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 2498325 0 83 gly Glycosylation 0:12 arg1 human apolipoprotein E human apolipoprotein E PUBTATOR apolipoprotein E 348 Glycosylation of human apolipoprotein E. 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. 27399812 3 95 gly glycopeptide 516:527 arg2 true high-throughput glycopeptide analysis true high-throughput glycopeptide analysis glycopeptide Efficient data interpretation constitutes one of the major challenges to be overcome before true high-throughput glycopeptide analysis can be achieved. 26274980 5 49 gly glycoproteins 1546:1558 arg1 even relatively simple glycoproteins even relatively simple glycoproteins Fterm glycoproteins This work highlights the continued requirement of using complementary technologies to accurately profile even relatively simple glycoproteins and illustrates important challenges associated with the analysis of unconventional protein N-glycosylation. 8626443 3 39 gly unglycosylated 510:523 arg1 unglycosylated ACET unglycosylated ACET Cterm ACET Similarly, unglycosylated ACET synthesized in HeLa cells, by using a cDNA in which all five potential N-glycosylation sites had been mutated, was inactive and rapidly degraded. 8626443 3 43 gly N-glycosylation 601:615 arg2 all five potential N-glycosylation sites all five potential N-glycosylation sites sites Similarly, unglycosylated ACET synthesized in HeLa cells, by using a cDNA in which all five potential N-glycosylation sites had been mutated, was inactive and rapidly degraded. 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. 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. 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. 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. 23723439 8 29 gly glycosylated 1609:1620 arg1 the sulfated α-DG the sulfated α-DG Cterm DG 1605 Furthermore, using an in vitro enzymatic assay system, we demonstrated that the sulfated α-DG by HNK-1ST is no longer glycosylated by LARGE. 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. 32111832 3 30 gly glycosylated 365:376 arg1 a glycosylated Golgi-resident membrane protein a glycosylated Golgi-resident membrane protein Fterm protein 235623 SPRING is a glycosylated Golgi-resident membrane protein and its ablation in Hap1 cells, Hepa1-6 hepatoma cells, and primary murine hepatocytes reduces SREBP signaling. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 23723439 2 0 gly attached 420:427 arg1 its extracellular α-DG subunit AND O-mannosyl glycans its extracellular α-DG subunit O-mannosyl glycans Cterm DG subunit 1605 Since the ligand-binding activity of DG strictly depends on O-mannosyl glycans attached to its extracellular α-DG subunit, aberrant glycosylation causes dystroglycanopathy, a subclass of congenital muscular dystrophy. 9883900 8 41 gly O-glycosylated 1224:1237 arg1 Thr-152 Thr-152 insulin 3488 Thr-152 According to mass spectrometric and sequence analysis, Thr-152 was shown to be O-glycosylated. 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. 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. 26274980 0 52 gly serine 209:214 arg1 Complementary LC-MS/MS-Based N-Glycan serine Complementary LC-MS/MS-Based N-Glycan serine Complementary LC-MS/MS-Based N-Glycan, N-Glycopeptide, and Intact N-Glycoprotein Profiling Reveals Unconventional Asn71-Glycosylation of Human Neutrophil Cathepsin G. Neutrophil cathepsin G (nCG) is a central serine protease in the human innate immune system, but the importance of its N-glycosylation remains largely undescribed. 26274980 0 78 gly Asn71-Glycosylation 114:132 arg1 nCG nCG Cterm nCG 1511 Complementary LC-MS/MS-Based N-Glycan, N-Glycopeptide, and Intact N-Glycoprotein Profiling Reveals Unconventional Asn71-Glycosylation of Human Neutrophil Cathepsin G. Neutrophil cathepsin G (nCG) is a central serine protease in the human innate immune system, but the importance of its N-glycosylation remains largely undescribed. 26274980 0 78 gly Asn71-Glycosylation 114:132 arg1 Human Neutrophil Cathepsin G. Neutrophil cathepsin G Human Neutrophil Cathepsin G. Neutrophil cathepsin G PUBTATOR Neutrophil cathepsin G 1511 Complementary LC-MS/MS-Based N-Glycan, N-Glycopeptide, and Intact N-Glycoprotein Profiling Reveals Unconventional Asn71-Glycosylation of Human Neutrophil Cathepsin G. Neutrophil cathepsin G (nCG) is a central serine protease in the human innate immune system, but the importance of its N-glycosylation remains largely undescribed. 31959827 0 83 gly O-glycoforms 12:23 arg1 the IgA1 hinge region the IgA1 hinge region region Analysis of O-glycoforms of the IgA1 hinge region by sequential deglycosylation. 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. 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. 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. 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. 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. 35377815 1 38 gly glycoprotein 112:123 arg1 The glycoprotein von Willebrand factor The glycoprotein von Willebrand factor Fterm glycoprotein The glycoprotein von Willebrand factor (VWF) contributes to hemostasis by stanching injuries in blood vessel walls. 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. 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). 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. 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. 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. 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. 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. 18491227 9 20 gly N-glycosylation 1457:1471 arg1 Asn-633 E-cadherin expression Asn-633 E-cadherin P12830 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 P12830 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 P12830 Asn-633 In conclusion, this study revealed that N-glycosylation at Asn-633 is essential for E-cadherin expression, folding and trafficking. 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. 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. 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). 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). 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. 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). 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 eotaxin 6356 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. 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. 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. 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. 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. 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. 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. 2498325 1 25 gly threonine 77:85 arg1 The carbohydrate attachment site threonine 194 The carbohydrate attachment site apolipoprotein E 348 threonine 194 The carbohydrate attachment site is threonine 194. 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. 16698036 1 75 gly beta-hexosaminidase 147:165 arg1 Hex A beta-hexosaminidase Hex A OGER beta-hexosaminidase Lysosomal beta-hexosaminidase A (Hex A) is essential for the degradation of GM2 gangliosides in the central and peripheral nervous system. 32815518 1 31 gly glycoprotein 101:112 arg1 The glycoprotein uromodulin The glycoprotein uromodulin Fterm glycoprotein The glycoprotein uromodulin (UMOD) is the most abundant protein in human urine and forms filamentous homopolymers that encapsulate and aggregate uropathogens, promoting pathogen clearance by urine excretion. 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. 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. 3353370 8 64 gly chain 1717:1721 arg1 the leucine-rich tandem repeats alpha chain the leucine-rich tandem repeats PUBTATOR alpha chain 2217 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. 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. 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. 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. 16040958 0 54 gly glycosylation 9:21 arg2 Asn3 Asn3 C1INH P05155 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. 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. 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. 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). 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). 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). 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). 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. 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. 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. 20826823 6 6 gly glycosylated 1046:1057 arg1 the potential glycan sites the potential glycan sites At least eight of 10 of the potential glycan sites are glycosylated; three C-terminal sites were sufficient for expression of active N domain, whereas two N-terminal sites are important for its thermal stability. 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. 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. 3497398 10 72 gly 2-glycoprotein 1677:1690 arg1 human leucine-rich alpha 2-glycoprotein human leucine-rich alpha 2-glycoprotein Fterm 2-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. 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. 21515415 4 19 gly utilized 664:671 arg2 all six sites all six sites sites The apparent size of each of the six PLTP mutants was slightly less than that of wild type by Western blot, indicating that all six sites are glycosylated or utilized. 21515415 4 69 gly glycosylated 648:659 arg1 all six sites all six sites sites The apparent size of each of the six PLTP mutants was slightly less than that of wild type by Western blot, indicating that all six sites are glycosylated or utilized. 