X-ray structure of the Ca2+-binding interaction domain of C1s.
12788922	0	66	part_of	C1s	58:60	arg1	the Ca2+-binding interaction domain	C1s		the Ca2+-binding interaction domain		PUBTATOR	Site	C1s	716	domain	X-ray structure of the Ca2+-binding interaction domain of C1s.
9118998	7	18	gly	attached	1438:1445	arg2	glucose AND Thr201			Thr201	glucose					Thr201	The presence of O-linked monosaccharides (glucose attached to Ser71, Ser193 and fucose at Thr201) was tentatively ascertained by combining Edman degradation and MALDI-MS.
9118998	7	18	gly	attached	1438:1445	arg2	Ser193 AND glucose			Ser71, Ser193	glucose					Ser71, Ser193	The presence of O-linked monosaccharides (glucose attached to Ser71, Ser193 and fucose at Thr201) was tentatively ascertained by combining Edman degradation and MALDI-MS.
15869464	10	20	part_of	positions	1920:1928	arg1	OPN	OPN		positions		PUBTATOR	Site	OPN	6696	positions	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	10	60	part_of	OPN	1952:1954	arg1	positions	OPN		positions		PUBTATOR	Site	OPN	6696	positions	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	10	90	part_of	PTMs	1944:1947	arg1	positions	PTMs		positions		PUBTATOR	Site	PTMs	5763	positions	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
23041369	6	28	part_of	NPP1	947:950	arg1	the N-terminal somatomedin B-like domains	NPP1		the N-terminal somatomedin B-like domains		PUBTATOR	Site	NPP1	5167	domains	Remarkably, the N-terminal somatomedin B-like domains of NPP1, unlike those in NPP2, are flexible and do not contact the catalytic domain.
6816276	5	41	gly	moieties	616:623	arg1	the mu chain constant region			the mu chain constant region	the mu chain constant region		Site			region	The general type and location of carbohydrate moieties in the mu chain constant region are completely conserved between mouse and human mu chains.
16474139	11	54	part_of	protein	1894:1900	arg1	the ectodomain	protein		the ectodomain		Fterm	Site	protein		ectodomain	In addition, we showed that substitution of serine and threonine residues in the ectodomain of the 3a protein abolished the addition of the O-linked sugars.
17614963	8	41	part_of	fibronectin	1526:1536	arg1	juvenile-specific fibronectin fragments	fibronectin		juvenile-specific fibronectin fragments		PUBTATOR	Site	fibronectin	2335	fragments	This is the first report on the identification and characterization of juvenile-specific fibronectin fragments excreted into urine.
16274239	10	38	gly	N-glycosylation	1882:1896	arg2	a specific N-glycosylation site			a specific N-glycosylation site						site	This is the first study of which we are aware to show that selective glycosylation of a specific N-glycosylation site can produce two functionally distinct receptors.
16274239	10	43	gly	glycosylation	1854:1866	arg1	a specific N-glycosylation site			a specific N-glycosylation site						site	This is the first study of which we are aware to show that selective glycosylation of a specific N-glycosylation site can produce two functionally distinct receptors.
14769026	9	25	gly	occupied	1397:1404	arg2	Asn 662			Asn 662						Asn 662	An additional consensus sequence for N-glycosylation at Asn 662 is likely occupied.
14769026	9	25	gly	occupied	1397:1404	arg2	An additional consensus sequence			An additional consensus sequence						sequence	An additional consensus sequence for N-glycosylation at Asn 662 is likely occupied.
12970363	6	1	part_of	motifs	906:911	arg1	TRPC6	TRPC6		motifs		PUBTATOR	Site	TRPC6	7225	motifs	Two NX(S/T) motifs in TRPC6 were mutated (Asn to Gln) by in vitro mutagenesis to delete one or both extracellular N-linked glycosylation sites.
7511099	3	40	gly	arm	1177:1179	arg1	the terminal galactose				the terminal galactose						Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	3	44	gly	AFP	946:948	arg1	the terminal galactose	Desialylated AFP			the terminal galactose	PUBTATOR		Desialylated AFP	174		Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	3	48	gly	arm	1052:1054	arg1	the galactose				the galactose						Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	3	63	gly	Desialylated	933:944	arg1	Desialylated AFP	Desialylated AFP				PUBTATOR		Desialylated AFP	174		Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
22187327	3	17	gly	ICAM-5	519:524	arg1	the N-glycans	ICAM-5			the N-glycans	PUBTATOR		ICAM-5	15898		Here, we produced fifteen ICAM-5 gene constructs, in which each potential N-glycosylation site was mutated, to elucidate the function of the N-glycans of ICAM-5, and observed the effects of transfection of them on a neuronal cell line, Neuro-2a (N2a).
22187327	3	58	gly	N-glycosylation	439:453	arg2	each potential N-glycosylation site			each potential N-glycosylation site						site	Here, we produced fifteen ICAM-5 gene constructs, in which each potential N-glycosylation site was mutated, to elucidate the function of the N-glycans of ICAM-5, and observed the effects of transfection of them on a neuronal cell line, Neuro-2a (N2a).
8627329	0	2	gly	oligosaccharide	9:23	arg1	the 75-kDa neurotrophin receptor	neurotrophin receptor			oligosaccharide	PUBTATOR		neurotrophin receptor	4923		O-linked oligosaccharide on the 75-kDa neurotrophin receptor.
479158	10	54	gly	glycopeptide	838:849	arg2	One glycopeptide unit			One glycopeptide unit						glycopeptide	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
10419520	6	64	gly	glycosylation	965:977	arg2	glycosylation site mapping			glycosylation site mapping						site	Here, we use protease protection and glycosylation site mapping to define the topology of S2P in ER membranes.
19951703	8	52	gly	deglycosylated	1054:1067	arg1	the deglycosylated UGT1A9	the deglycosylated UGT1A9				PUBTATOR		UGT1A9	54600		To the contrary, the deglycosylated UGT1A9, which was produced by the treatment with Endo H under the non-denaturing condition, showed the same enzyme kinetics as the control.
1569071	11	62	part_of	IGF-II	2258:2263	arg1	the E domain peptide	IGF-II		the E domain peptide		PUBTATOR	Site	IGF-II	P01344	peptide	Finally, the association of O-linked oligosaccharide with the E domain peptide of IGF-II was confirmed by demonstrating the specificity of binding of the Ser66-Lys88 asialoglycopeptide to jackfruit lectin.
12911312	8	68	part_of	present	949:955	arg1	this isoform AND seven cysteines	this isoform		seven cysteines		Fterm	AminoAcid	isoform		cysteines	In this isoform, a single selenocysteine and seven cysteines are present.
2243102	2	26	gly	glycoproteins	145:157	arg1	lamp-1	lamp-1				PUBTATOR		lamp-1	3916		Lysosome membrane glycoproteins, lamp-1 and lamp-2, have been shown to contain 18 and 16 N-glycans, some of which are modified by poly-N-acetyl-lactosamine.
2243102	2	26	gly	glycoproteins	145:157	arg1	Lysosome membrane glycoproteins	Lysosome membrane glycoproteins				Fterm		glycoproteins			Lysosome membrane glycoproteins, lamp-1 and lamp-2, have been shown to contain 18 and 16 N-glycans, some of which are modified by poly-N-acetyl-lactosamine.
2243102	2	26	gly	glycoproteins	145:157	arg1	lamp-2	lamp-2				PUBTATOR		lamp-2	3920		Lysosome membrane glycoproteins, lamp-1 and lamp-2, have been shown to contain 18 and 16 N-glycans, some of which are modified by poly-N-acetyl-lactosamine.
2243102	2	29	gly	contain	198:204	arg1	lamp-1 AND 18 and 16 N-glycans	lamp-1			18 and 16 N-glycans	PUBTATOR		lamp-1	3916		Lysosome membrane glycoproteins, lamp-1 and lamp-2, have been shown to contain 18 and 16 N-glycans, some of which are modified by poly-N-acetyl-lactosamine.
2243102	2	29	gly	contain	198:204	arg1	Lysosome membrane glycoproteins AND 18 and 16 N-glycans	Lysosome membrane glycoproteins			18 and 16 N-glycans	Fterm		glycoproteins			Lysosome membrane glycoproteins, lamp-1 and lamp-2, have been shown to contain 18 and 16 N-glycans, some of which are modified by poly-N-acetyl-lactosamine.
2243102	2	29	gly	contain	198:204	arg1	lamp-2 AND 18 and 16 N-glycans	lamp-2			18 and 16 N-glycans	PUBTATOR		lamp-2	3920		Lysosome membrane glycoproteins, lamp-1 and lamp-2, have been shown to contain 18 and 16 N-glycans, some of which are modified by poly-N-acetyl-lactosamine.
1281977	4	23	gly	glycopeptides	693:705	arg1	N-acetylglucosamine linkages			glycopeptides	N-acetylglucosamine linkages					glycopeptides	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	4	51	gly	glycoproteins	675:687	arg1	N-acetylglucosamine linkages	glycoproteins			N-acetylglucosamine linkages	Fterm		glycoproteins			The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
29932112	4	9	part_of	Panx2	571:575	arg1	the predicted N-glycosylation site	Panx2		the predicted N-glycosylation site		PUBTATOR	Site	Panx2	56666	site	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
19855092	4	83	gly	glycans	700:706	arg1	Thr residues			Thr residues	Thr residues		AminoAcid			Thr residues	Using a variety of biochemical approaches we demonstrated that sialylation occurs on previously unidentified O-linked glycans on Thr residues of the variable domain in human adiponectin.
19855092	4	83	gly	glycans	700:706	arg1	the variable domain			the variable domain	the variable domain		Site			domain	Using a variety of biochemical approaches we demonstrated that sialylation occurs on previously unidentified O-linked glycans on Thr residues of the variable domain in human adiponectin.
21827946	3	6	part_of	VEGFR2	475:480	arg1	VEGFR2 domain 3	VEGFR2		VEGFR2 domain 3		PUBTATOR	Site	VEGFR2	3791	domain	The two Fab fragments bind at opposite ends of VEGFR2 domain 3; 1121B directly blocks VEGF binding, whereas 6.64 may prevent receptor dimerization by perturbing the domain 3:domain 4 interface.
21827946	3	17	part_of	Fab	436:438	arg1	The two Fab fragments	Fab		The two Fab fragments		PUBTATOR	Site	Fab	2187	fragments	The two Fab fragments bind at opposite ends of VEGFR2 domain 3; 1121B directly blocks VEGF binding, whereas 6.64 may prevent receptor dimerization by perturbing the domain 3:domain 4 interface.
16895906	2	10	gly	sialylated	286:295	arg1	sialylated glycans				sialylated glycans						The CD33-related siglecs show complex recognition patterns for sialylated glycans.
15066430	4	19	part_of	domain	1010:1015	arg1	CPD-2	CPD		domain		OGER	Site	CPD	O75976	domain	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
3665914	1	60	gly	fucose	244:249	arg1	glycoprotein	glycoprotein			fucose	Fterm		glycoprotein			The first demonstration of the presence of a 6-deoxyhexose other than fucose in glycoprotein.
3665914	1	72	gly	glycoprotein	254:265	arg1	glycoprotein	glycoprotein				Fterm		glycoprotein			The first demonstration of the presence of a 6-deoxyhexose other than fucose in glycoprotein.
8286855	7	53	gly	Thr-glycosylation	940:956	arg1	Xaa-Pro-Xaa-Xaa			Xaa-Pro-Xaa-Xaa						Pro	Three motifs are associated with Thr-glycosylation: Xaa-Pro-Xaa-Xaa where at least one Xaa = Thr; Thr-Xaa-Xaa-Xaa where at least one Xaa = Thr; Xaa-Xaa-Thr-Xaa where at least one X = Arg or Lys.
8286855	7	53	gly	Thr-glycosylation	940:956	arg1	Thr-Xaa-Xaa-Xaa			Thr						Thr	Three motifs are associated with Thr-glycosylation: Xaa-Pro-Xaa-Xaa where at least one Xaa = Thr; Thr-Xaa-Xaa-Xaa where at least one Xaa = Thr; Xaa-Xaa-Thr-Xaa where at least one X = Arg or Lys.
1900431	5	3	gly	threonine-61	615:626	arg1	Fucosylation			threonine-61	Fucosylation					threonine-61	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	5	32	gly	observed	632:639	arg2	t-PA AND Fucosylation	t-PA			Fucosylation	PUBTATOR		t-PA	5327		Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	5	13	gly	Fucosylation	599:610	arg1	threonine-61	t-PA		threonine-61		PUBTATOR		t-PA	5327	threonine-61	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
15454184	9	12	gly	present	1330:1336	arg1	Asn95 AND the triantennary structures			Asn95	the triantennary structures					Asn95	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
19571171	1	55	gly	Golgi-resident	152:165	arg1	N-Acetylglucosamine-6-sulfotransferase-1	Golgi-resident			N-Acetylglucosamine-6-sulfotransferase-1	Cterm		Golgi-resident			N-Acetylglucosamine-6-sulfotransferase-1 (GlcNAc6ST-1) is a Golgi-resident glycoprotein that is responsible for sulfation of the l-selectin ligand on endothelial cells.
19571171	1	37	gly	glycoprotein	167:178	arg1	N-Acetylglucosamine-6-sulfotransferase-1	glycoprotein			N-Acetylglucosamine-6-sulfotransferase-1	Fterm		glycoprotein			N-Acetylglucosamine-6-sulfotransferase-1 (GlcNAc6ST-1) is a Golgi-resident glycoprotein that is responsible for sulfation of the l-selectin ligand on endothelial cells.
14699159	0	90	gly	Underglycosylation	0:17	arg1	ATF6	ATF6				PUBTATOR		ATF6	22926		Underglycosylation of ATF6 as a novel sensing mechanism for activation of the unfolded protein response.
7462199	0	43	gly	globulin	57:64	arg1	the sugar chains	cold-insoluble globulin			the sugar chains	PUBTATOR		cold-insoluble globulin	2335		Structural studies of the sugar chains of cold-insoluble globulin isolated from human plasma.
12408961	6	41	gly	N-glycosylated	816:829	arg1	Human and mouse CREG2	Human and mouse CREG2				PUBTATOR		CREG2	263764		Human and mouse CREG2 are N-glycosylated in HeLa cells and deletion of amino-terminal sequences completely abolishes N-glycosylation, indicating that the N termini of both proteins may function as signal sequences.
6785754	1	75	part_of	Fc-like	109:115	arg1	an Fc-like fragment	Fc-like		an Fc-like fragment		Cterm	Site	Fc-like		fragment	The complete amino acid sequence of an Fc-like fragment designated Fc delta (t) and obtained by limited proteolysis with trypsin of an intact myeloma IgD protein (NIG-65) has been determined.
11152692	1	21	gly	leucine-rich	70:81	arg1	the leucine-rich repeat protein family			leucine	the leucine-rich repeat protein family					leucine	a novel member of the leucine-rich repeat protein family closely related to decorin and biglycan.
10704524	10	88	gly	A	1763:1763	arg1	the oligosaccharide structures	alpha-galactosidase A			the oligosaccharide structures	OGER		alpha-galactosidase A	P06280		Comparison of the oligosaccharide structures of alpha-GalNAc and alpha-galactosidase A, an evolutionary-related and highly homologous exoglycosidase, indicated that alpha-GalNAc had more completed complex chains, presumably due to differences in enzyme structure/domains, rate of biosynthesis, and/or aggregation of the overexpressed recombinant enzymes.
1908233	4	18	gly	glycopeptides	654:666	arg2	sequencing glycopeptides			sequencing glycopeptides						glycopeptides	After sequencing glycopeptides derived from two cell surface glycoproteins, a Thr-O-glycosylation motif of Xaa-Pro-Xaa-Xaa, where at least one Xaa = Thr(Sac), has been defined.
1908233	4	37	gly	glycoproteins	698:710	arg1	two cell surface glycoproteins	two cell surface glycoproteins				Fterm		glycoproteins			After sequencing glycopeptides derived from two cell surface glycoproteins, a Thr-O-glycosylation motif of Xaa-Pro-Xaa-Xaa, where at least one Xaa = Thr(Sac), has been defined.
1908233	4	43	gly	Thr-O-glycosylation	715:733	arg2	a Thr-O-glycosylation motif			a Thr-O-glycosylation motif						motif	After sequencing glycopeptides derived from two cell surface glycoproteins, a Thr-O-glycosylation motif of Xaa-Pro-Xaa-Xaa, where at least one Xaa = Thr(Sac), has been defined.
10207176	8	22	gly	C-mannosylated	1154:1167	arg1	more C-mannosylated proteins	more C-mannosylated proteins				Fterm		proteins			However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
2498325	8	7	part_of	Apolipoprotein	1176:1189	arg1	Gly196----Ser	Apolipoprotein E		Gly196----Ser		PUBTATOR	AminoAcid	Apolipoprotein E	348	Ser	Apolipoprotein E(Thr194----Asn,Gly196----Ser), which introduces a potential site for N-glycosylation at position 194, was secreted with a higher apparent molecular weight than native, O-glycosylated apoE.
29757379	0	58	gly	glycosite	38:46	arg2	Quiescin sulfhydryl oxidase 1 (QSOX1) glycosite mutation			Quiescin sulfhydryl oxidase 1 (QSOX1) glycosite mutation						glycosite	Quiescin sulfhydryl oxidase 1 (QSOX1) glycosite mutation perturbs secretion but not Golgi localization.
17925379	3	14	gly	glycosylated	693:704	arg1	Panx3	Panx3				PUBTATOR		Panx3	116337		Furthermore, N-glycosidase treatment showed that both Panx1 (approximately 41-48 kD species) and Panx3 (approximately 43 kD) were glycosylated, whereas N-linked glycosylation-defective mutants exhibited a decreased ability to be transported to the cell surface.
17925379	3	14	gly	glycosylated	693:704	arg1	Panx1	Panx1				PUBTATOR		Panx1	24145		Furthermore, N-glycosidase treatment showed that both Panx1 (approximately 41-48 kD species) and Panx3 (approximately 43 kD) were glycosylated, whereas N-linked glycosylation-defective mutants exhibited a decreased ability to be transported to the cell surface.
23395175	6	12	gly	region	863:868	arg1	O-GlcNAcylation				O-GlcNAcylation						In addition, O-GlcNAcylation of a region in PER2 known to regulate human sleep phase (S662-S674) competes with phosphorylation of this region, and this interplay is at least partly mediated by glucose levels.
23395175	6	29	gly	O-GlcNAcylation	842:856	arg1	PER2	PER2			O-GlcNAcylation	PUBTATOR		PER2	8864		In addition, O-GlcNAcylation of a region in PER2 known to regulate human sleep phase (S662-S674) competes with phosphorylation of this region, and this interplay is at least partly mediated by glucose levels.
20006580	2	34	gly	glycosylated	346:357	arg1	a single residue			a single residue						residue	Using site directed mutagenesis and Western immunoblotting a single residue of both orthologues was found to be glycosylated upon heterologous expression.
11710528	3	39	gly	glycopeptides	516:528	arg2	hTR glycopeptides			hTR glycopeptides						glycopeptides	The composition analysis of hTR glycopeptides revealed that Con A-I contains both mannose and fucose, whereas Con A-III has mannose exclusively.
21138434	6	44	part_of	subunit	1439:1445	arg1	utilised N-glycosylation sites	h5-HT3B subunit		utilised N-glycosylation sites		Cterm	Site	h5-HT3B subunit	9177	sites	The present study has identified utilised N-glycosylation sites of the h5-HT3B subunit and demonstrated that they promote subunit expression in the cell membrane; a prerequisite for 5-HT(3) receptor function.
15454184	4	53	gly	N-glycosylation	532:546	arg2	two potential N-glycosylation sites			sites, Asn95 and Asn259						sites, Asn95 and Asn259	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	53	gly	N-glycosylation	532:546	arg2	Asn259			sites, Asn95 and Asn259						sites, Asn95 and Asn259	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	53	gly	N-glycosylation	532:546	arg2	Asn259			sites, Asn95 and Asn259						sites, Asn95 and Asn259	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
3038148	0	65	part_of	tonin	59:63	arg1	The complete amino acid sequence	tonin		The complete amino acid sequence		PUBTATOR	Site	tonin	24841	sequence	The complete amino acid sequence of rat submaxillary gland tonin does contain the aspartic acid at the active site: confirmation by protein sequence analysis.
3038148	0	68	part_of	contain	70:76	arg1	The complete amino acid sequence AND the aspartic acid	The complete amino acid sequence		the aspartic acid						aspartic acid	The complete amino acid sequence of rat submaxillary gland tonin does contain the aspartic acid at the active site: confirmation by protein sequence analysis.
23234360	1	8	gly	O-glycosylation	128:142	arg1	extracellular proteins	proteins		residues		Fterm		proteins		residues	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	1	29	gly	O-glycosylation	128:142	arg1	Ser/Thr residues			residues	Ser/Thr residues		Site			residues	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	1	29	gly	O-glycosylation	128:142	arg1	extracellular proteins	proteins		residues	O-glycosylation	Fterm		proteins		residues	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	1	29	gly	O-glycosylation	128:142	arg1	Ser/Thr residues	proteins		residues	Ser/Thr residues	Fterm	Site	proteins		residues	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	1	29	gly	O-glycosylation	128:142	arg1	extracellular proteins	proteins			O-glycosylation	Fterm		proteins			The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
16212939	2	73	gly	N-glycosylation	323:337	arg1	target proteins	proteins		peptide		Fterm		proteins		peptide	We investigated the effect of N-glycosylation of the secretion enhancer peptide on the secretion of target proteins.
20044576	1	23	part_of	laminin-G	217:225	arg1	laminin-G domains	laminin		laminin-G domains		OGER	Site	laminin		domains	Alpha-dystroglycan (alpha-DG) is a cell-surface glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains and certain arenaviruses.
20044576	1	42	part_of	containing	206:215	arg1	both extracellular matrix proteins AND laminin-G domains	both extracellular matrix proteins		laminin-G domains		Fterm	Site	proteins		domains	Alpha-dystroglycan (alpha-DG) is a cell-surface glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains and certain arenaviruses.
7107587	6	61	gly	glycopeptides	545:557	arg2	glycopeptides			glycopeptides						glycopeptides	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
21264968	6	5	gly	Thr1	2169:2172	arg1	a single α-GalNAc residue			residue at Thr1, Thr6	a single α-GalNAc residue					residue at Thr1, Thr6	The solution structures determined by NMR spectroscopic studies elicited that the preferential introduction of α-GalNAc at Thr10 of MUC4 stabilizes specifically a β-like extended backbone structure at this area, whereas other synthetic models with a single α-GalNAc residue at Thr1, Thr6, or Thr15 did not exhibit any converged three-dimensional structure at the proximal peptide moiety.
21264968	6	59	gly	Thr15	2184:2188	arg1	a single α-GalNAc residue			Thr15	a single α-GalNAc residue					Thr15	The solution structures determined by NMR spectroscopic studies elicited that the preferential introduction of α-GalNAc at Thr10 of MUC4 stabilizes specifically a β-like extended backbone structure at this area, whereas other synthetic models with a single α-GalNAc residue at Thr1, Thr6, or Thr15 did not exhibit any converged three-dimensional structure at the proximal peptide moiety.
21264968	6	91	gly	Thr6	2175:2178	arg1	a single α-GalNAc residue			residue at Thr1, Thr6	a single α-GalNAc residue					residue at Thr1, Thr6	The solution structures determined by NMR spectroscopic studies elicited that the preferential introduction of α-GalNAc at Thr10 of MUC4 stabilizes specifically a β-like extended backbone structure at this area, whereas other synthetic models with a single α-GalNAc residue at Thr1, Thr6, or Thr15 did not exhibit any converged three-dimensional structure at the proximal peptide moiety.
16679516	0	86	gly	Ser-2730	55:62	arg1	A single chondroitin 6-sulfate oligosaccharide unit			Ser-2730	A single chondroitin 6-sulfate oligosaccharide unit					Ser-2730	A single chondroitin 6-sulfate oligosaccharide unit at Ser-2730 of human thyroglobulin enhances hormone formation and limits proteolytic accessibility at the carboxyl terminus.
1898343	0	30	gly	elastase	43:50	arg1	Carbohydrate structure	pancreatic elastase 1			Carbohydrate structure	PUBTATOR		pancreatic elastase 1	1990		Carbohydrate structure of human pancreatic elastase 1.
20332087	3	30	gly	MPO	470:472	arg1	the N-glycan composition	MPO			the N-glycan composition	PUBTATOR		MPO	4353		Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated.
20332087	3	48	gly	MPO	517:519	arg1	the N-glycan composition	MPO			the N-glycan composition	PUBTATOR		MPO	4353		Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated.
3427055	3	66	part_of	SPARC	587:591	arg1	the SPARC sequence	SPARC		the SPARC sequence		PUBTATOR	Site	SPARC	6678	sequence	In view of the calcium binding activity reported for osteonectin, we analyzed the SPARC sequence and found two putative calcium binding domains.
1694179	12	37	gly	glycosylated	1694:1705	arg2	this site	protein C		site		Cterm		protein C		site	The percentage of protein C that is glycosylated at this site may therefore depend at least in part on the rate of disulfide bond formation which may in turn be related to the rate of protein synthesis.
11447134	11	19	gly	fucosylated	1528:1538	arg1	some carbohydrate structures				some carbohydrate structures						In both cases the glycosylation belongs to the mannose-core- or high-mannose-type, and some carbohydrate structures are fucosylated.
9023546	3	35	part_of	EGF-1	388:392	arg1	recombinant human factor VII EGF-1 domain	factor VII EGF		recombinant human factor VII EGF-1 domain		OGER	Site	factor VII EGF	P08709	domain	The assay uses recombinant human factor VII EGF-1 domain as acceptor substrate and GDP-fucose as donor substrate.
9023546	3	77	part_of	VII	384:386	arg1	recombinant human factor VII EGF-1 domain	factor VII EGF		recombinant human factor VII EGF-1 domain		OGER	Site	factor VII EGF	P08709	domain	The assay uses recombinant human factor VII EGF-1 domain as acceptor substrate and GDP-fucose as donor substrate.
17330941	11	8	gly	glycopeptides	1416:1428	arg2	cysteine-containing glycopeptides			cysteine-containing glycopeptides						glycopeptides	We show that analysis by cysteine-containing glycopeptides allows detection of low-abundance proteins such as the epidermal growth factor receptor, the Vitamin K-dependent protein Z, the hepatocyte growth factor activator, and the lymphatic endothelium-specific hyaluronan receptor as these proteins were not detected in the glycopeptide control analysis.
17330941	11	27	gly	glycopeptide	1696:1707	arg2	the glycopeptide control analysis			the glycopeptide control analysis						glycopeptide	We show that analysis by cysteine-containing glycopeptides allows detection of low-abundance proteins such as the epidermal growth factor receptor, the Vitamin K-dependent protein Z, the hepatocyte growth factor activator, and the lymphatic endothelium-specific hyaluronan receptor as these proteins were not detected in the glycopeptide control analysis.
9501084	0	20	part_of	form	107:110	arg1	the collagen-binding epitope	form of BM-40		the collagen-binding epitope		PUBTATOR	Site	form of BM-40	6678	epitope	Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin.
19038967	5	76	gly	deglycosylated	1016:1029	arg1	deglycosylated pro-TPP1	deglycosylated pro-TPP1				Cterm	AminoAcid	TPP1			The crystal structure of deglycosylated pro-TPP1 was determined at 1.85 angstroms resolution.
20145116	7	32	part_of	receptor	1015:1022	arg1	left-handed twisted receptor domains	receptor		left-handed twisted receptor domains		Fterm	Site	receptor		domains	This structure reveals a symmetrical 22 complex, in which left-handed twisted receptor domains wrap around the 2-fold axis of VEGF-C.
1900431	7	11	part_of	factor	978:983	arg1	the epidermal growth factor domains	factor		the epidermal growth factor domains		Fterm	Site	factor		domains	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	7	39	part_of	found	993:997	arg2	fibrinolytic proteins AND the epidermal growth factor domains	fibrinolytic proteins		the epidermal growth factor domains		Fterm	Site	proteins		domains	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
11150294	2	15	part_of	MUPP1	429:433	arg1	the 10th PDZ domain	MUPP1		the 10th PDZ domain		OGER	Site	MUPP1	O55164	domain	Here we report that the C terminus of the 5-hydroxytryptamine type 2C (5-HT(2C)) receptor selectively interacts with the 10th PDZ domain of MUPP1.
11150294	2	74	part_of	receptor	370:377	arg1	the C terminus	receptor		the C terminus		Fterm	Site	receptor		terminus	Here we report that the C terminus of the 5-hydroxytryptamine type 2C (5-HT(2C)) receptor selectively interacts with the 10th PDZ domain of MUPP1.
6327299	0	3	gly	glycocalicin	73:84	arg1	the O-linked carbohydrate chains	glycocalicin			the O-linked carbohydrate chains	Fterm		glycocalicin			Structural studies on the O-linked carbohydrate chains of human platelet glycocalicin.
11912203	9	61	gly	glycosylated	1397:1408	arg1	the four glycosylated lysines			the four glycosylated lysines						lysines	Functional analysis revealed that full-length adiponectin produced by mammalian cells is much more potent than bacterially generated adiponectin in enhancing the ability of subphysiological concentrations of insulin to inhibit gluconeogenesis in primary rat hepatocytes, whereas this insulin-sensitizing ability was significantly attenuated when the four glycosylated lysines were substituted with arginines.
19467646	9	6	gly	glycosylated	1172:1183	arg1	BDNF	BDNF		pro		PUBTATOR		BDNF	627	pro	Treatment with N-glycanase and plasmin reduced the size of the higher molecular weight bands, confirming the glycosylated pro-form of BDNF.
24090084	10	6	part_of	glycoproteins	1641:1653	arg1	863 unique intact N-linked glycopeptides	glycoproteins		863 unique intact N-linked glycopeptides		Fterm	Site	glycoproteins		glycopeptides	This multidimensional approach allowed confident identification of 863 unique intact N-linked glycopeptides from 161 rat brain glycoproteins.
18508581	5	16	gly	used	759:762	arg2	All three N-glycosylation consensus sequences			All three N-glycosylation consensus sequences						sequences	All three N-glycosylation consensus sequences within EpCAM's extracellular domain were used in human and murine cells.
15536627	3	58	gly	site	539:542	arg1	the carbohydrates			site	the carbohydrates					site	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
11080501	0	106	gly	N-glycosylation	48:62	arg1	the human gastrointestinal carcinoma antigen GA733-2	GA733-2		sites		OGER		GA733-2	P16422	sites	Determination of disulfide bond assignments and N-glycosylation sites of the human gastrointestinal carcinoma antigen GA733-2 (CO17-1A, EGP, KS1-4, KSA, and Ep-CAM).
29741879	8	14	gly	glycosites	1752:1761	arg2	1 731 N-linked glycosites			1 731 N-linked glycosites						glycosites	Together, 11 292 N-linked glycopeptides corresponding to 1 731 N-linked glycosites from 883 human glycoproteins were identified from the two data sets.
29741879	8	54	gly	glycopeptides	1706:1718	arg2	11 292 N-linked glycopeptides			11 292 N-linked glycopeptides						glycopeptides	Together, 11 292 N-linked glycopeptides corresponding to 1 731 N-linked glycosites from 883 human glycoproteins were identified from the two data sets.
29741879	8	84	gly	glycoproteins	1778:1790	arg1	883 human glycoproteins	883 human glycoproteins				Fterm		glycoproteins			Together, 11 292 N-linked glycopeptides corresponding to 1 731 N-linked glycosites from 883 human glycoproteins were identified from the two data sets.
21917917	9	1	gly	N-glycosylated	1478:1491	arg1	a large N-glycosylated, extracellular loop domain			a large N-glycosylated, extracellular loop domain						domain	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21402931	8	42	part_of	contain	1352:1358	arg1	endoglin AND this cleavage site	endoglin		this cleavage site		PUBTATOR	Site	endoglin	2022	site	Nonpolymerizing ZP proteins such as betaglycan and endoglin do not contain this cleavage site.
21402931	8	42	part_of	contain	1352:1358	arg1	Nonpolymerizing ZP proteins AND this cleavage site	Nonpolymerizing ZP proteins		this cleavage site		Fterm	Site	proteins		site	Nonpolymerizing ZP proteins such as betaglycan and endoglin do not contain this cleavage site.
8202534	2	28	gly	glycoproteins	472:484	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			We show here that its single N-linked biantennary oligosaccharide does not display the microheterogeneity usually characteristic of glycoproteins.
7599134	5	55	gly	N-glycosylation	874:888	arg2	the ATIII N-glycosylation sites			the ATIII N-glycosylation sites						sites	Consensus sequences (CSs) of the ATIII N-glycosylation sites are N-X-S for 135 and N-X-T for 96, 155, and 192.
17563389	6	16	gly	glycosylation	1154:1166	arg2	both N-linked glycosylation sites			both N-linked glycosylation sites						sites	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
29391424	1	7	gly	glycopeptides	107:119	arg2	glycopeptides			glycopeptides						glycopeptides	Workflows capable of determining glycopeptides in large-scale are missing in the field of glycoproteomics.
6203908	5	73	gly	attached	288:295	arg1	asparagine residues 32, 47, 224, 373, 387, 846, 968, and 1401 AND Glucosamine-based oligosaccharide groups			asparagine residues 32, 47, 224, 373, 387, 846, 968, and 1401	Glucosamine-based oligosaccharide groups					asparagine residues 32, 47, 224, 373, 387, 846, 968, and 1401	Glucosamine-based oligosaccharide groups are attached to asparagine residues 32, 47, 224, 373, 387, 846, 968, and 1401.
15173186	11	76	gly	glycosylation	1691:1703	arg2	all four predicted glycosylation sites			all four predicted glycosylation sites						sites	Using site-directed mutagenesis, we have found that in Toll-like receptor 2 extracellular domain all four predicted glycosylation sites are substituted, although one site is inefficiently core-glycosylated and its removal drastically affects secretion.
15173186	11	99	gly	core-glycosylated	1763:1779	arg1	one site			one site						site	Using site-directed mutagenesis, we have found that in Toll-like receptor 2 extracellular domain all four predicted glycosylation sites are substituted, although one site is inefficiently core-glycosylated and its removal drastically affects secretion.
10639192	5	7	gly	glycosylation	651:663	arg2	the possible glycosylation sites			the possible glycosylation sites						sites	N-linked carbohydrates are present at each of the possible glycosylation sites.
10639192	5	57	gly	present	619:625	arg1	the possible glycosylation sites AND N-linked carbohydrates			sites	N-linked carbohydrates					sites	N-linked carbohydrates are present at each of the possible glycosylation sites.
2514791	4	21	gly	located	1453:1459	arg2	Asn-448 AND sulfated oligosaccharides			Asn-448	sulfated oligosaccharides					Asn-448	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	101	gly	sialylated	1330:1339	arg1	both neutral and sialylated oligosaccharides				both neutral and sialylated oligosaccharides						Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	46	gly	N-glycosylated	853:866	arg1	type II t-PA	t-PA		Asn-184 and Asn-448		PUBTATOR		t-PA	5327	Asn-184 and Asn-448	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	46	gly	N-glycosylated	853:866	arg2	Asn-448			Asn-117 and Asn-448						Asn-117 and Asn-448	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	46	gly	N-glycosylated	853:866	arg1	type II t-PA	t-PA		Asn-117 and Asn-448		PUBTATOR		t-PA	5327	Asn-117 and Asn-448	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	46	gly	N-glycosylated	853:866	arg1	type II t-PA	t-PA		Asn-117 and Asn-448		PUBTATOR		t-PA	5327	Asn-117 and Asn-448	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
10944330	0	28	part_of	Fab	17:19	arg1	the Fab fragment	structure of the Fab		the Fab fragment		PUBTATOR	Site	structure of the Fab	2187	fragment	Structure of the Fab fragment from F124, a monoclonal antibody specific for hepatitis B surface antigen.
21712440	2	66	part_of	APP/Aβ	506:511	arg1	released APP/Aβ glycopeptides	APP/Aβ 		released APP/Aβ glycopeptides		PUBTATOR	Site	APP/Aβ 	351	glycopeptides	Although APP is a well-known membrane glycoprotein carrying both N- and O-glycans, nothing is known about the occurrence of released APP/Aβ glycopeptides in cerebrospinal fluid (CSF).
6587378	2	30	gly	has	330:332	arg1	The protein AND five attached glucosamine-containing oligosaccharides	The protein			five attached glucosamine-containing oligosaccharides	Fterm		protein			The protein consists of 326 amino acids and has five attached glucosamine-containing oligosaccharides.
15454184	7	41	gly	rhFS	1014:1017	arg1	the oligosaccharides	rhFS			the oligosaccharides	Cterm		rhFS			This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
3353370	0	102	gly	glycoprotein	44:55	arg1	human platelet glycoprotein Ib	human platelet glycoprotein Ib				Fterm		glycoprotein			The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence.
7683678	8	16	part_of	24p3	1236:1239	arg1	the deduced sequences	24p3		the deduced sequences		Cterm	Site	24p3		sequences	The sequence did not match any known human protein, but showed a high degree of similarity with the deduced sequences of rat alpha 2-microglobulin-related protein and the mouse protein 24p3.
7683678	8	17	part_of	protein	1206:1212	arg1	the deduced sequences	alpha 2-microglobulin-related protein		the deduced sequences		PUBTATOR	Site	alpha 2-microglobulin-related protein	170496	sequences	The sequence did not match any known human protein, but showed a high degree of similarity with the deduced sequences of rat alpha 2-microglobulin-related protein and the mouse protein 24p3.
30237853	8	4	gly	O-glycopeptides	1518:1532	arg2	O-glycopeptides			O-glycopeptides						O-glycopeptides	We accurately quantified 729 N-glycoproteins spanning 1,310 unique N-glycosylation sites and observed 954 and 965 unique intact N- and O-glycopeptides, respectively, across the two disease conditions.
30237853	8	34	gly	N-glycoproteins	1412:1426	arg1	729 N-glycoproteins	729 N-glycoproteins				Fterm		N-glycoproteins			We accurately quantified 729 N-glycoproteins spanning 1,310 unique N-glycosylation sites and observed 954 and 965 unique intact N- and O-glycopeptides, respectively, across the two disease conditions.
30237853	8	42	gly	N-glycosylation	1450:1464	arg2	1,310 unique N-glycosylation sites			1,310 unique N-glycosylation sites						sites	We accurately quantified 729 N-glycoproteins spanning 1,310 unique N-glycosylation sites and observed 954 and 965 unique intact N- and O-glycopeptides, respectively, across the two disease conditions.
18420026	6	9	part_of	glycoprotein	1539:1550	arg1	a single glycosylation site	glycoprotein		a single glycosylation site		Fterm	Site	glycoprotein		site	Based on the results of N-Glycosidase F treatment with human fetal brain tissue and lysates from transient transfection with human wild-type or glycosylation site mutant NECL1 in 293ET cells, we demonstrated that human NECL1 is an N-linked glycoprotein with a single glycosylation site at position N290KS.
17157876	8	22	gly	subunit	1816:1822	arg1	the central leucine-rich repeat tandem	CPN2 subunit			the central leucine-rich repeat tandem	PUBTATOR		CPN2 subunit	1370		In tetrameric CPN, each CPN1 subunit might interact with the central leucine-rich repeat tandem of the cognate CPN2 subunit via a unique hydrophobic surface patch wrapping around the catalytic domain-TT interface, exposing the two active centers.
17157876	8	56	gly	leucine-rich	1769:1780	arg1	the central leucine-rich repeat tandem			leucine	the central leucine-rich repeat tandem					leucine	In tetrameric CPN, each CPN1 subunit might interact with the central leucine-rich repeat tandem of the cognate CPN2 subunit via a unique hydrophobic surface patch wrapping around the catalytic domain-TT interface, exposing the two active centers.
20133774	7	54	part_of	PTPRG	1236:1240	arg1	a discrete region	PTPRG		a discrete region		PUBTATOR	Site	PTPRG	19270	region	This site contacts a discrete region of PTPRG composed primarily of an extended beta-hairpin loop found in both PTPRG and PTPRZ.
19017797	2	60	part_of	FMS	482:484	arg1	D1-D3	FMS		D1-D3		OGER	SiteSequence	FMS	P07333	D1-D3	We report a 2.4 A crystal structure of M-CSF bound to the first 3 domains (D1-D3) of FMS.
19017797	2	60	part_of	FMS	482:484	arg1	the first 3 domains	FMS		the first 3 domains		OGER	Site	FMS	P07333	domains	We report a 2.4 A crystal structure of M-CSF bound to the first 3 domains (D1-D3) of FMS.
16877748	4	64	gly	sialylated	670:679	arg1	complex-type N-glycans				complex-type N-glycans						MIP-2 induction is glycosylation dependent, as it is strongly enhanced when sICAM-1 carries sialylated, complex-type N-glycans as synthesized by wild-type Chinese hamster ovary (CHO) cells.
16877748	4	45	gly	carries	662:668	arg1	sICAM-1 AND complex-type N-glycans	sICAM-1			complex-type N-glycans	Cterm		sICAM-1	3383		MIP-2 induction is glycosylation dependent, as it is strongly enhanced when sICAM-1 carries sialylated, complex-type N-glycans as synthesized by wild-type Chinese hamster ovary (CHO) cells.
19017259	9	1	gly	linked	1539:1544	arg2	Thr AND (Sialyl) Galbeta1-3GalNAc			Thr(14) and Ser(174)	(Sialyl) Galbeta1-3GalNAc					Thr(14) and Ser(174)	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	1	gly	linked	1539:1544	arg1	14 AND (Sialyl) Galbeta1-3GalNAc			Thr(14) and Ser(174)	(Sialyl) Galbeta1-3GalNAc					Thr(14) and Ser(174)	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	1	gly	linked	1539:1544	arg1	14 AND (Sialyl) Galbeta1-3GalNAc			Thr(14) and Ser(174)	(Sialyl) Galbeta1-3GalNAc					Thr(14) and Ser(174)	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	1	gly	linked	1539:1544	arg1	175 AND (Sialyl) Galbeta1-3GalNAc			Thr(175)	(Sialyl) Galbeta1-3GalNAc					Thr(175)	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	1	gly	linked	1539:1544	arg1	Asn(117) AND (Sialyl) Galbeta1-3GalNAc			Asn(117) and Asn(167)	(Sialyl) Galbeta1-3GalNAc					Asn(117) and Asn(167)	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	24	gly	glycosylated	1678:1689	arg1	228			Asn(228)						Asn(228)	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
15677325	4	6	part_of	has	774:776	arg1	GluR6 AND a tyrosine	GluR6		a tyrosine		PUBTATOR	AminoAcid	GluR6	2898	tyrosine	Subtle differences in these contacts provide a structural explanation for why GluR2 L483Y and GluR3 L507Y are nondesensitizing, but GluR6, which has a tyrosine at that site, is not.
2363690	5	29	gly	present	976:982	arg1	IgG2 AND Unusual monoantennary oligosaccharides	IgG2			Unusual monoantennary oligosaccharides	OGER		IgG2	P01859		Unusual monoantennary oligosaccharides present in IgG2 and IgG3 proteins were isolated and their structures determined.
2363690	5	29	gly	present	976:982	arg1	IgG3 AND Unusual monoantennary oligosaccharides	IgG3			Unusual monoantennary oligosaccharides	PUBTATOR		IgG3 proteins	P01860		Unusual monoantennary oligosaccharides present in IgG2 and IgG3 proteins were isolated and their structures determined.
19088065	11	61	gly	isoforms	1426:1433	arg1	glycans	isoforms			glycans	Fterm		isoforms			The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	11	77	gly	glycopeptide	1453:1464	arg2	glycopeptide			glycopeptide						glycopeptide	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
8615697	1	16	part_of	contains	216:223	arg1	The amino acid sequence AND 20 putative N-linked glycosylation sites	The amino acid sequence		20 putative N-linked glycosylation sites						sites	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
9677334	11	9	gly	Arg10	1485:1489	arg1	specific determinants			Arg10 and Arg17 residues	specific determinants					Arg10 and Arg17 residues	Moreover we found that the Arg10 and Arg17 residues of TPO seem to be specific determinants for TPO/c-Mpl recognition.
9677334	11	66	gly	Arg17	1495:1499	arg1	specific determinants			Arg10 and Arg17 residues	specific determinants					Arg10 and Arg17 residues	Moreover we found that the Arg10 and Arg17 residues of TPO seem to be specific determinants for TPO/c-Mpl recognition.
9677334	11	70	gly	TPO	1513:1515	arg1	specific determinants	TPO			specific determinants	PUBTATOR		TPO	7066		Moreover we found that the Arg10 and Arg17 residues of TPO seem to be specific determinants for TPO/c-Mpl recognition.
8407880	2	18	gly	released	330:337	arg1	the glycopeptides AND The oligosaccharides			the glycopeptides	The oligosaccharides					glycopeptides	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with 2-aminopyridine at the reducing ends.
8407880	2	24	gly	glycopeptides	348:360	arg2	the glycopeptides			the glycopeptides						glycopeptides	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with 2-aminopyridine at the reducing ends.
10383441	1	9	gly	glycoprotein	162:173	arg1	a secretory glycoprotein	a secretory glycoprotein				Fterm		glycoprotein			We have reported that bovine DNase I, a secretory glycoprotein, acquires mannose 6-phosphate residues on 12.6% of its Asn-linked oligosaccharides when expressed in COS-1 cells and that the extent of phosphorylation increases to 79.2% when lysines are placed at positions 27 and 74 of the mature protein (Nishikawa, A., Gregory, W. , Frenz, J., Cacia, J., and Kornfeld, S. (1997) J. Biol.
10383441	1	9	gly	glycoprotein	162:173	arg1	bovine DNase I	bovine DNase I				PUBTATOR		DNase I	282217		We have reported that bovine DNase I, a secretory glycoprotein, acquires mannose 6-phosphate residues on 12.6% of its Asn-linked oligosaccharides when expressed in COS-1 cells and that the extent of phosphorylation increases to 79.2% when lysines are placed at positions 27 and 74 of the mature protein (Nishikawa, A., Gregory, W. , Frenz, J., Cacia, J., and Kornfeld, S. (1997) J. Biol.
10383441	1	11	gly	Asn-linked	230:239	arg1	its Asn-linked oligosaccharides			Asn	its Asn-linked oligosaccharides					Asn	We have reported that bovine DNase I, a secretory glycoprotein, acquires mannose 6-phosphate residues on 12.6% of its Asn-linked oligosaccharides when expressed in COS-1 cells and that the extent of phosphorylation increases to 79.2% when lysines are placed at positions 27 and 74 of the mature protein (Nishikawa, A., Gregory, W. , Frenz, J., Cacia, J., and Kornfeld, S. (1997) J. Biol.
24279413	5	0	gly	glycopeptides	947:959	arg2	glycopeptides			glycopeptides						glycopeptides	Scoring algorithms are presented for tandem mass spectra of glycopeptides resulting from collision-induced dissociation (CID), higher-energy C-trap dissociation (HCD), and electron transfer dissociation (ETD) fragmentation modes.
20473317	3	27	part_of	RET	582:584	arg1	higher and lower vertebrate RET CLD regions	RET		higher and lower vertebrate RET CLD regions		PUBTATOR	Site	RET	5979	regions	CLD1 structural elements and disulfide composition are unique to mammals, indicating an unexpected structural diversity within higher and lower vertebrate RET CLD regions.
11904304	4	51	gly	-glycosylated	876:888	arg1	c-Myc	c-Myc				PUBTATOR		c-Myc	4609		Using these antibodies together with a commercial anti-Thr-58-phosphorylated c-Myc antibody, we simultaneously detected three forms of c-Myc (Thr-58-unmodified, -phosphorylated, and -glycosylated).
20511397	7	32	gly	sialylated	1385:1394	arg1	cell-derived apoE	cell-derived apoE				PUBTATOR		apoE	348		Comparison of plasma and cellular/secreted apoE from the same donor confirmed that cell-derived apoE is more extensively sialylated than plasma apoE.
22967898	5	34	gly	N-glycosylation	571:585	arg1	cathepsin V	cathepsin V				PUBTATOR		cathepsin V	1515		N-glycosylation of cathepsin V was important for transportation to lysosome, secretion, and activity in HT1080 cells.
18490449	6	1	gly	contained	1089:1097	arg1	myelin Opalin AND O-glycans	myelin Opalin			O-glycans	PUBTATOR		Opalin	226115		Enzymatic deglycosylation showed that myelin Opalin contained N- and O-glycans, and that the O-glycans, at least, had negatively charged sialic acids.
18490449	6	1	gly	contained	1089:1097	arg1	myelin Opalin AND N-	myelin Opalin			N-	PUBTATOR		Opalin	226115		Enzymatic deglycosylation showed that myelin Opalin contained N- and O-glycans, and that the O-glycans, at least, had negatively charged sialic acids.
10413465	0	12	part_of	E	126:126	arg1	carboxy-terminal domains	apolipoprotein E		carboxy-terminal domains		PUBTATOR	Site	apolipoprotein E	348	domains	Contribution of cysteine 158, the glycosylation site threonine 194, the amino- and carboxy-terminal domains of apolipoprotein E in the binding to amyloid peptide beta (1-40).
24530628	5	20	gly	glycopeptide	804:815	arg2	each glycopeptide			each glycopeptide						glycopeptide	We also provide data showing that the acetone-precipitated glycopeptide enrichment was successful in acquiring a more comprehensive MS/MS data set for the various glycoforms of each glycopeptide in crude human serum.
24530628	5	27	gly	glycopeptide	681:692	arg2	the acetone-precipitated glycopeptide enrichment			the acetone-precipitated glycopeptide enrichment						glycopeptide	We also provide data showing that the acetone-precipitated glycopeptide enrichment was successful in acquiring a more comprehensive MS/MS data set for the various glycoforms of each glycopeptide in crude human serum.
24530628	5	65	gly	glycoforms	785:794	arg1	each glycopeptide			each glycopeptide						glycopeptide	We also provide data showing that the acetone-precipitated glycopeptide enrichment was successful in acquiring a more comprehensive MS/MS data set for the various glycoforms of each glycopeptide in crude human serum.
2511201	0	9	part_of	factors	176:182	arg1	the first epidermal growth factor-like domain	factors		the first epidermal growth factor-like domain		Fterm	Site	factors		domain	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	53	part_of	residue	110:116	arg1	human factors	factors		residue		Fterm	AminoAcid	factors		serine residue	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
3458201	0	77	gly	1B-glycoprotein	42:56	arg1	1B-glycoprotein	1B-glycoprotein				PUBTATOR		alpha 1B-glycoprotein	1		Amino acid sequence of human plasma alpha 1B-glycoprotein: homology to the immunoglobulin supergene family.
7947762	2	2	part_of	RNase	397:401	arg1	position 7	RNase		position 7		OGER	SpecificSite	RNase	P07998	tryptophan residue at position 7	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
12171601	2	0	gly	[ECL2	457:461	arg1	Asn(222)-->Ala			Asn(222)-->Ala						Ala	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	0	gly	[ECL2	457:461	arg1	Asn(222)-->Gln			Asn(222)-->Gln						Asn(222)	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	90	gly	glycosylation	320:332	arg2	glycosylation sequons			glycosylation sequons							Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
9705299	6	45	gly	glycosylated	1001:1012	arg1	G6Pase	G6Pase		Asn96		PUBTATOR		G6Pase	2538	Asn96	Western blot and in vitro translation studies showed that G6Pase is glycosylated only at Asn96, further validating the nine-transmembrane topology model.
9336835	7	92	gly	glycopeptides	1153:1165	arg2	the glycopeptides			the glycopeptides						glycopeptides	Edman sequence analysis was then used to confirm the identities of the glycopeptides and to define the attachment sites within each peptide.
19153605	5	12	part_of	FS	587:588	arg1	the FS domain	structure of the FS		the FS domain		Cterm	Site	structure of the FS	10418	domain	We determined the structure of the FS domain at 1.8-A resolution.
19303388	3	17	part_of	protein	605:611	arg1	a peptide	myelin basic protein		a peptide		PUBTATOR	Site	myelin basic protein	17196	peptide	We show that a microbial peptide, common to several major classes of bacteria, can induce MS-like disease in humanized mice by crossreacting with a T cell receptor (TCR) that also recognizes a peptide from myelin basic protein, a candidate MS autoantigen.
3422739	1	5	gly	glycoprotein	180:191	arg1	a nonpolymorphic glycoprotein	a nonpolymorphic glycoprotein				Fterm		glycoprotein			The invariant chain (Ii), a nonpolymorphic glycoprotein that associates with the immunoregulatory Ia proteins encoded by the major histocompatibility complex, has a proteoglycan form (Ii-CS) that bears a chondroitin sulfate glycosaminoglycan.
3422739	1	46	gly	has	296:298	arg1	a nonpolymorphic glycoprotein AND a proteoglycan form	a nonpolymorphic glycoprotein			a proteoglycan form	Fterm		glycoprotein			The invariant chain (Ii), a nonpolymorphic glycoprotein that associates with the immunoregulatory Ia proteins encoded by the major histocompatibility complex, has a proteoglycan form (Ii-CS) that bears a chondroitin sulfate glycosaminoglycan.
3422739	1	46	gly	has	296:298	arg1	Ii AND a proteoglycan form	Ii			a proteoglycan form	Cterm		(Ii)			The invariant chain (Ii), a nonpolymorphic glycoprotein that associates with the immunoregulatory Ia proteins encoded by the major histocompatibility complex, has a proteoglycan form (Ii-CS) that bears a chondroitin sulfate glycosaminoglycan.
3422739	1	18	gly	bears	333:337	arg1	Ii-CS AND a chondroitin sulfate glycosaminoglycan	Ii-CS			a chondroitin sulfate glycosaminoglycan	Cterm		Ii			The invariant chain (Ii), a nonpolymorphic glycoprotein that associates with the immunoregulatory Ia proteins encoded by the major histocompatibility complex, has a proteoglycan form (Ii-CS) that bears a chondroitin sulfate glycosaminoglycan.
24338010	4	1	part_of	NPP4	879:882	arg1	the corresponding region	NPP4		the corresponding region		PUBTATOR	Site	NPP4	22875	region	Comparative structural analysis reveals a tripartite lysine claw in NPP1 that stabilizes the terminal phosphate of ATP, whereas the corresponding region of NPP4 contains features that hinder this binding orientation, thereby inhibiting ATP hydrolysis.
16877748	9	58	gly	glycosylated	1690:1701	arg1	All nine consensus sequences			All nine consensus sequences						sequences	All nine consensus sequences for N-glycosylation were found to be glycosylated.
11098061	0	72	gly	N-glycosylation	45:59	arg1	the human signal transducer gp130	gp130		sites		PUBTATOR		gp130	P40189	sites	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	0	72	gly	N-glycosylation	45:59	arg2	the extracellular domain			domain						domain	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	0	72	gly	N-glycosylation	45:59	arg1	the human signal transducer gp130	gp130		domain		PUBTATOR		gp130	P40189	domain	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	0	72	gly	N-glycosylation	45:59	arg1	the human signal transducer gp130	gp130		domain		PUBTATOR		gp130	P40189	domain	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11904304	1	20	gly	Thr-58	311:316	arg1	O-linked N-acetylglucosamine			Thr-58	O-linked N-acetylglucosamine					Thr-58	Previously, we reported that c-Myc is glycosylated by O-linked N-acetylglucosamine at Thr-58, a known phosphorylation site and a mutational hot spot in lymphomas.
11904304	1	25	gly	glycosylated	263:274	arg1	c-Myc	c-Myc				PUBTATOR		c-Myc	4609		Previously, we reported that c-Myc is glycosylated by O-linked N-acetylglucosamine at Thr-58, a known phosphorylation site and a mutational hot spot in lymphomas.
18795891	0	27	part_of	tetraspanin	106:116	arg1	tetraspanin microdomains	tetraspanin		tetraspanin microdomains		Fterm	Site	tetraspanin		microdomains	Identification of Tspan9 as a novel platelet tetraspanin and the collagen receptor GPVI as a component of tetraspanin microdomains.
3200844	11	4	part_of	glycoprotein	1571:1582	arg1	The partial sequence	glycoprotein		The partial sequence		Fterm	Site	glycoprotein		sequence	The partial sequence of the 62-kDa nuclear pore glycoprotein shows little similarity to other characterized proteins and elucidates structural features of a member of the family of nuclear pore glycoproteins.
9054441	8	23	gly	plasminogen	1365:1375	arg1	sialylation	plasminogen			sialylation	OGER		plasminogen	P00747		These findings provide a structural basis for some of the observed microheterogeneity, and have implications with regard to the known functional consequences of the extent of sialylation of plasminogen.
9054441	8	55	gly	sialylation	1350:1360	arg1	plasminogen	plasminogen				OGER		plasminogen	P00747		These findings provide a structural basis for some of the observed microheterogeneity, and have implications with regard to the known functional consequences of the extent of sialylation of plasminogen.
16002699	6	3	gly	glycosylation	881:893	arg2	the N78 and N110 glycosylation sites			the N78 and N110 glycosylation sites						sites	C122-independent dimerization of CTLA-4 involved N-glycosylation, because further mutation of the N78 and N110 glycosylation sites abrogated dimerization.
12970363	11	35	gly	glycosylated	1655:1666	arg1	an additional second glycosylated site			an additional second glycosylated site						site	Reciprocally, engineering of an additional second glycosylated site in TRPC3 to mimic the glycosylation status in TRPC6 markedly reduced TRPC3 basal activity.
21712440	9	91	part_of	protein	1767:1773	arg1	a Tyr residue	protein		a Tyr residue		Fterm	AminoAcid	protein		Tyr residue	APP/Aβ sialylated O-glycans, including that of a Tyr residue, the first in a mammalian protein, may modulate APP processing, inhibiting the amyloidogenic pathway associated with AD.
11320094	4	68	part_of	contains	818:825	arg1	ABCR AND eight glycosylation sites	ABCR		eight glycosylation sites		PUBTATOR	Site	ABCR	24	sites	Using trypsin digestion, site-directed mutagenesis, concanavalin A binding, and endoglycosidase digestion, we show that ABCR contains eight glycosylation sites.
8407981	1	64	part_of	P-450	111:115	arg1	N terminus	cytochrome P-450		N terminus		PUBTATOR	Site	cytochrome P-450	4051	terminus	Evidence for localization of N terminus of microsomal cytochrome P-450 in the lumen.
16037490	7	70	gly	sites	1711:1715	arg1	N-glycan structures			sites	N-glycan structures					sites	In addition, the method was applied to apolipoprotein B-100 (apoB100) whose N-glycan structures at 17 of 19 potential sites have been reported, and characterized the remaining sites.
11258925	8	7	gly	peptides	1293:1300	arg1	Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587			Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587						Asn 396-Arg 414	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	7	gly	peptides	1293:1300	arg1	Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587			Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587						Thr 576-Arg 587	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	7	gly	peptides	1293:1300	arg1	GlcNAc containing Asn 580			GlcNAc containing Asn 580						Asn 580	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	54	gly	glycosylation	1213:1225	arg2	the Asn 53 and Asn 130 sites			Asn 53 and Asn 130 sites						Asn 53 and Asn 130 sites	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	54	gly	glycosylation	1213:1225	arg1	the Asn 53 and Asn 130 sites			Asn 53 and Asn 130 sites						Asn 53 and Asn 130 sites	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	54	gly	glycosylation	1213:1225	arg1	the Asn 53 and Asn 130 sites			Asn 53 and Asn 130 sites						Asn 53 and Asn 130 sites	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	54	gly	glycosylation	1213:1225	arg1	the Asn 53 and Asn 130 sites			Asn 53 and Asn 130 sites						Asn 53 and Asn 130 sites	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	54	gly	glycosylation	1213:1225	arg1	the Asn 53 and Asn 130 sites			Asn 53 and Asn 130 sites						Asn 53 and Asn 130 sites	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	54	gly	glycosylation	1213:1225	arg1	the Asn 53 and Asn 130 sites			Asn 53 and Asn 130 sites						Asn 53 and Asn 130 sites	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
22333914	4	48	part_of	extracellular	804:816	arg1	the only extracellular domain	r		the only extracellular domain		PUBTATOR	Site	r	151	domain	The GAIN domain is evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations.
3567160	0	6	gly	G	110:110	arg1	the N-linked oligosaccharides	human normal and pathological immunoglobulin G			the N-linked oligosaccharides	Cterm		human normal and pathological immunoglobulin G			Comparative structural study of the N-linked oligosaccharides of human normal and pathological immunoglobulin G.
26828122	0	27	gly	glycoprotein	66:77	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			The human colonic thiamine pyrophosphate transporter (hTPPT) is a glycoprotein and N-linked glycosylation is important for its function.
20511397	0	48	gly	Glycosylation	0:12	arg1	macrophage-derived human apolipoprotein E	macrophage-derived human apolipoprotein E				PUBTATOR		apolipoprotein E	348		Glycosylation and sialylation of macrophage-derived human apolipoprotein E analyzed by SDS-PAGE and mass spectrometry: evidence for a novel site of glycosylation on Ser290.
20511397	0	55	gly	E	73:73	arg1	sialylation	apolipoprotein E			sialylation	PUBTATOR		apolipoprotein E	348		Glycosylation and sialylation of macrophage-derived human apolipoprotein E analyzed by SDS-PAGE and mass spectrometry: evidence for a novel site of glycosylation on Ser290.
20511397	0	59	gly	sialylation	18:28	arg1	macrophage-derived human apolipoprotein E	macrophage-derived human apolipoprotein E				PUBTATOR		apolipoprotein E	348		Glycosylation and sialylation of macrophage-derived human apolipoprotein E analyzed by SDS-PAGE and mass spectrometry: evidence for a novel site of glycosylation on Ser290.
20511397	0	73	gly	glycosylation	148:160	arg2	a novel site			a novel site						site	Glycosylation and sialylation of macrophage-derived human apolipoprotein E analyzed by SDS-PAGE and mass spectrometry: evidence for a novel site of glycosylation on Ser290.
21752865	11	20	gly	N-glycosylated	1756:1769	arg1	BRI2	BRI2		Asn170		PUBTATOR		BRI2	9445	Asn170	Our results confirm the theoretical predictions that BRI2 is N-glycosylated at Asn170 and show that this post-translational modification is essential for its expression at the cell surface but not for its proteolytic processing.
18715980	3	50	gly	proteins	542:549	arg1	various N-linked carbohydrates	SPINKL proteins			various N-linked carbohydrates	PUBTATOR		SPINKL proteins	77424		Further analysis identified several SPINKL proteins with various N-linked carbohydrates.
9030779	7	9	gly	glycosylation	875:887	arg2	glycosylation site five			glycosylation site five						site	Absence of glycosylation site five resulted in rapid cleavage of the primary translation product to an enzymatically inactive protein which accumulated inside the endoplasmic reticulum/Golgi, whereas deletion of glycosylation site six led to the formation of an inactive ASM precursor, also retained inside the endoplasmic reticulum/Golgi.
9030779	7	33	gly	glycosylation	1076:1088	arg2	glycosylation site six			glycosylation site six						site	Absence of glycosylation site five resulted in rapid cleavage of the primary translation product to an enzymatically inactive protein which accumulated inside the endoplasmic reticulum/Golgi, whereas deletion of glycosylation site six led to the formation of an inactive ASM precursor, also retained inside the endoplasmic reticulum/Golgi.
6833285	13	58	part_of	possesses	1530:1538	arg1	the B-chain AND a short alpha-helical region	the B-chain		a short alpha-helical region		Fterm	Site	B-chain		region	In agreement with the CD analysis, the B-chain lacks beta-conformation but possesses a short alpha-helical region.
2808371	0	51	part_of	isoforms	76:83	arg1	discrete peptide	protein 4.1 isoforms		discrete peptide		PUBTATOR	Site	protein 4.1 isoforms	281753	peptide	O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.
2513186	0	45	gly	activator	71:79	arg1	Carbohydrate structure	tissue plasminogen activator			Carbohydrate structure	PUBTATOR		tissue plasminogen activator	P00750		Carbohydrate structure of recombinant human uterine tissue plasminogen activator expressed in mouse epithelial cells.
23050552	9	69	part_of	regions	1167:1173	arg1	human fibrinogen	fibrinogen		regions		PUBTATOR	Site	fibrinogen	2244	regions	Moreover, we describe seven novel O-glycosylation regions in human fibrinogen, all occupied by a monosialylated T-antigen.
21733844	5	35	gly	Nonglycosylated	679:693	arg1	Nonglycosylated protein	Nonglycosylated protein				Fterm		protein			Nonglycosylated protein was isolated using both glycan affinity chromatography and through mutating asparagine 133 to a glutamine.
10889209	3	5	part_of	have	493:496	arg1	GIRK4 AND one extracellular consensus N-glycosylation site	GIRK4		one extracellular consensus N-glycosylation site		PUBTATOR	Site	GIRK4	3762	site	Both GIRK1 and GIRK4 have one extracellular consensus N-glycosylation site.
10889209	3	5	part_of	have	493:496	arg1	GIRK1 AND one extracellular consensus N-glycosylation site	GIRK1		one extracellular consensus N-glycosylation site		PUBTATOR	Site	Both GIRK1	3760	site	Both GIRK1 and GIRK4 have one extracellular consensus N-glycosylation site.
29402915	7	58	gly	glycosylation	1340:1352	arg1	cubilin protein	cubilin protein		residues		PUBTATOR		cubilin protein	8029	residues	Quantitative mass spectrometry and mutagenesis demonstrated that N-linked glycosylation of at least 4 residues of cubilin protein was required for its surface targeting.
29757379	6	52	gly	glycosylation	871:883	arg2	a highly conserved N-linked glycosylation site			a highly conserved N-linked glycosylation site						site	We found a highly conserved N-linked glycosylation site to be required for QSOX1 secretion from fibroblasts and other cell types.
8243461	6	19	gly	deglycosylation	1288:1302	arg1	bovine factor X1	bovine factor X1				Cterm		factor X1			The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
3442327	0	13	gly	glycoproteins	106:118	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Identification method for twelve oligomannose-type sugar chains thought to be processing intermediates of glycoproteins.
3463996	5	26	gly	glycosylation	1099:1111	arg2	a potential glycosylation site			a potential glycosylation site						site	In particular, two conserved sequences in the propeptide that may be functionally significant include a potential glycosylation site and the presence of a single cysteine at position 59.
3463996	5	26	gly	glycosylation	1099:1111	arg2	position 59			cysteine at position 59						cysteine at position 59	In particular, two conserved sequences in the propeptide that may be functionally significant include a potential glycosylation site and the presence of a single cysteine at position 59.
3463996	5	26	gly	glycosylation	1099:1111	arg2	a single cysteine			cysteine at position 59						cysteine at position 59	In particular, two conserved sequences in the propeptide that may be functionally significant include a potential glycosylation site and the presence of a single cysteine at position 59.
3463996	5	26	gly	glycosylation	1099:1111	arg2	a single cysteine			cysteine at position 59						cysteine at position 59	In particular, two conserved sequences in the propeptide that may be functionally significant include a potential glycosylation site and the presence of a single cysteine at position 59.
18340083	0	43	gly	Glycosylation	0:12	arg1	Asn-76			Asn-76						Asn-76	Glycosylation of Asn-76 in mouse GPIHBP1 is critical for its appearance on the cell surface and the binding of chylomicrons and lipoprotein lipase.
21669976	2	0	gly	O-glycosylated	252:265	arg1	the KCNE1 regulatory subunit	the KCNE1 regulatory subunit				Fterm		subunit			Here, we show the KCNE1 regulatory subunit is O-glycosylated with mucin-type glycans in vivo.
25802287	6	3	gly	glycosites	1013:1022	arg2	distinct glycosites			distinct glycosites						glycosites	Mining for distinct glycosites is performed by searching for the predicted deglycosylated peptides in the treated trace.
25802287	6	111	gly	deglycosylated	1068:1081	arg1	the predicted deglycosylated peptides			the predicted deglycosylated peptides						peptides	Mining for distinct glycosites is performed by searching for the predicted deglycosylated peptides in the treated trace.
7107587	12	15	part_of	fibrinogen	1334:1343	arg1	the glycopeptides	fibrinogen		the glycopeptides		PUBTATOR	Site	fibrinogen	2244	glycopeptides	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
17614963	0	31	part_of	fibronectin	24:34	arg1	novel fibronectin fragments	fibronectin		novel fibronectin fragments		PUBTATOR	Site	fibronectin	2335	fragments	Identification of novel fibronectin fragments detected specifically in juvenile urine.
6619126	12	3	part_of	Ser	1873:1875	arg1	the donor LG glycoprotein	glycoprotein		Ser		Fterm	AminoAcid	glycoprotein		Ser	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
20378933	7	47	gly	deglycosylation	1115:1129	arg2	N58			N58						N58	Flow cytometry analysis of IgA binding to CHO cells transfected with mutated FcalphaR showed that deglycosylation of FcalphaR at individual N44, N120, N156, N165 or N177 site did not affect IgA binding but deglycosylation at N58 resulted in marked increase of IgA binding.
20378933	7	84	gly	deglycosylation	1007:1021	arg1	IgA binding	IgA		N44, N120, N156, N165		OGER		IgA	P11912	N44, N120, N156, N165	Flow cytometry analysis of IgA binding to CHO cells transfected with mutated FcalphaR showed that deglycosylation of FcalphaR at individual N44, N120, N156, N165 or N177 site did not affect IgA binding but deglycosylation at N58 resulted in marked increase of IgA binding.
20378933	7	84	gly	deglycosylation	1007:1021	arg1	N120, N156, N165 or N177 site	IgA		N177 site		OGER		IgA	P11912	N177 site	Flow cytometry analysis of IgA binding to CHO cells transfected with mutated FcalphaR showed that deglycosylation of FcalphaR at individual N44, N120, N156, N165 or N177 site did not affect IgA binding but deglycosylation at N58 resulted in marked increase of IgA binding.
1567356	4	80	gly	variants	672:679	arg1	the glycan structures	variants			the glycan structures	Fterm		variants			The ability to quantify the glycoforms present at each site allows us to extend the earlier results of others and resolve the remaining questions concerning the glycan structures of these variants.
3542989	4	8	part_of	terminus	452:459	arg1	the 198th residue	terminus		the 198th residue						residue	The active site serine is the 198th residue from the amino terminus.
3542989	4	8	part_of	terminus	452:459	arg1	The active site serine	terminus		The active site serine						serine	The active site serine is the 198th residue from the amino terminus.
8202534	7	20	gly	glycoprotein	1055:1066	arg1	the complete glycoprotein structure	the complete glycoprotein structure				Fterm		glycoprotein			The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	7	26	gly	homogeneity	986:996	arg1	SAP	SAP				PUBTATOR		SAP	325		The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	7	47	gly	SAP	1001:1003	arg1	The protein and glycan homogeneity	SAP			The protein and glycan homogeneity	PUBTATOR		SAP	325		The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
17525160	0	45	gly	glycosylation	9:21	arg2	threonine 27			threonine 27						threonine 27	O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.
12731890	4	10	gly	glycosylation	879:891	arg1	an atypical NNC site			an atypical NNC site						site	We also confirm the partial glycosylation of an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells.
1883960	1	59	gly	phosphoglycoproteins	339:358	arg1	differentially modified phosphoglycoproteins	differentially modified phosphoglycoproteins				Fterm		phosphoglycoproteins			Human interleukin-6 (IL-6) secreted by cytokine- or endotoxin-induced fibroblasts, monocytes, keratinocytes, endometrial stromal cells, and endothelial cells, when analyzed under denaturing and reducing conditions, consists of a set of differentially modified phosphoglycoproteins of molecular mass in the range from 23 to 30 kD (a set of at least three O-glycosylated 23- to 25-kD species and a set of at least three N- and O-glycosylated 28- to 30-kD species).
23661698	7	29	gly	glycosylation	993:1005	arg2	the glycosylation site			the glycosylation site						site	Mutations in the glycosylation site on ephrin-A1 result in protein aggregation and mislocalization.
28279966	3	6	part_of	metalloproteinase	487:503	arg1	thrombospondin type 1 motif	metalloproteinase		thrombospondin type 1 motif		Fterm	Site	metalloproteinase		motif	Interestingly, plasmin has been successfully used as an alternative to ADAMTS13 (a disintegrin and metalloproteinase with thrombospondin type 1 motif) in a mouse model of thrombotic thrombocytopenic purpura.
28279966	3	27	part_of	type	525:528	arg1	thrombospondin type 1 motif	thrombospondin type 1		thrombospondin type 1 motif		OGER	Site	thrombospondin type 1	P35441	motif	Interestingly, plasmin has been successfully used as an alternative to ADAMTS13 (a disintegrin and metalloproteinase with thrombospondin type 1 motif) in a mouse model of thrombotic thrombocytopenic purpura.
28279966	3	30	part_of	disintegrin	471:481	arg1	thrombospondin type 1 motif	disintegrin		thrombospondin type 1 motif		Fterm	Site	disintegrin		motif	Interestingly, plasmin has been successfully used as an alternative to ADAMTS13 (a disintegrin and metalloproteinase with thrombospondin type 1 motif) in a mouse model of thrombotic thrombocytopenic purpura.
9450956	11	25	part_of	protein	1370:1376	arg1	the protein recognition motif	protein		the protein recognition motif		Fterm	Site	protein		motif	The frequent occurrence of the protein recognition motif suggests that C-glycosides could be part of the structure of more proteins than assumed so far.
8243461	2	69	part_of	protease-digested	290:306	arg1	protease-digested glycopeptides	protease		protease-digested glycopeptides		Fterm	Site	protease		glycopeptides	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	2	71	part_of	peptides	490:497	arg1	sites	peptides		sites						sites	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	2	99	part_of	X	404:404	arg1	the activation peptides	factor X		the activation peptides		OGER	Site	factor X	P00742	peptides	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
18586680	4	45	part_of	Asp-413	773:779	arg1	human O-GlcNAcase	O-GlcNAcase		Asp-413		PUBTATOR	SpecificSite	O-GlcNAcase	10724	Asp-413	The caspase-3 cleavage site of O-GlcNAcase, mapped by Edman sequencing, is a noncanonical recognition site that occurs after Asp-413 of the SVVD sequence in human O-GlcNAcase.
18586680	4	3	part_of	caspase-3	652:660	arg1	The caspase-3 cleavage site	caspase-3		site		PUBTATOR	Site	caspase-3	836	site	The caspase-3 cleavage site of O-GlcNAcase, mapped by Edman sequencing, is a noncanonical recognition site that occurs after Asp-413 of the SVVD sequence in human O-GlcNAcase.
18586680	4	41	part_of	O-GlcNAcase	679:689	arg1	The caspase-3 cleavage site	O-GlcNAcase		site		PUBTATOR	Site	O-GlcNAcase	10724	site	The caspase-3 cleavage site of O-GlcNAcase, mapped by Edman sequencing, is a noncanonical recognition site that occurs after Asp-413 of the SVVD sequence in human O-GlcNAcase.
9136890	1	78	gly	has	137:139	arg1	TfR AND three N-linked oligosaccharides	TfR			three N-linked oligosaccharides	PUBTATOR		TfR	7037		The human transferrin receptor (TfR) has three N-linked oligosaccharides.
9136890	1	78	gly	has	137:139	arg1	The human transferrin receptor AND three N-linked oligosaccharides	The human transferrin receptor			three N-linked oligosaccharides	PUBTATOR		transferrin receptor	7037		The human transferrin receptor (TfR) has three N-linked oligosaccharides.
24841998	7	12	part_of	proteins	1036:1043	arg1	total 27 N-glycosylation sites	proteins		total 27 N-glycosylation sites		Fterm	Site	proteins		sites	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
24841998	7	19	part_of	proteins	1065:1072	arg1	total 27 N-glycosylation sites	proteins		total 27 N-glycosylation sites		Fterm	Site	proteins		sites	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
8757293	5	38	part_of	sites	835:839	arg1	the related proteinase	proteinase		sites		PUBTATOR	Site	proteinase	100616102	sites	In general, the substrate binding sites, S4 to S3', are more polar than comparable sites in the related proteinase, human leukocyte elastase.
8757293	5	38	part_of	sites	835:839	arg1	human leukocyte elastase	human leukocyte elastase		sites		OGER	Site	human leukocyte elastase	P08246	sites	In general, the substrate binding sites, S4 to S3', are more polar than comparable sites in the related proteinase, human leukocyte elastase.
25456591	8	85	gly	glycosylation	1411:1423	arg2	26 glycosylation sites			26 glycosylation sites						sites	A total of 26 glycosylation sites each of which corresponds to 1-4 glycans were positively mapped and confirmed.
14573609	2	25	part_of	heparanase	301:310	arg1	The predicted amino acid sequence	heparanase		The predicted amino acid sequence		PUBTATOR	Site	heparanase	10855	sequence	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
10092871	3	71	gly	unglycosylated	456:469	arg1	MMP-1	MMP-1				PUBTATOR		MMP-1	4312		MMP-1 is secreted as both glycosylated and unglycosylated species, and the two forms have been shown to be identical with respect to substrate specificity, specific activity and inhibitory profile.
10092871	3	82	gly	glycosylated	439:450	arg1	MMP-1	MMP-1				PUBTATOR		MMP-1	4312		MMP-1 is secreted as both glycosylated and unglycosylated species, and the two forms have been shown to be identical with respect to substrate specificity, specific activity and inhibitory profile.
8130392	3	53	gly	rHPC	570:573	arg1	the carbohydrate moiety	rHPC			the carbohydrate moiety	OGER		rHPC	P52873		In seeking to elucidate the molecular basis for the improved efficacy of the recombinant antithrombotic drug, we focused on the carbohydrate moiety of rHPC.
25759508	8	19	gly	N-glycosylation	1214:1228	arg1	the Fc CH2 domain			the Fc CH2 domain						domain	For IgG3 samples from six donors we found similar O-glycan structures and site occupancies, whereas for the same samples the conserved N-glycosylation of the Fc CH2 domain showed considerable interindividual variation.
19838169	4	1	gly	glycosylation	604:616	arg2	36 N-linked and 44 O-linked glycosylation sites			36 N-linked and 44 O-linked glycosylation sites						sites	We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
19838169	4	32	gly	glycoproteins	627:639	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
7780197	6	35	part_of	found	886:890	arg2	the TfR AND Asn-727	the TfR		Asn-727		PUBTATOR	SpecificSite	TfR	7037	Asn-727	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
29992770	5	12	gly	N-glycopeptides	748:762	arg2	the statistically significantly different N-glycopeptides			the statistically significantly different N-glycopeptides						N-glycopeptides	Quantitative label-free N-glycoproteomics is performed, with MS/MS analysis of the statistically significantly different N-glycopeptides.
28973932	4	20	part_of	EC	1099:1100	arg1	EC domains	EC		EC domains		Cterm	Site	EC	Q8NE62	domains	KO of all four TMTC genes in HEK293 cells resulted in specific loss of cdh and pcdh O-Man glycosylation, whereas combined KO of TMTC1 and TMTC3 resulted in selective loss of O-Man glycans on specific β-strands of EC domains, suggesting that each isoenzyme serves a different function.
21669976	3	45	gly	glycosylation	312:324	arg2	O-linked glycosylation sites			O-linked glycosylation sites						sites	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
16497731	6	11	gly	glycosylation	1002:1014	arg1	multiple conserved proline and lysine residues			proline and lysine residues						proline and lysine residues	PTMs identified in murine and bovine adiponectin include hydroxylation of multiple conserved proline and lysine residues and glycosylation of hydroxylysines.
1381905	12	34	gly	glycosylation	1926:1938	arg1	receptor binding	receptor binding				Fterm		receptor			The N-linked glycosylation, particularly that at Asn93 and at Asn65, adversely affects in vitro biological activity and receptor binding.
11912203	10	35	gly	glycosylation	1606:1618	arg1	the four lysines			the four lysines						lysines	These results indicate that full-length adiponectin produced by mammalian cells is functionally active as an insulin sensitizer and that hydroxylation and glycosylation of the four lysines in the collagenous domain might contribute to this activity.
11912203	10	48	gly	glycosylation	1606:1618	arg1	the collagenous domain			domain						domain	These results indicate that full-length adiponectin produced by mammalian cells is functionally active as an insulin sensitizer and that hydroxylation and glycosylation of the four lysines in the collagenous domain might contribute to this activity.
4091823	16	13	gly	glycoprotein	1810:1821	arg1	glycoprotein molecules	glycoprotein molecules				Fterm		glycoprotein			do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
24721674	6	24	gly	N-glycosylation	1347:1361	arg2	811 N-glycosylation sites			811 N-glycosylation sites						sites	200μg total protein digest was processed using this approach, leading to the identification of 811 N-glycosylation sites from 567 proteins within two experimental replicates.
21173149	7	9	gly	N-glycosylation	936:950	arg2	positions 88 and 115			positions 88 and 115						positions 88 and 115,	The γ-subunit contains two in vivo used N-glycosylation sites at positions 88 and 115, equipped with high mannose-type oligosaccharides.
21173149	7	9	gly	N-glycosylation	936:950	arg2	two in vivo used N-glycosylation sites			two in vivo used N-glycosylation sites						sites	The γ-subunit contains two in vivo used N-glycosylation sites at positions 88 and 115, equipped with high mannose-type oligosaccharides.
9852066	5	29	gly	glycosylation	1106:1118	arg2	Three O-linked glycosylation sites			Three O-linked glycosylation sites						sites	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
18988733	4	0	part_of	p65	721:723	arg1	Thr-322	NFkappaB p65		Thr-322 and Thr-352		PUBTATOR	SpecificSite	NFkappaB p65	4790	Thr-322 and Thr-352	Also, we demonstrate that both Thr-322 and Thr-352 of NFkappaB p65 can be modified with O-GlcNAc, but modification on Thr-352, not Thr-322, is important for transcriptional activation.
24161696	6	55	gly	glycosylated	1187:1198	arg1	the fully glycosylated and partially glycosylated N229Q Kv3.1b proteins	the fully glycosylated and partially glycosylated N229Q Kv3.1b proteins				Fterm		proteins			Further both the fully glycosylated and partially glycosylated N229Q Kv3.1b proteins formed higher density particles in outgrowths compared to cell body.
24161696	6	112	gly	glycosylated	1214:1225	arg1	the fully glycosylated and partially glycosylated N229Q Kv3.1b proteins	the fully glycosylated and partially glycosylated N229Q Kv3.1b proteins				Fterm		proteins			Further both the fully glycosylated and partially glycosylated N229Q Kv3.1b proteins formed higher density particles in outgrowths compared to cell body.
23027977	1	23	gly	glycoprotein	139:150	arg1	Enpp1	Enpp1				PUBTATOR		Enpp1	5167		Enpp1 is a membrane-bound glycoprotein that regulates bone mineralization by hydrolyzing extracellular nucleotide triphosphates to produce pyrophosphate.
23027977	1	23	gly	glycoprotein	139:150	arg1	a membrane-bound glycoprotein	a membrane-bound glycoprotein				Fterm		glycoprotein			Enpp1 is a membrane-bound glycoprotein that regulates bone mineralization by hydrolyzing extracellular nucleotide triphosphates to produce pyrophosphate.
7068558	0	9	gly	asparagine-linked	94:110	arg1	four novel complex-type asparagine-linked sugar chains			asparagine	four novel complex-type asparagine-linked sugar chains					asparagine	Structural study of the sugar chains of human lactoferrin: finding of four novel complex-type asparagine-linked sugar chains.
7068558	0	44	gly	lactoferrin	46:56	arg1	the sugar chains	lactoferrin			the sugar chains	OGER		lactoferrin	P02788		Structural study of the sugar chains of human lactoferrin: finding of four novel complex-type asparagine-linked sugar chains.
18214858	4	50	gly	fucosylated	834:844	arg1	total fucosylated di-				total fucosylated di-						Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	4	60	gly	haptoglobin	886:896	arg1	tri-	haptoglobin			tri-	PUBTATOR		haptoglobin	3240		Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	4	60	gly	haptoglobin	886:896	arg1	tetra-branched glycans	haptoglobin			tetra-branched glycans	PUBTATOR		haptoglobin	3240		Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	4	60	gly	haptoglobin	886:896	arg1	total fucosylated di-	haptoglobin			total fucosylated di-	PUBTATOR		haptoglobin	3240		Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
17286803	10	56	part_of	CLN3	1489:1492	arg1	different cytoplasmic domains	CLN3		different cytoplasmic domains		OGER	Site	CLN3	Q13286	domains	The data suggest that co-operative signal structures in different cytoplasmic domains of CLN3 are required for efficient sorting and for transport to the lysosome.
7263706	1	10	part_of	gamma-subunit	138:150	arg1	The complete amino acid sequence	gamma-subunit		The complete amino acid sequence		Fterm	Site	gamma-subunit		sequence	The complete amino acid sequence of the gamma-subunit of mouse submaxillary gland 7 S nerve growth factor has been determined from analyses of the peptides generated by cyanogen bromide, trypsin, and chymotrypsin from the naturally occurring fragments.
15340146	8	23	gly	O-GlcNAc-glycosylated	1177:1197	arg1	25 O-GlcNAc-glycosylated proteins	proteins			25 O-GlcNAc-glycosylated proteins	Fterm		proteins			Using this approach, we discovered 25 O-GlcNAc-glycosylated proteins from the brain, including regulatory proteins associated with gene expression, neuronal signaling, and synaptic plasticity.
3665914	2	39	gly	polysialoglycoprotein	349:369	arg1	polysialoglycoprotein	polysialoglycoprotein				Fterm		polysialoglycoprotein			An oligosaccharide alditol, dHex-GalNAc-Gal-Gal-GalNAcol, has been isolated from polysialoglycoprotein, which was derived from the unfertilized eggs of Savelinus leucomaenis pluvius (a salmonid fish, Iwana in Japanese), by alkaline borohydride treatment followed by exhaustive digestion with sialidase.
3665914	2	50	gly	isolated	335:342	arg1	polysialoglycoprotein AND dHex-GalNAc-Gal-Gal-GalNAcol	polysialoglycoprotein			dHex-GalNAc-Gal-Gal-GalNAcol	Fterm		polysialoglycoprotein			An oligosaccharide alditol, dHex-GalNAc-Gal-Gal-GalNAcol, has been isolated from polysialoglycoprotein, which was derived from the unfertilized eggs of Savelinus leucomaenis pluvius (a salmonid fish, Iwana in Japanese), by alkaline borohydride treatment followed by exhaustive digestion with sialidase.
3665914	2	50	gly	isolated	335:342	arg1	polysialoglycoprotein AND An oligosaccharide alditol	polysialoglycoprotein			An oligosaccharide alditol	Fterm		polysialoglycoprotein			An oligosaccharide alditol, dHex-GalNAc-Gal-Gal-GalNAcol, has been isolated from polysialoglycoprotein, which was derived from the unfertilized eggs of Savelinus leucomaenis pluvius (a salmonid fish, Iwana in Japanese), by alkaline borohydride treatment followed by exhaustive digestion with sialidase.
9030779	8	61	gly	glycosylation	1352:1364	arg2	the second and third glycosylation sites			the second and third glycosylation sites						sites	Our results also provide evidence that the site of early proteolytic cleavage of newly synthesized ASM must be located between the second and third glycosylation sites.
