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. 20505120 5 33 part_of Eph 677:679 arg1 the Eph ligand-binding domain Eph the Eph ligand-binding domain PUBTATOR Site Eph P21709 domain The structures reveal an elongated architecture with novel Eph/Eph interactions, both within and outside of the Eph ligand-binding domain, that suggest the molecular mechanism underlying Eph/ephrin clustering. 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. 2775232 4 0 part_of receptors 970:978 arg1 the conservative positions receptors the conservative positions Fterm Site receptors positions Given the extensive structural similarity among the two-chain alpha-subunits of Arg-Gly-Asp adhesion receptors and the conservative positions of cysteine residues in their amino acid sequences, the intrachain and interchain disulphide-bond pattern found here in GPIIb will most probably be conserved in all two-chain alpha-subunits of these receptors. 2775232 4 8 part_of sequences 1052:1060 arg1 the conservative positions sequences the conservative positions positions Given the extensive structural similarity among the two-chain alpha-subunits of Arg-Gly-Asp adhesion receptors and the conservative positions of cysteine residues in their amino acid sequences, the intrachain and interchain disulphide-bond pattern found here in GPIIb will most probably be conserved in all two-chain alpha-subunits of these receptors. 2775232 4 8 part_of sequences 1052:1060 arg1 the two-chain alpha-subunits subunits sequences OGER Site subunits 3674 sequences Given the extensive structural similarity among the two-chain alpha-subunits of Arg-Gly-Asp adhesion receptors and the conservative positions of cysteine residues in their amino acid sequences, the intrachain and interchain disulphide-bond pattern found here in GPIIb will most probably be conserved in all two-chain alpha-subunits of these receptors. 2775232 4 90 part_of alpha-subunits 931:944 arg1 their amino acid sequences subunits their amino acid sequences OGER Site subunits 3674 sequences Given the extensive structural similarity among the two-chain alpha-subunits of Arg-Gly-Asp adhesion receptors and the conservative positions of cysteine residues in their amino acid sequences, the intrachain and interchain disulphide-bond pattern found here in GPIIb will most probably be conserved in all two-chain alpha-subunits of these receptors. 15728350 0 6 part_of ICAM-3 90:95 arg1 the binding domains ICAM-3 the binding domains PUBTATOR Site ICAM-3 3385 domains An atomic resolution view of ICAM recognition in a complex between the binding domains of ICAM-3 and integrin alphaLbeta2. 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. 11706042 10 59 part_of TLR4 1789:1792 arg1 N-linked sites TLR4 N-linked sites PUBTATOR Site TLR4 7099 sites This suggests that the functional integrity of the LPS receptor depends both on the surface expression of at least three proteins, CD14, MD-2, and TLR4, and that N-linked sites of both MD-2 and TLR4 are essential in maintaining the functional integrity of this receptor. 11706042 10 62 part_of MD-2 1780:1783 arg1 N-linked sites MD-2 N-linked sites PUBTATOR Site MD-2 23643 sites This suggests that the functional integrity of the LPS receptor depends both on the surface expression of at least three proteins, CD14, MD-2, and TLR4, and that N-linked sites of both MD-2 and TLR4 are essential in maintaining the functional integrity of this receptor. 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. 25053408 5 26 part_of PCFT 781:784 arg1 the seven cysteine (Cys) residues PCFT the seven cysteine (Cys) residues PUBTATOR Site PCFT 113235 residues In this study we mutated the seven cysteine (Cys) residues of human PCFT to serine, creating Cys-less PCFT. 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. 9539702 0 13 part_of molecule-1 85:94 arg1 the N-terminal two domains intercellular adhesion molecule-1 the N-terminal two domains PUBTATOR Site intercellular adhesion molecule-1 3383 domains A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1. 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. 22601780 3 6 part_of contains 344:351 arg1 Del-1 AND 2 discoidin-like domains Del-1 2 discoidin-like domains 3 epidermal growth factor (EGF)-like repeats PUBTATOR Site Del-1 10085 domains Del-1 contains 3 epidermal growth factor (EGF)-like repeats and 2 discoidin-like domains. 9883900 2 53 part_of IGFBP-5 346:352 arg1 fragments IGFBP-5 fragments PUBTATOR Site IGFBP-5 3488 fragments We screened for circulating fragments of human IGFBP-5 in human hemofiltrate. 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. 23010571 1 50 part_of ADAMTS 311:316 arg1 ADAMTS ancillary domains ADAMTS ADAMTS ancillary domains PUBTATOR Site ADAMTS 11504 domains ADAMTS-like proteins are related to ADAMTS metalloproteases by their similarity to ADAMTS ancillary domains. 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. 1740433 6 83 part_of A-SAA 941:945 arg1 the corresponding region SAA the corresponding region OGER Site SAA P0DJI8 region The 112-residue mature molecule is 8 residues longer than human A-SAA; the size difference is due to the presence of an octapeptide between positions 70 and 77 that is not found in the corresponding region of human A-SAA. 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. 19467646 1 23 part_of OBJECTIVE 85:93 arg1 polypeptides |OBJECTIVE Growth| polypeptides Cterm Site |OBJECTIVE Growth| polypeptides OBJECTIVE Growth factors, including brain-derived neurotrophic factor (BDNF), are polypeptides that are involved in the maintenance, survival, and death of central and peripheral cells. 19467646 1 28 part_of Growth 95:100 arg1 polypeptides |OBJECTIVE Growth| polypeptides Cterm Site |OBJECTIVE Growth| polypeptides OBJECTIVE Growth factors, including brain-derived neurotrophic factor (BDNF), are polypeptides that are involved in the maintenance, survival, and death of central and peripheral cells. 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. 20823119 6 58 part_of HR 842:843 arg1 the HR glycopeptides HR the HR glycopeptides Cterm Site HR 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). 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. 33837739 3 51 part_of hZIP4 549:553 arg1 the extracellular domain hZIP4 the extracellular domain PUBTATOR Site hZIP4 55630 domain These mutations occur not only in the conserved transmembrane zinc transport machinery, but also in the extracellular domain (ECD) of hZIP4, which is only present in a fraction of mammalian ZIPs. 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. 20044576 3 12 part_of alpha-DG 609:616 arg1 the mucin-like domain DG, the mucin-like domain PUBTATOR Site DG, 1605 domain Using mass spectrometry- and nuclear magnetic resonance (NMR)-based structural analyses, we identified a phosphorylated O-mannosyl glycan on the mucin-like domain of recombinant alpha-DG, which was required for laminin binding. 18703501 3 16 part_of IX 548:549 arg1 the CA IX catalytic domain CA IX the CA IX catalytic domain PUBTATOR Site CA IX 768 domain The recombinant proteins consisted of either the CA IX catalytic domain only (CA form) or the extracellular domain, which included both the proteoglycan and catalytic domains (PG + CA form). 18703501 3 66 part_of CA 545:546 arg1 the CA IX catalytic domain CA IX the CA IX catalytic domain PUBTATOR Site CA IX 768 domain The recombinant proteins consisted of either the CA IX catalytic domain only (CA form) or the extracellular domain, which included both the proteoglycan and catalytic domains (PG + CA form). 21148085 8 5 part_of VEGF-D 1091:1096 arg1 N-terminally truncated VEGF-D polypeptides VEGF-D N-terminally truncated VEGF-D polypeptides PUBTATOR Site VEGF-D 2277 polypeptides Both receptor binding and functional assays of N-terminally truncated VEGF-D polypeptides indicated that the residues between the reported proteolytic cleavage sites are important for VEGF-D binding and activation of VEGFR-3, but not of VEGFR-2. 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 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. 8670172 0 111 part_of CD59 66:69 arg1 Structural composition CD59 Structural composition OGER Site CD59 P13987 position Structural composition and functional characterization of soluble CD59: heterogeneity of the oligosaccharide and glycophosphoinositol (GPI) anchor revealed by laser-desorption mass spectrometric analysis. 15044018 0 10 gly glycoprotein 87:98 arg1 a glycoprotein a glycoprotein Fterm glycoprotein The islet-specific glucose-6-phosphatase-related protein, implicated in diabetes, is a glycoprotein embedded in the endoplasmic reticulum membrane. 19122660 1 19 part_of Sortilin 99:106 arg1 the Sortilin ectodomain structure of the Sortilin the Sortilin ectodomain PUBTATOR Site structure of the Sortilin 6272 ectodomain The structure of the Sortilin ectodomain in complex with neurotensin has been determined at 2-A resolution, revealing that the C-terminal part of neurotensin binds in the tunnel of a ten-bladed beta-propeller domain. 1533657 7 9 part_of SCR2 1083:1086 arg1 identical sequences SCR2 sequences PUBTATOR Site SCR2 5937 sequences Amino acid comparison of these factor H-related proteins showed identical leader sequences, an exchange of three amino acids in SCR1, identical sequences of SCR2, and a lower degree of homology between SCR3-4 (h24 and h29) and SCR4-5 (h37 and h42). 8069634 0 31 part_of N2 72:73 arg1 the human lactotransferrin N2 fragment lactotransferrin N2 the human lactotransferrin N2 fragment OGER Site lactotransferrin N2 P02788 fragment Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety. 8069634 0 82 part_of lactotransferrin 55:70 arg1 the human lactotransferrin N2 fragment lactotransferrin N2 the human lactotransferrin N2 fragment OGER Site lactotransferrin N2 P02788 fragment Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety. 3342889 1 40 part_of L 165:165 arg1 The complete amino acid sequences cathepsin L The complete amino acid sequences PUBTATOR Site cathepsin L 1514 sequences The complete amino acid sequences of human kidney cathepsin H (EC 3.4.22.16) and human kidney cathepsin L (EC 3.4.22.15) were determined. 3342889 1 64 part_of cathepsin 111:119 arg1 The complete amino acid sequences cathepsin H The complete amino acid sequences PUBTATOR Site cathepsin H 1512 sequences The complete amino acid sequences of human kidney cathepsin H (EC 3.4.22.16) and human kidney cathepsin L (EC 3.4.22.15) were determined. 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. 1883960 4 63 part_of terminus 1094:1101 arg1 the 28- to 30-kD N- and O-glycosylated IL-6 IL-6 terminus PUBTATOR Site IL-6 3569 terminus Amino acid sequencing revealed that the major amino terminus in the fibroblast-derived 23- to 25-kD O-glycosylated IL-6 was at Ala28 whereas the major amino terminus in the 28- to 30-kD N- and O-glycosylated IL-6 was at Val30, suggesting that targeting of newly synthesized IL-6 polypeptides into the two different processing pathways in fibroblasts may be keyed to differences in the signal peptide cleavage site. 1883960 4 72 part_of IL-6 1211:1214 arg1 newly synthesized IL-6 polypeptides IL-6 newly synthesized IL-6 polypeptides PUBTATOR Site IL-6 3569 polypeptides Amino acid sequencing revealed that the major amino terminus in the fibroblast-derived 23- to 25-kD O-glycosylated IL-6 was at Ala28 whereas the major amino terminus in the 28- to 30-kD N- and O-glycosylated IL-6 was at Val30, suggesting that targeting of newly synthesized IL-6 polypeptides into the two different processing pathways in fibroblasts may be keyed to differences in the signal peptide cleavage site. 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. 1581307 4 42 part_of protein 720:726 arg1 691 residues protein 691 residues Fterm Site protein residues The final model, comprising 5321 protein atoms (691 residues), 2 Cu2+ ions, 2 (bi)carbonate ions, and 308 solvent molecules has good stereochemistry (rms deviation of bond lengths from standard values of 0.018 A) and gives a crystallographic R value of 0.196 for 43,525 reflections in the range 7.5-2.1-A resolution. 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. 3497398 4 48 part_of Additional 592:601 arg1 Additional fragments Additional Additional fragments Cterm Site Additional fragments Additional fragments were obtained by treatment of native glycocalicin with trypsin, Staphylococcus aureus V8 protease, and Serratia marcescens protease. 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). 