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. 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. 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. 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. 8670172 14 8 gly CD59 1926:1929 arg1 N-linked oligosaccharide CD59 N-linked oligosaccharide OGER CD59 P13987 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. 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. 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. 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. 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). 21606496 5 39 gly 2B4 641:643 arg1 sialylation 2B4 sialylation OGER 2B4 Q9BZW8 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 OGER 2B4 Q9BZW8 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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). 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. 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. 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. 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. 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. 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. 22576872 7 13 gly Tyr10 1315:1319 arg1 O-glycans Tyr10 O-glycans Amyloid precursor protein 351 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). 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 21763278 10 62 gly contained 1037:1045 arg1 residue Thr-71 AND little O-glycans residue Thr-71 little O-glycans BNP 4879 Thr-71 In HL-1 cardiomyocytes, residue Thr-71 contained little O-glycans, and pro-BNP WT and T71A mutant were processed similarly. 18703501 7 48 gly glycosylation 1295:1307 arg2 Asn(309) CA IX Asn(309) 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 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 CA IX Asn(309) high mannose-type glycan structures 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 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. 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 11450 Uptake of desialylated adiponectin by isolated primary rat hepatocytes was also accelerated, suggesting a role for the hepatic asialoglycoprotein receptor. 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. 23742080 10 47 gly N-glycosylation 1467:1481 arg1 residue N183 residue N183 TMEM106B p 54664 residue N183 Cycloheximide treatment experiments revealed that S185 degrades faster than T185 TMEM106B, potentially due to differences in N-glycosylation at residue N183. 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. 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. 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. 15014436 9 43 gly TSP-5/COMP 1091:1100 arg1 the T3 repeats TSP the T3 repeats PUBTATOR TSP 1311 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. 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. 12022871 8 4 gly glycosylated 1241:1252 arg1 Human TGH Human TGH PUBTATOR Human TGH 1066 Human TGH was glycosylated in the insect cells. 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. 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. 16870210 0 41 gly peptide 39:45 arg1 Structural determinants peptide Structural determinants peptide Structural determinants of natriuretic peptide receptor specificity and degeneracy. 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. 3881423 7 42 gly glycoproteins 1259:1271 arg1 neutral alpha-glucosidase AB neutral alpha-glucosidase AB OGER neutral alpha-glucosidase AB Q14697 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 OGER neutral alpha-glucosidase AB Q14697 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. 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. 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. 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. 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. 27399812 6 20 gly glycopeptides 913:925 arg2 glycopeptides glycopeptides glycopeptides We have analyzed MS data sets from two separate glycopeptide enrichment protocols targeting sialylated glycopeptides and chondroitin sulfate linkage region glycopeptides, respectively. 27399812 6 33 gly glycopeptides 966:978 arg2 sialylated glycopeptides and chondroitin sulfate linkage region glycopeptides sialylated glycopeptides and chondroitin sulfate linkage region glycopeptides glycopeptides We have analyzed MS data sets from two separate glycopeptide enrichment protocols targeting sialylated glycopeptides and chondroitin sulfate linkage region glycopeptides, respectively. 27399812 6 72 gly glycopeptide 858:869 arg2 two separate glycopeptide enrichment protocols two separate glycopeptide enrichment protocols glycopeptide We have analyzed MS data sets from two separate glycopeptide enrichment protocols targeting sialylated glycopeptides and chondroitin sulfate linkage region glycopeptides, respectively. 27399812 6 75 gly sialylated 902:911 arg1 sialylated glycopeptides and chondroitin sulfate linkage region glycopeptides sialylated glycopeptides and chondroitin sulfate linkage region glycopeptides glycopeptides We have analyzed MS data sets from two separate glycopeptide enrichment protocols targeting sialylated glycopeptides and chondroitin sulfate linkage region glycopeptides, respectively. 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. 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"). 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) asporin 54829 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) asporin 54829 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) asporin 54829 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) asporin 54829 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). 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). 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. 8069634 6 30 gly glycoprotein 1121:1132 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. 27399812 9 26 gly modifications 1539:1551 arg1 the linkage region the linkage region the linkage region Site region These signatures were further used to guide database searches leading to the identification and validation of a large number of glycopeptide variants including novel deoxyhexose (fucose) modifications in the linkage region of chondroitin sulfate proteoglycans. 27399812 9 36 gly variants 1493:1500 arg1 novel deoxyhexose (fucose) modifications variants novel deoxyhexose (fucose) modifications Fterm variants These signatures were further used to guide database searches leading to the identification and validation of a large number of glycopeptide variants including novel deoxyhexose (fucose) modifications in the linkage region of chondroitin sulfate proteoglycans. 27399812 9 87 gly glycopeptide 1480:1491 arg1 novel deoxyhexose (fucose) modifications glycopeptide novel deoxyhexose (fucose) modifications glycopeptide These signatures were further used to guide database searches leading to the identification and validation of a large number of glycopeptide variants including novel deoxyhexose (fucose) modifications in the linkage region of chondroitin sulfate proteoglycans. 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. 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. 20823119 7 41 gly O-glycosylation 1219:1233 arg2 all O-glycosylation sites all O-glycosylation sites sites The IgA-specific proteases provided a variety of IgA1 HR fragments that allowed unambiguous localization of all O-glycosylation sites in the six most abundant glycoforms, including the sites deficient in Gal. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 31959827 2 73 gly sialylation 374:384 arg1 Ser/Thr-linked N-acetylgalactosamine Ser/Thr-linked N-acetylgalactosamine IgA1 hinge region (HR) has up to six clustered O-glycans consisting of Ser/Thr-linked N-acetylgalactosamine with β1,3-linked galactose and variable sialylation. 31959827 2 31 gly has 249:251 arg1 IgA1 hinge region AND up to six clustered O-glycans IgA1 hinge region up to six clustered O-glycans region IgA1 hinge region (HR) has up to six clustered O-glycans consisting of Ser/Thr-linked N-acetylgalactosamine with β1,3-linked galactose and variable sialylation. 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. 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. 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. 1694179 9 28 gly glycosylated 1241:1252 arg1 beta protein C protein C asparagine 329 OGER protein C P02810 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 protein C P02810 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 protein C asparagine 329 OGER protein C P02810 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. 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. 8393577 4 53 gly glycosylation 1060:1072 arg2 Asn-70 Asn-70 cathepsin D 1509 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. 20357243 1 65 gly G 235:235 arg1 glycans human immunoglobulin G glycans Cterm human immunoglobulin G EndoS from Streptococcus pyogenes is an immunomodulating enzyme that specifically hydrolyzes glycans from human immunoglobulin G and thereby affects antibody effector functions. 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. 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. 23723439 1 61 gly glycoprotein 170:181 arg1 a cell surface glycoprotein glycoprotein Dystroglycan Fterm glycoprotein Dystroglycan (DG) is a cell surface glycoprotein that connects extracellular matrix molecules to the intracellular cytoskeleton, functioning as mechanical and signaling axes in various physiological events. 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. 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. 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)). 