19561611	5	27	part_of	Ca2+	820:823	arg1	the Hh Zn2+ and Ca2+ binding sites--functions	Ca2		the Hh Zn2+ and Ca2+ binding sites--functions		OGER	Site	Ca2	P00918	sites--functions	The interaction determinants, confirmed by biophysical studies and mutagenesis, reveal previously uncharacterized and distinct functions for the Hh Zn2+ and Ca2+ binding sites--functions that may be common to all vertebrate Hh proteins.
1456441	4	27	gly	glycopeptide	613:624	arg2	glycopeptide			glycopeptide						glycopeptide	The glycopeptide fractions were then individually digested with N-glycanase.
23376777	3	88	gly	glycosylation	393:405	arg2	the four putative extracellular N-linked glycosylation sites	KCC4		sites		PUBTATOR		KCC4	20499	sites	Site-directed mutagenesis was performed on the four putative extracellular N-linked glycosylation sites of KCC4 to determine the role of these sites in KCC4 half-life, cell surface expression, and transporter activity, as well as in KCC4-dependent tumor formation.
30301806	5	51	part_of	NAAA	877:880	arg1	the otherwise buried active site	NAAA		the otherwise buried active site		PUBTATOR	Site	NAAA	27163	site	Self-proteolysis exposes the otherwise buried active site of NAAA to allow catalysis.
2498325	4	56	gly	glycosylated	570:581	arg1	asialo-apoE	asialo-apoE				PUBTATOR		apoE	348		Sequence analysis and amino sugar analysis of this peptide derived from asialo-, monosialo-, or disialo-apoE indicated that the carbohydrate moiety is attached only to Thr194 in monosialo- and disialo-apoE and that asialo-apoE is not glycosylated.
2498325	4	89	gly	attached	487:494	arg2	Thr194 AND the carbohydrate moiety			Thr194	the carbohydrate moiety					Thr194	Sequence analysis and amino sugar analysis of this peptide derived from asialo-, monosialo-, or disialo-apoE indicated that the carbohydrate moiety is attached only to Thr194 in monosialo- and disialo-apoE and that asialo-apoE is not glycosylated.
2393398	7	25	gly	attachment	1020:1029	arg1	the peptide AND fucose			the peptide	fucose					peptide	The site of attachment of fucose to the peptide has been localized towards the N-terminus (within first 23 amino acids) of the protein.
7106126	2	55	gly	glycosylation	297:309	arg2	The glycosylation sites			The glycosylation sites						sites	The glycosylation sites were identified by a new procedure for the detection of the glycosylated derivatives released by Edman degradation.
3514617	6	120	part_of	CNBr	645:648	arg1	the CNBr fragments	CNBr		the CNBr fragments		Cterm	Site	CNBr		fragments	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
12901863	4	11	part_of	site	599:602	arg1	ABCC6	ABCC6		site		PUBTATOR	Site	ABCC6	368	site	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
9343410	4	13	part_of	Sp1	696:698	arg1	the model Sp1 peptide	Sp1		the model Sp1 peptide		OGER	Site	Sp1	Q8N907	peptide	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	4	52	part_of	Sp1	773:775	arg1	this 97-amino-acid domain	Sp1		this 97-amino-acid domain		OGER	Site	Sp1	Q8N907	domain	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
6619126	14	101	gly	glycoprotein	2432:2443	arg1	the major glycoprotein	glycoprotein			N-linked carbohydrate units	Fterm		glycoprotein			The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
7841792	4	42	part_of	Casebrook	694:702	arg1	glycopeptide	albumin Casebrook		glycopeptide		OGER	Site	albumin Casebrook	P02768	glycopeptide	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
20511397	5	58	part_of	Thr	1037:1039	arg1	both cellular and secreted apoE	apoE		Thr		PUBTATOR	SpecificSite	apoE	348	Thr(194)	Our results identify eight different glycoforms with (HexNAc)(2)-Hex(2)-(NeuAc)(2) being the most complex glycan detected on Thr(194) in both cellular and secreted apoE.
21712440	0	36	gly	glycosylations	66:79	arg1	amyloid precursor protein/amyloid beta-peptides			amyloid precursor protein/amyloid beta-peptides						beta-peptides	Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid beta-peptides in human cerebrospinal fluid.
8323299	1	53	gly	glycosylated	198:209	arg1	The lysosomal membrane glycoproteins	The lysosomal membrane glycoproteins				Fterm		glycoproteins			The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	53	gly	glycosylated	198:209	arg1	lamp-2	lamp-2				PUBTATOR		lamp-2	3920		The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	53	gly	glycosylated	198:209	arg1	lamp-1	lamp-1				PUBTATOR		lamp-1	3916		The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	69	gly	glycoproteins	150:162	arg1	The lysosomal membrane glycoproteins	The lysosomal membrane glycoproteins				Fterm		glycoproteins			The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	69	gly	glycoproteins	150:162	arg1	lamp-2	lamp-2				PUBTATOR		lamp-2	3920		The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	69	gly	glycoproteins	150:162	arg1	lamp-1	lamp-1				PUBTATOR		lamp-1	3916		The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
1326557	10	67	gly	utilized	2238:2245	arg2	three additional potential chondroitin sulfate attachment sites			three additional potential chondroitin sulfate attachment sites						sites	In the adult form of the proteoglycan (which represents the C-terminal half of neurocan) a single 32-kDa chondroitin 4-sulfate chain is linked at serin-944, whereas three additional potential chondroitin sulfate attachment sites (only two of which are utilized) are present in the larger proteoglycan species.
30392906	6	33	gly	glycosylation	705:717	arg2	a unique glycosylation site			a unique glycosylation site						site	Unexpectedly, we found Asn50 is a unique glycosylation site and the glycosylation mediates its interaction with ConA.
30392906	6	33	gly	glycosylation	705:717	arg2	Asn50			Asn50						Asn50	Unexpectedly, we found Asn50 is a unique glycosylation site and the glycosylation mediates its interaction with ConA.
19153605	4	11	part_of	F-spondin	479:487	arg1	an N-terminal F-spondin (FS) domain	N-terminal F-spondin		an N-terminal F-spondin (FS) domain		PUBTATOR	Site	N-terminal F-spondin	10418	domain	Mindin comprises an N-terminal F-spondin (FS) domain and C-terminal thrombospondin type 1 repeat (TSR).
19153605	4	16	part_of	N-terminal	468:477	arg1	an N-terminal F-spondin (FS) domain	N-terminal F-spondin		an N-terminal F-spondin (FS) domain		PUBTATOR	Site	N-terminal F-spondin	10418	domain	Mindin comprises an N-terminal F-spondin (FS) domain and C-terminal thrombospondin type 1 repeat (TSR).
19153605	4	19	part_of	FS	490:491	arg1	an N-terminal F-spondin (FS) domain	FS		an N-terminal F-spondin (FS) domain		Cterm	Site	FS	10418	domain	Mindin comprises an N-terminal F-spondin (FS) domain and C-terminal thrombospondin type 1 repeat (TSR).
20934432	6	45	part_of	IFN	765:767	arg1	the IFN site	IFN		the IFN site		PUBTATOR	Site	IFN	3439	site	The ligand-receptor interface includes helix A, loop AB, and helix F on the IFN site, as well as loops primarily from the N-terminal domain and inter-domain hinge region of IFN-λR1.
20934432	6	53	part_of	IFN-λR1	862:868	arg1	inter-domain hinge region	IFN-λR1		inter-domain hinge region		PUBTATOR	Site	IFN-λR1	163702	region	The ligand-receptor interface includes helix A, loop AB, and helix F on the IFN site, as well as loops primarily from the N-terminal domain and inter-domain hinge region of IFN-λR1.
20934432	6	53	part_of	IFN-λR1	862:868	arg1	the N-terminal domain	IFN-λR1		the N-terminal domain		PUBTATOR	Site	IFN-λR1	163702	domain	The ligand-receptor interface includes helix A, loop AB, and helix F on the IFN site, as well as loops primarily from the N-terminal domain and inter-domain hinge region of IFN-λR1.
2668275	9	20	gly	glycosylated	963:974	arg1	161 and 346 residues			161 and 346 residues						residues	Two glycosylated luminally oriented domains of 161 and 346 residues are separated by a hydrophobic domain spanning the membrane twice in opposite directions.
2668275	9	20	gly	glycosylated	963:974	arg1	Two glycosylated luminally oriented domains			Two glycosylated luminally oriented domains						domains	Two glycosylated luminally oriented domains of 161 and 346 residues are separated by a hydrophobic domain spanning the membrane twice in opposite directions.
7642555	11	69	gly	glycosylation	1333:1345	arg1	this biologically significant amino acid residue			residue						residue	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
23242014	8	23	gly	glycosylation	1074:1086	arg1	the HCV envelope protein E2	the HCV envelope protein E2				Cterm		E2			Here, we have investigated in detail the O-linked glycosylation of the HCV envelope protein E2 expressed in and isolated from human embryonic kidney (HEK 293) cells.
6725284	9	23	gly	GlcNAc	1441:1446	arg1	a Fuc residue			a Fuc residue	a Fuc residue		AminoAcid			residue at	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	9	30	gly	Asn-linked	1430:1439	arg1	the Asn-linked GlcNAc			Asn	the Asn-linked GlcNAc					Asn	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
2415652	4	36	gly	beta	1033:1036	arg1	the O-linked oligosaccharides	hCG beta			the O-linked oligosaccharides	PUBTATOR		hCG beta	1082		Oligosaccharides, O-linked to serine or threonine, were present in ElBre hCG beta, presumably on its CTE as judged by the complete binding of desialylated ElBre hCG beta to immobilized peanut agglutinin (this lectin is specific for terminal galactose linked beta 1----3 to N-acetylgalactosamine, a disaccharide exposed after desialylation of the O-linked oligosaccharides of standard hCG beta).
2415652	4	46	gly	desialylation	970:982	arg1	the O-linked oligosaccharides				the O-linked oligosaccharides						Oligosaccharides, O-linked to serine or threonine, were present in ElBre hCG beta, presumably on its CTE as judged by the complete binding of desialylated ElBre hCG beta to immobilized peanut agglutinin (this lectin is specific for terminal galactose linked beta 1----3 to N-acetylgalactosamine, a disaccharide exposed after desialylation of the O-linked oligosaccharides of standard hCG beta).
2415652	4	110	gly	desialylated	787:798	arg1	desialylated ElBre hCG beta	desialylated ElBre hCG beta				PUBTATOR		ElBre hCG beta	1082		Oligosaccharides, O-linked to serine or threonine, were present in ElBre hCG beta, presumably on its CTE as judged by the complete binding of desialylated ElBre hCG beta to immobilized peanut agglutinin (this lectin is specific for terminal galactose linked beta 1----3 to N-acetylgalactosamine, a disaccharide exposed after desialylation of the O-linked oligosaccharides of standard hCG beta).
2415652	4	98	gly	present	701:707	arg2	ElBre hCG beta AND Oligosaccharides	ElBre hCG beta			Oligosaccharides	PUBTATOR		ElBre hCG beta	1082		Oligosaccharides, O-linked to serine or threonine, were present in ElBre hCG beta, presumably on its CTE as judged by the complete binding of desialylated ElBre hCG beta to immobilized peanut agglutinin (this lectin is specific for terminal galactose linked beta 1----3 to N-acetylgalactosamine, a disaccharide exposed after desialylation of the O-linked oligosaccharides of standard hCG beta).
10207177	1	29	gly	glycoproteins	232:244	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Most cell surface molecules are glycoproteins consisting of linear arrays of globular domains containing stretches of amino acid sequence with similarities to regions in other proteins.
9705299	0	30	gly	Asparagine-linked	0:16	arg1	Asparagine-linked oligosaccharides			Asparagine	Asparagine-linked oligosaccharides					Asparagine	Asparagine-linked oligosaccharides are localized to a luminal hydrophilic loop in human glucose-6-phosphatase.
18715980	4	31	part_of	has	607:609	arg1	The SPINKL protein AND six conserved cysteine residues	The SPINKL protein		six conserved cysteine residues		PUBTATOR	AminoAcid	SPINKL protein	77424	cysteine residues	The SPINKL protein has six conserved cysteine residues that are nearly identical to those of members of the SPINK protein family.
19343721	4	15	gly	glycosylate	765:775	arg1	the Asn-X-Cys sequon			the Asn-X-Cys sequon						sequon	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
11390601	4	89	gly	glycosylation	883:895	arg2	The glycosylation site mutations			The glycosylation site mutations						site	The glycosylation site mutations near the V1/V2 loop compromised the use of CCR5 and CXCR4 equally.
22576872	2	42	part_of	Endogenous	324:333	arg1	Endogenous Aβ peptides	Endogenous Aβ 		Endogenous Aβ peptides		PUBTATOR	Site	Endogenous Aβ 	351	peptides	Endogenous Aβ peptides reflect the APP processing, and greater knowledge of different APP degradation pathways is important to understand the mechanism underlying AD pathology.
22576872	2	77	part_of	Aβ	335:336	arg1	Endogenous Aβ peptides	Endogenous Aβ 		Endogenous Aβ peptides		PUBTATOR	Site	Endogenous Aβ 	351	peptides	Endogenous Aβ peptides reflect the APP processing, and greater knowledge of different APP degradation pathways is important to understand the mechanism underlying AD pathology.
18780401	4	21	gly	glycoproteins	674:686	arg1	profiling N-linked glycoproteins	profiling N-linked glycoproteins				Fterm		glycoproteins			To achieve this objective, profiling N-linked glycoproteins of human milk was performed by Hydrophilic Interaction LC (HILIC) and MS analysis.
2136357	0	29	gly	glycoprotein	108:119	arg1	human and bovine uromodulin	human and bovine uromodulin				PUBTATOR		uromodulin	281567		Pregnancy-associated changes in oligomannose oligosaccharides of human and bovine uromodulin (Tamm-Horsfall glycoprotein).
2136357	0	29	gly	glycoprotein	108:119	arg1	Tamm-Horsfall glycoprotein	Tamm-Horsfall glycoprotein				OGER		Tamm-Horsfall glycoprotein	P07911		Pregnancy-associated changes in oligomannose oligosaccharides of human and bovine uromodulin (Tamm-Horsfall glycoprotein).
2136357	0	64	gly	uromodulin	82:91	arg1	oligomannose oligosaccharides	uromodulin			oligomannose oligosaccharides	PUBTATOR		uromodulin	281567		Pregnancy-associated changes in oligomannose oligosaccharides of human and bovine uromodulin (Tamm-Horsfall glycoprotein).
1710976	12	4	gly	residues	1461:1468	arg1	364-368			364-368						residues 364-368	Peptide Asn-Gly-Ser (residues 427-429) is the most probable candidate for glycosylation; literature data suggests that deamidation occurs in the stretch Glu-Asn-Gly-Lys-Asp (residues 364-368) and Asn-Gly-Asn-Cys (residues 474-477).
1710976	12	48	gly	residues	1500:1507	arg1	474-477			474-477						residues 474-477	Peptide Asn-Gly-Ser (residues 427-429) is the most probable candidate for glycosylation; literature data suggests that deamidation occurs in the stretch Glu-Asn-Gly-Lys-Asp (residues 364-368) and Asn-Gly-Asn-Cys (residues 474-477).
10639192	6	4	gly	attached	712:719	arg2	Asp 301 AND high-mannose chains			Asn 62 and Asp 301	high-mannose chains					Asn 62 and Asp 301	It appears that high-mannose chains are attached to Asn 62 and Asp 301, while complex chains are at Asn 188.
22387313	5	51	gly	N-glycosylation	735:749	arg2	six positions			six positions						positions	Using site-directed mutagenesis (N to Q) we showed that N-glycosylation occured at six positions.
22688517	2	57	gly	N-glycosylation	216:230	arg1	LOX-1	LOX-1				PUBTATOR		LOX-1	4973		The N-glycosylation of LOX-1 has been shown to affect its biological functions in vivo and modulate the pathogenesis of atherosclerosis.
10978165	6	14	gly	glycosylated	659:670	arg1	1-74	1-74				Cterm		1-74	6358		These peptides were isolated from a peptide library of human blood filtrate and represent predominantly HCC-1 (1-74) and glycosylated HCC-1 (1-74).
10978165	6	14	gly	glycosylated	659:670	arg1	glycosylated HCC-1	glycosylated HCC-1				PUBTATOR		HCC-1	6358		These peptides were isolated from a peptide library of human blood filtrate and represent predominantly HCC-1 (1-74) and glycosylated HCC-1 (1-74).
12590919	2	27	gly	glycosylation	290:302	arg1	hENT2	hENT2				PUBTATOR		hENT2	3177		It is not known whether glycosylation affects the functions of hENT2 or where hENT2 is glycosylated.
12590919	2	29	gly	glycosylated	353:364	arg1	hENT2	hENT2				PUBTATOR		hENT2	3177		It is not known whether glycosylation affects the functions of hENT2 or where hENT2 is glycosylated.
26207632	4	52	gly	O-glycosylation	643:657	arg1	the Obif protein	Obif protein		serine residue 36		OGER		Obif protein	Q8R138	serine residue 36	RESULTS: First, we found that O-glycosylation of the Obif protein occurs at serine residue 36 in the Obif extracellular domain.
8407880	0	57	gly	factor	71:76	arg1	the N-linked oligosaccharides	hepatocyte growth factor			the N-linked oligosaccharides	PUBTATOR		hepatocyte growth factor	24446		Structural study of the N-linked oligosaccharides of hepatocyte growth factor by two-dimensional sugar mapping.
16452088	1	18	gly	proteins	226:233	arg1	O-GlcNAc	proteins			O-GlcNAc	Fterm		proteins			O-GlcNAc is a widespread dynamic carbohydrate modification of cytosolic and nuclear proteins with features analogous to phosphorylation.
16452088	1	18	gly	proteins	226:233	arg1	a widespread dynamic carbohydrate modification	proteins			a widespread dynamic carbohydrate modification	Fterm		proteins			O-GlcNAc is a widespread dynamic carbohydrate modification of cytosolic and nuclear proteins with features analogous to phosphorylation.
16452088	1	41	gly	modification	188:199	arg3	cytosolic and nuclear proteins AND a widespread dynamic carbohydrate modification	cytosolic and nuclear proteins			a widespread dynamic carbohydrate modification	Fterm		proteins			O-GlcNAc is a widespread dynamic carbohydrate modification of cytosolic and nuclear proteins with features analogous to phosphorylation.
2793860	6	13	gly	linked	958:963	arg1	Thr AND The O-linked chains			Thr	The O-linked chains					Thr in position 3	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	6	60	gly	site	1048:1051	arg1	natural human IL-2	IL-2			site	PUBTATOR		IL-2	P60568		The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
1517205	5	14	gly	positions	1234:1242	arg1	55-63			55-63						positions 55	hIX-GP1 was further digested with asparaginyl endopeptidase, and two glycopeptides containing Ser-61, named N-3 (positions 59-63) and N-9 (positions 55-63), were isolated, respectively.
1517205	5	17	gly	glycopeptides	1164:1176	arg2	two glycopeptides			two glycopeptides						glycopeptides	hIX-GP1 was further digested with asparaginyl endopeptidase, and two glycopeptides containing Ser-61, named N-3 (positions 59-63) and N-9 (positions 55-63), were isolated, respectively.
1517205	5	23	gly	positions	1208:1216	arg1	59-63			59-63						positions 59	hIX-GP1 was further digested with asparaginyl endopeptidase, and two glycopeptides containing Ser-61, named N-3 (positions 59-63) and N-9 (positions 55-63), were isolated, respectively.
1731338	0	92	gly	galactoglycoprotein	36:54	arg1	human plasma galactoglycoprotein	human plasma galactoglycoprotein				PUBTATOR		galactoglycoprotein	6693		Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
10644446	6	12	part_of	contains	817:824	arg1	ANGPTL3 AND the four conserved cysteines	ANGPTL3		the four conserved cysteines		PUBTATOR	AminoAcid	ANGPTL3	27329	cysteines	ANGPTL3 contains the four conserved cysteines implicated in the intramolecular disulfide bonds within the FHD, but it does not contain two other cysteines that are found within the FHD of angiopoietins 1, 2, and 4.
19592704	5	54	gly	sites	807:811	arg1	the putative N-linked glycosylation sites			the putative N-linked glycosylation sites						sites	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	41	gly	glycosylation	793:805	arg2	Asn			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	41	gly	glycosylation	793:805	arg1	NCEH	NCEH		Asn(270), Asn(367), and Asn(389)		PUBTATOR		NCEH	57552	Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	41	gly	glycosylation	793:805	arg2	Asn(270)			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	41	gly	glycosylation	793:805	arg1	NCEH	NCEH		Asn(270), Asn(367), and Asn(389)		PUBTATOR		NCEH	57552	Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	41	gly	glycosylation	793:805	arg2	Asn(270)			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	41	gly	glycosylation	793:805	arg1	NCEH	NCEH		sites		PUBTATOR		NCEH	57552	sites	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	41	gly	glycosylation	793:805	arg2	Asn(270)	NCEH		Asn(270), Asn(367), and Asn(389)		PUBTATOR		NCEH	57552	Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	53	gly	glycosylated	860:871	arg1	Asn(270)			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	53	gly	glycosylated	860:871	arg1	NCEH	NCEH		Asn(270), Asn(367), and Asn(389)		PUBTATOR		NCEH	57552	Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	53	gly	glycosylated	860:871	arg1	Asn			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	53	gly	glycosylated	860:871	arg1	NCEH	NCEH		sites		PUBTATOR		NCEH	57552	sites	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	53	gly	glycosylated	860:871	arg1	NCEH	NCEH		Asn(270), Asn(367), and Asn(389)		PUBTATOR		NCEH	57552	Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	53	gly	glycosylated	860:871	arg1	Asn			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	53	gly	glycosylated	860:871	arg1	Asn	NCEH		Asn(270), Asn(367), and Asn(389)		PUBTATOR		NCEH	57552	Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	gly	sites	807:811	arg1	389			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	gly	sites	807:811	arg1	Asn(270)			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	gly	sites	807:811	arg1	367			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	gly	sites	807:811	arg1	Asn			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	gly	sites	807:811	arg1	Asn(270)			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	gly	sites	807:811	arg1	367			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	gly	sites	807:811	arg1	Asn			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	gly	sites	807:811	arg1	367			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	gly	sites	807:811	arg1	Asn			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	gly	sites	807:811	arg1	Asn			Asn(270), Asn(367), and Asn(389)						Asn(270), Asn(367), and Asn(389)	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
22399287	5	55	part_of	has	737:739	arg1	CNNM2 AND an intracellular C terminus	CNNM2		terminus		PUBTATOR	Site	CNNM2	54805	terminus	Here, membrane topology studies using intramolecular epitopes and immunocytochemistry showed that CNNM2 has an extracellular N terminus and an intracellular C terminus.
19299457	8	56	gly	N198	1045:1048	arg1	the glycan moiety			N198	the glycan moiety					N198	Because the immunogen for CS-17 generation was highly glycosylated, we also investigated whether the glycan moiety at N198, topologically adjacent to Y195 (a previously identified epitopic component), could contribute to the CS-17 epitope.
9712881	4	42	gly	glycosylation	461:473	arg2	the glycosylation site			the glycosylation site						site	Residues of the Ser643 (adjacent to the glycosylation site) to Ser690 region of cysteineless mutant (AE1C-) were replaced individually with cysteine.
22940367	5	7	part_of	GALNS	797:801	arg1	The active site	GALNS		The active site		PUBTATOR	Site	GALNS	2588	site	The active site of GALNS is a large, positively charged trench suitable for binding polyanionic substrates such as keratan sulfate and chondroitin-6-sulfate.
27313224	3	14	gly	glycoprotein	586:597	arg1	vesicle glycoprotein 2	vesicle glycoprotein 2				PUBTATOR		synaptic vesicle glycoprotein 2	9900		The luminal domain 4 (LD4) of the three synaptic vesicle glycoprotein 2 (SV2) isoforms A-C mediates uptake of the clinically most relevant serotype BoNT/A1.
27313224	3	14	gly	glycoprotein	586:597	arg1	SV2	SV2				PUBTATOR		SV2	9900		The luminal domain 4 (LD4) of the three synaptic vesicle glycoprotein 2 (SV2) isoforms A-C mediates uptake of the clinically most relevant serotype BoNT/A1.
12768205	3	41	part_of	has	395:397	arg1	FcalphaRI AND two immunoglobulin-like domains	FcalphaRI		two immunoglobulin-like domains		PUBTATOR	Site	FcalphaRI	2204	domains	FcalphaRI has two immunoglobulin-like domains that are oriented at approximately right angles to each other.
28775322	6	2	part_of	receptors	1391:1399	arg1	the EGF-like domains	receptors		the EGF-like domains		Fterm	Site	receptors		domains	Finally, we show that Protein O-glucosyltransferase 1 has co-evolved with EGF-like domains of the type found in Notch.POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors.
28775322	6	20	part_of	EGF-like	1217:1224	arg1	EGF-like domains	EGF		EGF-like domains		OGER	Site	EGF	P01133	domains	Finally, we show that Protein O-glucosyltransferase 1 has co-evolved with EGF-like domains of the type found in Notch.POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors.
28775322	6	24	part_of	EGF-like	1345:1352	arg1	the EGF-like domains	EGF		the EGF-like domains		OGER	Site	EGF	P01133	domains	Finally, we show that Protein O-glucosyltransferase 1 has co-evolved with EGF-like domains of the type found in Notch.POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors.
28775322	6	52	part_of	Notch	1365:1369	arg1	the EGF-like domains	Notch		the EGF-like domains		PUBTATOR	Site	Notch	31293	domains	Finally, we show that Protein O-glucosyltransferase 1 has co-evolved with EGF-like domains of the type found in Notch.POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors.
8702538	0	51	gly	glycosylation	18:30	arg2	A single N-linked glycosylation site			A single N-linked glycosylation site						site	A single N-linked glycosylation site is implicated in the regulation of ligand recognition by the I-type lectins CD22 and CD33.
7744025	9	10	gly	glycosylation	1788:1800	arg1	Thr9			Thr9						Thr9	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	9	10	gly	glycosylation	1788:1800	arg2	Ser20			Ser20						Ser20	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
8243461	0	88	part_of	X	105:105	arg1	the activation peptides	factor X		the activation peptides		OGER	Site	factor X	P00742	peptides	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
3665914	0	80	gly	polysialoglycoprotein	112:132	arg1	polysialoglycoprotein	polysialoglycoprotein				Fterm		polysialoglycoprotein			Identification and determination of absolute and anomeric configurations of the 6-deoxyaltrose residue found in polysialoglycoprotein of Salvelinus leucomaenis pluvius eggs.
30659065	11	97	gly	sites	1914:1918	arg1	sites N279 and N439			sites N279 and N439						sites N279 and N439	IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms.
30659065	11	97	gly	sites	1914:1918	arg1	N439			sites N279 and N439						sites N279 and N439	IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms.
30659065	11	97	gly	sites	1914:1918	arg1	N439			sites N279 and N439						sites N279 and N439	IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms.
31125343	7	10	part_of	site	1083:1086	arg1	HEPHL1	HEPHL1		site		OGER	Site	HEPHL1	Q6MZM0	site	The paternal mutation (c.3176T>C; p.Met1059Thr) changed a highly conserved methionine that is part of a typical type I copper binding site in HEPHL1.
16894147	4	13	part_of	L1	717:718	arg1	the L1 domain	1		the L1 domain		Cterm	Site	1		domain	The first is at the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet.
14573609	2	6	gly	glycosylated	398:409	arg1	glycosylated heparanase	glycosylated heparanase				PUBTATOR		heparanase	10855		The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	2	33	gly	N-glycosylation	334:348	arg2	six putative N-glycosylation sites			six putative N-glycosylation sites						sites	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
24977290	4	76	gly	presence	627:634	arg1	plasma derived ADAMTS13 AND putative O-fucosylation, C-mannosylation and N-linked glycosylation sites	plasma derived ADAMTS13			putative O-fucosylation, C-mannosylation and N-linked glycosylation sites	PUBTATOR		ADAMTS13	Q76LX8		OBJECTIVES: Here we investigated the presence of putative O-fucosylation, C-mannosylation and N-linked glycosylation sites on plasma derived ADAMTS13.
12731890	2	43	gly	glycosylation	349:361	arg1	a secreted form	form of the receptor		sites		Fterm		form of the receptor		sites	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	2	43	gly	glycosylation	349:361	arg1	the full-length, membrane-bound receptor	receptor		sites		Fterm		receptor		sites	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
3264725	2	54	part_of	factor	440:445	arg1	10 gamma-carboxylated, N-terminally located glutamic acid residues	factor VIIa		10 gamma-carboxylated, N-terminally located glutamic acid residues		Cterm	AminoAcid	factor VIIa		glutamic acid residues	Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues.
3264725	2	54	part_of	factor	440:445	arg1	1 beta-hydroxylated aspartic acid residue	factor VIIa		1 beta-hydroxylated aspartic acid residue		Cterm	AminoAcid	factor VIIa		aspartic acid residue	Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues.
3264725	2	54	part_of	factor	440:445	arg1	2 N-glycosylated asparagine residues	factor VIIa		2 N-glycosylated asparagine residues		Cterm	AminoAcid	factor VIIa		asparagine residues	Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues.
3264725	2	113	part_of	VIIa	447:450	arg1	10 gamma-carboxylated, N-terminally located glutamic acid residues	factor VIIa		10 gamma-carboxylated, N-terminally located glutamic acid residues		Cterm	AminoAcid	factor VIIa		glutamic acid residues	Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues.
3264725	2	113	part_of	VIIa	447:450	arg1	1 beta-hydroxylated aspartic acid residue	factor VIIa		1 beta-hydroxylated aspartic acid residue		Cterm	AminoAcid	factor VIIa		aspartic acid residue	Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues.
3264725	2	113	part_of	VIIa	447:450	arg1	2 N-glycosylated asparagine residues	factor VIIa		2 N-glycosylated asparagine residues		Cterm	AminoAcid	factor VIIa		asparagine residues	Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues.
8576151	11	64	part_of	collagenase-3	1859:1871	arg1	the active site sequence	collagenase-3		the active site sequence		PUBTATOR	Site	collagenase-3	4322	sequence	Unlike these collagenases, gelatin and the peptide substrates Mea-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 and Mca-Pro-Cha-Gly-Nva-His-Ala-Dpa-NH2 were efficiently hydrolyzed as well, as would be predicted from the similarities between the active site sequence of collagenase-3 (MMP-13) and the gelatinases A and B. Active collagenase-3 was inhibited in a 1:1 stoichiometric fashion by the tissue inhibitors of metalloproteinases, TIMP-1, TIMP-2, and TIMP-3.
6510521	4	38	part_of	CB1-CB4	577:583	arg1	Fragments	Fragments CB1		Fragments		PUBTATOR		Fragments CB1	1268		Fragments CB1-CB4 include 5 sites, where hexosamine oligosaccharides are attached (positions 1,41,164,217 and probably 223).
8460945	1	61	gly	attached	198:205	arg1	human erythropoietin AND the mucin-type sugar chains	human erythropoietin			the mucin-type sugar chains	PUBTATOR		erythropoietin	2056		Less is known about the mucin-type sugar chains attached to human erythropoietin as compared with N-linked sugar chains which structures and function have been well studied.
26563299	12	17	gly	glycosylation	1741:1753	arg1	IL-15	IL-15				PUBTATOR		IL-15	3600		Highly reproducible glycosylation of IL-15 and sIL-15Rα of two batches of hetIL-15 demonstrated consistent manufacturing and purification.
21609021	2	78	gly	region	412:417	arg1	the constant region N-glycan				the constant region N-glycan						One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	2	81	gly	immunoglobulin	448:461	arg1	the constant region N-glycan	immunoglobulin			the constant region N-glycan	Fterm		immunoglobulin			One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
15677325	0	30	part_of	subunit	34:40	arg1	the kainate receptor subunit GluR6 agonist-binding domain	subunit GluR6		the kainate receptor subunit GluR6 agonist-binding domain		OGER	Site	subunit GluR6	2898	domain	Structure of the kainate receptor subunit GluR6 agonist-binding domain complexed with domoic acid.
15677325	0	43	part_of	GluR6	42:46	arg1	the kainate receptor subunit GluR6 agonist-binding domain	subunit GluR6		the kainate receptor subunit GluR6 agonist-binding domain		OGER	Site	subunit GluR6	2898	domain	Structure of the kainate receptor subunit GluR6 agonist-binding domain complexed with domoic acid.
19379732	4	23	gly	N-glycosylation	1378:1392	arg1	hSVCT1 membrane targeting	hSVCT1 membrane targeting				PUBTATOR		hSVCT1	9963		However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
18642129	12	71	gly	modified	1741:1748	arg1	position Ser(60) and Ser(52) AND Glc			position Ser(60) and Ser(52)	Glc					position Ser(60) and Ser(52)	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	71	gly	modified	1741:1748	arg1	position Ser(60) and Ser(52) AND oligosaccharide structures			position Ser(60) and Ser(52)	oligosaccharide structures					position Ser(60) and Ser(52)	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	71	gly	modified	1741:1748	arg3	position Ser(60) and Ser(52) AND fucose			position Ser(60) and Ser(52)	fucose					position Ser(60) and Ser(52)	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	83	gly	O-glycosylated	1665:1678	arg1	FVII	FVII				OGER		FVII	P08709		Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	83	gly	O-glycosylated	1665:1678	arg1	the light chain	the light chain				OGER		chain	P08709		Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	1	gly	position	1702:1709	arg1	Ser(60)			position Ser(60) and Ser(52)						position Ser(60) and Ser(52)	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
17563389	0	94	gly	glycosylation	50:62	arg2	N-linked glycosylation sites			N-linked glycosylation sites						sites	Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor.
8323299	8	12	gly	proline-rich	1257:1268	arg1	the proline-rich O-glycan acceptor region			proline	the proline-rich O-glycan acceptor region					proline	The results indicated that the proline-rich O-glycan acceptor region does not adopt any typical periodic structure but differs from random-coil structure.
30899004	3	51	gly	glycopeptides	371:383	arg2	intact glycopeptides			intact glycopeptides						glycopeptides	A lack of suitable analytical methods for large-scale analyses of intact glycopeptides has limited our abilities both to address the degree of heterogeneity across the glycoproteome and to understand how this contributes biologically to complex systems.
1451807	4	20	gly	O-glycosylated	495:508	arg2	Thr7			Thr7						Thr7	In addition, part of the molecules are O-glycosylated at Thr7; O-glycosylation is heterogeneous due to variable decoration with neuraminic acid.
19276170	4	45	gly	sites	813:817	arg1	the type 3 repeats			sites	the type 3 repeats					sites	The CTD is a beta-sandwich that is composed of 15 antiparallel beta-strands, and the type 3 repeats are a contiguous series of calcium binding sites that associate with the CTD at multiple points.
23167757	5	76	part_of	PDIA2	904:908	arg1	the potential N-linked glycosylation sites	PDIA2		the potential N-linked glycosylation sites		PUBTATOR	Site	PDIA2	64714	sites	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
22766194	4	49	gly	N-glycosylation	782:796	arg2	the consensus N-glycosylation sites			the consensus N-glycosylation sites						sites	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
11081633	3	5	part_of	EGF	614:616	arg1	the lectin and EGF (LE) domains	EGF		the lectin and EGF (LE) domains		OGER	Site	EGF	P01133	domains	Here, we report crystal structures of human P- and E-selectin constructs containing the lectin and EGF (LE) domains co-complexed with SLe(X).
23285087	2	2	gly	N-glycosylation	303:317	arg2	Putative N-glycosylation sites			Putative N-glycosylation sites						sites	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	2	42	gly	glycosylated	458:469	arg1	glycosylated proteins	glycosylated proteins				Fterm		proteins			Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
16834341	3	33	gly	glycopeptides	370:382	arg1	human pituitary follicle stimulating hormone	follicle stimulating hormone		glycopeptides		Cterm		follicle stimulating hormone		glycopeptides	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
25081999	5	50	part_of	hSCP1	1014:1018	arg1	the Ser41 residue	hSCP1		the Ser41 residue		PUBTATOR	AminoAcid	hSCP1	58190	Ser41 residue	To gain insight into the PTM of hSCP1, we used the Western blot, immunoprecipitation, succinylayed wheat germ agglutininprecipitation, liquid chromatography-mass spectrometry analyses, and site-directed mutagenesis and identified the Ser41 residue of hSCP1 as the O-GlcNAc modification site.
10929010	0	43	gly	transferrin	27:37	arg1	N-glycan patterns	transferrin			N-glycan patterns	PUBTATOR		transferrin	7018		N-glycan patterns of human transferrin produced in Trichoplusia ni insect cells: effects of mammalian galactosyltransferase.
18768470	7	29	part_of	FSTL3	1395:1399	arg1	the N-terminal domain	FSTL3		the N-terminal domain		PUBTATOR	Site	FSTL3	10272	domain	Therefore, both structural and biochemical evidence support a significant interaction of the N-terminal domain of FSTL3 with activin A.
11502179	1	4	part_of	receptor	175:182	arg1	The amino-terminal ectodomain	TSH receptor		The amino-terminal ectodomain		PUBTATOR	Site	TSH receptor	7253	ectodomain	The amino-terminal ectodomain of the human TSH receptor has been expressed at the surface of CHO cells as a glycosylphosphatidylinositol-anchored molecule containing a 10-residue histidine tag close to its C terminus.
26598643	12	29	gly	O-glycosylation	1838:1852	arg2	23 O-glycosylation sites			23 O-glycosylation sites						sites	In total 23 O-glycosylation sites could be pinpointed.
20511397	3	77	gly	structures	590:599	arg1	plasma apoE	apoE			structures	PUBTATOR		apoE	348		Some of the glycan structures on plasma apoE are characterized; however, the more complicated structures on plasma and cellular/secreted apoE remain unidentified.
17650508	1	14	gly	glycoprotein	222:233	arg1	a secreted glycoprotein	a secreted glycoprotein				Fterm		glycoprotein			MYOC, a gene involved in different types of glaucoma, encodes myocilin, a secreted glycoprotein of unknown function, consisting of an N-terminal leucine-zipper-like domain, a central linker region, and a C-terminal olfactomedin-like domain.
17650508	1	14	gly	glycoprotein	222:233	arg1	myocilin	myocilin				PUBTATOR		myocilin	4653		MYOC, a gene involved in different types of glaucoma, encodes myocilin, a secreted glycoprotein of unknown function, consisting of an N-terminal leucine-zipper-like domain, a central linker region, and a C-terminal olfactomedin-like domain.
12297049	5	14	part_of	receptor	779:786	arg1	the CR1 domains	receptor		the CR1 domains		Fterm	Site	receptor		domains	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	5	30	part_of	CR1	759:761	arg1	the CR1 domains	CR1		the CR1 domains		OGER	Site	CR1	P17927	domains	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
11706042	8	74	gly	glycosylation	1416:1428	arg2	three or more N-linked glycosylation sites			three or more N-linked glycosylation sites						sites	Similar results were observed with TLR4 mutants lacking three or more N-linked glycosylation sites.
15486088	1	56	gly	Ser	339:341	arg1	residues			residues						Thr residues	UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases (ppGaNTases) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine from UDP-GalNAc to Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-alpha-1-O-Ser/Thr).
22000856	2	20	gly	domain	286:291	arg1	four β-propeller/EGF-like domain repeats				four β-propeller/EGF-like domain repeats						The LRP5/6 ectodomain contains four β-propeller/EGF-like domain repeats.
22000856	2	26	gly	contains	251:258	arg1	The LRP5/6 ectodomain AND four β-propeller/EGF-like domain repeats			The LRP5/6 ectodomain	four β-propeller/EGF-like domain repeats					ectodomain	The LRP5/6 ectodomain contains four β-propeller/EGF-like domain repeats.
2498325	9	15	gly	N-glycosylated	1435:1448	arg2	Asn194	apoE		Asn194		PUBTATOR		apoE	348	Asn194	Studies with tunicamycin indicated that this apoE was N-glycosylated at Asn194.
17395588	4	30	gly	fucosylated	732:742	arg1	the fucosylated residue				the fucosylated residue						Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	4	72	gly	O-fucosylation	464:477	arg1	Ser			Ser	Ser		AminoAcid			Ser	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	4	72	gly	O-fucosylation	464:477	arg1	Thr			Thr	Thr		AminoAcid			Thr	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
21148085	5	12	part_of	VEGFR-2	749:755	arg1	VEGFR-2 interacting residues	VEGFR-2		VEGFR-2 interacting residues		PUBTATOR	Site	VEGFR-2	3791	residues	Comparison of the VEGF-D and VEGF-C structures shows similar extended N-terminal helices, conserved overall folds, and VEGFR-2 interacting residues.
10200178	0	75	gly	protein	71:77	arg1	the N-linked glycans	protein			the N-linked glycans	Fterm		protein			Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions.
24977290	7	18	gly	O-fucosylated	1139:1151	arg1	six putative O-fucosylated sites			six putative O-fucosylated sites						sites	Moreover, six putative O-fucosylated sites were identified in the TSR domains of plasma ADAMTS13 by performing searches of the tandem mass spectrometry (MS/MS) data for loss of hexose (162 Da), deoxyhexose (146 Da), or hexose deoxyhexose(308 Da).
20145116	2	35	part_of	receptors	280:288	arg1	The extracellular domain	VEGF receptors		The extracellular domain		PUBTATOR	Site	VEGF receptors	7422	domain	The extracellular domain of VEGF receptors consists of seven immunoglobulin homology domains, which, upon ligand binding, promote receptor dimerization.
6619126	11	13	gly	glycopeptides	1700:1712	arg2	two CNBr glycopeptides			two CNBr glycopeptides						glycopeptides	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	11	147	gly	glycoproteins	1616:1628	arg1	these glycoproteins	these glycoproteins				Fterm		glycoproteins			Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
18491227	2	26	part_of	sites	352:356	arg1	E-cadherin	E-cadherin		sites		PUBTATOR	Site	E-cadherin	999	sites	In a previous study, we demonstrated that all of four potential N-glycosylation sites in E-cadherin are occupied by N-glycans in human breast carcinoma cells in vivo and the elimination of N-glycan at Asn-633 dramatically affected E-cadherin expression and made it degraded.
3980466	5	72	gly	glycosylation	945:957	arg2	each glycosylation site			each glycosylation site						site	The data indicate: 1) a unique distribution of oligosaccharide structures is present at each glycosylation site; 2) each site-specific oligosaccharide pattern is highly reproducible, independent of the number of in vivo tumor passages.
19651138	0	25	part_of	GluR2	25:29	arg1	the GluR2 amino-terminal domain	GluR2		the GluR2 amino-terminal domain		PUBTATOR	Site	GluR2	2891	domain	Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors.
16368742	1	7	gly	glycosylation	158:170	arg2	a consensus N-linked glycosylation motif			a consensus N-linked glycosylation motif						motif	We identified a consensus N-linked glycosylation motif within the pore-forming loop between the fifth and sixth transmembrane segments of the osmoresponsive transient receptor potential (TRP) channel TRPV4.
21138434	4	17	part_of	sequences	901:909	arg1	the h5-HT3B subunit	h5-HT3B subunit		sequences		Cterm	Site	h5-HT3B subunit	9177	sequences	Disruption of each consensus N-glycosylation sequences in the h5-HT3B subunit (N31S, N75S, N117S, N147S and N182S) resulted in a reduced molecular weight (by ∼ 2-4 kDa) of each mutant when expressed by HEK293 cells stably expressing the h5-HT3A subunit.
20133774	5	30	part_of	CNTN4	960:964	arg1	the N-terminal region	CNTN4		the N-terminal region		PUBTATOR	Site	CNTN4	269784	region	In these structures, the N-terminal region of CNTN4 adopts a horseshoe-like conformation found also in CNTN2 and most likely in all CNTNs.
26283364	5	15	gly	SSL3	785:788	arg1	the conserved Lewis(X) binding site	SSL3			the conserved Lewis(X) binding site	Cterm		SSL3	Q12988		The structure reveals that formation of the specific inhibitory complex is predominantly mediated by hydrophobic contacts between SSL3 and TLR2 and does not involve interaction of TLR2-glycans with the conserved Lewis(X) binding site of SSL3.
10669592	4	1	part_of	NEP	721:723	arg1	residues 52-749	NEP		residues 52-749		PUBTATOR	SpecificSite	NEP	4311	residues 52-749	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	4	1	part_of	NEP	721:723	arg1	the extracellular domain	NEP		the extracellular domain		PUBTATOR	Site	NEP	4311	domain	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
21047790	3	38	part_of	neurofascin	457:467	arg1	The four N-terminal Ig-like domains	neurofascin		The four N-terminal Ig-like domains		PUBTATOR	Site	neurofascin	23114	domains	The four N-terminal Ig-like domains of neurofascin form a horseshoe shape, akin to several other immunoglobulin superfamily cell adhesion molecules such as hemolin, axonin, and Dscam.
22750213	4	4	part_of	containing	695:704	arg1	PRiMA AND two putative N-linked glycosylation sites	PRiMA		two putative N-linked glycosylation sites		PUBTATOR	Site	PRiMA	170952	sites	PRiMA is a glycoprotein containing two putative N-linked glycosylation sites.
22750213	4	4	part_of	containing	695:704	arg1	a glycoprotein AND two putative N-linked glycosylation sites	a glycoprotein		two putative N-linked glycosylation sites		Fterm	Site	glycoprotein		sites	PRiMA is a glycoprotein containing two putative N-linked glycosylation sites.
18642129	5	84	gly	heterogeneity	732:744	arg1	pd-FVII	pd-FVII				OGER		FVII	P08709		N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	5	14	gly	O-glycosylation	692:706	arg1	pd-FVII	FVII		sites		OGER		FVII	P08709	sites	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
19692335	3	40	part_of	metalloproteinase	637:653	arg1	functional metalloproteinase domains	metalloproteinase		functional metalloproteinase domains		Fterm	Site	metalloproteinase		domains	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
3342257	4	25	gly	kappa-casein	1356:1367	arg1	Five oligosaccharide alditols	kappa-casein			Five oligosaccharide alditols	OGER		kappa-casein	P07498		Five oligosaccharide alditols (III-VII) were the novel carbohydrate chains of kappa-casein from mammalian milk.
3342257	4	25	gly	kappa-casein	1356:1367	arg1	the novel carbohydrate chains	kappa-casein			the novel carbohydrate chains	OGER		kappa-casein	P07498		Five oligosaccharide alditols (III-VII) were the novel carbohydrate chains of kappa-casein from mammalian milk.
26467158	3	16	gly	modified	418:425	arg1	BACE1 AND GlcNAc	BACE1			GlcNAc	PUBTATOR		BACE1	23821		We have recently found that BACE1 is modified with bisecting N-acetylglucosamine (GlcNAc) by N-acetylglucosaminyltransferase-III (GnT-III, encoded by the Mgat3 gene) and that GnT-III deficiency reduces Aβ-plaque formation in the brain by accelerating lysosomal degradation of BACE1.
26467158	3	16	gly	modified	418:425	arg3	BACE1 AND bisecting N-acetylglucosamine	BACE1			bisecting N-acetylglucosamine	PUBTATOR		BACE1	23821		We have recently found that BACE1 is modified with bisecting N-acetylglucosamine (GlcNAc) by N-acetylglucosaminyltransferase-III (GnT-III, encoded by the Mgat3 gene) and that GnT-III deficiency reduces Aβ-plaque formation in the brain by accelerating lysosomal degradation of BACE1.
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(542)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(61)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(205)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(357)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(135)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	the 11 potential N-glycosylation sites			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(361)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(109)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(531)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(61)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(205)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(357)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(135)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	the 11 potential N-glycosylation sites			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(361)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(109)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(531)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(205)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(357)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(135)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	the 11 potential N-glycosylation sites			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(361)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(109)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(531)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(357)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(135)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	the 11 potential N-glycosylation sites			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(361)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(109)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(531)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(135)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	the 11 potential N-glycosylation sites			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(361)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(109)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(531)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	the 11 potential N-glycosylation sites			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(361)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(109)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(531)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(361)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(109)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(531)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(109)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(531)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn(531)			sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)						sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542)	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
14718370	1	51	part_of	protein	152:158	arg1	this highly conserved protein domain	protein		this highly conserved protein domain		Fterm	Site	protein		domain	We expressed recombinant Cys subdomains in COS-7 cells to examine the role of this highly conserved protein domain in mucin biosynthesis.
7776966	0	110	gly	glycosylation	40:52	arg2	the sites			the sites						sites	Identification of the sites of N-linked glycosylation on the follicle-stimulating hormone (FSH) receptor and assessment of their role in FSH receptor function.
27175940	2	14	part_of	p27	474:476	arg1	the glycosylation sites	p27		the glycosylation sites		PUBTATOR	Site	p27	3429	sites	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	14	part_of	p27	474:476	arg1	Thr157	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR	AminoAcid	p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	14	part_of	p27	474:476	arg1	Ser2	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR	AminoAcid	p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	14	part_of	p27	474:476	arg1	Ser106	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR	AminoAcid	p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	14	part_of	p27	474:476	arg1	Thr198	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR	AminoAcid	p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	14	part_of	p27	474:476	arg1	Ser2	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR	AminoAcid	p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	14	part_of	p27	474:476	arg1	Ser106	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR	AminoAcid	p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	14	part_of	p27	474:476	arg1	Thr198	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR	AminoAcid	p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	14	part_of	p27	474:476	arg1	Ser106	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR	AminoAcid	p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	14	part_of	p27	474:476	arg1	Thr198	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR	AminoAcid	p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
27175940	2	14	part_of	p27	474:476	arg1	Thr198	p27		Ser2, Ser106, Ser110, Thr157, and Thr198		PUBTATOR	AminoAcid	p27	3429	Ser2, Ser106, Ser110, Thr157, and Thr198	The post-translational addition of O-GlcNAc to p27 occurs in HEK293T and HCC (hepatocellular carcinoma) cell lines, and we identified Ser2, Ser106, Ser110, Thr157, and Thr198 as the glycosylation sites of p27 based on the Q-TOF spectrum.
3665919	1	17	gly	glycoproteins	188:200	arg1	The carbohydrate chains	glycoproteins			The carbohydrate chains	Fterm		glycoproteins			The carbohydrate chains of the bronchial-mucus glycoproteins of six cystic fibrosis patients with blood group O were released by alkaline borohydride treatment.
12859190	5	36	part_of	EPOR	551:554	arg1	the recombinant extracellular domain	EPOR		the recombinant extracellular domain		PUBTATOR	Site	EPOR	2057	domain	Here we report that the first tryptophan in the motif of the recombinant extracellular domain of EPOR (sEPOR) expressed in HEK-EBNA cells carries a C-linked hexosyl residue.
12754519	0	56	gly	glycoproteins	46:58	arg1	N-linked glycoproteins	N-linked glycoproteins				Fterm		glycoproteins			Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
25939779	2	47	gly	glycopeptide	340:351	arg2	glycopeptide specificity			glycopeptide specificity						glycopeptide	The underlying molecular basis of how the lectin domains of GalNAc-Ts contribute to glycopeptide specificity and catalysis remains unclear.
3524673	10	15	part_of	site	1018:1021	arg1	fibronectin	fibronectin		site		PUBTATOR	Site	fibronectin	2335	site	The protein also contains the tetrapeptide sequence Arg-Gly-Asp-Ser (at residues 1744-1747), which may be a cell attachment site, as in fibronectin.
3524673	10	57	part_of	contains	911:918	arg1	The protein AND the tetrapeptide sequence Arg-Gly-Asp-Ser	The protein		the tetrapeptide sequence Arg-Gly-Asp-Ser		Fterm	Site	protein		Arg-Gly-Asp-Ser	The protein also contains the tetrapeptide sequence Arg-Gly-Asp-Ser (at residues 1744-1747), which may be a cell attachment site, as in fibronectin.
3524673	10	57	part_of	contains	911:918	arg1	The protein AND a cell attachment site	The protein		a cell attachment site		Fterm	Site	protein		site	The protein also contains the tetrapeptide sequence Arg-Gly-Asp-Ser (at residues 1744-1747), which may be a cell attachment site, as in fibronectin.
8390218	1	69	gly	1-antitrypsin	191:203	arg1	the sugar chains	alpha 1-antitrypsin			the sugar chains	PUBTATOR		alpha 1-antitrypsin	5265		Chemical structures of the sugar chains of alpha 1-antitrypsin (AAT) from patients with hepatocellular carcinoma (HCC) and from healthy individuals with a different affinity for Lens culinaris agglutinin (LCA) were examined by pyridylamination of their oligosaccharides and stepwise exoglycosidase digestion in combination with reversed-phase and size-fractionation high-performance liquid chromatography.
16332679	7	5	gly	O-glycosylation	937:951	arg1	Sp1	Sp1				OGER		Sp1	P08047		The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early (approximately 30 min), followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min.
10022822	3	26	part_of	type-1	523:528	arg1	the thyroglobulin type-1 domains	thyroglobulin type-1		the thyroglobulin type-1 domains		OGER	Site	thyroglobulin type-1	P01266	domains	The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L.
10022822	3	42	part_of	thyroglobulin	509:521	arg1	the thyroglobulin type-1 domains	thyroglobulin type-1		the thyroglobulin type-1 domains		OGER	Site	thyroglobulin type-1	P01266	domains	The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L.
10022822	3	43	part_of	p41	476:478	arg1	the p41 fragment	structure of the p41		the p41 fragment		PUBTATOR	Site	structure of the p41	2035	fragment	The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L.
21606496	4	7	gly	glycosylation	543:555	arg1	2B4	2B4				PUBTATOR		2B4	51744		Using a recombinant fusion protein of the extracellular domain of 2B4, we demonstrate that N-linked glycosylation of 2B4 is essential for the binding to its ligand CD48.
22745122	1	43	part_of	proteins	256:263	arg1	serine	proteins		serine and threonine residues		Fterm	AminoAcid	proteins		serine and threonine residues	O-linked-N-acetyl-glucosamine glycosylation (O-GlcNAcylation) of the serine and threonine residues of cellular proteins is a dynamic process and affects phosphorylation.
18061361	0	28	gly	glycosylation	63:75	arg1	the sodium-coupled bicarbonate transporter NCBE	the sodium-coupled bicarbonate transporter NCBE				OGER		bicarbonate transporter NCBE	Q9Y6M7		Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
2040277	0	0	gly	glycoproteins	107:119	arg1	respiratory-mucus glycoproteins	respiratory-mucus glycoproteins				Fterm		glycoproteins			Isolation and structural characterization of novel neutral oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
7681597	1	30	part_of	GPA-1	265:269	arg1	the glycopeptides	GPA		the glycopeptides		OGER	Site	GPA	P02724	glycopeptides	Glycophorin A was digested with glycoprotease (Pasteurella haemolytica) and the digest was fractionated by a combination of high-pressure column chromatographies to produce the glycopeptides GPA-1 to GPA-6.
9013598	1	68	gly	glycosylation	155:167	arg2	The sites			The sites						sites	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
22235133	6	19	part_of	IL-21R	886:891	arg1	the WSXWS motif	IL-21R		the WSXWS motif		PUBTATOR	Site	IL-21R	50615	motif	Here, we present the crystal structure of IL-21 bound to IL-21R and reveal that the WSXWS motif of IL-21R is C-mannosylated at the first tryptophan.
29741879	3	63	gly	glycopeptides	702:714	arg2	previously unidentified N-linked glycopeptides			previously unidentified N-linked glycopeptides						glycopeptides	In this study, we describe the reanalysis of global proteomic data from breast cancer xenograft tissues using recently developed software package GPQuest 2.0, revealing a large number of previously unidentified N-linked glycopeptides.
24090084	10	25	gly	glycoproteins	1641:1653	arg1	161 rat brain glycoproteins	161 rat brain glycoproteins				Fterm		glycoproteins			This multidimensional approach allowed confident identification of 863 unique intact N-linked glycopeptides from 161 rat brain glycoproteins.
24090084	10	80	gly	glycopeptides	1608:1620	arg1	161 rat brain glycoproteins	glycoproteins		glycopeptides		Fterm		glycoproteins		glycopeptides	This multidimensional approach allowed confident identification of 863 unique intact N-linked glycopeptides from 161 rat brain glycoproteins.
24721674	6	62	part_of	proteins	1378:1385	arg1	811 N-glycosylation sites	proteins		811 N-glycosylation sites		Fterm	Site	proteins		sites	200μg total protein digest was processed using this approach, leading to the identification of 811 N-glycosylation sites from 567 proteins within two experimental replicates.
9343410	6	1	gly	glycosylation	1174:1186	arg2	the mapped glycosylation site			the mapped glycosylation site						site	In HeLa cells, the mutation at the mapped glycosylation site was permissive for transcriptional activation.
1388166	3	65	gly	glycoproteins	569:581	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Oligosaccharides terminating with this sequence have previously been described on lutropin, thyrotropin, and pro-opiomelanocortin: glycoproteins synthesized in the anterior pituitary.
26859261	7	4	part_of	Izumo1	1603:1608	arg1	the amino-terminal domain	Izumo1		the amino-terminal domain		PUBTATOR	Site	Izumo1	284359	domain	Furthermore, structural similarity between Juno and the cholesterol-binding Niemann-Pick disease type C1 protein (NPC1) suggests how the modified binding surface of Juno may recognize the helical structure of the amino-terminal domain of Izumo1.
7574684	2	62	part_of	trkB	503:506	arg1	the extracellular domain	trkB		the extracellular domain		PUBTATOR	Site	trkB	4915	domain	The extracellular domain contains 398 amino acids and has a molecular weight of 60.6 kDa according to laser desorption mass spectrometry, indicating that the extracellular domain of trkB contains 33.3% carbohydrate moieties.
26146185	1	14	part_of	receptor	163:170	arg1	three scavenger receptor cysteine rich (SRCR) domains	receptor		three scavenger receptor cysteine rich (SRCR) domains		Fterm	Site	receptor		domains	CD6 is a transmembrane protein with an extracellular region containing three scavenger receptor cysteine rich (SRCR) domains.
26146185	1	19	part_of	protein	99:105	arg1	an extracellular region	protein		an extracellular region		Fterm	Site	protein		region	CD6 is a transmembrane protein with an extracellular region containing three scavenger receptor cysteine rich (SRCR) domains.
26146185	1	16	part_of	containing	136:145	arg1	an extracellular region AND three scavenger receptor cysteine rich (SRCR) domains	an extracellular region		three scavenger receptor cysteine rich (SRCR) domains						domains	CD6 is a transmembrane protein with an extracellular region containing three scavenger receptor cysteine rich (SRCR) domains.
19563754	4	8	part_of	NPC1	464:467	arg1	the N-terminal domain	NPC1		the N-terminal domain		PUBTATOR	Site	NPC1	O15118	domain	Here, we describe high-resolution structures of the N-terminal domain (NTD) of NPC1 and complexes with cholesterol and 25-hydroxycholesterol.
3651384	3	33	part_of	protein	516:522	arg1	the entire protein coding sequence	protein		the entire protein coding sequence		Fterm	Site	protein		sequence	A plasmid cDNA library was constructed from immunopurified mRNA, and a recombinant clone containing the entire protein coding sequence of SGP-2 was isolated.
3651384	3	56	part_of	SGP-2	543:547	arg1	the entire protein coding sequence	SGP-2		the entire protein coding sequence		PUBTATOR	Site	SGP-2	24854	sequence	A plasmid cDNA library was constructed from immunopurified mRNA, and a recombinant clone containing the entire protein coding sequence of SGP-2 was isolated.
9757569	0	23	gly	glycosylation	11:23	arg1	the residue			residue at position 14						residue at position 14	Effects of glycosylation of the residue at position 14 in ovine angiotensinogen on the human renin reaction.
9757569	0	23	gly	glycosylation	11:23	arg1	the human renin reaction	renin		residue at position 14		PUBTATOR		renin	5972	residue at position 14	Effects of glycosylation of the residue at position 14 in ovine angiotensinogen on the human renin reaction.
9757569	0	23	gly	glycosylation	11:23	arg1	the human renin reaction	renin		residue at position 14		PUBTATOR		renin	5972	residue at position 14	Effects of glycosylation of the residue at position 14 in ovine angiotensinogen on the human renin reaction.
10715549	10	39	gly	N-glycosylation	1664:1678	arg1	Asn			Asn(13)						Asn(13)	Moreover, N-glycosylation at Asn(13) does not prevent such aggregation, but instead plays an important role in correct folding for both LHbeta- and CGbeta-subunits to be secreted as monomer.
10715549	10	39	gly	N-glycosylation	1664:1678	arg2	Asn			Asn(13)						Asn(13)	Moreover, N-glycosylation at Asn(13) does not prevent such aggregation, but instead plays an important role in correct folding for both LHbeta- and CGbeta-subunits to be secreted as monomer.
10715549	10	39	gly	N-glycosylation	1664:1678	arg1	13			Asn(13)						Asn(13)	Moreover, N-glycosylation at Asn(13) does not prevent such aggregation, but instead plays an important role in correct folding for both LHbeta- and CGbeta-subunits to be secreted as monomer.
10715549	10	39	gly	N-glycosylation	1664:1678	arg2	Asn			Asn(13)						Asn(13)	Moreover, N-glycosylation at Asn(13) does not prevent such aggregation, but instead plays an important role in correct folding for both LHbeta- and CGbeta-subunits to be secreted as monomer.
10715549	10	39	gly	N-glycosylation	1664:1678	arg1	13			Asn(13)						Asn(13)	Moreover, N-glycosylation at Asn(13) does not prevent such aggregation, but instead plays an important role in correct folding for both LHbeta- and CGbeta-subunits to be secreted as monomer.
10715549	10	39	gly	N-glycosylation	1664:1678	arg1	13			Asn(13)						Asn(13)	Moreover, N-glycosylation at Asn(13) does not prevent such aggregation, but instead plays an important role in correct folding for both LHbeta- and CGbeta-subunits to be secreted as monomer.
25617829	0	15	gly	N-glycosylation	0:14	arg1	GPRC6A receptor expression	GPRC6A receptor				PUBTATOR		GPRC6A receptor	222545		N-glycosylation and disulfide bonding affects GPRC6A receptor expression, function, and dimerization.
22171320	7	67	gly	glycopeptides	1075:1087	arg2	Desialylated glycopeptides			Desialylated glycopeptides						glycopeptides	Desialylated glycopeptides, released through mild acid hydrolysis, were characterized by tandem MS experiments utilizing collision induced dissociation (CID) and electron capture dissociation fragmentation techniques.
22171320	7	125	gly	Desialylated	1062:1073	arg1	Desialylated glycopeptides			Desialylated glycopeptides						glycopeptides	Desialylated glycopeptides, released through mild acid hydrolysis, were characterized by tandem MS experiments utilizing collision induced dissociation (CID) and electron capture dissociation fragmentation techniques.
19299457	4	8	part_of	TSHR	624:627	arg1	TSHR hinge region residues 261-289	TSHR		TSHR hinge region residues 261-289		PUBTATOR	SpecificSite	TSHR	25360	residues 261-289	To characterize further the CS-17 epitope, we exploited the observation that CS-17 does not recognize a chimeric receptor with TSHR hinge region residues 261-289 replaced with homologous rat LH receptor residues (13 mismatches).
19299457	4	18	part_of	receptor	691:698	arg1	homologous rat LH receptor residues	receptor		homologous rat LH receptor residues		Fterm	Site	receptor		residues	To characterize further the CS-17 epitope, we exploited the observation that CS-17 does not recognize a chimeric receptor with TSHR hinge region residues 261-289 replaced with homologous rat LH receptor residues (13 mismatches).
19299457	4	81	part_of	receptor	610:617	arg1	TSHR hinge region residues 261-289	receptor		TSHR hinge region residues 261-289		Fterm	SpecificSite	receptor		residues 261-289	To characterize further the CS-17 epitope, we exploited the observation that CS-17 does not recognize a chimeric receptor with TSHR hinge region residues 261-289 replaced with homologous rat LH receptor residues (13 mismatches).
19159218	10	22	gly	N-glycosites	1736:1747	arg2	N-glycosites			N-glycosites						N-glycosites	This study clearly demonstrated that the coverage of N-glycosites could be significantly increased due to the adoption of multiple enzyme digestion.
17803912	3	23	part_of	TLR4	355:358	arg1	the full-length ectodomain	TLR4		the full-length ectodomain		PUBTATOR	Site	TLR4	21898	ectodomain	We determined the structure of the full-length ectodomain of the mouse TLR4 and MD-2 complex.
9013598	4	80	gly	glycosylated	998:1009	arg1	Asn72			Asn72						Asn72	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	4	72	gly	glycosylated	950:961	arg1	Asn155			sites, Asn155, Asn337, and Asn586						sites, Asn155, Asn337, and Asn586	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	4	72	gly	glycosylated	950:961	arg1	three other sites			sites, Asn155, Asn337, and Asn586						sites, Asn155, Asn337, and Asn586	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	4	72	gly	glycosylated	950:961	arg1	Asn337			sites, Asn155, Asn337, and Asn586						sites, Asn155, Asn337, and Asn586	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	4	72	gly	glycosylated	950:961	arg1	three other sites			sites, Asn155, Asn337, and Asn586						sites, Asn155, Asn337, and Asn586	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	4	72	gly	glycosylated	950:961	arg1	Asn337			sites, Asn155, Asn337, and Asn586						sites, Asn155, Asn337, and Asn586	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	4	72	gly	glycosylated	950:961	arg1	Asn337			sites, Asn155, Asn337, and Asn586						sites, Asn155, Asn337, and Asn586	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
26993603	0	38	gly	N-glycosylation	5:19	arg2	Asn144			Asn144						Asn144	GP73 N-glycosylation at Asn144 reduces hepatocellular carcinoma cell motility and invasiveness.
1737041	5	53	gly	GM-CSF	1122:1127	arg1	several carbohydrate-deficient mutants	GM-CSF			several carbohydrate-deficient mutants	PUBTATOR		GM-CSF	1437		Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	5	58	gly	glycoproteins	1018:1030	arg1	other secreted glycoproteins	other secreted glycoproteins				Fterm		glycoproteins			Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
12731887	6	30	part_of	p67	1145:1147	arg1	the (60)SGTS(63) sequence	p67		the (60)SGTS(63) sequence		PUBTATOR	Site	p67	64370	sequence	These results suggest that glycosylation within the (60)SGTS(63) sequence of p67 plays an important role in its stability and thus its regulation of protein synthesis by modulating the phosphorylation of the alpha-subunit of eIF2.
8404899	10	16	gly	sialylated	1685:1694	arg1	12-14 minimal Gal beta 1-->3GalNac-->T/S O-glycan structures				12-14 minimal Gal beta 1-->3GalNac-->T/S O-glycan structures						The amount of sugar involved in O-glycosylation associated with the peanut agglutinin reactivity suggests the presence of 12-14 minimal Gal beta 1-->3GalNac-->T/S O-glycan structures which are sialylated and fucosylated.
22351761	9	49	gly	N-glycosylated	1538:1551	arg1	N-glycosylated human glypican-1 core protein	N-glycosylated human glypican-1 core protein				Fterm		protein			The crystal structure of N-glycosylated human glypican-1 core protein at 2.5 Å, the first crystal structure of a vertebrate glypican, reveals the complete disulfide bond arrangement of the conserved Cys residues, and it also extends the structural knowledge of glypicans for one α-helix and two long loops.
18490449	11	99	gly	sialylglycosylated	1747:1764	arg1	highly sialylglycosylated Opalin	highly sialylglycosylated Opalin				PUBTATOR		Opalin	226115		These results suggest a role for highly sialylglycosylated Opalin in an intermembranous function of the myelin paranodal loops in the central nervous system.
22942287	5	13	gly	glycosylated	796:807	arg1	Asn			Asn(39)						Asn(39)	For example, Asn(39) is glycosylated, whereas Cys(85) mediates the assembly of higher order oligomeric structure.
2108149	9	80	gly	IgGs	1444:1447	arg1	the carbohydrate moieties	IgGs			the carbohydrate moieties	Cterm		IgGs			Analysis of the carbohydrate moieties of the gamma 1 chain from the homodimeric and heterodimeric IgGs and of the gamma 2b chain from the heterodimeric molecule demonstrates that the polypeptide structure of the heavy chain influences the terminal galactosylation of the glycan unit at the conserved site of glycosylation of IgGs.
2108149	9	1	gly	glycosylation	1654:1666	arg1	IgGs	IgGs		site		Cterm		IgGs		site	Analysis of the carbohydrate moieties of the gamma 1 chain from the homodimeric and heterodimeric IgGs and of the gamma 2b chain from the heterodimeric molecule demonstrates that the polypeptide structure of the heavy chain influences the terminal galactosylation of the glycan unit at the conserved site of glycosylation of IgGs.
10821832	1	59	gly	glycoprotein	331:342	arg1	a polytopic glycoprotein	a polytopic glycoprotein				Fterm		glycoprotein			The Niemann-Pick C1 (NPC1) protein is predicted to be a polytopic glycoprotein, and it contains a region with extensive homology to the sterol-sensing domains (SSD) of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-R) and sterol regulatory element binding protein cleavage-activating protein (SCAP).
10821832	1	59	gly	glycoprotein	331:342	arg1	The Niemann-Pick C1 (NPC1) protein	The Niemann-Pick C1 (NPC1) protein				Fterm		protein			The Niemann-Pick C1 (NPC1) protein is predicted to be a polytopic glycoprotein, and it contains a region with extensive homology to the sterol-sensing domains (SSD) of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-R) and sterol regulatory element binding protein cleavage-activating protein (SCAP).
3571235	4	9	part_of	sialoglycoprotein	624:640	arg1	the hydrophobic region	sialoglycoprotein		the hydrophobic region		Fterm	Site	sialoglycoprotein		region	The amino acid sequence of the intramembranous domain (residues 36-71) of glycophorin B was determined and found to be similar to that of the hydrophobic region of the major sialoglycoprotein (glycophorin A).
3571235	4	18	part_of	B	536:536	arg1	the intramembranous domain	glycophorin B		the intramembranous domain		PUBTATOR	Site	glycophorin B	2994	domain	The amino acid sequence of the intramembranous domain (residues 36-71) of glycophorin B was determined and found to be similar to that of the hydrophobic region of the major sialoglycoprotein (glycophorin A).
3571235	4	18	part_of	B	536:536	arg1	residues 36-71	glycophorin B		residues 36-71		PUBTATOR	SpecificSite	glycophorin B	2994	residues 36-71	The amino acid sequence of the intramembranous domain (residues 36-71) of glycophorin B was determined and found to be similar to that of the hydrophobic region of the major sialoglycoprotein (glycophorin A).
3571205	1	33	gly	Asparagine-linked	385:401	arg1	wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides			Asparagine	wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides					Asparagine	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	1	36	gly	glycoprotein	137:148	arg1	a predominant glycoprotein	a predominant glycoprotein				Fterm		glycoprotein			Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	1	36	gly	glycoprotein	137:148	arg1	Glycocalicin	Glycocalicin				Fterm		Glycocalicin			Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
22750213	4	34	gly	glycoprotein	682:693	arg1	PRiMA	PRiMA				PUBTATOR		PRiMA	170952		PRiMA is a glycoprotein containing two putative N-linked glycosylation sites.
22750213	4	34	gly	glycoprotein	682:693	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			PRiMA is a glycoprotein containing two putative N-linked glycosylation sites.
22750213	4	46	gly	glycosylation	728:740	arg2	two putative N-linked glycosylation sites			two putative N-linked glycosylation sites						sites	PRiMA is a glycoprotein containing two putative N-linked glycosylation sites.
8617200	4	2	gly	LTBP-1	842:847	arg1	the third 8-Cys repeat	LTBP-1			the third 8-Cys repeat	PUBTATOR		LTBP-1	4052		Immunoblotting of the fusion protein complexes indicated that the third 8-Cys repeat of LTBP-1 bound covalently to the LAP region of TGF-beta1.
8617200	4	8	gly	8-Cys	826:830	arg1	the third 8-Cys repeat			Cys	the third 8-Cys repeat					Cys	Immunoblotting of the fusion protein complexes indicated that the third 8-Cys repeat of LTBP-1 bound covalently to the LAP region of TGF-beta1.
7841792	1	5	gly	glycosylated	264:275	arg1	each glycosylated residue			each glycosylated residue						residue	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	1	50	gly	glycosylation	325:337	arg2	individual glycosylation sites			individual glycosylation sites						sites	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
20356844	3	4	part_of	MGAM	559:562	arg1	The N-terminal catalytic domain	MGAM		The N-terminal catalytic domain		PUBTATOR	Site	MGAM	8972	domain	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
22766194	9	5	gly	N-glycosylation	1567:1581	arg2	Asn			Asn(628)						Asn(628)	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg1	Asn			Asn(628)						Asn(628)	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg2	628			Asn(628)						Asn(628)	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg1	NEP activities	NEP		Asn(628)		PUBTATOR		NEP	4311	Asn(628)	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg1	Asn			Asn(628)						Asn(628)	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg2	628			Asn(628)						Asn(628)	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg1	NEP activities	NEP		Asn(628)		PUBTATOR		NEP	4311	Asn(628)	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg2	628			Asn(628)						Asn(628)	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg1	NEP activities	NEP		Asn(628)		PUBTATOR		NEP	4311	Asn(628)	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg1	NEP activities	NEP		Asn(628)		PUBTATOR		NEP	4311	Asn(628)	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
9883900	0	22	part_of	protein-5	118:126	arg1	circulating 13-kDa C-terminal fragments	protein-5		circulating 13-kDa C-terminal fragments		Fterm	Site	protein-5		fragments	Isolation and characterization of circulating 13-kDa C-terminal fragments of human insulin-like growth factor binding protein-5.
24967714	2	62	gly	present	341:347	arg2	gp120 AND 24 N-linked glycans	gp120			24 N-linked glycans	PUBTATOR		gp120	3700		Of the, on average, 24 N-linked glycans present on gp120, the glycan at Asn260 was reported to be essential for the correct expression of gp120 and gp41 in the virus particle and deletion of the N260 glycan in gp120 heavily compromised virus infectivity.
24967714	2	79	gly	Asn260	373:378	arg1	the glycan at Asn260			Asn260	the glycan at Asn260					Asn260	Of the, on average, 24 N-linked glycans present on gp120, the glycan at Asn260 was reported to be essential for the correct expression of gp120 and gp41 in the virus particle and deletion of the N260 glycan in gp120 heavily compromised virus infectivity.
2243102	6	49	gly	located	942:948	arg1	lamp-2 AND polylactosaminoglycans	lamp-2		Asn-34, Asn-93	polylactosaminoglycans	PUBTATOR		lamp-2	3920	Asn-34, Asn-93	Amino acid analysis and sequencing demonstrated that polylactosaminoglycans were located at Asn-34, Asn-93 and/or Asn-102, and Asn-195 and/or Asn-200 in lamp-1, and at Asn-4 and/or Asn-10, and Asn-279 in lamp-2.
29992770	3	77	gly	N-glycopeptides	395:409	arg2	specific N-glycopeptides			specific N-glycopeptides						N-glycopeptides	The authors aimed to use mass-spectrometry (MS) technology to find specific N-glycopeptides potentially serving as serum biomarkers for preclinical OSCC screening.
7462199	3	17	gly	glycoprotein	415:426	arg1	the glycoprotein	the glycoprotein				Fterm		glycoprotein			The yield of radioactive oligosaccharides indicated that the glycoprotein has four asparagine-linked sugar chains in one molecule.
7462199	3	21	gly	asparagine-linked	437:453	arg1	four asparagine-linked sugar chains			asparagine	four asparagine-linked sugar chains					asparagine	The yield of radioactive oligosaccharides indicated that the glycoprotein has four asparagine-linked sugar chains in one molecule.
7462199	3	10	gly	has	428:430	arg1	the glycoprotein AND four asparagine-linked sugar chains	the glycoprotein			four asparagine-linked sugar chains	Fterm		glycoprotein			The yield of radioactive oligosaccharides indicated that the glycoprotein has four asparagine-linked sugar chains in one molecule.
21053369	13	6	gly	observed	1784:1791	arg1	Asn157 AND hybrid type glycans			Asn157	hybrid type glycans					Asn157	High mannose and hybrid type glycans were only observed on Asn157.
21053369	13	6	gly	observed	1784:1791	arg1	Asn157 AND High mannose			Asn157	High mannose					Asn157	High mannose and hybrid type glycans were only observed on Asn157.
3200844	3	43	gly	glycoprotein	402:413	arg1	np62	np62				PUBTATOR		np62	65274		The major (62 kDa) nuclear pore glycoprotein (np62) was purified from rat liver nuclear envelopes by immunoaffinity chromatography and preparative gel electrophoresis.
3200844	3	43	gly	glycoprotein	402:413	arg1	The major (62 kDa) nuclear pore glycoprotein	The major (62 kDa) nuclear pore glycoprotein				Fterm		glycoprotein			The major (62 kDa) nuclear pore glycoprotein (np62) was purified from rat liver nuclear envelopes by immunoaffinity chromatography and preparative gel electrophoresis.
6427223	9	61	gly	glycosylated	1029:1040	arg2	only one site			site						site	Both carry carbohydrates in the Mr = 25,000 species whereas in the Mr = 20,000 species only one site is glycosylated.
9336835	1	78	gly	glycoprotein	126:137	arg1	Clusterin	Clusterin				PUBTATOR		Clusterin	1191		Clusterin is a ubiquitous, heterodimeric glycoprotein with multiple possible functions that are likely influenced by glycosylation.
9336835	1	78	gly	glycoprotein	126:137	arg1	a ubiquitous, heterodimeric glycoprotein	a ubiquitous, heterodimeric glycoprotein				Fterm		glycoprotein			Clusterin is a ubiquitous, heterodimeric glycoprotein with multiple possible functions that are likely influenced by glycosylation.
30140003	7	0	gly	N-glycoprotein	875:888	arg1	the substrate N-glycoprotein	the substrate N-glycoprotein				Fterm		N-glycoprotein	4249		In addition, interaction of the substrate N-glycoprotein with GnT-V likely contributes to protein-selective and site-specific glycan modification.
17591618	0	70	gly	factor	60:65	arg1	Site-specific N-glycan characterization	complement factor H			Site-specific N-glycan characterization	PUBTATOR		complement factor H	3075		Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	0	81	gly	glycoprotein	114:125	arg1	Site-specific N-glycan characterization	glycoprotein			Site-specific N-glycan characterization	Fterm		glycoprotein			Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
21056543	1	2	gly	glycoprotein	129:140	arg1	Protein C inhibitor	Protein C inhibitor				PUBTATOR		Protein C inhibitor	5104		Protein C inhibitor (PCI) is a 57-kDa glycoprotein that exists in many tissues and secretions in human.
21056543	1	2	gly	glycoprotein	129:140	arg1	a 57-kDa glycoprotein	a 57-kDa glycoprotein				Fterm		glycoprotein			Protein C inhibitor (PCI) is a 57-kDa glycoprotein that exists in many tissues and secretions in human.
7613477	6	37	gly	glycosylation	1278:1290	arg2	Two unanticipated O-linked glycosylation sites			Two unanticipated O-linked glycosylation sites						sites	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	6	56	gly	glycopeptide	1356:1367	arg2	the LCAT O-linked glycopeptide			the LCAT O-linked glycopeptide						glycopeptide	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
29402915	6	52	gly	glycosylation	1197:1209	arg1	cubilin	cubilin				PUBTATOR		cubilin	8029		Notably, the interaction between cubilin and amnionless was not sufficient, but amnionless-mediated glycosylation of cubilin was necessary for their surface expression.
30140003	4	12	part_of	GnT-V	534:538	arg1	human GnT-V luminal domain	GnT-V		human GnT-V luminal domain		PUBTATOR	Site	GnT-V	4249	domain	Here, we report crystal structures of human GnT-V luminal domain with a substrate analog.
18642129	9	80	gly	fucosylated	1308:1318	arg1	the triantennary glycans				the triantennary glycans						Moreover, the triantennary glycans were shown to be fucosylated.
2943741	6	77	gly	glycosylated	1415:1426	arg1	leukosialin	leukosialin				PUBTATOR		leukosialin	P16150		These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2023947	0	44	gly	fucosylation	40:51	arg1	the growth factor domain			domain	the growth factor domain		Site			domain	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
10861210	12	23	gly	attached	1581:1588	arg1	the endogenous site AND the oligosaccharide			the endogenous site	the oligosaccharide					site	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
26993603	3	12	gly	N-glycosylation	565:579	arg2	three GP73 N-glycosylation sites			three GP73 N-glycosylation sites						sites	We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398.
26993603	3	51	gly	sites	581:585	arg1	three GP73 N-glycosylation sites			three GP73 N-glycosylation sites						sites	We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398.
26993603	3	12	gly	N-glycosylation	565:579	arg2	Asn109			Asn109, Asn144 and Asn398						Asn109, Asn144 and Asn398	We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398.
26993603	3	12	gly	N-glycosylation	565:579	arg2	Asn398			Asn109, Asn144 and Asn398						Asn109, Asn144 and Asn398	We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398.
26993603	3	12	gly	N-glycosylation	565:579	arg2	Asn398			Asn109, Asn144 and Asn398						Asn109, Asn144 and Asn398	We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398.
26993603	3	51	gly	sites	581:585	arg1	Asn144			Asn109, Asn144 and Asn398						Asn109, Asn144 and Asn398	We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398.
26993603	3	51	gly	sites	581:585	arg1	Asn109			Asn109, Asn144 and Asn398						Asn109, Asn144 and Asn398	We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398.
26993603	3	51	gly	sites	581:585	arg1	Asn109			Asn109, Asn144 and Asn398						Asn109, Asn144 and Asn398	We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398.
19574954	5	18	part_of	factor	1011:1016	arg1	the Von Willebrand factor A-type domain	Von Willebrand factor A-type		the Von Willebrand factor A-type domain		OGER	Site	Von Willebrand factor A-type	P04275	domain	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	5	23	part_of	A-type	1018:1023	arg1	the Von Willebrand factor A-type domain	Von Willebrand factor A-type		the Von Willebrand factor A-type domain		OGER	Site	Von Willebrand factor A-type	P04275	domain	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
8702840	3	46	gly	modified	469:476	arg3	NF-L AND O-GlcNAc	NF-L			O-GlcNAc	PUBTATOR		NF-L	4747		NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	46	gly	modified	469:476	arg3	NF-M AND O-GlcNAc	NF-M			O-GlcNAc	PUBTATOR		NF-M	4741		NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	46	gly	modified	469:476	arg3	NF-L AND O-linked N-acetylglucosamine	NF-L			O-linked N-acetylglucosamine	PUBTATOR		NF-L	4747		NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	46	gly	modified	469:476	arg3	NF-M AND O-linked N-acetylglucosamine	NF-M			O-linked N-acetylglucosamine	PUBTATOR		NF-M	4741		NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
1512232	4	5	part_of	sites	613:617	arg1	transcription factors	factors		sites		Fterm	Site	factors		sites	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	4	40	part_of	factors	662:668	arg1	the actual sites	factors		the actual sites		Fterm	Site	factors		sites	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
2129367	10	3	gly	presence	1299:1306	arg2	protein Z AND the unique trisaccharide structure	protein Z			the unique trisaccharide structure	Cterm		protein Z			The presence of the unique trisaccharide structure in factors VII, IX and protein Z leads us to anticipate its biological role in the tissue factor pathway.
2129367	10	3	gly	presence	1299:1306	arg1	factors VII AND the unique trisaccharide structure	factors VII			the unique trisaccharide structure	Cterm		VII			The presence of the unique trisaccharide structure in factors VII, IX and protein Z leads us to anticipate its biological role in the tissue factor pathway.
22344443	3	3	part_of	receptor	561:568	arg1	amino terminus	receptor		amino terminus		Fterm	Site	receptor		terminus	Extracellular access to the binding pocket is occluded by the amino terminus and extracellular loops of the receptor.
10644446	5	9	part_of	455-acid	713:720	arg1	a 455-acid polypeptide	455-acid		a 455-acid polypeptide		Cterm	Site	455-acid		polypeptide	Murine ANGPTL3 is a 455-acid polypeptide encoded by seven exons on mouse chromosome 4, spanning about 11 kb of DNA.
10644446	5	27	part_of	Murine	693:698	arg1	a 455-acid polypeptide	Murine ANGPTL3		a 455-acid polypeptide		PUBTATOR	Site	Murine ANGPTL3	30924	polypeptide	Murine ANGPTL3 is a 455-acid polypeptide encoded by seven exons on mouse chromosome 4, spanning about 11 kb of DNA.
19864504	5	7	gly	glycosylation	864:876	arg2	all glycosylation sites			all glycosylation sites						sites	Depending on the culture conditions and the cell line expressing the enzyme, we detected a high variability of the high-mannose-type N-glycans which prevail at all glycosylation sites.
3497398	10	66	part_of	contains	1528:1535	arg1	The determined sequence AND residues 29-193	The determined sequence		residues 29-193						residues 29-193	The determined sequence of the alpha chain of glycoprotein Ib contains a region (residues 29-193) with seven repeats, which is indicative of gene duplication and is highly homologous to human leucine-rich alpha 2-glycoprotein.
3497398	10	66	part_of	contains	1528:1535	arg1	The determined sequence AND a region	The determined sequence		a region						region	The determined sequence of the alpha chain of glycoprotein Ib contains a region (residues 29-193) with seven repeats, which is indicative of gene duplication and is highly homologous to human leucine-rich alpha 2-glycoprotein.
27626375	3	48	part_of	receptors	561:569	arg1	the pore-forming transmembrane domains	receptors		the pore-forming transmembrane domains		Fterm	Site	receptors		domains	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
18340083	6	22	gly	glycan	846:851	arg1	GPIHBP1	GPIHBP1			glycan	PUBTATOR		GPIHBP1	68453		The glycan was marginally sensitive to endoglycosidase F2 digestion but resistant to endoglycosidase F3 digestion, suggesting that the glycan on GPIHBP1 is of the oligomannose type.
25759508	3	37	gly	O-glycosylation	402:416	arg1	the IgG3 hinge region			the IgG3 hinge region						region	This study reports partial O-glycosylation of the IgG3 hinge region, observed with nanoLC-ESI-IT-MS(/MS) analysis after proteolytic digestion.
8223648	5	62	gly	carry	502:506	arg1	natural IFN-omega 1 AND complex-type oligosaccharides	natural IFN-omega 1			complex-type oligosaccharides	PUBTATOR		IFN-omega 1	3467		While natural IFN-omega 1 was shown to carry complex-type oligosaccharides [Adolf, G. R., Maurer-Fogy, I., Kalsner, I. & Cantell, K. (1990) J. Biol.
16537470	3	86	gly	chain	621:625	arg1	the galactose moiety	chain			the galactose moiety	OGER		chain	12479		For GalA-GSL, a shorter fatty acyl chain, an absence of the 4-OH on the sphingosine tail and a 6'-COOH group on the galactose moiety account for its observed antigenic potency.
9136890	6	56	gly	containing	756:765	arg1	Peptides AND carbohydrate			Peptides	carbohydrate						Peptides containing carbohydrate were subjected to amino acid sequencing to identify the specific Asn residue.
1530634	3	21	part_of	R13-Ag	434:439	arg1	The amino acid sequence	R13-Ag		The amino acid sequence		PUBTATOR	Site	R13-Ag	12484	sequence	The amino acid sequence of the affinity-purified R13-Ag corresponded to that predicted from the cDNA for the murine heat-stable antigen.