27991905 5 4 part_of channel-like 908:919 arg1 the homologous channel-like region channel the homologous channel-like region Fterm Site channel region The TOP-domain fold is conserved among the polycystins, including the homologous channel-like region of PC1, and is the site of a cluster of ADPKD-associated missense variants. 27991905 5 16 part_of PC1 931:933 arg1 the homologous channel-like region PC1 the homologous channel-like region OGER Site PC1 P98161 region The TOP-domain fold is conserved among the polycystins, including the homologous channel-like region of PC1, and is the site of a cluster of ADPKD-associated missense variants. 10899108 4 0 part_of p40 570:572 arg1 Several charged residues p40 Several charged residues PUBTATOR Site p40 3578 residues Several charged residues from p35 and p40 intercalate to form a unique interlocking topography, shown by mutagenesis to be critical for p70 formation. 10899108 4 6 part_of p35 562:564 arg1 Several charged residues p35 Several charged residues PUBTATOR Site p35 3592 residues Several charged residues from p35 and p40 intercalate to form a unique interlocking topography, shown by mutagenesis to be critical for p70 formation. 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. 22333914 1 3 part_of conserved 239:247 arg1 a highly conserved autoproteolysis sequence d a highly conserved autoproteolysis sequence PUBTATOR Site d 23218 sequence The G protein-coupled receptor (GPCR) Proteolysis Site (GPS) of cell-adhesion GPCRs and polycystic kidney disease (PKD) proteins constitutes a highly conserved autoproteolysis sequence, but its catalytic mechanism remains unknown. 31125343 7 10 part_of site 1083:1086 arg1 HEPHL1 HEPHL1 site OGER Site HEPHL1 Q6MZM0 site The paternal mutation (c.3176T>C; p.Met1059Thr) changed a highly conserved methionine that is part of a typical type I copper binding site in HEPHL1. 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. 30069874 5 6 part_of has 781:783 arg1 only LYPD6 AND an NxI motif only LYPD6 an NxI motif PUBTATOR Site LYPD6 130574 motif Of the Ly6 protein family members, only LYPD6 has an NxI motif. 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. 16422668 5 33 part_of CH1 848:850 arg1 the CH1 domain CH1 the CH1 domain OGER Site CH1 Q9UBS9 domain The carbohydrate may act to shield part of the lateral surface of the CH1 domain and crowd the junction between the CH1 and CH2 domains, thereby limiting the segmental flexibility of the Fab arms in intact Yvo IgM, especially at low temperatures. 16422668 5 35 part_of CH1 894:896 arg1 the CH1 and CH2 domains CH1 the CH1 and CH2 domains OGER Site CH1 Q9UBS9 domains The carbohydrate may act to shield part of the lateral surface of the CH1 domain and crowd the junction between the CH1 and CH2 domains, thereby limiting the segmental flexibility of the Fab arms in intact Yvo IgM, especially at low temperatures. 16422668 5 81 part_of arms 969:972 arg1 intact Yvo IgM Yvo IgM arms Cterm Site Yvo IgM P01871 arms The carbohydrate may act to shield part of the lateral surface of the CH1 domain and crowd the junction between the CH1 and CH2 domains, thereby limiting the segmental flexibility of the Fab arms in intact Yvo IgM, especially at low temperatures. 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 Asn-633 Asn-633 In conclusion, this study revealed that N-glycosylation at Asn-633 is essential for E-cadherin expression, folding and trafficking. 18491227 9 20 gly N-glycosylation 1457:1471 arg1 E-cadherin expression E-cadherin Asn-633 PUBTATOR E-cadherin 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). 2737288 2 13 part_of containing 176:185 arg1 Two peptides AND the potential N-glycosylation sites Two peptides the potential N-glycosylation sites sites Two peptides, containing the potential N-glycosylation sites at Asn-86 and Asn-125, were isolated and analyzed by amino acid analysis, sequencing and carbohydrate component analysis. 16763549 5 25 part_of NRP1 795:798 arg1 the differential GAG composition NRP1 the differential GAG composition OGER Site NRP1 O14786 position Glycosylation increased VEGF binding in both cell types, but the differential GAG composition of NRP1 mediates opposite responsiveness to VEGF in ECs and SMCs. 25765764 6 21 part_of LRIG1-LRR-1Ig 923:935 arg1 The FLAG-tagged LRIG1-LRR-1Ig fragment FLAG-tagged LRIG1 The FLAG-tagged LRIG1-LRR-1Ig fragment PUBTATOR Site FLAG-tagged LRIG1 Q96JA1 fragment The FLAG-tagged LRIG1-LRR-1Ig fragment binds weakly to colon cancer cells regardless of the presence of EGFRs. 25765764 6 24 part_of FLAG-tagged 911:921 arg1 The FLAG-tagged LRIG1-LRR-1Ig fragment FLAG-tagged LRIG1 The FLAG-tagged LRIG1-LRR-1Ig fragment PUBTATOR Site FLAG-tagged LRIG1 Q96JA1 fragment The FLAG-tagged LRIG1-LRR-1Ig fragment binds weakly to colon cancer cells regardless of the presence of EGFRs. 29345911 6 24 part_of convertase 830:839 arg1 convertase cleavage site convertase convertase cleavage site Fterm Site convertase site To obtain more insight into the role of some of its post-translational modifications, we designed a mutant GPC3, sGPC3m, without its GPI anchor, convertase cleavage site, and glycosaminoglycan chains. 29345911 6 41 part_of GPI 818:820 arg1 convertase cleavage site GPI convertase cleavage site OGER Site GPI P06744 site To obtain more insight into the role of some of its post-translational modifications, we designed a mutant GPC3, sGPC3m, without its GPI anchor, convertase cleavage site, and glycosaminoglycan chains. 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). 21949356 9 74 part_of motif 1285:1289 arg1 the consensus sequence motif the consensus sequence sequence EGF16 of mouse Notch2, which has a diserine motif in the consensus sequence ( ), is also modified with either O-Xyl or O-glucose glycans in cells. 9153399 8 45 part_of ICAM-2 1268:1273 arg1 domains 1 and 2 ICAM-2 domains 1 and 2 PUBTATOR Site ICAM-2 3384 domains A bend between domains 1 and 2 of ICAM-2 and a tripod-like arrangement of N-linked glycans in the membrane-proximal region of domain 2 may be important for presenting the recognition surface to LFA-1. 9153399 8 57 part_of domains 1249:1255 arg1 the membrane-proximal region domains the membrane-proximal region region A bend between domains 1 and 2 of ICAM-2 and a tripod-like arrangement of N-linked glycans in the membrane-proximal region of domain 2 may be important for presenting the recognition surface to LFA-1. 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 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. 17005555 4 47 part_of Lingo-1 712:718 arg1 the ligand-binding ectodomain Lingo-1 the ligand-binding ectodomain PUBTATOR Site Lingo-1 84894 ectodomain Here we report on the crystal structure of the ligand-binding ectodomain of human Lingo-1 and show it has a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. 10022822 0 51 part_of Ii 49:50 arg1 MHC class II-associated p41 Ii fragment Ii MHC class II-associated p41 Ii fragment Cterm Site Ii fragment Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. 10022822 0 56 part_of p41 45:47 arg1 MHC class II-associated p41 Ii fragment p41 MHC class II-associated p41 Ii fragment Cterm Site p41 fragment Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. 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. 25765764 5 0 part_of LRIG1 739:743 arg1 the LRIG1 domains LRIG1 the LRIG1 domains PUBTATOR Site LRIG1 Q96JA1 domains We could not detect any binding of the LRIG1 domains or the LRIG1-LRR-1Ig fragment to the EGF receptor (EGFR), either in solution using biosensor analysis or when the EGFR was expressed on the cell surface. 25765764 5 44 part_of LRIG1-LRR-1Ig 760:772 arg1 the LRIG1-LRR-1Ig fragment LRIG1 the LRIG1-LRR-1Ig fragment PUBTATOR Site LRIG1 Q96JA1 fragment We could not detect any binding of the LRIG1 domains or the LRIG1-LRR-1Ig fragment to the EGF receptor (EGFR), either in solution using biosensor analysis or when the EGFR was expressed on the cell surface. 8636209 10 29 part_of gamma 1284:1288 arg1 the entire CY domain CD3 gamma the entire CY domain PUBTATOR Site CD3 gamma 917 domain Deletion of the entire CY domain of CD3 gamma did not prevent assembly and expression of the TCR. 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. 3542989 5 0 part_of cholinesterase 490:503 arg1 The sequence cholinesterase The sequence PUBTATOR Site cholinesterase 534616 sequence The sequence of human serum cholinesterase is 53.8% identical with the sequence of acetylcholinesterase from Torpedo californica and 28% identical with the carboxyl-terminal portion of bovine thyroglobulin. 3542989 5 2 part_of acetylcholinesterase 545:564 arg1 the sequence acetylcholinesterase the sequence OGER Site acetylcholinesterase P22303 sequence The sequence of human serum cholinesterase is 53.8% identical with the sequence of acetylcholinesterase from Torpedo californica and 28% identical with the carboxyl-terminal portion of bovine thyroglobulin. 2498325 1 25 gly threonine 77:85 arg1 The carbohydrate attachment site threonine 194 The carbohydrate attachment site threonine 194 The carbohydrate attachment site is threonine 194. 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. 1709161 11 9 part_of IGFBPs 1334:1339 arg1 10 repetitive domains IGFBPs 10 repetitive domains PUBTATOR Site IGFBPs 3487 domains A most intriguing homology exists between the COOH-terminal quarter of the five IGFBPs, 10 repetitive domains of human thyroglobulin, a gastrointestinal tumor-associated antigen, and the invariant chain of the class II histocompatibility antigen. 1709161 11 50 part_of thyroglobulin 1373:1385 arg1 10 repetitive domains thyroglobulin 10 repetitive domains OGER Site thyroglobulin P01266 domains A most intriguing homology exists between the COOH-terminal quarter of the five IGFBPs, 10 repetitive domains of human thyroglobulin, a gastrointestinal tumor-associated antigen, and the invariant chain of the class II histocompatibility antigen. 21569239 7 19 part_of F-spondin 939:947 arg1 F-spondin FS domain F-spondin F-spondin FS domain PUBTATOR Site F-spondin 10418 domain The unique feature of F-spondin FS domain is the presence of three disulfide bonds associated with the N- and C-termini of the domain and a highly conserved N-linked glycosylation site. 21138434 6 44 part_of subunit 1439:1445 arg1 utilised N-glycosylation sites h5-HT3B subunit utilised N-glycosylation sites Cterm Site h5-HT3B subunit 9177 sites The present study has identified utilised N-glycosylation sites of the h5-HT3B subunit and demonstrated that they promote subunit expression in the cell membrane; a prerequisite for 5-HT(3) receptor function. 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 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. 32616672 3 15 part_of epitopes 596:603 arg1 the regularly spaced arms epitopes the regularly spaced arms arms N-glycosylation mapping and biophysical assays revealed that uromodulin acts as a multivalent ligand for the bacterial type 1 pilus adhesin, presenting specific epitopes on the regularly spaced arms. 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). 22451694 6 46 part_of fibronectin 1084:1094 arg1 the auxiliary synergy site fibronectin the auxiliary synergy site PUBTATOR Site fibronectin 2335 site The structure also enabled the precise prediction of the acceptor residue for the auxiliary synergy site of fibronectin on the α5 subunit, which was experimentally confirmed by mutagenesis and kinetic binding assays. 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. 21148085 2 7 part_of proteins 311:318 arg1 C-terminal propeptides proteins C-terminal propeptides Fterm Site proteins propeptides VEGFR-3 ligands VEGF-C and VEGF-D are produced as precursor proteins with long N- and C-terminal propeptides and show enhanced VEGFR-2 and VEGFR-3 binding on proteolytic removal of the propeptides. 22547800 4 20 gly channel 791:797 arg1 a leucine-rich repeat (LRR)-containing membrane protein BK channel a leucine-rich repeat (LRR)-containing membrane protein OGER BK channel We recently identified a leucine-rich repeat (LRR)-containing membrane protein, LRRC26, as a BK channel auxiliary subunit, which causes an unprecedented large negative shift (∼140 mV) in voltage dependence of channel activation. 22547800 4 23 gly BK 788:789 arg1 a leucine-rich repeat (LRR)-containing membrane protein BK channel a leucine-rich repeat (LRR)-containing membrane protein OGER BK channel We recently identified a leucine-rich repeat (LRR)-containing membrane protein, LRRC26, as a BK channel auxiliary subunit, which causes an unprecedented large negative shift (∼140 mV) in voltage dependence of channel activation. 