8069634 0 24 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. 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. 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. 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. 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. 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. 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. 31471319 8 28 gly nonglycosylated 1262:1276 arg1 nonglycosylated ZNT1 nonglycosylated ZNT1 PUBTATOR ZNT1 7779 ZNT1 is N-glycosylated on Asn299 in the extracellular loop between transmembrane domains V and VI, and this appears to be involved in the regulation of ZNT1 stability, as nonglycosylated ZNT1 is more stable. 31471319 8 24 gly N-glycosylated 1099:1112 arg2 Asn299 ZNT1 Asn299 ZNT1 7779 Asn299 ZNT1 is N-glycosylated on Asn299 in the extracellular loop between transmembrane domains V and VI, and this appears to be involved in the regulation of ZNT1 stability, as nonglycosylated ZNT1 is more stable. 31471319 8 24 gly N-glycosylated 1099:1112 arg1 ZNT1 ZNT1 Asn299 PUBTATOR ZNT1 7779 Asn299 ZNT1 is N-glycosylated on Asn299 in the extracellular loop between transmembrane domains V and VI, and this appears to be involved in the regulation of ZNT1 stability, as nonglycosylated ZNT1 is more stable. 31471319 8 24 gly N-glycosylated 1099:1112 arg1 ZNT1 ZNT1 Asn299 PUBTATOR ZNT1 7779 Asn299 ZNT1 is N-glycosylated on Asn299 in the extracellular loop between transmembrane domains V and VI, and this appears to be involved in the regulation of ZNT1 stability, as nonglycosylated ZNT1 is more stable. 19855092 7 18 gly desialylated 1146:1157 arg1 desialylated adiponectin desialylated adiponectin PUBTATOR adiponectin 9370 Activity of desialylated adiponectin was comparable to control adiponectin in L6 myotubes and acute assays in adiponectin(-/-) mice. 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. 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. 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. 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. 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. 18405659 7 74 gly deglycosylated 1235:1248 arg1 the deglycosylated protein the deglycosylated protein Fterm protein Transport function and molecular size were unchanged when the double mutant was hemagglutinin (HA) tagged at either the NH(2) or COOH terminus and probed with an anti-HA antibody excluding degradation of the deglycosylated protein. 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. 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. 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. 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). 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. 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. 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. 11406581 2 10 gly asparagine-linked 382:398 arg1 the asparagine-linked glycan asparagine the asparagine-linked glycan asparagine In this report we show that S.pyogenes has the ability to hydrolyze the chitobiose core of the asparagine-linked glycan on immuno globulin G (IgG) when bacteria are grown in the presence of human plasma. 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. 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). 18764929 4 74 gly glycosylated 795:806 arg1 the full-length and glycosylated beta-DG the full-length and glycosylated beta-DG Cterm DG 1605 In this study, we identify a functional nuclear localization signal within beta-DG and show that, in addition to associating with alpha-DG at the cell surface, the full-length and glycosylated beta-DG autonomously traffics to the cytoplasm and nucleoplasm in a process that occurs independent of alpha-DG ligand binding. 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). 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. 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. 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. 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. 3202829 6 15 gly Glycosylation 772:784 arg2 Asn-88 Asn-88 ribonuclease Asn-88 Glycosylation at Asn-88 has not been observed previously in mammalian secretory RNases. 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. 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. 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. 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. 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. 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. 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. 21763278 6 20 gly carbohydrates 669:681 arg1 pro-BNP BNP carbohydrates PUBTATOR BNP 4879 Glycosidases and glycosylation inhibitors were used to examine carbohydrates on pro-BNP. 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. 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). 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). 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. 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 PCI sites, Asn-230, Asn-243, and Asn-319 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 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 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 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 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 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 83 gly N-glycosylation 1035:1049 arg2 Asn-230 PCI sites, Asn-230, Asn-243, and Asn-319 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 83 gly N-glycosylation 1035:1049 arg2 Asn-319 PCI sites, Asn-230, Asn-243, and Asn-319 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 83 gly N-glycosylation 1035:1049 arg2 all three potential N-glycosylation sites PCI sites, Asn-230, Asn-243, and Asn-319 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 83 gly N-glycosylation 1035:1049 arg2 Asn-319 PCI sites, Asn-230, Asn-243, and Asn-319 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 83 gly N-glycosylation 1035:1049 arg2 all three potential N-glycosylation sites PCI sites, Asn-230, Asn-243, and Asn-319 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 83 gly N-glycosylation 1035:1049 arg2 all three potential N-glycosylation sites PCI sites, Asn-230, Asn-243, and Asn-319 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. 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. 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. 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 OGER 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 human IgG3 site Asn392 IgG3 P01860 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. 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. 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. 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. 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. 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. 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. 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. 23723439 5 48 gly glycosylation 1095:1107 arg1 α-DG α-DG Cterm DG 1605 In this study, we investigated how HNK-1ST regulates the glycosylation of α-DG using deletion and mutation analyses. 27399812 2 64 gly glycopeptide 278:289 arg2 Current glycopeptide characterization Current glycopeptide characterization glycopeptide Current glycopeptide characterization relies on time-consuming manual interpretations and demands high levels of personal expertise. 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. 12878160 7 10 gly VIPL 890:893 arg1 The single N-linked glycan VIPL The single N-linked glycan PUBTATOR VIPL Q9H0V9 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. 10639192 6 4 gly attached 712:719 arg2 Asp 301 AND high-mannose chains Asn 62 and Asp 301 high-mannose chains prostatic acid phosphatase 55 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. 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. 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. 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. 10978165 6 14 gly glycosylated 659:670 arg1 glycosylated HCC-1 HCC-1 (1-74 PUBTATOR HCC-1 (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). 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. 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. 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. 27399812 8 100 gly CS-glycopeptide 1295:1309 arg2 CS-glycopeptide CS-glycopeptide CS-glycopeptide The combination of spectral clustering, oxonium ion intensity profiles, and precursor ion m/z shift distributions provided typical signatures for the initial assignment of different N-, O- and CS-glycopeptide classes and their respective glycoforms. 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%). 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). 21515415 7 68 gly glycosylation 1000:1012 arg2 the six glycosylation sites the six glycosylation sites sites Removal of N-glycosylation at any one of the six glycosylation sites resulted in a significant 35-78% decrease in PLTP activity, and a significant 29-80% decrease in PLTP specific activity compared to wild type. 19855092 10 88 gly desialylated 1724:1735 arg1 desialylated adiponectin desialylated adiponectin PUBTATOR adiponectin 11450 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. 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. 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. 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. 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. 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. 