26598643	8	34	gly	O-glycosylation	1465:1479	arg2	the O-glycosylation sites			the O-glycosylation sites						sites glycopeptides	To pinpoint the O-glycosylation sites glycopeptides were fragmented using electron transfer dissociation.
26598643	8	39	gly	glycopeptides	1487:1499	arg2	glycopeptides			glycopeptides						sites glycopeptides	To pinpoint the O-glycosylation sites glycopeptides were fragmented using electron transfer dissociation.
28489325	0	43	gly	Microheterogeneity	20:37	arg1	N-Glycans				N-Glycans						Reducing Macro- and Microheterogeneity of N-Glycans Enables the Crystal Structure of the Lectin and EGF-Like Domains of Human L-Selectin To Be Solved at 1.9 Å Resolution.
9748270	3	67	part_of	XVII	345:348	arg1	recombinant collagen XVII fragments	XVII		recombinant collagen XVII fragments		Cterm	Site	XVII		fragments	Using domain-specific antibodies against recombinant collagen XVII fragments, we identified two molecular forms of the collagen in human skin and epithelial cells.
26280335	5	14	part_of	nicastrin	803:811	arg1	nicastrin extracellular domain	nicastrin		nicastrin extracellular domain		PUBTATOR	Site	nicastrin	23385	domain	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	5	50	part_of	PS1	693:695	arg1	The active site	PS1		The active site		PUBTATOR	Site	PS1	P49768	site	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
15253437	4	2	gly	glycosylation	987:999	arg2	the glycosylation site			the glycosylation site						site	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	4	29	gly	glycopeptides	899:911	arg2	glycopeptides			glycopeptides						glycopeptides	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
2033371	1	38	gly	sialoglycoprotein	254:270	arg1	the major T lymphocyte sialoglycoprotein CD43	the major T lymphocyte sialoglycoprotein CD43				Fterm		sialoglycoprotein			The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
1421757	3	4	gly	O-glycosylation	426:440	arg2	the site			the site						site	Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104.
1421757	3	4	gly	O-glycosylation	426:440	arg2	Thr-104			Thr-104						Thr-104	Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104.
1898343	4	33	gly	glycopeptides	446:458	arg2	resulting glycopeptides			resulting glycopeptides						glycopeptides	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	4	51	gly	liberated	421:429	arg1	resulting glycopeptides AND Oligosaccharides			resulting glycopeptides	Oligosaccharides					glycopeptides	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
10022822	7	47	part_of	enzymes	1254:1260	arg1	the R-domain	enzymes		the R-domain		Fterm	Site	enzymes		R-domain	However, the different fold of the p41 fragment results in additional contacts with the top of the R-domain of the enzymes, which defines the specificity-determining S2 and S1' substrate-binding sites.
10022822	7	70	part_of	p41	1174:1176	arg1	the p41 fragment	p41		the p41 fragment		PUBTATOR	Site	p41	2035	fragment	However, the different fold of the p41 fragment results in additional contacts with the top of the R-domain of the enzymes, which defines the specificity-determining S2 and S1' substrate-binding sites.
19349973	4	47	gly	N-glycoproteins	1089:1103	arg1	the cell surface N-glycoproteins	the cell surface N-glycoproteins				Fterm		N-glycoproteins			A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	4	51	gly	N-glycoproteins	1140:1154	arg1	N-glycoproteins	N-glycoproteins				Fterm		N-glycoproteins			A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
3651384	2	13	gly	glycosylated	253:264	arg1	a cotranslationally glycosylated 64-kDa precursor	a cotranslationally glycosylated 64-kDa precursor				Fterm		precursor			Pulse-chase labeling shows that SGP-2 is synthesized as a cotranslationally glycosylated 64-kDa precursor that is modified to a negatively charged 73-kDa form before intracellular cleavage to the mature 47- and 34-kDa subunits.
3651384	2	13	gly	glycosylated	253:264	arg1	SGP-2	SGP-2				PUBTATOR		SGP-2	24854		Pulse-chase labeling shows that SGP-2 is synthesized as a cotranslationally glycosylated 64-kDa precursor that is modified to a negatively charged 73-kDa form before intracellular cleavage to the mature 47- and 34-kDa subunits.
2514791	2	115	part_of	t-PA	194:197	arg1	The t-PA polypeptide	t-PA		The t-PA polypeptide		PUBTATOR	Site	t-PA	5327	polypeptide	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
15066430	1	6	gly	glycoprotein	208:219	arg1	an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein	an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein				Fterm		glycoprotein			Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	1	6	gly	glycoprotein	208:219	arg1	Carboxypeptidase M	Carboxypeptidase M				PUBTATOR		Carboxypeptidase M	1368		Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
1326557	9	2	gly	O-glycosylation	1963:1977	arg2	25 potential threonine O-glycosylation sites			25 potential threonine O-glycosylation sites						sites	The proteoglycan contains six potential N-glycosylation sites and 25 potential threonine O-glycosylation sites.
1326557	9	90	gly	N-glycosylation	1914:1928	arg2	six potential N-glycosylation sites			six potential N-glycosylation sites						sites	The proteoglycan contains six potential N-glycosylation sites and 25 potential threonine O-glycosylation sites.
25759508	6	57	gly	O-glycosylation	907:921	arg2	the site			the site						site	NanoLC-ESI-IT-MS/MS with electron transfer dissociation fragmentation and CE-MS/MS with CID fragmentation were used to determine the site of IgG3 O-glycosylation.
1899031	1	2	gly	linked	165:170	arg1	Asn289 AND The oligosaccharide structures			Asn289	The oligosaccharide structures					Asn289	The oligosaccharide structures linked to Asn289 of a recombinant (r) variant (R561S) human plasminogen (HPg) expressed in Chinese hamster ovary (CHO) cells, after transfection of these cells with a plasmid containing the cDNA coding for the variant HPg, have been determined.
2226832	0	24	gly	glycoprotein	113:124	arg1	a human neutrophil granule-derived antibacterial and monocyte-specific chemotactic glycoprotein	glycoprotein		sequence		Fterm		glycoprotein		sequence	Amino acid sequence of CAP37, a human neutrophil granule-derived antibacterial and monocyte-specific chemotactic glycoprotein structurally similar to neutrophil elastase.
22556278	0	22	gly	subunits	45:52	arg1	O-GlcNAc sites	subunits			O-GlcNAc sites	Fterm		subunits			Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel biotin-cystamine tag.
22556278	0	26	gly	Hsp90	58:62	arg1	O-GlcNAc sites	Hsp90			O-GlcNAc sites	PUBTATOR		Hsp90	P08238		Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel biotin-cystamine tag.
23269669	9	51	gly	glycosylation	1561:1573	arg1	proteins	proteins				Fterm		proteins			Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
27551080	5	2	gly	glycoprotein	749:760	arg1	the primed Ebola virus glycoprotein	the primed Ebola virus glycoprotein				Fterm		glycoprotein			NPC1-MLD uses two protruding loops to bind NPC2, analogous to its interaction with the primed Ebola virus glycoprotein.
14711516	6	3	gly	Recombinant	1003:1013	arg1	GlcNAc	Recombinant Thy-1			GlcNAc	PUBTATOR		Recombinant Thy-1	P04216		Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5).
14711516	6	3	gly	Recombinant	1003:1013	arg1	2	Recombinant Thy-1			2	PUBTATOR		Recombinant Thy-1	P04216		Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5).
14711516	6	3	gly	Recombinant	1003:1013	arg1	Man	Recombinant Thy-1			Man	PUBTATOR		Recombinant Thy-1	P04216		Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5).
14711516	6	3	gly	Recombinant	1003:1013	arg1	5	Recombinant Thy-1			5	PUBTATOR		Recombinant Thy-1	P04216		Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5).
14711516	6	41	gly	oligosaccharides	1097:1112	arg1	asparagine 23 and 100			asparagine 23 and 100	asparagine 23 and 100		SpecificSite			asparagine 23 and 100	Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5).
14711516	6	41	gly	oligosaccharides	1097:1112	arg1	100			100	100		SpecificSite			asparagine 23 and 100	Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5).
26828122	6	51	gly	N-glycosylation	1118:1132	arg1	Asn(155)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg2	Asn(155)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg1	Asn(69)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg2	Asn(393)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg2	Asn(69)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg2	Asn(155)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg1	Asn(69)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg2	Asn(393)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg2	Asn(69)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg1	Asn(69)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg2	Asn(393)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg2	Asn(69)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg2	Asn(393)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg2	Asn(69)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
26828122	6	51	gly	N-glycosylation	1118:1132	arg2	Asn(69)			Asn(69), Asn(155), and Asn(393)						Asn(69), Asn(155), and Asn(393)	However, only N-glycosylation at Asn(69), Asn(155), and Asn(393) appeared to be important for transporter functionality possibly through an effect on protein conformation and/or interaction with its ligand (but not through changes in expression at the cell membrane as determined by live cell confocal imaging).
1472036	0	7	part_of	receptor	110:117	arg1	the extracellular domain	insulin receptor		the extracellular domain		PUBTATOR	Site	insulin receptor	3643	domain	Identification of a disulfide bridge connecting the alpha-subunits of the extracellular domain of the insulin receptor.
17286803	1	64	gly	glycoprotein	161:172	arg1	the polytopic lysosomal membrane glycoprotein CLN3	the polytopic lysosomal membrane glycoprotein CLN3				Fterm		glycoprotein			Mutations in the polytopic lysosomal membrane glycoprotein CLN3 result in a severe neurodegenerative disorder.
15253437	1	5	gly	glycoproteins	189:201	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	1	17	gly	attached	340:347	arg2	each glycosylation site AND all glycan structures			each glycosylation site	all glycan structures					site	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	1	62	gly	glycosylation	357:369	arg2	each glycosylation site			each glycosylation site						site	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
28753425	5	0	part_of	vasopressin-2	944:956	arg1	the phosphorylated vasopressin-2 receptor tail	vasopressin-2 receptor		the phosphorylated vasopressin-2 receptor tail		PUBTATOR	Site	vasopressin-2 receptor	554	tail	These two phospho-residues, together with E341, form an extensive network of electrostatic interactions with three positively charged pockets in arrestin in a mode that resembles binding of the phosphorylated vasopressin-2 receptor tail to β-arrestin-1.
28753425	5	12	part_of	receptor	958:965	arg1	the phosphorylated vasopressin-2 receptor tail	vasopressin-2 receptor		the phosphorylated vasopressin-2 receptor tail		PUBTATOR	Site	vasopressin-2 receptor	554	tail	These two phospho-residues, together with E341, form an extensive network of electrostatic interactions with three positively charged pockets in arrestin in a mode that resembles binding of the phosphorylated vasopressin-2 receptor tail to β-arrestin-1.
21308849	2	32	gly	leucine-rich	217:228	arg1	LRR			leucine	LRR					leucine	NgRs are composed of a leucine-rich repeat (LRR) region, thought to be structurally similar among the different isoforms of the receptor, and a divergent "stalk" region.
21308849	2	32	gly	leucine-rich	217:228	arg1	leucine-rich repeat			leucine	leucine-rich repeat					leucine	NgRs are composed of a leucine-rich repeat (LRR) region, thought to be structurally similar among the different isoforms of the receptor, and a divergent "stalk" region.
22660477	6	22	part_of	GBR2	747:750	arg1	the GBR2 ectodomain	structure of the GBR2		the GBR2 ectodomain		Cterm	Site	structure of the GBR2		ectodomain	We present the crystal structure of the GBR2 ectodomain, which reveals a polar heterodimeric interface.
15014436	8	44	part_of	TSP	1037:1039	arg1	the TSP C-terminal region	TSP		the TSP C-terminal region		OGER	Site	TSP	P07996	region	The central architectural role of calcium explains how it is critical for the functions of the TSP C-terminal region.
1400872	3	22	part_of	SHBG	685:688	arg1	the SHBG polypeptide	SHBG		the SHBG polypeptide		PUBTATOR	Site	SHBG	P04278	polypeptide	Sequence analysis of these exons revealed a point mutation encoding an amino acid substitution (Asp --> Asn) at residue 327 in the SHBG polypeptide, and the same mutation was identified in three siblings who also appear to be homozygous for this trait.
22226965	3	36	gly	modified	487:494	arg1	PPARγ AND O-GlcNAc	PPARγ			O-GlcNAc	PUBTATOR		PPARγ 	19016		Here, we report that PPARγ is modified by O-GlcNAc in 3T3-L1 adipocytes.
15486088	5	26	gly	located	949:955	arg1	the active-site face AND the three potential lectin domain carbohydrate-binding sites			the active-site face	the three potential lectin domain carbohydrate-binding sites					face	Each of the three potential lectin domain carbohydrate-binding sites (alpha, beta, and gamma) is located on the active-site face of the enzyme, suggesting a mechanism by which the transferase may accommodate multiple conformations of glycosylated acceptor substrates.
15486088	5	74	gly	domain	887:892	arg1	the three potential lectin domain carbohydrate-binding sites				the three potential lectin domain carbohydrate-binding sites						Each of the three potential lectin domain carbohydrate-binding sites (alpha, beta, and gamma) is located on the active-site face of the enzyme, suggesting a mechanism by which the transferase may accommodate multiple conformations of glycosylated acceptor substrates.
26271046	10	56	part_of	GluA2	1803:1807	arg1	the N413	GluA2		the N413		PUBTATOR	SpecificSite	GluA2	2891	N413	The HNK-1 epitope on N-glycan at the N413 of GluA2 was also involved in the cell surface expression of GluA1.
16732286	3	1	part_of	factor	472:477	arg1	the three epidermal growth factor domains	factor		the three epidermal growth factor domains		Fterm	Site	factor		domains	In contrast to prediction, Tie2 contains not two but three immunoglobulin (Ig) domains, which fold together with the three epidermal growth factor domains into a compact, arrowhead-shaped structure.
16732286	3	13	part_of	contains	364:371	arg1	Tie2 AND not two but three immunoglobulin (Ig) domains	Tie2		not two but three immunoglobulin (Ig) domains		PUBTATOR	Site	Tie2	7010	domains	In contrast to prediction, Tie2 contains not two but three immunoglobulin (Ig) domains, which fold together with the three epidermal growth factor domains into a compact, arrowhead-shaped structure.
8615697	2	2	gly	glycopeptides	293:305	arg2	the glycopeptides			the glycopeptides						glycopeptides	We have characterized the glycopeptides contained in a tryptic digest of hTG in order to determine which sites are actually linked to carbohydrate.
21980294	0	63	gly	glycoprotein	34:45	arg1	herpes simplex virus glycoprotein D	herpes simplex virus glycoprotein D				PUBTATOR		glycoprotein D	2532		Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1.
2215480	1	35	gly	glycoprotein	227:238	arg1	a T-cell-derived glycoprotein	a T-cell-derived glycoprotein				Fterm		glycoprotein			T-cell-replacing factor (TRF)/IL-5 is a T-cell-derived glycoprotein which has pleiotropic activity on lymphoid and myeloid cells.
2215480	1	35	gly	glycoprotein	227:238	arg1	T-cell-replacing factor (TRF)/IL-5	T-cell-replacing factor (TRF)/IL-5				PUBTATOR		IL-5	16191		T-cell-replacing factor (TRF)/IL-5 is a T-cell-derived glycoprotein which has pleiotropic activity on lymphoid and myeloid cells.
1059087	1	12	gly	sialoglycoprotein	114:130	arg1	Glycophorin	Glycophorin				Fterm		Glycophorin			Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	1	12	gly	sialoglycoprotein	114:130	arg1	the major sialoglycoprotein	the major sialoglycoprotein				Fterm		sialoglycoprotein			Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
28775322	2	12	part_of	EGF-like	339:346	arg1	folded EGF-like domains	EGF		folded EGF-like domains		OGER	Site	EGF	P01133	domains	Protein O-glucosyltransferase 1 shows specificity for folded EGF-like domains, it can only glycosylate serine residues in the C1XSXPC2 motif, and it possesses an uncommon dual donor substrate specificity.
16212939	0	46	gly	N-Glycosylation	0:14	arg1	secretion enhancer peptide			secretion enhancer peptide						peptide	N-Glycosylation of secretion enhancer peptide as influencing factor for the secretion of target proteins from Saccharomyces cerevisiae.
11390601	2	85	part_of	sites	426:430	arg1	gp120	gp120		sites		PUBTATOR	Site	gp120	155971	sites	In this study, specific glycosylation sites on gp120 of a dualtropic primary HIV-1 isolate, DH12, were eliminated by site-directed mutagenesis and the properties of the resulting mutant envelopes were evaluated using a recombinant vaccinia virus-based cell-to-cell fusion assay alone or in the context of viral infections.
25485983	1	6	gly	glycoforms	191:200	arg1	this key anticoagulant serpin	this key anticoagulant serpin				Fterm		serpin			The inefficient glycosylation of consensus sequence on N135 in antithrombin explains the two glycoforms of this key anticoagulant serpin found in plasma: α and β, with four and three N-glycans, respectively.
25485983	1	41	gly	glycosylation	114:126	arg1	N135			N135						N135	The inefficient glycosylation of consensus sequence on N135 in antithrombin explains the two glycoforms of this key anticoagulant serpin found in plasma: α and β, with four and three N-glycans, respectively.
25485983	1	41	gly	glycosylation	114:126	arg1	antithrombin	antithrombin		N135		PUBTATOR		antithrombin	462	N135	The inefficient glycosylation of consensus sequence on N135 in antithrombin explains the two glycoforms of this key anticoagulant serpin found in plasma: α and β, with four and three N-glycans, respectively.
25485983	1	41	gly	glycosylation	114:126	arg1	antithrombin	antithrombin		N135		PUBTATOR		antithrombin	462	N135	The inefficient glycosylation of consensus sequence on N135 in antithrombin explains the two glycoforms of this key anticoagulant serpin found in plasma: α and β, with four and three N-glycans, respectively.
25485983	1	41	gly	glycosylation	114:126	arg1	antithrombin	antithrombin		sequence		PUBTATOR		antithrombin	462	sequence	The inefficient glycosylation of consensus sequence on N135 in antithrombin explains the two glycoforms of this key anticoagulant serpin found in plasma: α and β, with four and three N-glycans, respectively.
2668275	6	70	part_of	STS	715:717	arg1	most, if not all, sequences	STS		most, if not all, sequences		Cterm	Site	STS	412	sequences	The resistance of STS toward proteinase K after translocation into microsomes suggests that most, if not all, sequences of STS are exposed at the luminal side of microsomes.
3571205	3	42	gly	trisialylated	913:925	arg1	trisialylated complex-type oligosaccharide-alditols				trisialylated complex-type oligosaccharide-alditols						The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
15454184	1	51	gly	glycoprotein	135:146	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Follistatin (FS), a glycoprotein, plays an important role in cell growth and differentiation through the neutralization of the biological activities of activins.
15454184	1	51	gly	glycoprotein	135:146	arg1	Follistatin	Follistatin				PUBTATOR		Follistatin (FS)	10468		Follistatin (FS), a glycoprotein, plays an important role in cell growth and differentiation through the neutralization of the biological activities of activins.
20837471	5	33	gly	O-glycosylation	910:924	arg1	proteins	proteins				Fterm		proteins			We hypothesized that the GalNAc-T2 transferase performed critical O-glycosylation of proteins involved in lipid metabolism.
16877748	0	27	gly	molecule-1	86:95	arg1	N-glycan structures	intercellular adhesion molecule-1			N-glycan structures	PUBTATOR		intercellular adhesion molecule-1	15894		N-glycan structures and N-glycosylation sites of mouse soluble intercellular adhesion molecule-1 revealed by MALDI-TOF and FTICR mass spectrometry.
16877748	0	53	gly	N-glycosylation	24:38	arg2	N-glycosylation sites	intercellular adhesion molecule-1		sites		PUBTATOR		intercellular adhesion molecule-1	15894	sites	N-glycan structures and N-glycosylation sites of mouse soluble intercellular adhesion molecule-1 revealed by MALDI-TOF and FTICR mass spectrometry.
15498570	0	24	gly	glycoprotein	78:89	arg1	hPAP21	hPAP21				PUBTATOR		hPAP21	84279		N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	0	24	gly	glycoprotein	78:89	arg1	a novel human secreted glycoprotein	a novel human secreted glycoprotein				Fterm		glycoprotein			N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	0	41	gly	N-glycosylation	0:14	arg1	hPAP21	hPAP21				PUBTATOR		hPAP21	84279		N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	0	41	gly	N-glycosylation	0:14	arg1	a novel human secreted glycoprotein	a novel human secreted glycoprotein				Fterm		glycoprotein			N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
23269669	6	71	part_of	sites	1139:1143	arg1	GC-C	GC-C		sites		PUBTATOR	Site	GC-C	2984	sites	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
12483204	3	11	part_of	DPP-IV	434:439	arg1	the extracellular region	DPP-IV		the extracellular region		PUBTATOR	Site	DPP-IV	1803	region	We have determined the 2.5 A structure of the extracellular region of DPP-IV in complex with the inhibitor valine-pyrrolidide.
10871631	0	82	gly	glycoproteins	70:82	arg1	lumenal glycoproteins	lumenal glycoproteins				Fterm		glycoproteins			Torsin A and its torsion dystonia-associated mutant forms are lumenal glycoproteins that exhibit distinct subcellular localizations.
10871631	0	82	gly	glycoproteins	70:82	arg1	Torsin A	Torsin A				PUBTATOR		Torsin A	1861		Torsin A and its torsion dystonia-associated mutant forms are lumenal glycoproteins that exhibit distinct subcellular localizations.
1885588	8	37	gly	asparagine-linked	1446:1462	arg1	asparagine-linked oligosaccharide			asparagine	asparagine-linked oligosaccharide					asparagine	Such an orientation of the catalytic domain may facilitate the sequential processing of asparagine-linked oligosaccharide, soon after its transfer en bloc by the oligosaccharyl transferase complex in the lumen of endoplasmic reticulum.
7620335	5	77	gly	glycosylation	943:955	arg2	each glycosylation site			each glycosylation site						site	Structures of oligosaccharides and their contents at each glycosylation site were determined by a two-dimensional sugar mapping method.
27161523	3	36	part_of	isoforms	572:579	arg1	extracellular regions	isoforms		extracellular regions		Fterm	Site	isoforms		regions	Here, we report crystal structures for extracellular regions from four mouse Pcdh isoforms (α4, α7, β6, and β8), revealing a canonical head-to-tail interaction mode for homophilic trans dimers comprising primary intermolecular EC1:EC4 and EC2:EC3 interactions.
2511201	4	117	gly	linked	851:856	arg2	a serine residue AND such carbohydrate moieties			a serine residue	such carbohydrate moieties					serine residue	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	4	0	gly	contain	816:822	arg1	protein Z AND such carbohydrate moieties	protein Z			such carbohydrate moieties	Cterm		protein Z			We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	4	0	gly	contain	816:822	arg1	bovine protein Z AND such carbohydrate moieties	bovine protein Z			such carbohydrate moieties	Cterm		bovine protein Z			We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	4	0	gly	contain	816:822	arg1	human factors VII AND such carbohydrate moieties	human factors VII			such carbohydrate moieties	Cterm		VII			We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
20188224	4	71	gly	glycopeptides	578:590	arg2	glycopeptides			glycopeptides						glycopeptides	A method tailored to enable detailed analysis of the PGRN oligosaccharides and glycopeptides has been developed.
16834341	3	30	part_of	hormone	435:441	arg1	the negatively charged glycopeptides	follicle stimulating hormone		the negatively charged glycopeptides		Cterm	Site	follicle stimulating hormone		glycopeptides	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
11372680	4	10	part_of	protein	597:603	arg1	8 potential sites	protein		8 potential sites		Fterm	Site	protein		sites	The cDNA predicts a signal peptide containing 21 amino acids and a mature protein of 427 residues with 8 potential sites for N-linked glycosylation.
11372680	4	55	part_of	peptide	550:556	arg1	8 potential sites	peptide		8 potential sites						sites	The cDNA predicts a signal peptide containing 21 amino acids and a mature protein of 427 residues with 8 potential sites for N-linked glycosylation.
17395588	0	101	gly	O-fucosylation	0:13	arg1	ADAMTS-like-1/punctin-1	ADAMTS-like-1			O-fucosylation	PUBTATOR		ADAMTS-like-1	92949		O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily.
17395588	0	101	gly	O-fucosylation	0:13	arg1	ADAMTS-like-1/punctin-1	ADAMTS-like-1			thrombospondin type 1 repeats	PUBTATOR		ADAMTS-like-1	92949		O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily.
7827751	5	44	gly	Domain	654:659	arg1	Domain Col 1				Domain Col 1						Domain Col 1 was joined by disulfide bonds into a trimer, while Col 2 appeared as a mixture of monomers and disulfide-linked dimers.
1381905	10	10	gly	glycosylated	1746:1757	arg2	Asn120			Asn120						Asn120	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	10	gly	glycosylated	1746:1757	arg2	Asn120			Asn120, Asn93, and Asn65						Asn120, Asn93, and Asn65	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	10	gly	glycosylated	1746:1757	arg2	Asn93			Asn120, Asn93, and Asn65						Asn120, Asn93, and Asn65	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	10	gly	glycosylated	1746:1757	arg2	Asn93			Asn120, Asn93, and Asn65						Asn120, Asn93, and Asn65	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
2775232	8	99	part_of	domains	1616:1622	arg1	beta-subunits	beta-subunits		domains		Fterm	Site	beta-subunits		domains	Some of the general features of the structure of GPIIb, such as the existence of distinct domains in the alpha- and beta-subunits, as well as the identification of well-defined points in its external topography, are discussed.
21606496	2	56	gly	glycosylated	276:287	arg1	2B4	2B4				PUBTATOR		2B4	51744		Here we show that 2B4 is heavily and differentially glycosylated in primary human NK cells and NK cell lines.
12200435	4	46	gly	glycoprotein	645:656	arg1	Human Dpl	Human Dpl				PUBTATOR		Human Dpl	23627		Human Dpl appears to be a glycosylphosphatidylinositol-anchored glycoprotein with N- and O-linked sugars.
12200435	4	46	gly	glycoprotein	645:656	arg1	a glycosylphosphatidylinositol-anchored glycoprotein	glycoprotein			N-	Fterm		glycoprotein			Human Dpl appears to be a glycosylphosphatidylinositol-anchored glycoprotein with N- and O-linked sugars.
12200435	4	46	gly	glycoprotein	645:656	arg1	a glycosylphosphatidylinositol-anchored glycoprotein	glycoprotein			O-linked sugars	Fterm		glycoprotein			Human Dpl appears to be a glycosylphosphatidylinositol-anchored glycoprotein with N- and O-linked sugars.
21500857	6	4	gly	contains	735:742	arg1	AP180 AND a phosphorylated O-GlcNAc	AP180			a phosphorylated O-GlcNAc	PUBTATOR		AP180	65178		We now show that AP180 purified from rat brain contains a phosphorylated O-GlcNAc (O-GlcNAc-P) within a highly conserved sequence.
21500857	6	4	gly	contains	735:742	arg1	AP180 AND O-GlcNAc-P	AP180			O-GlcNAc-P	PUBTATOR		AP180	65178		We now show that AP180 purified from rat brain contains a phosphorylated O-GlcNAc (O-GlcNAc-P) within a highly conserved sequence.
22846177	5	54	part_of	vimentin	736:743	arg1	vimentin serine 71	vimentin		vimentin serine 71		PUBTATOR	SpecificSite	vimentin	7431	serine 71	The interaction with GlcNAc-bearing polymers promoted the cell surface recruitment of vimentin followed by the phosphorylation of vimentin serine 71 and the increase in tetrameric vimentin disassembled from vimentin filaments in HeLa cells.
12034704	6	23	part_of	protein	1020:1026	arg1	The protein C binding site	protein C		The protein C binding site		OGER	Site	protein C	P02810	site	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
12034704	6	43	part_of	domain	1117:1122	arg1	The protein C binding site	domain		The protein C binding site						site	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
12034704	6	66	part_of	C	1028:1028	arg1	The protein C binding site	protein C		The protein C binding site		OGER	Site	protein C	P02810	site	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
7727388	6	24	gly	occupied	1059:1066	arg2	the four potential Asn-linked glycosylation sites			the four potential Asn-linked glycosylation sites						sites	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	48	gly	glycosylation	1035:1047	arg2	the four potential Asn-linked glycosylation sites			the four potential Asn-linked glycosylation sites						sites	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	79	gly	occupied	1059:1066	arg1	N349			N349						N349	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	79	gly	occupied	1059:1066	arg1	N248			N248						N248	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	79	gly	occupied	1059:1066	arg1	N41			N41						N41	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
11912203	0	22	part_of	adiponectin	99:109	arg1	the collagenous domain	adiponectin		the collagenous domain		PUBTATOR	Site	adiponectin	9370	domain	Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin.
30659065	4	50	gly	N-glycosylation	852:866	arg2	a single N-glycosylation site			a single N-glycosylation site						site	Although IgGs usually have a single N-glycosylation site and are well studied, other antibody isotypes, e.g. IgA and IgM, that are the first responders in certain diseases, have two to five sites/monomer of antibody, and little is known about their N-glycosylation.
19951703	7	57	gly	unglycosylated	943:956	arg1	The unglycosylated UGT1A9	The unglycosylated UGT1A9				PUBTATOR		UGT1A9	54600		The unglycosylated UGT1A9 was almost inactive, which was not an indirect effect of ER stress.
23846701	9	62	part_of	HC	1095:1096	arg1	β-domains	HC		β-domains		Cterm	Site	HC	6947	β-domains	In addition, the α- and β-domains of HC form several unique interdomain contacts and have a higher shape complementarity than those of intrinsic factor and transcobalamin.
3980466	9	123	gly	underglycosylated	1695:1711	arg1	a more C-terminal underglycosylated site			a more C-terminal underglycosylated site						site	The alpha-chains of each class II antigen also contain a more C-terminal underglycosylated site where sialylation and branching are reduced to differing degrees depending upon the site.
9334252	8	13	gly	C-mannosylated	1457:1470	arg1	Recombinant RNase 2	Recombinant RNase 2				PUBTATOR		Recombinant RNase 2	6036		Recombinant RNase 2 isolated from insect cells, plant protoplasts, and Escherichia coli was not C-mannosylated.
1371281	0	54	gly	glycosylation	42:54	arg1	human cytokeratin 8 and 18	human cytokeratin 8 and 18				PUBTATOR		cytokeratin 8	3856		Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.
9574531	1	6	gly	glycosylation	219:231	arg2	Asn94			Asn94						Asn94	The HLA-DR hemizygous B lymphoblastoid cell line, 10.24.6, has a DRA mutation (Pro96-->Ser) that creates a novel glycosylation site at Asn94.
9574531	1	6	gly	glycosylation	219:231	arg2	a novel glycosylation site			a novel glycosylation site						site	The HLA-DR hemizygous B lymphoblastoid cell line, 10.24.6, has a DRA mutation (Pro96-->Ser) that creates a novel glycosylation site at Asn94.
2040275	2	50	gly	attached	385:392	arg2	the oligosaccharide AND the glycosylation site			the glycosylation site	the oligosaccharide					site	The peptide is isolated as a set of glycoforms, varying only in the sequence of the oligosaccharide attached at the glycosylation site.
2040275	2	72	gly	glycosylation	401:413	arg2	the glycosylation site			the glycosylation site						site	The peptide is isolated as a set of glycoforms, varying only in the sequence of the oligosaccharide attached at the glycosylation site.
10821832	1	10	part_of	reductase	471:479	arg1	the sterol-sensing domains	3-hydroxy-3-methylglutaryl-coenzyme A reductase		the sterol-sensing domains		PUBTATOR	Site	3-hydroxy-3-methylglutaryl-coenzyme A reductase	3156	domains	The Niemann-Pick C1 (NPC1) protein is predicted to be a polytopic glycoprotein, and it contains a region with extensive homology to the sterol-sensing domains (SSD) of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-R) and sterol regulatory element binding protein cleavage-activating protein (SCAP).
10821832	1	12	part_of	protein	555:561	arg1	the sterol-sensing domains	sterol regulatory element binding protein cleavage-activating protein		the sterol-sensing domains		PUBTATOR	Site	sterol regulatory element binding protein cleavage-activating protein	22937	domains	The Niemann-Pick C1 (NPC1) protein is predicted to be a polytopic glycoprotein, and it contains a region with extensive homology to the sterol-sensing domains (SSD) of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-R) and sterol regulatory element binding protein cleavage-activating protein (SCAP).
1388166	4	38	gly	glycoproteins	833:845	arg1	these glycoproteins	these glycoproteins				Fterm		glycoproteins			A GalNAc-transferase that recognizes the tripeptide motif Pro-Xaa-Arg/Lys 6-9 residues N-terminal to Asn glycosylation sites accounts for the specific addition of GalNAc to the oligosaccharide acceptor on these glycoproteins, whereas a GalNAc beta 1,4GlcNAc beta 1, 2Man alpha-4-sulfotransferase accounts for the addition of sulfate.
1388166	4	66	gly	glycosylation	727:739	arg2	Asn glycosylation sites			Asn glycosylation sites						sites	A GalNAc-transferase that recognizes the tripeptide motif Pro-Xaa-Arg/Lys 6-9 residues N-terminal to Asn glycosylation sites accounts for the specific addition of GalNAc to the oligosaccharide acceptor on these glycoproteins, whereas a GalNAc beta 1,4GlcNAc beta 1, 2Man alpha-4-sulfotransferase accounts for the addition of sulfate.
1388166	4	74	gly	acceptor	815:822	arg1	these glycoproteins	glycoproteins			acceptor	Fterm		glycoproteins			A GalNAc-transferase that recognizes the tripeptide motif Pro-Xaa-Arg/Lys 6-9 residues N-terminal to Asn glycosylation sites accounts for the specific addition of GalNAc to the oligosaccharide acceptor on these glycoproteins, whereas a GalNAc beta 1,4GlcNAc beta 1, 2Man alpha-4-sulfotransferase accounts for the addition of sulfate.
17157876	0	29	part_of	kininase	51:58	arg1	the human carboxypeptidase N (kininase I) catalytic domain	kininase I		the human carboxypeptidase N (kininase I) catalytic domain		PUBTATOR	Site	kininase I	1369	domain	Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain.
17157876	0	49	part_of	N	48:48	arg1	the human carboxypeptidase N (kininase I) catalytic domain	carboxypeptidase N		the human carboxypeptidase N (kininase I) catalytic domain		PUBTATOR	Site	carboxypeptidase N	1369	domain	Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain.
17157876	0	97	part_of	carboxypeptidase	31:46	arg1	the human carboxypeptidase N (kininase I) catalytic domain	carboxypeptidase N		the human carboxypeptidase N (kininase I) catalytic domain		PUBTATOR	Site	carboxypeptidase N	1369	domain	Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain.
8962717	7	44	gly	glycosylation	1202:1214	arg2	consensus glycosylation sites	proteins		sites		Fterm		proteins		sites	The large hydrodynamic mass of these oligosaccharides could influence ligand binding, an effect which is likely to vary with the difference in consensus glycosylation sites of proteins related to p170 i.e. p185erbB2/neu, p180erbB3 and p180erbB4.
18768590	7	64	gly	glycosylated	1189:1200	arg1	The complexly glycosylated TRPV5	The complexly glycosylated TRPV5				OGER		TRPV5	Q9NQA5		The complexly glycosylated TRPV5 that appears at the plasma membrane was increased by WNK3.
10092871	8	5	gly	sialylated	1357:1366	arg1	sialylated LacdiNAc				sialylated LacdiNAc						On the other hand, HT-1080 cells produce MMP-1 that has a heterogeneous glycosylation pattern, comprising diantennary glycans carrying Lewis X, LacdiNAc, sialylated LacdiNAc and GalNAc beta 1,4 (Fuc alpha 1,3)GlcNAc (LacdiNAc analogue of Lewis X) as terminal elements.
12218058	2	11	gly	glycosylation	402:414	arg2	Asn(91)			Asn(91)						Asn(91)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	11	gly	glycosylation	402:414	arg2	six potential N-linked glycosylation sites			six potential N-linked glycosylation sites						sites	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	11	gly	glycosylation	402:414	arg2	Asn(599)			Asn(599)						Asn(599)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	11	gly	glycosylation	402:414	arg2	Asn(142)			Asn(142)						Asn(142)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	11	gly	glycosylation	402:414	arg2	Asn(332)			Asn(332)						Asn(332) and Asn(363)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	gly	sites	416:420	arg1	prodomain			prodomain						prodomain	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	gly	sites	416:420	arg1	Asn(142)			Asn(142)						Asn(142)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	gly	sites	416:420	arg1	Asn(332)			Asn(332)						Asn(332) and Asn(363)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	gly	sites	416:420	arg1	six potential N-linked glycosylation sites			six potential N-linked glycosylation sites						sites	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	gly	sites	416:420	arg1	Asn(599)			Asn(599)						Asn(599)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	gly	sites	416:420	arg1	Asn(91)			Asn(91)						Asn(91)	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	gly	sites	416:420	arg1	CUB3 domain			domain						domain	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	gly	sites	416:420	arg1	metalloproteinase domain			domain						domain	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	gly	sites	416:420	arg1	metalloproteinase domain			domain						domain	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
18815274	7	36	part_of	SV2A	930:933	arg1	the fourth luminal domain	SV2A		the fourth luminal domain		PUBTATOR	Site	SV2A	64051	domain	Furthermore, we found disruption of a N-glycosylation site (N573Q) within the fourth luminal domain of SV2A rendered the mutant unable to mediate the entry of BoNT/E and also reduced the entry of BoNT/A.
24706782	9	63	gly	glycosylation	1272:1284	arg2	the glycosylation sites			the glycosylation sites						sites	A glycosylated model of pentameric IgM exhibits different accessibility of the glycosylation sites, explaining site-specific glycosylation.
24927598	7	39	part_of	N102	1011:1014	arg1	ZIP14	ZIP14		N102		PUBTATOR	SpecificSite	ZIP14	23516	N102	Asparagine-linked (N-linked) glycosylation of ZIP14, particularly the glycosylation at N102, was required for efficient membrane extraction of ZIP14 and therefore is necessary for its iron sensitivity.
7511099	2	4	gly	monosialylated	721:734	arg1	alpha 2-->6 monosialylated galactose				alpha 2-->6 monosialylated galactose						By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	16	gly	arm	769:771	arg1	alpha 2-->6 monosialylated galactose				alpha 2-->6 monosialylated galactose						By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	45	gly	arm	687:689	arg1	galactose				galactose						By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	56	gly	sialylated	890:899	arg1	the alpha 2-->6 sialylated galactose				the alpha 2-->6 sialylated galactose						By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	72	gly	sialylated	817:826	arg1	alpha 2-->3 sialylated galactose				alpha 2-->3 sialylated galactose						By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	81	gly	disialo-AFP	788:798	arg1	alpha 2-->3 sialylated galactose	AFP			alpha 2-->3 sialylated galactose	PUBTATOR		AFP	174		By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	66	gly	monosialylated	629:642	arg1	AFP-P2	AFP				PUBTATOR		AFP	174		By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
19358553	5	34	gly	glycopeptide	1236:1247	arg2	glycopeptide purification			glycopeptide purification						glycopeptide	For glycopeptide purification, a range of hydrophilic and graphite materials packed in microcolumn format proved capable of performing desalting without loss of quantitative information, but highlighted the column capacity as a critical parameter.
11372680	6	34	part_of	contains	818:825	arg1	mouse ZPI AND P1-P1'	mouse ZPI		P1-P1'		PUBTATOR	SiteSequence	ZPI	217847	P1-P1	Like human ZPI, mouse ZPI contains tyrosine-serine (P1-P1') at its reactive center in contrast to the rat molecule which contains tyrosine-cysteine.
7107587	0	33	gly	fibrinogen	32:41	arg1	Carbohydrate structure	fibrinogen			Carbohydrate structure	PUBTATOR		fibrinogen	2244		Carbohydrate structure of human fibrinogen.
10814696	2	64	gly	glycosylation	563:575	arg1	arylsulfatase A	arylsulfatase A				PUBTATOR		arylsulfatase A	410		To understand the significance of any changes in the glycosylation of arylsulfatase A in cancer, it is important to know the structure of its carbohydrate component in normal tissue.
1472036	1	17	part_of	alpha-subunits	243:256	arg1	the region	subunits		the region		OGER	Site	subunits	3643	region	The alpha 2 beta 2 structure of the insulin receptor has previously been shown to involve one disulfide bridge between the alpha-subunits in the region containing Cys435, Cys468 and Cys524.
1472036	1	5	part_of	containing	272:281	arg1	the region AND Cys468			Cys435, Cys468 and Cys524						Cys435, Cys468 and Cys524	The alpha 2 beta 2 structure of the insulin receptor has previously been shown to involve one disulfide bridge between the alpha-subunits in the region containing Cys435, Cys468 and Cys524.
1472036	1	5	part_of	containing	272:281	arg1	the region AND Cys435			Cys435, Cys468 and Cys524						Cys435, Cys468 and Cys524	The alpha 2 beta 2 structure of the insulin receptor has previously been shown to involve one disulfide bridge between the alpha-subunits in the region containing Cys435, Cys468 and Cys524.
1472036	1	5	part_of	containing	272:281	arg1	the region AND Cys435			Cys435, Cys468 and Cys524						Cys435, Cys468 and Cys524	The alpha 2 beta 2 structure of the insulin receptor has previously been shown to involve one disulfide bridge between the alpha-subunits in the region containing Cys435, Cys468 and Cys524.
20881961	4	46	part_of	semaphorin	679:688	arg1	the semaphorin 6A (Sema6A) receptor-binding fragment	semaphorin 6A		the semaphorin 6A (Sema6A) receptor-binding fragment		PUBTATOR	Site	semaphorin 6A	57556	fragment	Here we report the crystal structures of the semaphorin 6A (Sema6A) receptor-binding fragment and the plexin A2 (PlxnA2) ligand-binding fragment in both their pre-signalling (that is, before binding) and signalling (after complex formation) states.
20881961	4	48	part_of	Sema6A	694:699	arg1	the semaphorin 6A (Sema6A) receptor-binding fragment	Sema6A		the semaphorin 6A (Sema6A) receptor-binding fragment		PUBTATOR	Site	Sema6A	57556	fragment	Here we report the crystal structures of the semaphorin 6A (Sema6A) receptor-binding fragment and the plexin A2 (PlxnA2) ligand-binding fragment in both their pre-signalling (that is, before binding) and signalling (after complex formation) states.
20881961	4	56	part_of	A2	743:744	arg1	the plexin A2 (PlxnA2) ligand-binding fragment	plexin A2		the plexin A2 (PlxnA2) ligand-binding fragment		PUBTATOR	Site	plexin A2	5362	fragment	Here we report the crystal structures of the semaphorin 6A (Sema6A) receptor-binding fragment and the plexin A2 (PlxnA2) ligand-binding fragment in both their pre-signalling (that is, before binding) and signalling (after complex formation) states.
20881961	4	77	part_of	receptor-binding	702:717	arg1	the semaphorin 6A (Sema6A) receptor-binding fragment	receptor		the semaphorin 6A (Sema6A) receptor-binding fragment		Fterm	Site	receptor		fragment	Here we report the crystal structures of the semaphorin 6A (Sema6A) receptor-binding fragment and the plexin A2 (PlxnA2) ligand-binding fragment in both their pre-signalling (that is, before binding) and signalling (after complex formation) states.
25374123	10	46	gly	fucosylation	1539:1550	arg1	three hybrid and four complex glycopeptides			three hybrid and four complex glycopeptides						glycopeptides	Finally, we specifically found that three hybrid and four complex glycopeptides of triantennary forms with outer fucosylation increased in HCC human plasma.
25374123	10	25	gly	glycopeptides	1492:1504	arg2	three hybrid and four complex glycopeptides			glycopeptides	outer fucosylation					glycopeptides	Finally, we specifically found that three hybrid and four complex glycopeptides of triantennary forms with outer fucosylation increased in HCC human plasma.
25374123	10	25	gly	glycopeptides	1492:1504	arg1	triantennary forms			glycopeptides	triantennary forms					glycopeptides	Finally, we specifically found that three hybrid and four complex glycopeptides of triantennary forms with outer fucosylation increased in HCC human plasma.
1737041	3	43	gly	GM-CSF	719:724	arg1	the carbohydrate modification characteristic	GM-CSF			the carbohydrate modification characteristic	PUBTATOR		GM-CSF	1437		Previous studies have failed to detect a significant functional role for the carbohydrate modification characteristic of human GM-CSF.
2040275	7	35	gly	glycosylation	1179:1191	arg2	the glycosylation site			the glycosylation site						site	However, the presence of oligosaccharide causes a decrease in the conformational mobility of the backbone and sidechains of the peptide in the region of the glycosylation site.
24884609	5	12	part_of	ITIH4	745:749	arg1	ITIH4 tryptic/GluC glycopeptides	ITIH4		ITIH4 tryptic/GluC glycopeptides		PUBTATOR	Site	ITIH4	3700	glycopeptides	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	22	part_of	tryptic/GluC	751:762	arg1	ITIH4 tryptic/GluC glycopeptides	GluC		ITIH4 tryptic/GluC glycopeptides		PUBTATOR	Site	GluC	57733	glycopeptides	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	part_of	ITIH4	665:669	arg1	the four ITIH4 N-X-S/T sequons	ITIH4		N81, N207, N517, and N577		PUBTATOR	SpecificSite	ITIH4	3700	N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	part_of	ITIH4	665:669	arg1	N517	ITIH4		N81, N207, N517, and N577		PUBTATOR	SpecificSite	ITIH4	3700	N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	part_of	ITIH4	665:669	arg1	N577	ITIH4		N81, N207, N517, and N577		PUBTATOR	SpecificSite	ITIH4	3700	N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	part_of	ITIH4	665:669	arg1	N207	ITIH4		N81, N207, N517, and N577		PUBTATOR	SpecificSite	ITIH4	3700	N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	part_of	ITIH4	665:669	arg1	N517	ITIH4		N81, N207, N517, and N577		PUBTATOR	SpecificSite	ITIH4	3700	N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	part_of	ITIH4	665:669	arg1	N577	ITIH4		N81, N207, N517, and N577		PUBTATOR	SpecificSite	ITIH4	3700	N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	part_of	ITIH4	665:669	arg1	N207	ITIH4		N81, N207, N517, and N577		PUBTATOR	SpecificSite	ITIH4	3700	N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	part_of	ITIH4	665:669	arg1	N577	ITIH4		N81, N207, N517, and N577		PUBTATOR	SpecificSite	ITIH4	3700	N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	part_of	ITIH4	665:669	arg1	N207	ITIH4		N81, N207, N517, and N577		PUBTATOR	SpecificSite	ITIH4	3700	N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	part_of	ITIH4	665:669	arg1	N207	ITIH4		N81, N207, N517, and N577		PUBTATOR	SpecificSite	ITIH4	3700	N81, N207, N517, and N577	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
2813359	0	69	gly	erythropoietin	88:101	arg1	sugar chain structure	erythropoietin			sugar chain structure	PUBTATOR		erythropoietin	2056		Relationship between sugar chain structure and biological activity of recombinant human erythropoietin produced in Chinese hamster ovary cells.
10200178	8	5	gly	-fucosylation	1505:1517	arg1	terminal HexNAc residues				terminal HexNAc residues						Some sixty structures have been found characterized by neutral and sialylated bi-, tri-, and tetraantennary complex-type bearing outer-arm alpha(1-3)-fucosylation (the Lewisx and sialyl-Lewisx epitopes), core alpha(1,6) fucosylation, and the presence of terminal HexNAc residues.
10200178	8	22	gly	fucosylation	1576:1587	arg1	terminal HexNAc residues				terminal HexNAc residues						Some sixty structures have been found characterized by neutral and sialylated bi-, tri-, and tetraantennary complex-type bearing outer-arm alpha(1-3)-fucosylation (the Lewisx and sialyl-Lewisx epitopes), core alpha(1,6) fucosylation, and the presence of terminal HexNAc residues.
10200178	8	94	gly	sialylated	1423:1432	arg1	neutral and sialylated bi-				neutral and sialylated bi-						Some sixty structures have been found characterized by neutral and sialylated bi-, tri-, and tetraantennary complex-type bearing outer-arm alpha(1-3)-fucosylation (the Lewisx and sialyl-Lewisx epitopes), core alpha(1,6) fucosylation, and the presence of terminal HexNAc residues.
7613477	8	16	gly	sialylated	1678:1687	arg1	sialylated triantennary oligosaccharides				sialylated triantennary oligosaccharides						These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	8	35	gly	fucosylated	1722:1732	arg1	fucosylated sialylated biantennary oligosaccharides				fucosylated sialylated biantennary oligosaccharides						These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	8	73	gly	glycopeptides	1640:1652	arg2	These glycopeptides			These glycopeptides						glycopeptides	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	8	89	gly	sialylated	1734:1743	arg1	fucosylated sialylated biantennary oligosaccharides				fucosylated sialylated biantennary oligosaccharides						These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	8	53	gly	bear	1673:1676	arg1	These glycopeptides AND fucosylated sialylated biantennary oligosaccharides			These glycopeptides	fucosylated sialylated biantennary oligosaccharides					glycopeptides	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	8	53	gly	bear	1673:1676	arg1	These glycopeptides AND sialylated triantennary oligosaccharides			These glycopeptides	sialylated triantennary oligosaccharides					glycopeptides	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
9689040	7	16	part_of	fibrinogen	921:930	arg1	gamma-chain carboxyl domains	fibrinogen		gamma-chain carboxyl domains		PUBTATOR	Site	fibrinogen	2244	domains	Comparison with structures of the beta- and gamma-chain carboxyl domains of human fibrinogen revealed that the binding cleft is essentially neutral and should not bind Gly-Pro-Arg or Gly-His-Arg peptides of the sort bound by those other domains.
26013384	0	10	part_of	Ser126	59:64	arg1	Human Recombinant Erythropoietin	Erythropoietin		Ser126		PUBTATOR	AminoAcid	Erythropoietin	2056	Ser126	Structural Identification of a Non-Glycosylated Variant at Ser126 for O-Glycosylation Site from EPO BRP, Human Recombinant Erythropoietin by LC/MS Analysis.
29932112	6	13	part_of	Panx2	886:890	arg1	the only N-glycosylation site	Panx2		the only N-glycosylation site		PUBTATOR	Site	Panx2	56666	site	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	6	13	part_of	Panx2	886:890	arg1	N86	Panx2		N86		PUBTATOR	SpecificSite	Panx2	56666	N86	Our results showed that N86 is the only N-glycosylation site of Panx2.
20959806	5	6	gly	Snail1	847:852	arg1	O-GlcNAc modification	Snail1			O-GlcNAc modification	PUBTATOR		Snail1	6615		Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	5	14	gly	EMT	937:939	arg1	cellular glucose metabolism	EMT			cellular glucose metabolism	OGER		EMT	Q08881		Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	5	15	gly	modification	831:842	arg3	Snail1 AND O-GlcNAc modification	Snail1			O-GlcNAc modification	PUBTATOR		Snail1	6615		Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
18508581	6	17	gly	glycosylation	804:816	arg2	asparagine198			asparagine198						asparagine198	We show that glycosylation at asparagine198 is crucial for protein stability.
11502179	10	60	part_of	receptor	1530:1537	arg1	the soluble ectodomain	TSH receptor		the soluble ectodomain		PUBTATOR	Site	TSH receptor	7253	ectodomain	Contrary to all currently available assays, the soluble ectodomain of the TSH receptor purified in a functionally competent conformation allows direct studies of its interactions with TSH and autoantibodies and opens the way to structural studies.
11390601	2	103	gly	glycosylation	412:424	arg2	specific glycosylation sites			specific glycosylation sites						sites	In this study, specific glycosylation sites on gp120 of a dualtropic primary HIV-1 isolate, DH12, were eliminated by site-directed mutagenesis and the properties of the resulting mutant envelopes were evaluated using a recombinant vaccinia virus-based cell-to-cell fusion assay alone or in the context of viral infections.
1421757	2	12	gly	glycopeptide	307:318	arg2	a glycopeptide			a glycopeptide						glycopeptide	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
14764083	10	2	gly	glycosylation	1332:1344	arg2	Asn281			Asn281						Asn281	Hence, glycosylation at Asn281 protects bLF against cleavage by trypsin at Lys282.
2498325	7	68	part_of	Apolipoprotein	945:958	arg1	Thr194----Ala	Apolipoprotein E		Thr194----Ala		PUBTATOR	AminoAcid	Apolipoprotein E	348	Thr194	Apolipoprotein E(Thr194----Ala) was secreted exclusively as the asialo isoform, confirming that Thr194 is the site of carbohydrate attachment in these cells and indicating that glycosylation of apoE is not essential for secretion.
9677334	12	42	gly	O-glycosylation	1606:1620	arg2	the O-glycosylation site			the O-glycosylation site						site	We also demonstrate that the O-glycosylation site located at position 110 of TPO is not necessary for the bioactivity of the cytokine.
24816101	4	9	gly	glycosylated	639:650	arg1	glycosylated SGSH	glycosylated SGSH				OGER		SGSH	P51688		Here, the crystal structure of glycosylated SGSH is presented at 2 Å resolution.
21402931	8	37	gly	Nonpolymerizing	1285:1299	arg1	betaglycan	Nonpolymerizing ZP			betaglycan	Cterm		Nonpolymerizing ZP			Nonpolymerizing ZP proteins such as betaglycan and endoglin do not contain this cleavage site.
21402931	8	52	gly	ZP	1301:1302	arg1	betaglycan	Nonpolymerizing ZP			betaglycan	Cterm		Nonpolymerizing ZP			Nonpolymerizing ZP proteins such as betaglycan and endoglin do not contain this cleavage site.
3264725	0	87	part_of	VIIa	72:75	arg1	Amino acid sequence	factor VIIa		Amino acid sequence		Cterm	Site	factor VIIa		sequence	Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells.
21980294	6	28	part_of	residues	914:921	arg1	the unliganded gD	gD		residues		Cterm	AminoAcid	gD	2532	residues in	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
20739279	9	15	gly	glycosylation	1134:1146	arg1	60			Asn(60)						Asn(60)	Although glycosylation of SynCAM 2 at Asn(60) reduces adhesion, N-glycans at Asn(70)/Asn(104) of SynCAM 1 increase its interactions.
20739279	9	15	gly	glycosylation	1134:1146	arg1	SynCAM 2	SynCAM 2		Asn(60)		PUBTATOR		SynCAM 2	253559	Asn(60)	Although glycosylation of SynCAM 2 at Asn(60) reduces adhesion, N-glycans at Asn(70)/Asn(104) of SynCAM 1 increase its interactions.
20739279	9	15	gly	glycosylation	1134:1146	arg1	Asn			Asn(60)						Asn(60)	Although glycosylation of SynCAM 2 at Asn(60) reduces adhesion, N-glycans at Asn(70)/Asn(104) of SynCAM 1 increase its interactions.
20739279	9	15	gly	glycosylation	1134:1146	arg2	Asn			Asn(60)						Asn(60)	Although glycosylation of SynCAM 2 at Asn(60) reduces adhesion, N-glycans at Asn(70)/Asn(104) of SynCAM 1 increase its interactions.
20739279	9	15	gly	glycosylation	1134:1146	arg1	SynCAM 2	SynCAM 2		Asn(60)		PUBTATOR		SynCAM 2	253559	Asn(60)	Although glycosylation of SynCAM 2 at Asn(60) reduces adhesion, N-glycans at Asn(70)/Asn(104) of SynCAM 1 increase its interactions.
20739279	9	15	gly	glycosylation	1134:1146	arg1	Asn			Asn(60)						Asn(60)	Although glycosylation of SynCAM 2 at Asn(60) reduces adhesion, N-glycans at Asn(70)/Asn(104) of SynCAM 1 increase its interactions.
20739279	9	15	gly	glycosylation	1134:1146	arg2	Asn			Asn(60)						Asn(60)	Although glycosylation of SynCAM 2 at Asn(60) reduces adhesion, N-glycans at Asn(70)/Asn(104) of SynCAM 1 increase its interactions.
20739279	9	15	gly	glycosylation	1134:1146	arg1	Asn	SynCAM 2		Asn(60)		PUBTATOR		SynCAM 2	253559	Asn(60)	Although glycosylation of SynCAM 2 at Asn(60) reduces adhesion, N-glycans at Asn(70)/Asn(104) of SynCAM 1 increase its interactions.
20739279	9	15	gly	glycosylation	1134:1146	arg2	Asn	SynCAM 2		Asn(60)		PUBTATOR		SynCAM 2	253559	Asn(60)	Although glycosylation of SynCAM 2 at Asn(60) reduces adhesion, N-glycans at Asn(70)/Asn(104) of SynCAM 1 increase its interactions.
20739279	9	15	gly	glycosylation	1134:1146	arg2	Asn			Asn(60)						Asn(60)	Although glycosylation of SynCAM 2 at Asn(60) reduces adhesion, N-glycans at Asn(70)/Asn(104) of SynCAM 1 increase its interactions.
11595658	5	21	gly	glycosylation	686:698	arg2	each glycosylation site			each glycosylation site						site	Two sets of mutations were performed for each glycosylation site: N to Q and S/T to A, respectively.
18642129	1	6	gly	glycoprotein	141:152	arg1	Factor VII	Factor VII				OGER		Factor VII	P08709		Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	1	6	gly	glycoprotein	141:152	arg1	a vitamin K-dependent glycoprotein	a vitamin K-dependent glycoprotein				Fterm		glycoprotein			Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
10861210	2	70	gly	contained	502:510	arg1	Human AE1 AND a high-mannose oligosaccharide	Human AE1			a high-mannose oligosaccharide	PUBTATOR		Human AE1	6521		Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained a high-mannose oligosaccharide.
19139490	2	42	gly	glycoproteins	338:350	arg1	CF glycoproteins	CF glycoproteins				Fterm		glycoproteins			Global profiling and quantitative characterization of CF glycoproteins may reveal potent biomarkers for clinical applications.
24530628	0	54	gly	glycopeptide	10:21	arg2	Selective glycopeptide			Selective glycopeptide						glycopeptide	Selective glycopeptide profiling by acetone enrichment and LC/MS.
1710976	12	12	part_of	Peptide	1287:1293	arg1	Peptide Asn-Gly-Ser	Peptide		Peptide Asn-Gly-Ser		OGER	Site	Peptide		Asn-Gly-Ser	Peptide Asn-Gly-Ser (residues 427-429) is the most probable candidate for glycosylation; literature data suggests that deamidation occurs in the stretch Glu-Asn-Gly-Lys-Asp (residues 364-368) and Asn-Gly-Asn-Cys (residues 474-477).
1710976	12	12	part_of	Peptide	1287:1293	arg1	residues 427-429	Peptide		residues 427-429		OGER	SpecificSite	Peptide		residues 427-429	Peptide Asn-Gly-Ser (residues 427-429) is the most probable candidate for glycosylation; literature data suggests that deamidation occurs in the stretch Glu-Asn-Gly-Lys-Asp (residues 364-368) and Asn-Gly-Asn-Cys (residues 474-477).
3555489	1	28	part_of	enkephalinase	266:278	arg1	the complete 742 amino acid sequence	enkephalinase		the complete 742 amino acid sequence		PUBTATOR	Site	enkephalinase	24590	sequence	cDNA clones encoding rat enkephalinase (neutral endopeptidase, EC 3.4.24.11) have been isolated in lambda gt10 libraries from both brain and kidney mRNAs and the complete 742 amino acid sequence of rat enkephalinase is presented.
19855092	0	33	gly	adiponectin	28:38	arg1	Sialic acid modification	adiponectin			Sialic acid modification	PUBTATOR		adiponectin	11450		Sialic acid modification of adiponectin is not required for multimerization or secretion but determines half-life in circulation.
19855092	0	96	gly	modification	12:23	arg1	adiponectin AND Sialic acid modification	adiponectin			Sialic acid modification	PUBTATOR		adiponectin	11450		Sialic acid modification of adiponectin is not required for multimerization or secretion but determines half-life in circulation.
8757293	8	51	gly	attached	1426:1433	arg1	Asn 159 AND a disaccharide unit			Asn 159	a disaccharide unit					Asn 159	The PR3 structure includes a disaccharide unit (N-linked 2-acetamido-2-deoxy-beta-D-glucopyranose and 1,6-linked alpha-L-fucopyranose) covalently attached to Asn 159.
26563299	3	32	gly	glycosylation	531:543	arg1	hetIL-15	hetIL-15				PUBTATOR		IL-15	3600		Favorable pharmacokinetic properties are associated with the heterodimeric formation and the glycosylation of hetIL-15, which, however, remains largely uncharacterized.
3542989	2	7	gly	attached	306:313	arg2	9 asparagines AND nine carbohydrate chains			9 asparagines	nine carbohydrate chains					asparagines	The protein contains 574 amino acids per subunit and nine carbohydrate chains attached to 9 asparagines.
3542989	2	18	gly	contains	240:247	arg1	The protein AND nine carbohydrate chains	The protein			nine carbohydrate chains	Fterm		protein			The protein contains 574 amino acids per subunit and nine carbohydrate chains attached to 9 asparagines.
9597769	2	28	gly	O-glycosylation	282:296	arg2	O-glycosylation sites			O-glycosylation sites						sites	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	70	gly	glycosylated	527:538	arg1	an overlapping sequence			an overlapping sequence						sequence	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
7776966	11	23	gly	nonglycosylated	1737:1751	arg1	nonglycosylated mutant receptors	nonglycosylated mutant receptors				Fterm		receptors			However, FSH binding activity is not observed with nonglycosylated mutant receptors where both sites have been collectively disrupted.
17576745	6	62	part_of	GPS	1165:1167	arg1	the GPS domain	GPS		the GPS domain		OGER	Site	GPS		domain	In contrast to the wild-type protein, disease-associated GPR56 missense mutations in the tip of the N-terminal domain (R38Q, R38W, Y88C and C91S) produce proteins with reduced intracellular trafficking and poor cell surface expression, whereas the two mutations in the GPS domain (C346S and W349S) produce proteins with dramatically impaired cleavage that fail to traffic beyond the endoplasmic reticulum.
17576745	6	71	part_of	N-terminal	996:1005	arg1	the N-terminal domain	N-terminal		the N-terminal domain		Cterm	Site	N-terminal		domain	In contrast to the wild-type protein, disease-associated GPR56 missense mutations in the tip of the N-terminal domain (R38Q, R38W, Y88C and C91S) produce proteins with reduced intracellular trafficking and poor cell surface expression, whereas the two mutations in the GPS domain (C346S and W349S) produce proteins with dramatically impaired cleavage that fail to traffic beyond the endoplasmic reticulum.
8939990	3	23	part_of	mac25	403:407	arg1	the human mac25 propeptide	mac25		the human mac25 propeptide		PUBTATOR	Site	mac25	3490	propeptide	The deduced amino acid sequence of the human mac25 propeptide shares a 20-25% identity to human insulin-like growth factor-binding proteins (IGFBPs), suggesting that mac25 could be another member of the IGFBP family.
23602662	1	30	gly	glycoprotein	139:150	arg1	a widely distributed membrane glycoprotein	a widely distributed membrane glycoprotein				Fterm		glycoprotein			CD200 is a widely distributed membrane glycoprotein that regulates myeloid cell activity through its interaction with an inhibitory receptor (CD200R).
23602662	1	30	gly	glycoprotein	139:150	arg1	CD200	CD200				PUBTATOR		CD200	4345		CD200 is a widely distributed membrane glycoprotein that regulates myeloid cell activity through its interaction with an inhibitory receptor (CD200R).
2775232	5	61	gly	N-glycosylated	1309:1322	arg1	the five N-glycosylated asparagine residues			the five N-glycosylated asparagine residues						asparagine residues	The N-linked glycosylation points found here in platelet GPIIb are the same as the five N-glycosylated asparagine residues suggested after cDNA sequencing of human erythroleukaemic-cell GPIIb [Poncz, Eisman, Heindenreich, Silver, Vilaire, Surrey, Schwartz & Bennett (1987) J. Biol.
24141704	5	2	part_of	glycosyltransferase	650:668	arg1	the PaTox glycosyltransferase domain	glycosyltransferase		the PaTox glycosyltransferase domain		Fterm	Site	glycosyltransferase		domain	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	5	24	part_of	PaTox	644:648	arg1	the PaTox glycosyltransferase domain	PaTox		the PaTox glycosyltransferase domain		Cterm	Site	PaTox		domain	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
18467335	12	69	part_of	PCI	1565:1567	arg1	the N-terminal region	PCI		the N-terminal region		OGER	Site	PCI	P05154	region	These results thus demonstrate that the N-linked glycans and the N-terminal region of blood-derived PCI in different ways affect the cofactor-enhanced rates of thrombin inhibition and provide information on the mechanisms by which this may be achieved.
8798614	5	60	gly	glycosylation	972:984	arg2	the site			the site						site	In this study, we specifically examined how deletion or transposition of the site of N-linked glycosylation in the CD59 polypeptide affects its MAC inhibitory function.
8798614	5	60	gly	glycosylation	972:984	arg1	the CD59 polypeptide			the CD59 polypeptide						polypeptide	In this study, we specifically examined how deletion or transposition of the site of N-linked glycosylation in the CD59 polypeptide affects its MAC inhibitory function.
24977290	6	78	gly	glycosylation	964:976	arg2	the 10 predicted N-linked glycosylation sites			the 10 predicted N-linked glycosylation sites						sites	Nine of the 10 predicted N-linked glycosylation sites were identified in or near the metalloproteinase,spacer, thrombospondin type 1 repeat (TSR1) and the CUB domain of plasma ADAMTS13.
12435857	6	35	gly	glycosylated	1209:1220	arg1	its fully glycosylated wild-type mature protein	its fully glycosylated wild-type mature protein				Fterm		protein			In contrast to its fully glycosylated wild-type mature protein, the mutant THTR-1 protein underwent only the initial stage of N-linked glycosylation.
27313224	5	62	gly	N-glycosylation	939:953	arg1	SV2C	SV2C				PUBTATOR		SV2C	22987		Here, we expressed human SV2C-LD4 fused to human IgG-Fc in prokaryotic and eukaryotic expression systems to analyse the effect of N-glycosylation of SV2C on the interaction with BoNT/A1.
8349699	6	100	part_of	synthase-1	883:892	arg1	the three glycosylation sites	PGH synthase-1		the three glycosylation sites		PUBTATOR	Site	PGH synthase-1	19224	sites	N-Glycosylation consensus sequences corresponding to the three glycosylation sites of ovine PGH synthase-1 are conserved in the deduced amino acid sequences of PGH synthases-2.
18780401	3	55	gly	glycoproteins	613:625	arg1	N-linked glycoproteins	N-linked glycoproteins				Fterm		glycoproteins			A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
9722584	6	53	gly	N-glycosylation	939:953	arg2	six putative N-glycosylation sites			six putative N-glycosylation sites						sites	CILP has 30 cysteines and six putative N-glycosylation sites.
17040911	7	75	gly	Asn-270	1481:1487	arg1	the glycans			Asn-152 and Asn-270	the glycans					Asn-152 and Asn-270	Site-directed mutagenesis demonstrated that no single glycan was essential for oligomer formation; however, the combined absence of the glycans at Asn-152 and Asn-270 in the protease domain hindered intersubunit disulfide bond formation, prevented noncovalent associations, and abolished enzymatic activity.
17040911	7	80	gly	Asn-152	1469:1475	arg1	the glycans			Asn-152 and Asn-270	the glycans					Asn-152 and Asn-270	Site-directed mutagenesis demonstrated that no single glycan was essential for oligomer formation; however, the combined absence of the glycans at Asn-152 and Asn-270 in the protease domain hindered intersubunit disulfide bond formation, prevented noncovalent associations, and abolished enzymatic activity.
1421757	1	0	gly	glycosylation	177:189	arg2	three N-linked and one O-linked glycosylation sites			three N-linked and one O-linked glycosylation sites						sites	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	1	30	gly	glycoprotein	121:132	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	1	30	gly	glycoprotein	121:132	arg1	The human transferrin receptor	The human transferrin receptor				PUBTATOR		transferrin receptor	7018		The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
7014218	6	20	gly	attached	748:755	arg1	the peptide AND the oligosaccharide chain			the peptide	the oligosaccharide chain					peptide	the oligosaccharide chain is attached to the peptide by an N-glycosidic bond to asparagine-17.
3497398	10	36	gly	region	1539:1544	arg1	seven repeats			region	seven repeats					region	The determined sequence of the alpha chain of glycoprotein Ib contains a region (residues 29-193) with seven repeats, which is indicative of gene duplication and is highly homologous to human leucine-rich alpha 2-glycoprotein.
3497398	10	38	gly	residues	1547:1554	arg1	29-193			29-193						residues 29-193	The determined sequence of the alpha chain of glycoprotein Ib contains a region (residues 29-193) with seven repeats, which is indicative of gene duplication and is highly homologous to human leucine-rich alpha 2-glycoprotein.
3497398	10	41	gly	glycoprotein	1512:1523	arg1	glycoprotein Ib	glycoprotein Ib				Fterm		glycoprotein			The determined sequence of the alpha chain of glycoprotein Ib contains a region (residues 29-193) with seven repeats, which is indicative of gene duplication and is highly homologous to human leucine-rich alpha 2-glycoprotein.
8567640	3	39	part_of	held	351:354	arg1	previously held suppositions	held		previously held suppositions		OGER	Site	held	O14497	positions	The resultant model diverges significantly from previously held suppositions of structure based primarily on hydropathy analysis.
18787108	9	59	part_of	C1q	1532:1534	arg1	their globular C1q domain	C1q		their globular C1q domain		OGER	Site	C1q		domain	Biochemical analysis demonstrates that adiponectin and CTRP9 associate via their globular C1q domain, and this interaction does not require their conserved N-terminal cysteines or their collagen domains.
2573604	11	1	gly	O-glycosylation	1981:1995	arg1	a microvillar hydrolase	a microvillar hydrolase				Fterm		hydrolase			These data represent the first direct evidence for O-glycosylation of a microvillar hydrolase at a site immediately adjacent to the membrane anchor and indicates that even small clusters of Thr and Ser can be O-glycosylated.
26510530	1	66	gly	glycoproteins	163:175	arg1	the top eight abundant glycoproteins	the top eight abundant glycoproteins				Fterm		glycoproteins			A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
3980466	3	34	gly	glycosylation	592:604	arg2	potential N-linked glycosylation sites			potential N-linked glycosylation sites						sites	This cell line simultaneously synthesizes two classes of major histocompatibility antigens that, within each class, share a high degree of amino acid sequence homology and possess potential N-linked glycosylation sites at invariant positions.
3980466	3	34	gly	glycosylation	592:604	arg2	invariant positions			invariant positions						positions	This cell line simultaneously synthesizes two classes of major histocompatibility antigens that, within each class, share a high degree of amino acid sequence homology and possess potential N-linked glycosylation sites at invariant positions.
6619128	4	68	part_of	IgD	441:443	arg1	the hinge region	IgD		the hinge region		OGER	Site	IgD	P01880	region	In this communication, we present the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH.
11567096	3	36	part_of	rCRFR1	653:658	arg1	the N-terminal domain	rCRFR1		the N-terminal domain		PUBTATOR	Site	rCRFR1	58959	domain	The low production rate of the N-terminal domain of rCRFR1 (rCRFR1-NT) by transfected HEK 293 cells, was increased by a factor of 100 in the presence of kifunensine.
12901863	6	18	gly	glycosylation	1049:1061	arg1	the normal and pathological variants	the normal and pathological variants				Fterm		variants			The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
9295302	5	24	part_of	sequons	799:805	arg1	this protein	protein		sequons		Fterm		protein			To aid in determining the topology most likely to be correct, we have identified which of the 14 N-glycosylation sequons in this protein are utilized.
6833285	0	11	gly	2HS-glycoprotein	54:69	arg1	human plasma alpha 2HS-glycoprotein	human plasma alpha 2HS-glycoprotein				PUBTATOR		alpha 2HS-glycoprotein	197		Characterization of the B-chain of human plasma alpha 2HS-glycoprotein.
18815274	9	9	gly	glycosylated	1250:1261	arg1	SV2A	SV2A				PUBTATOR		SV2A	64051		Together, the data reported here demonstrate that glycosylated SV2A and SV2B act in conjunction with gangliosides to mediate the entry of BoNT/E into neurons.
20406422	0	82	gly	glycoprotein	41:52	arg1	the CLN7 membrane glycoprotein	the CLN7 membrane glycoprotein				Fterm		glycoprotein			Lysosomal targeting of the CLN7 membrane glycoprotein and transport via the plasma membrane require a dileucine motif.
2001369	0	41	gly	CD4	53:55	arg1	Carbohydrate structures	CD4			Carbohydrate structures	PUBTATOR		CD4	920		Carbohydrate structures of recombinant soluble human CD4 expressed in Chinese hamster ovary cells.
4742735	2	8	part_of	immunoglobulin	288:301	arg1	the constant regions	immunoglobulin		the constant regions		Fterm	Site	immunoglobulin		regions	The homology of the constant regions of immunoglobulin micro, gamma, alpha, and epsilon heavy chains reveals evolutionary relationships and suggests that two genes code for each heavy chain.
17711303	2	27	gly	glycosylated	378:389	arg1	the receptor	the receptor				Fterm		receptor			FLAG-hKOR was resolved as a broad and diffuse 55-kDa band and a less diffuse 45-kDa band by immunoblotting, indicating that the receptor is glycosylated.
2059624	6	31	part_of	r-HPg	1628:1632	arg1	N289	r-HPg		N289		Cterm	SpecificSite	r-HPg	P00747	N289	At an intermediate time period window, of 20-60 h, p.i., a mixture of complex-type oligosaccharides, totaling approximately 77% of the glycans, with various levels of branching and outer arm completion, and high-mannose type of oligosaccharides, totaling approximately 23% of the glycans, was assembled on N289 of the r-HPg produced.
2049076	8	22	gly	carries	1210:1216	arg1	natural IFN-alpha 2 AND O-linked carbohydrates	IFN-alpha 2		Thr-106	O-linked carbohydrates	PUBTATOR		IFN-alpha 2	3440	Thr-106	These results suggested that Thr-106 of natural IFN-alpha 2 carries O-linked carbohydrates.
15750791	3	4	gly	glycosylated	422:433	arg1	Edg-1/S1P1	Edg-1/S1P1				PUBTATOR		S1P1	1901		Our recent novel studies established that Edg-1/S1P1 is glycosylated in its N-terminal extracellular portion and further identified the specific glycosylation site as asparagine 30.
15750791	3	18	gly	glycosylation	511:523	arg2	the specific glycosylation site			the specific glycosylation site						site	Our recent novel studies established that Edg-1/S1P1 is glycosylated in its N-terminal extracellular portion and further identified the specific glycosylation site as asparagine 30.
7918467	8	46	gly	N-glycosylation	841:855	arg2	sites			sites						sites	In addition, sites of N-glycosylation were found at Asn45 and Asn78.
10022822	0	51	part_of	Ii	49:50	arg1	MHC class II-associated p41 Ii fragment	p41 Ii		MHC class II-associated p41 Ii fragment		PUBTATOR	Site	p41 Ii	2035	fragment	Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S.
10022822	0	56	part_of	p41	45:47	arg1	MHC class II-associated p41 Ii fragment	p41 Ii		MHC class II-associated p41 Ii fragment		PUBTATOR	Site	p41 Ii	2035	fragment	Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S.
22809326	7	23	part_of	DC-LAMP	957:963	arg1	the conserved domain	DC-LAMP		the conserved domain		PUBTATOR	Site	DC-LAMP	27074	domain	RESULTS: The crystal structure of the conserved domain of human DC-LAMP was solved.
21908432	3	18	part_of	GPIbβ	368:372	arg1	the GPIbβ ectodomain	GPIbβ 		the GPIbβ ectodomain		PUBTATOR	Site	GPIbβ 	2812	ectodomain	We have crystallized the GPIbβ ectodomain (GPIbβ(E)) and determined the structure to show a single leucine-rich repeat with N- and C-terminal disulphide-bonded capping regions.
2141278	3	52	part_of	EGF-like	708:715	arg1	the epidermal growth factor-like (EGF-like) region	EGF		the epidermal growth factor-like (EGF-like) region		OGER	Site	EGF	P01133	region	Fragment alpha 2, which comprised the epidermal growth factor-like (EGF-like) region of C1-s, was heterogeneous, starting at serine 97 or phenylalanine 105 and ending at lysine 195.
2141278	3	60	part_of	factor-like	695:705	arg1	the epidermal growth factor-like (EGF-like) region	factor		the epidermal growth factor-like (EGF-like) region		Fterm	Site	factor		region	Fragment alpha 2, which comprised the epidermal growth factor-like (EGF-like) region of C1-s, was heterogeneous, starting at serine 97 or phenylalanine 105 and ending at lysine 195.
2141278	3	66	part_of	C1-s	728:731	arg1	the epidermal growth factor-like (EGF-like) region	C1-s		the epidermal growth factor-like (EGF-like) region		PUBTATOR	Site	C1-s	716	region	Fragment alpha 2, which comprised the epidermal growth factor-like (EGF-like) region of C1-s, was heterogeneous, starting at serine 97 or phenylalanine 105 and ending at lysine 195.
22171320	13	128	gly	O-glycosylation	2120:2134	arg2	29 O-glycosylation sites			29 O-glycosylation sites						sites	We defined 29 O-glycosylation sites which have, to our knowledge, not been previously reported.
23894062	8	84	gly	N-glycosylation	1170:1184	arg2	a N-glycosylation site			a N-glycosylation site						site	We showed a SOST peptide (SOST-S146, with homology to a bacterial glycotransferase peptide) binds to a NOG peptide (NOG-N54), which contains a N-glycosylation site.
19880749	0	48	part_of	ADAMTS13	50:57	arg1	the noncatalytic domains	ADAMTS13		the noncatalytic domains		PUBTATOR	Site	ADAMTS13	11093	domains	Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple discontinuous exosites for von Willebrand factor.
10413465	6	23	part_of	apoE4	1298:1302	arg1	position 158	apoE4		position 158		PUBTATOR	SpecificSite	apoE4	348	cysteine at position 158	In contrast, introduction of cysteine at position 158 of apoE4 (Arg112, Cys158) increased the SDS-stable binding of apoE to Abeta to the levels similar to those observed in apoE2.
7613477	7	22	part_of	contains	1566:1573	arg1	apolipoprotein D AND potential N-linked glycosylation sites	apolipoprotein D		potential N-linked glycosylation sites		PUBTATOR	Site	apolipoprotein D	347	sites	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	7	22	part_of	contains	1566:1573	arg1	a copurifying protein AND potential N-linked glycosylation sites	a copurifying protein		potential N-linked glycosylation sites		Fterm	Site	protein		sites	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
30237853	10	14	gly	glycopeptides	1729:1741	arg2	intact glycopeptides			intact glycopeptides						glycopeptides	This study has generated a panel of intact glycopeptides that has a potential for PCa detection.
11595658	0	38	gly	N-glycosylation	0:14	arg1	CRF receptor type 1	CRF receptor type 1				PUBTATOR		CRF receptor type 1	1394		N-glycosylation of CRF receptor type 1 is important for its ligand-specific interaction.
7654718	9	52	part_of	BAL	1412:1414	arg1	the C-tail region	BAL		the C-tail region		OGER	Site	BAL	P19835	region	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	9	94	part_of	C-tail	1395:1400	arg1	the C-tail region	C-tail		the C-tail region		Cterm	Site	C-tail		region	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
19571171	0	8	gly	N-glycosylation	11:25	arg1	GlcNAc-6-sulfotransferase 1	GlcNAc-6-sulfotransferase 1				Fterm		GlcNAc-6-sulfotransferase 1			Effects of N-glycosylation on the activity and localization of GlcNAc-6-sulfotransferase 1.
12600216	7	7	gly	N-glycosylation	1153:1167	arg2	N-glycosylation sites			N-glycosylation sites						sites	In this study, we have determined which of the connecting loops are exposed to the extracellular milieu using two different methods: accessibility of substituted cysteine residues and insertion of N-glycosylation sites.
20511397	5	39	gly	detected	1025:1032	arg1	194 AND the most complex glycan			Thr(194)	the most complex glycan					Thr(194)	Our results identify eight different glycoforms with (HexNAc)(2)-Hex(2)-(NeuAc)(2) being the most complex glycan detected on Thr(194) in both cellular and secreted apoE.
2775232	3	5	part_of	residue	750:756	arg1	GPIIb	GPIIb		residue		PUBTATOR	AminoAcid	GPIIb	3674	cysteine residue	It could be established that each cysteine residue in GPIIb, beginning at alpha-Cys-56, is disulphide-bonded to its nearest neighbour in the amino acid sequence.
20837471	2	9	gly	contains	437:444	arg1	the processing site AND two potential GalNAc O-glycosylation sites immediately C-terminal (TT(226))			the processing site	two potential GalNAc O-glycosylation sites immediately C-terminal (TT(226))					site	ANGPTL3 undergoes proprotein convertase processing (RAPR(224)↓TT) for activation, and the processing site contains two potential GalNAc O-glycosylation sites immediately C-terminal (TT(226)).
1388166	1	92	gly	Asn-linked	225:234	arg1	sulfated Asn-linked oligosaccharides			Asn	sulfated Asn-linked oligosaccharides					Asn	Tissue factor pathway inhibitor (TFPI) produced by endothelial cells contains sulfated Asn-linked oligosaccharides.
1388166	1	88	gly	contains	207:214	arg1	TFPI AND sulfated Asn-linked oligosaccharides	TFPI			sulfated Asn-linked oligosaccharides	PUBTATOR		TFPI	7035		Tissue factor pathway inhibitor (TFPI) produced by endothelial cells contains sulfated Asn-linked oligosaccharides.
1388166	1	88	gly	contains	207:214	arg1	Tissue factor pathway inhibitor AND sulfated Asn-linked oligosaccharides	Tissue factor pathway inhibitor			sulfated Asn-linked oligosaccharides	PUBTATOR		Tissue factor pathway inhibitor	7035		Tissue factor pathway inhibitor (TFPI) produced by endothelial cells contains sulfated Asn-linked oligosaccharides.
6619126	1	107	gly	glycoprotein	90:101	arg1	the MM glycoprotein	the MM glycoprotein				Fterm		glycoprotein			A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
1731338	0	30	part_of	CD43	99:102	arg1	the extracellular region	CD43		the extracellular region		PUBTATOR	Site	CD43	6693	region	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
1731338	0	44	part_of	galactoglycoprotein	36:54	arg1	Amino acid sequence	galactoglycoprotein		Amino acid sequence		PUBTATOR	Site	galactoglycoprotein	6693	sequence	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
19017797	4	52	part_of	FMS	853:855	arg1	FMS domains D4 and D5	FMS		FMS domains D4 and D5		OGER	Site	FMS	P07333	domains	Calorimetric data indicate that M-CSF cannot dimerize FMS without receptor-receptor interactions mediated by FMS domains D4 and D5.
1993171	10	9	part_of	IL-4	1236:1239	arg1	the third and fifth cysteines	IL-4		the third and fifth cysteines		PUBTATOR	AminoAcid	IL-4	3565	cysteines	Sequence analysis of the peptides containing the third and fifth cysteines of human IL-4 also demonstrated that only one of the potential N-glycosylation sites is used by C127 mammary tumor cells.
1993171	10	29	part_of	containing	1186:1195	arg1	the peptides AND the third and fifth cysteines	the peptides		the third and fifth cysteines						cysteines	Sequence analysis of the peptides containing the third and fifth cysteines of human IL-4 also demonstrated that only one of the potential N-glycosylation sites is used by C127 mammary tumor cells.
15486088	5	27	part_of	enzyme	988:993	arg1	the active-site face	enzyme		the active-site face		Fterm	Site	enzyme		face	Each of the three potential lectin domain carbohydrate-binding sites (alpha, beta, and gamma) is located on the active-site face of the enzyme, suggesting a mechanism by which the transferase may accommodate multiple conformations of glycosylated acceptor substrates.
23959878	6	7	gly	deglycosylated	924:937	arg1	native and deglycosylated hIDUA	native and deglycosylated hIDUA				PUBTATOR		hIDUA	3425		The kinetics of native and deglycosylated hIDUA suggested that the N-glycan is also involved in catalytic processes.
7092891	0	0	part_of	sequence	11:18	arg1	the hinge region	sequence		the hinge region						region	Amino acid sequence of galactosamine-containing glycopeptides in the hinge region of a human immunoglobulin D.
7092891	0	1	part_of	D	108:108	arg1	the hinge region	a human immunoglobulin D		the hinge region		Cterm	Site	a human immunoglobulin D		region	Amino acid sequence of galactosamine-containing glycopeptides in the hinge region of a human immunoglobulin D.
12718853	4	22	gly	leucine-rich	614:625	arg1	LRR			leucine	LRR					leucine	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	4	22	gly	leucine-rich	614:625	arg1	a leucine-rich repeat			leucine	a leucine-rich repeat					leucine	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
1820200	1	29	part_of	gonadotrophin	268:280	arg1	individual N-glycosylation sites	glycoprotein hormone human chorionic gonadotrophin (hCG)		individual N-glycosylation sites		PUBTATOR	Site	glycoprotein hormone human chorionic gonadotrophin (hCG)	93659	sites	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
3200844	4	86	gly	glycopeptide	566:577	arg2	a glycopeptide			a glycopeptide						glycopeptide	After CNBr fragmentation, a glycopeptide was isolated and microsequenced.
18676855	3	12	part_of	NGEP	665:668	arg1	the extracellular regions	NGEP		the extracellular regions		PUBTATOR	Site	NGEP	Q6IWH7	regions	To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
18676855	3	23	part_of	NGEP	744:747	arg1	the NGEP sequence	NGEP		the NGEP sequence		PUBTATOR	Site	NGEP	Q6IWH7	sequence	To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
26598643	6	36	gly	O-glycopeptide	1110:1123	arg2	Enriched O-glycopeptide fractions			Enriched O-glycopeptide fractions						O-glycopeptide	Enriched O-glycopeptide fractions were subjected to mass spectrometric analysis using reversed-phase liquid chromatography coupled online to an ion trap mass spectrometer operated in positive-ion mode.
1457969	4	51	gly	glycopeptides	674:686	arg2	hTSH alpha glycopeptides			hTSH alpha glycopeptides						glycopeptides	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	4	89	gly	liberated	648:656	arg1	hTSH alpha glycopeptides AND The oligosaccharides	hTSH beta		glycopeptides	The oligosaccharides	PUBTATOR		hTSH beta	7252	glycopeptides	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
17924658	0	75	gly	glycosylation	65:77	arg2	glycosylation sites	gamma-glutamyltranspeptidase		sites		PUBTATOR		gamma-glutamyltranspeptidase	102724197	sites	Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human gamma-glutamyltranspeptidase.
8942648	0	22	part_of	ser1	87:90	arg1	Peptide	Peptide		ser1		OGER	AminoAcid	Peptide		ser1	Peptide, disulfide, and glycosylation mapping of recombinant human thrombopoietin from ser1 to Arg246.