22547800 4 55 gly leucine-rich 720:731 arg1 LRR leucine LRR leucine We recently identified a leucine-rich repeat (LRR)-containing membrane protein, LRRC26, as a BK channel auxiliary subunit, which causes an unprecedented large negative shift (∼140 mV) in voltage dependence of channel activation. 22547800 4 55 gly leucine-rich 720:731 arg1 a leucine-rich repeat leucine a leucine-rich repeat leucine We recently identified a leucine-rich repeat (LRR)-containing membrane protein, LRRC26, as a BK channel auxiliary subunit, which causes an unprecedented large negative shift (∼140 mV) in voltage dependence of channel activation. 11502179 0 19 part_of receptor 118:125 arg1 a soluble bioactive amino-terminal extracellular domain thyrotropin receptor a soluble bioactive amino-terminal extracellular domain PUBTATOR Site thyrotropin receptor 7253 domain Purification and characterization of a soluble bioactive amino-terminal extracellular domain of the human thyrotropin receptor. 18491227 7 44 part_of E-cadherin 1216:1225 arg1 cytoplasmic domain E-cadherin cytoplasmic domain OGER Site E-cadherin P12830 domain It was observed that the ration of M4 E-cadherin binding to calnexin was significantly increased compared with that of other variants, suggesting that it was a misfolded protein, though cytoplasmic domain of M4 E-cadherin could associate with beta-catenin. 3123586 5 9 part_of apoC-III 726:733 arg1 the mutant apoC-III polypeptide apoC-III the mutant apoC-III polypeptide PUBTATOR Site apoC-III 345 polypeptide As a result of this amino acid replacement, the mutant apoC-III polypeptide is not glycosylated. 8089145 2 34 part_of contains 408:415 arg1 The larger subunit AND Gly-X-Ser-X-Gly The larger subunit Gly-X-Ser-X-Gly OGER Site subunit 313 Gly-X-Ser-X-Gly The larger subunit contains an amino acid sequence (Gly-X-Ser-X-Gly) that is found at the active sites of many lipases, while the smaller subunit has amino acid sequence similarity to saposins (sphingolipid activator proteins), cofactors for sphingolipid glycohydrolases. 8089145 2 34 part_of contains 408:415 arg1 The larger subunit AND an amino acid sequence The larger subunit an amino acid sequence OGER Site subunit 313 sequence The larger subunit contains an amino acid sequence (Gly-X-Ser-X-Gly) that is found at the active sites of many lipases, while the smaller subunit has amino acid sequence similarity to saposins (sphingolipid activator proteins), cofactors for sphingolipid glycohydrolases. 17924658 10 80 gly glycosylation 1926:1938 arg2 the seven N-linked glycosylation sites the seven N-linked glycosylation sites sites Incubation of the enzyme with a mechanism-based inhibitor, enzymatic digest, and mass spectrometric analysis provided the first unambiguous identification of Thr381 as the active site nucleophile of human gamma-glutamyltranspeptidase, and confirmed four of the seven N-linked glycosylation sites. 1709161 6 53 part_of BP-4 724:727 arg1 The prepeptide sequences BP-4 and -5 The prepeptide sequences PUBTATOR Site BP-4 and -5 Q13323 sequences The prepeptide sequences of BP-4 and -5 contain 27 and 21, the mature proteins 213 and 237 amino acids, respectively (Mr = 22,610 and 25,980). 1709161 6 94 part_of -5 733:734 arg1 The prepeptide sequences BP-4 and -5 The prepeptide sequences PUBTATOR Site BP-4 and -5 Q13323 sequences The prepeptide sequences of BP-4 and -5 contain 27 and 21, the mature proteins 213 and 237 amino acids, respectively (Mr = 22,610 and 25,980). 30069874 6 0 part_of LYPD6 822:826 arg1 the LYPD6 NxI motif LYPD6 the LYPD6 NxI motif PUBTATOR Site LYPD6 130574 motif Since mutations in the LYPD6 NxI motif abolish or severely reduce interaction with LRP6, our results indicate its key role in the interaction of LYPD6 with LRP6. 19561611 5 27 part_of Ca2+ 820:823 arg1 the Hh Zn2+ and Ca2+ binding sites--functions Ca2 the Hh Zn2+ and Ca2+ binding sites--functions OGER Site Ca2 P00918 sites--functions The interaction determinants, confirmed by biophysical studies and mutagenesis, reveal previously uncharacterized and distinct functions for the Hh Zn2+ and Ca2+ binding sites--functions that may be common to all vertebrate Hh proteins. 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. 3877053 10 16 part_of XII 1477:1479 arg1 The carboxyl-terminal region factor XII The carboxyl-terminal region PUBTATOR Site factor XII P00748 region The carboxyl-terminal region of factor XII shares considerable amino acid sequence homology with other serine proteases including trypsin and many clotting factors. 11325591 3 34 part_of subsite 810:816 arg1 rat granzyme B. CONCLUSIONS The above differences account for the variation in substrate specificity among granzyme B, other serine proteases and the caspases, and enable the design of specific inhibitors that can probe the physiological functions of these proteins and the disease states with which they are associated granzyme B subsite PUBTATOR Site granzyme B 171528 subsite The Asp-specific S1 subsite of human granzyme B is significantly larger and less charged than the corresponding Asp-specific site in the apoptosis-promoting caspases, and also larger than the corresponding subsite in rat granzyme B. CONCLUSIONS The above differences account for the variation in substrate specificity among granzyme B, other serine proteases and the caspases, and enable the design of specific inhibitors that can probe the physiological functions of these proteins and the disease states with which they are associated. 11325591 3 64 part_of B 650:650 arg1 The Asp-specific S1 subsite granzyme B The Asp-specific S1 subsite PUBTATOR Site granzyme B 3002 subsite The Asp-specific S1 subsite of human granzyme B is significantly larger and less charged than the corresponding Asp-specific site in the apoptosis-promoting caspases, and also larger than the corresponding subsite in rat granzyme B. CONCLUSIONS The above differences account for the variation in substrate specificity among granzyme B, other serine proteases and the caspases, and enable the design of specific inhibitors that can probe the physiological functions of these proteins and the disease states with which they are associated. 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. 9875849 3 28 part_of receptor 429:436 arg1 the antibody-binding domains IgE receptor the antibody-binding domains OGER Site IgE receptor P01854 domains We have solved the X-ray crystal structure of the antibody-binding domains of the human IgE receptor at 2.4 A resolution. 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. 15687489 6 6 part_of enzyme 832:837 arg1 the DUF323 domain formylglycine-generating enzyme domain PUBTATOR Site formylglycine-generating enzyme 285362 domain Both proteins belong to a large family of pro- and eukaryotic proteins containing the DUF323 domain, a formylglycine-generating enzyme domain of unknown three-dimensional structure. 15687489 6 33 part_of formylglycine-generating 807:830 arg1 the DUF323 domain formylglycine-generating enzyme domain PUBTATOR Site formylglycine-generating enzyme 285362 domain Both proteins belong to a large family of pro- and eukaryotic proteins containing the DUF323 domain, a formylglycine-generating enzyme domain of unknown three-dimensional structure. 15687489 6 9 part_of containing 775:784 arg1 pro- and eukaryotic proteins AND the DUF323 domain proteins domain Fterm Site proteins domain Both proteins belong to a large family of pro- and eukaryotic proteins containing the DUF323 domain, a formylglycine-generating enzyme domain of unknown three-dimensional structure. 26274980 0 16 part_of G 188:188 arg1 Unconventional Asn71-Glycosylation Neutrophil cathepsin G Unconventional Asn71-Glycosylation PUBTATOR AminoAcid Neutrophil cathepsin G 1511 Asn71 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. 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. 11080501 0 30 part_of GA733-2 118:124 arg1 N-glycosylation sites GA733-2 N-glycosylation sites OGER Site GA733-2 P16422 sites Determination of disulfide bond assignments and N-glycosylation sites of the human gastrointestinal carcinoma antigen GA733-2 (CO17-1A, EGP, KS1-4, KSA, and Ep-CAM). 15378069 4 6 part_of beta3 582:586 arg1 the beta3 I domain beta3 I the beta3 I domain PUBTATOR Site beta3 I 10312 domain Allostery in the beta3 I domain alters three metal binding sites, associated loops and alpha1- and alpha7-helices. 15378069 4 51 part_of I 588:588 arg1 the beta3 I domain beta3 I the beta3 I domain PUBTATOR Site beta3 I 10312 domain Allostery in the beta3 I domain alters three metal binding sites, associated loops and alpha1- and alpha7-helices. 11741940 11 110 part_of protein 1932:1938 arg1 Phe protein Asp(41) and Phe(50) Fterm SpecificSite protein Asp(41) and Phe(50) The predominant N terminus was Ser(31), although minor amounts of the protein with Asp(41) and Phe(50) as the N termini were observed. 11741940 11 110 part_of protein 1932:1938 arg1 Asp(41) protein Asp(41) and Phe(50) Fterm SpecificSite protein Asp(41) and Phe(50) The predominant N terminus was Ser(31), although minor amounts of the protein with Asp(41) and Phe(50) as the N termini were observed. 11741940 11 110 part_of protein 1932:1938 arg1 Asp(41) protein Asp(41) and Phe(50) Fterm SpecificSite protein Asp(41) and Phe(50) The predominant N terminus was Ser(31), although minor amounts of the protein with Asp(41) and Phe(50) as the N termini were observed. 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. 35294879 3 12 part_of enzyme 583:588 arg1 the enzyme substrate-binding domain enzyme the enzyme substrate-binding domain Fterm Site enzyme 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. 15173186 6 20 part_of contain 889:895 arg1 all Toll-like receptors AND N-linked glycosylation consensus sites all Toll-like receptors N-linked glycosylation consensus sites Fterm Site receptors sites Additionally, all Toll-like receptors contain N-linked glycosylation consensus sites, and Toll-like receptor 4 requires glycosylation for function. 12527193 7 65 part_of has 992:994 arg1 CRB3 AND a very short extracellular domain CRB3 a very short extracellular domain PUBTATOR Site CRB3 92359 domain In contrast to Drosophila Crumbs and CRB1, CRB3 has a very short extracellular domain but like these proteins it has a conserved intracellular domain that allows it to complex with Pals1 and PATJ. 1544894 5 18 gly fucosylated 943:953 arg2 Thr-90 factor XII Thr-90 OGER factor XII P00748 Thr-90 We found that factor XII is fully fucosylated at Thr-90. 7477400 3 24 part_of CLIP 477:480 arg1 the CLIP fragment CLIP the CLIP fragment PUBTATOR Site CLIP 6249 fragment The structure shows that the CLIP fragment binds to DR3 in a way almost identical to that in which antigenic peptides bind class II histocompatibility glycoproteins. 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. 17372356 4 14 part_of enzyme 882:887 arg1 the S1' site enzyme the S1' site Fterm Site enzyme site In addition, models were constructed for binding of the inhibitors willardiine, homoibotenate, L-2-amino-4-phosphonobutanoic acid and L-serine-O-sulfate to the S1' site of the enzyme. 20696930 4 48 part_of HER2 528:531 arg1 the HER2 extracellular domain HER2 the HER2 extracellular domain PUBTATOR Site HER2 2064 domain Here we determined the structure of Zher2 in solution and the crystal structure of Zher2 in complex with the HER2 extracellular domain. 10531415 6 104 part_of site 890:893 arg1 the D1 receptor receptor site Fterm Site receptor site Mutation of a comparable site in the D1 receptor at position N5 had no effect on the delivery of the D1 receptor to the cell surface. 18930737 6 45 part_of PIP 831:833 arg1 The amino acid sequence PIP The amino acid sequence PUBTATOR Site PIP 5304 sequence The amino acid sequence of PIP contains one potential N-glycosylation site at Asn77, and the same is found glycosylated with four sugar residues. 18930737 6 66 part_of contains 835:842 arg1 The amino acid sequence AND one potential N-glycosylation site The amino acid sequence one potential N-glycosylation site site The amino acid sequence of PIP contains one potential N-glycosylation site at Asn77, and the same is found glycosylated with four sugar residues. 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. 4055801 7 14 part_of protein 894:900 arg1 two single-chain polypeptide fragments protein two single-chain polypeptide fragments Fterm Site protein fragments C9 can be cleaved by alpha-thrombin into two single-chain polypeptide fragments: C9a (Mr = 28,000) and C9b (Mr = 38,000), which are the amino- and carboxyl-terminal segments of the protein, respectively. 4055801 7 30 part_of polypeptide 771:781 arg1 two single-chain polypeptide fragments polypeptide two single-chain polypeptide fragments Fterm Site polypeptide fragments C9 can be cleaved by alpha-thrombin into two single-chain polypeptide fragments: C9a (Mr = 28,000) and C9b (Mr = 38,000), which are the amino- and carboxyl-terminal segments of the protein, respectively. 