18491227 8 40 gly E-cadherin 1305:1314 arg1 N-glycans E-cadherin N-glycans OGER E-cadherin P12830 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 18070108 10 27 gly N-glycosylation 1548:1562 arg2 an unusual recognition motif motif motif Thus, flexibility within the binding epitope of BMP-6 and an unusual recognition motif, i.e. an N-glycosylation motif, possibly play an important role in type I receptor specificity of BMP-6. 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. 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. 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. 31959827 8 48 gly glycopeptides 930:942 arg2 glycopeptides glycopeptides glycopeptides Twelve variants of glycopeptides corresponding to the HR with three to six O-glycans were detected; nine glycopeptides carried up to three Gd O-glycans. 31959827 8 61 gly glycopeptides 1016:1028 arg2 nine glycopeptides nine glycopeptides glycopeptides Twelve variants of glycopeptides corresponding to the HR with three to six O-glycans were detected; nine glycopeptides carried up to three Gd O-glycans. 31959827 8 81 gly carried 1030:1036 arg1 nine glycopeptides AND up to three Gd O-glycans nine glycopeptides up to three Gd O-glycans glycopeptides Twelve variants of glycopeptides corresponding to the HR with three to six O-glycans were detected; nine glycopeptides carried up to three Gd O-glycans. 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. 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. 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. 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. 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). 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. 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. 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. 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. 1694179 0 45 gly glycosylated 22:33 arg2 asparagine 329 protein C asparagine 329 OGER protein C P02810 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. 21763278 3 31 gly glycosylation 355:367 arg1 pro-BNP pro-BNP PUBTATOR AminoAcid BNP 4879 In this study, we analyzed glycosylation and proteolytic processing of pro-BNP in cardiomyocytes. 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. 34234349 4 36 gly α1 682:683 arg1 IV 1 IV PUBTATOR 1 28881 Ziconotide is thoroughly coordinated by helices P1 and P2, which support the selectivity filter, and the extracellular loops (ECLs) in repeats II, III and IV of α1. 34234349 4 36 gly α1 682:683 arg1 repeats II, III and IV 1 repeats II, III and IV PUBTATOR 1 28881 Ziconotide is thoroughly coordinated by helices P1 and P2, which support the selectivity filter, and the extracellular loops (ECLs) in repeats II, III and IV of α1. 34234349 4 36 gly α1 682:683 arg1 II 1 II PUBTATOR 1 28881 Ziconotide is thoroughly coordinated by helices P1 and P2, which support the selectivity filter, and the extracellular loops (ECLs) in repeats II, III and IV of α1. 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. 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. 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. 21199866 4 2 gly glycosylated 534:545 arg1 endogenous ABCB6 endogenous ABCB6 PUBTATOR ABCB6 10058 In this study, we show that endogenous ABCB6 is glycosylated in multiple cell types, indicating trafficking through the endoplasmic reticulum (ER), and has only one atypical site for glycosylation (NXC) in its amino terminus. 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. 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. 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. 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. 27399812 5 76 gly glycopeptide 782:793 arg2 glycopeptide MS/MS-spectra glycopeptide MS/MS-spectra glycopeptide Here we present SweetNET: a data-oriented bioinformatics workflow for efficient analysis of hundreds of thousands of glycopeptide MS/MS-spectra. 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. 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. 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. 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. 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. 21056543 6 7 gly Thr20 1101:1105 arg1 NeuAcGalGalNAc Thr20 NeuAcGalGalNAc protein C inhibitor P05154 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 protein C inhibitor P05154 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 protein C inhibitor P05154 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 protein C inhibitor P05154 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 protein C inhibitor P05154 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. 16445295 6 43 gly unglycosylated 984:997 arg1 an unglycosylated variant an unglycosylated variant Fterm variant Asn219 was also found in an unglycosylated variant. 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. 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. 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. 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 factor IX Ser-61 a tetrasaccharide O-fucosidically factor IX P00740 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. 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. 16445295 7 61 gly attached 1108:1115 arg1 Asn22 AND the glycan Asn22 the glycan thrombin-activatable fibrinolysis inhibitor 1361 Asn22 Four of the glycans, Asn51, Asn63, Asn86, and Asn219 displayed microheterogeneity, while the glycan attached to Asn22 appeared to be homogeneous. 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. 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. 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. 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). 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. 8069634 13 62 gly lectin 2232:2237 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. 21515415 5 12 gly N-glycosylation 711:725 arg2 each N-glycosylation site each N-glycosylation site site The size of the carbohydrate at each N-glycosylation site ranged from 3.14 to 4.2kDa. 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. 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. 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. 10531415 0 46 gly glycosylation 9:21 arg1 dopamine receptors D1, dopamine receptors PUBTATOR D1, dopamine receptors 25802 N-linked glycosylation is required for plasma membrane localization of D5, but not D1, dopamine receptors in transfected mammalian cells. 9342320 2 68 gly glycosylated 388:399 arg1 glycosylated human IFN-beta glycosylated human IFN-beta PUBTATOR IFN-beta 3440 To achieve a better understanding of the structural basis for the different activities of alpha and beta IFNs, we have determined the crystal structure of glycosylated human IFN-beta at 2.2-A resolution by molecular replacement. 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). 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. 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. 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. 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. 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. 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. 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). 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. 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. 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. 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. 8626443 1 1 gly unglycosylated 338:351 arg1 enzymatically active ACET proteins enzymatically active ACET proteins Fterm proteins For facilitating crystallization and structural studies of the testicular isozyme of angiotensin-converting enzyme (ACE,), we attempted the production of enzymatically active ACET proteins which are unglycosylated or underglycosylated. 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. 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. 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. 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. 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. 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. 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. 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. 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 -L-iduronidase 3425 Asn372 Unexpectedly, the N-glycan attached to Asn372 interacts with iduronate analogs in the active site and is required for enzymatic activity. 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. 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. 17018531 5 36 gly utilized 952:959 arg2 Asn-116 Asn-116 NPC2 10577 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 NPC2 10577 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. 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. 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. 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. 27399812 7 21 gly glycopeptide 1046:1057 arg2 the glycopeptide MS/MS data the glycopeptide MS/MS data glycopeptide Molecular networking was performed to organize the glycopeptide MS/MS data based on spectral similarities. 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. 35294879 3 30 gly attached 567:574 arg2 the enzyme substrate-binding domain AND a chondroitin/dermatan sulfate glycosaminoglycan (GAG) chain the enzyme substrate-binding domain a chondroitin/dermatan sulfate glycosaminoglycan (GAG) chain domain Here we show that human Sulf-2 (HSulf-2) harbors a chondroitin/dermatan sulfate glycosaminoglycan (GAG) chain, attached to the enzyme substrate-binding domain. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 28060820 4 38 gly N- 916:917 arg1 sequon sequon sequon N- and O-glycosylation were dispensable for signaling of the IL-6R, but proteolysis was orchestrated by an N- and O-glycosylated sequon near the cleavage site and an N-glycan exosite in domain D1. 