8942648	0	25	part_of	thrombopoietin	67:80	arg1	Peptide	thrombopoietin		Peptide		PUBTATOR		thrombopoietin	7066		Peptide, disulfide, and glycosylation mapping of recombinant human thrombopoietin from ser1 to Arg246.
15616124	9	22	gly	glycosylation	1397:1409	arg2	N332			N332						N332	We propose that the cotranslational conformation(s) of FVII are unfavorable for glycosylation at N332, whereas a more favorable conformation is obtained during the posttranslational folding.
3980466	6	32	part_of	contain	1145:1151	arg1	H-2Kk AND two and three sites	H-2Kk		two and three sites		PUBTATOR	Site	H-2Kk	14972	sites	The heavy chain of the class I antigens, H-2Kk and H-2Dk contain two and three sites, respectively, in which biantennary structures predominate.
2511201	1	45	part_of	residue	300:306	arg1	bovine blood coagulation factors	factors		residue		Fterm	AminoAcid	factors		serine residue	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	92	part_of	factors	386:392	arg1	the first epidermal growth factor-like domains	factors		the first epidermal growth factor-like domains		Fterm	Site	factors		domains	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
7574684	1	22	part_of	trkB	173:176	arg1	An extracellular domain	trkB		An extracellular domain		PUBTATOR	Site	trkB	4915	domain	An extracellular domain of a human neurotrophin receptor trkB was expressed in Chinese hamster ovary cells and isolated as a glycoprotein possessing binding activity for brain-derived neurotrophic factor.
18514042	0	45	gly	glycosylation	13:25	arg1	human serum glycoproteins	human serum glycoproteins				Fterm		glycoproteins			Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
18514042	0	64	gly	glycoproteins	51:63	arg1	human serum glycoproteins	human serum glycoproteins				Fterm		glycoproteins			Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
26792860	7	40	part_of	possesses	950:958	arg1	SMPDL3A AND a unique C-terminal domain	SMPDL3A		a unique C-terminal domain		PUBTATOR	Site	Additionally, SMPDL3A	57319	domain	Additionally, SMPDL3A possesses a unique C-terminal domain formed from a cluster of four α-helices that appears to distinguish this protein family from other phosphoesterases.
2642896	7	41	gly	residues	872:879	arg1	-Asn-Ser-Ser-			-Asn-Ser-Ser-						-Asn-Ser-Ser-	The recognition sequence for N-glycosylation was seen at two positions of amino acid residues 51-53 (-Asn-Ser-Ser-) and 78-80 (-Asn-Leu-Thr-) counted from the first Met.
2642896	7	41	gly	residues	872:879	arg1	51-53			51-53						residues 51-53	The recognition sequence for N-glycosylation was seen at two positions of amino acid residues 51-53 (-Asn-Ser-Ser-) and 78-80 (-Asn-Leu-Thr-) counted from the first Met.
2642896	7	41	gly	residues	872:879	arg1	-Asn-Leu-Thr-			-Asn-Leu-Thr-						-Asn-Leu-Thr-	The recognition sequence for N-glycosylation was seen at two positions of amino acid residues 51-53 (-Asn-Ser-Ser-) and 78-80 (-Asn-Leu-Thr-) counted from the first Met.
19122660	2	12	part_of	factor-beta	409:419	arg1	the prodomain	factor-beta		the prodomain		Fterm	Site	factor-beta		prodomain	Binding competition studies suggest that additional binding sites, for example, for the prodomain of nerve growth factor-beta, are present in the tunnel and that competition for binding relates to the restricted space inside the propeller.
7642555	0	52	gly	glycosylated	9:20	arg2	threonine 58	c-Myc		threonine 58		PUBTATOR		c-Myc	4609	threonine 58	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	0	52	gly	glycosylated	9:20	arg2	a known phosphorylation site	c-Myc		site		PUBTATOR		c-Myc	4609	site	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
8486673	10	5	gly	non-glycosylated	1587:1602	arg1	The non-glycosylated rat CRP	The non-glycosylated rat CRP				PUBTATOR		CRP	25419		The non-glycosylated rat CRP, however, was still able to bind to phosphorylcholine-Sepharose and to be secreted by hepatocytes.
8435067	3	50	gly	glycosylation	485:497	arg2	seven potential glycosylation sites			seven potential glycosylation sites						sites	The primary structure of lysosomal alpha-glucosidase, as deduced from the cDNA sequence, indicates that there are seven potential glycosylation sites.
16274239	1	57	part_of	receptor	186:193	arg1	579	epidermal growth factor receptor		N(579)		PUBTATOR	SpecificSite	epidermal growth factor receptor	13649	N(579)	We have investigated functional effects of glycosylation at N(579) of the epidermal growth factor receptor (EGFR).
3345750	0	9	gly	glycoproteins	77:89	arg1	respiratory-mucus glycoproteins	respiratory-mucus glycoproteins				Fterm		glycoproteins			Primary structure of neutral oligosaccharides derived from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis, determined by combination of 500-MHz 1H-NMR spectroscopy and quantitative sugar analysis.
3345750	0	19	gly	derived	46:52	arg2	respiratory-mucus glycoproteins AND neutral oligosaccharides	respiratory-mucus glycoproteins			neutral oligosaccharides	Fterm		glycoproteins			Primary structure of neutral oligosaccharides derived from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis, determined by combination of 500-MHz 1H-NMR spectroscopy and quantitative sugar analysis.
7014218	3	0	gly	glycoprotein	306:317	arg1	the S-carboxamidomethylated or S-aminoethylated glycoprotein	the S-carboxamidomethylated or S-aminoethylated glycoprotein				Fterm		glycoprotein			The peptides obtained by digestion of the S-carboxamidomethylated or S-aminoethylated glycoprotein with trypsin and Staphylococcus aureus protease were sequenced by manual Edman degradation.
8163535	1	63	part_of	sites	251:255	arg1	the core protein	protein		sites		Fterm	Site	protein		sites	Most proteoglycans bear either chondroitin sulfate or heparan sulfate chains linked to serine residues at Ser-Gly attachment sites on the core protein.
23662732	0	34	gly	glycoprotein	101:112	arg1	glycoprotein mixtures	glycoprotein mixtures				Fterm		glycoprotein			Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
16407218	3	86	part_of	has	609:611	arg1	four identical 180-kDa subunits AND eight N-linked glycosylation sites	four identical 180-kDa subunits		eight N-linked glycosylation sites		OGER	Site	subunits	2	sites	We isolated the serum protease inhibitor alpha(2) macroglobulin (alpha2M), a heavily glycosylated thiol ester protein (TEP) composed of four identical 180-kDa subunits, each of which has eight N-linked glycosylation sites.
16263699	0	83	gly	N-glycosylation	15:29	arg2	N-glycosylation sites			N-glycosylation sites						sites	Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.
12944413	8	39	gly	sialylated	1387:1396	arg1	sialylated N-glycans				sialylated N-glycans						A physical interaction between myosin and SERT was apparent; however, defects in sialylated N-glycans impaired association of SERT with myosin as well as the stimulation of the serotonin uptake function in the cGMP-dependent pathway.
8962717	1	25	part_of	receptor	251:258	arg1	The extracellular domain	receptor		The extracellular domain		Fterm	Site	receptor		domain	The extracellular domain (621 N-terminal amino acids) of the p170 epidermal growth factor (EGF) receptor has eleven consensus N-linked glycosylation sites.
8962717	1	16	part_of	has	260:262	arg1	the p170 epidermal growth factor (EGF) receptor AND eleven consensus N-linked glycosylation sites	receptor		sites		Fterm	Site	receptor		sites	The extracellular domain (621 N-terminal amino acids) of the p170 epidermal growth factor (EGF) receptor has eleven consensus N-linked glycosylation sites.
24226769	0	65	gly	glycosylates	28:39	arg1	Notch	Notch				PUBTATOR		Notch	100037842		The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type and laterality.
8962717	0	56	gly	glycosylation	16:28	arg1	the epidermal growth factor receptor	epidermal growth factor receptor		domain		PUBTATOR		epidermal growth factor receptor	P00533	domain	Analysis of the glycosylation patterns of the extracellular domain of the epidermal growth factor receptor expressed in Chinese hamster ovary fibroblasts.
10207176	3	28	gly	C-mannosylated	533:546	arg1	Trp-319beta			Trp-319beta						Trp	Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319beta is (partially) C-mannosylated.
9884403	1	45	gly	glycoprotein	138:149	arg1	human Tamm-Horsfall glycoprotein	human Tamm-Horsfall glycoprotein				OGER		Tamm-Horsfall glycoprotein	P07911		The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	0	gly	N-glycosylation	93:107	arg2	The N-glycosylation sites	Tamm-Horsfall glycoprotein		sites		OGER		Tamm-Horsfall glycoprotein	P07911	sites	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
16601115	5	28	gly	glycosylation	1014:1026	arg1	cystatin F	cystatin F		sites		PUBTATOR		cystatin F	8530	sites	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
10029548	5	65	gly	glycosylation	894:906	arg1	Ser-32			Ser-32						Ser-32	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
15458386	11	4	gly	N-glycosylation	1525:1539	arg1	the putative metal-binding sites			the putative metal-binding sites						sites	Our results indicate that alk-SMase activity is severely affected by defective N-glycosylation and structural alterations of the putative metal-binding sites and the predicted active core.
2226797	1	7	gly	N-glycosylation	242:256	arg2	a single N-glycosylation site			a single N-glycosylation site						site	The carbohydrate structures of a genetically engineered human tissue plasminogen activator variant bearing a single N-glycosylation site at Asn 448 are reported.
2226797	1	24	gly	variant	217:223	arg1	The carbohydrate structures	tissue plasminogen activator variant			The carbohydrate structures	PUBTATOR		tissue plasminogen activator variant	P00750		The carbohydrate structures of a genetically engineered human tissue plasminogen activator variant bearing a single N-glycosylation site at Asn 448 are reported.
27780639	5	30	part_of	ATX	870:872	arg1	the active site	ATX		the active site		PUBTATOR	Site	ATX	5168	site	X-ray crystallography has revealed that these compounds have an unexpected binding mode in that they do not interact with the active site zinc ions but instead occupy the hydrophobic LPC pocket extending from the active site of ATX together with occupying the LPA 'exit' channel.
479158	6	67	gly	asparagine288-based	406:424	arg1	an asparagine288-based branched carbohydrate structure			asparagine288	an asparagine288-based branched carbohydrate structure					asparagine288	Plasminogen variant 1 contains an asparagine288-based branched carbohydrate structure, which has been established in the immediately preceding manuscript.
479158	6	23	gly	contains	394:401	arg1	Plasminogen variant 1 AND an asparagine288-based branched carbohydrate structure	Plasminogen variant 1			an asparagine288-based branched carbohydrate structure	OGER		Plasminogen variant 1	P00747		Plasminogen variant 1 contains an asparagine288-based branched carbohydrate structure, which has been established in the immediately preceding manuscript.
2498325	6	63	gly	glycosylation	872:884	arg2	glycosylation sites			glycosylation sites						sites	Site-specific mutants of apoE, designed to eliminate or alter glycosylation sites, were expressed in HeLa cells by acute transfection.
447737	5	2	gly	released	903:910	arg2	the glycopeptide AND Sugars			the glycopeptide	Sugars					glycopeptide	Sugars released from the glycopeptide by various glycosidases were also quantitated.
447737	5	15	gly	glycopeptide	921:932	arg2	the glycopeptide			the glycopeptide						glycopeptide	Sugars released from the glycopeptide by various glycosidases were also quantitated.
1421756	1	64	gly	contains	193:200	arg1	TfR AND Ser/Thr-linked (O-linked) oligosaccharides	TfR			Ser/Thr-linked (O-linked) oligosaccharides	PUBTATOR		TfR	7037		We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	1	64	gly	contains	193:200	arg1	the human transferrin receptor AND Ser/Thr-linked (O-linked) oligosaccharides	the human transferrin receptor			Ser/Thr-linked (O-linked) oligosaccharides	PUBTATOR		transferrin receptor	7037		We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
12911312	3	55	gly	glycosylation	447:459	arg2	sites			sites						sites	Mass spectrometry was used to identify sites of glycosylation on the full-length protein.
3514617	8	146	gly	glycopeptide	1021:1032	arg2	CNBr glycopeptide B			CNBr glycopeptide B						glycopeptide	The studies focused on CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81.
19656770	6	70	gly	N-glycosylation	1188:1202	arg2	the N-glycosylation sites			the N-glycosylation sites						sites	The identification of the N-glycosylation sites on the extracellular domain of the proteins allowed for the determination of the orientation of the identified proteins within the plasma membrane.
12775711	0	8	gly	glycoprotein	65:76	arg1	the 39-kDa glycoprotein	the 39-kDa glycoprotein				Fterm		glycoprotein			Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes.
2065054	2	58	part_of	r-HPg	1153:1157	arg1	Asn289	HPg		Asn289		Cterm	AminoAcid	HPg	5340	Asn289	In order to investigate whether a more general capability of lepidopteran insect cells to produce complex oligosaccharide existed, and to identify the chemical nature of the types of oligosaccharides that such insect cells were able to assemble, we have infected Mamestra brassicae (IZD-MBO503) cells for 48 h with a recombinant (r) baculovirus containing the [R561E]human plasminogen (HPg) cDNA and characterized the nature of the glycopeptidase F (GF) released N-linked oligosaccharides contained on Asn289 of the r-HPg expressed by these cells.
20188224	8	28	gly	deglycosylated	1157:1170	arg1	deglycosylated protein	deglycosylated protein				Fterm		protein			In-gel tryptic digestion was further applied to the gel pieces containing deglycosylated protein, for N-glycosylation site determination.
22020283	4	25	part_of	HLA	1090:1092	arg1	an 'innate HLA sensor' domain	HLA		an 'innate HLA sensor' domain		OGER	Site	HLA		domain	First, the D0 domain, a distinguishing feature of the KIR3D family, extended towards β2-microglobulin and abutted a region of the HLA molecule with limited polymorphism, thereby acting as an 'innate HLA sensor' domain.
17525160	5	91	gly	contains	590:597	arg1	the extracellular amino terminus AND O-linked polysaccharides			the extracellular amino terminus	O-linked polysaccharides					terminus	We demonstrate that the extracellular amino terminus of hCTR1 also contains O-linked polysaccharides.
3980466	13	38	gly	glycoproteins	2358:2370	arg1	structurally related glycoproteins	structurally related glycoproteins				Fterm		glycoproteins			These data suggest that subtle changes in peptide structure are reflected in the extent of sialylation and branching of oligosaccharides found at corresponding glycosylation sites of structurally related glycoproteins.
3980466	13	50	gly	sialylation	2245:2255	arg1	oligosaccharides				oligosaccharides						These data suggest that subtle changes in peptide structure are reflected in the extent of sialylation and branching of oligosaccharides found at corresponding glycosylation sites of structurally related glycoproteins.
3980466	13	74	gly	found	2291:2295	arg2	corresponding glycosylation sites AND oligosaccharides	glycoproteins		sites	oligosaccharides	Fterm		glycoproteins		sites	These data suggest that subtle changes in peptide structure are reflected in the extent of sialylation and branching of oligosaccharides found at corresponding glycosylation sites of structurally related glycoproteins.
3980466	13	87	gly	glycosylation	2314:2326	arg2	corresponding glycosylation sites	glycoproteins		sites		Fterm		glycoproteins		sites	These data suggest that subtle changes in peptide structure are reflected in the extent of sialylation and branching of oligosaccharides found at corresponding glycosylation sites of structurally related glycoproteins.
21138434	6	73	gly	identified	1382:1391	arg1	a prerequisite			a prerequisite						prerequisite	The present study has identified utilised N-glycosylation sites of the h5-HT3B subunit and demonstrated that they promote subunit expression in the cell membrane; a prerequisite for 5-HT(3) receptor function.
21138434	6	23	gly	N-glycosylation	1402:1416	arg2	utilised N-glycosylation sites	h5-HT3B subunit		sites		Cterm		h5-HT3B subunit	9177	sites	The present study has identified utilised N-glycosylation sites of the h5-HT3B subunit and demonstrated that they promote subunit expression in the cell membrane; a prerequisite for 5-HT(3) receptor function.
23209641	2	75	part_of	adiponectin	427:437	arg1	the collagenous domain	adiponectin		the collagenous domain		PUBTATOR	Site	adiponectin	Q15848	domain	Here we demonstrate for the first time that LH3 also modifies the lysine residues in the collagenous domain of adiponectin, which has important roles in glucose and lipid metabolism and inflammation.
23209641	2	85	part_of	residues	389:396	arg1	adiponectin	adiponectin		residues		PUBTATOR	AminoAcid	adiponectin	Q15848	lysine residues	Here we demonstrate for the first time that LH3 also modifies the lysine residues in the collagenous domain of adiponectin, which has important roles in glucose and lipid metabolism and inflammation.
14658030	8	35	gly	glycosylated	1712:1723	arg1	all six consensus sequences			all six consensus sequences						sequences	By using these procedures all six consensus sequences were shown to be glycosylated; the observation of an unmodified peptide with the consensus sequence N-1 indicates only partial glycosylation at this site.
14658030	8	54	gly	glycosylation	1822:1834	arg1	this site			this site						site	By using these procedures all six consensus sequences were shown to be glycosylated; the observation of an unmodified peptide with the consensus sequence N-1 indicates only partial glycosylation at this site.
19836338	2	70	part_of	EphA4	332:336	arg1	the EphA4 ligand binding domain	structure of the EphA4		the EphA4 ligand binding domain		PUBTATOR	Site	structure of the EphA4	2043	domain	We have solved the crystal structure of the EphA4 ligand binding domain alone and in complex with (1) ephrinB2 and (2) ephrinA2.
17896794	0	33	gly	modification	48:59	arg3	the tyrosine 3-monooxygenase AND O-GlcNAc modification			the tyrosine 3-monooxygenase	O-GlcNAc modification					tyrosine 3	N-propanoylmannosamine interferes with O-GlcNAc modification of the tyrosine 3-monooxygenase and stimulates dopamine secretion.
17896794	0	61	gly	3-monooxygenase	77:91	arg1	O-GlcNAc modification			tyrosine 3	O-GlcNAc modification					tyrosine 3	N-propanoylmannosamine interferes with O-GlcNAc modification of the tyrosine 3-monooxygenase and stimulates dopamine secretion.
19855092	8	64	gly	desialylated	1300:1311	arg1	desialylated adiponectin	desialylated adiponectin				PUBTATOR		adiponectin	11450		In contrast, plasma clearance of desialylated adiponectin was accelerated compared with that of control adiponectin, implicating a role for this modification in determining the half-life of circulating adiponectin.
10889209	6	0	gly	glycosylated	1021:1032	arg2	Asn			Asn(132)						Asn(132)	This finding may partly account for the reason that GIRK4 is not glycosylated at Asn(132), either as a homomer or when coexpressed with GIRK1.
10889209	6	0	gly	glycosylated	1021:1032	arg1	GIRK4	GIRK4		Asn(132)		PUBTATOR		GIRK4	3762	Asn(132)	This finding may partly account for the reason that GIRK4 is not glycosylated at Asn(132), either as a homomer or when coexpressed with GIRK1.
10889209	6	0	gly	glycosylated	1021:1032	arg1	GIRK4	GIRK4		Asn(132)		PUBTATOR		GIRK4	3762	Asn(132)	This finding may partly account for the reason that GIRK4 is not glycosylated at Asn(132), either as a homomer or when coexpressed with GIRK1.
17703189	0	51	gly	glycoprotein	8:19	arg1	The CNS glycoprotein Shadoo	The CNS glycoprotein Shadoo				Fterm		glycoprotein			The CNS glycoprotein Shadoo has PrP(C)-like protective properties and displays reduced levels in prion infections.
7538124	0	75	gly	glycosylation	46:58	arg1	human keratin 18	keratin 18		sites		PUBTATOR		keratin 18	3875	sites	Identification and mutational analysis of the glycosylation sites of human keratin 18.
15657036	10	44	part_of	sequence	1159:1166	arg1	The first two cysteine residues	sequence		The first two cysteine residues						cysteine residues	The first two cysteine residues are located in the sequence preceding the N-terminal protease-resistant domain.
16169851	5	13	part_of	HVEM	588:591	arg1	the N-terminal cysteine-rich domain	HVEM		the N-terminal cysteine-rich domain		PUBTATOR	Site	HVEM	8764	domain	This structure shows that BTLA binds the N-terminal cysteine-rich domain of HVEM and employs a unique binding surface compared with other CD28-like receptors.
23234360	2	70	gly	glycopeptide	475:486	arg2	glycopeptide			glycopeptide						glycopeptide	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	2	73	gly	O-glycopeptides	344:358	arg2	O-glycopeptides			O-glycopeptides						O-glycopeptides	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	2	81	gly	glycoproteins	391:403	arg1	tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins	tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins				Fterm		glycoproteins			We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
17330941	0	20	gly	glycopeptides	81:93	arg2	cysteine-containing tryptic glycopeptides			cysteine-containing tryptic glycopeptides						glycopeptides	Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides.
2001369	3	53	gly	Asn-linked	623:632	arg1	the Asn-linked oligosaccharides			Asn	the Asn-linked oligosaccharides					Asn	In the present study, the structures of the Asn-linked oligosaccharides of soluble rCD4 have been elucidated.
2001369	3	58	gly	rCD4	662:665	arg1	the Asn-linked oligosaccharides	rCD4			the Asn-linked oligosaccharides	PUBTATOR		rCD4	24932		In the present study, the structures of the Asn-linked oligosaccharides of soluble rCD4 have been elucidated.
7106126	5	13	part_of	sialoglycoproteins	910:927	arg1	a certain region	sialoglycoproteins		a certain region		Fterm	Site	sialoglycoproteins		region	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
11258925	9	63	gly	glycosylated	1451:1462	arg1	the Asn 396 site			the Asn 396 site						Asn 396 site	It was not possible to conclusively determine whether the Asn 396 site was glycosylated via an MS/MS experiment, so the tryptic digest was deglycosylated to confirm the presence of the glycopeptides.
11258925	9	79	gly	glycopeptides	1561:1573	arg2	the glycopeptides			the glycopeptides						glycopeptides	It was not possible to conclusively determine whether the Asn 396 site was glycosylated via an MS/MS experiment, so the tryptic digest was deglycosylated to confirm the presence of the glycopeptides.
15677325	1	54	part_of	GluR6	212:216	arg1	the glycosylated ligand-binding (S1S2) domain	subunit GluR6		the glycosylated ligand-binding (S1S2) domain		OGER	Site	subunit GluR6	2898	domain	We report the crystal structure of the glycosylated ligand-binding (S1S2) domain of the kainate receptor subunit GluR6, in complex with the agonist domoate.
17005555	4	54	gly	leucine-rich	778:789	arg1	leucine-rich repeat			leucine	leucine-rich repeat					leucine	Here we report on the crystal structure of the ligand-binding ectodomain of human Lingo-1 and show it has a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules.
20881961	5	22	part_of	Sema6A	903:908	arg1	the Sema6A ectodomain	Sema6A		the Sema6A ectodomain		PUBTATOR	Site	Sema6A	57556	ectodomain	Before binding, the Sema6A ectodomain was in the expected 'face-to-face' homodimer arrangement, similar to that adopted by Sema3A and Sema4D, whereas PlxnA2 was in an unexpected 'head-on' homodimer arrangement.
10419520	1	11	part_of	proteins	261:268	arg1	the NH(2)-terminal domains	proteins		the NH(2)-terminal domains		Fterm	Site	proteins		domains	In sterol-depleted mammalian cells, a two-step proteolytic process releases the NH(2)-terminal domains of sterol regulatory element-binding proteins (SREBPs) from membranes of the endoplasmic reticulum (ER).
16335952	2	77	gly	glycoprotein	569:580	arg1	glycoprotein capture	glycoprotein capture				Fterm		glycoprotein			Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	2	87	gly	N-glycoproteins	499:513	arg1	human plasma N-glycoproteins	human plasma N-glycoproteins				Fterm		N-glycoproteins			Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
3840370	5	41	part_of	protein	832:838	arg1	the sequence	protein		the sequence		Fterm	Site	protein		sequence	The plasmid clones isolated allowed the unambiguous determination of 1717 nucleotides of cDNA sequence between the codon for the 32nd amino acid in the sequence of C4b-binding protein and the 164th nucleotide in the 3' non-translated region.
8615697	10	42	part_of	containing	1757:1766	arg1	peptides AND the same amino acid sequence	peptides		the same amino acid sequence						sequence	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
12718853	0	23	part_of	Nogo	17:20	arg1	the Nogo receptor ectodomain	structure of the Nogo receptor		the Nogo receptor ectodomain		PUBTATOR	Site	structure of the Nogo receptor	65078	ectodomain	Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition.
12718853	0	36	part_of	receptor	22:29	arg1	the Nogo receptor ectodomain	structure of the Nogo receptor		the Nogo receptor ectodomain		PUBTATOR	Site	structure of the Nogo receptor	65078	ectodomain	Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition.
1457969	1	76	gly	asparagine-linked	100:116	arg1	The asparagine-linked carbohydrate structures			asparagine	The asparagine-linked carbohydrate structures					asparagine	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	1	9	gly	glycosylation	163:175	arg1	human thyrotrophin	thyrotrophin		sites		Fterm		thyrotrophin		sites	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
23756652	2	41	gly	leucine-rich	247:258	arg1	leucine-rich repeat-containing G-protein-coupled receptor 4 (LGR4)			leucine	leucine-rich repeat-containing G-protein-coupled receptor 4 (LGR4)					leucine	Recently, leucine-rich repeat-containing G-protein-coupled receptor 4 (LGR4), LGR5, and LGR6 have been identified as receptors for RSPOs.
25327667	8	36	gly	glycopeptides	1043:1055	arg2	Three sulfated/phosphorylated glycopeptides			Three sulfated/phosphorylated glycopeptides						glycopeptides	Three sulfated/phosphorylated glycopeptides were detected, the identification of which was supported by tandem MS data.
26271046	5	87	gly	N-glycans	903:911	arg1	GluA2	GluA2			N-glycans	PUBTATOR		GluA2	2891		Moreover, it is thought that other N-glycans on GluA2 also have potential roles in the regulation of AMPAR functions.
22187327	4	13	gly	glycosylation	683:695	arg2	the most N-terminal glycosylation site			the most N-terminal glycosylation site						site	Only the N54Q mutant, which is the mutant for the most N-terminal glycosylation site, failed to induce filopodia-like protrusions in N2a cells.
18703501	7	25	part_of	contains	1209:1216	arg1	CA IX AND Asn(309)	CA IX		Asn(309)		PUBTATOR	SpecificSite	CA IX	768	Asn(309)	Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures.
18703501	7	25	part_of	contains	1209:1216	arg1	CA IX AND a unique N-linked glycosylation site	CA IX		a unique N-linked glycosylation site		PUBTATOR	Site	CA IX	768	site	Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures.
28377511	3	19	part_of	receptors	588:596	arg1	the cysteine-rich domain	FZD receptors		the cysteine-rich domain		PUBTATOR	Site	FZD receptors	7855	domain	Despite the progress in biochemical understanding of Wnt-FZD receptor interactions, the molecular basis for recognition of Wnt cis-unsaturated fatty acyl groups by the cysteine-rich domain (CRD) of FZD receptors remains elusive.
3353370	9	72	part_of	protein	1958:1964	arg1	the carboxyl terminus	protein		the carboxyl terminus		Fterm	Site	protein		terminus	The amino-terminal region of the beta chain of GPIb is followed by a transmembrane segment of 25 amino acids and an intracellular segment of 34 amino acids at the carboxyl terminus of the protein.
18467335	7	84	gly	epitopes	894:901	arg1	Fucose residues			epitopes	Fucose residues					epitopes	Fucose residues were identified both on the core GlcNAc and as parts of sialyl-Le(a/x) epitopes.
24342833	6	41	part_of	β-catenin	956:964	arg1	Serine 23	-catenin		Serine 23		PUBTATOR	SpecificSite	-catenin	1499	Serine 23	RESULTS: Serine 23 of β-catenin was determined as a site for O-GlcNAc modification which regulated its subcellular distribution, its interactions with cellular partners and consequently its transcriptional activity.
24342833	6	41	part_of	β-catenin	956:964	arg1	a site	-catenin		a site		PUBTATOR	Site	-catenin	1499	site	RESULTS: Serine 23 of β-catenin was determined as a site for O-GlcNAc modification which regulated its subcellular distribution, its interactions with cellular partners and consequently its transcriptional activity.
10677208	0	63	part_of	LTBP-1	114:119	arg1	the third eight-cysteine domain	LTBP-1		the third eight-cysteine domain		OGER	AminoAcid	LTBP-1	Q14766	cysteine domain	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10769135	0	46	part_of	alpha-amylase	40:52	arg1	the human pancreatic alpha-amylase active site	pancreatic alpha-amylase		the human pancreatic alpha-amylase active site		PUBTATOR	Site	pancreatic alpha-amylase	279	site	Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques.
10769135	0	90	part_of	pancreatic	29:38	arg1	the human pancreatic alpha-amylase active site	pancreatic alpha-amylase		the human pancreatic alpha-amylase active site		PUBTATOR	Site	pancreatic alpha-amylase	279	site	Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques.
17330941	5	19	gly	N-glycosylated	661:674	arg1	tethered N-glycosylated tryptic peptides			tethered N-glycosylated tryptic peptides						peptides	After trypsinization and extensive washing, tethered N-glycosylated tryptic peptides are released from the gel using PNGase F. Biotinylated cysteinyl-containing glycopeptides are then affinity selected using a monomeric avidin gel and analyzed by LC-MS/MS.
17330941	5	54	gly	glycopeptides	769:781	arg2	PNGase F. Biotinylated cysteinyl-containing glycopeptides			PNGase F. Biotinylated cysteinyl-containing glycopeptides						glycopeptides	After trypsinization and extensive washing, tethered N-glycosylated tryptic peptides are released from the gel using PNGase F. Biotinylated cysteinyl-containing glycopeptides are then affinity selected using a monomeric avidin gel and analyzed by LC-MS/MS.
15662415	3	17	part_of	receptor	430:437	arg1	the extracellular hormone-binding domain	receptor		the extracellular hormone-binding domain		Fterm	Site	receptor		domain	We present here the 2.9-A-resolution structure of a partially deglycosylated complex of human FSH bound to the extracellular hormone-binding domain of its receptor (FSHR(HB)).
6203908	13	58	part_of	2-macroglobulin	1383:1397	arg1	sequences	alpha 2-macroglobulin		sequences		PUBTATOR	Site	alpha 2-macroglobulin	2	sequences	A comparison of stretches of sequences from alpha 2-macroglobulin with partial sequence data for complement components C3 and C4 indicates that these proteins are evolutionary related.
11696579	7	29	part_of	Akt	1496:1498	arg1	the Akt phosphorylation site	Akt		the Akt phosphorylation site		PUBTATOR	Site	Akt	207	site	In contrast, when myc-tagged human eNOS carried a mutation at the Akt phosphorylation site (Ser1177), O-linked N-acetylglucosamine modification was unchanged by hyperglycemia and phospho-eNOS was undetectable.
11696579	7	29	part_of	Akt	1496:1498	arg1	Ser1177	Akt		Ser1177		PUBTATOR	AminoAcid	Akt	207	Ser1177	In contrast, when myc-tagged human eNOS carried a mutation at the Akt phosphorylation site (Ser1177), O-linked N-acetylglucosamine modification was unchanged by hyperglycemia and phospho-eNOS was undetectable.
1421756	3	75	part_of	TfR	423:425	arg1	the external domain	TfR		the external domain		PUBTATOR	Site	TfR	7037	domain	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	3	79	part_of	domain	409:414	arg1	A 70 kDa fragment	domain		A 70 kDa fragment						fragment	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
19413349	8	55	gly	glycosylation	1428:1440	arg2	the two N-linked glycosylation sites			the two N-linked glycosylation sites						sites	Finally, neither in vivo N-linked deglycosylation nor mutations of the two N-linked glycosylation sites significantly affected melanopsin function measured by Fos induction after light stimulation.
19413349	8	90	gly	deglycosylation	1378:1392	arg1	melanopsin function	melanopsin function				PUBTATOR		melanopsin	192223		Finally, neither in vivo N-linked deglycosylation nor mutations of the two N-linked glycosylation sites significantly affected melanopsin function measured by Fos induction after light stimulation.
12297049	1	46	part_of	EGFR	205:208	arg1	a truncated human EGFR ectodomain	EGFR		a truncated human EGFR ectodomain		PUBTATOR	Site	EGFR	1956	ectodomain	We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha.
18702514	3	29	gly	unglycosylated	458:471	arg1	human pancreatic lipase-related protein 2	human pancreatic lipase-related protein 2				PUBTATOR		pancreatic lipase-related protein 2	5408		Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	3	29	gly	unglycosylated	458:471	arg1	HPLRP2	HPLRP2				OGER		HPLRP2	P54318		Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
1388166	2	32	gly	sequence	381:388	arg1	the sequence SO4-4GalNAc beta 1				the sequence SO4-4GalNAc beta 1						We have determined that greater than 70% of the oligosaccharides on recombinant TFPI expressed in 293 cells terminate with the sequence SO4-4GalNAc beta 1, 4GlcNAc beta 1, 2Man alpha.
1388166	2	32	gly	sequence	381:388	arg1	4GlcNAc beta 1				4GlcNAc beta 1						We have determined that greater than 70% of the oligosaccharides on recombinant TFPI expressed in 293 cells terminate with the sequence SO4-4GalNAc beta 1, 4GlcNAc beta 1, 2Man alpha.
1388166	2	48	gly	TFPI	334:337	arg1	the oligosaccharides	TFPI			the oligosaccharides	PUBTATOR		TFPI	7035		We have determined that greater than 70% of the oligosaccharides on recombinant TFPI expressed in 293 cells terminate with the sequence SO4-4GalNAc beta 1, 4GlcNAc beta 1, 2Man alpha.
1388166	2	75	gly	oligosaccharides	302:317	arg1	recombinant TFPI	TFPI			oligosaccharides	PUBTATOR		TFPI	7035		We have determined that greater than 70% of the oligosaccharides on recombinant TFPI expressed in 293 cells terminate with the sequence SO4-4GalNAc beta 1, 4GlcNAc beta 1, 2Man alpha.
8053566	5	9	gly	glycoprotein	1057:1068	arg1	well-characterized proteins	well-characterized proteins				Fterm		proteins			Glycopeptides from well-characterized proteins, fetuin, alpha 1-acid glycoprotein, and tissue plasminogen activator were also analyzed to confirm exoglycosidase specificity for glycopeptides and establish the quantitative significance of the relative intensities of peaks in the mass spectra.
8053566	5	9	gly	glycoprotein	1057:1068	arg1	alpha 1-acid glycoprotein	alpha 1-acid glycoprotein				Fterm		glycoprotein			Glycopeptides from well-characterized proteins, fetuin, alpha 1-acid glycoprotein, and tissue plasminogen activator were also analyzed to confirm exoglycosidase specificity for glycopeptides and establish the quantitative significance of the relative intensities of peaks in the mass spectra.
8053566	5	69	gly	glycopeptides	1165:1177	arg2	glycopeptides			glycopeptides						glycopeptides	Glycopeptides from well-characterized proteins, fetuin, alpha 1-acid glycoprotein, and tissue plasminogen activator were also analyzed to confirm exoglycosidase specificity for glycopeptides and establish the quantitative significance of the relative intensities of peaks in the mass spectra.
12794637	4	19	part_of	furin	854:858	arg1	the decanoyl-Arg-Val-Lys-Arg-chloromethylketone (dec-RVKR-cmk)-inhibited mouse furin ectodomain	furin		the decanoyl-Arg-Val-Lys-Arg-chloromethylketone (dec-RVKR-cmk)-inhibited mouse furin ectodomain		PUBTATOR	Site	furin	18550	ectodomain	The 2.6 A crystal structure of the decanoyl-Arg-Val-Lys-Arg-chloromethylketone (dec-RVKR-cmk)-inhibited mouse furin ectodomain, the first PC structure, reveals an eight-stranded jelly-roll P domain associated with the catalytic domain.
23167757	7	72	gly	glycosylation	1257:1269	arg1	PDIA2 protein-protein interactions	PDIA2 protein-protein interactions				PUBTATOR		PDIA2	64714		Nevertheless, in HeLa cells, both wild-type and N127/284/516Q mutant PDIA2 proteins localize to the ER, but not the ER-Golgi intermediate compartment, suggesting that glycosylation is important for PDIA2 protein-protein interactions but not subcellular localization.
8436110	0	13	gly	glycoproteins	110:122	arg1	respiratory-mucus glycoproteins	respiratory-mucus glycoproteins				Fterm		glycoproteins			Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
8436110	0	43	gly	sialylated	51:60	arg1	novel sialylated oligosaccharide-alditols				novel sialylated oligosaccharide-alditols						Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
12421832	9	89	part_of	contains	1255:1262	arg1	The pro-MBP subunit AND 12 cysteine residues	The pro-MBP subunit		12 cysteine residues		OGER	AminoAcid	subunit	5069	cysteine residues	The pro-MBP subunit contains 12 cysteine residues, of which 10 have been accounted for.
3514617	9	117	gly	Asn-linked	1411:1420	arg1	a single Asn-linked carbohydrate unit			Asn	a single Asn-linked carbohydrate unit					Asn	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
28165004	6	7	part_of	PD-1	779:782	arg1	the IgV domain	PD-1		the IgV domain		PUBTATOR	Site	PD-1	P18621	domain	Structural and functional analyses unexpectedly reveal an N-terminal loop outside the IgV domain of PD-1.
17711303	5	65	gly	contains	876:883	arg1	the hKOR AND O-linked glycan	the hKOR			O-linked glycan	PUBTATOR		hKOR	4986		FLAG-hKOR was reduced to lower Mr bands by neuraminidase and O-glycosidase, indicating that the hKOR contains O-linked glycan.
18065761	2	1	part_of	heparin-binding	371:385	arg1	the high affinity heparin-binding domain	heparin		the high affinity heparin-binding domain		Fterm	Site	heparin		domain	We have previously determined the structure of the high affinity heparin-binding domain of TSP-1, designated TSPN-1, in association with the synthetic heparin, Arixtra.
18065761	2	31	part_of	TSP-1	397:401	arg1	the high affinity heparin-binding domain	TSP-1		the high affinity heparin-binding domain		PUBTATOR	Site	TSP-1	7057	domain	We have previously determined the structure of the high affinity heparin-binding domain of TSP-1, designated TSPN-1, in association with the synthetic heparin, Arixtra.
10715549	9	56	gly	glycosylation	1587:1599	arg2	Asn			Asn(30)						Asn(30)	These results indicate that the backbone structure consisting of 114 amino acids and N-linked glycosylation at Asn(30) is involved in the aggregation of LHbeta.
10715549	9	56	gly	glycosylation	1587:1599	arg1	30			Asn(30)						Asn(30)	These results indicate that the backbone structure consisting of 114 amino acids and N-linked glycosylation at Asn(30) is involved in the aggregation of LHbeta.
10715549	9	56	gly	glycosylation	1587:1599	arg1	Asn			Asn(30)						Asn(30)	These results indicate that the backbone structure consisting of 114 amino acids and N-linked glycosylation at Asn(30) is involved in the aggregation of LHbeta.
10715549	9	56	gly	glycosylation	1587:1599	arg1	30			Asn(30)						Asn(30)	These results indicate that the backbone structure consisting of 114 amino acids and N-linked glycosylation at Asn(30) is involved in the aggregation of LHbeta.
10715549	9	56	gly	glycosylation	1587:1599	arg1	Asn			Asn(30)						Asn(30)	These results indicate that the backbone structure consisting of 114 amino acids and N-linked glycosylation at Asn(30) is involved in the aggregation of LHbeta.
10715549	9	56	gly	glycosylation	1587:1599	arg1	Asn			Asn(30)						Asn(30)	These results indicate that the backbone structure consisting of 114 amino acids and N-linked glycosylation at Asn(30) is involved in the aggregation of LHbeta.
2059624	4	13	part_of	r-HPg	947:951	arg1	N289	r-HPg		N289		Cterm	SpecificSite	r-HPg	P00747	N289	At the earliest postinfection (p.i.) time period studied, i.e., 0-20 h, virtually all (96%) of the oligosaccharides released with glycopeptidase F from N289 of the expressed r-HPg were of the high-mannose type and comprised nearly the full range of such structures, containing 3-9 mannose units.
2842863	2	46	part_of	SAP-2	363:367	arg1	the derived amino acid sequence	SAP-2		the derived amino acid sequence		PUBTATOR	Site	SAP-2	2004	sequence	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
21757702	1	80	part_of	contain	197:203	arg1	Notch receptors AND multiple predicted sites	Notch receptors		multiple predicted sites		PUBTATOR	Site	Notch receptors	18128	sites	Notch activity is regulated by both O-fucosylation and O-glucosylation, and Notch receptors contain multiple predicted sites for both.
10889209	8	6	gly	N-glycosylation	1526:1540	arg1	ROMK1	ROMK1				PUBTATOR		ROMK1	3758		Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg1	GIRK1	GIRK1		Asn(119)		PUBTATOR		GIRK1	3760	Asn(119)	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg2	119			Asn(119)						Asn(119)	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg1	119			Asn(119)						Asn(119)	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg2	Asn			Asn(119)						Asn(119)	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg2	119	GIRK1		Asn(119)		PUBTATOR		GIRK1	3760	Asn(119)	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg1	119	GIRK1		Asn(119)		PUBTATOR		GIRK1	3760	Asn(119)	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg2	Asn	GIRK1		Asn(119)		PUBTATOR		GIRK1	3760	Asn(119)	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg1	119			Asn(119)						Asn(119)	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg2	Asn			Asn(119)						Asn(119)	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg2	Asn			Asn(119)						Asn(119)	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10383441	4	35	part_of	contains	571:578	arg1	murine DNase I AND Lys27	DNase I		Lys27 and Lys74		PUBTATOR	AminoAcid	DNase I	13419	Lys27 and Lys74	We now demonstrate that murine DNase I, which contains Lys27 and Lys74, is phosphorylated only 20.9% when expressed in the same COS-1 cell system.
3356193	5	38	gly	NeuAc	718:722	arg1	porcine plasminogen	plasminogen			NeuAc	OGER		plasminogen	P00747		In porcine plasminogen the sialic acid is mainly NeuAc; the Man alpha 1----6 branch, however, is only partially sialylated.
3356193	5	56	gly	sialylated	781:790	arg1	the Man alpha 1----6 branch				the Man alpha 1----6 branch						In porcine plasminogen the sialic acid is mainly NeuAc; the Man alpha 1----6 branch, however, is only partially sialylated.
16170054	2	40	gly	glycoproteins	393:405	arg1	murine epidermis and dermis glycoproteins	murine epidermis and dermis glycoproteins				Fterm		glycoproteins			Aiming to elucidate the N-glycosylation of murine epidermis and dermis glycoproteins, here we used a novel approach for focused proteomics.
16170054	2	51	gly	N-glycosylation	346:360	arg1	murine epidermis and dermis glycoproteins	murine epidermis and dermis glycoproteins				Fterm		glycoproteins			Aiming to elucidate the N-glycosylation of murine epidermis and dermis glycoproteins, here we used a novel approach for focused proteomics.
9054441	0	20	gly	trisaccharide	41:53	arg1	Ser-248			Ser-248	Ser-248		SpecificSite			Ser-248	Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2.
9054441	0	67	gly	sialylated	30:39	arg1	a novel O-linked sialylated trisaccharide				a novel O-linked sialylated trisaccharide						Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2.
22333914	2	24	part_of	∼320-residue	423:434	arg1	a much larger ∼320-residue domain	r ∼320-residue		a much larger ∼320-residue domain		PUBTATOR	Site	r ∼320-residue	151	domain	Here, we show that unexpectedly the ∼40-residue GPS motif represents an integral part of a much larger ∼320-residue domain that we termed GPCR-Autoproteolysis INducing (GAIN) domain.
22333914	2	28	part_of	GPS	368:370	arg1	unexpectedly the ∼40-residue GPS motif	GPS		unexpectedly the ∼40-residue GPS motif		OGER	Site	GPS		motif	Here, we show that unexpectedly the ∼40-residue GPS motif represents an integral part of a much larger ∼320-residue domain that we termed GPCR-Autoproteolysis INducing (GAIN) domain.
22333914	2	35	part_of	GPCR-Autoproteolysis	458:477	arg1	GPCR-Autoproteolysis INducing (GAIN) domain	d GPCR		GPCR-Autoproteolysis INducing (GAIN) domain		PUBTATOR	Site	d GPCR	23218	domain	Here, we show that unexpectedly the ∼40-residue GPS motif represents an integral part of a much larger ∼320-residue domain that we termed GPCR-Autoproteolysis INducing (GAIN) domain.
22333914	2	41	part_of	larger	416:421	arg1	a much larger ∼320-residue domain	l		a much larger ∼320-residue domain		PUBTATOR	Site	l	23218	domain	Here, we show that unexpectedly the ∼40-residue GPS motif represents an integral part of a much larger ∼320-residue domain that we termed GPCR-Autoproteolysis INducing (GAIN) domain.
14749323	6	4	part_of	site	931:934	arg1	mOAT1	mOAT1		site		PUBTATOR	SpecificSite	mOAT1	18399	site Asp-39	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	6	94	part_of	site	995:998	arg1	hOAT1	hOAT1		site		PUBTATOR	Site	hOAT1	9356	site	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
24121512	6	21	part_of	cdAE1	1228:1232	arg1	55-356	cdAE1		55-356		Cterm	SpecificSite	cdAE1	6521	residues 55-356	A 2.1-Å resolution crystal structure of cdΔ54AE1 (residues 55-356 of cdAE1) lacking the amino-terminal and carboxyl-terminal disordered regions, produced at physiological pH, revealed an extensive hydrogen-bonded network involving Arg(283) and Glu(85).
12526797	2	13	part_of	ICAM-1	366:371	arg1	Glu-34	ICAM-1		Glu-34		PUBTATOR	SpecificSite	ICAM-1	3383	Glu-34	The I domain Mg2+ directly coordinates Glu-34 of ICAM-1, and a dramatic swing of I domain residue Glu-241 enables a critical salt bridge.
28089369	5	8	part_of	sites	744:748	arg1	Notch1	Notch1		sites		PUBTATOR	Site	Notch1	18128	sites	We found that Lunatic and Manic Fringe modified similar sites on Notch1, while Radical Fringe modified a subset.
3667593	5	17	gly	galactose	833:841	arg1	the human IFN-beta	IFN-beta			galactose	PUBTATOR		IFN-beta	3456		NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	5	54	gly	desialylated	984:995	arg1	enzymatically desialylated IFN-beta	enzymatically desialylated IFN-beta				PUBTATOR		IFN-beta	3456		NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
17715132	5	1	gly	glycosylated	694:705	arg1	Pannexin1	Pannexin1		Asn-254		PUBTATOR		Pannexin1	24145	Asn-254	We show for the first time that Pannexin1 is glycosylated at Asn-254 and that this residue is important for plasma membrane targeting.
1421756	9	78	part_of	contains	1449:1456	arg1	s-TfR AND Thr104	TfR		Thr104		PUBTATOR	AminoAcid	TfR	7037	Thr104	From human serum we purified the cleaved, soluble form of the TfR (s-TfR), which contains Thr104, but lacks Thr96.
20877282	7	13	part_of	semaphorin	1694:1703	arg1	the amino-terminal seven-bladed β-propeller (sema) domains	semaphorin		the amino-terminal seven-bladed β-propeller (sema) domains		Fterm	Site	semaphorin		domains	Furthermore, the shared generic architecture of the complexes, formed through conserved contacts of the amino-terminal seven-bladed β-propeller (sema) domains of both semaphorin and plexin, suggests that a common mode of interaction triggers all semaphorin-plexin based signalling, while distinct insertions within or between blades of the sema domains determine binding specificity.
20877282	7	52	part_of	plexin	1709:1714	arg1	the amino-terminal seven-bladed β-propeller (sema) domains	plexin		the amino-terminal seven-bladed β-propeller (sema) domains		Fterm	Site	plexin		domains	Furthermore, the shared generic architecture of the complexes, formed through conserved contacts of the amino-terminal seven-bladed β-propeller (sema) domains of both semaphorin and plexin, suggests that a common mode of interaction triggers all semaphorin-plexin based signalling, while distinct insertions within or between blades of the sema domains determine binding specificity.
14764083	1	6	gly	glycoprotein	150:161	arg1	an iron-binding glycoprotein	an iron-binding glycoprotein				Fterm		glycoprotein			Lactoferrin (LF) is an iron-binding glycoprotein of the innate host defence system.
14764083	1	6	gly	glycoprotein	150:161	arg1	Lactoferrin	Lactoferrin				PUBTATOR		Lactoferrin	280846		Lactoferrin (LF) is an iron-binding glycoprotein of the innate host defence system.
29095159	3	37	gly	leucine-rich	499:510	arg1	the NgR ligand-binding leucine-rich repeat (LRR) domain			leucine	the NgR ligand-binding leucine-rich repeat (LRR) domain					leucine	The available structures of the NgR ligand-binding leucine-rich repeat (LRR) domain have an artificial disulfide pattern owing to truncated C-terminal construct boundaries.
24692546	4	1	gly	deglycosylated	650:663	arg1	deglycosylated FSH	deglycosylated FSH				OGER		FSH			It also predicts that, upon dissociation of the FSHR trimer into monomers, the binding of glycosylated FSH, but not deglycosylated FSH, would increase 3-fold, and that the dissociated monomers would in turn enhance FSHR binding and signaling activities by 3-fold.
24692546	4	29	gly	glycosylated	624:635	arg1	glycosylated FSH	glycosylated FSH				OGER		FSH			It also predicts that, upon dissociation of the FSHR trimer into monomers, the binding of glycosylated FSH, but not deglycosylated FSH, would increase 3-fold, and that the dissociated monomers would in turn enhance FSHR binding and signaling activities by 3-fold.
9539703	4	68	part_of	ICAM-1	647:652	arg1	the two amino-terminal domains	ICAM-1		the two amino-terminal domains		PUBTATOR	Site	ICAM-1	3383	domains	The three-dimensional atomic structure of the two amino-terminal domains (D1 and D2) of ICAM-1 has been determined to 2.2-A resolution and fitted into a cryoelectron microscopy reconstruction of a rhinovirus-ICAM-1 complex.
7916636	4	39	part_of	contain	471:477	arg1	urinary kallikrein AND a Lys-162	urinary kallikrein		a Lys-162		PUBTATOR	SpecificSite	kallikrein	9622	Lys-162	The human kallikrein gene and urinary kallikrein both contain a Lys-162 instead of the reported Glu-162.
10715549	4	46	part_of	LHbeta	1064:1069	arg1	the Asn(13)	LHbeta		the Asn(13)		PUBTATOR	SpecificSite	LHbeta	3972	Asn(13)	No aggregation was seen when N-linked oligosaccharides were attached to the Asn(13) of LHbeta.
26195816	6	24	part_of	LCAT	751:754	arg1	the region	LCAT		the region		PUBTATOR	Site	LCAT	P04180	region	Subdomain 1 contains the region of LCAT shown to be required for interfacial activation, while subdomain 2 contains the lid and amino acids that shape the substrate binding pocket.
25092234	7	60	gly	glycopeptides	999:1011	arg2	hFXI glycopeptides			hFXI glycopeptides						glycopeptides	Analysis of hFXI glycopeptides by LC-MS/MS enabled site-specific glycan profiling and occupancy.
3264725	7	19	gly	N-glycosylated	1475:1488	arg1	322			Asparagine residues 145 and 322						Asparagine residues 145 and 322	Asparagine residues 145 and 322 were found to be fully N-glycosylated in human plasma factor VIIa.
3264725	7	19	gly	N-glycosylated	1475:1488	arg1	human plasma factor VIIa	factor VIIa		Asparagine residues 145 and 322		Cterm		factor VIIa		Asparagine residues 145 and 322	Asparagine residues 145 and 322 were found to be fully N-glycosylated in human plasma factor VIIa.
3264725	7	19	gly	N-glycosylated	1475:1488	arg2	322			Asparagine residues 145 and 322						Asparagine residues 145 and 322	Asparagine residues 145 and 322 were found to be fully N-glycosylated in human plasma factor VIIa.
3264725	7	19	gly	N-glycosylated	1475:1488	arg2	Asparagine residues 145 and 322			Asparagine residues 145 and 322						Asparagine residues 145 and 322	Asparagine residues 145 and 322 were found to be fully N-glycosylated in human plasma factor VIIa.
3264725	7	19	gly	N-glycosylated	1475:1488	arg1	human plasma factor VIIa	factor VIIa		Asparagine residues 145 and 322		Cterm		factor VIIa		Asparagine residues 145 and 322	Asparagine residues 145 and 322 were found to be fully N-glycosylated in human plasma factor VIIa.
3264725	7	19	gly	N-glycosylated	1475:1488	arg2	322			Asparagine residues 145 and 322						Asparagine residues 145 and 322	Asparagine residues 145 and 322 were found to be fully N-glycosylated in human plasma factor VIIa.
3264725	7	19	gly	N-glycosylated	1475:1488	arg2	Asparagine residues 145 and 322			Asparagine residues 145 and 322						Asparagine residues 145 and 322	Asparagine residues 145 and 322 were found to be fully N-glycosylated in human plasma factor VIIa.
3264725	7	19	gly	N-glycosylated	1475:1488	arg2	322	factor VIIa		Asparagine residues 145 and 322		Cterm		factor VIIa		Asparagine residues 145 and 322	Asparagine residues 145 and 322 were found to be fully N-glycosylated in human plasma factor VIIa.
3264725	7	19	gly	N-glycosylated	1475:1488	arg2	Asparagine residues 145 and 322	factor VIIa		Asparagine residues 145 and 322		Cterm		factor VIIa		Asparagine residues 145 and 322	Asparagine residues 145 and 322 were found to be fully N-glycosylated in human plasma factor VIIa.
3264725	7	19	gly	N-glycosylated	1475:1488	arg2	Asparagine residues 145 and 322			Asparagine residues 145 and 322						Asparagine residues 145 and 322	Asparagine residues 145 and 322 were found to be fully N-glycosylated in human plasma factor VIIa.
14693913	2	99	gly	glycoprotein	358:369	arg1	The 76.3-kDa glycoprotein	The 76.3-kDa glycoprotein				Fterm		glycoprotein			The 76.3-kDa glycoprotein was associated with 75-80 Man and a small amount of GlcNAc.
8344280	0	63	gly	glycoprotein	50:61	arg1	human interleukin 2 glycoprotein variants	human interleukin 2 glycoprotein variants				PUBTATOR		interleukin 2 glycoprotein	3558		Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus-infected Sf21 cells.
1059087	0	54	gly	glycophorin	78:88	arg1	oligosaccharide attachment sites	glycophorin			oligosaccharide attachment sites	Fterm		glycophorin			Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
7525874	1	61	gly	protein	163:169	arg1	The carbohydrate structures	beta-trace protein			The carbohydrate structures	PUBTATOR		beta-trace protein	5730		The carbohydrate structures of beta-trace protein from human cerebrospinal fluid have been elucidated.
8323299	7	1	part_of	lamp-1	1218:1223	arg1	residues 167 to 190	lamp-1		residues 167 to 190		PUBTATOR	SpecificSite	lamp-1	3916	residues 167	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
9449027	0	37	gly	beta-subunits	53:65	arg1	Carbohydrate and peptide structure	beta-subunits			Carbohydrate and peptide structure	Fterm		beta-subunits			Carbohydrate and peptide structure of the alpha- and beta-subunits of human chorionic gonadotropin from normal and aberrant pregnancy and choriocarcinoma.
9449027	0	68	gly	peptide	17:23	arg1	Carbohydrate and peptide structure				Carbohydrate and peptide structure						Carbohydrate and peptide structure of the alpha- and beta-subunits of human chorionic gonadotropin from normal and aberrant pregnancy and choriocarcinoma.
27768895	3	52	part_of	PKD2	454:457	arg1	The PKD2 voltage-sensor domain	PKD2		The PKD2 voltage-sensor domain		PUBTATOR	Site	PKD2	Q13563	domain	The PKD2 voltage-sensor domain retains two of four gating charges commonly found in those of voltage-gated ion channels.
2141278	4	1	gly	occupied	1085:1092	arg2	position 134			position 134						position 134	This fragment was reduced and alkylated and then digested with elastase, and three peptides covering positions 131-135, 131-139, and 131-140 were characterized by amino acid analysis, Edman degradation, and mass spectrometry, showing that position 134 of C1-s is occupied partly by an asparagine (47%) and partly by an erythro-beta-hydroxyasparagine, in contrast with the homologous position (150) of C1-r which only contains erythro-beta-hydroxyasparagine.
19139490	4	61	gly	glycoproteins	704:716	arg1	CF glycoproteins	CF glycoproteins				Fterm		glycoproteins			Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
22556278	6	86	gly	sites	953:957	arg1	proteasome subunits	subunits			sites	Fterm		subunits			Therefore, identification of O-GlcNAcylation sites on proteasome subunits essentially requires effective enrichment strategies.
8798614	1	68	gly	glycoprotein	176:187	arg1	a glycosylphosphatidylinositol-anchored membrane glycoprotein	a glycosylphosphatidylinositol-anchored membrane glycoprotein				Fterm		glycoprotein			CD59 is a glycosylphosphatidylinositol-anchored membrane glycoprotein that serves as the principle cellular inhibitor of the C5b-9 membrane attack complex (MAC) of human complement.
8798614	1	68	gly	glycoprotein	176:187	arg1	CD59	CD59				PUBTATOR		CD59	966		CD59 is a glycosylphosphatidylinositol-anchored membrane glycoprotein that serves as the principle cellular inhibitor of the C5b-9 membrane attack complex (MAC) of human complement.
1898343	1	24	gly	glycoprotein	93:104	arg1	Human pancreatic elastase 1	Human pancreatic elastase 1				PUBTATOR		Human pancreatic elastase 1	1990		Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	24	gly	glycoprotein	93:104	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	41	gly	N-glycosylation	131:145	arg2	two potential N-glycosylation sites			two potential N-glycosylation sites						sites	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	27	gly	carries	167:173	arg1	two potential N-glycosylation sites AND a carbohydrate moiety [Wendorf			two potential N-glycosylation sites	a carbohydrate moiety [Wendorf					sites	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
22576872	3	8	part_of	Aβ	526:527	arg1	longer Aβ peptides	Aβ 		longer Aβ peptides		PUBTATOR	Site	Aβ 	351	peptides	When one analyzes longer Aβ peptides by low-energy collision-induced dissociation tandem mass spectrometry (MS/MS), mainly long b-fragments are observed, limiting the possibility to determine variations such as amino acid variants or post-translational modifications (PTMs) within the N-terminal half of the peptide.
20457942	2	13	gly	glycoprotein	172:183	arg1	RhCG	RhCG				PUBTATOR		RhCG	51458		Human Rh C glycoprotein (RhCG) forms a trimeric complex that plays an essential role in ammonia excretion and renal pH regulation.
20457942	2	13	gly	glycoprotein	172:183	arg1	Human Rh C glycoprotein	Human Rh C glycoprotein				PUBTATOR		Human Rh C glycoprotein	51458		Human Rh C glycoprotein (RhCG) forms a trimeric complex that plays an essential role in ammonia excretion and renal pH regulation.
23829323	8	46	gly	glycosylation	1769:1781	arg2	the four haptoglobin N-linked glycosylation sites			the four haptoglobin N-linked glycosylation sites						sites	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	8	56	gly	glycopeptide	1584:1595	arg2	glycopeptide identifications			glycopeptide identifications						glycopeptide	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
17715132	4	34	gly	glycosylation	564:576	arg2	three putative N-linked glycosylation sites			three putative N-linked glycosylation sites						sites	Using site-directed mutagenesis we analyzed three putative N-linked glycosylation sites and examined the effects of each mutation on channel expression.
23285087	4	27	gly	sites	866:870	arg1	three glycosylation sites			three glycosylation sites						sites	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	61	gly	glycosylation	852:864	arg2	three glycosylation sites			three glycosylation sites						sites	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	27	gly	sites	866:870	arg1	Asn134			Asn134, Asn503 and Asn516						Asn134, Asn503 and Asn516	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	27	gly	sites	866:870	arg1	Asn516			Asn134, Asn503 and Asn516						Asn134, Asn503 and Asn516	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	27	gly	sites	866:870	arg1	Asn516			Asn134, Asn503 and Asn516						Asn134, Asn503 and Asn516	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	61	gly	glycosylation	852:864	arg2	Asn503			Asn134, Asn503 and Asn516						Asn134, Asn503 and Asn516	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	61	gly	glycosylation	852:864	arg2	Asn134			Asn134, Asn503 and Asn516						Asn134, Asn503 and Asn516	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	61	gly	glycosylation	852:864	arg2	Asn134			Asn134, Asn503 and Asn516						Asn134, Asn503 and Asn516	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
19656770	0	30	gly	glycosite	78:86	arg2	glycosite occupancy			glycosite occupancy						glycosite	The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation.
25187573	12	98	part_of	STP-rich	2084:2091	arg1	the central STP-rich region	STP		the central STP-rich region		OGER	Site	STP	P50225	region	These glycosylation sites were focused in the central STP-rich region, giving the domain a negative charge.
2141278	0	8	part_of	factor	95:100	arg1	the epidermal growth factor homology region	factor		the epidermal growth factor homology region		Fterm	Site	factor		region	Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region.
2141278	0	63	part_of	C1-s	58:61	arg1	a fragment	C1-s		a fragment		PUBTATOR	Site	C1-s	716	fragment	Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region.
2141278	0	2	part_of	containing	63:72	arg1	C1-s AND the epidermal growth factor homology region	C1-s		the epidermal growth factor homology region		PUBTATOR	Site	C1-s	716	region	Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region.
22483115	4	32	part_of	Fab	576:578	arg1	the Fab fragment	Fab		the Fab fragment		PUBTATOR	Site	Fab	2187	fragment	The crystal structure of the monomeric DDR1 extracellular region bound to the Fab fragment of mAb 3E3 reveals that the collagen-binding discoidin (DS) domain is tightly associated with the following DS-like domain, which contains the epitopes of all mAbs.
22483115	4	38	part_of	DDR1	537:540	arg1	the monomeric DDR1 extracellular region	DDR1		the monomeric DDR1 extracellular region		PUBTATOR	Site	DDR1	780	region	The crystal structure of the monomeric DDR1 extracellular region bound to the Fab fragment of mAb 3E3 reveals that the collagen-binding discoidin (DS) domain is tightly associated with the following DS-like domain, which contains the epitopes of all mAbs.
22483115	4	11	part_of	contains	719:726	arg1	the following DS-like domain AND the epitopes	the following DS-like domain		the epitopes						epitopes	The crystal structure of the monomeric DDR1 extracellular region bound to the Fab fragment of mAb 3E3 reveals that the collagen-binding discoidin (DS) domain is tightly associated with the following DS-like domain, which contains the epitopes of all mAbs.
7688323	3	24	part_of	GPIIb	635:639	arg1	this GPIIb domain	GPIIb		this GPIIb domain		PUBTATOR	Site	GPIIb	3674	domain	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	3	25	part_of	GPIIb	497:501	arg1	the GPIIb fragment 704-856	GPIIb		the GPIIb fragment 704-856		PUBTATOR	Site	GPIIb	3674	fragment	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	3	33	part_of	contains	520:527	arg1	the GPIIb fragment 704-856 AND the whole Baka epitope	the GPIIb fragment 704-856		the whole Baka epitope						epitope	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
8702538	2	27	gly	glycoproteins	418:430	arg1	selected cell surface glycoproteins	selected cell surface glycoproteins				Fterm		glycoproteins			Recent work has shown that CD22 specifically recognizes sialic acid linked alpha2,6 to terminal N-linked oligosaccharides on selected cell surface glycoproteins.
8702538	2	47	gly	oligosaccharides	376:391	arg1	selected cell surface glycoproteins	glycoproteins			oligosaccharides	Fterm		glycoproteins			Recent work has shown that CD22 specifically recognizes sialic acid linked alpha2,6 to terminal N-linked oligosaccharides on selected cell surface glycoproteins.
8436110	5	33	gly	sialylated	665:674	arg1	medium-size sialylated oligosaccharides				medium-size sialylated oligosaccharides						In the present work, medium-size sialylated oligosaccharides were obtained after ion-exchange chromatography and were subsequently separated into 36 fractions utilizing gel filtration, HPLC on normal-phase alkylamine-bonded silica and reverse-phase HPLC.
2015821	0	70	gly	1-antichymotrypsin	60:77	arg1	the glycans	alpha 1-antichymotrypsin			the glycans	PUBTATOR		alpha 1-antichymotrypsin	12		Structure determination of the glycans of human-serum alpha 1-antichymotrypsin using 1H-NMR spectroscopy and deglycosylation by N-glycanase.
25261253	3	14	part_of	IL-18Rα	375:381	arg1	the ectodomain	IL-18Rα,		the ectodomain		PUBTATOR	Site	IL-18Rα,	8809	ectodomain	Here we report the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition.
25261253	3	17	part_of	structure	333:341	arg1	the ectodomain	structure of IL-18		the ectodomain		PUBTATOR	Site	structure of IL-18	3606	ectodomain	Here we report the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition.
23878260	3	53	part_of	VEGFRs	489:494	arg1	The extracellular domain	VEGFRs		The extracellular domain		PUBTATOR	Site	VEGFRs	2324	domain	The extracellular domain of VEGFRs consists of seven Ig homology domains; domains 1-3 (D1-3) are responsible for ligand binding, and the membrane-proximal domains 4-7 (D4-7) are involved in structural rearrangements essential for receptor dimerization and activation.
18491227	3	52	gly	N-glycosylation	628:642	arg1	Asn-633			Asn-633						Asn-633	In this study we investigated the molecular mechanism of E-cadherin, which lacks N-glycosylation at Asn-633 (M4), degradation and the role of the N-glycan at Asn-633 in E-cadherin folding.
19656770	6	11	part_of	proteins	1245:1252	arg1	the extracellular domain	proteins		the extracellular domain		Fterm	Site	proteins		domain	The identification of the N-glycosylation sites on the extracellular domain of the proteins allowed for the determination of the orientation of the identified proteins within the plasma membrane.
19656770	6	44	part_of	sites	1204:1208	arg1	the proteins	proteins		sites		Fterm	Site	proteins		sites	The identification of the N-glycosylation sites on the extracellular domain of the proteins allowed for the determination of the orientation of the identified proteins within the plasma membrane.
7106126	1	21	gly	sialoglycoprotein	207:223	arg1	a minor human erythrocyte membrane sialoglycoprotein	a minor human erythrocyte membrane sialoglycoprotein				Fterm		sialoglycoprotein			The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	1	4	gly	glycopeptide	154:165	arg1	a minor human erythrocyte membrane sialoglycoprotein	sialoglycoprotein		glycopeptide		Fterm		sialoglycoprotein		glycopeptide	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
9343410	3	2	part_of	Sp1	485:487	arg1	the previously characterized glutamine-rich transactivation domain	Sp1		the previously characterized glutamine-rich transactivation domain		OGER	Site	Sp1	Q8N907	domain	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
7620335	3	64	gly	released	656:663	arg1	the glycopeptides AND N-linked oligosaccharides			the glycopeptides	N-linked oligosaccharides					glycopeptides	N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion were derivatized with 2-aminopyridine.
7620335	3	98	gly	glycopeptides	674:686	arg2	the glycopeptides			the glycopeptides						glycopeptides	N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion were derivatized with 2-aminopyridine.
21917917	9	5	part_of	contains	1397:1404	arg1	SNAT4 AND 10 transmembrane domains	SNAT4		10 transmembrane domains		PUBTATOR	Site	SNAT4	55089	domains	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	9	5	part_of	contains	1397:1404	arg1	SNAT4 AND a large N-glycosylated, extracellular loop domain	SNAT4		a large N-glycosylated, extracellular loop domain		PUBTATOR	Site	SNAT4	55089	domain	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
3353370	7	28	part_of	contains	1330:1337	arg1	The amino-terminal region AND a leucine-rich sequence	The amino-terminal region		a leucine-rich sequence						sequence	The amino-terminal region of the beta chain contains a leucine-rich sequence of 24 amino acids that is similar to a sequence that occurs as seven tandem repeats in the alpha chain of GPIb and nine tandem repeats in leucine-rich alpha 2-glycoprotein.
11258925	0	25	part_of	sites	38:42	arg1	cyclooxygenase-2	cyclooxygenase-2		sites		PUBTATOR	Site	cyclooxygenase-2	5743	sites	Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry.
10207176	4	53	part_of	protein	676:682	arg1	the same region	protein		the same region		Fterm	Site	protein		region	This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor.
21965667	5	17	part_of	site	739:742	arg1	the receptor	receptor		site		Fterm	Site	receptor		site	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	5	36	part_of	FcγRI	684:688	arg1	positioned	FcγRI		positioned		PUBTATOR	Site	FcγRI	2209	position	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	5	36	part_of	FcγRI	684:688	arg1	the D3 domain	FcγRI		the D3 domain		PUBTATOR	Site	FcγRI	2209	domain	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	5	61	part_of	IgG	727:729	arg1	the putative IgG binding site	IgG		the putative IgG binding site		Cterm	Site	IgG		site	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
7776966	1	101	part_of	contains	184:191	arg1	FSHR AND a large extracellular domain	FSHR		a large extracellular domain		PUBTATOR	Site	FSHR	2492	domain	The FSH receptor (FSHR) contains a large extracellular domain in which exist three potential sites for N-linked glycosylation.
7776966	1	101	part_of	contains	184:191	arg1	The FSH receptor AND a large extracellular domain	The FSH receptor		a large extracellular domain		PUBTATOR	Site	FSH receptor	2492	domain	The FSH receptor (FSHR) contains a large extracellular domain in which exist three potential sites for N-linked glycosylation.
25265424	5	23	part_of	carry	847:851	arg1	all three proteins AND H epitopes	all three proteins		H epitopes		Fterm	Site	proteins		epitopes	MSn analysis of permethylated detached glycans confirms the presence of LeY glycoforms on haptoglobin, which cannot be detected in hemopexin or complement factor H; all three proteins carry Lewis and H epitopes.
9169007	9	47	part_of	site	1655:1658	arg1	the X-ray structure	X-ray structure of antithrombin		site		PUBTATOR	Site	X-ray structure of antithrombin	462	site	The extent of heparin-affinity enhancement was correlated with the distance of the mutated glycosylation site to the putative heparin-binding site in the X-ray structure of antithrombin.
9169007	9	75	part_of	heparin-binding	1639:1653	arg1	the putative heparin-binding site	heparin		the putative heparin-binding site		Fterm	Site	heparin		site	The extent of heparin-affinity enhancement was correlated with the distance of the mutated glycosylation site to the putative heparin-binding site in the X-ray structure of antithrombin.
18929574	4	8	part_of	CD8alphabeta	660:671	arg1	the CD8alphabeta immunoglobulin-like ectodomains	structure of the CD8alphabeta		the CD8alphabeta immunoglobulin-like ectodomains		Cterm	Site	structure of the CD8alphabeta	12525	ectodomains	To elucidate the molecular basis for this inhibition, the crystal structure of the CD8alphabeta immunoglobulin-like ectodomains were determined in complex with mAb YTS156.7 Fab at 2.7 A resolution.
16046623	5	39	gly	observed	885:892	arg2	the six predicted N-glycosylation sites AND sugar units			the six predicted N-glycosylation sites	sugar units					sites	Secondly, sugar units are clearly observed at two of the six predicted N-glycosylation sites.
16046623	5	53	gly	N-glycosylation	922:936	arg2	the six predicted N-glycosylation sites			the six predicted N-glycosylation sites						sites	Secondly, sugar units are clearly observed at two of the six predicted N-glycosylation sites.
18780401	7	29	gly	N-glycosylated	1150:1163	arg1	63 N-glycosylated sites			63 N-glycosylated sites						sites	Using this strategy, 32 different glycoproteins were identified and 63 N-glycosylated sites encrypted in them were located.
18780401	7	61	gly	glycoproteins	1113:1125	arg1	32 different glycoproteins	32 different glycoproteins				Fterm		glycoproteins			Using this strategy, 32 different glycoproteins were identified and 63 N-glycosylated sites encrypted in them were located.
6619128	0	19	gly	IgD	68:70	arg1	the O-glycosidically linked oligosaccharides	IgD			the O-glycosidically linked oligosaccharides	OGER		IgD	P01880		Structures of the O-glycosidically linked oligosaccharides of human IgD.
8334986	4	21	gly	glycosylation	479:491	arg2	the glycosylation sites			the glycosylation sites						sites	Electron density at two of the glycosylation sites for parts of the carbohydrate moieties was observed.
8702840	0	0	gly	motif	72:76	arg1	Cytoplasmic O-GlcNAc modification				Cytoplasmic O-GlcNAc modification						Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	0	49	gly	domain	46:51	arg1	Cytoplasmic O-GlcNAc modification			domain	Cytoplasmic O-GlcNAc modification					domain	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	0	44	gly	modification	21:32	arg1	the KSP repeat motif AND Cytoplasmic O-GlcNAc modification			domain	Cytoplasmic O-GlcNAc modification					domain	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
24977290	6	90	part_of	ADAMTS13	1106:1113	arg1	the CUB domain	ADAMTS13		the CUB domain		PUBTATOR	Site	ADAMTS13	Q76LX8	domain	Nine of the 10 predicted N-linked glycosylation sites were identified in or near the metalloproteinase,spacer, thrombospondin type 1 repeat (TSR1) and the CUB domain of plasma ADAMTS13.
1371281	6	16	gly	CK18	879:882	arg1	N-acetylglucosamine/protein molecule	CK18			N-acetylglucosamine/protein molecule	PUBTATOR		CK18	3875		Using chemical analysis, the stoichiometry of glycosylation was found to be 1.5 and 2 molecules of N-acetylglucosamine/protein molecule of CK8 and CK18, respectively.
1371281	6	33	gly	CK8	871:873	arg1	N-acetylglucosamine/protein molecule	CK8			N-acetylglucosamine/protein molecule	PUBTATOR		CK8	3856		Using chemical analysis, the stoichiometry of glycosylation was found to be 1.5 and 2 molecules of N-acetylglucosamine/protein molecule of CK8 and CK18, respectively.
14707133	1	28	gly	glypican-1	193:202	arg1	a glycosylphosphatidylinositol-linked heparan sulfate proteoglycan	glypican-1			a glycosylphosphatidylinositol-linked heparan sulfate proteoglycan	PUBTATOR		glypican-1	58920		The core protein of glypican-1, a glycosylphosphatidylinositol-linked heparan sulfate proteoglycan, can bind Cu(II) or Zn(II) ions and undergo S-nitrosylation in the presence of nitric oxide.
21932778	7	35	gly	N-glycosylated	1267:1280	arg1	N-glycosylated glypican-1	N-glycosylated glypican-1				PUBTATOR		N-glycosylated glypican-1	2817		N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	7	68	gly	N-deglycosylated	1138:1153	arg1	N-deglycosylated glypican-1	N-deglycosylated glypican-1				PUBTATOR		N-deglycosylated glypican-1	2817		N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
26993603	5	33	gly	Removal	712:718	arg2	N-glycans AND Asn144			Asn144	N-glycans					Asn144	Removal of N-glycans at Asn144 enhanced the motility and invasiveness of hepatocellular carcinoma cells, possibly due to inhibition of cell adhesion related to the changes of cell membrane glycosylation.
21827946	2	7	part_of	Fab	260:262	arg1	the 1121B Fab fragment	1121B Fab		the 1121B Fab fragment		PUBTATOR	Site	1121B Fab	2187	fragment	We have determined the structure of the 1121B Fab fragment in complex with domain 3 of VEGFR2, as well as the structure of a different neutralizing anti-VEGFR2 antibody, 6.64, also in complex with VEGFR2 domain 3.
21827946	2	9	part_of	1121B	254:258	arg1	the 1121B Fab fragment	1121B Fab		the 1121B Fab fragment		PUBTATOR	Site	1121B Fab	2187	fragment	We have determined the structure of the 1121B Fab fragment in complex with domain 3 of VEGFR2, as well as the structure of a different neutralizing anti-VEGFR2 antibody, 6.64, also in complex with VEGFR2 domain 3.
21827946	2	18	part_of	VEGFR2	301:306	arg1	domain 3	VEGFR2		domain 3		PUBTATOR	Site	VEGFR2	3791	domain	We have determined the structure of the 1121B Fab fragment in complex with domain 3 of VEGFR2, as well as the structure of a different neutralizing anti-VEGFR2 antibody, 6.64, also in complex with VEGFR2 domain 3.
21827946	2	22	part_of	VEGFR2	411:416	arg1	VEGFR2 domain 3	VEGFR2		VEGFR2 domain 3		PUBTATOR	Site	VEGFR2	3791	domain	We have determined the structure of the 1121B Fab fragment in complex with domain 3 of VEGFR2, as well as the structure of a different neutralizing anti-VEGFR2 antibody, 6.64, also in complex with VEGFR2 domain 3.
17591618	2	96	gly	N-glycosylation	366:380	arg2	nine potential N-glycosylation sites			nine potential N-glycosylation sites						sites	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	2	102	gly	glycoprotein	327:338	arg1	CFH	CFH				PUBTATOR		CFH	P08603		CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	2	102	gly	glycoprotein	327:338	arg1	a 155-kDa glycoprotein	a 155-kDa glycoprotein				Fterm		glycoprotein			CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
12527193	0	34	gly	linked	51:56	arg2	protein AND Mammalian Crumbs3	protein			Mammalian Crumbs3	Fterm		protein			Mammalian Crumbs3 is a small transmembrane protein linked to protein associated with Lin-7 (Pals1).
32155444	6	20	part_of	S	1052:1052	arg1	conserved S epitopes	S		conserved S epitopes		Cterm	Site	S	43740568	epitopes	Finally, we demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination.
19508227	2	15	gly	glycosylation	346:358	arg2	two distinct glycosylation sites			two distinct glycosylation sites						sites	Its most abundant form contained only mannose-rich sugar chains but two distinct glycosylation sites could also contain complex carbohydrates.
19508227	2	4	gly	contain	377:383	arg1	two distinct glycosylation sites AND complex carbohydrates			two distinct glycosylation sites	complex carbohydrates					sites	Its most abundant form contained only mannose-rich sugar chains but two distinct glycosylation sites could also contain complex carbohydrates.
26271046	3	95	gly	GluA2	669:673	arg1	N-linked glycans	GluA2			N-linked glycans	PUBTATOR		GluA2	2891		To date, a unique trisaccharide (HSO3-3GlcAβ1-3Galβ1-4GlcNAc), human natural killer-1 (HNK-1) carbohydrate, was found expressed specifically on N-linked glycans of GluA2 and regulated the cell surface expression of AMPAR and the spine maturation process.
12151713	5	4	part_of	lactoferrin	666:676	arg1	both N-glycosylation sites	lactoferrin		both N-glycosylation sites		OGER	Site	lactoferrin	P02788	sites	The results indicated that both N-glycosylation sites of recombinant lactoferrin are mainly substituted by typical plant paucimannose-type glycans, with beta1,2-xylose and alpha1,3-linked fucose at the proximal N-acetylglucosamine, and that complex-type glycans with Lewis(a) determinants are not present in maize recombinant lactoferrin.
14760718	0	10	gly	N-glycosylated	14:27	arg1	N-glycosylated proteins	N-glycosylated proteins				Fterm		proteins			Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.
3571235	5	26	part_of	C	741:741	arg1	the hydrophobic domain	glycophorin C		the hydrophobic domain		PUBTATOR	Site	glycophorin C	2995	domain	The amino acid sequence of the hydrophobic domain (residues 49-88) of glycophorin C, that was also determined, agreed completely with the structure recently deduced from cDNA sequencing.
3571235	5	26	part_of	C	741:741	arg1	residues 49-88	glycophorin C		residues 49-88		PUBTATOR	SpecificSite	glycophorin C	2995	residues 49-88	The amino acid sequence of the hydrophobic domain (residues 49-88) of glycophorin C, that was also determined, agreed completely with the structure recently deduced from cDNA sequencing.
7538124	6	47	part_of	serines	1022:1028	arg1	K18	K18		serines		PUBTATOR	AminoAcid	K18	3875	serines	The identified sites occur on three serines in the head domain of K18.
7538124	6	84	part_of	K18	1052:1054	arg1	the head domain	K18		the head domain		PUBTATOR	Site	K18	3875	domain	The identified sites occur on three serines in the head domain of K18.
7780197	5	6	gly	contains	794:801	arg1	the Asn-727 site AND high-mannose or Endo-H-sensitive hybrid oligosaccharides			the Asn-727 site	high-mannose or Endo-H-sensitive hybrid oligosaccharides					Asn-727 site	These studies suggested that the Asn-727 site contains high-mannose or Endo-H-sensitive hybrid oligosaccharides.
28402104	5	2	gly	glycosylated	956:967	arg1	the predicted glycosylation sites			the predicted glycosylation sites						sites	Further analysis revealed that green cone opsin exists as a dimer in both dark (inactive) and bleached (active) states, and that the predicted glycosylation sites at N32 and N34 are indeed glycosylated.
28402104	5	89	gly	glycosylation	910:922	arg2	the predicted glycosylation sites			the predicted glycosylation sites						sites	Further analysis revealed that green cone opsin exists as a dimer in both dark (inactive) and bleached (active) states, and that the predicted glycosylation sites at N32 and N34 are indeed glycosylated.
28402104	5	89	gly	glycosylation	910:922	arg2	N32			N32 and N34						N32 and N34	Further analysis revealed that green cone opsin exists as a dimer in both dark (inactive) and bleached (active) states, and that the predicted glycosylation sites at N32 and N34 are indeed glycosylated.
14699159	9	69	gly	glycosylation	1805:1817	arg1	p90ATF6	p90ATF6				Cterm		p90ATF6	22926		Because accumulation of underglycosylated proteins in the ER is a potent inducer for the UPR, these studies uncover a novel mechanism whereby the glycosylation status of p90ATF6 can serve as a sensor for ER homeostasis, resulting in ATF6 activation to trigger the UPR.
14699159	9	80	gly	underglycosylated	1683:1699	arg1	underglycosylated proteins	underglycosylated proteins				Fterm		proteins			Because accumulation of underglycosylated proteins in the ER is a potent inducer for the UPR, these studies uncover a novel mechanism whereby the glycosylation status of p90ATF6 can serve as a sensor for ER homeostasis, resulting in ATF6 activation to trigger the UPR.
2277032	2	9	gly	glycoprotein	391:402	arg1	The enzyme	The enzyme				Fterm		enzyme			The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule.
2277032	2	9	gly	glycoprotein	391:402	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule.
2277032	2	51	gly	containing	405:414	arg1	The enzyme AND 10 mannose	The enzyme			10 mannose	Fterm		enzyme			The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule.
2277032	2	51	gly	containing	405:414	arg1	The enzyme AND 2 sialic acid residues	The enzyme			2 sialic acid residues	Fterm		enzyme			The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule.
2277032	2	51	gly	containing	405:414	arg1	The enzyme AND 1 fucose	The enzyme			1 fucose	Fterm		enzyme			The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule.
2277032	2	51	gly	containing	405:414	arg1	The enzyme AND 7 galactose	The enzyme			7 galactose	Fterm		enzyme			The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule.
2277032	2	51	gly	containing	405:414	arg1	The enzyme AND 6 glucosamine	The enzyme			6 glucosamine	Fterm		enzyme			The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule.
2277032	2	51	gly	containing	405:414	arg1	a glycoprotein AND 10 mannose	a glycoprotein			10 mannose	Fterm		glycoprotein			The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule.
2277032	2	51	gly	containing	405:414	arg1	a glycoprotein AND 2 sialic acid residues	a glycoprotein			2 sialic acid residues	Fterm		glycoprotein			The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule.
2277032	2	51	gly	containing	405:414	arg1	a glycoprotein AND 1 fucose	a glycoprotein			1 fucose	Fterm		glycoprotein			The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule.
2277032	2	51	gly	containing	405:414	arg1	a glycoprotein AND 7 galactose	a glycoprotein			7 galactose	Fterm		glycoprotein			The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule.
2277032	2	51	gly	containing	405:414	arg1	a glycoprotein AND 6 glucosamine	a glycoprotein			6 glucosamine	Fterm		glycoprotein			The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule.
26902720	3	18	gly	glycoprotein	475:486	arg1	a glycoprotein afamin	a glycoprotein afamin				Fterm		glycoprotein			We purified N-terminally tagged recombinant Wnt3a secreted from cells and accidentally discovered that Wnt3a co-purified with a glycoprotein afamin derived from the bovine serum included in the media.
7629073	7	11	part_of	enzyme	926:931	arg1	the catalytic domain	enzyme		the catalytic domain		Fterm	Site	enzyme		domain	Their overlapping sequences (from amino acid 152) are identical, except for three point mutations that result in three amino acid differences in the catalytic domain of the enzyme (Thr411, Leu468, and Ser592 in clone 4 to Met411, Phe468, and Phe592 in clone 16, respectively).
7629073	7	34	part_of	Thr411	934:939	arg1	clone 4	clone 4		Thr411		PUBTATOR	AminoAcid	clone 4	22116	Thr411, Leu468, and Ser592	Their overlapping sequences (from amino acid 152) are identical, except for three point mutations that result in three amino acid differences in the catalytic domain of the enzyme (Thr411, Leu468, and Ser592 in clone 4 to Met411, Phe468, and Phe592 in clone 16, respectively).
7629073	7	37	part_of	Leu468	942:947	arg1	clone 4	clone 4		Leu468		PUBTATOR	AminoAcid	clone 4	22116	Thr411, Leu468, and Ser592	Their overlapping sequences (from amino acid 152) are identical, except for three point mutations that result in three amino acid differences in the catalytic domain of the enzyme (Thr411, Leu468, and Ser592 in clone 4 to Met411, Phe468, and Phe592 in clone 16, respectively).
7629073	7	100	part_of	Ser592	954:959	arg1	clone 4	clone 4		Ser592		PUBTATOR	AminoAcid	clone 4	22116	Thr411, Leu468, and Ser592	Their overlapping sequences (from amino acid 152) are identical, except for three point mutations that result in three amino acid differences in the catalytic domain of the enzyme (Thr411, Leu468, and Ser592 in clone 4 to Met411, Phe468, and Phe592 in clone 16, respectively).
16622833	1	46	gly	glycoprotein	140:151	arg1	a well-known glycoprotein	a well-known glycoprotein				Fterm		glycoprotein			Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	1	46	gly	glycoprotein	140:151	arg1	Human alpha1-antitrypsin	Human alpha1-antitrypsin				PUBTATOR		Human alpha1-antitrypsin	5265		Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
10207176	3	32	part_of	IL-12	433:437	arg1	C-terminal peptides	IL-12		C-terminal peptides		OGER	Site	IL-12		peptides	Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319beta is (partially) C-mannosylated.
10206894	1	11	gly	Zn-alpha2-glycoprotein	81:102	arg1	a soluble protein	a soluble protein				Fterm		protein			Zn-alpha2-glycoprotein (ZAG) is a soluble protein that is present in serum and other body fluids.