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. 16362042 5 42 part_of Gas6 782:785 arg1 the major and minor Gas6 binding sites Gas6 the major and minor Gas6 binding sites PUBTATOR Site Gas6 2621 sites Structure-based mutagenesis, protein binding assays and receptor activation experiments demonstrate that both the major and minor Gas6 binding sites are required for productive transmembrane signalling. 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. 16456079 3 6 part_of receptor 497:504 arg1 The three domains receptor The three domains Fterm Site receptor domains The three domains of urokinase receptor form a concave shape with a central cone-shaped cavity where the urokinase fragment inserts. 30639100 2 31 part_of receptor 308:315 arg1 a single-domain antibody fragment receptor a single-domain antibody fragment Fterm Site receptor fragment By stabilizing the receptor with a single-domain antibody fragment ("nanobody") discovered using a synthetic yeast-displayed library, we determined the crystal structure of active-state human AT1R bound to an AngII analog with partial agonist activity. 22451694 5 51 part_of α5β1 940:943 arg1 the top face α5 the top face Cterm Site α5 face The RGD-binding pocket is situated at the center of a trenchlike exposed surface on the top face of α5β1 devoid of glycosylation sites. 2243102 6 15 part_of Asn-34 953:958 arg1 lamp-1 lamp-1 Asn-34 PUBTATOR SpecificSite lamp-1 3916 Asn-34, Asn-93 Amino acid analysis and sequencing demonstrated that polylactosaminoglycans were located at Asn-34, Asn-93 and/or Asn-102, and Asn-195 and/or Asn-200 in lamp-1, and at Asn-4 and/or Asn-10, and Asn-279 in lamp-2. 12788922 0 39 part_of Ca2+-binding 23:34 arg1 the Ca2+-binding interaction domain structure of the Ca2 the Ca2+-binding interaction domain OGER Site structure of the Ca2 P00918 domain X-ray structure of the Ca2+-binding interaction domain of C1s. 12788922 0 66 part_of C1s 58:60 arg1 the Ca2+-binding interaction domain C1s the Ca2+-binding interaction domain PUBTATOR Site C1s 716 domain X-ray structure of the Ca2+-binding interaction domain of C1s. 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. 16476442 3 41 part_of angiotensin 484:494 arg1 the two hemoregulatory peptides angiotensin I the two hemoregulatory peptides PUBTATOR Site angiotensin I 183 peptides Both domains are capable of cleaving the two hemoregulatory peptides angiotensin I and bradykinin, but differ in their affinities for a range of other substrates and inhibitors. 22106953 3 26 part_of enzyme 537:542 arg1 the active site enzyme the active site Fterm Site enzyme site On the basis of residual electron density, a lysine residue has been modeled in the active site of the enzyme; thus, the structure corresponds to an enzyme-product complex. 28661582 3 13 part_of tyrosinase-like 543:557 arg1 the typical tyrosinase-like subdomain tyrosinase the typical tyrosinase-like subdomain OGER Site tyrosinase P14679 subdomain Herein we show that the typical tyrosinase-like subdomain of TYRP1 contains two zinc ions in the active site instead of copper ions as found in tyrosinases, which explains why TYRP1 does not exhibit tyrosinase redox activity. 28661582 3 35 part_of TYRP1 572:576 arg1 the typical tyrosinase-like subdomain TYRP1 the typical tyrosinase-like subdomain OGER Site TYRP1 P17643 subdomain Herein we show that the typical tyrosinase-like subdomain of TYRP1 contains two zinc ions in the active site instead of copper ions as found in tyrosinases, which explains why TYRP1 does not exhibit tyrosinase redox activity. 1544894 1 7 part_of EGF 406:408 arg1 their EGF domains EGF their EGF domains PUBTATOR Site EGF 1950 domains We and others have demonstrated that tissue plasminogen activator (t-PA) and prourokinase are modified by the attachment of fucose to equivalent threonine residues within their EGF domains. 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. 8172892 1 105 part_of IX 234:235 arg1 the activation peptide coagulation factor IX the activation peptide OGER Site coagulation factor IX P00740 peptide O-Linked oligosaccharide chains were identified in the activation peptide (AP) of human blood coagulation factor IX. 9690478 5 37 part_of IGF-IR 694:699 arg1 the first three domains IGF-IR the first three domains PUBTATOR Site IGF-IR 3480 domains We now present the structure of the first three domains of IGF-IR (L1-Cys-rich-L2) determined to 2.6 A resolution. 17005555 0 42 part_of Lingo-1 21:27 arg1 the Lingo-1 ectodomain structure of the Lingo-1 the Lingo-1 ectodomain PUBTATOR Site structure of the Lingo-1 84894 ectodomain The structure of the Lingo-1 ectodomain, a module implicated in central nervous system repair inhibition. 10756055 5 67 part_of Env-coreceptor 1132:1145 arg1 the Env-coreceptor contact sites Env the Env-coreceptor contact sites PUBTATOR Site Env 100616444 sites They also suggest a possible explanation for the various observations of restricted virus entry in some cell types and further our understanding of the framework of elements that represent the Env-coreceptor contact sites. 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. 22848655 12 40 part_of MSPβ 1807:1810 arg1 the putative MSPβ binding site MSPβ the putative MSPβ binding site PUBTATOR Site MSPβ 4477 site Mapping of the dimer interface using the RON homology to Met, MSP homology to Hepatocyte Growth Factor (HGF), and the structure of the Met/HGF complex shows the dimer interface overlapping with the putative MSPβ binding site. 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. 7683678 8 16 part_of 24p3 1236:1239 arg1 the deduced sequences 24p3 the deduced sequences Cterm Site 24p3 sequences The sequence did not match any known human protein, but showed a high degree of similarity with the deduced sequences of rat alpha 2-microglobulin-related protein and the mouse protein 24p3. 7683678 8 17 part_of protein 1206:1212 arg1 the deduced sequences alpha 2-microglobulin-related protein the deduced sequences PUBTATOR Site alpha 2-microglobulin-related protein 170496 sequences The sequence did not match any known human protein, but showed a high degree of similarity with the deduced sequences of rat alpha 2-microglobulin-related protein and the mouse protein 24p3. 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. 19141282 2 23 part_of IL-7Ralpha 257:266 arg1 the IL-7Ralpha ectodomain IL-7Ralpha the IL-7Ralpha ectodomain PUBTATOR Site IL-7Ralpha 3575 ectodomain We report that the IL-7Ralpha ectodomain uses glycosylation to modulate its binding constants to IL-7, unlike the other receptors in the gamma(c) family. 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. 32815518 4 49 part_of ZPC 711:713 arg1 The immunoglobulin-like ZPN and ZPC subdomains ZPC The immunoglobulin-like ZPN and ZPC subdomains PUBTATOR Site ZPC 7784 subdomains The immunoglobulin-like ZPN and ZPC subdomains of each monomer are separated by a long linker that interacts with the preceding ZPC and following ZPN subdomains by β-sheet complementation. 9539703 0 69 part_of ICAM-1 57:62 arg1 the two amino-terminal domains ICAM-1 the two amino-terminal domains PUBTATOR Site ICAM-1 3383 domains The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand. 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. 8089145 1 44 part_of Acyloxyacyl 131:141 arg1 a precursor polypeptide Acyloxyacyl hydrolase a precursor polypeptide PUBTATOR Site Acyloxyacyl hydrolase 313 polypeptide Acyloxyacyl hydrolase, a leukocyte enzyme that acts on bacterial lipopolysaccharides (LPSs) and many glycerolipids, is synthesized as a precursor polypeptide that undergoes internal disulfide linkage before being proteolytically processed into two subunits. 22576872 7 13 gly Tyr10 1315:1319 arg1 O-glycans Tyr10 O-glycans Tyr10 Further, sialylated core 1 like O-glycans at Tyr10, recently discovered in human Aβ (a previously unknown glycosylation type), were identified also in cat cerebrospinal fluid (CSF). 22576872 7 51 gly sialylated 1279:1288 arg1 sialylated core 1 sialylated core 1 Further, sialylated core 1 like O-glycans at Tyr10, recently discovered in human Aβ (a previously unknown glycosylation type), were identified also in cat cerebrospinal fluid (CSF). 16046623 4 19 part_of channel 703:709 arg1 Leu469 channel Leu469 Fterm AminoAcid channel Leu469 Firstly, Leu469 at the substrate channel may play a key role in controlling the substrate entry; depending on its conformation, it either blocks or gives access to the active site. 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. 27768895 3 52 part_of PKD2 454:457 arg1 The PKD2 voltage-sensor domain PKD2 The PKD2 voltage-sensor domain PUBTATOR Site PKD2 Q13563 domain The PKD2 voltage-sensor domain retains two of four gating charges commonly found in those of voltage-gated ion channels. 21712440 5 33 part_of Aβ1-X 1152:1156 arg1 27 glycopeptides Aβ1 27 glycopeptides PUBTATOR Site Aβ1 100034700 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. 22932899 4 21 part_of hAPN 601:604 arg1 the dimeric ectodomain hAPN the dimeric ectodomain PUBTATOR Site hAPN 290 ectodomain Reported here are the high resolution x-ray crystal structures of the dimeric ectodomain of hAPN and its complexes with angiotensin IV and the peptidomimetic inhibitors, amastatin and bestatin. 11081633 4 0 part_of PSGL-1 761:766 arg1 the N-terminal domain PSGL-1 the N-terminal domain PUBTATOR Site PSGL-1 6404 domain We also present the crystal structure of P-selectin LE co-complexed with the N-terminal domain of human PSGL-1 modified by both tyrosine sulfation and SLe(X). 3497398 5 64 part_of alpha-chain 889:899 arg1 the alpha-chain polypeptide alpha-chain the alpha-chain polypeptide PUBTATOR Site alpha-chain 2217 polypeptide Analysis of all these fragments provided data that allowed determination of the continuous sequence corresponding to approximately half of the alpha-chain polypeptide. 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. 11866528 10 8 part_of BST-1 1483:1487 arg1 the sequences BST-1 the sequences PUBTATOR Site BST-1 683 sequences The three key residues are invariant among the sequences of BST-1, CD38, and Aplysia cyclase, and hence this substrate recognition mode and catalytic scheme appear to be common in the cyclase family. 11866528 10 58 part_of CD38 1490:1493 arg1 the sequences CD38 the sequences OGER Site CD38 P28907 sequences The three key residues are invariant among the sequences of BST-1, CD38, and Aplysia cyclase, and hence this substrate recognition mode and catalytic scheme appear to be common in the cyclase family. 11866528 10 75 part_of cyclase 1508:1514 arg1 the sequences cyclase the sequences Fterm Site cyclase sequences The three key residues are invariant among the sequences of BST-1, CD38, and Aplysia cyclase, and hence this substrate recognition mode and catalytic scheme appear to be common in the cyclase family. 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. 25561468 7 66 part_of N-terminal 1002:1011 arg1 the N-terminal fragment N-terminal the N-terminal fragment Cterm Site N-terminal fragment Removal of the N-terminal fragment (ICA512-NTF) preceding ME ICA512 allows an ICA512-ΔNTF G553D mutant to exit the endoplasmic reticulum, and ICA512-ΔNTF is constitutively delivered to the cell surface. 22451694 2 15 part_of α5β1 269:272 arg1 the α5β1 integrin headpiece fragment structure of the α5 the α5β1 integrin headpiece fragment Cterm Site structure of the α5 fragment A crystal structure of the α5β1 integrin headpiece fragment bound by an allosteric inhibitory antibody was determined at a 2.9-Å resolution both in the absence and presence of a ligand peptide containing the Arg-Gly-Asp (RGD) sequence. 22451694 2 14 part_of containing 435:444 arg1 a ligand peptide AND the Arg-Gly-Asp (RGD) sequence a ligand peptide the Arg-Gly-Asp (RGD) sequence sequence A crystal structure of the α5β1 integrin headpiece fragment bound by an allosteric inhibitory antibody was determined at a 2.9-Å resolution both in the absence and presence of a ligand peptide containing the Arg-Gly-Asp (RGD) sequence. 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. 27238017 4 39 part_of contains 593:600 arg1 NPC1 AND three distinct lumenal domains NPC1 three distinct lumenal domains PUBTATOR Site NPC1 4864 domains NPC1 contains 13 transmembrane segments (TMs) and three distinct lumenal domains A (also designated NTD), C, and I. TMs 2-13 exhibit a typical resistance-nodulation-cell division fold, among which TMs 3-7 constitute the sterol-sensing domain conserved in several proteins involved in cholesterol metabolism and signaling. 