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. 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. 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). 17395589 0 38 gly O-fucosylation 0:13 arg1 ADAMTS13 secretion ADAMTS13 secretion PUBTATOR ADAMTS13 11093 O-fucosylation is required for ADAMTS13 secretion. 2498325 7 85 gly glycosylation 1122:1134 arg1 apoE apoE PUBTATOR apoE P02649 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. 19508227 0 14 gly Glycosylation 0:12 arg1 tetraspanin Tspan-1 Tspan-1 sites OGER Tspan-1 O60635 sites Glycosylation of tetraspanin Tspan-1 at four distinct sites promotes its transition through the endoplasmic reticulum. 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. 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. 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. 21712440 5 22 gly glycosylated 1253:1264 arg2 Tyr10 Tyr10 amyloid precursor protein P05067 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 19004833 8 26 gly N-glycosylation 1278:1292 arg1 enzyme activity enzyme activity Fterm enzyme In addition, we show that proper N-glycosylation of DS-epimerase 1 is required for enzyme activity. 19004833 8 26 gly N-glycosylation 1278:1292 arg1 DS-epimerase 1 DS-epimerase 1 OGER DS-epimerase 1 Q9UL01 In addition, we show that proper N-glycosylation of DS-epimerase 1 is required for enzyme activity. 1451807 1 0 gly O-glycosylation 65:79 arg2 Thr7 Thr7 tumor necrosis factor beta 7124 Thr7 Variable O-glycosylation at Thr7, proteolytic processing, and allelic variation. 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. 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. 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 DNase X cDNAs 1774 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. 11406581 5 33 gly glycan 781:786 arg1 IgG IgG glycan Cterm IgG EndoS is required for the activity on IgG, as an isogenic EndoS mutant could not hydrolyze the glycan on IgG. 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. 1451807 3 11 gly N-glycosylated 377:390 arg2 Asn62 Asn62 tumor necrosis factor beta 7124 Asn62 All components are N-glycosylated at Asn62; N-glycosylation does not contribute to heterogeneity. 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. 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. 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. 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 PUBTATOR MD-2 23643 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. 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. 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. 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. 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. 12888562 8 43 gly glycosylated 1500:1511 arg1 the Cys399 the Cys399 NTPDase2 954 Cys399 Neither the Cys399 nor Asn443 mutants were fully glycosylated, and both were retained in the endoplasmic reticulum. 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. 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. 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. 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. 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. 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. 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 PUBTATOR NPC2 10577 One form of the disease is caused by a deficiency in NPC2, a soluble lysosomal glycoprotein that binds cholesterol. 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. 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. 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. 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. 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. 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. 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). 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. 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. 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. 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. 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). 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. 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. 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. 22160680 1 7 gly attached 175:182 arg2 a maltosaccharide chain AND Tyr195 Tyr195 a maltosaccharide chain glycogenin P46976 Tyr195 Glycogenin initiates the synthesis of a maltosaccharide chain covalently attached to itself on Tyr195 via a stepwise glucosylation reaction, priming glycogen synthesis. 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). 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. 18930737 6 41 gly N-glycosylation 858:872 arg2 Asn77 Asn77 ZAG 563 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. 1517205 0 16 gly linked 55:60 arg1 serine 61 AND a tetrasaccharide Human factor IX serine 61 a tetrasaccharide factor IX P00740 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. 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. 18405659 5 11 gly glycosylation 791:803 arg2 two canonical glycosylation sites two canonical glycosylation sites sites Substitution of asparagine residues of two canonical glycosylation sites to glutamine, individually, yielded a ~47 kDa protein; substitution of both sites gave a smaller (~35 kDa) protein. 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. 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. 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. 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. 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. 11080501 7 65 gly glycosylated 1479:1490 arg1 Asn175 Asn175 GA733-2 P16422 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 GA733-2 P16422 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 GA733-2 P16422 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 GA733-2 P16422 Asn88 Of the three potential N-linked glycosylation sites, Asn175 was not glycosylated, whereas Asn88 was completely glycosylated, and Asn51 was partially glycosylated. 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. 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. 12122212 7 38 gly glycosylation 1154:1166 arg1 CD21 CD21 Cterm 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. 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. 35835865 1 2 gly glycoproteins 300:312 arg1 the Rhesus glycoproteins the Rhesus glycoproteins Fterm glycoproteins The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. 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. 2498325 11 66 gly sialylated 1689:1698 arg1 multiply sialylated apoE multiply sialylated apoE PUBTATOR apoE P02649 The transfected wild-type cells secreted multiply sialylated apoE. 18070108 8 70 gly N-glycosylation 1220:1234 arg1 the wrist epitope epitope epitope Further studies investigating the interaction of BMP-6 with different ectodomains of type I receptors revealed that N-glycosylation at Asn73 of BMP-6 in the wrist epitope is crucial for recognition by the activin receptor type I. 18070108 8 70 gly N-glycosylation 1220:1234 arg2 Asn73 BMP-6 Asn73 BMP-6 654 Asn73 Further studies investigating the interaction of BMP-6 with different ectodomains of type I receptors revealed that N-glycosylation at Asn73 of BMP-6 in the wrist epitope is crucial for recognition by the activin receptor type I. 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. 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. 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. 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. 31959827 6 26 gly O-glycopeptide 747:760 arg2 the HR O-glycopeptide profiles the HR O-glycopeptide profiles O-glycopeptide We combined an automated quantitative analysis of the HR O-glycopeptide profiles with sequential deglycosylation to remove all but Gd O-glycans from the HR. 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). 20826823 3 63 gly glycosylation 527:539 arg1 the protein the protein Fterm protein Structural studies of ACE have been fraught with severe difficulties because of surface glycosylation of the protein. 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 l-selectin 6402 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 l-selectin 6402 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 l-selectin 6402 N196, N410, and N428 We determined that glycans are added at three of four potential N-linked glycosylation sites: N196, N410, and N428. 31959827 12 44 gly O-glycoforms 1521:1532 arg1 pathogenic IgA1 HR O-glycoforms pathogenic IgA1 HR O-glycoforms PUBTATOR IgA1 P01876 The new workflow for quantitative profiling of IgA1 HR O-glycoforms with site-specific resolution will enable identification of pathogenic IgA1 HR O-glycoforms in IgAN. 31959827 12 45 gly O-glycoforms 1429:1440 arg1 IgA1 HR O-glycoforms IgA1 HR O-glycoforms PUBTATOR IgA1 P01876 The new workflow for quantitative profiling of IgA1 HR O-glycoforms with site-specific resolution will enable identification of pathogenic IgA1 HR O-glycoforms in IgAN. 26274980 2 17 gly α2,3-sialylated 946:960 arg1 α2,3-sialylated complex N-glycans α2,3-sialylated complex N-glycans The fully occupied Asn71 carried unconventional N-glycosylation consisting of truncated chitobiose core (GlcNAcβ: 55.2%; Fucα1,6GlcNAcβ: 22.7%), paucimannosidic N-glycans (Manβ1,4GlcNAcβ1,4GlcNAcβ: 10.6%; Manβ1,4GlcNAcβ1,4(Fucα1,6)GlcNAcβ: 7.9%; Manα1,6Manβ1,4GlcNAcβ1,4GlcNAcβ: 3.7%, trace level of Manα1,6Manβ1,4GlcNAcβ1,4(Fucα1,6)GlcNAcβ), and trace levels of monoantennary α2,6- and α2,3-sialylated complex N-glycans. 