10206894	1	11	gly	Zn-alpha2-glycoprotein	81:102	arg1	ZAG	ZAG				PUBTATOR		ZAG	563		Zn-alpha2-glycoprotein (ZAG) is a soluble protein that is present in serum and other body fluids.
10206894	1	11	gly	Zn-alpha2-glycoprotein	81:102	arg1	Zn-alpha2-glycoprotein	Zn-alpha2-glycoprotein				PUBTATOR		Zn-alpha2-glycoprotein	563		Zn-alpha2-glycoprotein (ZAG) is a soluble protein that is present in serum and other body fluids.
19299457	12	83	part_of	TSHR	1753:1756	arg1	the TSHR leucine-rich domain	TSHR		the TSHR leucine-rich domain		PUBTATOR	Site	TSHR	25360	domain	In summary, the present data indicate that the discontinuous epitope of CS-17, a TSHR inverse agonist and TSH antagonist, includes a component in the hinge region as well as the convex surface of the TSHR leucine-rich domain.
18420935	4	31	part_of	TLR3-ECD	711:718	arg1	the two TLR3-ECD C-terminal domains	TLR3		the two TLR3-ECD C-terminal domains		PUBTATOR	Site	TLR3	142980	domains	Each TLR3-ECD binds dsRNA at two sites located at opposite ends of the TLR3 horseshoe, and an intermolecular contact between the two TLR3-ECD C-terminal domains coordinates and stabilizes the dimer.
15152093	0	52	gly	N-glycosylation	22:36	arg2	the N-glycosylation sites			the N-glycosylation sites						sites	Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity.
12408961	3	44	part_of	protein	394:400	arg1	protein sequences	protein		protein sequences		Fterm	Site	protein		sequences	The predicted human and mouse protein sequences exhibit 35% identity with CREG protein.
14711516	4	4	gly	N-glycosylation	752:766	arg1	recombinant chicken Thy-1	Thy-1		site		PUBTATOR		Thy-1	P04216	site	The disulfide linkage pattern and glycoform distribution on each N-glycosylation site of recombinant chicken Thy-1 from both cell lines were determined by a combination of amino-terminal sequencing and mass spectrometry.
7681597	4	12	gly	glycopeptides	691:703	arg2	the glycopeptides			the glycopeptides						glycopeptides	The Tn antigenicity, as assayed by the binding to a monoclonal anti-Tn antibody (MLS 128), was found exclusively in the glycopeptides including three (cluster I) or four (cluster II) consecutive residues of GalNAc-Ser/Thr, whereas the glycopeptide (GPA-2) containing two nonconsecutive GalNAc-Ser/Thr residues had practically no Tn antigenicity.
7681597	4	21	gly	glycopeptide	806:817	arg2	the glycopeptide			the glycopeptide						glycopeptide	The Tn antigenicity, as assayed by the binding to a monoclonal anti-Tn antibody (MLS 128), was found exclusively in the glycopeptides including three (cluster I) or four (cluster II) consecutive residues of GalNAc-Ser/Thr, whereas the glycopeptide (GPA-2) containing two nonconsecutive GalNAc-Ser/Thr residues had practically no Tn antigenicity.
7681597	4	48	gly	three	715:719	arg1	consecutive residues			consecutive residues						residues	The Tn antigenicity, as assayed by the binding to a monoclonal anti-Tn antibody (MLS 128), was found exclusively in the glycopeptides including three (cluster I) or four (cluster II) consecutive residues of GalNAc-Ser/Thr, whereas the glycopeptide (GPA-2) containing two nonconsecutive GalNAc-Ser/Thr residues had practically no Tn antigenicity.
7681597	4	25	gly	containing	827:836	arg1	GPA-2 AND two nonconsecutive GalNAc-Ser/Thr residues	GPA-2		glycopeptide	two nonconsecutive GalNAc-Ser/Thr residues	OGER		GPA-2	P02724	glycopeptide	The Tn antigenicity, as assayed by the binding to a monoclonal anti-Tn antibody (MLS 128), was found exclusively in the glycopeptides including three (cluster I) or four (cluster II) consecutive residues of GalNAc-Ser/Thr, whereas the glycopeptide (GPA-2) containing two nonconsecutive GalNAc-Ser/Thr residues had practically no Tn antigenicity.
9118998	2	75	part_of	contains	507:514	arg1	The protein AND 36 cysteine residues	The protein		36 cysteine residues		Fterm	AminoAcid	protein		cysteine residues	The protein contains 36 cysteine residues arranged in six epidermal-growth-factor-like domains.
9449027	11	38	gly	sialylation	2592:2602	arg1	both N- and O-linked antennae				both N- and O-linked antennae						For hCG from individual diabetic pregnancy, the principal N-linked structure (34.7%) was consistent with a biantennary oligosaccharide previously reported only in carcinoma; and sialylation of both N- and O-linked antennae was significantly decreased compared to that of normal pregnancy.
8615697	1	102	gly	glycosylation	246:258	arg2	20 putative N-linked glycosylation sites			20 putative N-linked glycosylation sites						sites	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
22688517	6	24	gly	glycosylation	1145:1157	arg1	recombinant human LOX-1	LOX-1		site		PUBTATOR		LOX-1	4973	site	With this approach, one potential glycosylation site of recombinant human LOX-1 on Asn(139) is readily identified and found to carry heterogeneous complex type N-glycans.
22688517	6	30	gly	carry	1238:1242	arg1	recombinant human LOX-1 AND heterogeneous complex type N-glycans	LOX-1		site	heterogeneous complex type N-glycans	PUBTATOR		LOX-1	4973	site	With this approach, one potential glycosylation site of recombinant human LOX-1 on Asn(139) is readily identified and found to carry heterogeneous complex type N-glycans.
19571171	8	71	gly	misglycosylated	1592:1606	arg1	misglycosylated enzyme	misglycosylated enzyme				Fterm		enzyme			Altered trafficking of mutants may be associated with the mechanisms by which misglycosylated enzyme is degraded.
26146185	6	43	part_of	sites	733:737	arg1	CD166	CD166		sites		PUBTATOR	Site	CD166	214	sites	We characterized the binding sites on CD6 and CD166 and showed that a SNP in CD6 causes glycosylation that hinders the CD6/CD166 interaction.
26146185	6	43	part_of	sites	733:737	arg1	CD6	CD6		sites		PUBTATOR	Site	CD6	923	sites	We characterized the binding sites on CD6 and CD166 and showed that a SNP in CD6 causes glycosylation that hinders the CD6/CD166 interaction.
17956937	1	105	gly	antigen	225:231	arg1	The oligosaccharide structures	prostate specific antigen			The oligosaccharide structures	OGER		prostate specific antigen	P07288		The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
10731668	2	38	gly	attached	405:412	arg2	an atypical N-glycosylation consensus sequence AND one oligosaccharide chain			an atypical N-glycosylation consensus sequence	one oligosaccharide chain					sequence	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	32	gly	contains	370:377	arg1	the CHO sEGFR AND one oligosaccharide chain	the CHO sEGFR			one oligosaccharide chain	PUBTATOR		CHO sEGFR	P00533		We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
30237853	7	82	gly	O-glycopeptides	1297:1311	arg2	O-glycopeptides			O-glycopeptides						O-glycopeptides	The isolated N- and O-glycopeptides were detected and quantified using high resolution mass spectrometry.
27599734	4	52	part_of	NAG-W-NAG	722:730	arg1	stacked residues	NAG		stacked residues		OGER	Site	NAG	P54802	residues	The characteristic structural features of IFNγR2 are concentrated in its N-terminal domain: an extensive π-cation motif of stacked residues KWRWRH, a NAG-W-NAG sandwich (where NAG stands for N-acetyl-D-glucosamine) and finally a helix formed by residues 78-85, which is unique among class 2 receptors.
21980294	5	59	part_of	nectin-1	589:596	arg1	the first Ig-domain	nectin-1		the first Ig-domain		PUBTATOR	Site	nectin-1	Q15223	Ig-domain	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
15454184	8	62	gly	glycopeptides	1163:1175	arg2	the glycopeptides			the glycopeptides						glycopeptides	Site-specific glycosylation was deduced on the basis of the mass spectra of the glycopeptides.
9405696	3	2	gly	glycosylated	536:547	arg1	BCNG-1	BCNG-1				PUBTATOR		BCNG-1	15165		BCNG-1 is expressed exclusively in the brain, as a glycosylated protein of approximately 132 kDa.
9405696	3	2	gly	glycosylated	536:547	arg1	a glycosylated protein	a glycosylated protein				Fterm		protein			BCNG-1 is expressed exclusively in the brain, as a glycosylated protein of approximately 132 kDa.
3342889	4	60	gly	glycosylated	428:439	arg1	a proteolytic fragment			a proteolytic fragment						fragment	The glycosylated mini chain is a proteolytic fragment of the propeptide of cathepsin H. Human cathepsin L has 217 amino acid residues and an Mr of 23720.
7841792	0	15	gly	glycopeptide	63:74	arg2	a glycopeptide			a glycopeptide						glycopeptide	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
7841792	0	61	gly	glycosylated	29:40	arg1	a single glycosylated asparagine site			a single glycosylated asparagine site						asparagine site	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
8702538	8	96	gly	glycoprotein	1372:1383	arg1	myelin-associated glycoprotein	myelin-associated glycoprotein				OGER		myelin-associated glycoprotein	P20916		Site-directed mutagenesis of similar NC(T/S) motifs in the first or second Ig domains of the I-type lectins myelin-associated glycoprotein, and sialoadhesin did not disrupt their ability to mediate sialic acid binding.
8615697	6	80	gly	glycopeptides	828:840	arg2	the recovered glycopeptides			the recovered glycopeptides						glycopeptides	Each of the recovered glycopeptides contained a consensus sequence for N-linked glycosylation.
7947762	4	25	gly	attachment	678:687	arg1	a C-position AND a hexose residue			a C-position	a hexose residue					position	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
12743029	0	40	part_of	CUB1-EGF-CUB2	25:37	arg1	the CUB1-EGF-CUB2 region	EGF		the CUB1-EGF-CUB2 region		PUBTATOR	Site	EGF	1950	region	Crystal structure of the CUB1-EGF-CUB2 region of mannose-binding protein associated serine protease-2.
18657508	4	7	part_of	SIRPgamma	730:738	arg1	the N-terminal domains	SIRPgamma		the N-terminal domains		PUBTATOR	Site	SIRPgamma	55423	domains	We have also determined structures of the N-terminal domains of SIRPbeta, SIRPbeta(2), and SIRPgamma; proteins that are closely related to SIRPalpha but bind CD47 with negligible or reduced affinity.
4055801	9	40	part_of	C9b	1179:1181	arg1	The C9a and C9b polypeptide regions	C9b		The C9a and C9b polypeptide regions		Cterm	Site	C9b		regions	The C9a and C9b polypeptide regions have been mapped on poly(C9) by immunoelectron microscopy.
4055801	9	56	part_of	polypeptide	1183:1193	arg1	The C9a and C9b polypeptide regions	polypeptide		The C9a and C9b polypeptide regions		Fterm	Site	polypeptide		regions	The C9a and C9b polypeptide regions have been mapped on poly(C9) by immunoelectron microscopy.
23756651	2	21	part_of	RNF43	357:361	arg1	RNF43 ectodomains	RNF43		RNF43 ectodomains		PUBTATOR	Site	RNF43	54894	ectodomains	The structure of RSPO1 bound to both LGR5 and RNF43 ectodomains confirms their physical linkage.
19506079	6	10	part_of	sites	813:817	arg1	CaMKIV	CaMKIV		sites		PUBTATOR	Site	CaMKIV	814	sites	Furthermore, we identify at least five sites of GlcNAcylation on CaMKIV.
25374123	4	6	gly	N-glycopeptides	780:794	arg2	tryptic N-glycopeptides			tryptic N-glycopeptides						N-glycopeptides	Vitronectin was purified with immunoprecipitation by monoclonal antibody from plasma and digested to tryptic N-glycopeptides.
27314333	7	69	part_of	Rspo2	1281:1285	arg1	Rspo2 N-glycosylation site	Rspo2		Rspo2 N-glycosylation site		PUBTATOR	Site	Rspo2	340419	site	Similar effect can be observed in the N137 Rspo1 or Rspo3 mutant engineered with Rspo2 N-glycosylation site.
21615908	4	34	part_of	2.5-kbp	550:556	arg1	A 2.5-kbp genomic sequence fragment	kbp		A 2.5-kbp genomic sequence fragment		OGER	Site	kbp	Q6ZPU9	fragment	A 2.5-kbp genomic sequence fragment upstream of the coding sequence is sufficient to drive and regulate fibin expression through stimulation by glucocorticoids, activators of the protein kinase C signalling pathways and manganese ions.
9118998	4	22	gly	glycosylations	711:724	arg2	all C-terminal peptides			all C-terminal peptides						peptides	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	83	gly	glycosylation	876:888	arg1	Thr244			Thr244						Thr244	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	22	gly	glycosylations	711:724	arg2	Thr244			residues Thr235, Thr244 and Thr248						residues Thr235, Thr244 and Thr248	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	22	gly	glycosylations	711:724	arg2	Thr248			residues Thr235, Thr244 and Thr248						residues Thr235, Thr244 and Thr248	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	22	gly	glycosylations	711:724	arg2	Thr235			residues Thr235, Thr244 and Thr248						residues Thr235, Thr244 and Thr248	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	22	gly	glycosylations	711:724	arg2	Thr248			residues Thr235, Thr244 and Thr248						residues Thr235, Thr244 and Thr248	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	22	gly	glycosylations	711:724	arg2	Thr235			residues Thr235, Thr244 and Thr248						residues Thr235, Thr244 and Thr248	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	22	gly	glycosylations	711:724	arg2	Thr235			residues Thr235, Thr244 and Thr248						residues Thr235, Thr244 and Thr248	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	25	gly	residues	831:838	arg1	residues Thr235, Thr244 and Thr248			residues Thr235, Thr244 and Thr248						residues Thr235, Thr244 and Thr248	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	25	gly	residues	831:838	arg1	Thr244			residues Thr235, Thr244 and Thr248						residues Thr235, Thr244 and Thr248	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	25	gly	residues	831:838	arg1	Thr235			residues Thr235, Thr244 and Thr248						residues Thr235, Thr244 and Thr248	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	25	gly	residues	831:838	arg1	Thr244			residues Thr235, Thr244 and Thr248						residues Thr235, Thr244 and Thr248	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	25	gly	residues	831:838	arg1	Thr235			residues Thr235, Thr244 and Thr248						residues Thr235, Thr244 and Thr248	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
9118998	4	25	gly	residues	831:838	arg1	Thr235			residues Thr235, Thr244 and Thr248						residues Thr235, Thr244 and Thr248	O-linked glycosylations of the NeuNAc alpha2-3Gal beta1-3(NeuNAc alpha2-6)GalNAc type were present on all C-terminal peptides at residues Thr235, Thr244 and Thr248, although glycosylation on Thr244 was only partial.
12731890	3	64	gly	glycosylated	638:649	arg1	the sites			the sites						sites	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	50	gly	glycosylated	564:575	arg1	the naturally expressed human EGF receptor	EGF receptor		sites		PUBTATOR		EGF receptor	1956	sites	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	50	gly	glycosylated	564:575	arg2	the 11 canonical sites			sites						sites	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	50	gly	glycosylated	564:575	arg2	the 11 canonical sites	EGF receptor		sites		PUBTATOR		EGF receptor	1956	sites	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12151713	1	6	gly	glycoproteins	205:217	arg1	recombinant glycoproteins	recombinant glycoproteins				Fterm		glycoproteins			In order to determine the N-glycosylation potential of maize, a monocotyledon expression system for the production of recombinant glycoproteins, human lactoferrin was used as a model.
17768338	2	38	gly	glycoprotein	230:241	arg1	a 340 kDa tetrameric glycoprotein	a 340 kDa tetrameric glycoprotein				Fterm		glycoprotein			BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	38	gly	glycoprotein	230:241	arg1	BChE	BChE				PUBTATOR		BChE	590		BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
19167329	6	11	gly	glycosylation	934:946	arg1	a carboxyl-terminal glycosylation site			a carboxyl-terminal glycosylation site						site	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
19167329	6	24	gly	glycosylation	971:983	arg2	a carboxyl-terminal glycosylation site			a carboxyl-terminal glycosylation site						site	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
3179269	1	60	gly	erythropoietin	165:178	arg1	the N-linked oligosaccharides	erythropoietin			the N-linked oligosaccharides	PUBTATOR		erythropoietin	2056		The structures of the N-linked oligosaccharides of the urinary erythropoietin (u-EPO) purified from urine of aplastic anemic patients were analyzed and compared with those for recombinant erythropoietin (r-EPO) prepared with baby hamster kidney (BHK) cells.
14769026	11	92	gly	glycosylation	1582:1594	arg1	the predicted stalk region			the predicted stalk region						region	In addition, O-linked glycosylation is observed in the predicted stalk region of NL1, prior to the transmembrane spanning domain.
27966990	6	52	gly	N-glycosylation	1076:1090	arg2	at least one occupied N-glycosylation site			at least one occupied N-glycosylation site						site	The data demonstrated that all seven VEGFR-2 immunoglobulin-like domains have at least one occupied N-glycosylation site.
8357534	3	10	gly	site	527:530	arg1	the carbohydrate structures			site	the carbohydrate structures					site	Analysis of a minor form of elastase (E-1) and cathepsin G (C-1) indicates that the carbohydrate structures at each glycosylation site are complex-type bi-antennary chains usually associated with secretory glycoproteins.
8357534	3	10	gly	site	527:530	arg1	complex-type bi-antennary chains			site	complex-type bi-antennary chains					site	Analysis of a minor form of elastase (E-1) and cathepsin G (C-1) indicates that the carbohydrate structures at each glycosylation site are complex-type bi-antennary chains usually associated with secretory glycoproteins.
8357534	3	23	gly	glycosylation	513:525	arg2	each glycosylation site			each glycosylation site						site	Analysis of a minor form of elastase (E-1) and cathepsin G (C-1) indicates that the carbohydrate structures at each glycosylation site are complex-type bi-antennary chains usually associated with secretory glycoproteins.
8357534	3	50	gly	glycoproteins	603:615	arg1	secretory glycoproteins	secretory glycoproteins				Fterm		glycoproteins			Analysis of a minor form of elastase (E-1) and cathepsin G (C-1) indicates that the carbohydrate structures at each glycosylation site are complex-type bi-antennary chains usually associated with secretory glycoproteins.
7574684	6	47	gly	glycosylated	1061:1072	arg1	10 sites			10 sites						sites	Among 12 potential N-linked glycosylation sites proposed in the soluble domain of trkB, 10 sites are actually glycosylated.
7574684	6	51	gly	glycosylation	979:991	arg2	12 potential N-linked glycosylation sites			12 potential N-linked glycosylation sites						sites	Among 12 potential N-linked glycosylation sites proposed in the soluble domain of trkB, 10 sites are actually glycosylated.
10066782	9	52	gly	N-glycosylation	1415:1429	arg2	the four potential N-glycosylation sites			the four potential N-glycosylation sites						sites	Of the four potential N-glycosylation sites, carbohydrate moieties were identified on Asn36, Asn74, and Asn202, but not on Asn226.
15173186	9	9	gly	glycosylation	1339:1351	arg2	consensus glycosylation sites			consensus glycosylation sites						sites	We have also analyzed where consensus glycosylation sites are located in the extracellular domains of other human Toll-like receptors.
18308854	5	13	gly	glycosylation	930:942	arg2	glycosylation sites			glycosylation sites						sites	To map glycosylation sites, the asparagines at the each of the four N-linked glycosylation consensus sites were mutagenized to glutamines.
18308854	5	39	gly	glycosylation	1000:1012	arg2	the four N-linked glycosylation consensus sites			the four N-linked glycosylation consensus sites						sites	To map glycosylation sites, the asparagines at the each of the four N-linked glycosylation consensus sites were mutagenized to glutamines.
9822688	7	42	gly	occupied	867:874	arg2	The lid domain			The lid domain						domain	The lid domain occupied the closed position, suggesting that rPLRP2 should show interfacial activation.
3567160	10	20	gly	oligosaccharide	1686:1700	arg1	this paraprotein	paraprotein			oligosaccharide	Fterm		paraprotein			It is of particular interest that in this paraprotein the major component is a biantennary complex-type oligosaccharide that lacks a fucose residue and an oligosaccharide with the structure (Formula: see text) exists as one of the most abundant components.
10978165	5	10	part_of	HCC-1	522:526	arg1	two distinct HCC-1 peptides	HCC-1		two distinct HCC-1 peptides		PUBTATOR	Site	HCC-1	6358	peptides	Western blot analysis of human plasma extracts revealed a HCC-1 immunoreactive double band at 8-10 kDa indicating the presence of two distinct HCC-1 peptides.
11226831	1	2	gly	found	139:143	arg1	nuclear and cytoplasmic proteins AND O-linked N-acetylglucosamine	nuclear and cytoplasmic proteins			O-linked N-acetylglucosamine	Fterm		proteins			O-linked N-acetylglucosamine (O-GlcNAc) is a highly dynamic and abundant modification found on nuclear and cytoplasmic proteins of nearly all eukaryotes.
8615697	13	39	part_of	hTG	2262:2264	arg1	the 20 putative sites	hTG		the 20 putative sites		OGER	Site	hTG	P01266	sites	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	13	64	part_of	residues	2281:2288	arg1	hTG	hTG		residues		OGER	SpecificSite	hTG	P01266	asparagine residues 91, 477, 1849, and 2102	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
21550978	7	38	part_of	hPAR	1516:1519	arg1	Asn(250)	hPAR(1)		Asn(250)		PUBTATOR	SpecificSite	hPAR(1)	2149	Asn(250)	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
14573609	5	2	gly	glycosylation	697:709	arg1	heparanase	heparanase				PUBTATOR		heparanase	10855		Treatment with a glycosylation inhibitor demonstrated that glycosylation was not required for the activity of heparanase.
3542989	1	28	part_of	cholinesterase	108:121	arg1	The complete amino acid sequence	cholinesterase		The complete amino acid sequence		PUBTATOR	Site	cholinesterase	534616	sequence	The complete amino acid sequence of human serum cholinesterase (choline esterase II (unspecific), EC 3.1.1.8) was determined by Edman degradation of purified peptides.
7654718	9	90	gly	chains	1381:1386	arg1	the C-tail region			the C-tail region	the C-tail region		Site			region	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
9054441	3	68	gly	contain	308:314	arg1	Thr-345 AND only an O-linked oligosaccharide	Plasminogen 2		Thr-345	only an O-linked oligosaccharide	OGER		Plasminogen 2	P00747	Thr-345	Plasminogen 2 is known to contain only an O-linked oligosaccharide at Thr-345.
7929098	6	15	part_of	terminus	1033:1040	arg1	a tagged epitope	terminus		a tagged epitope						epitope	The C terminus was localized as intracellular based on antibody recognition and protease sensitivity of a tagged epitope at the C terminus.
8344278	4	25	gly	found	981:985	arg1	this saposin AND bisecting N-acetylglucosamine residues	this saposin			bisecting N-acetylglucosamine residues	Fterm		saposin			Saposin C contains (a) a predominance of oligomannose-type oligosaccharides and monoantennary oligosaccharides and (b) the presence of four different oligosaccharides having bisecting N-acetylglucosamine residues (found only in this saposin).
20622017	10	84	part_of	sites	1319:1323	arg1	renal GGT	GGT		sites		OGER	Site	GGT		sites	Two glycosylation sites on renal GGT were modified exclusively by neutral glycans.
12799386	10	20	gly	occupied	1372:1379	arg2	4/4 potential N-linkage sites			4/4 potential N-linkage sites						sites	The zona proteins are highly glycosylated and 4/4 potential N-linkage sites on ZP1, 6/6 on ZP2, and 5/6 on ZP3 are occupied.
12799386	10	78	gly	glycosylated	1286:1297	arg1	The zona proteins	The zona proteins				Fterm		proteins			The zona proteins are highly glycosylated and 4/4 potential N-linkage sites on ZP1, 6/6 on ZP2, and 5/6 on ZP3 are occupied.
30899004	6	1	gly	glycopeptides	1232:1244	arg2	intact glycopeptides			intact glycopeptides						glycopeptides	Moreover, we use this large-scale glycoproteomic dataset to develop several visualizations that will prove useful for analyzing intact glycopeptides in future studies.
23345538	6	23	part_of	proteins	1229:1236	arg1	131 glycopeptides	proteins		131 glycopeptides		Fterm	Site	proteins		glycopeptides	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
19556306	3	45	gly	TLR4	599:602	arg1	complex type N-glycans	TLR4			complex type N-glycans	PUBTATOR		TLR4	7099		Lectin blot and cell surface biotinylation revealed that TLR4 exhibited the 110 kDa protein with high mannose type N-glycans and the 130 kDa protein with complex type N-glycans and that only the 130 kDa TLR4 with complex type N-glycans was expressed on the cell surface.
19556306	3	64	gly	protein	537:543	arg1	complex type N-glycans	protein			complex type N-glycans	Fterm		protein			Lectin blot and cell surface biotinylation revealed that TLR4 exhibited the 110 kDa protein with high mannose type N-glycans and the 130 kDa protein with complex type N-glycans and that only the 130 kDa TLR4 with complex type N-glycans was expressed on the cell surface.
19556306	3	64	gly	protein	537:543	arg1	high mannose type N-glycans	protein			high mannose type N-glycans	Fterm		protein			Lectin blot and cell surface biotinylation revealed that TLR4 exhibited the 110 kDa protein with high mannose type N-glycans and the 130 kDa protein with complex type N-glycans and that only the 130 kDa TLR4 with complex type N-glycans was expressed on the cell surface.
19556306	3	70	gly	protein	480:486	arg1	complex type N-glycans	110 kDa protein			complex type N-glycans	OGER		110 kDa protein	Q9H1K0		Lectin blot and cell surface biotinylation revealed that TLR4 exhibited the 110 kDa protein with high mannose type N-glycans and the 130 kDa protein with complex type N-glycans and that only the 130 kDa TLR4 with complex type N-glycans was expressed on the cell surface.
19556306	3	70	gly	protein	480:486	arg1	high mannose type N-glycans	110 kDa protein			high mannose type N-glycans	OGER		110 kDa protein	Q9H1K0		Lectin blot and cell surface biotinylation revealed that TLR4 exhibited the 110 kDa protein with high mannose type N-glycans and the 130 kDa protein with complex type N-glycans and that only the 130 kDa TLR4 with complex type N-glycans was expressed on the cell surface.
19654028	3	42	gly	N-glycosylated	604:617	arg1	all six extracellular asparagines			all six extracellular asparagines						asparagines	Site-directed mutagenesis confirmed that all six extracellular asparagines are N-glycosylated and that the Ser/Thr/Pro cluster in the "stalk" domain juxtaposed to the cysteine-rich domains (CRDs) is a major site for the likely mucine-type of O-glycosylation.
3514617	13	37	gly	carbohydrates	2205:2217	arg1	the intact N protein	protein			carbohydrates	Fterm		protein			The much decreased levels of these carbohydrates in the intact N protein, corroborated the latter finding.
14970177	5	50	gly	glycosylated	1036:1047	arg1	glycosylated hIL-6	glycosylated hIL-6				OGER		hIL-6	P05231		As distinct from vIL-6, unglycosylated hIL-6 is as potent as glycosylated hIL-6 in stimulating B cell proliferation.
14970177	5	58	gly	unglycosylated	999:1012	arg1	unglycosylated hIL-6	unglycosylated hIL-6				OGER		hIL-6	P05231		As distinct from vIL-6, unglycosylated hIL-6 is as potent as glycosylated hIL-6 in stimulating B cell proliferation.
17040911	7	68	part_of	protease	1496:1503	arg1	the protease domain	protease		the protease domain		Fterm	Site	protease		domain	Site-directed mutagenesis demonstrated that no single glycan was essential for oligomer formation; however, the combined absence of the glycans at Asn-152 and Asn-270 in the protease domain hindered intersubunit disulfide bond formation, prevented noncovalent associations, and abolished enzymatic activity.
20813955	4	28	part_of	JAML	804:807	arg1	a JAML intracellular sequence motif	JAML		a JAML intracellular sequence motif		PUBTATOR	Site	JAML	120425	motif	Biochemical and mutagenesis studies illustrate how CAR-mediated clustering of JAML recruits phosphoinositide 3-kinase (P13K) to a JAML intracellular sequence motif as delineated for the alphabeta T cell costimulatory receptor CD28.
19556306	2	44	gly	TLR4	291:294	arg1	the N-glycan	TLR4			the N-glycan	PUBTATOR		TLR4	7099		The purposes of this study were to characterize the N-glycan of TLR4 and to investigate the roles of MD-2 in N-linked glycosylation and cell surface expression of TLR4.
19556306	2	66	gly	glycosylation	345:357	arg1	TLR4	TLR4				PUBTATOR		TLR4	7099		The purposes of this study were to characterize the N-glycan of TLR4 and to investigate the roles of MD-2 in N-linked glycosylation and cell surface expression of TLR4.
26620227	3	50	gly	glycosylation	455:467	arg2	this glycosylation site			this glycosylation site						site	The SNP causes an altered N-linked glycosylation modification at Asn129 of proSP-B, e.g. the C allele with this glycosylation site but not in the T allele.
1694115	0	40	gly	glycopeptide	20:31	arg2	glycopeptide			glycopeptide						glycopeptide	Unique structure of glycopeptide from alpha-fetoprotein produced in human hepatoma cell line, as determined by 1H-nuclear magnetic resonance spectroscopy.
28252640	2	41	part_of	BoNT/A1	419:425	arg1	the receptor-binding domain	BoNT		the receptor-binding domain		Cterm	Site	BoNT		domain	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	62	part_of	SV2C	492:495	arg1	the luminal domain	SV2C		the luminal domain		PUBTATOR	Site	SV2C	22987	domain	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
2842863	6	12	gly	glycosylation	966:978	arg2	potential glycosylation sites			potential glycosylation sites						sites, and proline residues	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
6833285	6	18	gly	linked	883:888	arg1	residue 6 AND a trisaccharide			residue 6	a trisaccharide					residue 6	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
6833285	6	18	gly	linked	883:888	arg1	serine AND a trisaccharide			serine	a trisaccharide					serine	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
6833285	6	18	gly	linked	883:888	arg2	residue 6 AND the carbohydrate unit			residue 6	the carbohydrate unit					residue 6	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
6833285	6	18	gly	linked	883:888	arg2	serine AND the carbohydrate unit			serine	the carbohydrate unit					serine	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
3497198	4	35	part_of	H-2Kb	676:680	arg1	Asn176	H-2Kb		Asn176		PUBTATOR	AminoAcid	H-2Kb	14972	Asn176	Asn176 of both H-2Kk and H-2Kb contained the same ratio (2.8 to 1) of bi- to monosialylated chains.
3497198	4	45	part_of	H-2Kk	666:670	arg1	Asn176	H-2Kk		Asn176		PUBTATOR	AminoAcid	H-2Kk	14972	Asn176	Asn176 of both H-2Kk and H-2Kb contained the same ratio (2.8 to 1) of bi- to monosialylated chains.
23744091	1	15	part_of	Fc	147:148	arg1	Fc region	Fc		Fc region		Cterm	Site	Fc		region	Engaging inhibitory FcγRIIb by Fc region has been recently reported to be an attractive approach for improving the efficacy of antibody therapeutics.
15807535	9	4	gly	glycosylated	1709:1720	arg1	glycosylated ABCG2	glycosylated ABCG2				PUBTATOR		ABCG2	Q9UNQ0		Furthermore, in crude membrane preparations, neither the basal nor the prazosin-stimulated ( approximately 2-fold) ATPase activities of ABCG2 (N596Q) were affected compared to glycosylated ABCG2.
22187327	2	7	gly	ICAM-5	309:314	arg1	the N-glycan structures	ICAM-5			the N-glycan structures	PUBTATOR		ICAM-5	15898		Although we have determined the N-glycan structures of ICAM-5 in a previous report, their function is unknown.
27294781	1	50	gly	glycosylated	376:387	arg1	glycosylated human SV2C	glycosylated human SV2C				PUBTATOR		SV2C	22987		Here we report a 2.0-Å-resolution crystal structure of the BoNT/A1 receptor-binding domain in complex with its neuronal receptor, glycosylated human SV2C.
27294781	1	50	gly	glycosylated	376:387	arg1	its neuronal receptor	its neuronal receptor				Fterm		receptor			Here we report a 2.0-Å-resolution crystal structure of the BoNT/A1 receptor-binding domain in complex with its neuronal receptor, glycosylated human SV2C.
27966990	5	0	gly	occupancy	895:903	arg2	N-glycosylation site occupancy			N-glycosylation site occupancy						site	The objectives of the present study were to characterize N-glycosylation sites in VEGFR-2 via enzymatic release of the glycans and concomitant incorporation of 18O into formerly N-glycosylated sites followed by tandem mass spectrometry (MS/MS) analysis to determine N-glycosylation site occupancy and the site-specific N-glycan heterogeneity of VEGFR-2 glycopeptides.
27966990	5	6	gly	N-glycosylation	665:679	arg2	N-glycosylation sites			N-glycosylation sites						sites	The objectives of the present study were to characterize N-glycosylation sites in VEGFR-2 via enzymatic release of the glycans and concomitant incorporation of 18O into formerly N-glycosylated sites followed by tandem mass spectrometry (MS/MS) analysis to determine N-glycosylation site occupancy and the site-specific N-glycan heterogeneity of VEGFR-2 glycopeptides.
27966990	5	9	gly	N-glycosylation	874:888	arg2	N-glycosylation site occupancy			N-glycosylation site occupancy						site	The objectives of the present study were to characterize N-glycosylation sites in VEGFR-2 via enzymatic release of the glycans and concomitant incorporation of 18O into formerly N-glycosylated sites followed by tandem mass spectrometry (MS/MS) analysis to determine N-glycosylation site occupancy and the site-specific N-glycan heterogeneity of VEGFR-2 glycopeptides.
27966990	5	68	gly	heterogeneity	936:948	arg1	VEGFR-2 glycopeptides			VEGFR-2 glycopeptides						glycopeptides	The objectives of the present study were to characterize N-glycosylation sites in VEGFR-2 via enzymatic release of the glycans and concomitant incorporation of 18O into formerly N-glycosylated sites followed by tandem mass spectrometry (MS/MS) analysis to determine N-glycosylation site occupancy and the site-specific N-glycan heterogeneity of VEGFR-2 glycopeptides.
27966990	5	79	gly	N-glycosylated	786:799	arg1	formerly N-glycosylated sites			formerly N-glycosylated sites						sites	The objectives of the present study were to characterize N-glycosylation sites in VEGFR-2 via enzymatic release of the glycans and concomitant incorporation of 18O into formerly N-glycosylated sites followed by tandem mass spectrometry (MS/MS) analysis to determine N-glycosylation site occupancy and the site-specific N-glycan heterogeneity of VEGFR-2 glycopeptides.
27966990	5	0	gly	occupancy	895:903	arg2	VEGFR-2 glycopeptides			glycopeptides						glycopeptides	The objectives of the present study were to characterize N-glycosylation sites in VEGFR-2 via enzymatic release of the glycans and concomitant incorporation of 18O into formerly N-glycosylated sites followed by tandem mass spectrometry (MS/MS) analysis to determine N-glycosylation site occupancy and the site-specific N-glycan heterogeneity of VEGFR-2 glycopeptides.
27966990	5	23	gly	glycopeptides	961:973	arg1	the site-specific N-glycan heterogeneity			glycopeptides	the site-specific N-glycan heterogeneity					glycopeptides	The objectives of the present study were to characterize N-glycosylation sites in VEGFR-2 via enzymatic release of the glycans and concomitant incorporation of 18O into formerly N-glycosylated sites followed by tandem mass spectrometry (MS/MS) analysis to determine N-glycosylation site occupancy and the site-specific N-glycan heterogeneity of VEGFR-2 glycopeptides.
10383441	1	17	part_of	protein	407:413	arg1	positions 27 and 74	protein		positions 27 and 74		Fterm	Site	protein		positions 27 and 74	We have reported that bovine DNase I, a secretory glycoprotein, acquires mannose 6-phosphate residues on 12.6% of its Asn-linked oligosaccharides when expressed in COS-1 cells and that the extent of phosphorylation increases to 79.2% when lysines are placed at positions 27 and 74 of the mature protein (Nishikawa, A., Gregory, W. , Frenz, J., Cacia, J., and Kornfeld, S. (1997) J. Biol.
27551080	0	0	part_of	NPC1	69:72	arg1	NPC1 middle lumenal domain	structure of NPC1		NPC1 middle lumenal domain		PUBTATOR	Site	structure of NPC1	4864	domain	Clues to the mechanism of cholesterol transfer from the structure of NPC1 middle lumenal domain bound to NPC2.
10995228	7	11	part_of	site	898:901	arg1	mER-beta	mER		site		PUBTATOR	Site	mER	13983	site	The major site of O-GlcNAc on mER-beta from Sf9 cells is Ser(16) near the N-terminus.
2808371	2	38	gly	containing	340:349	arg1	the proteolytic fragment AND the O-GlcNAc moiety			the proteolytic fragment	the O-GlcNAc moiety					fragment	We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase.
8262907	4	14	gly	located	816:822	arg2	Asn-122 AND A sugar chain			Asn-122	A sugar chain					Asn-122	A sugar chain was located only at Asn-122 of the two putative sites of N-glycosylation that were present per subunit.
8262907	4	48	gly	Asn-122	832:838	arg1	A sugar chain			Asn-122	A sugar chain					Asn-122	A sugar chain was located only at Asn-122 of the two putative sites of N-glycosylation that were present per subunit.
8262907	4	72	gly	N-glycosylation	869:883	arg2	the two putative sites			the two putative sites						sites	A sugar chain was located only at Asn-122 of the two putative sites of N-glycosylation that were present per subunit.
25092234	9	39	gly	glycosite	1266:1274	arg2	a new glycosite			a new glycosite						glycosite	We also identified a new glycosite of the noncanonical format NXC at N145 , occupied at around 5%.
3056714	2	27	gly	glycosylated	366:377	arg1	a heterogeneously glycosylated precursor	a heterogeneously glycosylated precursor				Fterm		precursor			The CT29-LAP was synthesized in BHK cells as a heterogeneously glycosylated precursor that was tightly membrane associated.
3056714	2	27	gly	glycosylated	366:377	arg1	The CT29-LAP	The CT29-LAP				PUBTATOR		CT29	57082		The CT29-LAP was synthesized in BHK cells as a heterogeneously glycosylated precursor that was tightly membrane associated.
10921916	7	31	gly	carbohydrate	1035:1046	arg1	CD45	CD45			carbohydrate	PUBTATOR		CD45	5788		The interaction between CD45 and GII is dependent on the active site of GII, is mediated through the carbohydrate on CD45, and can be inhibited with mannose.
12297049	0	51	part_of	receptor	57:64	arg1	a truncated epidermal growth factor receptor extracellular domain	epidermal growth factor receptor		a truncated epidermal growth factor receptor extracellular domain		PUBTATOR	Site	epidermal growth factor receptor	1956	domain	Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
9501084	1	47	part_of	BM-40	223:227	arg1	The extracellular calcium-binding domain	BM-40		The extracellular calcium-binding domain		PUBTATOR	Site	BM-40	6678	domain	The extracellular calcium-binding domain (positions 138-286) of the matrix protein BM-40 possesses a binding epitope of moderate affinity for several collagen types.
9501084	1	47	part_of	BM-40	223:227	arg1	positions 138-286	BM-40		positions 138-286		PUBTATOR	Site	BM-40	6678	positions 138	The extracellular calcium-binding domain (positions 138-286) of the matrix protein BM-40 possesses a binding epitope of moderate affinity for several collagen types.
9501084	1	57	part_of	possesses	229:237	arg1	the matrix protein BM-40 AND a binding epitope	BM-40		epitope		PUBTATOR	Site	BM-40	6678	epitope	The extracellular calcium-binding domain (positions 138-286) of the matrix protein BM-40 possesses a binding epitope of moderate affinity for several collagen types.
16107205	2	78	gly	glycosylation	521:533	arg2	a potential N-linked glycosylation site			a potential N-linked glycosylation site						site	A sequence comparison reveals some conserved characteristics: all the mammalian DNase X proteins have an N-terminal signal peptide, a potential N-linked glycosylation site and a C-terminal hydrophobic domain.
17015441	7	81	gly	glycosylation	1117:1129	arg2	The glycosylation site			The glycosylation site						site	The glycosylation site is flanked in the pore by two cysteine residues that we mutated, to prove that they are involved in a conserved double cysteine motif, which is essential for channel function.
17525160	5	52	part_of	hCTR1	579:583	arg1	the extracellular amino terminus	hCTR1		the extracellular amino terminus		PUBTATOR	Site	hCTR1	1317	terminus	We demonstrate that the extracellular amino terminus of hCTR1 also contains O-linked polysaccharides.
17956937	0	46	gly	antigen	50:56	arg1	Oligosaccharide profiles	prostate specific antigen			Oligosaccharide profiles	OGER		prostate specific antigen	P07288		Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	0	59	gly	glycopeptide	150:161	arg2	glycopeptide			glycopeptide						glycopeptide	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
16679516	0	25	part_of	thyroglobulin	73:85	arg1	Ser-2730	thyroglobulin		Ser-2730		OGER	SpecificSite	thyroglobulin	P01266	Ser-2730	A single chondroitin 6-sulfate oligosaccharide unit at Ser-2730 of human thyroglobulin enhances hormone formation and limits proteolytic accessibility at the carboxyl terminus.
8357534	4	44	gly	contain	715:721	arg1	the isoforms E-3 and C-3 AND exclusively truncated, oligomannose-type chains	isoforms		positions	exclusively truncated, oligomannose-type chains	Fterm		isoforms		positions	In contrast, the isoforms E-3 and C-3, the major forms of elastase and cathepsin G respectively, contain exclusively truncated, oligomannose-type chains at the same positions in the sequence of each protein.
8357534	4	44	gly	contain	715:721	arg1	C-3 AND exclusively truncated, oligomannose-type chains	E-3 and C-3		positions	exclusively truncated, oligomannose-type chains	PUBTATOR		E-3 and C-3	P01024	positions	In contrast, the isoforms E-3 and C-3, the major forms of elastase and cathepsin G respectively, contain exclusively truncated, oligomannose-type chains at the same positions in the sequence of each protein.
8357534	4	44	gly	contain	715:721	arg1	E-3 AND exclusively truncated, oligomannose-type chains	E-3 and C-3		positions	exclusively truncated, oligomannose-type chains	PUBTATOR		E-3 and C-3	P01024	positions	In contrast, the isoforms E-3 and C-3, the major forms of elastase and cathepsin G respectively, contain exclusively truncated, oligomannose-type chains at the same positions in the sequence of each protein.
8357534	4	44	gly	contain	715:721	arg1	E-3 AND exclusively truncated, oligomannose-type chains	E-3 and C-3		positions	exclusively truncated, oligomannose-type chains	PUBTATOR		E-3 and C-3	P01024	positions	In contrast, the isoforms E-3 and C-3, the major forms of elastase and cathepsin G respectively, contain exclusively truncated, oligomannose-type chains at the same positions in the sequence of each protein.
1150658	11	11	gly	found	2170:2174	arg2	residues 13, 30, 121, 127, 132, and 138 AND Oligosaccharide side chains			residues 13, 30, 121, 127, 132, and 138	Oligosaccharide side chains					residues 13, 30, 121, 127, 132, and 138	Oligosaccharide side chains are found at residues 13, 30, 121, 127, 132, and 138.
23376777	10	97	gly	glycosylation	1744:1756	arg1	KCC4	KCC4				PUBTATOR		KCC4	20499		We propose that glycosylation is essential for the surface expression, stabilization, and bioactivity of KCC4.
16037490	6	25	gly	O-glycosylation	1356:1370	arg2	another mucin-type O-glycosylation site			another mucin-type O-glycosylation site						site	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
8069634	4	71	gly	glycoprotein	748:759	arg1	the complete glycoprotein	the complete glycoprotein				Fterm		glycoprotein			While the structures of several lectins complexed with incomplete oligosaccharides have been solved, no previous structure has included the complete glycoprotein.
8798614	3	69	part_of	CD59	619:622	arg1	Asn18	CD59		Asn18		PUBTATOR	AminoAcid	CD59	966	Asn18	The deduced amino acid sequences of CD59 homologues identified in Old and New World primates as well as in rat reveal that the motif for N-linked glycosylation at the residue corresponding to Asn18 of human CD59 is invariably conserved, despite considerable sequence divergence elsewhere in the protein.
3877053	3	31	part_of	XIIa	345:348	arg1	regions	factor XIIa		regions		Cterm	Site	factor XIIa		regions	These oligonucleotides encoded regions of beta-factor XIIa as predicted from the amino acid sequence.
7599134	7	59	part_of	N-X-A	1303:1307	arg1	N-X-A consensus sequences	N-X-A		N-X-A consensus sequences		Cterm	Site	N-X-A		sequences	ATIIIs with N-X-S, N-X-T, and N-X-A consensus sequences were expressed in baculovirus-infected insect cells.
18234225	4	84	part_of	enzyme	787:792	arg1	both S1 and S1' sites	enzyme		both S1 and S1' sites		Fterm	Site	enzyme		sites	In this article, we have extended structural characterization of GCPII to its S1 site by using dipeptide-based inhibitors that interact with both S1 and S1' sites of the enzyme.
3038148	5	66	gly	N-glycosylation	1030:1044	arg2	two N-glycosylation sites			two N-glycosylation sites						sites	Moreover, the revised structure led (a) to the assignment of Arg, Asn, and Val residues instead of His, Asp, and Gly at positions 63, 165, and 169, respectively; (b) to the assignment of residues occupying an overlapping sequence at positions 165-171, and finally (c) to the localization of two N-glycosylation sites at positions 82 and 165.
3038148	5	34	gly	positions	1055:1063	arg1	82			positions 82 and 165						positions 82 and 165	Moreover, the revised structure led (a) to the assignment of Arg, Asn, and Val residues instead of His, Asp, and Gly at positions 63, 165, and 169, respectively; (b) to the assignment of residues occupying an overlapping sequence at positions 165-171, and finally (c) to the localization of two N-glycosylation sites at positions 82 and 165.
18420577	4	13	gly	O-GlcNAc	687:694	arg1	hepatic FoxO1	FoxO1			O-GlcNAc	PUBTATOR		FoxO1	2308		Here we show that O-GlcNAc on hepatic FoxO1 is increased in diabetes.
8672508	3	44	gly	modified	550:557	arg3	Nup214 AND O-linked N-acetylglucosamine	Nup214			O-linked N-acetylglucosamine	PUBTATOR		Nup214	8021		Nonmembrane nucleoporins Nup153, Nup214, and Nup358 that are modified by O-linked N-acetylglucosamine and recognized by a monoclonal antibody were phosphorylated throughout the cell cycle and hyperphosphorylated during M phase.
8672508	3	44	gly	modified	550:557	arg3	Nup358 AND O-linked N-acetylglucosamine	Nup358			O-linked N-acetylglucosamine	PUBTATOR		Nup358	5903		Nonmembrane nucleoporins Nup153, Nup214, and Nup358 that are modified by O-linked N-acetylglucosamine and recognized by a monoclonal antibody were phosphorylated throughout the cell cycle and hyperphosphorylated during M phase.
8672508	3	44	gly	modified	550:557	arg3	Nup153 AND O-linked N-acetylglucosamine	Nup153			O-linked N-acetylglucosamine	PUBTATOR		Nup153	9972		Nonmembrane nucleoporins Nup153, Nup214, and Nup358 that are modified by O-linked N-acetylglucosamine and recognized by a monoclonal antibody were phosphorylated throughout the cell cycle and hyperphosphorylated during M phase.
22988105	4	25	part_of	ectoprotein	729:739	arg1	a major fragment	ectoprotein		a major fragment		Fterm	Site	ectoprotein		fragment	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	4	60	part_of	sheddase	794:801	arg1	a major fragment	sheddase		a major fragment		Fterm	Site	sheddase		fragment	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
12659834	2	15	part_of	beta	510:513	arg1	An N-terminus sequence	interleukin 1 beta		An N-terminus sequence		PUBTATOR	Site	interleukin 1 beta	3553	sequence	An N-terminus sequence (Ser5-Ala28) of human interleukin 1 beta (hIL-1 beta) was used as synthetic prosequence of recombinant HBV surface antigen (pre-S), secreted from S. cerevisiae.
8336134	4	24	part_of	peptides	518:525	arg1	the sequence	peptides		the sequence						sequence	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
17980170	11	39	part_of	NAAA	1312:1315	arg1	N-glycosylation sites	NAAA		N-glycosylation sites		PUBTATOR	Site	NAAA	27163	sites	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
8942648	12	16	gly	monosialylated	1699:1712	arg1	the monosialylated and disialylated GalGalNAc-S/T structures				the monosialylated and disialylated GalGalNAc-S/T structures						The O-glycans are of the mucin type with the monosialylated and disialylated GalGalNAc-S/T structures predominating.
23878260	4	47	part_of	VEGFR-3	795:801	arg1	VEGFR-3 domains D1-2	VEGFR-3		VEGFR-3 domains D1-2		PUBTATOR	Site	VEGFR-3	2324	domains	Here we analyzed the crystal structures of VEGF-C in complex with VEGFR-3 domains D1-2 and of the VEGFR-3 D4-5 homodimer.
26846330	4	38	gly	glycoprotein	598:609	arg1	Ebola viral glycoprotein	Ebola viral glycoprotein				Fterm		glycoprotein			Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
9334252	4	18	gly	Trp-7	688:692	arg1	C-mannosylated			Trp-7	C-mannosylated					Trp-7	The enzyme was C-mannosylated at Trp-7, showing that the modification occurs intracellularly, before secretion of the protein.
9334252	4	54	gly	C-mannosylated	670:683	arg1	C-mannosylated			Trp-7	C-mannosylated					Trp-7	The enzyme was C-mannosylated at Trp-7, showing that the modification occurs intracellularly, before secretion of the protein.
9334252	4	54	gly	C-mannosylated	670:683	arg1	The enzyme	enzyme		Trp-7		Fterm		enzyme		Trp-7	The enzyme was C-mannosylated at Trp-7, showing that the modification occurs intracellularly, before secretion of the protein.
9334252	4	54	gly	C-mannosylated	670:683	arg1	The enzyme	enzyme			C-mannosylated	Fterm		enzyme			The enzyme was C-mannosylated at Trp-7, showing that the modification occurs intracellularly, before secretion of the protein.
7620335	1	44	part_of	X	311:311	arg1	the factor X activation peptide	factor X		the factor X activation peptide		OGER	Site	factor X	P00742	peptide	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	95	part_of	factor	304:309	arg1	the factor X activation peptide	factor X		the factor X activation peptide		OGER	Site	factor X	P00742	peptide	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
15702487	12	71	gly	glycopeptide	2060:2071	arg2	a glycopeptide			a glycopeptide						glycopeptide	These spectra allowed, by comparison, detection of a glycopeptide (several glycoforms) and elucidation of peptide sequence.
25374123	0	65	gly	N-glycosylation	35:49	arg1	vitronectin	vitronectin				PUBTATOR		vitronectin	7448		In-depth analysis of site-specific N-glycosylation in vitronectin from human plasma by tandem mass spectrometry with immunoprecipitation.
22187327	1	5	gly	glycoprotein	196:207	arg1	a dendritically polarized type I membrane glycoprotein	a dendritically polarized type I membrane glycoprotein				Fterm		glycoprotein			Intercellular adhesion molecule-5 (ICAM-5, telencephalin) is a dendritically polarized type I membrane glycoprotein, and promotes dendritic filopodia formation.
22187327	1	5	gly	glycoprotein	196:207	arg1	Intercellular adhesion molecule-5	Intercellular adhesion molecule-5				PUBTATOR		Intercellular adhesion molecule-5	15898		Intercellular adhesion molecule-5 (ICAM-5, telencephalin) is a dendritically polarized type I membrane glycoprotein, and promotes dendritic filopodia formation.
16037490	3	34	gly	sites	788:792	arg1	glycan heterogeneities			sites	glycan heterogeneities					sites	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	3	62	gly	N-glycosylation	772:786	arg2	seven N-glycosylation sites			seven N-glycosylation sites						sites	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16492764	2	0	part_of	GCSF	449:452	arg1	the Ig-like domains	GCSF-R and GCSF		the Ig-like domains		PUBTATOR	Site	GCSF-R and GCSF	1441	domains	The GCSF:GCSF-R complex formed a 2:2 stoichiometry by means of a cross-over interaction between the Ig-like domains of GCSF-R and GCSF.
16492764	2	14	part_of	GCSF-R	438:443	arg1	the Ig-like domains	GCSF-R and GCSF		the Ig-like domains		PUBTATOR	Site	GCSF-R and GCSF	1441	domains	The GCSF:GCSF-R complex formed a 2:2 stoichiometry by means of a cross-over interaction between the Ig-like domains of GCSF-R and GCSF.
9654101	5	42	gly	core-fucosylated	1047:1062	arg1	core-fucosylated biantennary glycans				core-fucosylated biantennary glycans						The IFN-alpha14c N-glycans were shown to exhibit core-fucosylated biantennary glycans, with about 10% carrying an additional alpha1,3-linked fucose unit at the antennae.
16274239	4	50	gly	glycosylation	718:730	arg1	579			N(579)						N(579)	Analysis of epitope accessibility suggests that the lack of glycosylation at N(579) weakens auto-inhibitory tether interactions, and cross-linking experiments suggest a somewhat elevated level of preformed N579Q-EGFR dimers in the absence of ligand relative to wild-type EGFR (WT-EGFR).
16274239	4	50	gly	glycosylation	718:730	arg2	N			N(579)						N(579)	Analysis of epitope accessibility suggests that the lack of glycosylation at N(579) weakens auto-inhibitory tether interactions, and cross-linking experiments suggest a somewhat elevated level of preformed N579Q-EGFR dimers in the absence of ligand relative to wild-type EGFR (WT-EGFR).
16274239	4	50	gly	glycosylation	718:730	arg1	N			N(579)						N(579)	Analysis of epitope accessibility suggests that the lack of glycosylation at N(579) weakens auto-inhibitory tether interactions, and cross-linking experiments suggest a somewhat elevated level of preformed N579Q-EGFR dimers in the absence of ligand relative to wild-type EGFR (WT-EGFR).
16274239	4	50	gly	glycosylation	718:730	arg2	N			N(579)						N(579)	Analysis of epitope accessibility suggests that the lack of glycosylation at N(579) weakens auto-inhibitory tether interactions, and cross-linking experiments suggest a somewhat elevated level of preformed N579Q-EGFR dimers in the absence of ligand relative to wild-type EGFR (WT-EGFR).
16274239	4	50	gly	glycosylation	718:730	arg1	N			N(579)						N(579)	Analysis of epitope accessibility suggests that the lack of glycosylation at N(579) weakens auto-inhibitory tether interactions, and cross-linking experiments suggest a somewhat elevated level of preformed N579Q-EGFR dimers in the absence of ligand relative to wild-type EGFR (WT-EGFR).
16274239	4	50	gly	glycosylation	718:730	arg1	N			N(579)						N(579)	Analysis of epitope accessibility suggests that the lack of glycosylation at N(579) weakens auto-inhibitory tether interactions, and cross-linking experiments suggest a somewhat elevated level of preformed N579Q-EGFR dimers in the absence of ligand relative to wild-type EGFR (WT-EGFR).
6427223	8	34	gly	glycosylation	904:916	arg2	two possible Asn-X-Ser/Thr glycosylation sites			two possible Asn-X-Ser/Thr glycosylation sites						sites	There are two possible Asn-X-Ser/Thr glycosylation sites.
8349699	7	10	part_of	site	1039:1042	arg1	murine PGH synthase-2	PGH synthase-2		site		PUBTATOR	Site	PGH synthase-2	19225	site	Using site-directed mutagenesis, we determined that there is an additional site of N-glycosylation in murine PGH synthase-2 located at Asn580.
20622017	0	46	gly	glycosylation	26:38	arg1	renal and hepatic γ-glutamyl transpeptidase	renal and hepatic γ-glutamyl transpeptidase				PUBTATOR		-glutamyl transpeptidase	102724197		Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
9884403	3	13	gly	glycosylation	719:731	arg2	the glycosylation sites			the glycosylation sites						sites	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
9884403	3	20	gly	microheterogeneity	684:701	arg1	the glycosylation sites			the glycosylation sites	the glycosylation sites		Site			sites	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
8631363	8	73	gly	0-glycosylated	1262:1275	arg1	tumor necrosis factor-alpha	tumor necrosis factor-alpha				PUBTATOR		tumor necrosis factor-alpha	7124		About 20% of tumor necrosis factor-alpha was found to be 0-glycosylated, based on the results of the sugar composition and structure analyses.
17082223	8	41	gly	Bsep	1644:1647	arg1	one glycan	Bsep			one glycan	PUBTATOR		Bsep	83569		To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	8	44	gly	glycosylation	1466:1478	arg1	glycans			site	glycans					site	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
11733580	0	5	gly	O-glycans	11:19	arg1	the NH2-terminal domain			the NH2-terminal domain	the NH2-terminal domain		Site			domain	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	0	5	gly	O-glycans	11:19	arg1	CC chemokine receptor 5	CC chemokine receptor 5			O-glycans	PUBTATOR		CC chemokine receptor 5	1234		Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
1150658	2	26	part_of	subunits	145:152	arg1	The amino acid sequences	subunits		The amino acid sequences		Fterm	Site	subunits		sequences	The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin have been determined.
14658030	0	62	part_of	NCAM	84:87	arg1	N-glycosylation sites	NCAM		N-glycosylation sites		PUBTATOR	Site	NCAM	17967	sites	Identification of N-glycosylation sites of the murine neural cell adhesion molecule NCAM by MALDI-TOF and MALDI-FTICR mass spectrometry.
18775496	1	7	part_of	threonine	160:168	arg1	Notch receptors	receptors		threonine		Fterm	AminoAcid	receptors		threonine	Protein O-fucosyltransferase 1 (Pofut1) transfers fucose to serine or threonine on proteins, including Notch receptors, that contain EGF repeats with a particular consensus sequence.
18775496	1	7	part_of	threonine	160:168	arg1	proteins	proteins		threonine		Fterm	AminoAcid	proteins		threonine	Protein O-fucosyltransferase 1 (Pofut1) transfers fucose to serine or threonine on proteins, including Notch receptors, that contain EGF repeats with a particular consensus sequence.
18775496	1	15	part_of	serine	150:155	arg1	Notch receptors	receptors		serine		Fterm	AminoAcid	receptors		serine	Protein O-fucosyltransferase 1 (Pofut1) transfers fucose to serine or threonine on proteins, including Notch receptors, that contain EGF repeats with a particular consensus sequence.
18775496	1	15	part_of	serine	150:155	arg1	proteins	proteins		serine		Fterm	AminoAcid	proteins		serine	Protein O-fucosyltransferase 1 (Pofut1) transfers fucose to serine or threonine on proteins, including Notch receptors, that contain EGF repeats with a particular consensus sequence.
27966990	7	5	part_of	sites	1339:1343	arg1	VEGFR-2	VEGFR-2		sites		PUBTATOR	Site	VEGFR-2	P35968	sites	MS/MS analyses of glycopeptides and deamidated, deglycosylated (PNGase F-treated) peptides from ectopically expressed VEGFR-2 in porcine aortic endothelial (PAE) cells identified N-glycans at the majority of the 17 potential N-glycosylation sites on VEGFR-2 in a site-specific manner.
27966990	7	71	part_of	VEGFR-2	1216:1222	arg1	deamidated, deglycosylated (PNGase F-treated) peptides	VEGFR-2		deamidated, deglycosylated (PNGase F-treated) peptides		PUBTATOR	Site	VEGFR-2	P35968	peptides	MS/MS analyses of glycopeptides and deamidated, deglycosylated (PNGase F-treated) peptides from ectopically expressed VEGFR-2 in porcine aortic endothelial (PAE) cells identified N-glycans at the majority of the 17 potential N-glycosylation sites on VEGFR-2 in a site-specific manner.
15044018	3	11	gly	glycoprotein	589:600	arg1	IGRP	IGRP				PUBTATOR		IGRP	57818		We show that IGRP is a glycoprotein, held in the endoplasmic reticulum by nine transmembrane domains, which is degraded in cells predominantly through the proteasome pathway that generates the major histocompatibility complex class I-presented peptides.
15044018	3	11	gly	glycoprotein	589:600	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			We show that IGRP is a glycoprotein, held in the endoplasmic reticulum by nine transmembrane domains, which is degraded in cells predominantly through the proteasome pathway that generates the major histocompatibility complex class I-presented peptides.
21752865	4	61	gly	N-glycosylated	857:870	arg2	Asn170	BRI2		Asn170		PUBTATOR		BRI2	9445	Asn170	In support, bioinformatics analysis indicated that BRI2 bears the consensus sequence Asn-Thr-Ser (residues 170-173) and could be N-glycosylated at Asn170.
7629073	6	83	part_of	protein	551:557	arg1	a cytoplasmic tail	protein		a cytoplasmic tail		Fterm	Site	protein		tail	Clone 4 encodes a type II membrane protein of 641 amino acids with a cytoplasmic tail of 35 amino acids, followed by a transmembrane domain and a large C-terminal catalytic domain, whereas clone 16 encodes only the last 471 amino acids.
16859706	6	12	part_of	TPST1	957:961	arg1	the transmembrane domain	TPST1		the transmembrane domain		PUBTATOR	Site	TPST1	8460	domain	In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment.
11390601	0	49	gly	glycosylation	9:21	arg2	N-linked glycosylation sites			N-linked glycosylation sites						sites	N-linked glycosylation sites adjacent to and within the V1/V2 and the V3 loops of dualtropic human immunodeficiency virus type 1 isolate DH12 gp120 affect coreceptor usage and cellular tropism.
25153361	5	8	part_of	alpha-1-acid	862:873	arg1	5 sequons	alpha-1-acid		5 sequons		Cterm		alpha-1-acid			We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
9852066	0	52	gly	O-glycosylation	20:34	arg2	Phosphorylation and O-glycosylation sites	CGA79-439		sites		Cterm		CGA79-439	1113	sites	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	0	52	gly	O-glycosylation	20:34	arg1	human chromogranin A	chromogranin A		sites		PUBTATOR		chromogranin A	1113	sites	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
19413349	0	37	gly	deglycosylated	9:22	arg1	N-linked deglycosylated melanopsin	N-linked deglycosylated melanopsin				PUBTATOR		melanopsin	192223		N-linked deglycosylated melanopsin retains its responsiveness to light.
18508581	3	1	gly	glycosylation	497:509	arg1	EpCAM	EpCAM				PUBTATOR		EpCAM	4072		We have uncovered differential glycosylation of EpCAM as a means to discriminate normal from malignant tissues.
2401370	2	21	part_of	asparaginase	279:290	arg1	rat liver asparaginase gene sequences	asparaginase		rat liver asparaginase gene sequences		Fterm	Site	asparaginase		sequences	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	2	15	part_of	containing	258:267	arg1	a 221-bp PCR amplified fragment AND rat liver asparaginase gene sequences	a 221-bp PCR amplified fragment		rat liver asparaginase gene sequences						sequences	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
21932778	2	51	gly	N-glycosylation	291:305	arg2	potential N-glycosylation sites			potential N-glycosylation sites						sites	The primary structures of glypican core proteins contain potential N-glycosylation sites, but the importance of N-glycosylation in glypicans has never been investigated in detail.
12545205	10	49	gly	contained	1634:1642	arg1	N-cadherin AND complex type chains	N-cadherin			complex type chains	PUBTATOR		N-cadherin	1000		In addition, N-cadherin from WM9 (lymphomodus metastatic site) and A375 (solid tumor metastatic site) contained complex type chains with alpha2-3 sialic acid (positive reaction with Maackia amurensis agglutinin--MAA).
24632570	3	32	part_of	TSLP	587:590	arg1	a mechanistic prerequisite	TSLP		a mechanistic prerequisite		PUBTATOR	Site	TSLP	53603	prerequisite	Binding of TSLP to TSLPR is a mechanistic prerequisite for recruitment of IL-7Rα to the high-affinity ternary complex, which we propose is coupled to a structural switch in TSLP at the crossroads of the cytokine-receptor interfaces.
30237853	3	48	gly	glycoprotein	491:502	arg1	potential glycoprotein cancer markers	potential glycoprotein cancer markers				Fterm		glycoprotein			However, quantitative glycoproteomics strategies to detect potential glycoprotein cancer markers from complex biospecimen are only just emerging.
8069634	11	26	gly	fucosylated	1814:1824	arg1	fucosylated oligosaccharides				fucosylated oligosaccharides						CONCLUSIONS: Our results explain the observation that Viciae lectins have a higher affinity for fucosylated oligosaccharides than for unfucosylated ones, whereas the affinity of ConA for these types of oligosaccharides is similar.
8069634	11	44	gly	unfucosylated	1852:1864	arg1	unfucosylated ones				unfucosylated ones						CONCLUSIONS: Our results explain the observation that Viciae lectins have a higher affinity for fucosylated oligosaccharides than for unfucosylated ones, whereas the affinity of ConA for these types of oligosaccharides is similar.
29391424	3	32	gly	glycoprotein	469:480	arg1	custom glycoprotein databases	custom glycoprotein databases				Fterm		glycoprotein			The steps in adopting the Mascot search engine for intact glycopeptide analysis included: (i) assigning one letter codes for monosaccharides, (ii) linearizing glycan sequences and (iii) preparing custom glycoprotein databases.
29391424	3	65	gly	glycopeptide	324:335	arg2	intact glycopeptide analysis			intact glycopeptide analysis						glycopeptide	The steps in adopting the Mascot search engine for intact glycopeptide analysis included: (i) assigning one letter codes for monosaccharides, (ii) linearizing glycan sequences and (iii) preparing custom glycoprotein databases.
7780197	6	19	gly	Glycosylation	861:873	arg1	Asn-727			Asn-727						Asn-727	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
1991473	6	48	part_of	hLH	817:819	arg1	Asn30	hLH beta		Asn30		PUBTATOR	AminoAcid	hLH beta	3972	Asn30	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	60	part_of	hLH	795:797	arg1	Asn52	hLH alpha		Asn52		PUBTATOR	AminoAcid	hLH alpha	1081	Asn52	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
21676880	0	47	part_of	KCNE1	59:63	arg1	type I transmembrane KCNE1 peptides	KCNE1		type I transmembrane KCNE1 peptides		PUBTATOR	Site	KCNE1	3753	peptides	Post-translational N-glycosylation of type I transmembrane KCNE1 peptides: implications for membrane protein biogenesis and disease.
6427223	1	7	gly	glycosylation	91:103	arg2	sites			sites						sites	Complete amino acid sequence and determination of sites of glycosylation.
21752865	8	19	gly	N-glycosylation	1296:1310	arg1	BRI2 trafficking	BRI2 trafficking				PUBTATOR		BRI2	9445		To examine the effect of N-glycosylation on BRI2 trafficking at the cell surface, we performed biotinylation and (35)S methionine pulse-chase experiments.
19952283	6	37	part_of	narpin	1008:1013	arg1	the narpin peptide	narpin		the narpin peptide		Fterm	Site	narpin		peptide	We show that both Np55 and the narpin peptide induce neurite outgrowth through FGFR1 activation and that Np55 increases synaptic calcium concentration in an FGFR1-dependent manner.
17896794	6	50	gly	attachment	1051:1060	arg2	serine AND O-linked N-acetylglucosamine			serine and threonine residues	O-linked N-acetylglucosamine					serine and threonine residues	Intracellular attachment of O-linked N-acetylglucosamine to serine and threonine residues hinders phosphorylation, thereby regulating the activity of the proteins concerned.
21569239	0	25	part_of	F-spondin	68:76	arg1	the Ca²+-binding, glycosylated F-spondin domain	F-spondin		the Ca²+-binding, glycosylated F-spondin domain		PUBTATOR	Site	F-spondin	10418	domain	The structure of the Ca²+-binding, glycosylated F-spondin domain of F-spondin - A C2-domain variant in an extracellular matrix protein.
21569239	0	44	part_of	F-spondin	48:56	arg1	the Ca²+-binding, glycosylated F-spondin domain	F-spondin		the Ca²+-binding, glycosylated F-spondin domain		PUBTATOR	Site	F-spondin	10418	domain	The structure of the Ca²+-binding, glycosylated F-spondin domain of F-spondin - A C2-domain variant in an extracellular matrix protein.
8477709	5	32	gly	monosialylated	1059:1072	arg1	monosialylated (70%) or disialylated (30%) forms				monosialylated (70%) or disialylated (30%) forms						Almost all of the innermost GlcNAc residues were alpha 1-6 fucosylated and NeuAc was exclusively alpha 2-3 linked to Gal beta 1-4GlcNAc-R; 60% of the protein was found to be O-glycosylated at Ser126; structures were monosialylated (70%) or disialylated (30%) forms of the Gal beta 1-3GalNAc core type.
8477709	5	32	gly	monosialylated	1059:1072	arg1	the Gal beta 1-3GalNAc core type				the Gal beta 1-3GalNAc core type						Almost all of the innermost GlcNAc residues were alpha 1-6 fucosylated and NeuAc was exclusively alpha 2-3 linked to Gal beta 1-4GlcNAc-R; 60% of the protein was found to be O-glycosylated at Ser126; structures were monosialylated (70%) or disialylated (30%) forms of the Gal beta 1-3GalNAc core type.
8477709	5	40	gly	disialylated	1083:1094	arg1	monosialylated (70%) or disialylated (30%) forms				monosialylated (70%) or disialylated (30%) forms						Almost all of the innermost GlcNAc residues were alpha 1-6 fucosylated and NeuAc was exclusively alpha 2-3 linked to Gal beta 1-4GlcNAc-R; 60% of the protein was found to be O-glycosylated at Ser126; structures were monosialylated (70%) or disialylated (30%) forms of the Gal beta 1-3GalNAc core type.
8477709	5	40	gly	disialylated	1083:1094	arg1	the Gal beta 1-3GalNAc core type				the Gal beta 1-3GalNAc core type						Almost all of the innermost GlcNAc residues were alpha 1-6 fucosylated and NeuAc was exclusively alpha 2-3 linked to Gal beta 1-4GlcNAc-R; 60% of the protein was found to be O-glycosylated at Ser126; structures were monosialylated (70%) or disialylated (30%) forms of the Gal beta 1-3GalNAc core type.
8477709	5	82	gly	fucosylated	902:912	arg1	the innermost GlcNAc residues				the innermost GlcNAc residues						Almost all of the innermost GlcNAc residues were alpha 1-6 fucosylated and NeuAc was exclusively alpha 2-3 linked to Gal beta 1-4GlcNAc-R; 60% of the protein was found to be O-glycosylated at Ser126; structures were monosialylated (70%) or disialylated (30%) forms of the Gal beta 1-3GalNAc core type.
8477709	5	13	gly	O-glycosylated	1017:1030	arg1	the protein	protein		Ser126		Fterm		protein		Ser126	Almost all of the innermost GlcNAc residues were alpha 1-6 fucosylated and NeuAc was exclusively alpha 2-3 linked to Gal beta 1-4GlcNAc-R; 60% of the protein was found to be O-glycosylated at Ser126; structures were monosialylated (70%) or disialylated (30%) forms of the Gal beta 1-3GalNAc core type.
8404899	2	7	gly	glycoprotein	276:287	arg1	only a 100-kDa glycoprotein	only a 100-kDa glycoprotein				Fterm		glycoprotein			For the detected glycoproteins, only a 100-kDa glycoprotein varied in the pancreatic juice from a normal patient (i.e. without any pancreatic disorder) compared to the pancreatic juice from a patient suffering from chronic pancreatitis.
8404899	2	62	gly	glycoproteins	246:258	arg1	the detected glycoproteins	the detected glycoproteins				Fterm		glycoproteins			For the detected glycoproteins, only a 100-kDa glycoprotein varied in the pancreatic juice from a normal patient (i.e. without any pancreatic disorder) compared to the pancreatic juice from a patient suffering from chronic pancreatitis.
30765605	3	40	part_of	β2	469:470	arg1	The immunoglobulin domain	2		The immunoglobulin domain		PUBTATOR	Site	2	10242	domain	The immunoglobulin domain of β2 interacts with the shoulder of the pore domain through a disulfide bond.
7263706	5	15	gly	attached	918:925	arg1	Asn-78 AND An N-linked carbohydrate side chain			Asn-78	An N-linked carbohydrate side chain					Asn-78	An N-linked carbohydrate side chain is attached to Asn-78 in at least a majority of tee gamma-molecules.
19383836	4	27	gly	glycosylation	570:582	arg1	ABCC11	ABCC11				PUBTATOR		ABCC11	85320		We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	4	27	gly	glycosylation	570:582	arg1	the variant protein	the variant protein				Fterm		protein			We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
8068684	9	59	gly	glycosylation	1729:1741	arg2	the N75 N-linked putative glycosylation site			the N75 N-linked putative glycosylation site						site	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	9	105	gly	serine	1788:1793	arg1	residues			residues						serine and threonine residues	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8323299	0	76	part_of	glycoproteins	94:106	arg1	the hinge-like regions	glycoproteins		the hinge-like regions		Fterm	Site	glycoproteins		regions	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
6371807	5	19	gly	located	716:722	arg2	the amino-terminal region AND The galactosamine oligosaccharide			the amino-terminal region	The galactosamine oligosaccharide					region	The galactosamine oligosaccharide and one glucosamine oligosaccharide are located in the amino-terminal region, three of the glucosamine oligosaccharides are in the middle region, and one glucosamine oligosaccharide is in the carboxyl-terminal region of the protein.
6371807	5	19	gly	located	716:722	arg2	the amino-terminal region AND one glucosamine oligosaccharide			the amino-terminal region	one glucosamine oligosaccharide					region	The galactosamine oligosaccharide and one glucosamine oligosaccharide are located in the amino-terminal region, three of the glucosamine oligosaccharides are in the middle region, and one glucosamine oligosaccharide is in the carboxyl-terminal region of the protein.
6371807	5	26	gly	region	746:751	arg1	The galactosamine oligosaccharide			region	The galactosamine oligosaccharide					region	The galactosamine oligosaccharide and one glucosamine oligosaccharide are located in the amino-terminal region, three of the glucosamine oligosaccharides are in the middle region, and one glucosamine oligosaccharide is in the carboxyl-terminal region of the protein.
26702061	3	30	part_of	PECAM-1	931:937	arg1	the PECAM-1 homophilic-binding domain	structure of the PECAM-1		the PECAM-1 homophilic-binding domain		PUBTATOR	Site	structure of the PECAM-1	5175	domain	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
8349699	4	24	gly	glycosylation	545:557	arg2	Inactive PGH synthase-1 glycosylation site mutant			Inactive PGH synthase-1 glycosylation site mutant						site	Inactive PGH synthase-1 glycosylation site mutant proteins do not appear to achieve their native conformations.
26207632	9	38	gly	O-glycosylated	1685:1698	arg1	region			region						region	CONCLUSIONS: Our results, taken together with previous observations, indicate that Obif is a type Ia transmembrane protein whose N-terminal region is O-glycosylated.
21752865	0	42	gly	Glycosylation	0:12	arg1	BRI2	BRI2				PUBTATOR		BRI2	9445		Glycosylation of BRI2 on asparagine 170 is involved in its trafficking to the cell surface but not in its processing by furin or ADAM10.
2737288	0	9	gly	glycosylation	41:53	arg2	the glycosylation site	pancreatic elastase 1		site		PUBTATOR		pancreatic elastase 1	1990	site	Localization and characterization of the glycosylation site of human pancreatic elastase 1.
22351761	8	77	part_of	containing	1413:1422	arg1	glypican-1 AND the HS attachment domain	glypican-1		the HS attachment domain		PUBTATOR	Site	glypican-1	2817	domain	No additional electron density was observed for crystals of glypican-1 containing the HS attachment domain, and CD spectra of the two protein species were highly similar.
18340083	7	52	part_of	site	922:925	arg1	mouse GPIHBP1	GPIHBP1		site		PUBTATOR	Site	GPIHBP1	68453	site	Mutating the N-glycosylation site in mouse GPIHBP1 results in an accumulation of GPIHBP1 in the endoplasmic reticulum and a markedly reduced amount of the protein on the cell surface.
20571061	6	46	part_of	proteins	1229:1236	arg1	25 targeted glycopeptides	proteins		25 targeted glycopeptides		Fterm	Site	proteins		glycopeptides	Versatility of the reverse glycoblotting-assisted MRM assays was demonstrated by quantitative comparison of 25 targeted glycopeptides from 16 proteins between mice with homo and hetero types of diabetes disease model.
30559189	2	28	part_of	protein	274:280	arg1	a three-fingered LU domain	protein		domain		Fterm	Site	protein		domain	The LPL within capillaries is bound to GPIHBP1, an endothelial cell protein with a three-fingered LU domain and an N-terminal intrinsically disordered acidic domain.
29671580	3	39	gly	N-glycosites	638:649	arg2	identified N-glycosites			identified N-glycosites						N-glycosites	Our data indicated that half of identified N-glycosites were modified by at least two glycans, with a majority of them being sialylated.
6333684	0	42	part_of	interleukin	65:75	arg1	Amino acid sequence	interleukin 2		Amino acid sequence		PUBTATOR	Site	interleukin 2	3558	sequence	Amino acid sequence and post-translational modification of human interleukin 2.
11168369	0	24	gly	O-glycosylated	77:90	arg1	albumin Kénitra	albumin Kénitra				PUBTATOR		albumin Kénitra	213		A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
22159084	3	5	gly	glycosylated	324:335	arg1	SLC26A3	SLC26A3				PUBTATOR		SLC26A3	1811		It has been shown that SLC26A3 are glycosylated, with the attached carbohydrate being extracellular and perhaps modulating function.
22173220	5	49	gly	glycosylation	623:635	arg2	All seven predicted N-linked glycosylation sites			All seven predicted N-linked glycosylation sites						sites	All seven predicted N-linked glycosylation sites are exposed on the molecular surface, away from the dimer interface.
21569239	0	76	gly	glycosylated	35:46	arg1	the Ca²+-binding, glycosylated F-spondin domain	F-spondin		domain		PUBTATOR		F-spondin	10418	domain	The structure of the Ca²+-binding, glycosylated F-spondin domain of F-spondin - A C2-domain variant in an extracellular matrix protein.
9450956	0	22	gly	Trp-7	42:46	arg1	Recognition signal for C-mannosylation			Trp-7	Recognition signal for C-mannosylation					Trp-7	Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.
9450956	0	48	gly	C-mannosylation	23:37	arg1	RNase 2	RNase 2		Trp-7		PUBTATOR		RNase 2	6036	Trp-7	Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.
9450956	0	62	gly	C-mannosylation	23:37	arg1	RNase 2	RNase 2		Trp-7	C-mannosylation	PUBTATOR		RNase 2	6036	Trp-7	Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.
9450956	0	62	gly	C-mannosylation	23:37	arg1	RNase 2	RNase 2			C-mannosylation	PUBTATOR		RNase 2	6036		Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.
19692335	0	19	part_of	metalloproteinase	136:152	arg1	the ectodomain	metalloproteinase		the ectodomain		Fterm	Site	metalloproteinase		ectodomain	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	70	part_of	metalloproteinase-22	67:86	arg1	the ectodomain	metalloproteinase-22		the ectodomain		Fterm	Site	metalloproteinase-22		ectodomain	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	89	part_of	disintegrin	51:61	arg1	the ectodomain	disintegrin		the ectodomain		Fterm	Site	disintegrin		ectodomain	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
18533687	3	105	gly	glycosylation	439:451	arg2	positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346			positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346						positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	3	105	gly	glycosylation	439:451	arg2	six putative Asn-linked glycosylation sites			six putative Asn-linked glycosylation sites						sites	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
22511793	6	0	part_of	protein	1125:1131	arg1	a highly glycosylated luminal domain	protein		a highly glycosylated luminal domain		Fterm	Site	protein		domain	By differential membrane extraction and sequential mutagenesis of potential N-glycosylation sites, we identified TMEM106B as a type 2 integral membrane protein with a highly glycosylated luminal domain.
15807535	4	94	gly	glycosylated	776:787	arg1	only asparagine 596			only asparagine 596						asparagine 596	Site-directed mutagenesis experiments, in which each Asn was changed to Gln independently, revealed that only asparagine 596 is N-linked glycosylated.
1544894	1	17	gly	attachment	339:348	arg2	equivalent threonine residues AND fucose			equivalent threonine residues	fucose					threonine residues	We and others have demonstrated that tissue plasminogen activator (t-PA) and prourokinase are modified by the attachment of fucose to equivalent threonine residues within their EGF domains.
16944957	6	20	gly	glycosylation	657:669	arg1	a given site			site						site	Our method furthermore senses the nature of glycan structures and can detect differential glycosylation on a given site.
10419520	9	33	part_of	S2P	1212:1214	arg1	the long hydrophilic sequences	S2P		the long hydrophilic sequences		PUBTATOR	Site	S2P	51360	sequences	All three of the long hydrophilic sequences of S2P can be glycosylated, indicating that they all project into the lumen.
15504740	7	13	part_of	ASIC2a	1384:1389	arg1	the intracellular amino termini	ASIC2a		the intracellular amino termini		PUBTATOR	Site	ASIC2a	40	termini	Finally, we used cell permeabilization studies to confirm the intracellular amino termini of ASIC2a.
11226831	9	25	part_of	sites	852:856	arg1	mER-alpha	mER		sites		PUBTATOR	Site	mER	13982	sites	Analyses of glycopeptides identified two additional sites of modification on mER-alpha, at Ser(10) and Thr(50) near the N-terminus.
25802287	5	17	gly	glycopeptides	978:990	arg2	the intact glycopeptides			the intact glycopeptides						glycopeptides	After fractionation, each other spot is treated with PNGaseF to generate two correlated traces within one run, one with treated spots where glycans are enzymatically released from the peptides, and one containing the intact glycopeptides.
25802287	5	51	gly	released	920:927	arg1	the peptides AND glycans			the peptides	glycans					peptides	After fractionation, each other spot is treated with PNGaseF to generate two correlated traces within one run, one with treated spots where glycans are enzymatically released from the peptides, and one containing the intact glycopeptides.
1059087	0	54	part_of	glycophorin	78:88	arg1	Amino-acid sequence	glycophorin		Amino-acid sequence		Fterm	Site	glycophorin		sequence	Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
7654718	1	30	gly	characteristics	133:147	arg1	C-tail	C-tail			characteristics	Cterm		C-tail			Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	1	30	gly	characteristics	133:147	arg1	C-terminal region			C-terminal region	C-terminal region		Site			region	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7525874	9	36	gly	monosialylated	1075:1088	arg1	the monosialylated oligosaccharide fractions				the monosialylated oligosaccharide fractions						Especially in the neutral, but also in the monosialylated oligosaccharide fractions, many incomplete antennae consisting of N-acetylglucosamine only were present.
25187573	10	79	gly	glycopeptide	1764:1775	arg2	The site-specific glycopeptide analysis			The site-specific glycopeptide analysis						glycopeptide	The site-specific glycopeptide analysis covered 82% of the protein sequence and showed that lubricin glycosylation displays both micro- and macroheterogeneity.
2513186	8	10	gly	linked	1420:1425	arg1	position six AND additional Gal(alpha 1-3) substituents			position six	additional Gal(alpha 1-3) substituents					position	As a characteristic feature, part of the triantennary glycans at Asn184 and Asn448 contain additional Gal(alpha 1-3) substituents and/or sulfate groups linked to position six of beta-galactosyl residues forming NeuAc(alpha 2-3)[HO3S-6]Gal(beta 1-4) units.
2513186	8	54	gly	Asn184	1333:1338	arg1	the triantennary glycans			Asn184 and Asn448	the triantennary glycans					Asn184 and Asn448	As a characteristic feature, part of the triantennary glycans at Asn184 and Asn448 contain additional Gal(alpha 1-3) substituents and/or sulfate groups linked to position six of beta-galactosyl residues forming NeuAc(alpha 2-3)[HO3S-6]Gal(beta 1-4) units.
2513186	8	60	gly	Asn448	1344:1349	arg1	the triantennary glycans			Asn184 and Asn448	the triantennary glycans					Asn184 and Asn448	As a characteristic feature, part of the triantennary glycans at Asn184 and Asn448 contain additional Gal(alpha 1-3) substituents and/or sulfate groups linked to position six of beta-galactosyl residues forming NeuAc(alpha 2-3)[HO3S-6]Gal(beta 1-4) units.
9712881	2	46	part_of	AE1	223:225	arg1	Glu681	AE1		Glu681		PUBTATOR	AminoAcid	AE1	6521	Glu681	Glu681 of human AE1 may form part of the anion translocation apparatus and the permeability barrier.
22159084	6	62	gly	glycosylated	670:681	arg1	the mature glycosylated form	form of SLC26A3				PUBTATOR		form of SLC26A3	1811		Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
28784760	4	12	part_of	NPC1	642:645	arg1	residues 314-1,278	NPC1		residues 314-1,278		PUBTATOR	SpecificSite	NPC1	4864	residues 314	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
2386787	5	0	gly	carbohydrate	1405:1416	arg1	proteins	proteins			carbohydrate	Fterm		proteins			This is the first direct identification of complex carbohydrate in proteins produced in insect cells and demonstrates that trimming and processing of high-mannose carbohydrate into complex-type oligosaccharide can occur.
20511397	2	13	gly	glycosylated/sialylated	523:545	arg1	plasma apoE	plasma apoE				PUBTATOR		apoE	348		Cellular apoE and plasma apoE exist as multiple glycosylated and sialylated glycoforms with plasma apoE being less glycosylated/sialylated than cell-derived apoE.
20511397	2	52	gly	sialylated	473:482	arg1	multiple glycosylated and sialylated glycoforms				multiple glycosylated and sialylated glycoforms						Cellular apoE and plasma apoE exist as multiple glycosylated and sialylated glycoforms with plasma apoE being less glycosylated/sialylated than cell-derived apoE.
20511397	2	63	gly	glycosylated	456:467	arg1	multiple glycosylated and sialylated glycoforms				multiple glycosylated and sialylated glycoforms						Cellular apoE and plasma apoE exist as multiple glycosylated and sialylated glycoforms with plasma apoE being less glycosylated/sialylated than cell-derived apoE.
3200844	8	8	part_of	CNBr	1135:1138	arg1	a second CNBr fragment	CNBr		a second CNBr fragment		Cterm	Site	CNBr		fragment	This open reading frame contained a CNBr fragment identical to the original glycopeptide sequence and a second CNBr fragment corresponding to a nonglycosylated peptide that was also isolated from the purified pore glycoprotein.
3200844	8	59	part_of	CNBr	1060:1063	arg1	a CNBr fragment	CNBr		a CNBr fragment		Cterm	Site	CNBr		fragment	This open reading frame contained a CNBr fragment identical to the original glycopeptide sequence and a second CNBr fragment corresponding to a nonglycosylated peptide that was also isolated from the purified pore glycoprotein.
22171320	9	24	gly	fucosylated	1596:1606	arg1	fucosylated core 2-like O-glycans				fucosylated core 2-like O-glycans						Additional glycoforms for specific N- and O-linked glycopeptides were also identified, e.g. tetra-antennary N-glycans and fucosylated core 2-like O-glycans.