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. 19855092 5 49 part_of adiponectin 851:861 arg1 adiponectin multimer composition adiponectin adiponectin multimer composition PUBTATOR Site adiponectin 9370 position Enzymatic removal of sialic acid or its underlying O-linked sugars did not affect adiponectin multimer composition. 21712440 8 21 part_of peptides 1610:1617 arg1 CSF CSF peptides OGER Site CSF peptides We observed an increase of up to 2.5 times of Tyr10 glycosylated Aβ peptides in CSF in six AD patients compared to seven non-AD patients. 21712440 8 31 part_of Aβ 1607:1608 arg1 Tyr10 glycosylated Aβ peptides Aβ Tyr10 glycosylated Aβ peptides PUBTATOR Site Aβ 351 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. 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. 15965977 4 15 part_of rhomboid 716:723 arg1 polypeptide sequence rhomboid polypeptide sequence PUBTATOR Site rhomboid 38168 sequence We present the cDNA cloning and polypeptide sequence of an atypically long human rhomboid, which, based on the absence of critical residues for serine protease activity, is not predicted to act as a serine protease. 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. 30069874 3 14 part_of LYPD6 440:444 arg1 the LYPD6 extracellular LU domain structure of the LYPD6 the LYPD6 extracellular LU domain PUBTATOR Site structure of the LYPD6 130574 domain We report here the 1.25 Å resolution structure of the LYPD6 extracellular LU domain and map its interaction with LRP6 by mutagenesis and surface plasmon resonance. 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. 10644446 4 28 part_of 460-amino-acid 444:457 arg1 a 460-amino-acid polypeptide 460-amino-acid a 460-amino-acid polypeptide Cterm Site 460-amino-acid polypeptide Human ANGPTL3 is a 460-amino-acid polypeptide with the characteristic structure of angiopoietins: a signal peptide, an extended helical domain predicted to form dimeric or trimeric coiled-coils, a short linker peptide, and a globular fibrinogen homology domain (FHD). 10644446 4 43 part_of Human 425:429 arg1 a 460-amino-acid polypeptide Human ANGPTL3 a 460-amino-acid polypeptide PUBTATOR Site Human ANGPTL3 27329 polypeptide Human ANGPTL3 is a 460-amino-acid polypeptide with the characteristic structure of angiopoietins: a signal peptide, an extended helical domain predicted to form dimeric or trimeric coiled-coils, a short linker peptide, and a globular fibrinogen homology domain (FHD). 19683538 6 24 gly glycoprotein 1071:1082 arg1 the alpha-NAGAL glycoprotein the alpha-NAGAL glycoprotein Cterm alpha-NAGAL glycoprotein 4668 To better understand how individual defects in the alpha-NAGAL glycoprotein lead to Schindler disease, we analyzed the effect of disease-causing mutations on the three-dimensional structure. 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. 29490423 6 40 part_of CD19 996:999 arg1 the extracellular domain CD19 the extracellular domain OGER Site CD19 P15391 domain Rather than a tandem of c-type immunoglobulin folds predicted from the amino acid sequence, the extracellular domain of CD19 exhibits an elongated β-sandwich formed by two immunoglobulin folds by swapping their C-terminal halves. 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. 22688517 5 67 part_of LOX-1 995:999 arg1 their corresponding attached site LOX-1 their corresponding attached site PUBTATOR Site LOX-1 4973 site Here, an approach using nonspecific protease (Pronase E) digestion followed by MALDI-QIT-TOF MS and multistage MS (MS(3)) analysis is explored to obtain site-specific N-glycosylation information of recombinant human LOX-1, in combination with glycan structure confirmation through characterizing released glycans using tandem MS. The results reveal that N-glycans structures as well as their corresponding attached site of LOX-1 can be identified simultaneously by direct MS analysis of glycopeptides from non-specific protease digestion. 23139753 4 32 part_of WFDC 468:471 arg1 two WFDC domains WFDC two WFDC domains Cterm Site WFDC domains HE-4 is a 124 amino acid long polypeptide with two WFDC domains. 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. 6371807 7 31 part_of contains 1182:1189 arg1 four regions AND three or four tryptophan residues four regions three or four tryptophan residues tryptophan residues Clusters of tryptophan residues occur in four regions, each of which contains three or four tryptophan residues separated by 0-12 other residues. 3840370 13 44 gly 2-glycoprotein 1955:1968 arg1 the non-complement beta 2-glycoprotein I the non-complement beta 2-glycoprotein I OGER beta 2-glycoprotein I P02749 These regions in C4b-binding protein are homologous with the three internal-homology regions that have been reported to be present within the Ba region of the complement enzyme factor B and also to the internal-homology regions found in the non-complement beta 2-glycoprotein I. 26902720 0 22 gly glycoprotein 80:91 arg1 a serum glycoprotein afamin/α-albumin a serum glycoprotein afamin/α-albumin Fterm glycoprotein Active and water-soluble form of lipidated Wnt protein is maintained by a serum glycoprotein afamin/α-albumin. 1544894 7 2 part_of VII 1141:1143 arg1 the first EGF domain factor VII the first EGF domain OGER Site factor VII P08709 domain It has been recently reported that the first EGF domain of human factor VII has O-linked fucose at the equivalent position (Ser-60) (Bjoern, S., Foster, D. C., Thim, L., Wiberg, F. C., Christensen, M., Komiyama, Y., Pedersen, A. H., and Kisiel, W. (1991) J. Biol. 1544894 7 27 part_of EGF 1114:1116 arg1 the first EGF domain EGF the first EGF domain PUBTATOR Site EGF 1950 domain It has been recently reported that the first EGF domain of human factor VII has O-linked fucose at the equivalent position (Ser-60) (Bjoern, S., Foster, D. C., Thim, L., Wiberg, F. C., Christensen, M., Komiyama, Y., Pedersen, A. H., and Kisiel, W. (1991) J. Biol. 16422668 4 32 part_of CH1 715:717 arg1 the CH1 domain CH1 the CH1 domain OGER Site CH1 Q9UBS9 domain The three-dimensional structure of the branched N-linked oligosaccharide associated with the CH1 domain (first constant domain of heavy chain) is reported. 3886654 4 24 part_of XII 554:556 arg1 the complete amino acid sequence factor XII the complete amino acid sequence OGER Site factor XII P00748 sequence 258, 10924-10933), the complete amino acid sequence of human factor XII has been established. 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. 15809306 6 22 part_of enzyme 1029:1034 arg1 the active site enzyme the active site Fterm Site enzyme site Comparison of the crystal structures of FAPalpha and DPPIV revealed one major difference in the vicinity of the Glu motif (Glu(203)-Glu(204) for FAPalpha; Glu(205)-Glu(206) for DPPIV) within the active site of the enzyme. 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 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) Asn(309) Asn(309) Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures. 18703501 7 48 gly glycosylation 1295:1307 arg2 a unique N-linked glycosylation site a unique N-linked glycosylation site site Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures. 18703501 7 69 gly bears 1330:1334 arg1 Asn(309) AND high mannose-type glycan structures Asn(309) high mannose-type glycan structures Asn(309) Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures. 18703501 7 69 gly bears 1330:1334 arg1 a unique N-linked glycosylation site AND high mannose-type glycan structures a unique N-linked glycosylation site high mannose-type glycan structures site Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures. 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. 16107205 2 62 part_of have 465:468 arg1 all the mammalian DNase X proteins AND an N-terminal signal peptide all the mammalian DNase X proteins an N-terminal signal peptide PUBTATOR Site DNase X proteins 515176 peptide A sequence comparison reveals some conserved characteristics: all the mammalian DNase X proteins have an N-terminal signal peptide, a potential N-linked glycosylation site and a C-terminal hydrophobic domain. 16107205 2 62 part_of have 465:468 arg1 all the mammalian DNase X proteins AND a C-terminal hydrophobic domain all the mammalian DNase X proteins a C-terminal hydrophobic domain PUBTATOR Site DNase X proteins 515176 domain A sequence comparison reveals some conserved characteristics: all the mammalian DNase X proteins have an N-terminal signal peptide, a potential N-linked glycosylation site and a C-terminal hydrophobic domain. 16107205 2 62 part_of have 465:468 arg1 all the mammalian DNase X proteins AND a potential N-linked glycosylation site all the mammalian DNase X proteins a potential N-linked glycosylation site PUBTATOR Site DNase X proteins 515176 site A sequence comparison reveals some conserved characteristics: all the mammalian DNase X proteins have an N-terminal signal peptide, a potential N-linked glycosylation site and a C-terminal hydrophobic domain. 9578468 0 41 gly O-glycosylated 42:55 arg1 human eotaxin human eotaxin PUBTATOR eotaxin 6356 Delayed production of biologically active O-glycosylated forms of human eotaxin by tumor-necrosis-factor-alpha-stimulated dermal fibroblasts. 29748286 2 6 part_of TcdB 429:432 arg1 a TcdB fragment TcdB a TcdB fragment Cterm Site TcdB fragment Here, we present the crystal structure of a TcdB fragment in complex with the cysteine-rich domain of human FZD2 at 2.5-angstrom resolution, which reveals an endogenous FZD-bound fatty acid acting as a co-receptor for TcdB binding. 29748286 2 26 part_of FZD2 493:496 arg1 the cysteine-rich domain FZD2 the cysteine-rich domain PUBTATOR Site FZD2 2535 domain Here, we present the crystal structure of a TcdB fragment in complex with the cysteine-rich domain of human FZD2 at 2.5-angstrom resolution, which reveals an endogenous FZD-bound fatty acid acting as a co-receptor for TcdB binding. 26274980 3 9 part_of Ser244 1146:1151 arg1 two C-terminal truncation variants variants Ser244 Fterm AminoAcid variants Ser244 High-resolution/mass accuracy LC-MS profiling of intact nCG confirmed the Asn71-glycoprofile and identified two C-terminal truncation variants at Arg243 (57.8%) and Ser244 (42.2%), both displaying oxidation of solvent-accessible Met152. 26274980 3 14 part_of Arg243 1127:1132 arg1 two C-terminal truncation variants variants Arg243 Fterm AminoAcid variants Arg243 High-resolution/mass accuracy LC-MS profiling of intact nCG confirmed the Asn71-glycoprofile and identified two C-terminal truncation variants at Arg243 (57.8%) and Ser244 (42.2%), both displaying oxidation of solvent-accessible Met152. 15628971 5 16 part_of C4ST-1 827:832 arg1 the C-terminal region C4ST-1 the C-terminal region PUBTATOR Site C4ST-1 314694 region We found that (i) treatment of recombinant C4ST-1 with peptide N-glycosidase F caused a marked decrease in activity, (ii) production of the active form of C4ST-1 by COS-7 cells transfected with cDNA of C4ST-1 was inhibited by tunicamycin, (iii) deletion of the N-glycosylation site located at the C-terminal region of C4ST-1 abolished activity, (iv) attachment of a single N-glycan at the C-terminal region supported production of the active form of C4ST-1, but the resulting recombinant enzyme was much more unstable at 37 degrees C than the control recombinant protein, and (v) truncation of C-terminal region up to the N-glycosylation site at the C-terminal region resulted in total loss of activity. 15628971 5 18 part_of region 1170:1175 arg1 the N-glycosylation site region the N-glycosylation site site We found that (i) treatment of recombinant C4ST-1 with peptide N-glycosidase F caused a marked decrease in activity, (ii) production of the active form of C4ST-1 by COS-7 cells transfected with cDNA of C4ST-1 was inhibited by tunicamycin, (iii) deletion of the N-glycosylation site located at the C-terminal region of C4ST-1 abolished activity, (iv) attachment of a single N-glycan at the C-terminal region supported production of the active form of C4ST-1, but the resulting recombinant enzyme was much more unstable at 37 degrees C than the control recombinant protein, and (v) truncation of C-terminal region up to the N-glycosylation site at the C-terminal region resulted in total loss of activity. 15477100 5 20 part_of ZAG 1032:1034 arg1 the ZAG binding site ZAG the ZAG binding site PUBTATOR Site ZAG 563 site Further support for PEG binding in the ZAG groove is provided by the finding that PEG displaces a fluorophore-tagged fatty acid from the ZAG binding site. 23742080 10 47 gly N-glycosylation 1467:1481 arg1 residue N183 residue N183 residue N183 Cycloheximide treatment experiments revealed that S185 degrades faster than T185 TMEM106B, potentially due to differences in N-glycosylation at residue N183. 