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). 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. 9030779 4 58 gly used 628:631 arg2 these sites these sites sites Evidence is presented that five of these sites are used. 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. 16679516 0 86 gly Ser-2730 55:62 arg1 A single chondroitin 6-sulfate oligosaccharide unit thyroglobulin Ser-2730 A single chondroitin 6-sulfate oligosaccharide unit thyroglobulin 7038 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. 12889478 1 32 gly L-selectin 333:342 arg1 several carbohydrate-modified ligands L-selectin several carbohydrate-modified ligands PUBTATOR L-selectin 6402 During lymphocyte homing to secondary lymphoid organs and instances of inflammatory trafficking, the rolling of leukocytes on vascular endothelium is mediated by transient interactions between L-selectin on leukocytes and several carbohydrate-modified ligands on the endothelium. 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. 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. 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. 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. 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. 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). 20823119 6 81 gly glycoforms 824:833 arg1 the HR glycopeptides the HR glycopeptides glycopeptides To address this problem, we analyzed all glycoforms of the HR glycopeptides of a Gal-deficient IgA1 myeloma protein, mimicking the aberrant IgA1 in patients with IgAN, by use of a combination of IgA-specific proteases + trypsin and AI-ECD Fourier transform ion cyclotron resonance (FT-ICR) tandem mass spectrometry (MS/MS). 20823119 6 68 gly glycopeptides 845:857 arg2 the HR glycopeptides glycopeptides a Gal-deficient IgA1 myeloma protein glycopeptides To address this problem, we analyzed all glycoforms of the HR glycopeptides of a Gal-deficient IgA1 myeloma protein, mimicking the aberrant IgA1 in patients with IgAN, by use of a combination of IgA-specific proteases + trypsin and AI-ECD Fourier transform ion cyclotron resonance (FT-ICR) tandem mass spectrometry (MS/MS). 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. 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. 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. 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. 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. 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. 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. 8172892 3 62 gly contained 487:495 arg1 AP beta AND galactosamine AP beta galactosamine PUBTATOR AP beta 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. 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. 27033522 3 19 gly glycosylation 483:495 arg2 potential glycosylation sites potential glycosylation sites sites To determine the functional differences among PEBP1-4 and the underlying mechanism for their actions, we performed a sequence alignment and found that PEBP4 contains a signal peptide and potential glycosylation sites, whereas PEBP1-3 are intracellular proteins. 26274980 1 26 gly macro-heterogeneity 506:524 arg1 nCG nCG Cterm nCG 1511 To facilitate such investigations, we here use complementary LC-MS/MS-based N-glycan, N-glycopeptide, and intact glycoprotein profiling to accurately establish the micro- and macro-heterogeneity of nCG from healthy individuals. 26274980 1 53 gly glycoprotein 444:455 arg1 complementary LC-MS/MS-based N-glycan, N-glycopeptide, and intact glycoprotein profiling complementary LC-MS/MS-based N-glycan, N-glycopeptide, and intact glycoprotein profiling To facilitate such investigations, we here use complementary LC-MS/MS-based N-glycan, N-glycopeptide, and intact glycoprotein profiling to accurately establish the micro- and macro-heterogeneity of nCG from healthy individuals. 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. 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. 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. 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. 1517205 7 84 gly linked 1565:1570 arg1 Ser-61 AND a tetrasaccharide Ser-61 a tetrasaccharide factor IX P00740 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. 35273390 0 27 gly glycoprotein 39:50 arg1 human glycoprotein 2 human glycoprotein 2 PUBTATOR glycoprotein 2 2813 Structure of the decoy module of human glycoprotein 2 and uromodulin and its interaction with bacterial adhesin FimH. 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. 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 CAP37 566 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. 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. 18491227 0 34 gly Unglycosylation 0:14 arg2 Asn-633 Asn-633 E-cadherin 999 Asn-633 Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD. 2013294 6 17 gly Asn77 623:627 arg1 A single N-glycosidic carbohydrate moiety Asn77 A single N-glycosidic carbohydrate moiety Secretory actin-binding protein 5304 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 Secretory actin-binding protein 5304 Asn77 A single N-glycosidic carbohydrate moiety is located at Asn77. 16040958 7 13 gly Asn 1499:1501 arg1 the N-linked carbohydrate Asn(3) the N-linked carbohydrate C1INH P05155 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. 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. 8069634 3 44 gly fucosylated 480:490 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. 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. 8626443 2 63 gly unglycosylated 462:475 arg1 an unglycosylated but inactive protein an unglycosylated but inactive protein Fterm protein Expression in Escherichia coli of the rabbit ACET cDNA resulted in the synthesis of an unglycosylated but inactive protein. 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. 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. 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. 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. 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. 20823119 0 83 gly IgA1 23:26 arg1 O-glycans IgA1 O-glycans PUBTATOR IgA1 P01876 Clustered O-glycans of IgA1: defining macro- and microheterogeneity by use of electron capture/transfer dissociation. 8489250 1 0 gly glycoprotein 235:246 arg1 recombinant human differentiation-stimulating factor recombinant human differentiation-stimulating factor OGER differentiation-stimulating factor P15018 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. 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. 31310764 1 24 gly glycoprotein 103:114 arg1 The mucin 2 glycoprotein The mucin 2 glycoprotein PUBTATOR mucin 2 glycoprotein Q02817 The mucin 2 glycoprotein assembles into a complex hydrogel that protects intestinal epithelia and houses the gut microbiome. 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 Tn glycophorin A P02724 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 Tn glycophorin A P02724 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 Tn glycophorin A P02724 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 Tn glycophorin A P02724 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. 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)). 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. 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. 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. 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. 16895906 2 10 gly sialylated 286:295 arg1 sialylated glycans sialylated glycans The CD33-related siglecs show complex recognition patterns for sialylated glycans. 21515415 2 54 gly N-glycosylation 262:276 arg2 six potential N-glycosylation sites six potential N-glycosylation sites sites It has six potential N-glycosylation sites. 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. 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. 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. 2361960 5 1 gly glycosylated 822:833 arg1 Thr-3 Thr-3 and Asn-28 interleukin 5 3567 Thr-3 and Asn-28 In addition, we concluded that Thr-3 and Asn-28 were glycosylated. 1694179 12 37 gly glycosylated 1694:1705 arg2 this site protein C site OGER protein C P02810 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. 19467646 9 51 gly glycosylated 1169:1180 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. 35377815 4 20 gly glycoproteins 583:595 arg1 the polymeric glycoproteins the polymeric glycoproteins Fterm glycoproteins VWF evolved from gel-forming mucins, the polymeric glycoproteins that coat and protect exposed epithelia. 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. 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. 31959827 3 25 gly glycoforms 392:401 arg1 IgA1 glycoforms IgA1 glycoforms PUBTATOR IgA1 P01876 IgA1 glycoforms with some galactose-deficient (Gd) HR O-glycans play a key role in IgAN pathogenesis. 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. 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. 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. 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. 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. 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. 8069634 5 19 gly glycopeptide 942:953 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 46 gly monoglycosylated 865:880 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). 20837471 7 53 gly glycosylation 1211:1223 arg1 Thr(226) ANGPTL3 Thr(226) ANGPTL3 Q9Y5C1 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 ANGPTL3 Thr(226) GalNAc-T2 glycosylation ANGPTL3 Q9Y5C1 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. 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. 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. 