22171320	9	48	gly	glycopeptides	1525:1537	arg2	O-linked glycopeptides			O-linked glycopeptides						glycopeptides	Additional glycoforms for specific N- and O-linked glycopeptides were also identified, e.g. tetra-antennary N-glycans and fucosylated core 2-like O-glycans.
11710528	0	7	gly	receptor	125:132	arg1	high mannose-type Asn-linked oligosaccharides	transferrin receptor			high mannose-type Asn-linked oligosaccharides	PUBTATOR		transferrin receptor	7037		Differential and cell-type specific microheterogeneity of high mannose-type Asn-linked oligosaccharides of human transferrin receptor.
11710528	0	53	gly	microheterogeneity	36:53	arg1	high mannose-type Asn-linked oligosaccharides				high mannose-type Asn-linked oligosaccharides						Differential and cell-type specific microheterogeneity of high mannose-type Asn-linked oligosaccharides of human transferrin receptor.
11710528	0	63	gly	Asn-linked	76:85	arg1	high mannose-type Asn-linked oligosaccharides			Asn	high mannose-type Asn-linked oligosaccharides					Asn	Differential and cell-type specific microheterogeneity of high mannose-type Asn-linked oligosaccharides of human transferrin receptor.
1388166	8	63	gly	glycosylation	1548:1560	arg2	the glycosylation site			the glycosylation site						site	TFPI contains the sequence Pro-Phe-Lys, 9 residues N-terminal to the glycosylation site at position 228; this tripeptide may act as the recognition sequence for the GalNAc-transferase.
19349973	3	8	gly	N-glycoprotein	921:934	arg1	cell surface N-glycoprotein markers	cell surface N-glycoprotein markers				Fterm		N-glycoprotein			We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
11226831	0	23	gly	Glycosylation	0:12	arg1	the murine estrogen receptor-alpha	the murine estrogen receptor-alpha				PUBTATOR		estrogen receptor	13982		Glycosylation of the murine estrogen receptor-alpha.
8407981	3	30	gly	glycosylation	303:315	arg1	arom	P-450(arom)				PUBTATOR		P-450(arom)	55010		The core glycosylation of P-450(arom) was examined with two heterologous expression systems, cultured insect cells and in vitro translation system.
21569239	7	80	gly	glycosylation	1083:1095	arg2	a highly conserved N-linked glycosylation site			a highly conserved N-linked glycosylation site						site	The unique feature of F-spondin FS domain is the presence of three disulfide bonds associated with the N- and C-termini of the domain and a highly conserved N-linked glycosylation site.
12888274	7	38	part_of	A	1058:1058	arg1	the active site	arylsulfatase A		the active site		PUBTATOR	Site	arylsulfatase A	410	site	The metal ion present in the active site of arylsulfatase A isolated from human placenta is Ca(2+) and not Mg(2+) as was found in the structure of the recombinant enzyme.
17711303	1	60	gly	glycosylation	144:156	arg1	FLAG-hKOR	FLAG-hKOR				PUBTATOR		hKOR	4986		We examined glycosylation of FLAG-hKOR expressed in CHO cells and determined its functional significance.
10092871	9	70	part_of	MMP-1	1539:1543	arg1	the MMP-1 sequence	MMP-1		the MMP-1 sequence		PUBTATOR	Site	MMP-1	4312	sequence	We also show that, of the two potential glycosylation sites in the MMP-1 sequence, only Asn120 is used.
447737	3	3	gly	glycopeptide	361:372	arg2	glycopeptide			glycopeptide						glycopeptide	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
18676855	6	47	gly	epitope	1129:1135	arg1	epitope tag				epitope tag						We produced mAb to three regions that are predicted to be intracellular based on the epitope tag data (amino acids 1-352, 441-501, and 868-933), and as predicted, the mAb only detected the protein in permeabilized cells.
19946266	5	58	part_of	channel	858:864	arg1	ion channel domains	channel		ion channel domains		Fterm	Site	channel		domains	A symmetry mismatch between the extracellular and ion channel domains is mediated by two pairs of conformationally distinct subunits, A/C and B/D.
2415652	7	80	gly	oligosaccharides	1364:1379	arg1	hCG beta	hCG beta			oligosaccharides	PUBTATOR		hCG beta	1082		In contrast, over 50% of the O-linked oligosaccharides in hCG beta from the JAr choriocarcinoma cell line are hexasaccharides.
2415652	7	117	gly	beta	1388:1391	arg1	hexasaccharides	hCG beta			hexasaccharides	PUBTATOR		hCG beta	1082		In contrast, over 50% of the O-linked oligosaccharides in hCG beta from the JAr choriocarcinoma cell line are hexasaccharides.
2415652	7	117	gly	beta	1388:1391	arg1	the O-linked oligosaccharides	hCG beta			the O-linked oligosaccharides	PUBTATOR		hCG beta	1082		In contrast, over 50% of the O-linked oligosaccharides in hCG beta from the JAr choriocarcinoma cell line are hexasaccharides.
10200178	2	102	gly	PrP	398:400	arg1	the N-linked glycans	PrP			the N-linked glycans	OGER		PrP	Q9NP58		A partial site-specific study of the N-linked glycans from hamster PrP has previously been carried out by mass spectrometry [Stahl, N., Baldwin, M. A., Teplow, D. B., Hood, L., Gibson, B. W., Burlingame, A. L., and Prusiner, S. B. (1993) Biochemistry 32, 1991-2002] and revealed that the glycosylation at Asn-181 (equivalent to mouse 180) is heterogeneous, comprising over 30 glycoforms.
10200178	2	92	gly	glycosylation	619:631	arg2	Asn-181			Asn-181						Asn-181	A partial site-specific study of the N-linked glycans from hamster PrP has previously been carried out by mass spectrometry [Stahl, N., Baldwin, M. A., Teplow, D. B., Hood, L., Gibson, B. W., Burlingame, A. L., and Prusiner, S. B. (1993) Biochemistry 32, 1991-2002] and revealed that the glycosylation at Asn-181 (equivalent to mouse 180) is heterogeneous, comprising over 30 glycoforms.
9883900	7	16	part_of	IGFBP-5	943:949	arg1	the central IGFBP-5 region	IGFBP-5		the central IGFBP-5 region		PUBTATOR	Site	IGFBP-5	3488	region	In addition, a smaller fragment with Mr 2722 of the central IGFBP-5 region was purified and showed the sequence HTRISELKAEAVKKDRRKKLTQS (residues 121-143) indicating plasma proteolysis of IGFBP-5 C-terminal to amino acids Lys-120, Ser-143, Lys-144, and Arg-188.
24721674	7	13	gly	N-glycosites	1470:1481	arg2	82 N-glycosites			82 N-glycosites						N-glycosites	Furthermore, 177 glycopeptides representing 82 N-glycosites with both glycan composition and peptide sequence were identified by high energy collision dissociation.
24721674	7	83	gly	glycopeptides	1440:1452	arg2	177 glycopeptides			177 glycopeptides						glycopeptides	Furthermore, 177 glycopeptides representing 82 N-glycosites with both glycan composition and peptide sequence were identified by high energy collision dissociation.
11738084	0	10	gly	glycosylated	43:54	arg1	a glycosylated variant	a glycosylated variant				Fterm		variant			The glycan structure of albumin Redhill, a glycosylated variant of human serum albumin.
16750161	4	27	gly	glycosylation	845:857	arg2	seven sites			seven sites						sites	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
6177036	1	7	part_of	immunoglobulin	179:192	arg1	variable-region immunoglobulin domains	immunoglobulin		variable-region immunoglobulin domains		Fterm	Site	immunoglobulin		domains	The amino acid sequences of mouse brain Thy-1 glycoproteins are shown to be homologous to those of variable-region immunoglobulin domains.
6177036	1	19	part_of	glycoproteins	110:122	arg1	The amino acid sequences	Thy-1 glycoproteins		The amino acid sequences		PUBTATOR	Site	Thy-1 glycoproteins	21838	sequences	The amino acid sequences of mouse brain Thy-1 glycoproteins are shown to be homologous to those of variable-region immunoglobulin domains.
15254193	8	44	gly	N-glycosylated	1164:1177	arg1	Most murine IFN-alpha	Most murine IFN-alpha				PUBTATOR		IFN-alpha	111654		Most murine IFN-alpha turned out to be N-glycosylated.
18815274	6	4	part_of	receptor	744:751	arg1	the extracellular domain	low-density lipoprotein receptor		the extracellular domain		PUBTATOR	Site	low-density lipoprotein receptor	16835	domain	The fourth luminal domain of SV2A or SV2B alone, expressed in chimeric receptors by replacing the extracellular domain of the low-density lipoprotein receptor, can restore the binding and entry of BoNT/E into neurons lacking SV2A/B.
18815274	6	10	part_of	SV2B	631:634	arg1	The fourth luminal domain	SV2B		The fourth luminal domain		PUBTATOR	Site	SV2B	64176	domain	The fourth luminal domain of SV2A or SV2B alone, expressed in chimeric receptors by replacing the extracellular domain of the low-density lipoprotein receptor, can restore the binding and entry of BoNT/E into neurons lacking SV2A/B.
18815274	6	15	part_of	SV2A	623:626	arg1	The fourth luminal domain	SV2A		The fourth luminal domain		PUBTATOR	Site	SV2A	64051	domain	The fourth luminal domain of SV2A or SV2B alone, expressed in chimeric receptors by replacing the extracellular domain of the low-density lipoprotein receptor, can restore the binding and entry of BoNT/E into neurons lacking SV2A/B.
11676606	6	69	gly	structures	768:777	arg1	sCD154	CD154			structures	PUBTATOR		CD154	959		Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
20805301	5	12	gly	glycosylation	689:701	arg1	CYP2W1	CYP2W1		Asn177		PUBTATOR		CYP2W1	54905	Asn177	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	12	gly	glycosylation	689:701	arg2	the only possible glycosylation site	CYP2W1		site		PUBTATOR		CYP2W1	54905	site	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
12731890	5	73	gly	glycosylated	1080:1091	arg1	an additional canonical site			an additional canonical site						site	We show that an additional canonical site in the secreted form of the receptor is fully glycosylated.
23959878	4	8	gly	attached	677:684	arg1	N372 AND the N-glycan			N372	the N-glycan					N372	Structural analysis revealed that the mannose residue of the N-glycan attached to N372 constituted a part of the substrate-binding pocket and interacted directly with a substrate.
10930422	3	17	gly	glycosylated	297:308	arg1	a highly glycosylated protein	a highly glycosylated protein				Fterm		protein			Reprimo is a highly glycosylated protein and, when ectopically expressed, it is localized in the cytoplasm and induces G(2) arrest of the cell cycle.
10930422	3	17	gly	glycosylated	297:308	arg1	Reprimo	Reprimo				PUBTATOR		Reprimo	56475		Reprimo is a highly glycosylated protein and, when ectopically expressed, it is localized in the cytoplasm and induces G(2) arrest of the cell cycle.
6267033	2	6	gly	glycopeptide	196:207	arg2	a human glycopeptide			a human glycopeptide						glycopeptide	The isolation and complete purification of a human glycopeptide representing the major immunoreactive form of the pituitary NH2-terminal segment of pro-opiomelanocortin is presented.
2737288	2	1	gly	N-glycosylation	201:215	arg2	the potential N-glycosylation sites			the potential N-glycosylation sites						sites	Two peptides, containing the potential N-glycosylation sites at Asn-86 and Asn-125, were isolated and analyzed by amino acid analysis, sequencing and carbohydrate component analysis.
10821832	4	50	gly	glycoprotein	973:984	arg1	this glycoprotein	this glycoprotein				Fterm		glycoprotein			Our data indicate that this glycoprotein contains 13 transmembrane domains, 3 large and 4 small luminal loops, 6 small cytoplasmic loops, and a cytoplasmic tail.
8053566	6	33	gly	glycosylation	1291:1303	arg2	Both TIMP glycosylation sites			Both TIMP glycosylation sites						sites	Both TIMP glycosylation sites exhibited extensive heterogeneity comprising mainly fucosylated complex oligosaccharides, but in different proportions.
8053566	6	34	gly	fucosylated	1363:1373	arg1	fucosylated complex oligosaccharides				fucosylated complex oligosaccharides						Both TIMP glycosylation sites exhibited extensive heterogeneity comprising mainly fucosylated complex oligosaccharides, but in different proportions.
19153605	10	29	part_of	FS	1152:1153	arg1	the FS and TSR domains	FS		the FS and TSR domains		Cterm	Site	FS	10418	domains	Through these dual interactions, the FS and TSR domains of mindin promote activation of both adaptive and innate immune responses.
19153605	10	55	part_of	mindin	1174:1179	arg1	the FS and TSR domains	mindin		the FS and TSR domains		PUBTATOR	Site	mindin	10417	domains	Through these dual interactions, the FS and TSR domains of mindin promote activation of both adaptive and innate immune responses.
29741879	5	74	part_of	glycoproteins	1211:1223	arg1	6 724 N-linked glycopeptides	glycoproteins		6 724 N-linked glycopeptides		Fterm	Site	glycoproteins		glycopeptides	Collectively, combined tandem mass spectrometry (MS/MS) analyses of global proteomic and phosphoproteomic data sets resulted in the identification of 6 724 N-linked glycopeptides from 617 glycoproteins derived from two breast cancer xenograft tissues.
16212939	1	67	part_of	hIL-1beta-derived	136:152	arg1	hIL-1beta-derived polypeptide	hIL-1beta		hIL-1beta-derived polypeptide		PUBTATOR	Site	hIL-1beta	3553	polypeptide	hIL-1beta-derived polypeptide, when fused to the N-terminal end of target proteins, exerts a potent secretion enhancer function in Saccharomyces cerevisiae.
4055801	7	14	part_of	protein	894:900	arg1	two single-chain polypeptide fragments	protein		two single-chain polypeptide fragments		Fterm	Site	protein		fragments	C9 can be cleaved by alpha-thrombin into two single-chain polypeptide fragments: C9a (Mr = 28,000) and C9b (Mr = 38,000), which are the amino- and carboxyl-terminal segments of the protein, respectively.
4055801	7	30	part_of	polypeptide	771:781	arg1	two single-chain polypeptide fragments	polypeptide		two single-chain polypeptide fragments		Fterm	Site	polypeptide		fragments	C9 can be cleaved by alpha-thrombin into two single-chain polypeptide fragments: C9a (Mr = 28,000) and C9b (Mr = 38,000), which are the amino- and carboxyl-terminal segments of the protein, respectively.
10441114	7	15	gly	asialoglycoprotein	1146:1163	arg1	sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures	sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures				Fterm		asialoglycoprotein			Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	7	73	gly	sialoglycoprotein	1091:1107	arg1	sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures	sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures				Fterm		sialoglycoprotein			Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10978165	10	52	gly	glycosylated	1253:1264	arg1	1-74	1-74				Cterm		1-74	6358		Our data imply that HCC-1 (1-74), HCC-1 (3-74), HCC-1 (4-74) and glycosylated HCC-1 (1-74) circulate in human blood.
10978165	10	52	gly	glycosylated	1253:1264	arg1	glycosylated HCC-1	glycosylated HCC-1				PUBTATOR		HCC-1	6358		Our data imply that HCC-1 (1-74), HCC-1 (3-74), HCC-1 (4-74) and glycosylated HCC-1 (1-74) circulate in human blood.
11439087	11	8	gly	N-glycosylation	1428:1442	arg1	sBST-1	sBST-1				Cterm		sBST-1	683		We conclude that N-glycosylation of sBST-1 facilitates the folding of the nascent polypeptide chain into a conformation that is conductive for intracellular transport and enzymic activity.
27384988	11	1	part_of	rpS3	1244:1247	arg1	the Asn 165 residue	rpS3		the Asn 165 residue		PUBTATOR	SpecificSite	rpS3	6188	Asn 165 residue	The results indicate that the Asn 165 residue of rpS3 is a critical site for N-linked glycosylation and passage through the ER-Golgi secretion pathway.
27384988	11	1	part_of	rpS3	1244:1247	arg1	a critical site	rpS3		a critical site		PUBTATOR	Site	rpS3	6188	site	The results indicate that the Asn 165 residue of rpS3 is a critical site for N-linked glycosylation and passage through the ER-Golgi secretion pathway.
29899144	3	12	part_of	GPIHBP1	504:510	arg1	The N-terminal domain	GPIHBP1		The N-terminal domain		PUBTATOR	Site	GPIHBP1	338328	domain	The N-terminal domain of GPIHBP1, an intrinsically disordered region (IDR) rich in acidic residues, is important for stabilizing LPL's catalytic domain against spontaneous and ANGPTL4-catalyzed unfolding.
23520111	6	36	gly	leucine-rich	719:730	arg1	leucine-rich repeat 14			leucine	leucine-rich repeat 14					leucine	The loop between leucine-rich repeat 14 (LRR14) and LRR15 was cleaved; however, the N- and C-terminal halves remained associated and contributed to ligand recognition and dimerization.
9023546	5	14	part_of	EGF	716:718	arg1	complete EGF domains	EGF		complete EGF domains		OGER	Site	EGF	P01133	domains	These synthetic peptides did not compromise complete EGF domains and did not contain all six cysteine residues that define the EGF structure.
9023546	5	30	part_of	contain	740:746	arg1	These synthetic peptides AND all six cysteine residues	These synthetic peptides		all six cysteine residues						cysteine residues	These synthetic peptides did not compromise complete EGF domains and did not contain all six cysteine residues that define the EGF structure.
6619128	11	18	gly	glycoproteins	1361:1373	arg1	membrane glycoproteins	membrane glycoproteins				Fterm		glycoproteins			These structures, however, have been described on a number of secreted and membrane glycoproteins.
14573609	3	21	gly	glycosylation	483:495	arg1	heparanase	heparanase				PUBTATOR		heparanase	10855		In this study, we examined the link between glycosylation and the function of heparanase in human tumor cell lines.
9757569	1	7	part_of	angiotensinogen	165:179	arg1	Ser14	angiotensinogen		Ser14		PUBTATOR	AminoAcid	angiotensinogen	P01019	Ser14	A mutant angiotensinogen, S14N, in which Ser14 of ovine angiotensinogen was replaced by Asn to form a N-glycosylation site, was produced in CHO cells.
20484118	3	40	gly	modified	403:410	arg3	the Ser/Thr residues AND O-GlcNAc			the Ser/Thr residues	O-GlcNAc					residues	Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes.
20484118	3	40	gly	modified	403:410	arg3	the Ser/Thr residues AND O-linked N-acetylglucosamine			the Ser/Thr residues	O-linked N-acetylglucosamine					residues	Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes.
2209609	2	57	gly	N-glycosylation	347:361	arg2	two N-glycosylation sites			two N-glycosylation sites						sites, Asn271 and Asn300	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	2	58	gly	glycoprotein	326:337	arg1	The glycoprotein	The glycoprotein				Fterm		glycoprotein			The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
25759508	9	83	gly	occupancy	1302:1310	arg2	the three O-glycosylation sites			the three O-glycosylation sites						sites	The occupancy of each of the three O-glycosylation sites was found to be ∼10% in six serum-derived IgG3 samples and ∼13% in two monoclonal IgG3 allotypes.
25759508	9	90	gly	O-glycosylation	1333:1347	arg2	the three O-glycosylation sites			the three O-glycosylation sites						sites	The occupancy of each of the three O-glycosylation sites was found to be ∼10% in six serum-derived IgG3 samples and ∼13% in two monoclonal IgG3 allotypes.
28489325	1	48	part_of	contains	243:250	arg1	L-Selectin AND seven N-glycosylation sites	L-Selectin		seven N-glycosylation sites		PUBTATOR	Site	L-Selectin	6402	sites	L-Selectin, a cell-adhesion receptor on the surface of most leukocytes, contains seven N-glycosylation sites.
28489325	1	48	part_of	contains	243:250	arg1	a cell-adhesion receptor AND seven N-glycosylation sites	a cell-adhesion receptor		seven N-glycosylation sites		Fterm	Site	receptor		sites	L-Selectin, a cell-adhesion receptor on the surface of most leukocytes, contains seven N-glycosylation sites.
24125761	6	81	gly	glycosylated	878:889	arg1	AADAC	AADAC		N78 and N282		PUBTATOR		AADAC	13	N78 and N282	This result indicated that AADAC was glycosylated at both N78 and N282.
24125761	6	81	gly	glycosylated	878:889	arg2	N78			N78 and N282						N78 and N282	This result indicated that AADAC was glycosylated at both N78 and N282.
24125761	6	81	gly	glycosylated	878:889	arg2	N78	AADAC		N78 and N282		PUBTATOR		AADAC	13	N78 and N282	This result indicated that AADAC was glycosylated at both N78 and N282.
6776528	0	30	part_of	chain	61:65	arg1	Complete amino acid sequence	chain		Complete amino acid sequence		OGER	Site	chain		sequence	Complete amino acid sequence of a mouse immunoglobulin alpha chain (MOPC 511).
3342889	6	52	part_of	cathepsins	808:817	arg1	known sequences	cathepsins H		known sequences		OGER	Site	cathepsins H	P25774	sequences	The fragments were aligned by comparison with known sequences of cathepsins H and L from other species.
6574504	2	39	part_of	B	287:287	arg1	the 220-residue sequence	cathepsin B		sequence		PUBTATOR	Site	cathepsin B	P07858	sequence	The 252-residue sequence of cathepsin B and the 220-residue sequence of cathepsin H were determined largely by automated Edman degradation of their intact polypeptide chains and of the two chains of each enzyme generated by limited proteolysis.
6574504	2	54	part_of	H	331:331	arg1	the 220-residue sequence	cathepsin H		sequence		Cterm	Site	cathepsin H		sequence	The 252-residue sequence of cathepsin B and the 220-residue sequence of cathepsin H were determined largely by automated Edman degradation of their intact polypeptide chains and of the two chains of each enzyme generated by limited proteolysis.
20534510	2	9	part_of	region	333:338	arg1	their prodomain sequences	region		their prodomain sequences						sequences	We show that PDGFs share a conserved region in their prodomain sequences which can remain noncovalently associated with the mature cystine-knot growth factor domain after processing.
3571235	4	1	gly	sialoglycoprotein	624:640	arg1	the major sialoglycoprotein	the major sialoglycoprotein				Fterm		sialoglycoprotein			The amino acid sequence of the intramembranous domain (residues 36-71) of glycophorin B was determined and found to be similar to that of the hydrophobic region of the major sialoglycoprotein (glycophorin A).
3571235	4	1	gly	sialoglycoprotein	624:640	arg1	glycophorin A	glycophorin A				PUBTATOR		glycophorin A	2993		The amino acid sequence of the intramembranous domain (residues 36-71) of glycophorin B was determined and found to be similar to that of the hydrophobic region of the major sialoglycoprotein (glycophorin A).
3840370	13	5	part_of	regions	1700:1706	arg1	C4b-binding protein	protein		regions		Fterm		protein			These regions in C4b-binding protein are homologous with the three internal-homology regions that have been reported to be present within the Ba region of the complement enzyme factor B and also to the internal-homology regions found in the non-complement beta 2-glycoprotein I.
3840370	13	82	part_of	found	1922:1926	arg1	the non-complement beta 2-glycoprotein I AND the internal-homology regions	the non-complement beta 2-glycoprotein I		the internal-homology regions		OGER	Site	beta 2-glycoprotein I	P02749	regions	These regions in C4b-binding protein are homologous with the three internal-homology regions that have been reported to be present within the Ba region of the complement enzyme factor B and also to the internal-homology regions found in the non-complement beta 2-glycoprotein I.
18467335	12	69	gly	PCI	1565:1567	arg1	the N-linked glycans	PCI			the N-linked glycans	OGER		PCI	P05154		These results thus demonstrate that the N-linked glycans and the N-terminal region of blood-derived PCI in different ways affect the cofactor-enhanced rates of thrombin inhibition and provide information on the mechanisms by which this may be achieved.
11152692	4	19	gly	leucine-rich	462:473	arg1	10 leucine-rich repeats			leucine	10 leucine-rich repeats					leucine	It contains a putative propeptide, 4 amino-terminal cysteines, 10 leucine-rich repeats, and 2 C-terminal cysteines.
8702840	6	7	gly	modified	704:711	arg3	NF-H AND O-GlcNAc	NF-H			O-GlcNAc	PUBTATOR		NF-H	4744		Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	6	12	gly	motif	847:851	arg1	the tail domain			the tail domain	the tail domain		Site			domain	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	6	12	gly	motif	847:851	arg1	a region			a region	a region		Site			region	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
3497398	1	83	gly	glycoprotein	213:224	arg1	the human platelet membrane glycoprotein	the human platelet membrane glycoprotein				Fterm		glycoprotein			We report the amino acid sequence of a 299-residue segment from the alpha chain of the human platelet membrane glycoprotein Ib.
26536155	6	5	gly	glycoprotein	1442:1453	arg1	glycoprotein standards	glycoprotein standards				Fterm		glycoprotein			The approach was evaluated on glycoprotein standards and also applied to investigate the glycosylation of human IgG3 providing details on the hitherto uncharacterized glycosylation site Asn392 of the CH3 domain.
26536155	6	38	gly	glycosylation	1501:1513	arg1	human IgG3	human IgG3				PUBTATOR		IgG3	P01860		The approach was evaluated on glycoprotein standards and also applied to investigate the glycosylation of human IgG3 providing details on the hitherto uncharacterized glycosylation site Asn392 of the CH3 domain.
26536155	6	33	gly	glycosylation	1579:1591	arg2	the hitherto uncharacterized glycosylation site Asn392			site Asn392						site Asn392	The approach was evaluated on glycoprotein standards and also applied to investigate the glycosylation of human IgG3 providing details on the hitherto uncharacterized glycosylation site Asn392 of the CH3 domain.
26536155	6	33	gly	glycosylation	1579:1591	arg2	the CH3 domain			domain						domain	The approach was evaluated on glycoprotein standards and also applied to investigate the glycosylation of human IgG3 providing details on the hitherto uncharacterized glycosylation site Asn392 of the CH3 domain.
12731890	6	3	gly	receptor	1261:1268	arg1	the oligosaccharides	receptor			the oligosaccharides	Fterm		receptor			While the pattern of glycosylation is the same for the sites shared by the full-length and the secreted forms of the receptor, the oligosaccharides of the full-length receptor are more extensively processed.
16834341	7	6	gly	Asn52	955:959	arg1	all complex type			Asn52	all complex type					Asn52	Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site.
16834341	7	11	gly	glycoforms	941:950	arg2	Asn52			Asn52						Asn52	Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site.
8404899	3	48	gly	O-glycosylated	541:554	arg1	This protein	protein				Fterm		protein			This protein, which is the only protein in human pancreatic juice which is O-glycosylated and N-glycosylated, was identified as the bile-salt-dependent lipase.
16407218	5	40	gly	lectin	956:961	arg1	carbohydrate recognition domains	lectin			carbohydrate recognition domains	Fterm		lectin			We investigated the mechanism of formation of complexes between alpha2M and MBL and concluded that they form by the direct binding of oligomannose glycans Man(5-7) occupying Asn-846 on alpha2M to the lectin domains (carbohydrate recognition domains) of MBL.
16407218	5	66	gly	MBL	1009:1011	arg1	carbohydrate recognition domains	MBL			carbohydrate recognition domains	PUBTATOR		MBL	4153		We investigated the mechanism of formation of complexes between alpha2M and MBL and concluded that they form by the direct binding of oligomannose glycans Man(5-7) occupying Asn-846 on alpha2M to the lectin domains (carbohydrate recognition domains) of MBL.
14764083	3	23	gly	unglycosylated	598:611	arg1	glycosylated and unglycosylated variants	glycosylated and unglycosylated variants				Fterm		variants			The analysis revealed that recombinant hLF (rhLF) with mutations Ile130-->Thr and Gly404-->Cys was about twofold more susceptible than glycosylated and unglycosylated variants with the naturally occurring Ile130 and Gly404.
14764083	3	66	gly	glycosylated	581:592	arg1	glycosylated and unglycosylated variants	glycosylated and unglycosylated variants				Fterm		variants			The analysis revealed that recombinant hLF (rhLF) with mutations Ile130-->Thr and Gly404-->Cys was about twofold more susceptible than glycosylated and unglycosylated variants with the naturally occurring Ile130 and Gly404.
10644446	7	47	part_of	contain	1046:1052	arg1	ANGPTL3 AND the characteristic calcium binding motif	ANGPTL3		the characteristic calcium binding motif		PUBTATOR	Site	ANGPTL3	27329	motif	ANGPTL3 also does not contain the characteristic calcium binding motif found in the other angiopoietins.
21676880	5	53	part_of	KCNE1	1089:1093	arg1	the KCNE1 post-translational site	KCNE1		the KCNE1 post-translational site		PUBTATOR	Site	KCNE1	3753	site	This long range inhibition is highly specific for post-translational N-glycosylation because mutagenic conversion of the KCNE1 post-translational site into a co-translational site restored both monoglycosylation and anterograde trafficking.
9030779	3	67	gly	N-glycosylation	471:485	arg2	Each N-glycosylation site			Each N-glycosylation site						site	Each N-glycosylation site was modified by site-directed mutagenesis and subsequently expressed in COS-1 cells.
8172892	0	89	part_of	IX	35:36	arg1	Activation peptide	factor IX		Activation peptide		OGER	Site	factor IX	P00740	peptide	Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to threonine residues at 159 and 169.
10066782	2	46	part_of	fibronectin-type	438:453	arg1	two fibronectin-type III (FN III) domains	fibronectin		two fibronectin-type III (FN III) domains		OGER	Site	fibronectin	P02751	domains	The extracellular "soluble" part of the IL-6R (sIL-6R) consists of three domains: an amino-terminal Ig-like domain and two fibronectin-type III (FN III) domains.
16766521	2	48	part_of	receptor	448:455	arg1	the corresponding sequence	receptor		the corresponding sequence		Fterm	Site	receptor		sequence	The receptor possesses a putative N-terminal signal peptide that is believed to be cleaved-off after mediating the endoplasmic reticulum targeting/insertion process, like the corresponding sequence of the homologous CRF(1) receptor.
16766521	2	32	part_of	possesses	238:246	arg1	The receptor AND a putative N-terminal signal peptide	The receptor		a putative N-terminal signal peptide		Fterm	Site	receptor		peptide	The receptor possesses a putative N-terminal signal peptide that is believed to be cleaved-off after mediating the endoplasmic reticulum targeting/insertion process, like the corresponding sequence of the homologous CRF(1) receptor.
18214858	6	3	gly	observed	1202:1209	arg2	this site AND di-fucosylated tetra-antennary N-glycans			this site	di-fucosylated tetra-antennary N-glycans					site	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	6	42	gly	derived	1085:1091	arg2	serum haptoglobin AND fucosylated N-glycans	serum haptoglobin			fucosylated N-glycans	PUBTATOR		haptoglobin	3240		While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	6	45	gly	di-fucosylated	1156:1169	arg1	di-fucosylated tetra-antennary N-glycans				di-fucosylated tetra-antennary N-glycans						While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	6	79	gly	fucosylated	1063:1073	arg1	fucosylated N-glycans				fucosylated N-glycans						While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
30237853	9	36	gly	N-glycopeptides	1618:1632	arg2	56 intact N-glycopeptides			56 intact N-glycopeptides						N-glycopeptides	Importantly, a panel of 56 intact N-glycopeptides perfectly discriminated PCa and BPH (ROC: AUC = 1).
21327254	5	5	gly	sites	884:888	arg1	Tau	Tau			sites	Cterm		Tau			Moreover, analytical difficulties have hampered the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS.
22750213	5	17	part_of	PRiMA	859:863	arg1	the asparagine-43	PRiMA		the asparagine-43		PUBTATOR	SpecificSite	PRiMA	170952	asparagine-43	By using site-directed mutagenesis, the asparagine-43 was identified to be the N-linked glycosylation site of PRiMA.
22750213	5	17	part_of	PRiMA	859:863	arg1	the N-linked glycosylation site	PRiMA		the N-linked glycosylation site		PUBTATOR	Site	PRiMA	170952	site	By using site-directed mutagenesis, the asparagine-43 was identified to be the N-linked glycosylation site of PRiMA.
1533657	5	57	gly	glycosylation	745:757	arg2	a single putative N-linked glycosylation site			a single putative N-linked glycosylation site						site	The secreted part is organized in four short consensus repeats (SCR) and has a single putative N-linked glycosylation site.
7613477	6	91	part_of	LCAT	1342:1345	arg1	the LCAT O-linked glycopeptide	LCAT		the LCAT O-linked glycopeptide		PUBTATOR	Site	LCAT	3931	glycopeptide	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
14970177	3	48	part_of	vIL-6	606:610	arg1	site N89	vIL		site N89		OGER	SpecificSite	vIL	P09327	N89	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
10861210	1	29	gly	N-glycosylated	367:380	arg1	other isoforms	other isoforms				Fterm		isoforms			The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	29	gly	N-glycosylated	367:380	arg1	AE2	AE2				PUBTATOR		AE2	6522		The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	29	gly	N-glycosylated	367:380	arg1	AE3	AE3				PUBTATOR		AE3	6508		The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	71	gly	attached	227:234	arg1	Asn(642) AND a single complex N-linked oligosaccharide			Asn(642)	a single complex N-linked oligosaccharide					Asn(642)	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
24308486	0	29	gly	glycoprotein	108:119	arg1	a heterodimeric glycoprotein	a heterodimeric glycoprotein				Fterm		glycoprotein			Site-specific N-glycosylation analysis of human immunoglobulin e. Immunoglobulin E (IgE) is a heterodimeric glycoprotein involved in antiparasitic and allergic immune reactions.
24308486	0	39	gly	N-glycosylation	14:28	arg1	IgE	IgE				PUBTATOR		IgE	P01854		Site-specific N-glycosylation analysis of human immunoglobulin e. Immunoglobulin E (IgE) is a heterodimeric glycoprotein involved in antiparasitic and allergic immune reactions.
24308486	0	39	gly	N-glycosylation	14:28	arg1	human immunoglobulin e. Immunoglobulin E	human immunoglobulin e. Immunoglobulin E				PUBTATOR		Immunoglobulin E	P01854		Site-specific N-glycosylation analysis of human immunoglobulin e. Immunoglobulin E (IgE) is a heterodimeric glycoprotein involved in antiparasitic and allergic immune reactions.
30659065	2	7	gly	N-glycosylation	331:345	arg1	the N-linked glycans			domain	the N-linked glycans					domain	The isotype/subclass of the antibody, the co-translational N-glycosylation on the CH2 domain, and the remodeling of the N-linked glycans during passage through the ER and Golgi are the known variables within the Fc domain that program antibody effector function.
30659065	2	25	gly	N-glycosylation	331:345	arg1	the CH2 domain			domain						domain	The isotype/subclass of the antibody, the co-translational N-glycosylation on the CH2 domain, and the remodeling of the N-linked glycans during passage through the ER and Golgi are the known variables within the Fc domain that program antibody effector function.
30659065	2	25	gly	N-glycosylation	331:345	arg1	the CH2 domain			domain	the N-linked glycans					domain	The isotype/subclass of the antibody, the co-translational N-glycosylation on the CH2 domain, and the remodeling of the N-linked glycans during passage through the ER and Golgi are the known variables within the Fc domain that program antibody effector function.
22688517	6	59	part_of	LOX-1	1185:1189	arg1	one potential glycosylation site	LOX-1		one potential glycosylation site		PUBTATOR	Site	LOX-1	4973	site	With this approach, one potential glycosylation site of recombinant human LOX-1 on Asn(139) is readily identified and found to carry heterogeneous complex type N-glycans.
7538124	5	23	part_of	K18	808:810	arg1	the major glycosylation sites	K18		the major glycosylation sites		PUBTATOR	Site	K18	3875	sites	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	5	83	part_of	K18	958:960	arg1	the glycopeptides	K18		the glycopeptides		PUBTATOR	Site	K18	3875	glycopeptides	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
15476821	7	45	part_of	DPPX	1005:1008	arg1	the active sites	DPPX		the active sites		PUBTATOR	Site	DPPX	1804	sites	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	7	48	part_of	DPP-IV	1014:1019	arg1	the active sites	DPP-IV		the active sites		PUBTATOR	Site	DPP-IV	1803	sites	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
20507882	1	33	gly	glycosylation	137:149	arg1	the extracellular protein alpha-dystroglycan				the extracellular protein alpha-dystroglycan						The glycosylation of the extracellular protein alpha-dystroglycan is important for its ligand-binding activity, and altered or blocked glycosylation is associated with several forms of congenital muscular dystrophies.
19159218	1	20	gly	glycoprotein	315:326	arg1	glycoprotein	glycoprotein				Fterm		glycoprotein			The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
23431362	3	40	gly	glycan	441:446	arg1	HIV-1 gp120	HIV-1 gp120			glycan	PUBTATOR		HIV-1 gp120	155971		One of these regions (N332) is characterized by an N-linked glycan at residue 332 on HIV-1 gp120 and is recognized by antibody 2G12 and by the recently reported antibodies PGT121-137, the latter isolated from three donors.
23431362	3	51	gly	residue	451:457	arg1	an N-linked glycan			residue 332	an N-linked glycan					residue 332	One of these regions (N332) is characterized by an N-linked glycan at residue 332 on HIV-1 gp120 and is recognized by antibody 2G12 and by the recently reported antibodies PGT121-137, the latter isolated from three donors.
1556128	1	30	gly	glycosylation	92:104	arg1	the mature protein	the mature protein				Fterm		protein			Multiple forms, primary structure, and glycosylation of the mature protein.
1512232	12	62	gly	glycosylation	2060:2072	arg2	All the glycosylation sites			All the glycosylation sites						sites	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
24125761	5	56	gly	deglycosylated	816:829	arg1	deglycosylated proteins	deglycosylated proteins				Fterm		proteins			A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
12096136	4	2	gly	F-spondin	697:705	arg1	the thrombospondin type 1 repeats	F-spondin			the thrombospondin type 1 repeats	PUBTATOR		F-spondin	10418		Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	4	27	gly	repeats	639:645	arg1	peptides			peptides	peptides		Site			peptides	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
2275556	6	32	part_of	Cathepsin	1135:1143	arg1	Cathepsin L polypeptides	Cathepsin L		Cathepsin L polypeptides		PUBTATOR	Site	Cathepsin L	13039	polypeptides	Cathepsin L polypeptides synthesized by quiescent, growing, and transformed cells displayed similar isoelectric focusing patterns, suggesting similar post-translational modification.
2275556	6	103	part_of	L	1145:1145	arg1	Cathepsin L polypeptides	Cathepsin L		Cathepsin L polypeptides		PUBTATOR	Site	Cathepsin L	13039	polypeptides	Cathepsin L polypeptides synthesized by quiescent, growing, and transformed cells displayed similar isoelectric focusing patterns, suggesting similar post-translational modification.
8670172	8	30	gly	found	1274:1278	arg2	two GPI-anchor variants AND Sialic acid	two GPI-anchor variants			Sialic acid	Fterm		variants			Sialic acid linked to an N-acetylhexosamine-galactose arm was found in two GPI-anchor variants.
8670172	8	77	gly	linked	1224:1229	arg2	an N-acetylhexosamine-galactose arm AND Sialic acid			an N-acetylhexosamine-galactose arm	Sialic acid						Sialic acid linked to an N-acetylhexosamine-galactose arm was found in two GPI-anchor variants.
23999306	1	10	gly	glycoproteins	201:213	arg1	many glycoproteins	many glycoproteins				Fterm		glycoproteins			Human β-galactoside α-2,6-sialyltransferase I (ST6Gal-I) establishes the final glycosylation pattern of many glycoproteins by transferring a sialyl moiety to a terminal galactose.
23999306	1	49	gly	α-2,6-sialyltransferase	112:134	arg1	ST6Gal-I	α-2,6-sialyltransferase I			ST6Gal-I	Fterm		α-2,6-sialyltransferase I			Human β-galactoside α-2,6-sialyltransferase I (ST6Gal-I) establishes the final glycosylation pattern of many glycoproteins by transferring a sialyl moiety to a terminal galactose.
23999306	1	69	gly	glycosylation	171:183	arg1	many glycoproteins	many glycoproteins				Fterm		glycoproteins			Human β-galactoside α-2,6-sialyltransferase I (ST6Gal-I) establishes the final glycosylation pattern of many glycoproteins by transferring a sialyl moiety to a terminal galactose.
12096136	5	11	gly	C-mannosylated	850:863	arg1	eight of ten Trp residues			eight of ten Trp residues						Trp residues	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides showed that eight of ten Trp residues in the TSRs of F-spondin are C-mannosylated.
18514042	2	18	gly	glycoproteins	319:331	arg1	abundant serum glycoproteins	abundant serum glycoproteins				Fterm		glycoproteins			In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	2	31	gly	glycosylation	278:290	arg1	abundant serum glycoproteins	abundant serum glycoproteins				Fterm		glycoproteins			In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
25517345	1	41	gly	glycoproteins	90:102	arg1	The glycoproteins	The glycoproteins				Fterm		glycoproteins			The glycoproteins on the surfaces of enveloped viruses, such as HIV, can be considered as a unique target for antiviral therapy.
7306483	3	48	part_of	CNBr	327:330	arg1	four CNBr fragments	CNBr		four CNBr fragments		Cterm	Site	CNBr		fragments	The sequence was completed by analyses of four CNBr fragments obtained from the intact molecule as well as tryptic peptides.
2226797	0	48	gly	variant	64:70	arg1	Carbohydrate structures	tissue plasminogen activator variant			Carbohydrate structures	PUBTATOR		tissue plasminogen activator variant	P00750		Carbohydrate structures of a human tissue plasminogen activator variant expressed in recombinant Chinese hamster ovary cells.
17322565	1	61	part_of	lipase	237:242	arg1	four of five putative N-linked glycosylation sites	endothelial lipase		four of five putative N-linked glycosylation sites		PUBTATOR	Site	endothelial lipase	9388	sites	We previously identified that four of five putative N-linked glycosylation sites of human endothelial lipase (EL) are utilized and suggested that the substitution of asparagine-116 (Asn-116) with alanine (Ala) (N116A) increased the hydrolytic activity of EL.
26859324	8	10	part_of	enzyme	1627:1632	arg1	the membrane-binding domain	enzyme		the membrane-binding domain		Fterm	Site	enzyme		domain	We also observe differential acetylation of COX-2 purified in various detergent systems and nanodiscs, indicating that detergent and lipid binding within the membrane-binding domain of the enzyme alters the rate of the acetylation reaction in vitro.
28973932	5	7	part_of	IPT/TIG	1207:1213	arg1	IPT/TIG domains	IPT		IPT/TIG domains		OGER	Site	IPT	Q9H3H1	domains	In addition, O-Man glycosylation of IPT/TIG domains of plexins and hepatocyte growth factor receptor was not affected in TMTC KO cells, suggesting the existence of yet another O-Man glycosylation machinery.
28973932	5	35	part_of	receptor	1263:1270	arg1	IPT/TIG domains	hepatocyte growth factor receptor		IPT/TIG domains		PUBTATOR	Site	hepatocyte growth factor receptor	4233	domains	In addition, O-Man glycosylation of IPT/TIG domains of plexins and hepatocyte growth factor receptor was not affected in TMTC KO cells, suggesting the existence of yet another O-Man glycosylation machinery.
29992770	11	55	gly	N-glycopeptides	1559:1573	arg2	These N-glycopeptides			These N-glycopeptides						N-glycopeptides	These N-glycopeptides are the lead candidates for validation as future diagnostic modalities of OSCC as early as stage I.
9574531	1	15	part_of	DRA	171:173	arg1	Pro96-->Ser	DRA		Pro96-->Ser		PUBTATOR	AminoAcid	DRA	1811	Pro96	The HLA-DR hemizygous B lymphoblastoid cell line, 10.24.6, has a DRA mutation (Pro96-->Ser) that creates a novel glycosylation site at Asn94.
6725284	1	40	gly	galactoglycoprotein	138:156	arg1	Human plasma galactoglycoprotein	Human plasma galactoglycoprotein				PUBTATOR		galactoglycoprotein	6693		Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
29226084	4	15	gly	N-glycosylation	814:828	arg2	disrupted consensus N-glycosylation site			disrupted consensus N-glycosylation site						site	The N-glycosylation inhibitor tunicamycin reduced the apparent molecular weight of immunoreactivity associated with myc-tagged GPR61 by 1-2 kDa, which was comparable to the evident molecular weight of the myc-tagged N12S GPR61 mutant with disrupted consensus N-glycosylation site.
6725284	7	58	gly	possesses	978:986	arg1	The protein AND approximately 40 hexasaccharides	The protein			approximately 40 hexasaccharides	Fterm		protein			The protein possesses approximately 40 hexasaccharides and 3 tetrasaccharides/mol.
6725284	7	58	gly	possesses	978:986	arg1	The protein AND 3 tetrasaccharides/mol	The protein			3 tetrasaccharides/mol	Fterm		protein			The protein possesses approximately 40 hexasaccharides and 3 tetrasaccharides/mol.
18340083	9	23	gly	N-glycosylation	1212:1226	arg2	the N-glycosylation site			the N-glycosylation site						site	Eliminating the N-glycosylation site in a truncated soluble version of GPIHBP1 causes a modest reduction in the secretion of the protein.
7514386	11	38	gly	glycoprotein	1523:1534	arg1	Try-panosoma brucei variant surface glycoprotein	Try-panosoma brucei variant surface glycoprotein				Fterm		glycoprotein			The backbone structure of the GPI anchor was similar to that of Try-panosoma brucei variant surface glycoprotein, but showed significant variations in its side-chain moieties.
9030779	0	59	gly	N-glycosylation	35:49	arg1	human acid sphingomyelinase	acid sphingomyelinase		sites		PUBTATOR		acid sphingomyelinase	6609	sites	Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis.
14711516	3	43	gly	glycosylation	672:684	arg2	the sites			the sites						sites	The novel isoform of Thy-1 differs from the previously reported chicken isoform by eight amino acid residues, but these changes do not alter the secondary structure content, the disulfide bond pattern, or the sites of glycosylation.
12122212	2	24	gly	glycoprotein	299:310	arg1	the EBV glycoprotein gp350/220	the EBV glycoprotein gp350/220				Fterm		glycoprotein			The N-terminal two short consensus repeats (SCR1-SCR2) of the receptor interact with the EBV glycoprotein gp350/220 and also with the natural CD21 ligand C3d.
12122212	2	28	gly	receptor	268:275	arg1	The N-terminal two short consensus repeats	receptor			The N-terminal two short consensus repeats	Fterm		receptor			The N-terminal two short consensus repeats (SCR1-SCR2) of the receptor interact with the EBV glycoprotein gp350/220 and also with the natural CD21 ligand C3d.
8702840	8	38	part_of	subunit	1332:1338	arg1	both head and tail domains	subunit		both head and tail domains		Fterm	Site	subunit		domains	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
27391701	9	42	part_of	protein	1555:1561	arg1	short protein binding regions	protein		short protein binding regions		Fterm	Site	protein		regions	Accordingly, IDPs were highly enriched in short protein binding regions called Molecular Recognition Features (MoRFs).
2514791	2	81	gly	N-glycosylation	230:244	arg2	four potential N-glycosylation sites			four potential N-glycosylation sites						sites	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	2	31	gly	I	288:288	arg1	Asn-117			Asn-117, -184, and -448						Asn-117, -184, and -448	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	2	31	gly	I	288:288	arg1	-184			Asn-117, -184, and -448						Asn-117, -184, and -448	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	2	31	gly	I	288:288	arg1	-184			Asn-117, -184, and -448						Asn-117, -184, and -448	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	2	35	gly	two	320:322	arg1	-448			Asn-117 and -448						Asn-117 and -448	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
20837704	2	34	part_of	EGFR	398:401	arg1	the extracellular domain	EGFR dimerized		the extracellular domain		PUBTATOR	Site	EGFR dimerized	1956	domain	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
15628971	6	51	gly	attached	1280:1287	arg1	C4ST-1 AND N-linked oligosaccharides	C4ST-1			N-linked oligosaccharides	PUBTATOR		C4ST-1	314694		These observations strongly suggest that N-linked oligosaccharides attached to C4ST-1 contribute to the production and stability of the active form of C4ST-1.
11703926	6	14	gly	region	821:826	arg1	potential surface determinants			region	potential surface determinants					region	Based on the structure, we have identified potential surface determinants of Eph/ephrin binding specificity and a ligand dimerization region.
9883900	8	41	gly	O-glycosylated	1224:1237	arg1	Thr-152			Thr-152						Thr-152	According to mass spectrometric and sequence analysis, Thr-152 was shown to be O-glycosylated.
21733844	3	29	gly	glycosylated	465:476	arg1	the protein	protein		Asn-133		Fterm		protein		Asn-133	Here we overproduced hAQP10 in the yeast Pichia pastoris and observed that the protein is glycosylated at Asn-133 in the extracellular loop C.
8615697	3	97	gly	glycosylation	509:521	arg2	these confirmed sites			these confirmed sites						sites	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
2403553	12	8	gly	chains	1734:1739	arg1	the receptor	receptor			chains	Fterm		receptor			The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	12	98	gly	oligosaccharides	1824:1839	arg1	receptors	receptors			oligosaccharides	Fterm		receptors			The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
15504740	6	30	gly	glycosylation	1147:1159	arg2	exogenous asparagine-linked glycosylation sites			exogenous asparagine-linked glycosylation sites						sites	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Arg-63			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Ala-81			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Lys-4			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-67			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-414			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	His-72			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-453			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-423			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Ala-81			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Lys-4			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-67			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-414			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	His-72			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-453			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-423			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Lys-4			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-67			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-414			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	His-72			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-453			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-423			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-67			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-414			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	His-72			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-453			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-423			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-414			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	His-72			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-453			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-423			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	His-72			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-453			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-423			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-453			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-423			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
15504740	6	30	gly	glycosylation	1147:1159	arg2	Tyr-423			Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453						Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453	We then introduced exogenous asparagine-linked glycosylation sites at Lys-4, Pro-37, Arg-63, Tyr-67, His-72, Ala-81, Tyr-414, Tyr-423, and Tyr-453 to define the transmembrane domain borders.
20696930	3	22	part_of	HER2	413:416	arg1	The 58 amino acid residue	HER2		The 58 amino acid residue		PUBTATOR	Site	HER2	2064	residue	The 58 amino acid residue Zher2 affibody molecule was previously engineered as a high-affinity binder of HER2.
20427278	0	75	gly	glycosylation	52:64	arg1	the amyloid precursor protein	the amyloid precursor protein				OGER		amyloid precursor protein	P05067		The novel membrane protein TMEM59 modulates complex glycosylation, cell surface expression, and secretion of the amyloid precursor protein.
1457969	5	43	gly	present	877:883	arg1	hTSH AND The N-glycans	hTSH			The N-glycans	OGER		hTSH			The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	5	43	gly	present	877:883	arg2	hTSH AND diantennary complex-type structures	hTSH			diantennary complex-type structures	OGER		hTSH			The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
14749323	8	5	gly	glycosylation	1484:1496	arg1	individual sites	OAT		sites		OGER		OAT	P04181	sites	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	8	5	gly	glycosylation	1484:1496	arg2	individual sites	OAT		sites		OGER		OAT	P04181	sites	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	8	5	gly	glycosylation	1484:1496	arg2	individual sites			sites						sites	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
7727388	0	23	part_of	homodimer	91:99	arg1	glycosylation sites	natriuretic peptide receptor-C homodimer		glycosylation sites		PUBTATOR	Site	natriuretic peptide receptor-C homodimer	4883	sites	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
24530628	4	42	gly	glycoproteins	484:496	arg1	model glycoproteins	model glycoproteins				Fterm		glycoproteins			Several lines of evidence using model glycoproteins suggest that our method is based on the different solubility between non-glycosylated and glycosylated peptides in acetone.
24530628	4	67	gly	glycosylated	588:599	arg1	glycosylated peptides			glycosylated peptides						peptides	Several lines of evidence using model glycoproteins suggest that our method is based on the different solubility between non-glycosylated and glycosylated peptides in acetone.
17018531	4	9	gly	glycosylated	620:631	arg1	glycosylated isoforms	glycosylated isoforms				Fterm		isoforms			Highly purified NPC2 consists of a complex mixture of glycosylated isoforms, similar to that observed in human brain autopsy specimens.
22040171	3	41	gly	glycosylation	612:624	arg2	4 glycosylation sites			4 glycosylation sites						sites	Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry MALDI-TOF MS analysis of the zymogen (47.7 kDa) treated with peptide-N-glycosidase F (PNGase F) identified 4 glycosylation sites, and acid cleavage of the zymogen into α- and β-subunits (14.6 and 33.3 kDa) activated the enzyme.
15807535	7	77	gly	glycosylated	1346:1357	arg1	the glycosylated ABCG2 protein	the glycosylated ABCG2 protein				PUBTATOR		ABCG2 protein	Q9UNQ0		Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
20534510	5	46	part_of	PDGF	843:846	arg1	the PDGF propeptides	PDGF		the PDGF propeptides		OGER	Site	PDGF		propeptides	The PDGF-B:PDGFRbeta interface is predominantly hydrophobic, and PDGFRs and the PDGF propeptides occupy overlapping positions on mature PDGFs, rationalizing the need of propeptides by PDGFs to cover functionally important hydrophobic surfaces during secretion.
23662732	4	28	gly	glycopeptides	689:701	arg2	glycopeptides			glycopeptides						glycopeptides	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
10715549	6	2	part_of	LHbeta	1240:1245	arg1	The carboxy-terminal regions	LHbeta		The carboxy-terminal regions		PUBTATOR	Site	LHbeta	3972	regions	The carboxy-terminal regions of neither LHbeta nor CGbeta were associated with their aggregation.
10715549	6	48	part_of	CGbeta	1251:1256	arg1	The carboxy-terminal regions	CGbeta		The carboxy-terminal regions		PUBTATOR	Site	CGbeta	1082	regions	The carboxy-terminal regions of neither LHbeta nor CGbeta were associated with their aggregation.
12743029	4	15	part_of	EGF-like	638:645	arg1	a Ca(2+)-binding EGF-like domain	EGF		a Ca(2+)-binding EGF-like domain		PUBTATOR	Site	EGF	1950	domain	MASPs have a modular structure consisting of an N-terminal CUB domain, a Ca(2+)-binding EGF-like domain, a second CUB domain, two complement control protein modules and a C-terminal serine protease domain.
7525874	6	64	gly	1,6-fucosylated	843:857	arg1	The innermost N-acetylglucosamine residues				The innermost N-acetylglucosamine residues						The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
10022822	4	5	part_of	p41	629:631	arg1	the p41 fragment	structure of the p41		the p41 fragment		PUBTATOR	Site	structure of the p41	2035	fragment	The structure of the p41 fragment demonstrates a novel fold, consisting of two subdomains, each stabilized by disulfide bridges.
12911312	5	53	gly	O-glycosylated	671:684	arg1	Threonine 346			Threonine 346						Threonine 346	Threonine 346 was variably O-glycosylated.
1885588	5	44	part_of	enzyme	913:918	arg1	the active site	enzyme		the active site		Fterm	Site	enzyme		site	This domain appeared to contain the active site of the enzyme and had the ability to bind to glucosidase I-specific affinity gel.
1885588	5	27	part_of	contain	882:888	arg1	This domain AND the active site	This domain		the active site						site	This domain appeared to contain the active site of the enzyme and had the ability to bind to glucosidase I-specific affinity gel.
10441114	4	70	part_of	collagen	666:673	arg1	noncollagenous domain 1	collagen XVIII		noncollagenous domain 1		PUBTATOR	Site	collagen XVIII	80781	domain	lacking the last and final three residues of the noncollagenous domain 1 (NC-1) of collagen XVIII, respectively.
16964247	1	20	part_of	site	197:200	arg1	p53	p53		site		PUBTATOR	Site	p53	7157	site	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood.
24103369	6	40	gly	sialylation	1000:1010	arg1	all glycopeptides			all glycopeptides						glycopeptides	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	6	85	gly	fucosylated	1047:1057	arg1	the fucosylated structure				the fucosylated structure						The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	6	86	gly	glycopeptides	1076:1088	arg1	the sialylation			glycopeptides	the sialylation					glycopeptides	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	6	86	gly	glycopeptides	1076:1088	arg1	the fucosylated structure			glycopeptides	the fucosylated structure					glycopeptides	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
30312582	1	29	gly	glycoprotein	165:176	arg1	a 98-kDa type 1 transmembrane glycoprotein	a 98-kDa type 1 transmembrane glycoprotein				Fterm		glycoprotein			Our group originally found and cloned cDNA for a 98-kDa type 1 transmembrane glycoprotein of unknown function.
14970177	3	7	gly	glycosylation	577:589	arg1	site N89			N89						N89	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
17395589	0	38	gly	O-fucosylation	0:13	arg1	ADAMTS13 secretion	ADAMTS13 secretion				PUBTATOR		ADAMTS13	11093		O-fucosylation is required for ADAMTS13 secretion.
3427055	9	6	part_of	Gla	1442:1444	arg1	Gla domain	Gla		Gla domain		OGER	Site	Gla	P06280	domain	As observed for cytoplasmic EF-hand-containing proteins and for Gla domain containing proteins, a major conformational transition is induced in BM-40 upon binding of several Ca2+ ions.
8344280	11	45	part_of	peptide	1670:1676	arg1	position 4	peptide		position 4						position 4,	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	11	52	part_of	interferon-beta	1687:1701	arg1	an 11-amino-acid peptide	interferon-beta		an 11-amino-acid peptide		PUBTATOR	Site	interferon-beta	3456	peptide	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	11	104	part_of	position	1706:1713	arg1	human interferon-beta	interferon-beta		position		PUBTATOR	Site	interferon-beta	3456	position 4,	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
24766575	3	4	gly	N-glycopeptide	649:662	arg2	N-glycopeptide spectra			N-glycopeptide spectra						N-glycopeptide	We performed an extensive validation and a high-throughput N-glycosylation study on serum and identified thousands of N-glycopeptide spectra with high confidence.
16763549	3	40	gly	NRP1	501:504	arg1	proteoglycan	NRP1			proteoglycan	OGER		NRP1	O14786		Here we show that a substantial fraction of NRP1 is proteoglycan modified with either heparan sulfate or chondroitin sulfate on a single conserved Ser.
16763549	3	44	gly	proteoglycan	509:520	arg1	a single conserved Ser			a single conserved Ser	a single conserved Ser		AminoAcid			Ser	Here we show that a substantial fraction of NRP1 is proteoglycan modified with either heparan sulfate or chondroitin sulfate on a single conserved Ser.
7477400	3	25	gly	glycoproteins	599:611	arg1	class II histocompatibility glycoproteins	class II histocompatibility glycoproteins				Fterm		glycoproteins			The structure shows that the CLIP fragment binds to DR3 in a way almost identical to that in which antigenic peptides bind class II histocompatibility glycoproteins.
17157876	7	55	part_of	sites	1591:1595	arg1	the membrane-anchored CPM	CPM		sites		OGER	Site	CPM	P14384	sites	Three Thr residues at the distal TT edge of CPN1 are O-linked to N-acetyl glucosamine sugars; equivalent sites in the membrane-anchored CPM are occupied by basic residues probably involved in membrane interaction.
8344946	5	11	part_of	sites	875:879	arg1	NF-L	NF-L		sites		PUBTATOR	Site	NF-L	4747	sites	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	5	11	part_of	sites	875:879	arg1	NF-M	NF-M		sites		PUBTATOR	Site	NF-M	4741	sites	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
23187000	5	44	gly	glycosylation	880:892	arg1	TIMP-1	TIMP-1				PUBTATOR		TIMP-1	7076		Because the TIMP-1 glycosylation participate in the interaction, aberrant glycosylation of TIMP-1 presumably affects the interaction, thereby leading to pathogenic dysfunction in cancer cells.
14699159	2	11	part_of	contains	413:420	arg1	a 90-kDa ER transmembrane protein AND three evolutionarily conserved N-linked glycosylation sites	a 90-kDa ER transmembrane protein		three evolutionarily conserved N-linked glycosylation sites		Fterm	Site	protein		sites	ATF6, a 90-kDa ER transmembrane protein, contains three evolutionarily conserved N-linked glycosylation sites within its carboxyl luminal domain.
14699159	2	11	part_of	contains	413:420	arg1	ATF6 AND three evolutionarily conserved N-linked glycosylation sites	ATF6		three evolutionarily conserved N-linked glycosylation sites		PUBTATOR	Site	ATF6	22926	sites	ATF6, a 90-kDa ER transmembrane protein, contains three evolutionarily conserved N-linked glycosylation sites within its carboxyl luminal domain.
17980170	11	9	gly	N-glycosylation	1396:1410	arg2	six potential N-glycosylation sites			six potential N-glycosylation sites						sites	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	11	51	gly	N-glycosylation	1281:1295	arg2	N-glycosylation sites	NAAA		sites		PUBTATOR		NAAA	27163	sites	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
12218058	8	23	part_of	BMP-1	1413:1417	arg1	the CUB domains	BMP-1		the CUB domains		PUBTATOR	Site	BMP-1	649	domains	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	8	64	part_of	sites	1385:1389	arg1	BMP-1	BMP-1		sites		PUBTATOR	Site	BMP-1	649	sites	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
26598643	4	23	gly	O-glycosylation	579:593	arg1	human blood plasma glycoproteins	human blood plasma glycoproteins				Fterm		glycoproteins			Here, we report on the site-specific O-glycosylation analysis of human blood plasma glycoproteins.
26598643	4	31	gly	glycoproteins	626:638	arg1	human blood plasma glycoproteins	human blood plasma glycoproteins				Fterm		glycoproteins			Here, we report on the site-specific O-glycosylation analysis of human blood plasma glycoproteins.
7620335	1	11	gly	residues	274:281	arg1	two O-linked oligosaccharides			Thr17 and Thr29 residues	two O-linked oligosaccharides					Thr17 and Thr29 residues	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	11	gly	residues	274:281	arg1	two N-linked oligosaccharides			Thr17 and Thr29 residues	two N-linked oligosaccharides					Thr17 and Thr29 residues	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	14	gly	residues	212:219	arg1	two O-linked oligosaccharides			Asn39 and Asn49 residues	two O-linked oligosaccharides					Asn39 and Asn49 residues	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	14	gly	residues	212:219	arg1	two N-linked oligosaccharides			Asn39 and Asn49 residues	two N-linked oligosaccharides					Asn39 and Asn49 residues	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	59	gly	has	159:161	arg1	Human blood coagulation factor X AND two N-linked oligosaccharides	Human blood coagulation factor X			two N-linked oligosaccharides	OGER		factor X	P00742		Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	59	gly	has	159:161	arg1	Human blood coagulation factor X AND two O-linked oligosaccharides	Human blood coagulation factor X			two O-linked oligosaccharides	OGER		factor X	P00742		Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
32366695	3	35	gly	SARS-CoV-2	356:365	arg1	22 N-linked glycan sequons	SARS			22 N-linked glycan sequons	OGER		SARS	P49591		SARS-CoV-2 S gene encodes 22 N-linked glycan sequons per protomer, which likely play a role in protein folding and immune evasion.
25187573	0	78	gly	glycopeptide	105:116	arg2	site-specific glycopeptide analysis			site-specific glycopeptide analysis						glycopeptide	The O-glycomap of lubricin, a novel mucin responsible for joint lubrication, identified by site-specific glycopeptide analysis.
11447134	9	4	gly	glycosylated	1191:1202	arg1	peptide			peptide						peptide	Carbohydrate structures were calculated from the mass difference between glycosylated and deglycosylated peptide.
9295302	8	82	part_of	sites	1356:1360	arg1	MRP	MRP		sites		PUBTATOR	Site	MRP	4363	sites	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
16445295	6	5	part_of	found	972:976	arg1	an unglycosylated variant AND Asn219	an unglycosylated variant		Asn219		Fterm	AminoAcid	variant		Asn219	Asn219 was also found in an unglycosylated variant.
21712440	7	4	gly	glycosylation	1498:1510	arg1	the Aβ1-38/40/42 isoforms	the Aβ1-38/40/42 isoforms				Fterm		isoforms			We could not detect any glycosylation of the Aβ1-38/40/42 isoforms.
7688323	1	17	gly	glycoprotein	247:258	arg1	platelet glycoprotein IIb	platelet glycoprotein IIb				Fterm		glycoprotein			The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
25153361	1	11	gly	glycosylation	139:151	arg2	several sites			several sites						sites	A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
25153361	1	28	gly	glycoprotein	97:108	arg1	A glycoprotein	A glycoprotein				Fterm		glycoprotein			A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
9405696	1	33	part_of	form	317:320	arg1	the SH3 domain	form of Src		the SH3 domain		PUBTATOR	Site	form of Src	20779	domain	We have isolated a novel cDNA, that appears to represent a new class of ion channels, by using the yeast two-hybrid system and the SH3 domain of the neural form of Src (N-src) as a bait.
8026573	0	31	gly	glycoprotein	99:110	arg1	the carbohydrate chains	glycoprotein			the carbohydrate chains	Fterm		glycoprotein			Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein.
11152692	2	4	gly	leucine-rich	177:188	arg1	the leucine-rich repeat family			leucine	the leucine-rich repeat family					leucine	Asporin, a novel member of the leucine-rich repeat family of proteins, was partially purified from human articular cartilage and meniscus.
23376777	6	13	gly	N360	1139:1142	arg1	Endo H-sensitive, high mannose-containing structures			N312 and N360 sites	Endo H-sensitive, high mannose-containing structures					N312 and N360 sites	Our data suggest that the glycan moieties at the N331 and N344 sites were Endo H-resistant, complex-form structures, and that the N312 and N360 sites were Endo H-sensitive, high mannose-containing structures.
23376777	6	17	gly	N312	1130:1133	arg1	Endo H-sensitive, high mannose-containing structures			N312 and N360 sites	Endo H-sensitive, high mannose-containing structures					N312 and N360 sites	Our data suggest that the glycan moieties at the N331 and N344 sites were Endo H-resistant, complex-form structures, and that the N312 and N360 sites were Endo H-sensitive, high mannose-containing structures.
23376777	6	56	gly	sites	1063:1067	arg1	the glycan moieties			N331 and N344 sites	the glycan moieties					N331 and N344 sites	Our data suggest that the glycan moieties at the N331 and N344 sites were Endo H-resistant, complex-form structures, and that the N312 and N360 sites were Endo H-sensitive, high mannose-containing structures.
23376777	6	56	gly	sites	1063:1067	arg1	Endo H-resistant, complex-form structures			N331 and N344 sites	Endo H-resistant, complex-form structures					N331 and N344 sites	Our data suggest that the glycan moieties at the N331 and N344 sites were Endo H-resistant, complex-form structures, and that the N312 and N360 sites were Endo H-sensitive, high mannose-containing structures.
20378933	6	5	gly	glycosylation	736:748	arg2	glycosylation site			glycosylation site						site	To identify which glycosylation site is responsible for increased IgA binding, we performed site-directed mutagenesis at each N-linked glycosylation site by changing asparagine to glutamine.
20378933	6	38	gly	glycosylation	853:865	arg2	each N-linked glycosylation site			each N-linked glycosylation site						site	To identify which glycosylation site is responsible for increased IgA binding, we performed site-directed mutagenesis at each N-linked glycosylation site by changing asparagine to glutamine.
12911312	1	28	part_of	cysteine	283:290	arg1	an extracellular glycoprotein	glycoprotein		cysteine		Fterm	AminoAcid	glycoprotein		cysteine	Rat selenoprotein P is an extracellular glycoprotein of 366 amino acid residues that is rich in cysteine and selenocysteine.
12911312	1	28	part_of	cysteine	283:290	arg1	Rat selenoprotein P	Rat selenoprotein P		cysteine		PUBTATOR	AminoAcid	Rat selenoprotein P	29360	cysteine	Rat selenoprotein P is an extracellular glycoprotein of 366 amino acid residues that is rich in cysteine and selenocysteine.
1533633	2	78	gly	glycosylation	331:343	arg2	the sites			the sites						sites	We have identified the sites of N-linked glycosylation and oligosaccharide phosphorylation on the alpha-subunit of beta-hexosaminidase and have determined the influence of the oligosaccharides on the folding and transport of the enzyme.
23319596	10	10	gly	hLOXL2	1578:1583	arg1	the N-glycan at Asn-644	hLOXL2			the N-glycan at Asn-644	PUBTATOR		hLOXL2	4017		These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.
16476442	0	0	part_of	enzyme	76:81	arg1	the N domain	angiotensin I-converting enzyme		the N domain		PUBTATOR	Site	angiotensin I-converting enzyme	183	domain	Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design.
7607222	7	67	gly	glycosylation	1019:1031	arg2	the same site			the same site						site	They all were from the same site of glycosylation (Thr5) and displayed the same core 2 structure: GlcNAc(beta 1-6)[Gal(beta 1-3)]GalNAc alpha-.
16321355	5	21	gly	glycopeptide	980:991	arg2	glycopeptide			glycopeptide						glycopeptide	Oligosaccharide composition was deduced from the molecular weight calculated from the observed mass of the glycopeptide and theoretical mass of the peptide.
6966283	3	52	gly	has	143:145	arg1	Human alpha 1-protease inhibitor AND three oligosaccharide side chains	Human alpha 1-protease inhibitor			three oligosaccharide side chains	PUBTATOR		Human alpha 1-protease inhibitor	5265		Human alpha 1-protease inhibitor has three oligosaccharide side chains attached to 3 separate asparaginyl residues of the protein by N-glycosyl linkages.
6966283	3	30	gly	attached	181:188	arg1	3 separate asparaginyl residues AND three oligosaccharide side chains	protein		residues	three oligosaccharide side chains	Fterm		protein		residues	Human alpha 1-protease inhibitor has three oligosaccharide side chains attached to 3 separate asparaginyl residues of the protein by N-glycosyl linkages.
20881961	6	45	part_of	homodimer	1296:1304	arg1	the top face	Sema6A homodimer		the top face		PUBTATOR	Site	Sema6A homodimer	57556	face	In contrast, the structure of the Sema6A-PlxnA2 signalling complex revealed a 2:2 heterotetramer in which the two PlxnA2 monomers dissociated from one another and docked onto the top face of the Sema6A homodimer using the same interface as the head-on homodimer, indicating that plexins undergo 'partner exchange'.
9822688	10	15	part_of	have	1257:1260	arg1	PTL AND similar active sites	PTL		similar active sites		PUBTATOR	Site	PTL	25702	sites	Although PTL and rPLRP2 have similar active sites, rPLRP2 has a broader substrate specificity that we confirmed using a monolayer technique.
9822688	10	15	part_of	have	1257:1260	arg1	rPLRP2 AND similar active sites	rPLRP2		similar active sites		PUBTATOR	Site	rPLRP2	117554	sites	Although PTL and rPLRP2 have similar active sites, rPLRP2 has a broader substrate specificity that we confirmed using a monolayer technique.
3463996	3	64	part_of	residues	691:698	arg1	mature (single chain) cathepsin B	cathepsin B		residues		PUBTATOR	AminoAcid	cathepsin B	1508	residues in	The nucleotide sequences predict that the primary structure of preprocathepsin B contains 339 amino acids organized as follows: a 17-residue NH2-terminal prepeptide sequence followed by a 62-residue propeptide region, 254 residues in mature (single chain) cathepsin B, and a 6-residue extension at the COOH terminus.
3463996	3	90	part_of	terminus	776:783	arg1	254 residues	terminus		254 residues						residues in	The nucleotide sequences predict that the primary structure of preprocathepsin B contains 339 amino acids organized as follows: a 17-residue NH2-terminal prepeptide sequence followed by a 62-residue propeptide region, 254 residues in mature (single chain) cathepsin B, and a 6-residue extension at the COOH terminus.
3463996	3	90	part_of	terminus	776:783	arg1	a 62-residue propeptide region	terminus		a 62-residue propeptide region						region	The nucleotide sequences predict that the primary structure of preprocathepsin B contains 339 amino acids organized as follows: a 17-residue NH2-terminal prepeptide sequence followed by a 62-residue propeptide region, 254 residues in mature (single chain) cathepsin B, and a 6-residue extension at the COOH terminus.
11676606	4	9	gly	glycosylation	544:556	arg2	asparagine 240			asparagine 240						asparagine 240	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
11676606	4	9	gly	glycosylation	544:556	arg2	a single N-linked glycosylation site			a single N-linked glycosylation site						site	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
24103369	5	19	gly	glycopeptide	863:874	arg2	the glycopeptide			the glycopeptide						glycopeptide	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	60	gly	present	927:933	arg2	each glycopeptide AND glycans			each glycopeptide	glycans					glycopeptide	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	91	gly	glycopeptide	943:954	arg2	each glycopeptide			each glycopeptide						glycopeptide	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
21569239	8	34	part_of	found	1130:1134	arg2	mindin AND The integrin-binding motif	mindin		The integrin-binding motif		PUBTATOR	Site	mindin	10417	motif	The integrin-binding motif found in mindin is not conserved in the F-spondin FS domain.
21569239	8	51	part_of	F-spondin	1170:1178	arg1	the F-spondin FS domain	F-spondin		the F-spondin FS domain		PUBTATOR	Site	F-spondin	10418	domain	The integrin-binding motif found in mindin is not conserved in the F-spondin FS domain.
7841792	2	55	gly	glycosylated	383:394	arg1	heavily glycosylated domains			heavily glycosylated domains						domains	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7683678	7	29	gly	N-glycosylation	1014:1028	arg2	one N-glycosylation site			one N-glycosylation site						site	It was susceptible to treatment with N-glycanase, and one N-glycosylation site was identified.
3877053	5	5	part_of	XII	662:664	arg1	the complete amino acid sequence	factor XII		the complete amino acid sequence		OGER	Site	factor XII	P00748	sequence	DNA sequence analysis of these overlapping clones showed that they contained DNA coding for part of an amino-terminal extension, the complete amino acid sequence of plasma factor XII, a TGA stop codon, a 3' untranslated region of 150 nucleotides, and a poly(A)+ tail.
3877053	5	5	part_of	XII	662:664	arg1	tail	factor XII		tail		OGER	Site	factor XII	P00748	tail	DNA sequence analysis of these overlapping clones showed that they contained DNA coding for part of an amino-terminal extension, the complete amino acid sequence of plasma factor XII, a TGA stop codon, a 3' untranslated region of 150 nucleotides, and a poly(A)+ tail.
3877053	5	5	part_of	XII	662:664	arg1	a 3' untranslated region	factor XII		a 3' untranslated region		OGER	Site	factor XII	P00748	region	DNA sequence analysis of these overlapping clones showed that they contained DNA coding for part of an amino-terminal extension, the complete amino acid sequence of plasma factor XII, a TGA stop codon, a 3' untranslated region of 150 nucleotides, and a poly(A)+ tail.
23209641	3	20	gly	glycosylation	547:559	arg1	the lysine residues	adiponectin		lysine residues		PUBTATOR		adiponectin	Q15848	lysine residues	Hydroxylation and, especially, glycosylation of the lysine residues of adiponectin have been shown to be essential for the formation of the more active high molecular weight adiponectin oligomers and thus for its function.
7107587	2	85	gly	fibrinogen	149:158	arg1	The carbohydrate composition	fibrinogen			The carbohydrate composition	PUBTATOR		fibrinogen	2244		The carbohydrate composition of fibrinogen and constituent S-carboxymethylated chains was determined.
12151713	5	21	gly	present	894:900	arg1	maize recombinant lactoferrin AND complex-type glycans	lactoferrin			complex-type glycans	OGER		lactoferrin	P02788		The results indicated that both N-glycosylation sites of recombinant lactoferrin are mainly substituted by typical plant paucimannose-type glycans, with beta1,2-xylose and alpha1,3-linked fucose at the proximal N-acetylglucosamine, and that complex-type glycans with Lewis(a) determinants are not present in maize recombinant lactoferrin.
12151713	5	20	gly	N-glycosylation	629:643	arg2	both N-glycosylation sites	lactoferrin		sites		OGER		lactoferrin	P02788	sites	The results indicated that both N-glycosylation sites of recombinant lactoferrin are mainly substituted by typical plant paucimannose-type glycans, with beta1,2-xylose and alpha1,3-linked fucose at the proximal N-acetylglucosamine, and that complex-type glycans with Lewis(a) determinants are not present in maize recombinant lactoferrin.
7925474	4	8	gly	glycosylated	603:614	arg1	up to ten O-glycosylation and N-glycosylation sites			up to ten O-glycosylation and N-glycosylation sites						sites	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	4	56	gly	N-glycosylation	548:562	arg2	up to ten O-glycosylation and N-glycosylation sites			up to ten O-glycosylation and N-glycosylation sites						sites	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7780197	0	45	gly	glycosylation	13:25	arg1	human transferrin receptor	transferrin receptor		site		PUBTATOR		transferrin receptor	7037	site	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	0	65	gly	contains	62:69	arg1	human transferrin receptor AND a high-mannose oligosaccharide	transferrin receptor		site	a high-mannose oligosaccharide	PUBTATOR		transferrin receptor	7037	site	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
11738084	2	53	gly	Redhill	287:293	arg1	-1 Arg			-1 Arg						Arg	We have determined the structure of the glycan bound to the double-mutant albumin Redhill (-1 Arg, 320 Ala-->Thr).
11738084	2	53	gly	Redhill	287:293	arg1	320 Ala-->Thr			320 Ala-->Thr						Ala	We have determined the structure of the glycan bound to the double-mutant albumin Redhill (-1 Arg, 320 Ala-->Thr).
10814696	0	29	gly	fucosylated	81:91	arg1	High-mannose-type oligosaccharides				High-mannose-type oligosaccharides						High-mannose-type oligosaccharides from human placental arylsulfatase A are core fucosylated as confirmed by MALDI MS. Despite numerous studies on arylsulfatase A, the structure of its glycans is not well understood.
10814696	0	30	gly	A	70:70	arg1	High-mannose-type oligosaccharides	arylsulfatase A			High-mannose-type oligosaccharides	PUBTATOR		arylsulfatase A	410		High-mannose-type oligosaccharides from human placental arylsulfatase A are core fucosylated as confirmed by MALDI MS. Despite numerous studies on arylsulfatase A, the structure of its glycans is not well understood.
12391027	3	47	part_of	contains	597:604	arg1	The front face AND the "recognition" face	The front face		the "recognition" face						face	The front face of the TSR contains a right-handed spiral, positively charged groove that might be the "recognition" face, mediating interactions with various ligands.
10978165	7	6	gly	position	768:775	arg1	the disaccharide N-acetylgalactosamine galactose			position 7	the disaccharide N-acetylgalactosamine galactose					position 7	Glycosylated HCC-1 exhibits a molecular mass of 9621 Da due to O-glycosylation at position 7 (Ser-7) with two N-acetylneuraminic acids and the disaccharide N-acetylgalactosamine galactose.
10978165	7	49	gly	O-glycosylation	749:763	arg2	position 7			position 7						position 7	Glycosylated HCC-1 exhibits a molecular mass of 9621 Da due to O-glycosylation at position 7 (Ser-7) with two N-acetylneuraminic acids and the disaccharide N-acetylgalactosamine galactose.
10978165	7	49	gly	O-glycosylation	749:763	arg2	Ser-7			Ser-7						Ser-7	Glycosylated HCC-1 exhibits a molecular mass of 9621 Da due to O-glycosylation at position 7 (Ser-7) with two N-acetylneuraminic acids and the disaccharide N-acetylgalactosamine galactose.
17360426	0	0	part_of	receptors	83:91	arg1	the extracellular regions	receptors		the extracellular regions		Fterm	Site	receptors		regions	Structures of the extracellular regions of the group II/III metabotropic glutamate receptors.
26563299	7	0	gly	N-glycosylation	1091:1105	arg2	The two potential IL-15 N-glycosylation sites			The two potential IL-15 N-glycosylation sites						sites	The two potential IL-15 N-glycosylation sites (Asn71 and Asn112) located at the IL-2 receptor interface were unoccupied.
26563299	7	82	gly	sites	1107:1111	arg1	The two potential IL-15 N-glycosylation sites			The two potential IL-15 N-glycosylation sites						sites	The two potential IL-15 N-glycosylation sites (Asn71 and Asn112) located at the IL-2 receptor interface were unoccupied.
26563299	7	0	gly	N-glycosylation	1091:1105	arg2	Asn71			Asn71 and Asn112						Asn71 and Asn112	The two potential IL-15 N-glycosylation sites (Asn71 and Asn112) located at the IL-2 receptor interface were unoccupied.
26563299	7	82	gly	sites	1107:1111	arg1	Asn112			Asn71 and Asn112						Asn71 and Asn112	The two potential IL-15 N-glycosylation sites (Asn71 and Asn112) located at the IL-2 receptor interface were unoccupied.
28753425	3	41	part_of	rhodopsin	559:567	arg1	the phosphorylated C terminus	rhodopsin		the phosphorylated C terminus		PUBTATOR	Site	rhodopsin	6010	terminus	Here, we report an X-ray free electron laser (XFEL) crystal structure of the rhodopsin-arrestin complex, in which the phosphorylated C terminus of rhodopsin forms an extended intermolecular β sheet with the N-terminal β strands of arrestin.
9501082	8	0	part_of	alpha6	1107:1112	arg1	RGD peptide	alpha6		RGD peptide		Cterm	Site	alpha6		peptide	Adhesion to M2BP was inhibited by antibodies to integrin beta1 subunits but not to alpha2 and alpha6 subunits, RGD peptide or lactose.
20595044	1	21	gly	glycoprotein	92:103	arg1	MD-1	MD-1				OGER		MD-1	O88188		MD-1 is a glycoprotein that associates with a B-cell-specific RP105 protein and has a low sequence identity of 16% to MD-2 that associates with Toll-like receptor 4 and recognizes endotoxic lipopolysaccharide.
20595044	1	21	gly	glycoprotein	92:103	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			MD-1 is a glycoprotein that associates with a B-cell-specific RP105 protein and has a low sequence identity of 16% to MD-2 that associates with Toll-like receptor 4 and recognizes endotoxic lipopolysaccharide.
23999306	8	41	gly	glycoprotein	1316:1327	arg1	any glycoprotein	any glycoprotein				Fterm		glycoprotein			The glycan binding mode can be generalized to any glycoprotein that is a substrate of ST6Gal-I.
27922006	4	16	part_of	MAG	458:460	arg1	the MAG full ectodomain	MAG		the MAG full ectodomain		PUBTATOR	Site	MAG	4099	ectodomain	We present crystal structures of the MAG full ectodomain, which reveal an extended conformation of five Ig domains and a homodimeric arrangement involving membrane-proximal domains Ig4 and Ig5.
9013598	2	78	gly	glycosylation	463:475	arg2	the seven potential N-linked glycosylation sites			the seven potential N-linked glycosylation sites						sites, Asn90 and Asn109	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	2	34	gly	glycosylated	525:536	arg1	Asn90			sites, Asn90 and Asn109						sites, Asn90 and Asn109	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	2	34	gly	glycosylated	525:536	arg1	the seven potential N-linked glycosylation sites			sites, Asn90 and Asn109						sites, Asn90 and Asn109	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	2	34	gly	glycosylated	525:536	arg1	the seven potential N-linked glycosylation sites			sites, Asn90 and Asn109						sites, Asn90 and Asn109	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
15901639	2	25	gly	glycoprotein	371:382	arg1	a 36-kDa glycoprotein	glycoprotein			an N-linked carbohydrate moiety	Fterm		glycoprotein			It was shown to be a 36-kDa glycoprotein with an N-linked carbohydrate moiety.
17558413	6	17	part_of	sites	1043:1047	arg1	mouse lumican	lumican		sites		OGER	Site	lumican	P51885	sites	Using this methodology we identified the sites and the order of sulfation of several peptides mediated by purified human tyrosylprotein sulfotransferases (TPSTs), and unambiguously determined the tyrosine sulfation sites in mouse lumican and human vitronectin.
17558413	6	17	part_of	sites	1043:1047	arg1	human vitronectin	vitronectin		sites		PUBTATOR	Site	vitronectin	7448	sites	Using this methodology we identified the sites and the order of sulfation of several peptides mediated by purified human tyrosylprotein sulfotransferases (TPSTs), and unambiguously determined the tyrosine sulfation sites in mouse lumican and human vitronectin.
24076154	10	9	gly	glycosylation	1561:1573	arg2	all the three putative N-linked glycosylation sites			all the three putative N-linked glycosylation sites						sites	A triple mutant of rIAP, where all the three putative N-linked glycosylation sites were mutated showed thermal instability and reduced activity.
12970363	5	58	gly	glycosylation	842:854	arg1	TRPC6	TRPC6				PUBTATOR		TRPC6	7225		To identify potential molecular correlates accounting for the functional difference, we analyzed the glycosylation pattern of TRPC6 compared with TRPC3.
2415652	8	5	gly	desialylated	1487:1498	arg1	desialylated JAr hCG beta	desialylated JAr hCG beta				PUBTATOR		JAr hCG beta	1082		Like desialylated ElBre hCG beta, desialylated JAr hCG beta bound completely to peanut agglutinin, but was incompletely recognized by antisera to the hCG beta-CTE.
2415652	8	62	gly	desialylated	1458:1469	arg1	desialylated ElBre hCG beta	desialylated ElBre hCG beta				PUBTATOR		ElBre hCG beta	1082		Like desialylated ElBre hCG beta, desialylated JAr hCG beta bound completely to peanut agglutinin, but was incompletely recognized by antisera to the hCG beta-CTE.
23209641	5	76	gly	glycosylated	1231:1242	arg1	the glycosylated hydroxylysine residues			the glycosylated hydroxylysine residues						residues	Circulating adiponectin levels in mutant mice lacking the lysyl hydroxylase activity of LH3 were significantly reduced, which indicates that LH3 is required for complete modification of lysine residues in adiponectin and the loss of some of the glycosylated hydroxylysine residues severely affects the secretion of adiponectin.
7663166	6	55	gly	N-glycosylated	977:990	arg1	rmOSF-2	rmOSF-2				Cterm		rmOSF-2	50706		N-Glycanase digestion resulted in the same mobility shift of OSF-2, indicating that rmOSF-2 expressed in insect cells is N-glycosylated.
23234360	3	12	gly	O-glycopeptides	665:679	arg2	O-glycopeptides			O-glycopeptides						O-glycopeptides	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	3	35	gly	glycopeptide	754:765	arg2	glycopeptide identification			glycopeptide identification						glycopeptide	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
11080501	8	3	part_of	thyroglobulin	1757:1769	arg1	GA733 type 2 motif	thyroglobulin		GA733 type 2 motif		OGER	Site	thyroglobulin	P01266	motif	These data show that the extracellular domain of the GA733-2 antigen consists of three distinct domains; a novel cysteine-rich N-terminal domain (GA733 type 1 motif), a cysteine-rich thyroglobulin type 1A domain (GA733 type 2 motif), and a unique nonglycosylated domain without cysteines (GA733 type 3 motif).