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. 2129367 0 58 part_of factors 100:106 arg1 the first EGF-like domain factors the first EGF-like domain Fterm Site factors domain A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z. Recently, we determined the complete amino acid sequence of bovine factor VII (Takeya, H. et al. (1988) J. Biol. 2129367 0 63 part_of residue 51:57 arg1 clotting factors factors residue Fterm AminoAcid factors serine residue A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z. Recently, we determined the complete amino acid sequence of bovine factor VII (Takeya, H. et al. (1988) J. Biol. 2129367 0 71 part_of EGF-like 72:79 arg1 the first EGF-like domain EGF the first EGF-like domain OGER Site EGF P01133 domain A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z. Recently, we determined the complete amino acid sequence of bovine factor VII (Takeya, H. et al. (1988) J. Biol. 2129367 0 77 part_of VII 208:210 arg1 the complete amino acid sequence factor VII the complete amino acid sequence PUBTATOR Site factor VII 2155 sequence A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z. Recently, we determined the complete amino acid sequence of bovine factor VII (Takeya, H. et al. (1988) J. Biol. 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. 20826823 0 49 part_of enzyme 47:52 arg1 The N domain enzyme The N domain Fterm Site enzyme domain The N domain of human angiotensin-I-converting enzyme: the role of N-glycosylation and the crystal structure in complex with an N domain-specific phosphinic inhibitor, RXP407. 6510521 2 9 part_of hemopexin 365:373 arg1 the N-terminal region hemopexin the N-terminal region PUBTATOR Site hemopexin 3263 region By sequence studies of fragments CB1-CB4 and peptides prepared by their enzyme cleavage, a continuous amino acid sequence of the N-terminal region of human hemopexin, comprising 220 amino acid residues, was determined. 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. 22660477 8 26 part_of GBR2 989:992 arg1 the GBR2 ectodomain GBR2 the GBR2 ectodomain Cterm Site GBR2 ectodomain Lastly, our structural and functional data indicate that the GBR2 ectodomain adopts a constitutively open conformation, suggesting a structural asymmetry in the active state of GABA(B) receptor that is unique to the GABAergic system. 1544894 3 62 part_of residues 646:653 arg1 protein C In protein C residues OGER Site In protein C P02810 residues In protein C, this site is 3 residues from the position of another post-translational modification, beta-hydroxylation of Asp-71. 12022871 8 4 gly glycosylated 1241:1252 arg1 Human TGH Human TGH PUBTATOR Human TGH 1066 Human TGH was glycosylated in the insect cells. 20507882 5 42 part_of Hex-O-Thr 899:907 arg1 Hex-O-Thr glycopeptides Hex Hex-O-Thr glycopeptides PUBTATOR AminoAcid Hex 3087 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. 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. 21712440 4 0 part_of APP/Aβ 868:873 arg1 37 APP/Aβ glycopeptides Aβ 37 APP/Aβ glycopeptides PUBTATOR Site Aβ 351 glycopeptides In addition to 33 unglycosylated APP/Aβ peptides, we identified 37 APP/Aβ glycopeptides with sialylated core 1 like O-glycans attached to Thr(-39, -21, -20, and -13), in a series of APP/AβX-15 glycopeptides, where X was -63, -57, -52, and -45, in relation to Asp1 of the Aβ sequence. 21712440 4 16 part_of Aβ 1072:1073 arg1 the Aβ sequence Aβ the Aβ sequence PUBTATOR Site Aβ 351 sequence In addition to 33 unglycosylated APP/Aβ peptides, we identified 37 APP/Aβ glycopeptides with sialylated core 1 like O-glycans attached to Thr(-39, -21, -20, and -13), in a series of APP/AβX-15 glycopeptides, where X was -63, -57, -52, and -45, in relation to Asp1 of the Aβ sequence. 21712440 4 43 part_of APP/Aβ 834:839 arg1 33 unglycosylated APP/Aβ peptides Aβ 33 unglycosylated APP/Aβ peptides PUBTATOR Site Aβ 351 peptides In addition to 33 unglycosylated APP/Aβ peptides, we identified 37 APP/Aβ glycopeptides with sialylated core 1 like O-glycans attached to Thr(-39, -21, -20, and -13), in a series of APP/AβX-15 glycopeptides, where X was -63, -57, -52, and -45, in relation to Asp1 of the Aβ sequence. 21712440 9 91 part_of protein 1767:1773 arg1 a Tyr residue protein a Tyr residue Fterm AminoAcid protein Tyr residue APP/Aβ sialylated O-glycans, including that of a Tyr residue, the first in a mammalian protein, may modulate APP processing, inhibiting the amyloidogenic pathway associated with AD. 25826155 0 67 part_of transcript 63:72 arg1 extracellular domain lectin-like transcript 1 extracellular domain PUBTATOR Site lectin-like transcript 1 29121 domain Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A. 25765764 1 30 part_of LRIG1-LRR-1Ig 259:271 arg1 three soluble fragments LRIG1 three soluble fragments OGER Site LRIG1 Q96JA1 fragments We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells. 25765764 1 30 part_of LRIG1-LRR-1Ig 259:271 arg1 the LRIG1-LRR-1Ig fragment LRIG1 the LRIG1-LRR-1Ig fragment OGER Site LRIG1 Q96JA1 fragment We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells. 25765764 1 42 part_of LRIG1-ECD 129:137 arg1 three soluble fragments LRIG1 three soluble fragments PUBTATOR Site LRIG1 26018 fragments We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells. 25765764 1 42 part_of LRIG1-ECD 129:137 arg1 the LRIG1-LRR-1Ig fragment LRIG1 the LRIG1-LRR-1Ig fragment PUBTATOR Site LRIG1 26018 fragment We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells. 25765764 1 42 part_of LRIG1-ECD 129:137 arg1 the LRIG1-3Ig (immunoglobulin-like) domain LRIG1 the LRIG1-3Ig (immunoglobulin-like) domain PUBTATOR Site LRIG1 26018 domain We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells. 25765764 1 47 part_of LRIG1-3Ig 211:219 arg1 three soluble fragments LRIG1 three soluble fragments PUBTATOR Site LRIG1 26018 fragments We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells. 25765764 1 47 part_of LRIG1-3Ig 211:219 arg1 the LRIG1-3Ig (immunoglobulin-like) domain LRIG1 the LRIG1-3Ig (immunoglobulin-like) domain PUBTATOR Site LRIG1 26018 domain We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells. 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. 8670172 3 11 part_of CD59 578:581 arg1 the detailed structural composition CD59 the detailed structural composition OGER Site CD59 P13987 position We have investigated the detailed structural composition of the naturally occurring soluble urinary CD59 (CD59u) using peptide mapping, anion-exchange chromatography, sequential exoglycosidase digestion and matrix-assisted laser-desorption mass spectrometry (MALDI-MS). 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. 27349982 0 4 part_of Saposin 65:71 arg1 the Saposin Domain Saposin the Saposin Domain Cterm Saposin Structure of Human Acid Sphingomyelinase Reveals the Role of the Saposin Domain in Activating Substrate Hydrolysis. 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. 18077410 6 44 part_of thrombin 1206:1213 arg1 thrombin exosite II thrombin thrombin exosite II PUBTATOR Site thrombin 2147 exosite In contrast, Ab75 bound at the backside of the cleft to a region corresponding to thrombin exosite II, which is known to interact with allosteric effector molecules. 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. 8636209 5 4 part_of gamma 673:677 arg1 the EC domain CD3 gamma the EC domain PUBTATOR Site CD3 gamma 917 domain Based on this model and on alignment studies, two potential interaction sites were predicted in the EC domain of CD3 gamma. 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) Asn(281) The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54). 11152692 11 24 gly O-glycosylation 1339:1353 arg2 Ser Ser(54) Ser(54) The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54). 11152692 11 33 gly N-glycosylation 1243:1257 arg2 Asn Asn(281) Asn(281) The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54). 11152692 11 33 gly N-glycosylation 1243:1257 arg2 Ser Ser(54) Ser(54) The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54). 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. 19119025 4 10 part_of ERp57 610:614 arg1 both ERp57 catalytic domains ERp57 both ERp57 catalytic domains OGER Site ERp57 P30101 domains The structure revealed that tapasin interacts with both ERp57 catalytic domains, accounting for the stability of the heterodimer, and provided an example of a protein disulfide isomerase family member interacting with substrate. 15696168 3 24 part_of Fab 393:395 arg1 the Fab fragment Fab the Fab fragment PUBTATOR Site Fab 2187 fragment Here we present the crystal structure of a soluble form of CD28 in complex with the Fab fragment of a mitogenic antibody. 10899108 5 40 part_of p35 715:717 arg1 A central arginine residue p35 A central arginine residue PUBTATOR AminoAcid p35 3592 arginine residue A central arginine residue from p35 projects into a deep pocket on p40, which may be an ideal target for a small molecule antagonist of IL-12 formation. 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. 22846996 5 10 part_of BTN3A 1032:1036 arg1 the BTN3A Ig-V domain BTN3A the BTN3A Ig-V domain Cterm Site BTN3A 10384 domain The 20.1 and 103.2 antibodies bind to separate epitopes on the BTN3A Ig-V domain with high affinity but likely with different valencies based on their binding orientation. 22846996 5 34 part_of epitopes 1016:1023 arg1 the BTN3A Ig-V domain epitopes the BTN3A Ig-V domain domain The 20.1 and 103.2 antibodies bind to separate epitopes on the BTN3A Ig-V domain with high affinity but likely with different valencies based on their binding orientation. 30140003 5 52 part_of GnT-V 580:584 arg1 GnT-V luminal domain GnT-V GnT-V luminal domain PUBTATOR Site GnT-V 4249 domain GnT-V luminal domain is composed of a GT-B fold and two accessary domains. 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. 11279095 3 46 part_of terminus 606:613 arg1 three cysteines terminus three cysteines cysteines The members of the ST8Sia gene family, including ST8Sia II and ST8Sia IV are unique in having three cysteines in sialylmotif L, one cysteine in sialylmotif S, and one cysteine at the COOH terminus. 11279095 3 46 part_of terminus 606:613 arg1 one cysteine cysteine cysteine The members of the ST8Sia gene family, including ST8Sia II and ST8Sia IV are unique in having three cysteines in sialylmotif L, one cysteine in sialylmotif S, and one cysteine at the COOH terminus. 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. 18703501 7 25 part_of contains 1209:1216 arg1 CA IX AND Asn(309) CA IX Asn(309) PUBTATOR SpecificSite CA IX 768 Asn(309) Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures. 18703501 7 25 part_of contains 1209:1216 arg1 CA IX AND a unique N-linked glycosylation site CA IX a unique N-linked glycosylation site PUBTATOR Site CA IX 768 site Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures. 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. 21199866 4 60 part_of has 638:640 arg1 endogenous ABCB6 AND only one atypical site endogenous ABCB6 only one atypical site PUBTATOR Site ABCB6 10058 site 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. 19276170 3 54 part_of COMP 612:615 arg1 the C-terminal domain COMP the C-terminal domain OGER Site COMP P49747 domain In this study, we determined the structure of a recombinant protein that contains the last epidermal growth factor repeat, the type 3 repeats and the C-terminal domain (CTD) of COMP to 3.15-A resolution limit by X-ray crystallography. 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. 16698036 6 23 part_of alpha-subunit 1016:1028 arg1 Only the alpha-subunit active site subunit Only the alpha-subunit active site OGER Site subunit P06865 site Only the alpha-subunit active site can hydrolyze GM2 gangliosides due to a flexible loop structure that is removed post-translationally from beta, and to the presence of alphaAsn423 and alphaArg424. 10899108 3 26 part_of found 506:510 arg1 the p40 subunit AND an N-terminal immunoglobulin-like domain the p40 subunit an N-terminal immunoglobulin-like domain PUBTATOR Site p40 subunit 3578 domain They also include the first description of an N-terminal immunoglobulin-like domain, found on the p40 subunit. 16169851 7 16 part_of BTLA 893:896 arg1 the extracellular domain BTLA the extracellular domain PUBTATOR Site BTLA 151888 domain Light scattering analysis demonstrates that the extracellular domain of BTLA is monomeric and that BTLA and HVEM form a 1:1 complex. 