20823119 2 4 gly region 268:273 arg1 galactose (Gal)-deficient hinge region (HR) O-glycans galactose (Gal)-deficient hinge region (HR) O-glycans Aberrantly glycosylated IgA1, with galactose (Gal)-deficient hinge region (HR) O-glycans, plays a pivotal role in the pathogenesis of the disease. 20823119 2 60 gly IgA1 225:228 arg1 galactose (Gal)-deficient hinge region (HR) O-glycans IgA1 galactose (Gal)-deficient hinge region (HR) O-glycans PUBTATOR IgA1 P01876 Aberrantly glycosylated IgA1, with galactose (Gal)-deficient hinge region (HR) O-glycans, plays a pivotal role in the pathogenesis of the disease. 20823119 2 65 gly glycosylated 212:223 arg1 Aberrantly glycosylated IgA1 Aberrantly glycosylated IgA1 PUBTATOR IgA1 P01876 Aberrantly glycosylated IgA1, with galactose (Gal)-deficient hinge region (HR) O-glycans, plays a pivotal role in the pathogenesis of the disease. 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. 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. 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. 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). 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. 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. 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. 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 Apolipoprotein E Thr194 the carbohydrate moiety Apolipoprotein E 348 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. 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. 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. 7681597 3 10 gly glycopeptides 491:503 arg2 The glycopeptides The glycopeptides glycopeptides The glycopeptides thus obtained were treated with sialidase and beta-galactosidase. 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. 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. 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. 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. 18703501 8 44 gly glycosylation 1520:1532 arg2 Thr(78) Thr(78) CA IX 768 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. 15378069 2 48 gly legs 281:284 arg1 the ectodomain the ectodomain the ectodomain Site ectodomain Integrin alpha and beta subunits form a head and two long legs in the ectodomain and span the membrane. 1451807 4 20 gly O-glycosylated 495:508 arg2 Thr7 Thr7 tumor necrosis factor beta 7124 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. 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. 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. 2498325 9 15 gly N-glycosylated 1435:1448 arg2 Asn194 apoE Asn194 PUBTATOR apoE P02649 Asn194 Studies with tunicamycin indicated that this apoE was N-glycosylated at Asn194. 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. 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. 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. 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. 21606496 4 7 gly glycosylation 543:555 arg1 2B4 2B4 OGER 2B4 Q9BZW8 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. 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. 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. 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. 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. 21056543 1 2 gly glycoprotein 129:140 arg1 Protein C inhibitor Protein C inhibitor OGER Protein C inhibitor P05154 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. 20823119 10 53 gly O-glycosylation 1777:1791 arg2 clustered sites clustered sites sites Furthermore, this work offers generally applicable principles for the analysis of clustered sites of O-glycosylation. 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, IX the unique trisaccharide structure PUBTATOR factors VII, IX 2155 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. 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. 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. 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. 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. 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. 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. 21606496 2 56 gly glycosylated 276:287 arg1 2B4 2B4 OGER 2B4 Q9BZW8 Here we show that 2B4 is heavily and differentially glycosylated in primary human NK cells and NK cell lines. 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. 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. 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 ZIP14 N102 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. 18508581 6 17 gly glycosylation 804:816 arg2 asparagine198 asparagine198 EpCAM 4072 asparagine198 We show that glycosylation at asparagine198 is crucial for protein stability. 3353370 7 45 gly repeats 1490:1496 arg1 the alpha chain alpha chain repeats PUBTATOR alpha chain 2217 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. 3353370 7 58 gly repeats 1439:1445 arg1 the alpha chain alpha chain repeats PUBTATOR alpha chain 2217 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. 12889478 0 5 gly L-selectin 57:66 arg1 Endoglycan L-selectin Endoglycan PUBTATOR L-selectin 6402 Endoglycan, a member of the CD34 family, functions as an L-selectin ligand through modification with tyrosine sulfation and sialyl Lewis x. 19855092 0 33 gly adiponectin 28:38 arg1 Sialic acid modification adiponectin Sialic acid modification PUBTATOR adiponectin 9370 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 9370 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 structure of PR3 5657 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. 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. 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. 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. 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. 15750791 3 4 gly glycosylated 422:433 arg1 Edg-1/S1P1 Edg-1/S1P1 PUBTATOR Edg-1 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. 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 apoE Thr(194) the most complex glycan 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. 8626443 4 9 gly N-glycosylation 749:763 arg2 the potential N-glycosylation sites the potential N-glycosylation sites sites Several ACET variants carrying mutations in one or more of the potential N-glycosylation sites were used to examine the role of glycosylation at specific sites on ACET synthesis, transport to the cell surface, cleavage processing, and enzyme activity. 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. 2668275 12 14 gly contain 1566:1572 arg1 STS AND mannose 6-phosphate residues STS mannose 6-phosphate residues OGER STS P08842 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. 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. 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. 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. 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. 27033522 9 2 gly epitope 1300:1306 arg1 a C-terminal epitope tag a C-terminal epitope tag Although overexpression of N-terminal tagged PEBP4 resulted in an inhibition of ERK activation by EGF, that with a C-terminal epitope tag did not have such an effect. 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. 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. 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. 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. 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. 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. 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. 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. 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. 21763278 0 43 gly Glycosylation 0:12 arg1 pro-B-type natriuretic peptide pro-B-type natriuretic peptide peptide Glycosylation and processing of pro-B-type natriuretic peptide in cardiomyocytes. 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. 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. 20826823 2 52 gly glycosylated 425:436 arg1 two domains domains domains ACE contains two domains, the N and C domains, both of which are heavily glycosylated. 28082515 5 20 gly glycosylation 862:874 arg2 the protein's seven glycosylation sites the protein's seven glycosylation sites sites ΔITILELP is a deletion that eliminates a consensus site on N66, one of the protein's seven 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. 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. 18491227 3 52 gly N-glycosylation 628:642 arg1 Asn-633 Asn-633 E-cadherin 999 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. 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. 2737288 3 17 gly glycosylated 389:400 arg1 only Asn-86 only Asn-86 pancreatic elastase 1 1990 Asn-86 The results demonstrate that only Asn-86 is glycosylated. 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). 25922362 6 45 gly desialylated 1481:1492 arg1 EGFR EGFR PUBTATOR EGFR 1956 Moreover, through western blots and mass spectrometry analysis, we found that EGFR immunoprecipitated from cells overexpressing active NEU3, unlike the receptor from mock cells and cells overexpressing inactive NEU3, is desialylated. 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. 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 Opsin 493763 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. 21763278 8 47 gly contained 840:848 arg1 recombinant pro-BNP AND O-glycans recombinant pro-BNP recombinant pro-BNP O-glycans PUBTATOR AminoAcid BNP 4879 pro We found that in HEK 293 cells, recombinant pro-BNP contained significant amounts of O-glycans with terminal oligosialic acids. 