11080501	8	3	part_of	thyroglobulin	1757:1769	arg1	a cysteine-rich thyroglobulin type 1A domain	thyroglobulin		a cysteine-rich thyroglobulin type 1A domain		OGER	Site	thyroglobulin	P01266	domain	These data show that the extracellular domain of the GA733-2 antigen consists of three distinct domains; a novel cysteine-rich N-terminal domain (GA733 type 1 motif), a cysteine-rich thyroglobulin type 1A domain (GA733 type 2 motif), and a unique nonglycosylated domain without cysteines (GA733 type 3 motif).
11080501	8	3	part_of	thyroglobulin	1757:1769	arg1	three distinct domains	thyroglobulin		three distinct domains		OGER	Site	thyroglobulin	P01266	domains	These data show that the extracellular domain of the GA733-2 antigen consists of three distinct domains; a novel cysteine-rich N-terminal domain (GA733 type 1 motif), a cysteine-rich thyroglobulin type 1A domain (GA733 type 2 motif), and a unique nonglycosylated domain without cysteines (GA733 type 3 motif).
2513186	10	44	gly	Asn184	1714:1719	arg1	Glycans			Asn184	Glycans					Asn184	Glycans at Asn184 were found to be less sialylated and sulfated.
2513186	10	68	gly	sialylated	1743:1752	arg1	Glycans				Glycans						Glycans at Asn184 were found to be less sialylated and sulfated.
15054092	4	33	gly	has	655:657	arg1	G8 AND a single N-linked glycan	G8			a single N-linked glycan	Cterm		G8	Q9H221		Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	27	gly	attached	684:691	arg1	Asn AND a single N-linked glycan			Asn(619)	a single N-linked glycan					Asn(619)	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg2	Asn			Asn(585) and Asn(592)						Asn(585) and Asn(592)	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg1	Asn			Asn(585) and Asn(592)						Asn(585) and Asn(592)	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg1	Asn			Asn(585) and Asn(592)						Asn(585) and Asn(592)	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg1	G5	G5		Asn(585) and Asn(592)		Cterm		G5	Q9H222	Asn(585) and Asn(592)	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg1	Asn			Asn(585) and Asn(592)						Asn(585) and Asn(592)	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg1	Asn			Asn(585) and Asn(592)						Asn(585) and Asn(592)	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg1	G5	G5		Asn(585) and Asn(592)		Cterm		G5	Q9H222	Asn(585) and Asn(592)	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg2	two asparagine residues			asparagine residues						asparagine residues	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg1	G5	G5		asparagine residues		Cterm		G5	Q9H222	asparagine residues	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg1	Asn			Asn(585) and Asn(592)						Asn(585) and Asn(592)	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg1	G5	G5		Asn(585) and Asn(592)		Cterm		G5	Q9H222	Asn(585) and Asn(592)	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg1	G5	G5		Asn(585) and Asn(592)		Cterm		G5	Q9H222	Asn(585) and Asn(592)	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
15054092	4	55	gly	glycosylated	624:635	arg1	G5	G5		asparagine residues		Cterm		G5	Q9H222	asparagine residues	Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosylated in G5 and that G8 has a single N-linked glycan attached to Asn(619).
22235133	7	13	part_of	IL-21R	1062:1067	arg1	the extracellular domain	IL-21R		the extracellular domain		PUBTATOR	Site	IL-21R	50615	domain	We furthermore demonstrate that a sugar chain bridges the two fibronectin domains that constitute the extracellular domain of IL-21R and anchors at the WSXWS motif through an extensive hydrogen bonding network, including mannosylation.
22235133	7	42	part_of	fibronectin	998:1008	arg1	the two fibronectin domains	fibronectin		the two fibronectin domains		OGER	Site	fibronectin	P02751	domains	We furthermore demonstrate that a sugar chain bridges the two fibronectin domains that constitute the extracellular domain of IL-21R and anchors at the WSXWS motif through an extensive hydrogen bonding network, including mannosylation.
28327546	3	81	gly	N-glycosylation	340:354	arg1	FVIII	FVIII		N582		PUBTATOR		FVIII	2157	N582	Here we characterize how hemophilia mutations near the unused N-glycosylation site of the A2 domain (N582) of FVIII affect protein conformation and intracellular trafficking.
28327546	3	81	gly	N-glycosylation	340:354	arg1	the A2 domain			domain						domain	Here we characterize how hemophilia mutations near the unused N-glycosylation site of the A2 domain (N582) of FVIII affect protein conformation and intracellular trafficking.
28327546	3	81	gly	N-glycosylation	340:354	arg1	FVIII	FVIII		domain		PUBTATOR		FVIII	2157	domain	Here we characterize how hemophilia mutations near the unused N-glycosylation site of the A2 domain (N582) of FVIII affect protein conformation and intracellular trafficking.
28327546	3	81	gly	N-glycosylation	340:354	arg1	FVIII	FVIII		domain		PUBTATOR		FVIII	2157	domain	Here we characterize how hemophilia mutations near the unused N-glycosylation site of the A2 domain (N582) of FVIII affect protein conformation and intracellular trafficking.
28327546	3	81	gly	N-glycosylation	340:354	arg1	FVIII	FVIII		site		PUBTATOR		FVIII	2157	site	Here we characterize how hemophilia mutations near the unused N-glycosylation site of the A2 domain (N582) of FVIII affect protein conformation and intracellular trafficking.
24841998	4	18	gly	sialylated	584:593	arg1	α-2,6 sialylated tryptic N-glycopeptides			α-2,6 sialylated tryptic N-glycopeptides						N-glycopeptides	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	4	33	gly	N-glycopeptides	603:617	arg2	α-2,6 sialylated tryptic N-glycopeptides			α-2,6 sialylated tryptic N-glycopeptides						N-glycopeptides	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
3353370	0	115	part_of	containing	92:101	arg1	both transmembrane proteins AND a leucine-rich amino acid sequence	both transmembrane proteins		a leucine-rich amino acid sequence		Fterm	Site	proteins		sequence	The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence.
1451807	3	11	gly	N-glycosylated	377:390	arg2	Asn62			Asn62						Asn62	All components are N-glycosylated at Asn62; N-glycosylation does not contribute to heterogeneity.
29391424	5	25	gly	glycosylation	668:680	arg2	970 unique glycosylation sites			970 unique glycosylation sites						sites	In a large-scale study, a total of 257 glycoproteins containing 970 unique glycosylation sites and 3447 non-redundant N-linked glycopeptide variants were identified in 24 serum samples.
29391424	5	42	gly	glycoproteins	632:644	arg1	257 glycoproteins	257 glycoproteins				Fterm		glycoproteins			In a large-scale study, a total of 257 glycoproteins containing 970 unique glycosylation sites and 3447 non-redundant N-linked glycopeptide variants were identified in 24 serum samples.
29391424	5	50	gly	glycopeptide	720:731	arg2	3447 non-redundant N-linked glycopeptide variants			3447 non-redundant N-linked glycopeptide variants						glycopeptide	In a large-scale study, a total of 257 glycoproteins containing 970 unique glycosylation sites and 3447 non-redundant N-linked glycopeptide variants were identified in 24 serum samples.
12731890	2	27	part_of	form	431:434	arg1	the glycosylation sites	form of the receptor		the glycosylation sites		Fterm	Site	form of the receptor		sites	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	2	46	part_of	receptor	404:411	arg1	the glycosylation sites	receptor		the glycosylation sites		Fterm	Site	receptor		sites	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
26811476	5	12	part_of	UMOD	844:847	arg1	polymerization regions	UMOD		polymerization regions		PUBTATOR	Site	UMOD	7369	regions	Here, we report the crystal structures of polymerization regions of human UMOD and mouse ZP2, an essential sperm receptor protein that is structurally related to UMOD but forms heteropolymers.
26811476	5	59	part_of	ZP2	859:861	arg1	polymerization regions	ZP2		polymerization regions		PUBTATOR	Site	ZP2	22787	regions	Here, we report the crystal structures of polymerization regions of human UMOD and mouse ZP2, an essential sperm receptor protein that is structurally related to UMOD but forms heteropolymers.
15454184	4	11	part_of	contains	509:516	arg1	FS AND two potential N-glycosylation sites	FS		sites, Asn95 and Asn259		Cterm	AminoAcid	FS	10468	sites, Asn95 and Asn259	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	11	part_of	contains	509:516	arg1	FS AND Asn259	FS		sites, Asn95 and Asn259		Cterm	AminoAcid	FS	10468	sites, Asn95 and Asn259	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	11	part_of	contains	509:516	arg1	FS AND Asn259	FS		sites, Asn95 and Asn259		Cterm	AminoAcid	FS	10468	sites, Asn95 and Asn259	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
3756141	4	2	gly	glycosylated	510:521	arg1	Another nine threonine residues			Another nine threonine residues						threonine residues	Another nine threonine residues are probably also glycosylated.
17293352	11	114	gly	-sialylated	1805:1815	arg1	(alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures				(alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures						For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
3881423	3	30	gly	glycoprotein	508:519	arg1	the glycoprotein processing enzyme glucosidase II	the glycoprotein processing enzyme glucosidase II				Fterm		glycoprotein			We now report genetic and biochemical evidence that neutral alpha-glucosidase AB is synonymous with the glycoprotein processing enzyme glucosidase II.
2668275	3	1	gly	N-glycosylation	398:412	arg2	four potential N-glycosylation sites			four potential N-glycosylation sites						sites	The deduced amino acid sequence comprises 583 amino acids with an N-terminal signal peptide of 21 or 23 residues and four potential N-glycosylation sites.
2668275	3	1	gly	N-glycosylation	398:412	arg2	21 or 23 residues			residues						residues	The deduced amino acid sequence comprises 583 amino acids with an N-terminal signal peptide of 21 or 23 residues and four potential N-glycosylation sites.
17330941	9	53	gly	N-glycosylation	1135:1149	arg2	104 N-glycosylation sites			104 N-glycosylation sites						sites	A total of 104 N-glycosylation sites were identified.
10091666	2	57	gly	glycosylated	405:416	arg1	All recombinant proteins	All recombinant proteins				Fterm		proteins			All recombinant proteins were shown by electrospray ionization mass spectrometry (ESI-MS) to be glycosylated and the site of attachment was shown to be Asn461 by peptide mapping in conjunction with ESI-MS.
23167757	5	18	gly	PDIA2	904:908	arg1	N284			N127, N284 and N516						N127, N284 and N516	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	18	gly	PDIA2	904:908	arg1	N127			N127, N284 and N516						N127, N284 and N516	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	18	gly	PDIA2	904:908	arg1	N127			N127, N284 and N516						N127, N284 and N516	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	37	gly	glycosylated	936:947	arg2	all three Asn residues			Asn residues						Asn residues	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	56	gly	glycosylation	875:887	arg1	human PDIA2	PDIA2		sites		PUBTATOR		PDIA2	64714	sites	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
25485983	0	10	part_of	antithrombin	84:95	arg1	N135	antithrombin		N135		PUBTATOR	SpecificSite	antithrombin	462	N135	Increased N-glycosylation efficiency by generation of an aromatic sequon on N135 of antithrombin.
25485983	0	57	part_of	sequon	66:71	arg1	N135	sequon		N135						N135	Increased N-glycosylation efficiency by generation of an aromatic sequon on N135 of antithrombin.
6689265	2	34	gly	glycosylated	362:373	arg1	Gc 1 protein	Gc 1 protein				PUBTATOR		Gc 1 protein	10562		It was found that only the Gc 1 protein (Gc1a isoform) was glycosylated, the glycan moiety representing about 1% of the protein.
6689265	2	34	gly	glycosylated	362:373	arg1	Gc1a isoform	Gc1a isoform				Fterm		isoform			It was found that only the Gc 1 protein (Gc1a isoform) was glycosylated, the glycan moiety representing about 1% of the protein.
10903744	2	24	part_of	MBP	404:406	arg1	this region	MBP		this region		PUBTATOR	Site	MBP	4155	region	Mutations in this region of human MBP are associated with immunodeficiency resulting from a reduction in the ability of the mutant MBPs to fix complement as well as from reduced serum concentrations.
7460900	2	14	gly	glycopeptides	354:366	arg2	the glycopeptides			the glycopeptides						glycopeptides	One of the glycopeptides allowed us to complete the C-terminal sequence of human caseinoglycopeptide previously published in part by others.
7460900	2	35	gly	caseinoglycopeptide	424:442	arg2	human caseinoglycopeptide			human caseinoglycopeptide						caseinoglycopeptide	One of the glycopeptides allowed us to complete the C-terminal sequence of human caseinoglycopeptide previously published in part by others.
3181129	5	22	part_of	contains	499:506	arg1	The predicted protein sequence AND a carboxy-terminal sequence			sequence						sequence	The predicted protein sequence contains 240 amino acids including a leader sequence of 22 residues and a carboxy-terminal sequence of 23 residues that is replaced in the processed molecule by a glycosyl-phosphatidylinositol anchor attached at serine 195.
18596036	9	58	part_of	MBL	1808:1810	arg1	a conserved lysine	MBL		a conserved lysine		PUBTATOR	AminoAcid	MBL	4153	lysine	This information allows us to propose a model of the MBL-MASP-1/3 interaction, involving a major electrostatic interaction between two acidic Ca(2+) ligands of MASP-1/3 and a conserved lysine of MBL.
7068558	1	4	gly	asparagine-linked	155:171	arg1	2 asparagine-linked sugar chains			asparagine	2 asparagine-linked sugar chains					asparagine	Human lactoferrin contains 2 asparagine-linked sugar chains in 1 molecule.
7068558	1	13	gly	contains	144:151	arg1	Human lactoferrin AND 2 asparagine-linked sugar chains	Human lactoferrin			2 asparagine-linked sugar chains	OGER		Human lactoferrin	P02788		Human lactoferrin contains 2 asparagine-linked sugar chains in 1 molecule.
1731338	6	50	part_of	CD43	1134:1137	arg1	the N-terminal (extracellular) polypeptide region	CD43		the N-terminal (extracellular) polypeptide region		PUBTATOR	Site	CD43	6693	region	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	6	62	part_of	galactoglycoprotein	1001:1019	arg1	the galactoglycoprotein polypeptide	galactoglycoprotein		the galactoglycoprotein polypeptide		PUBTATOR	Site	galactoglycoprotein	6693	polypeptide	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	6	88	part_of	polypeptide	1080:1090	arg1	the N-terminal (extracellular) polypeptide region	polypeptide		the N-terminal (extracellular) polypeptide region		Fterm	Site	polypeptide		region	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
19737401	8	57	part_of	BST-2	1136:1140	arg1	the BST-2 extracellular domain	BST-2		the BST-2 extracellular domain		PUBTATOR	Site	BST-2	684	domain	Analysis of single, double, or triple cysteine mutants revealed that any one of three cysteine residues present in the BST-2 extracellular domain was sufficient for BST-2 dimerization, for inhibition of virus release, and sensitivity to Vpu.
12970363	6	50	gly	glycosylation	1017:1029	arg2	both extracellular N-linked glycosylation sites			both extracellular N-linked glycosylation sites						sites	Two NX(S/T) motifs in TRPC6 were mutated (Asn to Gln) by in vitro mutagenesis to delete one or both extracellular N-linked glycosylation sites.
18775496	3	2	gly	Fucosylation	408:419	arg1	recombinant C45 agrin	recombinant C45 agrin				PUBTATOR		C45 agrin	O00468		Fucosylation of recombinant C45 agrin, both active (neural, z8) and inactive (muscle, z0) splice forms, was eliminated when agrin was overexpressed in Pofut1-deficient cells or by mutation of a consensus site for Pofut1 fucosylation (serine 1726 in the EGF4 domain).
18775496	3	40	gly	agrin	440:444	arg1	Fucosylation	C45 agrin			Fucosylation	PUBTATOR		C45 agrin	O00468		Fucosylation of recombinant C45 agrin, both active (neural, z8) and inactive (muscle, z0) splice forms, was eliminated when agrin was overexpressed in Pofut1-deficient cells or by mutation of a consensus site for Pofut1 fucosylation (serine 1726 in the EGF4 domain).
16362042	3	3	part_of	Gas6	480:483	arg1	the first laminin G-like domain	Gas6		the first laminin G-like domain		PUBTATOR	Site	Gas6	2621	domain	The crystal structure at 3.3 A resolution of a minimal human Gas6/Axl complex reveals an assembly of 2:2 stoichiometry, in which the two immunoglobulin-like domains of the Axl ectodomain are crosslinked by the first laminin G-like domain of Gas6, with no direct Axl/Axl or Gas6/Gas6 contacts.
16362042	3	10	part_of	laminin	455:461	arg1	the first laminin G-like domain	laminin		the first laminin G-like domain		OGER	Site	laminin		domain	The crystal structure at 3.3 A resolution of a minimal human Gas6/Axl complex reveals an assembly of 2:2 stoichiometry, in which the two immunoglobulin-like domains of the Axl ectodomain are crosslinked by the first laminin G-like domain of Gas6, with no direct Axl/Axl or Gas6/Gas6 contacts.
16362042	3	13	part_of	Axl	411:413	arg1	the Axl ectodomain	Axl		the Axl ectodomain		PUBTATOR	Site	Axl	558	ectodomain	The crystal structure at 3.3 A resolution of a minimal human Gas6/Axl complex reveals an assembly of 2:2 stoichiometry, in which the two immunoglobulin-like domains of the Axl ectodomain are crosslinked by the first laminin G-like domain of Gas6, with no direct Axl/Axl or Gas6/Gas6 contacts.
29581294	5	42	part_of	hLOXL2	731:736	arg1	the copper-binding site	hLOXL2		the copper-binding site		OGER	Site	hLOXL2	Q9Y4K0	site	Unexpectedly, the copper-binding site of hLOXL2 is occupied by zinc, which blocks LTQ generation and the enzymatic activity of hLOXL2 in our in vitro assay.
18815274	7	7	gly	N-glycosylation	865:879	arg2	a N-glycosylation site			a N-glycosylation site						site	Furthermore, we found disruption of a N-glycosylation site (N573Q) within the fourth luminal domain of SV2A rendered the mutant unable to mediate the entry of BoNT/E and also reduced the entry of BoNT/A.
24161696	8	38	gly	occupancy	1475:1483	arg2	the N-glycosylation sites			the N-glycosylation sites						sites	CONCLUSIONS: Our findings provide direct evidence that occupancy of the N-glycosylation sites of Kv3.1b contributes significantly to its lateral heterogeneity in membranes of neuronal-derived cells, and in turn alters cellular properties.
24161696	8	61	gly	N-glycosylation	1492:1506	arg2	the N-glycosylation sites	Kv3.1b		sites		Cterm		Kv3.1b		sites	CONCLUSIONS: Our findings provide direct evidence that occupancy of the N-glycosylation sites of Kv3.1b contributes significantly to its lateral heterogeneity in membranes of neuronal-derived cells, and in turn alters cellular properties.
9712881	0	70	part_of	protein	55:61	arg1	Glu681	AE1 protein		Glu681		PUBTATOR	AminoAcid	AE1 protein	6521	Glu681	Topology of the region surrounding Glu681 of human AE1 protein, the erythrocyte anion exchanger.
25265424	3	25	gly	glycoforms	356:365	arg1	hemopexin	hemopexin				PUBTATOR		hemopexin	3263		We present a case study that compares site specific glycoforms of four proteins including haptoglobin, complement factor H, kininogen-1, and hemopexin isolated from the same patient.
25265424	3	25	gly	glycoforms	356:365	arg1	four proteins	four proteins				Fterm		proteins			We present a case study that compares site specific glycoforms of four proteins including haptoglobin, complement factor H, kininogen-1, and hemopexin isolated from the same patient.
25265424	3	25	gly	glycoforms	356:365	arg1	kininogen-1	kininogen-1				PUBTATOR		kininogen-1	3827		We present a case study that compares site specific glycoforms of four proteins including haptoglobin, complement factor H, kininogen-1, and hemopexin isolated from the same patient.
25265424	3	25	gly	glycoforms	356:365	arg1	complement factor H	haptoglobin, complement factor H				PUBTATOR		haptoglobin, complement factor H	3240		We present a case study that compares site specific glycoforms of four proteins including haptoglobin, complement factor H, kininogen-1, and hemopexin isolated from the same patient.
11180632	0	18	gly	protein	112:118	arg1	the asparagine-linked sugar chains	cerebroside sulfate activator protein			the asparagine-linked sugar chains	OGER		cerebroside sulfate activator protein	P17900		Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	0	35	gly	asparagine-linked	17:33	arg1	the asparagine-linked sugar chains			asparagine	the asparagine-linked sugar chains					asparagine	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
7574684	6	24	part_of	trkB	1033:1036	arg1	the soluble domain	trkB		the soluble domain		PUBTATOR	Site	trkB	4915	domain	Among 12 potential N-linked glycosylation sites proposed in the soluble domain of trkB, 10 sites are actually glycosylated.
25374123	3	56	gly	N-glycopeptides	492:506	arg1	vitronectin	vitronectin		N-glycopeptides		PUBTATOR		vitronectin	7448	N-glycopeptides	Here, we systematically analyzed the site-specific N-glycopeptides of vitronectin in human plasma by tandem mass spectrometry combined with immunoprecipitation and hydrophilic interaction liquid chromatography (HILIC) enrichment.
25153361	8	66	part_of	containing	1462:1471	arg1	a hemagglutinin AND 9 N-glycosylation sequons	a hemagglutinin		9 N-glycosylation sequons		Fterm		hemagglutinin			We demonstrated the value of our system to define site-specific glycosylation using a hemagglutinin containing 9 N-glycosylation sequons from a single HILIC-C18-MS acquisition.
27314333	3	15	part_of	TSR1	500:503	arg1	a thrombospondin type 1 (TSR1) domain	TSR1		a thrombospondin type 1 (TSR1) domain		PUBTATOR	Site	TSR1	55720	domain	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
27314333	3	20	part_of	type	492:495	arg1	a thrombospondin type 1 (TSR1) domain	thrombospondin type 1		a thrombospondin type 1 (TSR1) domain		OGER	Site	thrombospondin type 1	P07996	domain	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
27314333	3	79	part_of	thrombospondin	477:490	arg1	a thrombospondin type 1 (TSR1) domain	thrombospondin type 1		a thrombospondin type 1 (TSR1) domain		OGER	Site	thrombospondin type 1	P07996	domain	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
22848655	11	114	part_of	Sema	1587:1590	arg1	the Sema domain	Sema		the Sema domain		PUBTATOR	Site	Sema	57556	domain	The RON Sema-PSI crystal packing generates a homodimer with interface formed by the Sema domain.
15454184	2	66	gly	glycosylation	308:320	arg1	recombinant human FS (rhFS)	recombinant human FS (rhFS)				Cterm		rhFS			In this study, we analyzed the glycosylation of recombinant human FS (rhFS) produced in Chinese hamster ovary cells.
23139753	4	32	part_of	WFDC	468:471	arg1	two WFDC domains	WFDC		two WFDC domains		Cterm	Site	WFDC		domains	HE-4 is a 124 amino acid long polypeptide with two WFDC domains.
24058541	3	17	part_of	has	298:300	arg1	CLN5 AND eight potential N-glycosylation sites	CLN5		eight potential N-glycosylation sites		PUBTATOR	Site	CLN5	O75503	sites	CLN5 has eight potential N-glycosylation sites based on the Asn-X-Thr/Ser consensus sequence.
15003450	5	25	gly	glycoprotein	700:711	arg1	the glycoprotein dimer	the glycoprotein dimer				Fterm		glycoprotein			N-linked carbohydrate appears at six sites in the glycoprotein dimer, revealing the basis for lysosomal transport via the mannose-6-phosphate receptor.
22809326	0	31	part_of	protein	82:88	arg1	the conserved domain	protein		the conserved domain		Fterm	Site	protein		domain	Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx.
10988252	9	12	gly	glycosylation	1604:1616	arg1	sEGFR	sEGFR				PUBTATOR		EGFR	1956		This first comprehensive glycosylation study on a human nonrecombinant receptor shows the immense heterogeneity of the glycosylation of sEGFR.
2013294	1	53	gly	glycoprotein	118:129	arg1	Secretory actin-binding protein	Secretory actin-binding protein				PUBTATOR		Secretory actin-binding protein	5304		Secretory actin-binding protein (SABP), a glycoprotein from human seminal plasma, was isolated according to Akiyama and Kimura [Akiyama, K. & Kimura, H. (1990) Biochim.
2013294	1	53	gly	glycoprotein	118:129	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			Secretory actin-binding protein (SABP), a glycoprotein from human seminal plasma, was isolated according to Akiyama and Kimura [Akiyama, K. & Kimura, H. (1990) Biochim.
8670172	5	88	part_of	Asn-77	888:893	arg1	a GPI-anchor	GPI		Asn-77		OGER	SpecificSite	GPI	P06744	Asn-77	Mass analysis of the isolated C-terminal peptide (T9) indicated that a GPI-anchor (at Asn-77) without an inositol-associated phospholipid was present in soluble CD59u.
3181129	8	14	part_of	antigen	1146:1152	arg1	the first two domains	carcinoembryonic antigen		the first two domains		PUBTATOR	Site	carcinoembryonic antigen	P06731	domains	The sequence matches particularly well with the extracellular parts of LFA-3 and CD2 antigens and the first two domains of carcinoembryonic antigen and non-specific, cross-reacting antigen.
21609021	4	29	part_of	IgG	816:818	arg1	the IgG glycopeptides	IgG		the IgG glycopeptides		Cterm	Site	IgG		glycopeptides	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
20188224	3	80	part_of	granulin	481:488	arg1	granulin domains	granulin		granulin domains		PUBTATOR	Site	granulin	2896	domains	PGRN is a glycoprotein, containing five N-glycosylation consensus sequons, three of which fall within granulin domains.
20188224	3	65	part_of	containing	403:412	arg1	PGRN AND five N-glycosylation consensus sequons	PGRN		five N-glycosylation consensus sequons		PUBTATOR		PGRN	2896		PGRN is a glycoprotein, containing five N-glycosylation consensus sequons, three of which fall within granulin domains.
20188224	3	65	part_of	containing	403:412	arg1	a glycoprotein AND five N-glycosylation consensus sequons	a glycoprotein		five N-glycosylation consensus sequons		Fterm		glycoprotein			PGRN is a glycoprotein, containing five N-glycosylation consensus sequons, three of which fall within granulin domains.
9748270	7	44	part_of	XVII	949:952	arg1	the collagen XVII ectodomain	XVII		the collagen XVII ectodomain		Cterm	Site	XVII		ectodomain	The soluble form exhibited molecular properties of the collagen XVII ectodomain: a triple-helical, N-glycosylated molecule of three 120-kDa polypeptides.
1997323	7	73	gly	glycopeptides	772:784	arg2	the glycopeptides			the glycopeptides						glycopeptides	Glycan structures were determined on the glycopeptides by employing GLC/MS and 400-MHz 1H-NMR spectroscopy.
2511201	1	75	gly	linked	281:286	arg1	a serine residue AND a unique trisaccharide			a serine residue	a unique trisaccharide					serine residue	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
10814696	3	68	gly	A	786:786	arg1	carbohydrate moieties	human placental arylsylfatase A			carbohydrate moieties	Cterm		human placental arylsylfatase A			In the present study we have analyzed carbohydrate moieties of human placental arylsylfatase A using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by Western blotting on Immobilon P and on-blot deglycosylation using PNGase F for glycan release.
7107587	1	64	gly	glycopeptides	102:114	arg2	glycosidase-treated glycopeptides			glycosidase-treated glycopeptides						glycopeptides	Use of 300-MHz 1H-NMR to characterize glycosidase-treated glycopeptides.
2403553	10	18	gly	oligosaccharides	1339:1354	arg1	the transferring receptors	receptors			oligosaccharides	Fterm		receptors			In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	21	gly	sialylated	1439:1448	arg1	the O-linked oligosaccharides				the O-linked oligosaccharides						In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	21	gly	sialylated	1439:1448	arg1	the neutral monosaccharide N-acetylgalactosamine				the neutral monosaccharide N-acetylgalactosamine						In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	21	gly	sialylated	1439:1448	arg1	the neutral disaccharide galactose-N-acetylgalactosamine				the neutral disaccharide galactose-N-acetylgalactosamine						In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
21389326	4	50	part_of	Flt3	915:918	arg1	extracellular domain 3	Flt3		extracellular domain 3		PUBTATOR	Site	Flt3	2322	domain	FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions.
9425062	7	16	gly	Asn	909:911	arg1	(Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2			Asn	(Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2					Asn	Analysis revealed three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2: all these were complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2.
9233787	8	52	part_of	site	1185:1188	arg1	follistatin	follistatin		site		OGER	Site	follistatin	P19883	site	This hairpin is likely to act as a rigid spacer in proteins containing tandemly repeated FS domains, such as follistatin and agrin, and forms the heparin-binding site in follistatin.
9233787	8	54	part_of	containing	1083:1092	arg1	follistatin AND tandemly repeated FS domains	follistatin		tandemly repeated FS domains		OGER	Site	follistatin	P19883	domains	This hairpin is likely to act as a rigid spacer in proteins containing tandemly repeated FS domains, such as follistatin and agrin, and forms the heparin-binding site in follistatin.
9233787	8	54	part_of	containing	1083:1092	arg1	proteins AND tandemly repeated FS domains	proteins		tandemly repeated FS domains		Fterm	Site	proteins		domains	This hairpin is likely to act as a rigid spacer in proteins containing tandemly repeated FS domains, such as follistatin and agrin, and forms the heparin-binding site in follistatin.
9233787	8	54	part_of	containing	1083:1092	arg1	agrin AND tandemly repeated FS domains	agrin		tandemly repeated FS domains		OGER	Site	agrin	O00468	domains	This hairpin is likely to act as a rigid spacer in proteins containing tandemly repeated FS domains, such as follistatin and agrin, and forms the heparin-binding site in follistatin.
21908432	3	45	gly	leucine-rich	442:453	arg1	a single leucine-rich repeat			leucine	a single leucine-rich repeat					leucine	We have crystallized the GPIbβ ectodomain (GPIbβ(E)) and determined the structure to show a single leucine-rich repeat with N- and C-terminal disulphide-bonded capping regions.
16859706	4	9	gly	bears	644:648	arg1	TPST1 AND N-linked glycosyl residues	TPST1		position Asn60 and Asn262	N-linked glycosyl residues	PUBTATOR	AminoAcid	TPST1	8460	position Asn60 and Asn262	PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262.
17534424	3	16	part_of	ClC-6	678:682	arg1	the ClC-6 COOH-terminal tail	ClC-6		the ClC-6 COOH-terminal tail		PUBTATOR	Site	ClC-6	1185	tail	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	53	part_of	epitope	663:669	arg1	the ClC-6 COOH-terminal tail	epitope		the ClC-6 COOH-terminal tail						tail	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
7727388	3	87	part_of	receptor	457:464	arg1	glycosylation sites	receptor		glycosylation sites		Fterm	Site	receptor		sites	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
6118137	0	53	gly	glycoprotein	16:27	arg1	Rat brain Thy-1 glycoprotein	Rat brain Thy-1 glycoprotein				PUBTATOR		Thy-1 glycoprotein	24832		Rat brain Thy-1 glycoprotein.
22745122	1	28	gly	threonine	225:233	arg1	O-linked-N-acetyl-glucosamine glycosylation			serine and threonine residues	O-linked-N-acetyl-glucosamine glycosylation					serine and threonine residues	O-linked-N-acetyl-glucosamine glycosylation (O-GlcNAcylation) of the serine and threonine residues of cellular proteins is a dynamic process and affects phosphorylation.
22745122	1	30	gly	serine	214:219	arg1	residues			serine and threonine residues	O-linked-N-acetyl-glucosamine glycosylation					serine and threonine residues	O-linked-N-acetyl-glucosamine glycosylation (O-GlcNAcylation) of the serine and threonine residues of cellular proteins is a dynamic process and affects phosphorylation.
22745122	1	33	gly	glycosylation	175:187	arg1	serine			serine and threonine residues						serine and threonine residues	O-linked-N-acetyl-glucosamine glycosylation (O-GlcNAcylation) of the serine and threonine residues of cellular proteins is a dynamic process and affects phosphorylation.
3877053	8	30	part_of	fibronectin	1224:1234	arg1	regions	fibronectin		regions		PUBTATOR	Site	fibronectin	2335	regions	Comparison of the structure of factor XII with other proteins revealed extensive sequence identity with regions of tissue-type plasminogen activator (the epidermal growth factor-like region and the kringle region) and fibronectin (type I and type II homologies).
3877053	8	83	part_of	activator	1145:1153	arg1	regions	tissue-type plasminogen activator		regions		PUBTATOR	Site	tissue-type plasminogen activator	5327	regions	Comparison of the structure of factor XII with other proteins revealed extensive sequence identity with regions of tissue-type plasminogen activator (the epidermal growth factor-like region and the kringle region) and fibronectin (type I and type II homologies).
12144777	4	42	part_of	site	468:471	arg1	the (alpha/beta)(8) barrel subunits	subunits		site		OGER	Site	subunits	1800	site	The active site in each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is composed of binuclear zinc ions bridged by the Glu125 side-chain located at the bottom of the barrel, and it faces toward the microvillar membrane of a kidney tubule.
25765764	1	30	part_of	LRIG1-LRR-1Ig	259:271	arg1	three soluble fragments	LRIG1		three soluble fragments		PUBTATOR	Site	LRIG1	26018	fragments	We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells.
25765764	1	30	part_of	LRIG1-LRR-1Ig	259:271	arg1	the LRIG1-LRR-1Ig fragment	LRIG1		the LRIG1-LRR-1Ig fragment		PUBTATOR	Site	LRIG1	26018	fragment	We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells.
25765764	1	42	part_of	LRIG1-ECD	129:137	arg1	three soluble fragments	LRIG1		three soluble fragments		PUBTATOR	Site	LRIG1	26018	fragments	We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells.
25765764	1	42	part_of	LRIG1-ECD	129:137	arg1	the LRIG1-LRR-1Ig fragment	LRIG1		the LRIG1-LRR-1Ig fragment		PUBTATOR	Site	LRIG1	26018	fragment	We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells.
25765764	1	42	part_of	LRIG1-ECD	129:137	arg1	the LRIG1-3Ig (immunoglobulin-like) domain	LRIG1		the LRIG1-3Ig (immunoglobulin-like) domain		PUBTATOR	Site	LRIG1	26018	domain	We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells.
25765764	1	47	part_of	LRIG1-3Ig	211:219	arg1	three soluble fragments	LRIG1		three soluble fragments		PUBTATOR	Site	LRIG1	26018	fragments	We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells.
25765764	1	47	part_of	LRIG1-3Ig	211:219	arg1	the LRIG1-3Ig (immunoglobulin-like) domain	LRIG1		the LRIG1-3Ig (immunoglobulin-like) domain		PUBTATOR	Site	LRIG1	26018	domain	We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells.
18467335	4	15	gly	heterogeneity	486:498	arg1	blood-derived PCI	blood-derived PCI				OGER		PCI	P05154		In this study we have for the first time provided a full explanation for the marked size heterogeneity of blood-derived PCI and identified functional differences between naturally occurring PCI variants.
12604466	7	6	gly	glycosylated	1089:1100	arg2	N597	NBCe1		N597 and N617		OGER		NBCe1	Q9Y6R1	N597 and N617	Immunoblotting of oocyte membrane extracts treated with PNGase F indicates that NBCe1 is normally glycosylated at N597 and N617 (both on the third extracellular loop).
6546754	2	11	gly	asparagine-linked	252:268	arg1	four asparagine-linked carbohydrate sites			asparagine	four asparagine-linked carbohydrate sites					asparagine	The zymogen consists of 739 amino acids, has four asparagine-linked carbohydrate sites, and has independently disulfide-bonded NH2- and COOH-terminal regions.
8174273	1	33	gly	chains	138:143	arg1	serum transferrin	transferrin			chains	PUBTATOR		transferrin	7018		The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	1	95	gly	asparagine-linked	114:130	arg1	The asparagine-linked sugar chains			asparagine	The asparagine-linked sugar chains					asparagine	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
7068558	4	19	gly	lactoferrin	775:785	arg1	the sugar chain moiety	lactoferrin			the sugar chain moiety	OGER		lactoferrin	P02788		A structural study of the oligosaccharides obtained from the two samples by sequential exoglycosidase digestion in combination with methylation analysis also gave the same results indicating that there is no racial difference both in quality and quantity of the sugar chain moiety of lactoferrin.
7613477	2	20	gly	glycopeptides	688:700	arg2	glycopeptides			glycopeptides						glycopeptides	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	2	26	gly	fragment	607:614	arg1	carbohydrate-specific fragment ions				carbohydrate-specific fragment ions						A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
25765764	0	20	part_of	LRIG1	0:4	arg1	LRIG1 extracellular domain	LRIG1		LRIG1 extracellular domain		PUBTATOR	Site	LRIG1	26018	domain	LRIG1 extracellular domain: structure and function analysis.
21676880	3	30	part_of	has	548:550	arg1	KCNE1 AND two distinct N-glycosylation sites	KCNE1		two distinct N-glycosylation sites		PUBTATOR	Site	KCNE1	3753	sites	We show that KCNE1 has two distinct N-glycosylation sites: a typical co-translational site and a consensus site ∼20 residues away that unexpectedly acquires N-glycans after protein synthesis (post-translational).
21676880	3	30	part_of	has	548:550	arg1	KCNE1 AND a consensus site	KCNE1		site		PUBTATOR	Site	KCNE1	3753	site	We show that KCNE1 has two distinct N-glycosylation sites: a typical co-translational site and a consensus site ∼20 residues away that unexpectedly acquires N-glycans after protein synthesis (post-translational).
19520913	3	20	part_of	LDLR	598:601	arg1	its cytoplasmic domain	LDLR		its cytoplasmic domain		PUBTATOR	Site	LDLR	16835	domain	LXR inhibits the LDL receptor (LDLR) pathway through transcriptional induction of Idol (inducible degrader of the LDLR), an E3 ubiquitin ligase that triggers ubiquitination of the LDLR on its cytoplasmic domain, thereby targeting it for degradation.
25385546	3	8	part_of	RPTPσ	540:544	arg1	the RPTPσ extracellular region	RPTPσ 		the RPTPσ extracellular region		PUBTATOR	Site	RPTPσ 	5802	region	Here, we report crystallographic, electron microscopic and small-angle X-ray scattering analyses, which reveal sufficient inter-domain flexibility in the RPTPσ extracellular region for interaction with both cis (same cell) and trans (opposite cell) ligands.
8286855	9	49	gly	glycosylation	1234:1246	arg1	GpA	GpA		domain		PUBTATOR		GpA	2993	domain	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	49	gly	glycosylation	1234:1246	arg1	the extracellular domain			domain						domain	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	49	gly	glycosylation	1234:1246	arg1	GpA	GpA		Ser/Thr		PUBTATOR		GpA	2993	Ser/Thr	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	49	gly	glycosylation	1234:1246	arg1	21 of 22 Ser/Thr			Ser/Thr						Ser/Thr	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	49	gly	glycosylation	1234:1246	arg1	the extracellular domain	GpA		domain		PUBTATOR		GpA	2993	domain	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	49	gly	glycosylation	1234:1246	arg1	21 of 22 Ser/Thr	GpA		Ser/Thr		PUBTATOR		GpA	2993	Ser/Thr	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
23661698	4	48	gly	deglycosylated	518:531	arg1	Ephrin-A1	Ephrin-A1				PUBTATOR		Ephrin-A1	1942		Ephrin-A1 was enzymatically deglycosylated, and its activity was evaluated in several assays using glioblastoma (GBM) cells and recombinant EphA2.
22750213	0	45	gly	glycosylation	9:21	arg1	globular tetrameric acetylcholinesterase	globular tetrameric acetylcholinesterase				PUBTATOR		acetylcholinesterase	11423		N-linked glycosylation of proline-rich membrane anchor (PRiMA) is not required for assembly and trafficking of globular tetrameric acetylcholinesterase.
22750213	0	45	gly	glycosylation	9:21	arg1	PRiMA	PRiMA				PUBTATOR		PRiMA	170952		N-linked glycosylation of proline-rich membrane anchor (PRiMA) is not required for assembly and trafficking of globular tetrameric acetylcholinesterase.
17503783	3	42	part_of	EGF-like	766:773	arg1	a novel, EGF-like domain	EGF		a novel, EGF-like domain		OGER	Site	EGF	P01133	domain	The crystal structure reveals a molecule composed of two closely associated domains: a catalytic domain that adopts a distorted (beta/alpha)8 barrel resembling that of bee venom hyaluronidase, and a novel, EGF-like domain, characteristic of involvement in protein-protein interactions and regulatory processes.
17503783	3	42	part_of	EGF-like	766:773	arg1	two closely associated domains	EGF		two closely associated domains		OGER	Site	EGF	P01133	domains	The crystal structure reveals a molecule composed of two closely associated domains: a catalytic domain that adopts a distorted (beta/alpha)8 barrel resembling that of bee venom hyaluronidase, and a novel, EGF-like domain, characteristic of involvement in protein-protein interactions and regulatory processes.
8702538	10	23	gly	glycosylation	1644:1656	arg2	a single N-linked glycosylation site			a single N-linked glycosylation site						site	These observations suggest that a single N-linked glycosylation site located at a similar position in the CD22 and CD33 glycoproteins is critical for regulating ligand recognition by both receptors.
8702538	10	29	gly	glycoproteins	1714:1726	arg1	the CD22 and CD33 glycoproteins	the CD22 and CD33 glycoproteins				PUBTATOR		CD33 glycoproteins	945		These observations suggest that a single N-linked glycosylation site located at a similar position in the CD22 and CD33 glycoproteins is critical for regulating ligand recognition by both receptors.
12438562	8	49	part_of	sites	1309:1313	arg1	the nucleoporin Nup155	Nup155		sites		PUBTATOR	Site	Nup155	117021	sites	BEMAD was then used on a purified nuclear pore complex preparation to map novel sites of O-GlcNAc modification on the Lamin B receptor and the nucleoporin Nup155.
12438562	8	49	part_of	sites	1309:1313	arg1	the Lamin B receptor	Lamin B receptor		sites		PUBTATOR	Site	Lamin B receptor	89789	sites	BEMAD was then used on a purified nuclear pore complex preparation to map novel sites of O-GlcNAc modification on the Lamin B receptor and the nucleoporin Nup155.
1533633	4	77	part_of	sites	744:748	arg1	the alpha-subunit	subunit		sites		OGER	Site	subunit	P06865	sites	By expression of the mutant cDNAs in COS-1 cells, each of the three glycosylation sites on the alpha-subunit was found to be modified by an oligosaccharide.
9786864	7	15	part_of	receptor	1111:1118	arg1	the C-terminal cytokine receptor homology domain	receptor		the C-terminal cytokine receptor homology domain		Fterm	Site	receptor		domain	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
11805077	0	13	gly	oligosaccharides	41:56	arg1	erythropoietin	erythropoietin			oligosaccharides	OGER		erythropoietin	P01588		Structural analysis of sulfated N-linked oligosaccharides in erythropoietin.
19855092	10	88	gly	desialylated	1724:1735	arg1	desialylated adiponectin	desialylated adiponectin				PUBTATOR		adiponectin	Q15848		Finally, after chronic administration in adiponectin(-/-) mice steady-state levels of desialylated adiponectin were lower than control adiponectin and failed to recapitulate the improvements in glucose and insulin tolerance tests observed with control adiponectin.
23285087	3	41	gly	glycosylation	640:652	arg2	the putative glycosylation sites			the putative glycosylation sites						sites	However, experimental evidence is still lacking on how such a post-translational modification affect the transport activity of OATPs and which of the putative glycosylation sites are utilized in these transporter proteins.
6966283	10	42	gly	position	1025:1032	arg1	mannose			position	mannose					position	B-type oligosaccharide chains have an additional trisaccharide, i.e. NeuAc 2 alpha leads to 3 Gal 1 beta leads to 4 GlcNAc attached to mannose at the (a) and/or (b) position of A-type chains by a beta 1 leads to 4 linkage.
29632068	6	57	part_of	CerS2	1033:1037	arg1	11 residues	CerS2		11 residues		PUBTATOR	Site	CerS2	29956	residues	The specificity of a chimeric protein, CerS5(299-309→CerS2), based on the backbone of CerS5 (which generates C16-ceramide), but containing 11 residues from CerS2 (which generates C22-C24-ceramides), was altered such that it generated C22-C24 and other ceramides.
29632068	6	61	part_of	containing	1005:1014	arg1	CerS5 AND 11 residues	CerS5		11 residues		PUBTATOR	Site	CerS5	91012	residues	The specificity of a chimeric protein, CerS5(299-309→CerS2), based on the backbone of CerS5 (which generates C16-ceramide), but containing 11 residues from CerS2 (which generates C22-C24-ceramides), was altered such that it generated C22-C24 and other ceramides.
17139081	5	33	gly	deglycosylated	774:787	arg1	the partially deglycosylated enzyme	the partially deglycosylated enzyme				Fterm		enzyme			The structure of intact fully glycosylated Cerezyme is virtually identical to that of the partially deglycosylated enzyme.
25568315	9	17	gly	N-glycosylation	1681:1695	arg1	the membrane processed NBCe1-A dimer	the membrane processed NBCe1-A dimer				PUBTATOR		NBCe1-A dimer	8671		Moreover, the formation of this unique structure is critically dependent on the finely tuned interplay between disulfide bonding and N-glycosylation in the membrane processed NBCe1-A dimer.
8344278	2	64	gly	glycoproteins	364:376	arg1	small glycoproteins	small glycoproteins				Fterm		glycoproteins			These saposins, together with saposin B, are small glycoproteins, derived from separate domains of a single precursor, prosaposin, and are required for the lysosomal hydrolysis of various sphingolipids.
17542669	5	27	part_of	2,500	690:694	arg1	2,500 A	large (2,500		A(2)		OGER	SpecificSite	large (2,500	Q8N3Y3	A(2)	The interface buried in the complex is large (2,500 A(2)) and an extensive network of ionic, polar, and hydrophobic bonding is involved in the interaction.
20378933	10	23	gly	glycosylation	1491:1503	arg1	glycosylation at N58 site			N58 site						N58 site	These data demonstrated that glycosylation at N58 site influenced FcalphaR binding to IgA.
18533687	0	92	gly	glycosylation	95:107	arg1	receptor function	receptor function				Fterm		receptor			Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	0	100	gly	glycosylation	31:43	arg2	the N-linked glycosylation sites	receptor		sites		Fterm		receptor		sites	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
17322565	6	63	part_of	EL	1066:1067	arg1	Asn-116	EL		Asn-116		PUBTATOR	SpecificSite	EL	9388	Asn-116	Finally, we introduced Asn-116 of EL into the analogous positions within LPL and HL, resulting in N-linked glycosylation at this site.
27314333	10	39	gly	Rspo1	1590:1594	arg1	N-glycan	Rspo1			N-glycan	PUBTATOR		Rspo1	284654		While N-glycan of Rspo1 plays a role in its intracellular stability, it had little effect on secreted Rspo1.
1731338	6	60	gly	galactoglycoprotein	1001:1019	arg1	the galactoglycoprotein polypeptide	the galactoglycoprotein polypeptide				PUBTATOR		galactoglycoprotein	6693		A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
16332679	0	95	gly	o-glycosylation	71:85	arg1	sp1	sp1				OGER		sp1	P08047		Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
8942648	13	42	part_of	TPO	1825:1827	arg1	the C-terminal domain	TPO		the C-terminal domain		PUBTATOR	Site	TPO	7066	domain	Furthermore, we propose that the C-terminal domain of TPO be further divided into two domains on the basis of sequence homology among the cloned sequences and glycosylation/structural features: an N-glycan domain (154-246) and an O-glycan domain (247-332).
19252480	6	49	part_of	TLR4	946:949	arg1	the conserved phenylalanines	TLR4		the conserved phenylalanines		OGER	AminoAcid	TLR4	O00206	phenylalanines	Five of the six lipid chains of LPS are buried deep inside the pocket and the remaining chain is exposed to the surface of MD-2, forming a hydrophobic interaction with the conserved phenylalanines of TLR4.
1544894	4	50	part_of	containing	768:777	arg1	peptides AND these sites	peptides		these sites						sites	We isolated peptides containing these sites to determine, primarily by mass spectrometric analysis, the presence of O-linked fucose and/or beta-hydroxyaspartate.
2113054	9	12	gly	glycopeptides	1559:1571	arg2	glycopeptides			glycopeptides						glycopeptides	The disulfide bonds of sCD4 were determined to be within domains 1, 2, and 4 and isolation of glycopeptides showed that both N-linked sites were glycosylated.
2113054	9	80	gly	glycosylated	1610:1621	arg1	both N-linked sites			both N-linked sites						sites	The disulfide bonds of sCD4 were determined to be within domains 1, 2, and 4 and isolation of glycopeptides showed that both N-linked sites were glycosylated.
8142896	4	17	gly	utilized	754:761	arg2	Asn69			Asn17 and Asn69						Asn17 and Asn69	Amino acid sequence analysis and ion spray mass spectrometry revealed that of the five potential sites for N-linked glycosylation, Asn17 and Asn69 were always utilized, whereas Asn62 and Asn162 were utilized in approximately one-third of the protein population.
8142896	4	60	gly	utilized	794:801	arg2	Asn162			Asn62 and Asn162						Asn62 and Asn162	Amino acid sequence analysis and ion spray mass spectrometry revealed that of the five potential sites for N-linked glycosylation, Asn17 and Asn69 were always utilized, whereas Asn62 and Asn162 were utilized in approximately one-third of the protein population.
2514791	6	103	part_of	t-PA	1894:1897	arg1	the same t-PA polypeptide	t-PA		the same t-PA polypeptide		PUBTATOR	Site	t-PA	5327	polypeptide	Further, the two cell lines express no glycoform in common, despite expressing the same t-PA polypeptide.
15099525	2	47	part_of	ICAM-1	263:268	arg1	an entire ICAM-1 extracellular fragment	ICAM-1		an entire ICAM-1 extracellular fragment		PUBTATOR	Site	ICAM-1	3383	fragment	Combined with the previously known N-terminal two-domain structure (D1D2), a model of an entire ICAM-1 extracellular fragment has been constructed.
16750161	3	5	gly	glycoprotein	652:663	arg1	The 108-amino acid CHO-expressed protein	The 108-amino acid CHO-expressed protein				Fterm		protein			The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	3	5	gly	glycoprotein	652:663	arg1	an O-linked glycoprotein	an O-linked glycoprotein				Fterm		glycoprotein			The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
8798614	2	31	gly	glycosylation	373:385	arg1	Asn18			Asn18						Asn18	Approximately 50% of the total apparent mass of CD59 is attributable to glycosylation of a single Asn (Asn18).
8798614	2	31	gly	glycosylation	373:385	arg1	a single Asn			a single Asn						Asn	Approximately 50% of the total apparent mass of CD59 is attributable to glycosylation of a single Asn (Asn18).
6192908	1	2	gly	alpha-fetoprotein	94:110	arg1	The carbohydrate moiety	alpha-fetoprotein			The carbohydrate moiety	PUBTATOR		alpha-fetoprotein	174		The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice was quantitatively released from the polypeptide chain as oligosaccharides by hydrazinolysis.
1820200	2	52	gly	glycopeptides	567:579	arg2	the glycopeptides			the glycopeptides						glycopeptides	Following purification by reverse-phase HPLC and identification by amino acid sequencing, the glycopeptides were analysed by one- and two-dimensional 1H NMR spectroscopy.
9169007	7	85	gly	glycoform	1192:1200	arg1	the low heparin affinity glycoform	the low heparin affinity glycoform				Fterm		heparin			These results demonstrate that heterogeneous glycosylation of Asn 155 of recombinant antithrombin is responsible for generating the low heparin affinity glycoform.
9169007	7	88	gly	glycosylation	1084:1096	arg1	Asn 155			Asn 155						Asn 155	These results demonstrate that heterogeneous glycosylation of Asn 155 of recombinant antithrombin is responsible for generating the low heparin affinity glycoform.
19139490	0	17	gly	fucosylated	62:72	arg1	core fucosylated glycoproteins	core fucosylated glycoproteins				Fterm		glycoproteins			A strategy for precise and large scale identification of core fucosylated glycoproteins.
19139490	0	22	gly	glycoproteins	74:86	arg1	core fucosylated glycoproteins	core fucosylated glycoproteins				Fterm		glycoproteins			A strategy for precise and large scale identification of core fucosylated glycoproteins.
22750213	3	41	gly	glycosylation	492:504	arg1	T	T				Cterm		T	11423		The glycosylation of AChE(T) is known to be required for its proper assembly and trafficking; however, the role of PRiMA glycosylation in the oligomer assembly has not been revealed.
22750213	3	41	gly	glycosylation	492:504	arg1	AChE	AChE				PUBTATOR		AChE	11423		The glycosylation of AChE(T) is known to be required for its proper assembly and trafficking; however, the role of PRiMA glycosylation in the oligomer assembly has not been revealed.
26783088	4	27	gly	occupied	633:640	arg2	the binuclear site			the binuclear site						site	We show that the binuclear site of SMPDL3a is occupied by two Zn(2+) ions and that excess Zn(2+) leads to inhibition of enzyme activity through binding to additional sites.
1381905	6	32	gly	glycosylated	1048:1059	arg1	cell-associated glycosylated SCF	cell-associated glycosylated SCF				OGER		SCF	P21583		Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
30127001	9	46	gly	site	1495:1498	arg1	serine 435			serine 435	serine 435		SpecificSite			serine 435	Mutation of the O-Glc modification site on EGF11 (serine 435) in combination with sensitizing O-fucose mutations in EGF8 or EGF12 affected cell-surface presentation of NOTCH1 or reduced activation of NOTCH1 by Delta-like1, respectively.
12620237	2	2	part_of	EGF	372:374	arg1	the 621 amino acid EGF receptor extracellular region	EGF		the 621 amino acid EGF receptor extracellular region		PUBTATOR	Site	EGF	1950	region	EGF activates its receptor by inducing dimerization of the 621 amino acid EGF receptor extracellular region.
18514042	4	19	gly	glycoproteins	827:839	arg1	commercially available glycoproteins	commercially available glycoproteins				Fterm		glycoproteins			Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
24134926	9	64	part_of	HAS2	1646:1649	arg1	serine 221 residue	HAS2		serine 221 residue		PUBTATOR	SpecificSite	HAS2	3037	serine 221 residue	Such highly dynamic and ubiquitous protein modification affects serine 221 residue of HAS2 that lead to a dramatic stabilization of the enzyme in the membranes.
1421756	2	63	gly	oligosaccharides	339:354	arg1	the receptor	receptor			oligosaccharides	Fterm		receptor			In the present study, we report our identification of the site of attachment of the O-linked oligosaccharides in the receptor.
18203274	6	15	gly	disialylated	798:809	arg1	mono- and disialylated N-glycans				mono- and disialylated N-glycans						Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
18203274	6	47	gly	glycoprotein	843:854	arg1	this glycoprotein	this glycoprotein				Fterm		glycoprotein			Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
18203274	6	50	gly	N-glycosylation	750:764	arg2	all nine potential N-glycosylation sites			all nine potential N-glycosylation sites						sites	Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
6785754	2	10	part_of	contains	275:282	arg1	The fragment AND 226 amino acid residues	The fragment		226 amino acid residues						residues	The fragment contains 226 amino acid residues and has a molecular weight of 32,000 per monomeric unit.
9030779	1	22	gly	asparagine-linked	209:225	arg1	asparagine-linked oligosaccharides			asparagine	asparagine-linked oligosaccharides					asparagine	Most soluble lysosomal enzymes require a mannose-6-phosphate recognition marker present on asparagine-linked oligosaccharides for proper targeting to lysosomes.
11371615	8	55	gly	O-GlcNAcylation	1386:1400	arg1	transcriptional regulation				transcriptional regulation						Thus, our studies provide direct evidence that O-GlcNAcylation of transcription factors is involved in transcriptional regulation.
11983428	2	17	part_of	protein-protein	371:385	arg1	A single sterile alpha motif (SAM) protein-protein interaction domain	protein		A single sterile alpha motif (SAM) protein-protein interaction domain		Fterm	Site	protein		domain	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	2	73	part_of	SAM	366:368	arg1	A single sterile alpha motif (SAM) protein-protein interaction domain	SAM		A single sterile alpha motif (SAM) protein-protein interaction domain		Cterm	Site	SAM		domain	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
19285951	3	6	gly	glycopeptide	698:709	arg2	HRG-derived glycopeptide affinity chromatography			HRG-derived glycopeptide affinity chromatography						glycopeptide	In the present study, we identified the alpha-subunit of ATP synthase as one of the HRG-binding proteins on the surface of T-cells by HRG-derived glycopeptide affinity chromatography and by a peptide mass finger printing method.
21037563	8	22	part_of	perforin	1472:1479	arg1	the perforin MACPF domain	perforin		the perforin MACPF domain		Fterm	Site	perforin		domain	Most unexpectedly, however, electron microscopy reveals that the orientation of the perforin MACPF domain in the pore is inside-out relative to the subunit arrangement in CDCs.
21037563	8	68	part_of	MACPF	1481:1485	arg1	the perforin MACPF domain	MACPF		the perforin MACPF domain		Cterm	Site	MACPF		domain	Most unexpectedly, however, electron microscopy reveals that the orientation of the perforin MACPF domain in the pore is inside-out relative to the subunit arrangement in CDCs.
18775496	6	1	part_of	agrin	1081:1085	arg1	the EGF4 domain	agrin		the EGF4 domain		PUBTATOR	Site	agrin	O00468	domain	In addition, Pofut1 gene and protein expression and Pofut1 activity of the EGF4 domain of agrin were modulated during neuromuscular development.
9884403	5	76	gly	glycosylation	1013:1025	arg2	Only glycosylation site Asn251			site Asn251						site Asn251	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9689040	6	47	gly	asparagine-linked	795:811	arg1	an asparagine-linked sugar cluster			asparagine	an asparagine-linked sugar cluster					asparagine	Virtually all of an asparagine-linked sugar cluster is present.
17395588	7	37	part_of	residues	1297:1304	arg1	TSR3	TSR3		residues		PUBTATOR	AminoAcid	TSR3	115939	residues in	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	7	37	part_of	residues	1297:1304	arg1	TSR2	TSR2		residues		PUBTATOR	AminoAcid	TSR2	90121	residues in	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
22678432	7	8	gly	IgG	1212:1214	arg1	released glycans	IgG			released glycans	Cterm		IgG			The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	7	14	gly	rHuEPO	1201:1206	arg1	released glycans	rHuEPO			released glycans	Cterm		rHuEPO	2056		The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	7	46	gly	glycopeptides	1393:1405	arg2	the glycopeptides			the glycopeptides						glycopeptides	The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
1908233	2	44	gly	acids	390:394	arg1	Ser			Ser and Thr						Ser and Thr	The O-glycosidic linkage of carbohydrate to the hydroxy amino acids Ser and Thr is a major form of post-translational modification.
17117926	7	41	part_of	Fz5	908:910	arg1	the extracellular domain	Fz5		the extracellular domain		PUBTATOR	Site	Fz5	7855	domain	Furthermore, the binding of Wnt-5a to the extracellular domain of Fz5 required palmitoylation of Wnt-5a.
9539703	0	69	part_of	ICAM-1	57:62	arg1	the two amino-terminal domains	ICAM-1		the two amino-terminal domains		PUBTATOR	Site	ICAM-1	3383	domains	The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand.
17525160	12	22	gly	glycosylation	1479:1491	arg2	Thr-27			Thr-27						Thr-27	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
7451505	2	13	gly	released	220:227	arg2	human ceruloplasmin AND the oligosaccharides	human ceruloplasmin			the oligosaccharides	PUBTATOR		ceruloplasmin	1356		The structures of the oligosaccharides released from human ceruloplasmin by hydrazinolysis were studied by sequential exoglycosidase digestion in combination with methylation analysis and periodate oxidation.
8489250	1	0	gly	glycoprotein	235:246	arg1	recombinant human differentiation-stimulating factor	recombinant human differentiation-stimulating factor				Fterm		factor			This report describes the post-translational modifications of recombinant human differentiation-stimulating factor, a 180-residue glycoprotein that is secreted from transfected Chinese hamster ovary cells.
8489250	1	0	gly	glycoprotein	235:246	arg1	a 180-residue glycoprotein	a 180-residue glycoprotein				Fterm		glycoprotein			This report describes the post-translational modifications of recombinant human differentiation-stimulating factor, a 180-residue glycoprotein that is secreted from transfected Chinese hamster ovary cells.
24530628	6	10	gly	glycopeptides	953:965	arg2	glycopeptides			glycopeptides						glycopeptides	We propose that this method is a powerful tool for the acquisition of reliable mass spectra from trace amounts of glycopeptides and an alternative to lectin affinity enrichment.
18250328	7	28	part_of	protein	1030:1036	arg1	a candidate NRX interaction site	protein		a candidate NRX interaction site		Fterm	Site	protein		site	On the opposite surface of the NL2A molecule, the positions of the A and B splice insertions identify a candidate NRX interaction site of the NL protein.
18250328	7	67	part_of	NRX	999:1001	arg1	a candidate NRX interaction site	NRX		a candidate NRX interaction site		PUBTATOR	Site	NRX	64359	site	On the opposite surface of the NL2A molecule, the positions of the A and B splice insertions identify a candidate NRX interaction site of the NL protein.
1371281	9	20	gly	sites	1256:1260	arg1	a single O-linked N-acetylglucosamine			sites	a single O-linked N-acetylglucosamine					sites	Our results show that CK8 and 18 are glycosylated at multiple sites with a single O-linked N-acetylglucosamine.
1371281	9	14	gly	glycosylated	1231:1242	arg2	multiple sites	CK8		sites		PUBTATOR		CK8	3856	sites	Our results show that CK8 and 18 are glycosylated at multiple sites with a single O-linked N-acetylglucosamine.
1997323	10	47	gly	glycoproteins	1173:1185	arg1	other plasma glycoproteins	other plasma glycoproteins				Fterm		glycoproteins			Thus, in rTf-3, both antennae were of the disialylated diantennary N-acetyllactosamine type which is frequently encountered in other plasma glycoproteins.
1997323	10	55	gly	type	1120:1123	arg1	rTf-3	rTf			type	Cterm		rTf	24825		Thus, in rTf-3, both antennae were of the disialylated diantennary N-acetyllactosamine type which is frequently encountered in other plasma glycoproteins.
1997323	10	67	gly	disialylated	1075:1086	arg1	the disialylated diantennary N-acetyllactosamine type				the disialylated diantennary N-acetyllactosamine type						Thus, in rTf-3, both antennae were of the disialylated diantennary N-acetyllactosamine type which is frequently encountered in other plasma glycoproteins.
8390218	0	42	gly	fucosylated	82:92	arg1	fucosylated biantennary glycan				fucosylated biantennary glycan						Structural analysis on the sugar chains of human alpha 1-antitrypsin: presence of fucosylated biantennary glycan in hepatocellular carcinoma.
8390218	0	85	gly	1-antitrypsin	55:67	arg1	the sugar chains	alpha 1-antitrypsin			the sugar chains	PUBTATOR		alpha 1-antitrypsin	5265		Structural analysis on the sugar chains of human alpha 1-antitrypsin: presence of fucosylated biantennary glycan in hepatocellular carcinoma.
9767079	6	37	part_of	terminus	1080:1087	arg1	a hemagglutinin (HA) epitope	terminus		a hemagglutinin (HA) epitope						epitope	Wild-type and Gln58-RFCs containing a hemagglutinin (HA) epitope at the carboxyl terminus were similarly functional and, by immunofluorescence staining with rhodamine-conjugated anti-HA antibody, were localized to plasma membranes.
25517345	3	6	gly	deletions	457:465	arg1	gp120	gp120			deletions	PUBTATOR		gp120	155971		It has been shown that long-term CBA pressure in vitro can result in mutant HIV-1 isolates with several N-linked glycan deletions on gp120.
18768590	6	26	part_of	WNK3	969:972	arg1	The kinase domain	WNK3		The kinase domain		PUBTATOR	Site	WNK3	Q9BYP7	domain	The kinase domain of WNK3 alone was sufficient to increase TRPV5-mediated Ca2+ transport, and the positive regulatory effect was abolished by the kinase-inactive D294A mutation in WNK3, indicating a kinase-dependent mechanism.
21402931	5	16	part_of	ZP-N	782:785	arg1	the ZP-N region	ZP		the ZP-N region		Cterm	Site	ZP		region	Similar to the ZP-N region, the ZP-C region also adopts an immunoglobulin-like fold, despite sharing no sequence homology and possessing different disulfide linkages.
21402931	5	24	part_of	ZP-C	799:802	arg1	the ZP-C region	ZP		the ZP-C region		Cterm	Site	ZP		region	Similar to the ZP-N region, the ZP-C region also adopts an immunoglobulin-like fold, despite sharing no sequence homology and possessing different disulfide linkages.
15066430	1	76	part_of	proteins	362:369	arg1	C-terminal basic residues	proteins		C-terminal basic residues		Fterm	Site	proteins		residues	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	1	80	part_of	peptides	349:356	arg1	C-terminal basic residues	peptides		C-terminal basic residues						residues	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
18514042	4	34	part_of	ceruloplasmin	678:690	arg1	Glycopeptide	ceruloplasmin		Glycopeptide		OGER	Site	ceruloplasmin	P00450	Glycopeptide	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	4	57	part_of	IgG	657:659	arg1	Glycopeptide	IgG		Glycopeptide		Cterm	Site	IgG		Glycopeptide	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	4	67	part_of	haptoglobin	662:672	arg1	Glycopeptide	haptoglobin		Glycopeptide		PUBTATOR	Site	haptoglobin	3240	Glycopeptide	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
20223216	4	20	part_of	receptor	649:656	arg1	peripheral receptor residues	receptor		peripheral receptor residues		Fterm	Site	receptor		residues	While retaining a similar mode of IL-13 binding to its related signaling receptor, IL-13Ralpha1, IL-13Ralpha2 uses peripheral receptor residues unused in the IL-13/IL-13Ralpha1 complex to generate a larger and more complementary interface for IL-13.
25458834	1	35	gly	O-glycoprotein	149:162	arg1	a transmembrane O-glycoprotein	a transmembrane O-glycoprotein				Fterm		O-glycoprotein			Podoplanin is a transmembrane O-glycoprotein that binds to C-type lectin-like receptor 2 (CLEC-2).
25458834	1	35	gly	O-glycoprotein	149:162	arg1	Podoplanin	Podoplanin				OGER		Podoplanin	Q86YL7		Podoplanin is a transmembrane O-glycoprotein that binds to C-type lectin-like receptor 2 (CLEC-2).
8163535	11	64	part_of	sequences	1638:1646	arg1	an exposed hydrophilic region	sequences		an exposed hydrophilic region						region	This cluster contains the sequences FSGSGTG and DGSGD, the former estimated to be in a hydrophobic pocket and the latter, similar to the sequence on the C-terminal cluster, in an exposed hydrophilic region.
6689265	1	28	gly	protein	198:204	arg1	the carbohydrate chain	vitamin D-binding protein			the carbohydrate chain	PUBTATOR		vitamin D-binding protein	2638		On a highly purified preparation, the structure of the carbohydrate chain of the human vitamin D-binding protein was investigated and two genetic forms of this protein were considered (Gc 2 and Gc 1 proteins).
8069634	3	27	gly	fucosylated	481:491	arg1	the fucosylated biantennary N-acetyllactosamine-type glycans				the fucosylated biantennary N-acetyllactosamine-type glycans						Lectins from the Viciae tribe have a high affinity for the fucosylated biantennary N-acetyllactosamine-type glycans which are to be found in the majority of N-glycosylproteins.
2033371	7	116	gly	carry	1216:1220	arg1	WAS lymphocyte CD43 AND predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	WAS lymphocyte CD43			predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	PUBTATOR		CD43	6693		WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
26791533	7	2	part_of	sites	1017:1021	arg1	50 glycoproteins	glycoproteins		sites		Fterm	Site	glycoproteins		sites	We have elucidated glycan compositions and proposed structures for 243 glycopeptides belonging to 73 N-glycosylation sites on 50 glycoproteins.
9786864	7	40	gly	glycosylated	1140:1151	arg1	Asn624			Asn624						Asn624	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
9786864	7	63	gly	residues	1062:1069	arg1	622-626			622-626						residues 622-626	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
23661698	9	52	gly	glycosylation	1255:1267	arg1	ephrin-A1	ephrin-A1				PUBTATOR		ephrin-A1	1942		These findings suggest that the glycosylation on ephrin-A1 plays a critical role in the binding and activation of the EphA2 receptor.
15173186	11	75	part_of	receptor	1640:1647	arg1	Toll-like receptor 2 extracellular domain	Toll-like receptor 2		Toll-like receptor 2 extracellular domain		PUBTATOR	Site	Toll-like receptor 2	7097	domain	Using site-directed mutagenesis, we have found that in Toll-like receptor 2 extracellular domain all four predicted glycosylation sites are substituted, although one site is inefficiently core-glycosylated and its removal drastically affects secretion.
16714295	2	4	gly	Glycosylation	182:194	arg1	intracellular proteins	intracellular proteins				Fterm		proteins			Glycosylation of intracellular proteins is a dynamic process that in several cases competes with and acts as a reciprocal modification system to phosphorylation.
29391424	5	70	part_of	containing	646:655	arg1	257 glycoproteins AND 970 unique glycosylation sites	257 glycoproteins		970 unique glycosylation sites		Fterm	Site	glycoproteins		sites	In a large-scale study, a total of 257 glycoproteins containing 970 unique glycosylation sites and 3447 non-redundant N-linked glycopeptide variants were identified in 24 serum samples.
28207759	3	67	gly	containing	437:446	arg1	recombinant GBA AND mannose-terminated N-linked glycans	recombinant GBA			mannose-terminated N-linked glycans	PUBTATOR		GBA	2629		Supplementing storage cells with lacking enzyme is accomplished via chronic intravenous administration of recombinant GBA containing mannose-terminated N-linked glycans, mediating the selective uptake by macrophages expressing mannose-binding lectin(s).
10821832	4	60	part_of	contains	986:993	arg1	this glycoprotein AND 13 transmembrane domains	this glycoprotein		13 transmembrane domains		Fterm	Site	glycoprotein		domains	Our data indicate that this glycoprotein contains 13 transmembrane domains, 3 large and 4 small luminal loops, 6 small cytoplasmic loops, and a cytoplasmic tail.
10821832	4	60	part_of	contains	986:993	arg1	this glycoprotein AND a cytoplasmic tail	this glycoprotein		a cytoplasmic tail		Fterm	Site	glycoprotein		tail	Our data indicate that this glycoprotein contains 13 transmembrane domains, 3 large and 4 small luminal loops, 6 small cytoplasmic loops, and a cytoplasmic tail.
17395588	5	68	gly	bear	927:930	arg1	the appropriate peptides AND a fucose monosaccharide			the appropriate peptides	a fucose monosaccharide					peptides	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	68	gly	bear	927:930	arg1	the appropriate peptides AND a fucose-glucose disaccharide			the appropriate peptides	a fucose-glucose disaccharide					peptides	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
27768895	5	34	part_of	PKD2	759:762	arg1	The extracellular domain	PKD2		The extracellular domain		PUBTATOR	Site	PKD2	Q13563	domain	The extracellular domain of PKD2, a hotspot for ADPKD pathogenic mutations, contributes to channel assembly and strategically interacts with the transmembrane core, likely serving as a physical substrate for extracellular stimuli to allosterically gate the channel.
18642129	8	43	gly	found	1216:1220	arg1	Asn AND triantennary structures			Asn(322)	triantennary structures					Asn(322)	Nevertheless, lower amounts of triantennary structures were found on Asn(322) compared to Asn(145).
1885588	0	81	gly	glycoprotein	53:64	arg1	a transmembrane endoplasmic reticular glycoprotein	a transmembrane endoplasmic reticular glycoprotein				Fterm		glycoprotein			Glucosidase I, a transmembrane endoplasmic reticular glycoprotein with a luminal catalytic domain.
8344946	6	58	gly	glycosylation	1145:1157	arg2	both major sites			both major sites						sites	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	6	28	gly	glycosylation	1145:1157	arg1	Ser27			Thr21 and Ser27						Thr21 and Ser27	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
21173149	7	17	part_of	contains	910:917	arg1	The γ-subunit AND two in vivo used N-glycosylation sites	The γ-subunit		two in vivo used N-glycosylation sites		Fterm	Site	γ-subunit		sites	The γ-subunit contains two in vivo used N-glycosylation sites at positions 88 and 115, equipped with high mannose-type oligosaccharides.
1380064	5	93	part_of	found	904:908	arg2	EoCP-2 AND serine residues	EoCP-2		serine residues		OGER	AminoAcid	EoCP	P13501	serine residues	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
1380064	5	93	part_of	found	904:908	arg2	EoCP-2 AND the residues 4 and 5	EoCP-2		the residues 4 and 5		OGER	SpecificSite	EoCP	P13501	residues 4 and 5	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
10978165	9	13	gly	nonglycosylated	1128:1142	arg1	1-74	1-74				Cterm		1-74	6358		In hemofiltrate approximately 3% of total HCC-1 represents HCC-1 (3-74) and approximately 1% represents HCC-1 (4-74) whereas the major products are nonglycosylated HCC-1 (1-74) and glycosylated HCC-1 (1-74).
10978165	9	13	gly	nonglycosylated	1128:1142	arg1	nonglycosylated HCC-1	nonglycosylated HCC-1				PUBTATOR		HCC-1	6358		In hemofiltrate approximately 3% of total HCC-1 represents HCC-1 (3-74) and approximately 1% represents HCC-1 (4-74) whereas the major products are nonglycosylated HCC-1 (1-74) and glycosylated HCC-1 (1-74).
10978165	9	18	gly	glycosylated	1161:1172	arg1	1-74	1-74				Cterm		1-74	6358		In hemofiltrate approximately 3% of total HCC-1 represents HCC-1 (3-74) and approximately 1% represents HCC-1 (4-74) whereas the major products are nonglycosylated HCC-1 (1-74) and glycosylated HCC-1 (1-74).
10978165	9	18	gly	glycosylated	1161:1172	arg1	glycosylated HCC-1	glycosylated HCC-1				PUBTATOR		HCC-1	6358		In hemofiltrate approximately 3% of total HCC-1 represents HCC-1 (3-74) and approximately 1% represents HCC-1 (4-74) whereas the major products are nonglycosylated HCC-1 (1-74) and glycosylated HCC-1 (1-74).
8942648	7	20	part_of	TPO	915:917	arg1	the amino acid sequence	TPO 1-246		the amino acid sequence		PUBTATOR	Site	TPO 1-246	256987	sequence	The results of our analysis of TPO indicate that the amino acid sequence of TPO 1-246 is as expected from the transfected cDNA with complete cleavage of the signal peptide.
9295302	5	26	gly	N-glycosylation	783:797	arg2	the 14 N-glycosylation sequons			the 14 N-glycosylation sequons							To aid in determining the topology most likely to be correct, we have identified which of the 14 N-glycosylation sequons in this protein are utilized.
2141278	4	56	part_of	C1-r	1223:1226	arg1	the homologous position	C1-r		the homologous position		PUBTATOR	Site	C1-r	715	position	This fragment was reduced and alkylated and then digested with elastase, and three peptides covering positions 131-135, 131-139, and 131-140 were characterized by amino acid analysis, Edman degradation, and mass spectrometry, showing that position 134 of C1-s is occupied partly by an asparagine (47%) and partly by an erythro-beta-hydroxyasparagine, in contrast with the homologous position (150) of C1-r which only contains erythro-beta-hydroxyasparagine.
2141278	4	61	part_of	C1-s	1077:1080	arg1	position 134	C1-s		position 134		PUBTATOR	Site	C1-s	716	position 134	This fragment was reduced and alkylated and then digested with elastase, and three peptides covering positions 131-135, 131-139, and 131-140 were characterized by amino acid analysis, Edman degradation, and mass spectrometry, showing that position 134 of C1-s is occupied partly by an asparagine (47%) and partly by an erythro-beta-hydroxyasparagine, in contrast with the homologous position (150) of C1-r which only contains erythro-beta-hydroxyasparagine.
3756141	5	70	part_of	protein	643:649	arg1	residues 1-120	protein		residues 1-120		Fterm	SpecificSite	protein		residues 1-120	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3567160	1	18	gly	G	190:190	arg1	oligosaccharides	immunoglobulin G			oligosaccharides	Cterm		immunoglobulin G			The structures of oligosaccharides of normal and pathological immunoglobulin G (IgG) are reported.
16332679	11	90	part_of	Sp1	1771:1773	arg1	common serine residues	Sp1		common serine residues		OGER	AminoAcid	Sp1	P08047	serine residues	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
10929010	2	31	gly	glycoforms	398:407	arg1	multiple transferrin glycoforms	multiple transferrin glycoforms				PUBTATOR		transferrin	7018		Metabolic radiolabeling of the intra- and extracellular protein fractions revealed the presence of multiple transferrin glycoforms with molecular weights lower than that observed for native human transferrin.
6118137	13	48	part_of	glycoprotein	1324:1335	arg1	The sequence	Thy-1 glycoprotein		The sequence		PUBTATOR	Site	Thy-1 glycoprotein	24832	sequence	The sequence of the Thy-1 glycoprotein showed homologies with immunoglobulin domains.
6574504	4	7	part_of	cathepsins	662:671	arg1	the amino acid sequences	cathepsins B		the amino acid sequences		OGER	Site	cathepsins B	P25774	sequences	Comparison of the amino acid sequences of cathepsins B and H with each other and with that of papain demonstrates a striking homology among their primary structures.
2737288	0	5	part_of	elastase	80:87	arg1	the glycosylation site	pancreatic elastase 1		the glycosylation site		PUBTATOR	Site	pancreatic elastase 1	1990	site	Localization and characterization of the glycosylation site of human pancreatic elastase 1.
29402915	7	48	part_of	protein	1388:1394	arg1	at least 4 residues	cubilin protein		at least 4 residues		PUBTATOR	Site	cubilin protein	8029	residues	Quantitative mass spectrometry and mutagenesis demonstrated that N-linked glycosylation of at least 4 residues of cubilin protein was required for its surface targeting.
11738084	4	19	gly	disialylated	573:584	arg1	a disialylated biantennary complex type oligosaccharide				a disialylated biantennary complex type oligosaccharide						The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	4	19	gly	disialylated	573:584	arg1	The glycan				The glycan						The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
8323299	5	72	gly	glycosylation	803:815	arg1	Ser-179			Ser-179 and Thr-181						Ser-179 and Thr-181	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	71	gly	glycosylation	697:709	arg2	Thr-185			Thr-185						Thr-185	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	71	gly	glycosylation	697:709	arg1	lamp-2	In lamp-2		Thr-185		PUBTATOR		In lamp-2	3920	Thr-185	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	71	gly	glycosylation	697:709	arg1	lamp-2	In lamp-2		Thr-185		PUBTATOR		In lamp-2	3920	Thr-185	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	71	gly	glycosylation	697:709	arg2	Ser-179			Ser-179 and Thr-181						Ser-179 and Thr-181	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	71	gly	glycosylation	697:709	arg1	lamp-2	In lamp-2		Ser-179 and Thr-181		PUBTATOR		In lamp-2	3920	Ser-179 and Thr-181	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	71	gly	glycosylation	697:709	arg1	lamp-2	In lamp-2		Ser-179 and Thr-181		PUBTATOR		In lamp-2	3920	Ser-179 and Thr-181	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
15809306	4	29	part_of	Known	557:561	arg1	Known DPPIV dipeptides	Known DPPIV		Known DPPIV dipeptides		PUBTATOR	Site	Known DPPIV	1803	dipeptides	Known DPPIV dipeptides are cleaved by FAPalpha with an approximately 100-fold decrease in catalytic efficiency compared with DPPIV.
15809306	4	41	part_of	DPPIV	563:567	arg1	Known DPPIV dipeptides	Known DPPIV		Known DPPIV dipeptides		PUBTATOR	Site	Known DPPIV	1803	dipeptides	Known DPPIV dipeptides are cleaved by FAPalpha with an approximately 100-fold decrease in catalytic efficiency compared with DPPIV.
30127001	3	42	gly	NOTCH1	497:502	arg1	Epidermal Growth Factor-like (EGF) repeat 11	NOTCH1			Epidermal Growth Factor-like (EGF) repeat 11	PUBTATOR		NOTCH1	4851		This serine occurs between conserved cysteines 3 and 4 of Epidermal Growth Factor-like (EGF) repeat 11 of NOTCH1, a site distinct from those modified by protein O-glucosyltransferase 1 (POGLUT1), suggesting that a different enzyme is responsible.
22624035	5	58	part_of	TSAP6	791:795	arg1	the third transmembrane domain	TSAP6		the third transmembrane domain		PUBTATOR	Site	TSAP6	55240	domain	In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6.
3410849	1	32	gly	glycopeptide	51:62	arg2	glycopeptide			glycopeptide						glycopeptide	A nephritogenic glycopeptide with alpha-N-glycosidic linkage.
9376680	0	32	gly	sequence	159:166	arg1	the carbohydrate sequence Gal(alpha1-3)GalNAc(alpha1-3)[Fuc(alpha1-2)]Gal				the carbohydrate sequence Gal(alpha1-3)GalNAc(alpha1-3)[Fuc(alpha1-2)]Gal						Structural analysis of oligosaccharide-alditols released by reductive beta-elimination from oviducal mucins of Bufo bufo: characterization of the carbohydrate sequence Gal(alpha1-3)GalNAc(alpha1-3)[Fuc(alpha1-2)]Gal.
8349699	7	45	gly	N-glycosylation	1047:1061	arg2	an additional site	PGH synthase-2		site		PUBTATOR		PGH synthase-2	19225	site	Using site-directed mutagenesis, we determined that there is an additional site of N-glycosylation in murine PGH synthase-2 located at Asn580.
9597769	0	53	gly	O-glycosylation	16:30	arg1	MUC1 tandem repeats			sites	MUC1 tandem repeats					sites	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
22000856	2	9	part_of	LRP5/6	233:238	arg1	The LRP5/6 ectodomain	LRP5		The LRP5/6 ectodomain		PUBTATOR	Site	LRP5	4041	ectodomain	The LRP5/6 ectodomain contains four β-propeller/EGF-like domain repeats.
19910922	0	0	part_of	subunit	76:82	arg1	the zinc-bound amino-terminal domain	NR2B subunit		the zinc-bound amino-terminal domain		PUBTATOR	Site	NR2B subunit	2904	domain	Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit.
8702840	2	31	part_of	neurofilament	342:354	arg1	three polypeptides, neurofilament (NF)-H, NF-M, and NF-L	neurofilament (NF)-H		three polypeptides, neurofilament (NF)-H, NF-M, and NF-L		PUBTATOR	Site	neurofilament (NF)-H	4744	polypeptides	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	2	56	part_of	NF	357:358	arg1	three polypeptides, neurofilament (NF)-H, NF-M, and NF-L	neurofilament (NF)-H		three polypeptides, neurofilament (NF)-H, NF-M, and NF-L		PUBTATOR	Site	neurofilament (NF)-H	4744	polypeptides	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
12794637	5	20	part_of	P4	1105:1106	arg1	lysine	P1 and P4		lysine		PUBTATOR	AminoAcid	P1 and P4	1423	lysine	Contoured surface loops shape the active site by cleft, thus explaining furin's stringent requirement for arginine at P1 and P4, and lysine at P2 sites by highly charge-complementary pockets.
12794637	5	20	part_of	P4	1105:1106	arg1	arginine	P1 and P4		arginine		PUBTATOR	AminoAcid	P1 and P4	1423	arginine	Contoured surface loops shape the active site by cleft, thus explaining furin's stringent requirement for arginine at P1 and P4, and lysine at P2 sites by highly charge-complementary pockets.
12794637	5	29	part_of	P1	1098:1099	arg1	lysine	P1 and P4		lysine		PUBTATOR	AminoAcid	P1 and P4	1423	lysine	Contoured surface loops shape the active site by cleft, thus explaining furin's stringent requirement for arginine at P1 and P4, and lysine at P2 sites by highly charge-complementary pockets.
12794637	5	29	part_of	P1	1098:1099	arg1	arginine	P1 and P4		arginine		PUBTATOR	AminoAcid	P1 and P4	1423	arginine	Contoured surface loops shape the active site by cleft, thus explaining furin's stringent requirement for arginine at P1 and P4, and lysine at P2 sites by highly charge-complementary pockets.
7541354	6	62	gly	vitronectin	738:748	arg1	The major oligosaccharides	vitronectin			The major oligosaccharides	PUBTATOR		vitronectin	7448		The major oligosaccharides of human vitronectin were of the diantennary N-acetyllactosamine type, with a lesser amount of the tri- and a small amount of the mono-antennary type, to which 1-3 mol sialic acid residues were linked, mostly through alpha 2-6 linkages, although alpha 2-3 linkages were also present.
10386995	3	21	gly	sites	619:623	arg1	synapsin I	synapsin I			sites	PUBTATOR		synapsin I	24949		Here, we identified seven in vivo O-GlcNAcylation sites on synapsin I by analysis of HPLC-purified digests of rat brain synapsin I.
8687384	1	14	gly	glycosylation	191:203	arg1	t-PA	t-PA				PUBTATOR		t-PA	5327		The glycosylation of tissue plasminogen activator (t-PA) obtained from the Bowes melanoma cell line was re-examined using methods of serial lectin affinity chromatography coupled with Bio-Gel P-4 gel filtration chromatography and exoglycosidase sequencing.
8687384	1	14	gly	glycosylation	191:203	arg1	tissue plasminogen activator	tissue plasminogen activator				OGER		tissue plasminogen activator	P00750		The glycosylation of tissue plasminogen activator (t-PA) obtained from the Bowes melanoma cell line was re-examined using methods of serial lectin affinity chromatography coupled with Bio-Gel P-4 gel filtration chromatography and exoglycosidase sequencing.
2514791	3	111	gly	N-glycosylation	644:658	arg2	the N-glycosylation sites			the N-glycosylation sites						sites	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
17255936	5	26	part_of	KIT	805:807	arg1	contact distinct KIT domains	KIT		contact distinct KIT domains		PUBTATOR	Site	KIT	3815	domains	Three surface epitopes on SCF, an extended loop, the B and C helices, and the N-terminal segment, contact distinct KIT domains, with two of the epitopes undergoing large conformational changes upon receptor binding.
17255936	5	27	part_of	SCF	716:718	arg1	the epitopes	SCF		the epitopes		PUBTATOR	Site	SCF	4254	epitopes	Three surface epitopes on SCF, an extended loop, the B and C helices, and the N-terminal segment, contact distinct KIT domains, with two of the epitopes undergoing large conformational changes upon receptor binding.
17255936	5	40	part_of	domains	809:815	arg1	the epitopes	domains		the epitopes						epitopes	Three surface epitopes on SCF, an extended loop, the B and C helices, and the N-terminal segment, contact distinct KIT domains, with two of the epitopes undergoing large conformational changes upon receptor binding.
17255936	5	59	part_of	epitopes	704:711	arg1	contact distinct KIT domains	epitopes		contact distinct KIT domains						domains	Three surface epitopes on SCF, an extended loop, the B and C helices, and the N-terminal segment, contact distinct KIT domains, with two of the epitopes undergoing large conformational changes upon receptor binding.