22387313 0 42 gly N-glycosylation 0:14 arg1 the mammalian dipeptidyl aminopeptidase-like protein 10 the mammalian dipeptidyl aminopeptidase-like protein 10 PUBTATOR dipeptidyl aminopeptidase-like protein 10 57628 N-glycosylation of the mammalian dipeptidyl aminopeptidase-like protein 10 (DPP10) regulates trafficking and interaction with Kv4 channels. 22387313 0 42 gly N-glycosylation 0:14 arg1 DPP10 DPP10 PUBTATOR DPP10 57628 N-glycosylation of the mammalian dipeptidyl aminopeptidase-like protein 10 (DPP10) regulates trafficking and interaction with Kv4 channels. 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. 2721499 4 49 part_of precursor 689:697 arg1 The sequence precursor The sequence Fterm Site precursor sequence The sequence of the SP-40,40 precursor bears a 77% identity to a rat sulphated glycoprotein-2 (SGP-2) which is the major secreted product of Sertoli cells. 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. 1581307 8 19 part_of protein 1498:1504 arg1 the protein domains protein the protein domains Fterm Site protein domains The protein structure is the same as for the diferric protein, Fe2Lf, demonstrating that the closure of the protein domains over the metal is the same in each case irrespective of whether Fe3+ or Cu2+ is bound and that copper could be transported and delivered to cells equally well as iron. 9690478 0 6 part_of receptor 86:93 arg1 the first three domains receptor the first three domains Fterm Site receptor domains Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor. 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. 14718370 2 33 part_of subdomains 233:242 arg1 MUC5B MUC5B subdomains PUBTATOR AminoAcid MUC5B Q9HC84 Cys1 and Cys5 and Cys1 and Cys3 subdomains The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium. 14718370 2 33 part_of subdomains 233:242 arg1 MUC5AC MUC5AC subdomains PUBTATOR AminoAcid MUC5AC P98088 Cys1 and Cys5 and Cys1 and Cys3 subdomains The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium. 14718370 2 75 part_of Cys1 201:204 arg1 MUC5B MUC5B Cys1 PUBTATOR AminoAcid MUC5B Q9HC84 Cys1 and Cys5 and Cys1 and Cys3 subdomains The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium. 14718370 2 75 part_of Cys1 201:204 arg1 MUC5AC MUC5AC Cys1 PUBTATOR AminoAcid MUC5AC P98088 Cys1 and Cys5 and Cys1 and Cys3 subdomains The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium. 14718370 2 80 part_of Cys5 210:213 arg1 MUC5B MUC5B Cys5 PUBTATOR AminoAcid MUC5B Q9HC84 Cys1 and Cys5 and Cys1 and Cys3 subdomains The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium. 14718370 2 80 part_of Cys5 210:213 arg1 MUC5AC MUC5AC Cys5 PUBTATOR AminoAcid MUC5AC P98088 Cys1 and Cys5 and Cys1 and Cys3 subdomains The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium. 14718370 2 84 part_of Cys1 219:222 arg1 MUC5B MUC5B Cys1 PUBTATOR AminoAcid MUC5B Q9HC84 Cys1 and Cys5 and Cys1 and Cys3 subdomains The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium. 14718370 2 84 part_of Cys1 219:222 arg1 MUC5AC MUC5AC Cys1 PUBTATOR AminoAcid MUC5AC P98088 Cys1 and Cys5 and Cys1 and Cys3 subdomains The entire Cys1 and Cys5 and Cys1 and Cys3 subdomains in MUC5AC and MUC5B, respectively, each with six carboxyl terminal histidine residues, were pulse-labeled with [(35)S]cysteine/methionine, and the labeled proteins were examined in the culture medium. 22052913 7 58 part_of Fstl3 851:855 arg1 the N-terminal domain Fstl3 the N-terminal domain PUBTATOR Site Fstl3 10272 domain The structure reveals that the N-terminal domain (ND) of Fstl3 interacts uniquely with myostatin as compared with activin A, because it utilizes different surfaces on the ligand. 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 asparagine 329 asparagine 329 It is asparagine 329 that is not glycosylated in beta protein C since antibodies to a synthetic peptide based on the sequence around this amino acid react only with beta protein C. 1694179 9 28 gly glycosylated 1241:1252 arg1 asparagine 329 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. 21763278 16 72 part_of Arg-76 1646:1651 arg1 pro-BNP BNP Arg-76 PUBTATOR SpecificSite BNP 4879 Arg-76 In HEK 293 cells, furin cleaved pro-BNP at Arg-76 whereas in cardiomyocytes corin cleaved pro-BNP at multiple residues including Arg-73, Arg-76 and Lys-79. 21712440 3 97 part_of Aβ 602:603 arg1 Aβ peptides Aβ Aβ peptides PUBTATOR Site Aβ 351 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. 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 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. 9722584 0 4 part_of protein 61:67 arg1 deduced amino acid sequence protein deduced amino acid sequence Fterm Site protein sequence Cloning and deduced amino acid sequence of a novel cartilage protein (CILP) identifies a proform including a nucleotide pyrophosphohydrolase. 17711303 12 66 gly N-glycosylation 1808:1822 arg1 the hKOR the hKOR PUBTATOR hKOR 4986 Thus, N-glycosylation of the hKOR plays important roles in stability and trafficking along the biosynthesis pathway of the receptor protein as well as agonist-induced receptor regulation. 18065761 0 47 part_of thrombospondin-1 57:72 arg1 the thrombospondin-1 N-terminal domain thrombospondin-1 the thrombospondin-1 N-terminal domain PUBTATOR Site thrombospondin-1 7057 domain Heparin-induced cis- and trans-dimerization modes of the thrombospondin-1 N-terminal domain. 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. 9883900 5 2 part_of IGFBP-5 661:667 arg1 C-terminal peptides IGFBP-5 C-terminal peptides PUBTATOR Site IGFBP-5 3488 peptides C-terminal peptides of IGFBP-5 with molecular masses of 13.3 and 13.5 kDa were purified by consecutive chromatographic steps and sequenced. 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. 23010571 0 35 part_of fibrillin-1- 114:125 arg1 A disintegrin-like and metalloprotease domain fibrillin-1 A disintegrin-like and metalloprotease domain PUBTATOR Site fibrillin-1 2200 domain A disintegrin-like and metalloprotease domain containing thrombospondin type 1 motif-like 5 (ADAMTSL5) is a novel fibrillin-1-, fibrillin-2-, and heparin-binding member of the ADAMTS superfamily containing a netrin-like module. 23010571 0 46 part_of fibrillin-2- 128:139 arg1 A disintegrin-like and metalloprotease domain fibrillin-2 A disintegrin-like and metalloprotease domain PUBTATOR Site fibrillin-2 2201 domain A disintegrin-like and metalloprotease domain containing thrombospondin type 1 motif-like 5 (ADAMTSL5) is a novel fibrillin-1-, fibrillin-2-, and heparin-binding member of the ADAMTS superfamily containing a netrin-like module. 25043189 3 10 part_of CSL362 622:627 arg1 the NTD epitope CSL the NTD epitope PUBTATOR Site CSL 1444 epitope Although extensive mutational analyses of the NTD epitope of CSL362 show minor overlap with the IL-3 binding site, CSL362 only inhibits IL-3 binding to the closed conformation, indicating alternative mechanisms for blocking IL-3 signaling. 25043189 3 23 part_of IL-3 657:660 arg1 the IL-3 binding site IL-3 the IL-3 binding site PUBTATOR Site IL-3 P08700 site Although extensive mutational analyses of the NTD epitope of CSL362 show minor overlap with the IL-3 binding site, CSL362 only inhibits IL-3 binding to the closed conformation, indicating alternative mechanisms for blocking IL-3 signaling. 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. 20837471 7 60 part_of peptide 1242:1248 arg1 the RAPR(224)↓TT processing site peptide the RAPR(224)↓TT processing site site We demonstrated that GalNAc-T2 glycosylation of Thr(226) in a peptide with the RAPR(224)↓TT processing site blocks in vitro furin cleavage. 8069634 5 96 part_of N2 862:863 arg1 the N2 monoglycosylated fragment N2 the N2 monoglycosylated fragment Cterm Site N2 fragment RESULTS We have determined the crystal structures of Lathyrus ochrus isolectin II complexed with the N2 monoglycosylated fragment of human lactotransferrin (18 kDa) and an isolated glycopeptide (2.1 kDa) fragment of human lactotransferrin (at 3.3 A and 2.8 A resolution, respectively). 8069634 5 15 part_of lactotransferrin 900:915 arg1 the N2 monoglycosylated fragment lactotransferrin fragment PUBTATOR Site lactotransferrin P02788 fragment RESULTS We have determined the crystal structures of Lathyrus ochrus isolectin II complexed with the N2 monoglycosylated fragment of human lactotransferrin (18 kDa) and an isolated glycopeptide (2.1 kDa) fragment of human lactotransferrin (at 3.3 A and 2.8 A resolution, respectively). 8069634 5 41 part_of lactotransferrin 983:998 arg1 the N2 monoglycosylated fragment lactotransferrin fragment PUBTATOR Site lactotransferrin P02788 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). 21712440 0 34 part_of precursor 92:100 arg1 amyloid precursor protein/amyloid beta-peptides amyloid precursor protein amyloid precursor protein/amyloid beta-peptides OGER Site amyloid precursor protein P05067 beta-peptides Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid beta-peptides in human cerebrospinal fluid. 21712440 0 85 part_of amyloid 84:90 arg1 amyloid precursor protein/amyloid beta-peptides amyloid precursor protein amyloid precursor protein/amyloid beta-peptides OGER Site amyloid precursor protein P05067 beta-peptides Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid beta-peptides in human cerebrospinal fluid. 21712440 0 87 part_of protein/amyloid 102:116 arg1 amyloid precursor protein/amyloid beta-peptides amyloid precursor protein amyloid precursor protein/amyloid beta-peptides OGER Site amyloid precursor protein P05067 beta-peptides Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid beta-peptides in human cerebrospinal fluid. 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. 3840370 13 5 part_of regions 1700:1706 arg1 C4b-binding protein protein regions Fterm protein These regions in C4b-binding protein are homologous with the three internal-homology regions that have been reported to be present within the Ba region of the complement enzyme factor B and also to the internal-homology regions found in the non-complement beta 2-glycoprotein I. 3840370 13 82 part_of found 1922:1926 arg1 the non-complement beta 2-glycoprotein I AND the internal-homology regions the non-complement beta 2-glycoprotein I the internal-homology regions OGER Site beta 2-glycoprotein I P02749 regions These regions in C4b-binding protein are homologous with the three internal-homology regions that have been reported to be present within the Ba region of the complement enzyme factor B and also to the internal-homology regions found in the non-complement beta 2-glycoprotein I. 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. 15606899 3 29 part_of BACE1 595:599 arg1 the cytosolic tail BACE1 the cytosolic tail PUBTATOR Site BACE1 23621 tail Co-localization and co-immunoprecipitation experiments confirmed that BACE1 and BRI3 co-localize and interact with each other via the cytosolic tail of BACE1. 1740433 8 5 part_of C-SAA 1078:1082 arg1 The C-SAA octapeptide SAA The C-SAA octapeptide PUBTATOR Site SAA P0DJI8 octapeptide The C-SAA octapeptide specifies the first two residues of a NSS tripeptide, the only potential N-linked glycosylation site in the molecule. 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 Asn299 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. 15099525 1 29 part_of ICAM-1 159:164 arg1 the three C-terminal domains 3-5 (D3-D5) ICAM-1 the three C-terminal domains 3-5 (D3-D5) PUBTATOR Site ICAM-1 3383 domains We have determined the 3.0 A crystal structure of the three C-terminal domains 3-5 (D3-D5) of ICAM-1. 2243102 3 56 gly polylactosaminoglycans 306:327 arg1 lamp-2 lamp-2 polylactosaminoglycans PUBTATOR lamp-2 3920 We have localized the polylactosaminoglycans to specific sites on lamp-1 and lamp-2 purified from human chronic myelogenous leukemia cells. 2243102 3 56 gly polylactosaminoglycans 306:327 arg1 lamp-1 lamp-1 polylactosaminoglycans PUBTATOR lamp-1 3916 We have localized the polylactosaminoglycans to specific sites on lamp-1 and lamp-2 purified from human chronic myelogenous leukemia cells. 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. 11279095 7 5 part_of terminus 1365:1372 arg1 the cysteine cysteine cysteine By using the same enzyme preparation and performing mass spectrometric analysis, we found that the first cysteine in sialylmotif L and the cysteine in sialylmotif S form a disulfide bridge, whereas the second cysteine in sialylmotif L and the cysteine at the COOH terminus form a second disulfide bridge. 2129367 5 69 part_of IX 639:640 arg1 Ser-53 factor IX Ser-53 PUBTATOR SpecificSite factor IX 2158 Ser-53 The same results were also obtained for a pentapeptide containing Ser-53 of factor IX and protein Z. Component sugar analysis revealed that the peptide contained 1 mol of glucose and 2 mol of xylose. 