12889478 2 34 gly glycosylated 608:619 arg1 their heavily glycosylated mucin domains their heavily glycosylated mucin domains domains Most L-selectin ligands such as CD34 and podocalyxin present sulfated carbohydrate structures (6-sulfated sialyl Lewis x or 6-sulfo-sLex) as a recognition determinant within their heavily glycosylated mucin domains. 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. 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. 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. 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. 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. 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. 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. 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. 8069634 4 21 gly glycoprotein 747:758 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. 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. 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. 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. 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. 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. 8069634 11 94 gly fucosylated 1811:1821 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 11 109 gly unfucosylated 1849:1861 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. 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. 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. 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. 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. 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. 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. 10978165 10 52 gly glycosylated 1253:1264 arg1 glycosylated HCC-1 HCC-1 (1-74 PUBTATOR HCC-1 (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. 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. 21763278 2 55 gly O-glycosylation 225:239 arg2 Thr-71 Thr-71 BNP 4879 Thr-71 Recent studies identified several O-glycosylation sites, including Thr-71, on human pro-BNP but the functional significance was unclear. 21763278 2 55 gly O-glycosylation 225:239 arg2 several O-glycosylation sites several O-glycosylation sites sites Recent studies identified several O-glycosylation sites, including Thr-71, on human pro-BNP but the functional significance was unclear. 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. 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. 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. 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. 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. 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. 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. 28060820 2 16 gly occupancy 560:568 arg2 all O- and N-glycosylation sites all O- and N-glycosylation sites sites Here, we use liquid chromatography-mass spectrometry to identify an sIL-6R form in human serum that originates from proteolytic cleavage, map its cleavage site between Pro-355 and Val-356, and determine the occupancy of all O- and N-glycosylation sites of the human sIL-6R. 28060820 2 12 gly N-glycosylation 584:598 arg2 all O- and N-glycosylation sites sIL sites OGER sIL Q15468 sites Here, we use liquid chromatography-mass spectrometry to identify an sIL-6R form in human serum that originates from proteolytic cleavage, map its cleavage site between Pro-355 and Val-356, and determine the occupancy of all O- and N-glycosylation sites of the human sIL-6R. 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. 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. 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. 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. 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. 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. 21712440 7 4 gly glycosylation 1498:1510 arg1 the Aβ1-38/40/42 isoforms the Aβ1-38/40/42 isoforms Cterm Aβ1-38/40/42 isoforms 100034700 We could not detect any glycosylation of the Aβ1-38/40/42 isoforms. 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. 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. 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-. 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. 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 HCC-1 Q14498 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. 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. 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. 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. 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. 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. 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. 18227435 5 36 gly O-glycosylated 873:886 arg2 Thr10 Thr10 BMP-15 9210 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. 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. 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. 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. 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. 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. 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. 12889478 4 44 gly L-selectin 821:830 arg1 endoglycan L-selectin endoglycan PUBTATOR L-selectin 6402 We report here that endoglycan, like the two other members of this family (CD34 and podocalyxin) can function as a L-selectin ligand. 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. 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. 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 OGER CD33 glycoproteins P20138 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. 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. 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. 22750213 3 41 gly glycosylation 492:504 arg1 T T Cterm T P22303 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 P22303 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. 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. 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. 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). 17542669 10 46 gly glycoprotein 1730:1741 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. 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. 10978165 9 13 gly nonglycosylated 1128:1142 arg1 nonglycosylated HCC-1 HCC-1 (1-74 PUBTATOR HCC-1 (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 HCC-1 (1-74 PUBTATOR HCC-1 (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). 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. 11741940 8 32 gly moiety 1571:1576 arg1 Asn sFRP-1 Asn Asn SpecificSite sFRP-1 6422 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 sFRP-1 172 172 SpecificSite sFRP-1 6422 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 sFRP-1 Asn sFRP-1 6422 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. 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. 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. 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. 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. 28082515 11 21 gly glycosylation 1834:1846 arg2 its remaining glycosylation sites its remaining glycosylation sites sites We proposed that the ΔITILELP mutation causes protein misfolding, ER retention and inability to be processed in the Golgi apparatus, and we demonstrated that ΔITILELP carries high-mannose glycans on all six of its remaining glycosylation sites. 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. 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. 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. 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. 27033522 8 36 gly -glycosylation 1136:1149 arg1 the secreted PEBP4 the secreted PEBP4 PUBTATOR PEBP4 157310 Mass spectrometry detected asparagine (N)-glycosylation on the secreted PEBP4. 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. 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. 23723439 4 12 gly glycosylation 998:1010 arg1 α-DG α-DG Cterm DG 1605 We previously reported that human natural killer-1 sulfotransferase (HNK-1ST), which was originally reported as one of the enzymes responsible for HNK-1 glycoepitope, had an ability to suppress the glycosylation and the function of α-DG. 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. 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. 22997138 6 56 gly glycosylation 1011:1023 arg1 the enzyme the enzyme Fterm enzyme Using biophotonic microarray imaging we were able to confirm glycosylation of the enzyme and show that the enzyme is decorated with a variety of oligosaccharide structures. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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). 8670172 9 73 gly chain 1339:1343 arg1 Asn-18 CD59u Asn-18 Asn-18 SpecificSite CD59u P13987 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 Cterm CD59u P13987 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 CD59u Asn-18 The N-linked carbohydrate side chain CD59u P13987 Asn-18 The N-linked carbohydrate side chain of CD59u (at Asn-18) also displayed considerable heterogeneity. 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. 8626443 6 22 gly glycosylation 1172:1184 arg2 only the third glycosylation site only the third glycosylation site site In contrast, ACETg3, which had only the third glycosylation site available, was unglycosylated, enzymatically inactive and rapidly degraded. 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. 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. 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. 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. 21615908 5 2 gly glycosylated 889:900 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 2 gly glycosylated 889:900 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. 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.