17255936	5	59	part_of	epitopes	704:711	arg1	SCF	SCF		epitopes		PUBTATOR	Site	SCF	4254	epitopes	Three surface epitopes on SCF, an extended loop, the B and C helices, and the N-terminal segment, contact distinct KIT domains, with two of the epitopes undergoing large conformational changes upon receptor binding.
24036510	3	16	part_of	fibronectin-like	501:516	arg1	a fibronectin-like domain	fibronectin		domain		PUBTATOR	Site	fibronectin	2335	domain	IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain.
24036510	3	39	part_of	TIM	426:428	arg1	a TIM barrel domain	TIM		domain		PUBTATOR	Site	TIM	7984	domain	IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain.
24036510	3	39	part_of	TIM	426:428	arg1	a fibronectin-like domain	TIM		domain		PUBTATOR	Site	TIM	7984	domain	IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain.
24036510	3	39	part_of	TIM	426:428	arg1	a fibronectin-like domain	TIM		domain		PUBTATOR	Site	TIM	7984	domain	IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain.
24036510	3	0	part_of	containing	444:453	arg1	a TIM barrel domain AND the catalytic site			site						site	IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain.
24036510	3	0	part_of	containing	444:453	arg1	a fibronectin-like domain AND the catalytic site			site						site	IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain.
24036510	3	0	part_of	containing	444:453	arg1	a fibronectin-like domain AND the catalytic site			site						site	IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain.
2547792	9	47	gly	glycoprotein	1419:1430	arg1	the labeled 45-kDa glycoprotein	the labeled 45-kDa glycoprotein				Fterm		glycoprotein			These results indicate that the labeled 45-kDa glycoprotein contains terminal sialic acid residues, explaining the low pI of this protein, and that it is characteristic for melanoma cells and hence part of the MSH receptor.
2547792	9	9	gly	contains	1432:1439	arg1	the labeled 45-kDa glycoprotein AND terminal sialic acid residues	the labeled 45-kDa glycoprotein			terminal sialic acid residues	Fterm		glycoprotein			These results indicate that the labeled 45-kDa glycoprotein contains terminal sialic acid residues, explaining the low pI of this protein, and that it is characteristic for melanoma cells and hence part of the MSH receptor.
7727388	2	56	gly	glycoprotein	242:253	arg1	a disulfide-linked homodimer	a disulfide-linked homodimer				PUBTATOR		homodimer	6647		This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	2	56	gly	glycoprotein	242:253	arg1	This cell surface glycoprotein	This cell surface glycoprotein				Fterm		glycoprotein			This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
29671580	1	1	gly	glycosylated	200:211	arg1	Most serum proteins	Most serum proteins				Fterm		proteins			Most serum proteins are N-linked glycosylated, and therefore the glycoproteomic profiling of serum is essential for characterization of serum proteins.
9883900	9	61	part_of	IGFBP-5	1272:1278	arg1	C-terminal IGFBP-5 fragments	IGFBP-5		C-terminal IGFBP-5 fragments		PUBTATOR	Site	IGFBP-5	3488	fragments	Fractions containing C-terminal IGFBP-5 fragments revealed significant IGF-I binding properties.
8142896	0	20	gly	receptor	102:109	arg1	the carbohydrate moieties	interferon gamma receptor			the carbohydrate moieties	PUBTATOR		interferon gamma receptor	3458		Structural analysis and localization of the carbohydrate moieties of a soluble human interferon gamma receptor produced in baculovirus-infected insect cells.
2793860	2	8	gly	glycoproteins	243:255	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	2	11	gly	O-glycosylation	224:238	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
3179269	2	41	gly	released	408:415	arg1	each EPO protein AND Asparagine-linked neutral oligosaccharides	each EPO protein			Asparagine-linked neutral oligosaccharides	PUBTATOR		EPO protein	2056		Asparagine-linked neutral oligosaccharides were released from each EPO protein by N-oligosaccharide glycopeptidase (almond) digestion.
3179269	2	52	gly	Asparagine-linked	360:376	arg1	Asparagine-linked neutral oligosaccharides			Asparagine	Asparagine-linked neutral oligosaccharides					Asparagine	Asparagine-linked neutral oligosaccharides were released from each EPO protein by N-oligosaccharide glycopeptidase (almond) digestion.
19167329	5	45	gly	glycosylation	775:787	arg1	an acceptor site			an acceptor site						site	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
6619126	0	78	gly	glycophorin	54:64	arg1	A carbohydrate structural variant	glycophorin A			A carbohydrate structural variant	PUBTATOR		glycophorin A	2993		A carbohydrate structural variant of MM glycoprotein (glycophorin A).
6619126	0	167	gly	glycoprotein	40:51	arg1	MM glycoprotein	glycoprotein			A carbohydrate structural variant	Fterm		glycoprotein			A carbohydrate structural variant of MM glycoprotein (glycophorin A).
26598643	2	52	gly	O-glycosylated	323:336	arg1	O-glycosylated proteins	O-glycosylated proteins				Fterm		proteins			The analysis, though, is quite challenging and time consuming, in particular for O-glycosylated proteins.
8223648	3	30	gly	N-glycosylated	335:348	arg2	the same site	Half		site		OGER		Half	Q9UNN4	site	Half of the protein purified by immunoaffinity chromatography was shown to be N-glycosylated at the same site as the natural IFN-omega 1.
10764840	0	49	gly	N-glycosylation	8:22	arg1	a recombinant human erythropoietin	a recombinant human erythropoietin				PUBTATOR		erythropoietin	2056		Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties.
12096136	0	31	gly	C-mannosylation	0:14	arg1	thrombospondin type 1 repeats				thrombospondin type 1 repeats						C-mannosylation and o-fucosylation of thrombospondin type 1 repeats.
12096136	0	38	gly	o-fucosylation	20:33	arg1	thrombospondin type 1 repeats				thrombospondin type 1 repeats						C-mannosylation and o-fucosylation of thrombospondin type 1 repeats.
1899031	0	20	part_of	plasminogen	74:84	arg1	asparagine-289	plasminogen		asparagine-289		PUBTATOR	SpecificSite	plasminogen	5340	asparagine-289	Oligosaccharide structures present on asparagine-289 of recombinant human plasminogen expressed in a Chinese hamster ovary cell line.
20378933	0	49	gly	Deglycosylation	0:14	arg1	N58			N58						N58	Deglycosylation of FcalphaR at N58 increases its binding to IgA.
7592613	5	15	gly	sialylated	903:912	arg1	sialylated lacNAc				sialylated lacNAc						The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	15	gly	sialylated	903:912	arg1	NeuAc alpha 2-6Gal beta 1-4GlcNAc				NeuAc alpha 2-6Gal beta 1-4GlcNAc						The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	28	gly	sialylated	958:967	arg1	NeuAc alpha 2-6Gal beta 1-4GlcNAc				NeuAc alpha 2-6Gal beta 1-4GlcNAc						The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	28	gly	sialylated	958:967	arg1	sialylated lacdiNAc				sialylated lacdiNAc						The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	51	gly	epitopes	763:770	arg1	the complex-type glycans			epitopes	the complex-type glycans					epitopes	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
15616124	3	2	gly	N-glycosylation	424:438	arg2	two N-glycosylation sites			two N-glycosylation sites						sites	Human FVII has two N-glycosylation sites (N145 and N322).
15616124	3	43	gly	sites	440:444	arg1	two N-glycosylation sites			two N-glycosylation sites						sites	Human FVII has two N-glycosylation sites (N145 and N322).
15616124	3	2	gly	N-glycosylation	424:438	arg2	N145			N145 and N322						N145 and N322	Human FVII has two N-glycosylation sites (N145 and N322).
15616124	3	43	gly	sites	440:444	arg1	N322			N145 and N322						N145 and N322	Human FVII has two N-glycosylation sites (N145 and N322).
2963625	1	0	part_of	protein	138:144	arg1	The complete amino acid sequence	protein		The complete amino acid sequence		Fterm	Site	protein		sequence	The complete amino acid sequence of the human complement system regulatory protein, factor H, has been derived from sequencing three overlapping cDNA clones.
10386995	5	47	part_of	synapsin	970:977	arg1	the regulatory domains	synapsin I		the regulatory domains		PUBTATOR	Site	synapsin I	24949	domains	The proximity of phosphorylation sites to O-GlcNAcylation sites in the regulatory domains of synapsin I suggests that O-GlcNAcylation may modulate phosphorylation and indirectly affect synapsin I interactions.
18703501	4	10	part_of	IX	775:776	arg1	the small transmembrane and intracytoplasmic regions	CA IX		the small transmembrane and intracytoplasmic regions		PUBTATOR	Site	CA IX	768	regions	The produced proteins lacked the small transmembrane and intracytoplasmic regions of CA IX.
24226769	7	31	gly	O-glycosylates	898:911	arg1	human NOTCH1 peptides			human NOTCH1 peptides						peptides	GALNT11 O-glycosylates human NOTCH1 peptides in vitro, thereby supporting a mechanism of Notch activation either by increasing ADAM17-mediated ectodomain shedding of the Notch receptor or by modification of specific EGF repeats.
12022871	9	13	gly	nonglycosylated	1349:1363	arg1	an active nonglycosylated enzyme	an active nonglycosylated enzyme				Fterm		enzyme			Mutagenesis of the putative N-glycosylation site (N79A) yielded an active nonglycosylated enzyme.
12022871	9	18	gly	N-glycosylation	1303:1317	arg2	the putative N-glycosylation site			the putative N-glycosylation site						site	Mutagenesis of the putative N-glycosylation site (N79A) yielded an active nonglycosylated enzyme.
11098061	0	37	part_of	gp130	126:130	arg1	the extracellular domain	gp130		the extracellular domain		PUBTATOR	Site	gp130	P40189	domain	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
32155444	2	34	gly	glycoproteins	180:192	arg1	Coronavirus spike (S) glycoproteins	Coronavirus spike (S) glycoproteins				Fterm		glycoproteins			Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies.
21264968	4	72	part_of	MUC4	1474:1477	arg1	naked MUC4 peptide	MUC4		naked MUC4 peptide		PUBTATOR	Site	MUC4	4585	peptide	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	127	part_of	containing	1629:1638	arg1	densely glycosylated MUC4 AND Thr6	MUC4		residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15		PUBTATOR	AminoAcid	MUC4	4585	residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	127	part_of	containing	1629:1638	arg1	densely glycosylated MUC4 AND Ser2	MUC4		residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15		PUBTATOR	AminoAcid	MUC4	4585	residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	127	part_of	containing	1629:1638	arg1	densely glycosylated MUC4 AND Thr10	MUC4		residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15		PUBTATOR	AminoAcid	MUC4	4585	residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	127	part_of	containing	1629:1638	arg1	densely glycosylated MUC4 AND Thr15	MUC4		residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15		PUBTATOR	AminoAcid	MUC4	4585	residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	127	part_of	containing	1629:1638	arg1	densely glycosylated MUC4 AND Ser2	MUC4		residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15		PUBTATOR	AminoAcid	MUC4	4585	residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	127	part_of	containing	1629:1638	arg1	densely glycosylated MUC4 AND Thr10	MUC4		residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15		PUBTATOR	AminoAcid	MUC4	4585	residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	127	part_of	containing	1629:1638	arg1	densely glycosylated MUC4 AND Thr15	MUC4		residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15		PUBTATOR	AminoAcid	MUC4	4585	residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	127	part_of	containing	1629:1638	arg1	densely glycosylated MUC4 AND Thr10	MUC4		residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15		PUBTATOR	AminoAcid	MUC4	4585	residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	127	part_of	containing	1629:1638	arg1	densely glycosylated MUC4 AND Thr15	MUC4		residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15		PUBTATOR	AminoAcid	MUC4	4585	residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
21264968	4	127	part_of	containing	1629:1638	arg1	densely glycosylated MUC4 AND Thr15	MUC4		residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15		PUBTATOR	AminoAcid	MUC4	4585	residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15	In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15.
18488039	3	50	gly	glycoproteins	494:506	arg1	both Nipah and Hendra attachment glycoproteins	both Nipah and Hendra attachment glycoproteins				Fterm		glycoproteins			Here we report crystal structures of both Nipah and Hendra attachment glycoproteins in complex with human EFNB2.
3524673	8	18	gly	linked	662:667	arg1	an Asn residue AND the carbohydrate chains			an Asn residue	the carbohydrate chains					Asn residue	One of the carbohydrate chains is linked to an Asn residue in the sequence Asn-Ser-Cys rather than the usual Asn-X-Ser/Thr sequence.
2415652	5	31	gly	beta	1142:1145	arg1	the carbohydrate-sensitive antiserum R141	hCG beta			the carbohydrate-sensitive antiserum R141	PUBTATOR		hCG beta	1082		ElBre hCG beta, however, was incompletely recognized by antisera specific for the CTE of standard hCG beta, especially the carbohydrate-sensitive antiserum R141.
10441114	8	93	part_of	collagen	1418:1425	arg1	the NC-1 domain	collagen XVIII		the NC-1 domain		PUBTATOR	Site	collagen XVIII	80781	domain	The described glycosylated endostatins may represent intermediates in the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
10861210	5	51	gly	N-glycosylation	756:770	arg2	the N-glycosylation site			the N-glycosylation site						site	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
22601780	3	6	gly	contains	344:351	arg1	Del-1 AND 3 epidermal growth factor (EGF)-like repeats	Del-1			3 epidermal growth factor (EGF)-like repeats	PUBTATOR		Del-1	10085		Del-1 contains 3 epidermal growth factor (EGF)-like repeats and 2 discoidin-like domains.
16622833	6	38	gly	attached	954:961	arg1	N70 AND triantennary structures			N70	triantennary structures					N70	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	14	gly	present	1015:1021	arg2	the isoforms AND exclusively diantennary structures	isoforms		site N271	exclusively diantennary structures	Fterm		isoforms		site N271	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	15	gly	present	1015:1021	arg2	site N271 AND exclusively diantennary structures			site N271	exclusively diantennary structures					site N271	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	15	gly	present	1015:1021	arg2	the isoforms AND exclusively diantennary structures	isoforms		site N271	exclusively diantennary structures	Fterm		isoforms		site N271	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	15	gly	present	1015:1021	arg2	site N271 AND exclusively diantennary structures	isoforms		site N271	exclusively diantennary structures	Fterm		isoforms		site N271	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	15	gly	present	1015:1021	arg2	the isoforms AND exclusively diantennary structures	isoforms		site N271	exclusively diantennary structures	Fterm		isoforms		site N271	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	15	gly	present	1015:1021	arg2	the isoforms AND exclusively diantennary structures	isoforms		site N271	exclusively diantennary structures	Fterm		isoforms		site N271	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
22809326	13	63	part_of	proteins	1666:1673	arg1	The conserved luminal domain	proteins		The conserved luminal domain		Fterm	Site	proteins		domain	CONCLUSION: The conserved luminal domain of lysosome-associated membrane proteins forms a previously unknown β-prism fold.
11567096	6	17	part_of	rCRFR1	1038:1043	arg1	the N-terminal domain	rCRFR1		the N-terminal domain		PUBTATOR	Site	rCRFR1	58959	domain	However, it was sufficiently high for rCRFR1-NT-Kif to serve as a model for the N-terminal domain of rCRFR1.
3980466	13	76	part_of	glycoproteins	2358:2370	arg1	corresponding glycosylation sites	glycoproteins		corresponding glycosylation sites		Fterm	Site	glycoproteins		sites	These data suggest that subtle changes in peptide structure are reflected in the extent of sialylation and branching of oligosaccharides found at corresponding glycosylation sites of structurally related glycoproteins.
19838198	3	34	part_of	IL-17RA	543:549	arg1	two fibronectin-type domains	IL-17RA		two fibronectin-type domains		OGER	Site	IL-17RA	Q96F46	domains	The mechanism of complex formation was unique for cytokines and involved the engagement of IL-17 by two fibronectin-type domains of IL-17RA in a groove between the IL-17 homodimer interface.
19838198	3	41	part_of	fibronectin-type	515:530	arg1	two fibronectin-type domains	fibronectin		two fibronectin-type domains		OGER	Site	fibronectin	P02751	domains	The mechanism of complex formation was unique for cytokines and involved the engagement of IL-17 by two fibronectin-type domains of IL-17RA in a groove between the IL-17 homodimer interface.
9233787	5	19	part_of	BM-40	676:680	arg1	one face	BM-40		one face		OGER	Site	BM-40	P09486	face	Residues implicated in cell binding, inhibition of cell spreading and disassembly of focal adhesions cluster on one face of BM-40, opposite the binding epitope for collagens and the N-linked carbohydrate.
2361960	1	11	gly	glycosylation	212:224	arg2	glycosylation sites			glycosylation sites						sites	The complete peptide map of purified recombinant human interleukin 5 (rhIL-5) was determined to verify its primary structure, glycosylation sites, and disulfide bonding structure.
16740002	3	29	gly	glycoproteins	462:474	arg1	Salivary glycoproteins	Salivary glycoproteins				Fterm		glycoproteins			Salivary glycoproteins were identified by the hydrazide coupling and release method.
12970363	7	86	gly	monoglycosylated	1252:1267	arg1	the monoglycosylated TRPC3 channel	the monoglycosylated TRPC3 channel				PUBTATOR		TRPC3 channel	7222		Immunoblotting analysis of HEK 293 cell lysates expressing TRPC6 wild type and mutants favors a model of TRPC6 that is dually glycosylated within the first (e1) and second extracellular loop (e2) as opposed to the monoglycosylated TRPC3 channel (Vannier, B., Zhu, X., Brown, D., and Birnbaumer, L. (1998) J. Biol.
6587378	0	39	part_of	2-glycoprotein	50:63	arg1	Complete amino acid sequence	beta 2-glycoprotein I		Complete amino acid sequence		OGER	Site	beta 2-glycoprotein I	P02749	sequence	Complete amino acid sequence of human plasma beta 2-glycoprotein I.
6684483	1	15	gly	glycoprotein	276:287	arg1	the glycoprotein	the glycoprotein				Fterm		glycoprotein			Sex hormone-binding globulin from human blood serum contains two biantennary N-linked oligosaccharide chains of the N-acetyllactosamine type and one O-linked oligosaccharide per one molecule of the glycoprotein.
6684483	1	32	gly	contains	130:137	arg1	Sex hormone-binding globulin AND one O-linked oligosaccharide	Sex hormone-binding globulin			one O-linked oligosaccharide	PUBTATOR		Sex hormone-binding globulin	6462		Sex hormone-binding globulin from human blood serum contains two biantennary N-linked oligosaccharide chains of the N-acetyllactosamine type and one O-linked oligosaccharide per one molecule of the glycoprotein.
6684483	1	32	gly	contains	130:137	arg1	Sex hormone-binding globulin AND two biantennary N-linked oligosaccharide chains	Sex hormone-binding globulin			two biantennary N-linked oligosaccharide chains	PUBTATOR		Sex hormone-binding globulin	6462		Sex hormone-binding globulin from human blood serum contains two biantennary N-linked oligosaccharide chains of the N-acetyllactosamine type and one O-linked oligosaccharide per one molecule of the glycoprotein.
2511201	8	52	gly	microheterogeneity	1499:1516	arg1	these O-linked sugar chains				these O-linked sugar chains						In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	8	95	gly	glycopeptides	1400:1412	arg2	two different glycopeptides			two different glycopeptides						glycopeptides	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	8	57	gly	contained	1420:1428	arg1	two different glycopeptides AND Xyl			two different glycopeptides	Xyl					glycopeptides	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	8	57	gly	contained	1420:1428	arg1	two different glycopeptides AND Glc			two different glycopeptides	Glc					glycopeptides	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
19656770	7	78	gly	glycoprotein	1362:1373	arg1	One glycoprotein transmembrane orientation	One glycoprotein transmembrane orientation				Fterm		glycoprotein			One glycoprotein transmembrane orientation was found to be inconsistent with Swiss-Prot annotations, whereas ambiguous annotations for 14 other proteins were resolved.
21712440	8	92	gly	glycosylated	1594:1605	arg1	Tyr10 glycosylated Aβ peptides			Tyr10 glycosylated Aβ peptides						peptides	We observed an increase of up to 2.5 times of Tyr10 glycosylated Aβ peptides in CSF in six AD patients compared to seven non-AD patients.
8636209	4	16	part_of	gamma	527:531	arg1	the EC domain	CD3 gamma		the EC domain		PUBTATOR	Site	CD3 gamma	917	domain	A computer model indicated that the EC domain of CD3 gamma folds as an Ig domain.
8344946	1	86	gly	moieties	97:104	arg1	neurofilament polypeptides L and M. Neurofilaments			neurofilament polypeptides L and M. Neurofilaments	neurofilament polypeptides L and M. Neurofilaments		Site			polypeptides	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
11676606	4	22	part_of	contains	517:524	arg1	Human CD154 AND a single N-linked glycosylation site	Human CD154		a single N-linked glycosylation site		PUBTATOR	Site	Human CD154	959	site	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
23010571	0	35	part_of	fibrillin-1-	114:125	arg1	A disintegrin-like and metalloprotease domain	fibrillin-1		A disintegrin-like and metalloprotease domain		PUBTATOR	Site	fibrillin-1	2200	domain	A disintegrin-like and metalloprotease domain containing thrombospondin type 1 motif-like 5 (ADAMTSL5) is a novel fibrillin-1-, fibrillin-2-, and heparin-binding member of the ADAMTS superfamily containing a netrin-like module.
23010571	0	46	part_of	fibrillin-2-	128:139	arg1	A disintegrin-like and metalloprotease domain	fibrillin-2		A disintegrin-like and metalloprotease domain		PUBTATOR	Site	fibrillin-2	2201	domain	A disintegrin-like and metalloprotease domain containing thrombospondin type 1 motif-like 5 (ADAMTSL5) is a novel fibrillin-1-, fibrillin-2-, and heparin-binding member of the ADAMTS superfamily containing a netrin-like module.
28775322	7	59	part_of	EGF-like	1487:1494	arg1	3 different EGF-like domains	EGF		3 different EGF-like domains		OGER	Site	EGF	P01133	domains	Here the authors report the structure of human POGLUT1 in complexes with 3 different EGF-like domains and donor substrates and shed light on the enzyme's substrate specificity and catalytic mechanism.
7781780	0	29	gly	erythropoietin	119:132	arg1	a mannose-6-phosphate containing oligomannosidic N-glycan	erythropoietin			a mannose-6-phosphate containing oligomannosidic N-glycan	PUBTATOR		erythropoietin	2056		Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
108268	1	40	gly	chain	109:113	arg1	the oligosaccharide moiety	J chain			the oligosaccharide moiety	PUBTATOR		J chain	3512		The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa has been established.
24279413	1	50	gly	attachment	162:171	arg2	amino acid residues AND sugars			amino acid residues	sugars					residues	Glycosylation is an important protein modification that involves enzymatic attachment of sugars to amino acid residues.
26013384	8	12	gly	O-glycosylated	997:1010	arg1	fully O-glycosylated rHu-EPO	fully O-glycosylated rHu-EPO				PUBTATOR		EPO	2056		It is concluded that the variant peak is non-O-glycosylated rHu-EPO and the main peak is fully O-glycosylated rHu-EPO at Ser126.
26013384	8	43	gly	non-O-glycosylated	943:960	arg1	non-O-glycosylated rHu-EPO	non-O-glycosylated rHu-EPO				PUBTATOR		EPO	2056		It is concluded that the variant peak is non-O-glycosylated rHu-EPO and the main peak is fully O-glycosylated rHu-EPO at Ser126.
7525874	2	87	gly	carries	237:243	arg1	This protein AND exclusively N-linked oligosaccharides	This protein		two sites	exclusively N-linked oligosaccharides	Fterm	Site	protein		sites	This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56).
7525874	2	87	gly	carries	237:243	arg1	This protein AND exclusively N-linked oligosaccharides	protein		Asn29 and Asn56	exclusively N-linked oligosaccharides	Fterm	AminoAcid	protein		Asn29 and Asn56	This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56).
3514617	7	41	gly	acid	893:896	arg1	The amino-terminal octapeptides			The amino-terminal octapeptides	The amino-terminal octapeptides		Site			octapeptides	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	7	134	gly	composition	915:925	arg1	The amino-terminal octapeptides			The amino-terminal octapeptides	The amino-terminal octapeptides		Site			octapeptides	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
22159084	13	78	gly	N-glycosylation	1706:1720	arg1	SLC26A3	SLC26A3				PUBTATOR		SLC26A3	1811		In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
18729387	12	32	gly	attached	1937:1944	arg1	the third Ig domain AND Man-5			the third Ig domain	Man-5					domain	Diverse oligosaccharides, including Lewis a/x-modified glycans, a brain-specific glycan known as BA-2, and Man-5, were found to be attached to the third Ig domain.
18729387	12	32	gly	attached	1937:1944	arg1	the third Ig domain AND a brain-specific glycan			the third Ig domain	a brain-specific glycan					domain	Diverse oligosaccharides, including Lewis a/x-modified glycans, a brain-specific glycan known as BA-2, and Man-5, were found to be attached to the third Ig domain.
18729387	12	32	gly	attached	1937:1944	arg2	the third Ig domain AND Diverse oligosaccharides			the third Ig domain	Diverse oligosaccharides					domain	Diverse oligosaccharides, including Lewis a/x-modified glycans, a brain-specific glycan known as BA-2, and Man-5, were found to be attached to the third Ig domain.
18729387	12	32	gly	attached	1937:1944	arg2	the third Ig domain AND Lewis a/x-modified glycans			the third Ig domain	Lewis a/x-modified glycans					domain	Diverse oligosaccharides, including Lewis a/x-modified glycans, a brain-specific glycan known as BA-2, and Man-5, were found to be attached to the third Ig domain.
20147294	8	11	part_of	ADA2	1148:1151	arg1	catalytic sites	ADA2		catalytic sites		PUBTATOR	Site	ADA2	51816	sites	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	8	59	part_of	ADA1	1157:1160	arg1	catalytic sites	ADA1		catalytic sites		PUBTATOR	Site	ADA1	117143	sites	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
16770729	1	38	part_of	contain	147:153	arg1	Voltage-gated K(+) channels AND a pore-forming domain	Voltage-gated K(+) channels		a pore-forming domain		Fterm	Site	channels		domain	Voltage-gated K(+) channels contain six membrane spanning segments and a pore-forming domain.
8142896	7	6	gly	mass	1193:1196	arg1	a hexasaccharide	mass 1,039			a hexasaccharide	OGER		mass 1,039	Q8WXG9		The predominant species was a hexasaccharide of molecular mass 1,039, containing a fucose subunit linked to the proximal N-acetylglucosamine residue: [formula: see text]
15869464	1	85	gly	glycoprotein	258:269	arg1	an integrin-binding highly phosphorylated glycoprotein	an integrin-binding highly phosphorylated glycoprotein				Fterm		glycoprotein			OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	1	85	gly	glycoprotein	258:269	arg1	OPN	OPN				PUBTATOR		OPN	6696		OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
23285087	5	21	gly	used	1039:1042	arg2	Asn516			Asn134 and Asn516						Asn134 and Asn516	Our results showed that Asn134 and Asn516 are used for glycosylation under normal conditions; however, when Asn134 was mutagenized, an additional asparagine at position 503 is involved in the glycosylation process.
9572875	8	58	part_of	positions	1343:1351	arg1	IGFBP-6	IGFBP-6		positions		PUBTATOR	Site	IGFBP-6	3489	positions	Native disulfide bond positions in IGFBP-6 were localized by means of observed disulfide-linked tryptic fragments, revealing that there are two disulfide-linked subdomains within each of the N- and C-terminal regions and confirming a previous suggestion that the latter regions are not interconnected.
22041449	0	60	part_of	G2	57:58	arg1	the ligand binding domain	netrin G2		the ligand binding domain		OGER	Site	netrin G2	Q96CW9	domain	Crystal structure of the ligand binding domain of netrin G2.
22023369	3	40	gly	sFcγRIIIa	568:576	arg1	the two N-glycans	FcγRIIIa			the two N-glycans	PUBTATOR		FcγRIIIa	2214		The crystal structure shows that one of the two N-glycans of sFcγRIIIa mediates the interaction with nonfucosylated Fc, thereby stabilizing the complex.
24393138	0	13	gly	glycoprotein	76:87	arg1	the intact glycoprotein	the intact glycoprotein				Fterm		glycoprotein			Glycan analysis of Prostate Specific Antigen (PSA) directly from the intact glycoprotein by HR-ESI/TOF-MS.
15662415	6	38	gly	glycoprotein	648:659	arg1	all glycoprotein hormones	all glycoprotein hormones				Fterm		glycoprotein			Our analysis suggests that all glycoprotein hormones bind to their receptors in this mode and that binding specificity is mediated by key interaction sites involving both the common alpha- and hormone-specific beta-subunits.
19855092	9	82	gly	asialoglycoprotein	1609:1626	arg1	the hepatic asialoglycoprotein receptor	the hepatic asialoglycoprotein receptor				Fterm		asialoglycoprotein			Uptake of desialylated adiponectin by isolated primary rat hepatocytes was also accelerated, suggesting a role for the hepatic asialoglycoprotein receptor.
19855092	9	97	gly	desialylated	1492:1503	arg1	desialylated adiponectin	desialylated adiponectin				PUBTATOR		adiponectin	Q15848		Uptake of desialylated adiponectin by isolated primary rat hepatocytes was also accelerated, suggesting a role for the hepatic asialoglycoprotein receptor.
21768335	3	54	gly	afucosylated	471:482	arg1	afucosylated IgGs	afucosylated IgGs				Cterm		IgGs			Although afucosylated IgGs exist naturally, a next generation of recombinant therapeutic, glycoenginereed antibodies is currently being developed to exploit this finding.
18093522	4	25	part_of	dimer	636:640	arg1	the opposite faces	neuroligin-1 dimer		the opposite faces		PUBTATOR	Site	neuroligin-1 dimer	22871	faces	Neuroligin-1 forms a constitutive dimer, and two neurexin-1 beta monomers bind to two identical surfaces on the opposite faces of the neuroligin-1 dimer to form a heterotetramer.
19683538	1	39	gly	glycopeptides	272:284	arg1	terminal alpha-N-acetylgalactosamine residues			glycopeptides	terminal alpha-N-acetylgalactosamine residues					glycopeptides	alpha-N-acetylgalactosaminidase (alpha-NAGAL; E.C. 3.2.1.49) is a lysosomal exoglycosidase that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids.
17117926	10	37	gly	glycosylation	1338:1350	arg1	Wnt-5a	Wnt-5a				PUBTATOR		Wnt-5a	7474		Thus the post-translational palmitoylation and glycosylation of Wnt-5a are important for the actions and secretion of Wnt-5a.
18203274	4	41	part_of	glycoprotein	562:573	arg1	A prerequisite	glycoprotein		A prerequisite		Fterm	Site	glycoprotein		prerequisite	A prerequisite for the therapeutic use of hBChE is a detailed characterization of this glycoprotein purified from human plasma.
7547911	4	24	gly	glycopeptide	800:811	arg2	a glycopeptide			a glycopeptide						glycopeptide	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	4	41	gly	moiety	788:793	arg1	a glycopeptide			a glycopeptide	a glycopeptide		Site			glycopeptide	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
27599734	6	32	part_of	receptor	1138:1145	arg1	both receptor domains	receptor		both receptor domains		Fterm	Site	receptor		domains	Structure-based bioinformatic analysis revealed independent evolutionary behaviour of both receptor domains and, together with multiple sequence alignment, identified putative binding sites for interferon-γ and receptor 1, the ligands of IFNγR2.
6333684	2	23	gly	glycosylation	279:291	arg1	position 3			threonine residue in position 3						threonine residue in position 3	For the most part, this heterogeneity was attributed to variations in glycosylation of the threonine residue in position 3 of the polypeptide chain.
21467029	4	1	part_of	COX	471:473	arg1	a COX active site	COX		a COX active site		OGER	Site	COX		site	Each monomer has a peroxidase and a COX active site.
3881423	0	51	gly	glycoprotein	49:60	arg1	the glycoprotein processing enzyme glucosidase II	the glycoprotein processing enzyme glucosidase II				Fterm		glycoprotein			Identity of neutral alpha-glucosidase AB and the glycoprotein processing enzyme glucosidase II.
27313224	6	40	gly	glycosylation	1051:1063	arg1	N565			N534, N559 and N565						N534, N559 and N565	Mass spectrometric analysis of gSV2CLD-Fc demonstrates glycosylation of N534, N559 and N565, the latter two residing at the BoNT/A interface.
27313224	6	40	gly	glycosylation	1051:1063	arg1	N559			N534, N559 and N565						N534, N559 and N565	Mass spectrometric analysis of gSV2CLD-Fc demonstrates glycosylation of N534, N559 and N565, the latter two residing at the BoNT/A interface.
27313224	6	40	gly	glycosylation	1051:1063	arg1	N559			N534, N559 and N565						N534, N559 and N565	Mass spectrometric analysis of gSV2CLD-Fc demonstrates glycosylation of N534, N559 and N565, the latter two residing at the BoNT/A interface.
12218058	8	60	gly	glycosylation	1371:1383	arg2	the glycosylation sites			the glycosylation sites						sites	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
24766575	1	13	gly	N-glycopeptides	333:347	arg2	N-glycopeptides			N-glycopeptides						N-glycopeptides	Study of site-specific N-glycosylation in complex sample remains a huge analytical challenge because protein glycosylation is structurally diverse in post-translational modifications, resulting in an intricacy of N-glycopeptides.
24125761	2	53	gly	glycoprotein	228:239	arg1	a glycoprotein	a glycoprotein				Fterm		glycoprotein			AADAC is a glycoprotein, but the role of glycosylation remains unclear.
24125761	2	53	gly	glycoprotein	228:239	arg1	AADAC	AADAC				PUBTATOR		AADAC	13		AADAC is a glycoprotein, but the role of glycosylation remains unclear.
19656770	4	83	gly	glycoproteins	829:841	arg1	128 bona fide cell surface-exposed N-linked glycoproteins	128 bona fide cell surface-exposed N-linked glycoproteins				Fterm		glycoproteins			128 bona fide cell surface-exposed N-linked glycoproteins, including 117 transmembrane, four glycosylphosphatidylinositol-anchored, five extracellular matrix, and two membrane-associated proteins were identified from mouse C2C12 myoblasts.
19656770	4	83	gly	glycoproteins	829:841	arg1	two membrane-associated proteins	two membrane-associated proteins				Fterm		proteins			128 bona fide cell surface-exposed N-linked glycoproteins, including 117 transmembrane, four glycosylphosphatidylinositol-anchored, five extracellular matrix, and two membrane-associated proteins were identified from mouse C2C12 myoblasts.
21138434	2	77	gly	N-glycosylation	373:387	arg1	the 5-HT3A subunit	the 5-HT3A subunit				PUBTATOR		5-HT3A subunit	3359		Since N-glycosylation of the 5-HT3A subunit impacts cell surface trafficking, the presence of N-glycosylation of the human (h) 5-HT3B subunit and the influence upon cell membrane expression was investigated.
21138434	2	83	gly	N-glycosylation	461:475	arg1	the human (h) 5-HT3B subunit	the human (h) 5-HT3B subunit				PUBTATOR		5-HT3B subunit	9177		Since N-glycosylation of the 5-HT3A subunit impacts cell surface trafficking, the presence of N-glycosylation of the human (h) 5-HT3B subunit and the influence upon cell membrane expression was investigated.
15628971	4	86	gly	attached	489:496	arg1	C4ST-1 AND the N-linked oligosaccharides	C4ST-1			the N-linked oligosaccharides	PUBTATOR		C4ST-1	314694		In the present paper, we investigated the functional role of the N-linked oligosaccharides attached to C4ST-1.
24751537	3	0	gly	glycoprotein	553:564	arg1	a previously uncharacterized integral membrane glycoprotein	a previously uncharacterized integral membrane glycoprotein				Fterm		glycoprotein			We report the identification and functional characterization of VGCC β-anchoring and -regulatory protein (BARP), a previously uncharacterized integral membrane glycoprotein expressed in neuroendocrine cells and neurons.
26791533	4	16	gly	glycopeptides	595:607	arg2	glycopeptides			glycopeptides						glycopeptides	We have devised a strategy to analyze glycopeptides from a complex, unknown mixture of protease-digested proteins.
1457416	1	0	gly	A-chain	240:246	arg1	the glycans	A-chain			the glycans	Fterm		A-chain			The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	1	59	gly	2HS-glycoprotein	270:285	arg1	human plasma alpha 2HS-glycoprotein	human plasma alpha 2HS-glycoprotein				PUBTATOR		alpha 2HS-glycoprotein	197		The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
30392906	0	3	part_of	protein	73:79	arg1	the extracellular domain	Myelin protein zero-like protein 1		the extracellular domain		PUBTATOR	Site	Myelin protein zero-like protein 1	9019	domain	Structural and biochemical studies of the extracellular domain of Myelin protein zero-like protein 1.
19678840	7	10	gly	occupancy	1730:1738	arg2	the co-catalytic zinc sites			the co-catalytic zinc sites						sites	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
17400922	0	35	part_of	ephrin-A5	31:39	arg1	the human ephrin-A5 ectodomain	ephrin-A5		the human ephrin-A5 ectodomain		PUBTATOR	Site	ephrin-A5	1946	ectodomain	Crystal structure of the human ephrin-A5 ectodomain.
29899144	0	66	part_of	domain	20:25	arg1	GPIHBP1	GPIHBP1		domain		PUBTATOR	Site	GPIHBP1	338328	domain	A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase.
12435857	8	105	part_of	THTR-1	1597:1602	arg1	the THTR-1 consensus N-glycosylation acceptor asparagine 63	THTR-1		the THTR-1 consensus N-glycosylation acceptor asparagine 63		PUBTATOR	SpecificSite	THTR-1	10560	asparagine 63	Consistently, either treatment with tunicamycin or substitution of the THTR-1 consensus N-glycosylation acceptor asparagine 63 with glutamine, abolished its glycosylation and plasma membrane targeting.
24018687	3	39	part_of	DDR1	724:727	arg1	asparagine 211	DDR1		asparagine 211		PUBTATOR	SpecificSite	DDR1	780	asparagine 211	Site-directed mutational analysis of the consensus N-glycosylation sites of the DDRs revealed that mutations of asparagine 213 of DDR2 and asparagine 211 of DDR1, a conserved N-glycosylation site among vertebrate DDRs, inhibited the generation of the high-molecular-mass isoform.
24018687	3	39	part_of	DDR1	724:727	arg1	a conserved N-glycosylation site	DDR1		a conserved N-glycosylation site		PUBTATOR	Site	DDR1	780	site	Site-directed mutational analysis of the consensus N-glycosylation sites of the DDRs revealed that mutations of asparagine 213 of DDR2 and asparagine 211 of DDR1, a conserved N-glycosylation site among vertebrate DDRs, inhibited the generation of the high-molecular-mass isoform.
24018687	3	53	part_of	DDR2	697:700	arg1	asparagine 213	DDR2		asparagine 213		PUBTATOR	SpecificSite	DDR2	4921	asparagine 213	Site-directed mutational analysis of the consensus N-glycosylation sites of the DDRs revealed that mutations of asparagine 213 of DDR2 and asparagine 211 of DDR1, a conserved N-glycosylation site among vertebrate DDRs, inhibited the generation of the high-molecular-mass isoform.
11371615	6	7	gly	domain	1086:1091	arg1	O-GlcNAcylation			domain	O-GlcNAcylation					domain	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
27314333	4	12	gly	N-glycosylated	695:708	arg1	Rspo3	Rspo3		N137		PUBTATOR		Rspo3	84870	N137	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	12	gly	N-glycosylated	695:708	arg1	human Rspo1	Rspo1		N137		PUBTATOR		Rspo1	284654	N137	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	12	gly	N-glycosylated	695:708	arg1	Rspo3	Rspo3		site		PUBTATOR		Rspo3	84870	site	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	12	gly	N-glycosylated	695:708	arg1	human Rspo1	Rspo1		site		PUBTATOR		Rspo1	284654	site	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	50	gly	N-glycosylated	789:802	arg2	N160	Rspo2		N160		PUBTATOR		Rspo2	340419	N160	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	50	gly	N-glycosylated	789:802	arg2	a position	Rspo2		position		PUBTATOR		Rspo2	340419	position	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
21550978	6	27	gly	glycosylated	1166:1177	arg1	hPAR(1)	hPAR(1)				PUBTATOR		hPAR(1)	2149		In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	all five consensus sites			all five consensus sites						sites	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	83	gly	sialylated	1183:1192	arg1	hPAR(1)	hPAR(1)				PUBTATOR		hPAR(1)	2149		In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn(259)			Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)						Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn(35)			Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)						Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn(62)			Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)						Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn(75)			Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)						Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn(35)			Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)						Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn(62)			Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)						Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn(75)			Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)						Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn(62)			Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)						Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn(75)			Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)						Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn(75)			Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)						Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259)	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
10715549	1	13	gly	glycoprotein	157:168	arg1	heterodimeric glycoprotein hormones	heterodimeric glycoprotein hormones				Fterm		glycoprotein			CG, LH, FSH, and TSH are a family of heterodimeric glycoprotein hormones that contain a common alpha-subunit, but differ in their hormone-specific beta-subunits.
25617829	3	18	gly	carries	520:526	arg1	the nutrient-sensing class C G protein-coupled receptor GPRC6A AND seven N-glycans	the nutrient-sensing class C G protein-coupled receptor GPRC6A			seven N-glycans	PUBTATOR		GPRC6A	222545		Herein, we show that the nutrient-sensing class C G protein-coupled receptor GPRC6A carries seven N-glycans and that one of these sites modulates surface expression whereas mutation of another site affects receptor function.
15102839	1	36	gly	glycoproteins	316:328	arg1	Asn-linked glycoproteins	Asn-linked glycoproteins				Fterm		glycoproteins			Three subfamilies of mammalian Class 1 processing alpha1,2-mannosidases (family 47 glycosidases) play critical roles in the maturation of Asn-linked glycoproteins in the endoplasmic reticulum (ER) and Golgi complex as well as influencing the timing and recognition for disposal of terminally unfolded proteins by ER-associated degradation.
8615697	7	20	gly	glycosylation	929:941	arg2	the 20 putative N-linked glycosylation sites			the 20 putative N-linked glycosylation sites						sites	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	7	104	gly	glycosylated	1024:1035	arg1	the mature protein	the mature protein				Fterm		protein			Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
10677208	8	87	gly	glycosylation	1537:1549	arg1	eight-cysteine domain protein-protein interactions			cysteine domain						cysteine domain	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
11080501	5	44	part_of	thyroglobulin	1178:1190	arg1	the thyroglobulin type 1A domain	thyroglobulin		the thyroglobulin type 1A domain		OGER	Site	thyroglobulin	P01266	domain	The next three disulfide linkages are Cys7-Cys8, Cys9-Cys10, and Cys11-Cys12, consistent with the recently determined disulfide pattern of the thyroglobulin type 1A domain of insulin-like growth factor-binding proteins 1 and 6.
11080501	5	59	part_of	proteins	1245:1252	arg1	the thyroglobulin type 1A domain	proteins 1		the thyroglobulin type 1A domain		Fterm	Site	proteins 1		domain	The next three disulfide linkages are Cys7-Cys8, Cys9-Cys10, and Cys11-Cys12, consistent with the recently determined disulfide pattern of the thyroglobulin type 1A domain of insulin-like growth factor-binding proteins 1 and 6.
10731668	1	56	gly	used	228:231	arg2	The extracellular domain			The extracellular domain						domain	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
1533633	4	1	gly	glycosylation	730:742	arg2	the three glycosylation sites			the three glycosylation sites						sites	By expression of the mutant cDNAs in COS-1 cells, each of the three glycosylation sites on the alpha-subunit was found to be modified by an oligosaccharide.
1533633	4	31	gly	modified	787:794	arg1	the three glycosylation sites AND an oligosaccharide			the three glycosylation sites	an oligosaccharide					sites	By expression of the mutant cDNAs in COS-1 cells, each of the three glycosylation sites on the alpha-subunit was found to be modified by an oligosaccharide.
24226769	7	72	part_of	NOTCH1	919:924	arg1	human NOTCH1 peptides	NOTCH1		human NOTCH1 peptides		PUBTATOR	Site	NOTCH1	100037842	peptides	GALNT11 O-glycosylates human NOTCH1 peptides in vitro, thereby supporting a mechanism of Notch activation either by increasing ADAM17-mediated ectodomain shedding of the Notch receptor or by modification of specific EGF repeats.
24103369	3	73	gly	N-glycosylation	387:401	arg2	four potential sites			four potential sites						sites	Hp β chain contains four potential sites of N-glycosylation.
7505568	5	5	gly	glycosylated	500:511	arg1	Asn332			Asn332						Asn332	Asn332 which was not recovered in the glycopeptide fractions was probably not glycosylated.
7505568	5	8	gly	glycopeptide	460:471	arg2	glycopeptide			glycopeptide						glycopeptide	Asn332 which was not recovered in the glycopeptide fractions was probably not glycosylated.
8163535	7	69	part_of	protein	1220:1226	arg1	this domain	protein		this domain		Fterm	Site	protein		domain	In contrast to the C-terminal cluster, the N-terminal cluster was always glycanated, suggesting that this domain of the core protein contains sequences responsible for the invariable attachment of glycosaminoglycan chains.
8163535	7	107	part_of	contains	1228:1235	arg1	the core protein AND sequences	protein		sequences		Fterm	Site	protein		sequences	In contrast to the C-terminal cluster, the N-terminal cluster was always glycanated, suggesting that this domain of the core protein contains sequences responsible for the invariable attachment of glycosaminoglycan chains.
25908590	5	43	part_of	IL1RAPL1	986:993	arg1	the Ig1 domain	IL1RAPL1		the Ig1 domain		PUBTATOR	Site	IL1RAPL1	11141	domain	The second splice insert functions as an adjustable linker that positions the Ig2 and Ig3 domains of PTPδ for simultaneously interacting with the Ig1 domain of IL1RAPL1 or IL-1RAcP.
25908590	5	44	part_of	IL-1RAcP	998:1005	arg1	the Ig1 domain	IL-1RAcP		the Ig1 domain		PUBTATOR	Site	IL-1RAcP	3556	domain	The second splice insert functions as an adjustable linker that positions the Ig2 and Ig3 domains of PTPδ for simultaneously interacting with the Ig1 domain of IL1RAPL1 or IL-1RAcP.
21269602	5	18	part_of	VE-cadherin	842:852	arg1	the VE-cadherin EC1-2 adhesive region	structure of the VE-cadherin EC1-2		the VE-cadherin EC1-2 adhesive region		PUBTATOR	Site	structure of the VE-cadherin EC1-2	1003	region	We also present the 2.1-Å-resolution crystal structure of the VE-cadherin EC1-2 adhesive region, which reveals homodimerization via the strand-swap mechanism common to classical cadherins.
21269602	5	23	part_of	EC1-2	854:858	arg1	the VE-cadherin EC1-2 adhesive region	structure of the VE-cadherin EC1-2		the VE-cadherin EC1-2 adhesive region		PUBTATOR	Site	structure of the VE-cadherin EC1-2	1003	region	We also present the 2.1-Å-resolution crystal structure of the VE-cadherin EC1-2 adhesive region, which reveals homodimerization via the strand-swap mechanism common to classical cadherins.
12956774	0	65	part_of	antigen/receptor	70:85	arg1	the extracellular domains	Duffy antigen/receptor for chemokines		the extracellular domains		PUBTATOR	Site	Duffy antigen/receptor for chemokines	2532	domains	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
10029548	0	68	gly	glycosylated	144:155	arg1	the N-lobe			N-lobe						N-lobe	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	0	68	gly	glycosylated	144:155	arg1	human transferrin	transferrin		N-lobe		PUBTATOR		transferrin	7018	N-lobe	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	0	68	gly	glycosylated	144:155	arg1	human transferrin	transferrin		N-lobe		PUBTATOR		transferrin	7018	N-lobe	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	0	68	gly	glycosylated	144:155	arg1	human transferrin	transferrin		serine-32		PUBTATOR		transferrin	7018	serine-32	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	0	68	gly	glycosylated	144:155	arg2	serine-32			serine-32						serine-32	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	0	68	gly	glycosylated	144:155	arg2	serine-32	transferrin		serine-32		PUBTATOR		transferrin	7018	serine-32	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
7107587	7	48	gly	glycopeptides	648:660	arg2	The glycopeptides			The glycopeptides						glycopeptides	The glycopeptides resulting from exoglycosidase digestions were examined with 300-MHz 1H-NMR spectroscopy, and the changes in the signals caused by selective removal of sugar residues were studied.
3134887	3	30	part_of	protein	384:390	arg1	The primary sequence	protein		The primary sequence		Fterm	Site	protein		sequence	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses.
7744025	4	12	gly	triglycosylated	862:876	arg1	triglycosylated peptides			triglycosylated peptides						peptides	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7008791	0	1	part_of	D	101:101	arg1	the Fc region	human immunoglobulin D		the Fc region		Cterm	Site	human immunoglobulin D		region	Amino acid sequence and location of the three glycopeptides in the Fc region of human immunoglobulin D.
7008791	0	3	part_of	sequence	11:18	arg1	the Fc region	sequence		the Fc region						region	Amino acid sequence and location of the three glycopeptides in the Fc region of human immunoglobulin D.
24884609	4	34	gly	glycopeptide	575:586	arg2	glycopeptide analyses			glycopeptide analyses						glycopeptide	Recombinant ITIH4 was analyzed to optimize glycopeptide analyses, followed by serum-derived ITIH4.
3840370	2	34	part_of	protein	379:385	arg1	The entire amino acid sequence	protein can		The entire amino acid sequence		OGER	Site	protein can	P35658	sequence	The entire amino acid sequence of the C4b-binding protein can be predicted from this study of the cloned cDNA when allied to a previous sequence study at the protein level [Chung, Gagnon & Reid (1985) Mol.
7538124	5	46	gly	3H-glycopeptide	837:851	arg2	the tryptic 3H-glycopeptide pattern			the tryptic 3H-glycopeptide pattern						3H-glycopeptide	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	5	67	gly	glycopeptides	941:953	arg2	the glycopeptides	K18		glycopeptides		PUBTATOR		K18	3875	glycopeptides	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	5	79	gly	glycosylation	785:797	arg1	K18	K18		sites		PUBTATOR		K18	3875	sites	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
11150294	3	52	part_of	receptor	501:508	arg1	the extreme C-terminal SSV sequence	receptor		the extreme C-terminal SSV sequence		Fterm	Site	receptor		sequence	Mutations in the extreme C-terminal SSV sequence of the 5-HT(2C) receptor confirmed that the SXV motif is critical for the interaction.
9933650	1	17	gly	glycoprotein	81:92	arg1	Tamm-Horsfall glycoprotein	Tamm-Horsfall glycoprotein				PUBTATOR		Tamm-Horsfall glycoprotein	7369		Tamm-Horsfall glycoprotein (THGP) and the oligosaccharide fraction liberated from THGP by hydrazinolysis inhibited tetanus toxoid-induced T cell proliferation.
9933650	1	17	gly	glycoprotein	81:92	arg1	THGP	THGP				PUBTATOR		THGP	7369		Tamm-Horsfall glycoprotein (THGP) and the oligosaccharide fraction liberated from THGP by hydrazinolysis inhibited tetanus toxoid-induced T cell proliferation.
9933650	1	43	gly	liberated	134:142	arg2	THGP AND the oligosaccharide fraction	THGP			the oligosaccharide fraction	PUBTATOR		THGP	7369		Tamm-Horsfall glycoprotein (THGP) and the oligosaccharide fraction liberated from THGP by hydrazinolysis inhibited tetanus toxoid-induced T cell proliferation.
15014436	7	61	gly	motif	888:892	arg1	T3 repeat 7			motif	T3 repeat 7					motif	The availability for cell attachment of an RGD motif in T3 repeat 7 is modulated by calcium loading.
16212939	4	55	part_of	IL-1ra	822:827	arg1	Asn84	IL-1ra		Asn84		PUBTATOR	AminoAcid	IL-1ra	3557	Asn84	The mutation of potential N-glycosylation site, by substituting Gln for either Asn7 of N-terminal 24 amino acids of hIL-1beta (Asn7Gln) or Asn84 of IL-1ra (Asn84Gln), resulted in a dramatic reduction of rhG-CSF secretion efficiency.
16212939	4	55	part_of	IL-1ra	822:827	arg1	Asn7	IL-1ra		Asn7		PUBTATOR	AminoAcid	IL-1ra	3557	Asn7	The mutation of potential N-glycosylation site, by substituting Gln for either Asn7 of N-terminal 24 amino acids of hIL-1beta (Asn7Gln) or Asn84 of IL-1ra (Asn84Gln), resulted in a dramatic reduction of rhG-CSF secretion efficiency.
9883900	2	53	part_of	IGFBP-5	346:352	arg1	fragments	IGFBP-5		fragments		PUBTATOR	Site	IGFBP-5	3488	fragments	We screened for circulating fragments of human IGFBP-5 in human hemofiltrate.
8885240	2	104	gly	glycosylation	756:768	arg2	N-linked glycosylation sites			N-linked glycosylation sites						sites	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
10092871	6	8	gly	MMP-1	1001:1005	arg1	the N-glycan structures	MMP-1			the N-glycan structures	PUBTATOR		MMP-1	4312		Using strategies based on sequential exoglycosidase digestion combined with matrix-assisted laser desorption ionization-time of flight MS and electrospray tandem MS, we have characterized the N-glycan structures of MMP-1, derived from human dermal fibroblasts and from the HT-1080 fibrosarcoma cell line.
18642129	0	75	gly	VII	93:95	arg1	O-glycans	coagulation factor VII			O-glycans	OGER		coagulation factor VII	P08709		Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.
18642129	0	75	gly	VII	93:95	arg1	N-	coagulation factor VII			N-	OGER		coagulation factor VII	P08709		Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.
22688517	3	77	gly	N-glycosylation	362:376	arg1	LOX-1	LOX-1				PUBTATOR		LOX-1	4973		However, the N-glycosylation pattern of LOX-1 has not been described yet.
28775322	1	22	part_of	EGF-like	216:223	arg1	Notch epidermal growth factor-like (EGF-like) domains	EGF		Notch epidermal growth factor-like (EGF-like) domains		OGER	Site	EGF	P01133	domains	Protein O-glucosyltransferase 1/Rumi-mediated glucosylation of Notch epidermal growth factor-like (EGF-like) domains plays an important role in Notch signaling.
28775322	1	66	part_of	Notch	180:184	arg1	Notch epidermal growth factor-like (EGF-like) domains	Notch		Notch epidermal growth factor-like (EGF-like) domains		PUBTATOR	Site	Notch	31293	domains	Protein O-glucosyltransferase 1/Rumi-mediated glucosylation of Notch epidermal growth factor-like (EGF-like) domains plays an important role in Notch signaling.
22601780	4	30	part_of	EGF	469:471	arg1	the second EGF domain	EGF		the second EGF domain		OGER	Site	EGF	P01133	domain	An Arg-Gly-Asp (RGD) motif in the second EGF domain (EGF2) mediates adhesion by endothelial cells and phagocytes.
22601780	4	42	part_of	motif	449:453	arg1	the second EGF domain	motif		the second EGF domain						domain	An Arg-Gly-Asp (RGD) motif in the second EGF domain (EGF2) mediates adhesion by endothelial cells and phagocytes.
18952059	2	4	part_of	domain	183:188	arg1	a conserved glycosylation site	domain		a conserved glycosylation site						site	It contains one immunoglobulin-like domain with a conserved glycosylation site within.
18234225	3	68	part_of	enzyme	609:614	arg1	the S1' site	enzyme		the S1' site		Fterm	Site	enzyme		site	Crystal structures of GCPII in complex with various ligands have provided insight into the binding of these ligands, particularly to the S1' site of the enzyme.
22688517	5	0	gly	glycopeptides	1059:1071	arg2	glycopeptides			glycopeptides						glycopeptides	Here, an approach using nonspecific protease (Pronase E) digestion followed by MALDI-QIT-TOF MS and multistage MS (MS(3)) analysis is explored to obtain site-specific N-glycosylation information of recombinant human LOX-1, in combination with glycan structure confirmation through characterizing released glycans using tandem MS. The results reveal that N-glycans structures as well as their corresponding attached site of LOX-1 can be identified simultaneously by direct MS analysis of glycopeptides from non-specific protease digestion.
22688517	5	67	gly	LOX-1	995:999	arg1	N-glycans structures	LOX-1			N-glycans structures	PUBTATOR		LOX-1	4973		Here, an approach using nonspecific protease (Pronase E) digestion followed by MALDI-QIT-TOF MS and multistage MS (MS(3)) analysis is explored to obtain site-specific N-glycosylation information of recombinant human LOX-1, in combination with glycan structure confirmation through characterizing released glycans using tandem MS. The results reveal that N-glycans structures as well as their corresponding attached site of LOX-1 can be identified simultaneously by direct MS analysis of glycopeptides from non-specific protease digestion.
15477100	5	20	part_of	ZAG	1032:1034	arg1	the ZAG binding site	ZAG		the ZAG binding site		PUBTATOR	Site	ZAG	563	site	Further support for PEG binding in the ZAG groove is provided by the finding that PEG displaces a fluorophore-tagged fatty acid from the ZAG binding site.
1708771	0	71	part_of	factor	69:74	arg1	Amino acid sequence	stem cell factor		Amino acid sequence		PUBTATOR	Site	stem cell factor	60427	sequence	Amino acid sequence and post-translational modification of stem cell factor isolated from buffalo rat liver cell-conditioned medium.
8323280	2	51	gly	N-glycosylated	406:419	arg1	A peptide			A peptide						peptide	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	2	51	gly	N-glycosylated	406:419	arg2	Asn62			Asn62						Asn62	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	2	87	gly	O-glycosylated	456:469	arg2	Thr7			Thr7						Thr7	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
7512967	8	46	gly	O-glycosylation	1225:1239	arg1	IgG2b	IgG2b				PUBTATOR		IgG2b	16016		A therapeutic significance of the O-glycosylation of IgG2b is briefly discussed.
1533633	0	64	gly	glycosylation	16:28	arg1	the alpha-subunit	the alpha-subunit				OGER		subunit	P06865		Analysis of the glycosylation and phosphorylation of the alpha-subunit of the lysosomal enzyme, beta-hexosaminidase A, by site-directed mutagenesis.
21615908	5	35	gly	glycosylated	891:902	arg1	an evolutionarily conserved protein	protein		Asn30		Fterm		protein		Asn30	Fibin is an evolutionarily conserved protein, carries a cleavable signal peptide (amino acids 1-18) and is glycosylated at Asn30.
21615908	5	35	gly	glycosylated	891:902	arg1	Fibin	Fibin		Asn30		PUBTATOR		Fibin	67606	Asn30	Fibin is an evolutionarily conserved protein, carries a cleavable signal peptide (amino acids 1-18) and is glycosylated at Asn30.
10769135	1	14	part_of	alpha-amylase	200:212	arg1	the active site region	pancreatic alpha-amylase		the active site region		PUBTATOR	Site	pancreatic alpha-amylase	279	region	We report a multifaceted study of the active site region of human pancreatic alpha-amylase.
1512232	8	95	gly	peptide	1546:1552	arg1	the SSS tandem repeat				the SSS tandem repeat						The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
28661582	4	9	part_of	tyrosinase	948:957	arg1	the tyrosinase subdomain	tyrosinase		the tyrosinase subdomain		OGER	Site	tyrosinase	P14679	subdomain	In addition, the structures reveal for the first time that the Cys-rich subdomain, which is unique to vertebrate melanogenic proteins, has an epidermal growth factor-like fold and is tightly associated with the tyrosinase subdomain.
18768470	6	57	part_of	FSTL3	1184:1188	arg1	the FSTL3 N-terminal domain	FSTL3		the FSTL3 N-terminal domain		PUBTATOR	Site	FSTL3	10272	domain	Furthermore, binding studies revealed that replacing the FSTL3 N-terminal domain with the corresponding FS domain considerably lowers activin A affinity.
15983417	4	29	part_of	IL-10R2	559:565	arg1	the IL-22R1 and IL-10R2 binding sites	IL-10R2		the IL-22R1 and IL-10R2 binding sites		OGER	Site	IL-10R2	Q08334	sites	However, 1-4 A main-chain differences are observed between the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites.
7599134	0	50	gly	glycosylation	8:20	arg1	antithrombin III asparagine-135			antithrombin III asparagine-135						asparagine-135	Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity.
25601083	3	20	part_of	Fic	526:528	arg1	a Fic (filamentation induced by cAMP) domain	Fic		a Fic (filamentation induced by cAMP) domain		Cterm	Site	Fic		domain	A family of enzymes, defined by the presence of a Fic (filamentation induced by cAMP) domain, catalyzes this adenylylation reaction.
15965977	7	64	part_of	EGF	1402:1404	arg1	the EGF core ectodomain	EGF		the EGF core ectodomain		OGER	Site	EGF	P01133	ectodomain	It is expressed as two forms with different lengths, forms dimers and interacts with TGF-alpha ligands through a luminal interaction with the EGF core ectodomain.
21987822	1	64	gly	O-glycosylated	182:195	arg1	α-dystroglycan	receptor			α-dystroglycan	Fterm		receptor			α-dystroglycan is a highly O-glycosylated extracellular matrix receptor that is required for anchoring of the basement membrane to the cell surface and for the entry of Old World arenaviruses into cells.
29992770	10	23	gly	N-glycopeptides	1458:1472	arg2	specific N-glycopeptides			specific N-glycopeptides						N-glycopeptides	CONCLUSIONS AND CLINICAL RELEVANCE: The authors are the first to suggest specific N-glycopeptides to serve as potential serum biomarkers to detect preclinical OSCC in patients.
17643119	1	2	part_of	subunit	237:243	arg1	the extracellular domain	subunit		the extracellular domain		Fterm	Site	subunit		domain	We determined the crystal structure of the extracellular domain of the mouse nicotinic acetylcholine receptor (nAChR) alpha1 subunit bound to alpha-bungarotoxin at 1.94 A resolution.
10871631	3	87	part_of	A	593:593	arg1	the C terminus	torsin A		the C terminus		PUBTATOR	Site	torsin A	1861	terminus	The deletion in DYT1 associated with torsion dystonia results in the loss of one of a pair of glutamic acid residues residing near the C terminus of torsin A (DeltaE-torsin A).
23001782	7	33	gly	N-glycoforms	1251:1262	arg1	Asn(351) N-glycoforms			Asn(351) N-glycoforms						Asn(351)	N-Glycoforms of Asn(367) were slightly more branched and core fucosylated than Asn(351) N-glycoforms due probably to a more surface-exposed glycosylation site.
23001782	7	102	gly	glycosylation	1303:1315	arg2	a more surface-exposed glycosylation site			a more surface-exposed glycosylation site						site	N-Glycoforms of Asn(367) were slightly more branched and core fucosylated than Asn(351) N-glycoforms due probably to a more surface-exposed glycosylation site.
2015821	2	21	gly	asparagine-linked	410:426	arg1	the asparagine-linked carbohydrate chains			asparagine	the asparagine-linked carbohydrate chains					asparagine	For each form the asparagine-linked carbohydrate chains were liberated as oligosaccharides by hydrazinolysis, submitted to reduction with NaBH4 after re-N-acetylation and further separated by affinity chromatography on a concanavalin-A-Sepharose column.
15340146	5	11	gly	O-GlcNAc-glycosylated	745:765	arg1	O-GlcNAc-glycosylated proteins				O-GlcNAc-glycosylated proteins						Herein we report the direct, high-throughput analysis of O-GlcNAc-glycosylated proteins from the mammalian brain.
8323280	7	65	gly	Desialylated	1524:1535	arg1	Desialylated rhLT	Desialylated rhLT				Cterm		Desialylated rhLT			Desialylated rhLT showed a lectin-like binding character to uromodulin similar to that of tumor necrosis factor, although intact rhLT did not.
24417605	7	21	gly	apolipoprotein	1058:1071	arg1	fetuin A. GM3	apolipoprotein CIII			fetuin A. GM3	PUBTATOR		apolipoprotein CIII	345		The observed O-glycans were all sialylated, and most contained a core 1 structure with two Neu5Acs, including those that were associated with apolipoprotein CIII (ApoC-III) and fetuin A. GM3 (monosialoganglioside, NeuAc2-3Gal1-4Glc-Cer) and GD3 (disialoganglioside, NeuAc2-8NeuAc2-3Gal1-4Glc-Cer) were the major gangliosides in HDL.
24417605	7	39	gly	sialylated	948:957	arg1	The observed O-glycans				The observed O-glycans						The observed O-glycans were all sialylated, and most contained a core 1 structure with two Neu5Acs, including those that were associated with apolipoprotein CIII (ApoC-III) and fetuin A. GM3 (monosialoganglioside, NeuAc2-3Gal1-4Glc-Cer) and GD3 (disialoganglioside, NeuAc2-8NeuAc2-3Gal1-4Glc-Cer) were the major gangliosides in HDL.
1512232	9	32	part_of	observed	1665:1672	arg1	SRF AND The other glycosylation sites	SRF		The other glycosylation sites		PUBTATOR	Site	SRF	6722	sites	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	9	102	part_of	region	1700:1705	arg1	The other glycosylation sites	region		The other glycosylation sites						sites	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
2136357	1	37	gly	glycoprotein	135:146	arg1	The urinary glycoprotein uromodulin	The urinary glycoprotein uromodulin				Fterm		glycoprotein			The urinary glycoprotein uromodulin (Tamm-Horsfall glycoprotein) exhibits a pregnancy-associated ability to inhibit antigen-specific T cell proliferation, and the activity is associated with a carbohydrate moiety [Muchmore and Decker (1985) Science 229:479-81; Hession et al., (1987) Science 237:1479-84; Muchmore, Shifrin and Decker (1987) J Immunol 138:2547-53].
2136357	1	47	gly	glycoprotein	174:185	arg1	The urinary glycoprotein uromodulin	The urinary glycoprotein uromodulin				PUBTATOR		uromodulin	7369		The urinary glycoprotein uromodulin (Tamm-Horsfall glycoprotein) exhibits a pregnancy-associated ability to inhibit antigen-specific T cell proliferation, and the activity is associated with a carbohydrate moiety [Muchmore and Decker (1985) Science 229:479-81; Hession et al., (1987) Science 237:1479-84; Muchmore, Shifrin and Decker (1987) J Immunol 138:2547-53].
2136357	1	47	gly	glycoprotein	174:185	arg1	Tamm-Horsfall glycoprotein	Tamm-Horsfall glycoprotein				OGER		Tamm-Horsfall glycoprotein	P07911		The urinary glycoprotein uromodulin (Tamm-Horsfall glycoprotein) exhibits a pregnancy-associated ability to inhibit antigen-specific T cell proliferation, and the activity is associated with a carbohydrate moiety [Muchmore and Decker (1985) Science 229:479-81; Hession et al., (1987) Science 237:1479-84; Muchmore, Shifrin and Decker (1987) J Immunol 138:2547-53].
22483115	0	7	part_of	Fab	89:91	arg1	an inhibitory Fab fragment	Fab		an inhibitory Fab fragment		PUBTATOR	Site	Fab	2187	fragment	Structure of the discoidin domain receptor 1 extracellular region bound to an inhibitory Fab fragment reveals features important for signaling.
22483115	0	31	part_of	receptor	34:41	arg1	the discoidin domain receptor 1 extracellular region	receptor 1		the discoidin domain receptor 1 extracellular region		Fterm	Site	receptor 1	780	region	Structure of the discoidin domain receptor 1 extracellular region bound to an inhibitory Fab fragment reveals features important for signaling.
24334224	0	37	gly	glycosylation	9:21	arg1	recombinant human granulocyte colony-stimulating factor	recombinant human granulocyte colony-stimulating factor				PUBTATOR		granulocyte colony-stimulating factor	1440		O-linked glycosylation analysis of recombinant human granulocyte colony-stimulating factor produced in glycoengineered Pichia pastoris by liquid chromatography and mass spectrometry.
19683538	5	49	part_of	enzyme	1000:1005	arg1	the active site	enzyme		the active site		Fterm	Site	enzyme		site	To investigate the binding specificity and catalytic mechanism of the human alpha-NAGAL enzyme, we determined three crystallographic complexes with different catalytic products bound in the active site of the enzyme.
8344280	2	76	gly	O-glycosylation	287:301	arg2	artificially introduced N-glycosylation or O-glycosylation sites			artificially introduced N-glycosylation or O-glycosylation sites						sites	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	2	79	gly	N-glycosylation	268:282	arg1	Human interleukin 2 (IL-2) and human IL-2 mutant proteins	Human interleukin 2 (IL-2) and human IL-2 mutant proteins				Fterm		proteins			Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
17330941	5	57	part_of	PNGase	725:730	arg1	PNGase F. Biotinylated cysteinyl-containing glycopeptides	PNGase F		PNGase F. Biotinylated cysteinyl-containing glycopeptides		OGER	Site	PNGase F	Q96IV0	glycopeptides	After trypsinization and extensive washing, tethered N-glycosylated tryptic peptides are released from the gel using PNGase F. Biotinylated cysteinyl-containing glycopeptides are then affinity selected using a monomeric avidin gel and analyzed by LC-MS/MS.
17330941	5	62	part_of	F.	732:733	arg1	PNGase F. Biotinylated cysteinyl-containing glycopeptides	PNGase F		PNGase F. Biotinylated cysteinyl-containing glycopeptides		OGER	Site	PNGase F	Q96IV0	glycopeptides	After trypsinization and extensive washing, tethered N-glycosylated tryptic peptides are released from the gel using PNGase F. Biotinylated cysteinyl-containing glycopeptides are then affinity selected using a monomeric avidin gel and analyzed by LC-MS/MS.
2001369	7	43	gly	carry	1137:1141	arg1	Asn-271 AND diantennary N-acetyllactosamine-type ("complex") oligosaccharides			Asn-271	diantennary N-acetyllactosamine-type ("complex") oligosaccharides					Asn-271	Asn-271 was found to carry diantennary N-acetyllactosamine-type ("complex") oligosaccharides, of which 8% were asialo, 55% were monosialyl, and 37% were disialyl.
20581009	3	31	gly	Endocan	567:573	arg1	the glycosaminoglycan (GAG) chain	Endocan			the glycosaminoglycan (GAG) chain	PUBTATOR		Endocan	11082		In this work, we characterized the glycosaminoglycan (GAG) chain of Endocan, purified either from the naturally producing human umbilical vein endothelial cells (HUVEC) or from a recombinant over-expression system in human embryonic kidney cells (HEK).
24134926	8	67	gly	attachment	1455:1464	arg2	specific aminoacid residues AND the monosaccharide β-N-acetylglucosamine			specific aminoacid residues	the monosaccharide β-N-acetylglucosamine					residues	However, the most general sensor of cellular nutritional status is the hexosamine biosynthetic pathway that brings to the formation of UDP-GlcNAc and intracellular protein glycosylation by O-linked attachment of the monosaccharide β-N-acetylglucosamine (O-GlcNAcylation) to specific aminoacid residues.
10929010	4	6	gly	Asn-linked	863:872	arg1	the Asn-linked N-acetylglucosamine			Asn	the Asn-linked N-acetylglucosamine					Asn	The attached oligosaccharides included high mannose, paucimannosidic, and hybrid structures with over 50% of these structures containing one fucose, alpha(1,6)-, or two fucoses, alpha(1,6)- and alpha(1,3)-, linked to the Asn-linked N-acetylglucosamine.
8670172	9	73	gly	chain	1339:1343	arg1	Asn-18			Asn-18	Asn-18		SpecificSite			Asn-18	The N-linked carbohydrate side chain of CD59u (at Asn-18) also displayed considerable heterogeneity.
8670172	9	92	gly	CD59u	1348:1352	arg1	The N-linked carbohydrate side chain	CD59u			The N-linked carbohydrate side chain	PUBTATOR		CD59u	966		The N-linked carbohydrate side chain of CD59u (at Asn-18) also displayed considerable heterogeneity.
8670172	9	96	gly	Asn-18	1358:1363	arg1	The N-linked carbohydrate side chain			Asn-18	The N-linked carbohydrate side chain					Asn-18	The N-linked carbohydrate side chain of CD59u (at Asn-18) also displayed considerable heterogeneity.
25374123	1	63	gly	glycoprotein	198:209	arg1	glycoprotein	glycoprotein				Fterm		glycoprotein			The characterization of site-specific microheterogeneity in glycoprotein is very important for understanding cell biology and disease processes.
19951703	4	6	gly	N-glycosylation	402:416	arg2	residues 71, 292, and 344			residues 71, 292, and 344						residues 71, 292, and 344	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	4	6	gly	N-glycosylation	402:416	arg2	the potential N-glycosylation sites			the potential N-glycosylation sites						sites	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	4	8	gly	glutamine	473:481	arg1	asparagine			asparagine						asparagine	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	4	11	gly	glycosylation	547:559	arg1	the glycan				the glycan						Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
20133774	2	27	part_of	PTPRG	409:413	arg1	the carbonic anhydrase-like domains	PTPRG		the carbonic anhydrase-like domains		PUBTATOR	Site	PTPRG	19270	domains	We report here the crystal structures of the carbonic anhydrase-like domains of PTPRZ and PTPRG and show that these domains interact directly with the second and third immunoglobulin repeats of the members of the contactin (CNTN) family of neural recognition molecules.
20133774	2	32	part_of	PTPRZ	399:403	arg1	the carbonic anhydrase-like domains	PTPRZ		the carbonic anhydrase-like domains		PUBTATOR	Site	PTPRZ	19283	domains	We report here the crystal structures of the carbonic anhydrase-like domains of PTPRZ and PTPRG and show that these domains interact directly with the second and third immunoglobulin repeats of the members of the contactin (CNTN) family of neural recognition molecules.
2129367	7	52	gly	released	908:915	arg1	the peptides AND The trisaccharide			the peptides	The trisaccharide					peptides	The trisaccharide was released from the peptides by means of beta-elimination reaction and its reducing end was identified as pyridylamino-glucose.
23527852	10	11	gly	fucosylated	1284:1294	arg1	fucosylated apolipoprotein-CIII isoforms				fucosylated apolipoprotein-CIII isoforms						These findings of fucosylated apolipoprotein-CIII isoforms warrant further research to elucidate the implications these glycoforms may have for the plethora of studies where alterations in apoCIII have been linked to the development of many different pathologies.
8617200	5	66	part_of	beta1-LAP	992:1000	arg1	Cys33	LAP		Cys33		PUBTATOR	AminoAcid	LAP	P11117	Cys33	The cysteine required for the association between LTBP-1 and beta1-LAP was mapped to Cys33 of beta1-LAP.
16650853	3	39	gly	glycosylated	539:550	arg1	glycosylated peptides			glycosylated peptides						peptides	Here we present crystal structures of the pp-GalNAc-T10 isozyme, which has specificity for glycosylated peptides, in complex with the hydrolyzed donor substrate UDP-GalNAc and in complex with GalNAc-serine.
29932112	10	20	gly	un-glycosylated	1353:1367	arg1	Panx1	Panx1				PUBTATOR		Panx1 and 2	24145		We found that the un-glycosylated forms of Panx1 and 2 can readily interact, regulating their localization and potentially their channel function in cells where they are co-expressed.
20450227	10	42	gly	glycosylation	1818:1830	arg2	human P2X(7) glycosylation sites			human P2X(7) glycosylation sites						sites	This is the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function.
8053566	0	64	gly	glycoprotein	34:45	arg1	glycoprotein carbohydrates				glycoprotein carbohydrates						Site-specific characterization of glycoprotein carbohydrates by exoglycosidase digestion and laser desorption mass spectrometry.
7629073	9	21	part_of	clone	1525:1529	arg1	the corresponding region	clone 4		the corresponding region		PUBTATOR	Site	clone 4	22116	region	When expressed in COS7 cells as a secreted protein A fusion protein, the catalytic domain of clone 16 displays alpha-1,2-mannosidase activity using [3H]mannose-labeled Man9GlcNAc as substrate, but the corresponding region of clone 4 is poorly secreted under identical conditions.
10551839	2	72	gly	C-mannosylated	387:400	arg1	only the first Trp			only the first Trp						Trp	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
22041449	4	16	part_of	contains	703:710	arg1	the LN domain region AND the binding site	the LN domain region		the binding site						site	Here, we use deletion analysis to show that the LN domain region of netrin Gs contains the binding site for NGLs to which they bind with 1:1 stoichiometry and sub-micromolar affinity.
2129367	0	58	part_of	factors	100:106	arg1	the first EGF-like domain	factors		the first EGF-like domain		Fterm	Site	factors		domain	A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z. Recently, we determined the complete amino acid sequence of bovine factor VII (Takeya, H. et al. (1988) J. Biol.
2129367	0	63	part_of	residue	51:57	arg1	clotting factors	factors		residue		Fterm	AminoAcid	factors		serine residue	A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z. Recently, we determined the complete amino acid sequence of bovine factor VII (Takeya, H. et al. (1988) J. Biol.
2129367	0	71	part_of	EGF-like	72:79	arg1	the first EGF-like domain	EGF		the first EGF-like domain		OGER	Site	EGF	P01133	domain	A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z. Recently, we determined the complete amino acid sequence of bovine factor VII (Takeya, H. et al. (1988) J. Biol.
2129367	0	77	part_of	VII	208:210	arg1	the complete amino acid sequence	factor VII		the complete amino acid sequence		OGER	Site	factor VII	P08709	sequence	A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z. Recently, we determined the complete amino acid sequence of bovine factor VII (Takeya, H. et al. (1988) J. Biol.
14699159	2	45	gly	glycosylation	462:474	arg2	three evolutionarily conserved N-linked glycosylation sites			three evolutionarily conserved N-linked glycosylation sites						sites	ATF6, a 90-kDa ER transmembrane protein, contains three evolutionarily conserved N-linked glycosylation sites within its carboxyl luminal domain.
6526384	3	28	part_of	contains	440:447	arg1	The protein AND 20 cysteine residues	The protein		20 cysteine residues		Fterm	AminoAcid	protein		cysteine residues	The protein contains 20 cysteine residues but, as a special feature, no methionine.
1421756	0	5	part_of	residue	52:58	arg1	the human transferrin receptor	transferrin receptor		residue		PUBTATOR	AminoAcid	transferrin receptor	7037	threonine residue	Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor.
7613477	5	51	part_of	LCAT	1156:1159	arg1	All four potential N-linked glycosylation sites	LCAT		All four potential N-linked glycosylation sites		PUBTATOR	Site	LCAT	3931	sites	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	51	part_of	LCAT	1156:1159	arg1	Asn384	LCAT		Asn20, Asn84, Asn272, and Asn384		PUBTATOR	AminoAcid	LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	51	part_of	LCAT	1156:1159	arg1	Asn84	LCAT		Asn20, Asn84, Asn272, and Asn384		PUBTATOR	AminoAcid	LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	51	part_of	LCAT	1156:1159	arg1	Asn84	LCAT		Asn20, Asn84, Asn272, and Asn384		PUBTATOR	AminoAcid	LCAT	3931	Asn20, Asn84, Asn272, and Asn384	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
14760718	3	28	gly	glycoproteins	461:473	arg1	glycoproteins	glycoproteins				Fterm		glycoproteins			The detailed characterization of glycoproteins in complex biological samples is extremely challenging.
22613618	3	27	gly	N-glycosylation	269:283	arg2	Two successive N-glycosylation consensus sites			Two successive N-glycosylation consensus sites						sites	Two successive N-glycosylation consensus sites, N228NS and N229ST, are present on the S1-S2 linker of rat Kv1.3.
9524075	8	68	gly	non-glycosylated	870:885	arg1	non-glycosylated procathepsin S	non-glycosylated procathepsin S				Cterm		non-glycosylated procathepsin S	1520		In vitro processing of glycosylated as well as of non-glycosylated procathepsin S gave fully active enzymes thus indicating that the oligosaccharide chain was not necessary for proper folding.
12731890	1	47	gly	glycoprotein	137:148	arg1	a transmembrane glycoprotein	a transmembrane glycoprotein				Fterm		glycoprotein			The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	1	47	gly	glycoprotein	137:148	arg1	The epidermal growth factor receptor	The epidermal growth factor receptor				PUBTATOR		epidermal growth factor receptor	1956		The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
27313224	4	32	part_of	PNG	797:799	arg1	PNG sites	PNG		sites		OGER	Site	PNG	Q96C90	sites	SV2C-LD4 exhibits the strongest protein-protein interaction and comprises five putative N-glycosylation sites (PNG sites).
16342937	0	104	gly	glycoproteins	56:68	arg1	zona pellucida glycoproteins	zona pellucida glycoproteins				Fterm		glycoproteins			Structural conservation of mouse and rat zona pellucida glycoproteins.
7654718	11	57	part_of	C-tail	1627:1632	arg1	the C-tail region	C-tail		the C-tail region		Cterm	Site	C-tail		region	These observations suggest the possibility that the C-tail region may contribute to adhesive activity in the physiological function of BAL.
21500857	9	5	part_of	AP180	1102:1106	arg1	A second AP180 tryptic peptide	AP180		A second AP180 tryptic peptide		PUBTATOR	Site	AP180	65178	peptide	Direct O-linkage of GlcNAc-P to a Thr residue was confirmed by electron transfer dissociation MS. A second AP180 tryptic peptide was also glycosyl phosphorylated, but the site of modification was not assigned.
11741940	8	32	gly	moiety	1571:1576	arg1	Asn			Asn	Asn		SpecificSite			Asn(172)	Analysis of glycosylation sites showed that sFRP-1 contains a relatively large carbohydrate moiety on Asn(172) (approximately 2.8 kDa), whereas Asn(262), the second potential N-linked glycosylation site, is not modified.
11741940	8	32	gly	moiety	1571:1576	arg1	172			172	172		SpecificSite			Asn(172)	Analysis of glycosylation sites showed that sFRP-1 contains a relatively large carbohydrate moiety on Asn(172) (approximately 2.8 kDa), whereas Asn(262), the second potential N-linked glycosylation site, is not modified.
11741940	8	42	gly	glycosylation	1491:1503	arg2	glycosylation sites			glycosylation sites						sites	Analysis of glycosylation sites showed that sFRP-1 contains a relatively large carbohydrate moiety on Asn(172) (approximately 2.8 kDa), whereas Asn(262), the second potential N-linked glycosylation site, is not modified.
11741940	8	100	gly	glycosylation	1663:1675	arg2	Asn			Asn						Asn(262)	Analysis of glycosylation sites showed that sFRP-1 contains a relatively large carbohydrate moiety on Asn(172) (approximately 2.8 kDa), whereas Asn(262), the second potential N-linked glycosylation site, is not modified.
11741940	8	100	gly	glycosylation	1663:1675	arg2	the second potential N-linked glycosylation site			the second potential N-linked glycosylation site						site	Analysis of glycosylation sites showed that sFRP-1 contains a relatively large carbohydrate moiety on Asn(172) (approximately 2.8 kDa), whereas Asn(262), the second potential N-linked glycosylation site, is not modified.
11741940	8	87	gly	contains	1530:1537	arg1	sFRP-1 AND a relatively large carbohydrate moiety	sFRP-1			a relatively large carbohydrate moiety	PUBTATOR		sFRP-1	6422		Analysis of glycosylation sites showed that sFRP-1 contains a relatively large carbohydrate moiety on Asn(172) (approximately 2.8 kDa), whereas Asn(262), the second potential N-linked glycosylation site, is not modified.
14711516	8	33	gly	glycoproteins	1572:1584	arg1	intact glycoproteins	intact glycoproteins				Fterm		glycoproteins			The ability to generate recombinant glycoproteins with restricted carbohydrate heterogeneity is the first step toward the systematic study of structure-function relationships in intact glycoproteins.
14711516	8	60	gly	glycoproteins	1423:1435	arg1	recombinant glycoproteins				recombinant glycoproteins						The ability to generate recombinant glycoproteins with restricted carbohydrate heterogeneity is the first step toward the systematic study of structure-function relationships in intact glycoproteins.
2943741	5	18	gly	beta	1066:1069	arg1	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH	Gal beta 1			NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH	OGER		Gal beta 1			On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
8670172	0	35	gly	heterogeneity	72:84	arg1	oligosaccharide				oligosaccharide						Structural composition and functional characterization of soluble CD59: heterogeneity of the oligosaccharide and glycophosphoinositol (GPI) anchor revealed by laser-desorption mass spectrometric analysis.
19196183	1	40	gly	glycosylated	265:276	arg1	all secreted proteins	all secreted proteins				Fterm		proteins			N-linked glycosylation is prevalent in proteins destined for extracellular environments; nearly all secreted proteins are glycosylated.
16263699	4	66	part_of	proteins	670:677	arg1	N-glycosylation sites	proteins		N-glycosylation sites		Fterm	Site	proteins		sites	Here we report the analysis of N-glycosylation sites of human platelet proteins.
16332679	13	22	gly	O-glycosylation	2075:2089	arg1	Sp1	Sp1				OGER		Sp1	P08047		Thus, O-glycosylation of Sp1 appears to be critical for its localization into the nucleus, where it undergoes obligatory phosphorylation that is needed for Sp1 to activate calmodulin gene expression.
20622017	8	34	gly	glycopeptides	1101:1113	arg2	hepatic GGT glycopeptides			hepatic GGT glycopeptides						glycopeptides	However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT.
2001369	11	70	gly	Asn-300	1755:1761	arg1	the N-acetyllactosamine structures			Asn-300	the N-acetyllactosamine structures					Asn-300	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	70	gly	Asn-300	1755:1761	arg1	the hybrid structures			Asn-300	the hybrid structures					Asn-300	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
17105447	1	23	gly	carry	161:165	arg1	Most soluble lysosomal proteins AND Man6P	Most soluble lysosomal proteins			Man6P	Fterm		proteins			Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	1	23	gly	carry	161:165	arg1	Most soluble lysosomal proteins AND a specific carbohydrate marker	Most soluble lysosomal proteins			a specific carbohydrate marker	Fterm		proteins			Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
8942648	3	86	part_of	residues	401:408	arg1	Peptide	Peptide		residues		OGER	SpecificSite	Peptide		residues 1	Peptide, disulfide, and glycosylation mapping of human TPO from residues 1 to 246 has been carried out using liquid chromatography-electrospray mass spectrometry (LC-ESMS).
8942648	3	91	part_of	TPO	392:394	arg1	Peptide	TPO		Peptide		PUBTATOR		TPO	7066		Peptide, disulfide, and glycosylation mapping of human TPO from residues 1 to 246 has been carried out using liquid chromatography-electrospray mass spectrometry (LC-ESMS).
9883900	3	26	part_of	IGFBP-5	395:401	arg1	IGFBP-5 peptides	IGFBP-5		IGFBP-5 peptides		PUBTATOR	Site	IGFBP-5	3488	peptides	Identification of IGFBP-5 peptides in the fractions of our peptide bank generated from hemofiltrate was performed by their immunoreactivity and their capacity to bind IGF-I.
3567160	2	58	gly	Asparagine-linked	212:228	arg1	Asparagine-linked neutral oligosaccharides			Asparagine	Asparagine-linked neutral oligosaccharides					Asparagine	Asparagine-linked neutral oligosaccharides were released by N-oligosaccharide glycopeptidase (almond) digestion.