28753425 4 28 part_of rhodopsin 685:693 arg1 rhodopsin C-terminal tail residues T336 and S338 rhodopsin rhodopsin C-terminal tail residues T336 and S338 PUBTATOR Site rhodopsin 6010 residues Phosphorylation was detected at rhodopsin C-terminal tail residues T336 and S338. 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. 18559974 7 3 part_of thrombin-cleavage 1250:1266 arg1 a cryptic thrombin-cleavage site thrombin a cryptic thrombin-cleavage site PUBTATOR Site thrombin 2147 site Release of the activation peptide increases dynamic flap mobility and in time this leads to conformational changes that disrupt the catalytic site and expose a cryptic thrombin-cleavage site present at Arg302. 22333914 5 2 part_of overall 1073:1079 arg1 the overall GAIN domain l GAIN the overall GAIN domain PUBTATOR Site l GAIN 23218 domain Functionally, the GAIN domain is both necessary and sufficient for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyse peptide bond hydrolysis. 22333914 5 10 part_of GAIN 1081:1084 arg1 the overall GAIN domain l GAIN the overall GAIN domain PUBTATOR Site l GAIN 23218 domain Functionally, the GAIN domain is both necessary and sufficient for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyse peptide bond hydrolysis. 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. 8172892 4 82 part_of AP 645:646 arg1 residues 157-165 AP alpha residues 157-165 PUBTATOR SpecificSite AP alpha 2028 residues 157-165 A nonapeptide (AP alpha-D4, residues 157-165) and an undecapeptide (AP alpha-D5, 166-176) derived from AP alpha contained Thr-159 and Thr-169, neither of which could be identified using a gas-phase protein sequencer. 8172892 4 71 part_of contained 742:750 arg1 AP alpha-D5, 166-176 AND Thr-159 AP alpha Thr-159 and Thr-169 PUBTATOR SpecificSite AP alpha 2028 Thr-159 and Thr-169 A nonapeptide (AP alpha-D4, residues 157-165) and an undecapeptide (AP alpha-D5, 166-176) derived from AP alpha contained Thr-159 and Thr-169, neither of which could be identified using a gas-phase protein sequencer. 15014436 2 55 part_of TSPs 242:245 arg1 The most highly conserved region TSPs The most highly conserved region Cterm Site TSPs 7057 region The most highly conserved region of all TSPs are the calcium-binding type 3 (T3) repeats and the C-terminal globular domain (CTD). 22448645 3 13 gly N-glycosylated 547:560 arg1 an N-glycosylated form an N-glycosylated form OGER N-glycosylated form of the 5-HT(7 P34969 Western blot analysis of HEK293T cells transiently expressing the 5-HT(7(a)) receptor in the presence of tunicamycin gave rise to a band shift, indicating the existence of an N-glycosylated form of the 5-HT(7(a)) receptor. 22448645 3 13 gly N-glycosylated 547:560 arg1 the 5-HT(7(a)) receptor the 5-HT(7(a)) receptor Fterm receptor Western blot analysis of HEK293T cells transiently expressing the 5-HT(7(a)) receptor in the presence of tunicamycin gave rise to a band shift, indicating the existence of an N-glycosylated form of the 5-HT(7(a)) receptor. 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. 11152692 10 10 part_of asporin 1116:1122 arg1 The deduced amino acid sequence asporin The deduced amino acid sequence PUBTATOR Site asporin 54829 sequence The deduced amino acid sequence of asporin was confirmed by mass spectrometry of the isolated protein resulting in 84% sequence coverage. 19855092 4 6 part_of adiponectin 756:766 arg1 Thr residues adiponectin Thr residues PUBTATOR AminoAcid adiponectin 9370 Thr residues Using a variety of biochemical approaches we demonstrated that sialylation occurs on previously unidentified O-linked glycans on Thr residues of the variable domain in human adiponectin. 19855092 4 6 part_of adiponectin 756:766 arg1 the variable domain adiponectin the variable domain PUBTATOR Site adiponectin 9370 domain Using a variety of biochemical approaches we demonstrated that sialylation occurs on previously unidentified O-linked glycans on Thr residues of the variable domain in human adiponectin. 19855092 4 66 part_of domain 740:745 arg1 human adiponectin adiponectin domain PUBTATOR Site adiponectin 9370 domain Using a variety of biochemical approaches we demonstrated that sialylation occurs on previously unidentified O-linked glycans on Thr residues of the variable domain in human adiponectin. 19855092 4 75 part_of residues 715:722 arg1 human adiponectin adiponectin residues PUBTATOR AminoAcid adiponectin 9370 Thr residues Using a variety of biochemical approaches we demonstrated that sialylation occurs on previously unidentified O-linked glycans on Thr residues of the variable domain in human adiponectin. 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. 21949356 2 12 part_of protein 291:297 arg1 a CAP10 domain protein a CAP10 domain Fterm Site protein domain Drosophila Rumi is a soluble, endoplasmic reticulum-retained protein with a CAP10 domain that functions as a protein O-glucosyltransferase. 21949356 2 48 part_of protein 243:249 arg1 a CAP10 domain protein a CAP10 domain Fterm Site protein domain Drosophila Rumi is a soluble, endoplasmic reticulum-retained protein with a CAP10 domain that functions as a protein O-glucosyltransferase. 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). 21525977 0 32 part_of NPC1L1 21:26 arg1 the NPC1L1 N-terminal domain structure of the NPC1L1 the NPC1L1 N-terminal domain PUBTATOR Site structure of the NPC1L1 29881 domain The structure of the NPC1L1 N-terminal domain in a closed conformation. 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. 19563754 0 30 part_of NPC1 34:37 arg1 N-terminal domain NPC1 N-terminal domain PUBTATOR Site NPC1 O15118 domain Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol. 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). 15014436 8 44 part_of TSP 1037:1039 arg1 the TSP C-terminal region TSP the TSP C-terminal region PUBTATOR Site TSP 7057 region The central architectural role of calcium explains how it is critical for the functions of the TSP C-terminal region. 26274980 4 42 part_of nCG 1272:1274 arg1 the active site nCG the active site Cterm Site nCG 1511 site Asn71 appeared proximal (~19 Å) to the active site of nCG, but due to the truncated nature of Asn71-glycans (~5-17 Å) we questioned their direct modulation of the proteolytic activity of the protein. 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. 29374258 0 36 part_of regions 90:96 arg1 the catalytic domain regions the catalytic domain domain Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain. 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 Asn-88 Glycosylation at Asn-88 has not been observed previously in mammalian secretory RNases. 22235133 3 2 part_of receptor 444:451 arg1 the class I cytokine receptor signature motif receptor the class I cytokine receptor signature motif Fterm Site receptor motif A hallmark of the class I cytokine receptors is the class I cytokine receptor signature motif (WSXWS). 22235133 3 54 part_of receptors 410:418 arg1 the class I cytokine receptor signature motif receptors the class I cytokine receptor signature motif Fterm Site receptors motif A hallmark of the class I cytokine receptors is the class I cytokine receptor signature motif (WSXWS). 15477100 1 67 gly Zn-alpha2-glycoprotein 70:91 arg1 ZAG ZAG PUBTATOR ZAG 563 Zn-alpha2-glycoprotein (ZAG) is a 41 kDa soluble protein that is present in most bodily fluids. 15477100 1 67 gly Zn-alpha2-glycoprotein 70:91 arg1 Zn-alpha2-glycoprotein Zn-alpha2-glycoprotein PUBTATOR Zn-alpha2-glycoprotein 563 Zn-alpha2-glycoprotein (ZAG) is a 41 kDa soluble protein that is present in most bodily fluids. 15477100 1 67 gly Zn-alpha2-glycoprotein 70:91 arg1 a 41 kDa soluble protein a 41 kDa soluble protein Fterm protein Zn-alpha2-glycoprotein (ZAG) is a 41 kDa soluble protein that is present in most bodily fluids. 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. 24692546 2 38 part_of FSHR 254:257 arg1 The FSHR extracellular domains FSHR The FSHR extracellular domains OGER Site FSHR P23945 domains The FSHR extracellular domains were observed in the crystal structure as a trimer, which enabled us to propose a novel model for the receptor activation mechanism. 8617200 4 19 part_of TGF-beta1 887:895 arg1 the LAP region TGF-beta1 the LAP region PUBTATOR Site TGF-beta1 4052 region Immunoblotting of the fusion protein complexes indicated that the third 8-Cys repeat of LTBP-1 bound covalently to the LAP region of TGF-beta1. 8617200 4 39 part_of LAP 873:875 arg1 the LAP region LAP the LAP region PUBTATOR Site LAP P17676 region Immunoblotting of the fusion protein complexes indicated that the third 8-Cys repeat of LTBP-1 bound covalently to the LAP region of TGF-beta1. 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. 4055801 12 55 part_of C9 1543:1544 arg1 the C9 polypeptide C9 the C9 polypeptide Cterm Site C9 polypeptide Thus, the C9a and C9b segments of the C9 polypeptide are not clearly segregated in poly(C9). 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. 19805286 4 12 part_of IX 595:596 arg1 the catalytic domain CA IX the catalytic domain PUBTATOR Site CA IX 768 domain Here we report the X-ray structure of the catalytic domain of CA IX in complex with a classical, clinically used sulfonamide inhibitor, acetazolamide. 12788922 4 26 part_of C1s 500:502 arg1 the interaction domain C1s the interaction domain PUBTATOR Site C1s P09871 domain The crystal structure of the interaction domain of C1s has been solved and refined to 1.5 A resolution. 9748270 7 44 part_of XVII 949:952 arg1 the collagen XVII ectodomain XVII the collagen XVII ectodomain Cterm Site XVII ectodomain The soluble form exhibited molecular properties of the collagen XVII ectodomain: a triple-helical, N-glycosylated molecule of three 120-kDa polypeptides. 27033522 3 39 part_of contains 443:450 arg1 PEBP4 AND potential glycosylation sites PEBP4 potential glycosylation sites PUBTATOR Site PEBP4 157310 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. 27033522 3 39 part_of contains 443:450 arg1 PEBP4 AND a signal peptide PEBP4 a signal peptide PUBTATOR Site PEBP4 157310 peptide 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. 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. 20534510 6 13 part_of PDGFRbeta 1300:1308 arg1 the third Ig domain PDGFRbeta the third Ig domain PUBTATOR Site PDGFRbeta 5159 domain A large-scale structural organization and rearrangement is observed for PDGF-B upon receptor binding, in which the PDGF-B L1 loop, disordered in the structure of the free form, adopts a highly specific conformation to form hydrophobic interactions with the third Ig domain of PDGFRbeta. 11602603 9 82 part_of epsilon 1375:1381 arg1 The amino acid sequence tryptase epsilon The amino acid sequence PUBTATOR Site tryptase epsilon Q9GZN4 sequence The amino acid sequence of human tryptase epsilon is 38-44% identical to those of human tryptase alpha, tryptase beta I, tryptase beta II, tryptase beta III, transmembrane tryptase/tryptase gamma, marapsin, and Esp-1/testisin. 20837471 6 0 part_of Thr 1105:1107 arg1 ANGPTL3 ANGPTL3 Thr PUBTATOR SpecificSite ANGPTL3 Q9Y5C1 Thr(226) Screening of a panel of proteins known to affect lipid metabolism for potential sites glycosylated by GalNAc-T2 led to identification of Thr(226) adjacent to the proprotein convertase processing site in ANGPTL3. 16492764 1 8 part_of receptor 259:266 arg1 a ligand binding region GCSF receptor a ligand binding region PUBTATOR Site GCSF receptor 1441 region A crystal structure of the signaling complex between human granulocyte colony-stimulating factor (GCSF) and a ligand binding region of GCSF receptor (GCSF-R), has been determined to 2.8 A resolution. 6510521 0 42 part_of hemopexin 54:62 arg1 the N-terminal region hemopexin the N-terminal region PUBTATOR Site hemopexin 3263 region Amino acid sequence of the N-terminal region of human hemopexin. 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). 3264725 3 66 part_of VIIa 727:730 arg1 the amino acid sequence factor VIIa the amino acid sequence Cterm Site factor VIIa sequence In the present study, the amino acid sequence and posttranslational modifications of recombinant factor VIIa as purified from the culture medium of a transfected baby hamster kidney cell line have been compared to human plasma factor VIIa. 16754968 1 36 part_of receptor 299:306 arg1 the extracellular domains receptor the extracellular domains Fterm Site receptor domains X-ray diffraction has been used to produce and refine a model of the extracellular domains of the beta common cytokine receptor. 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. 19196183 0 70 part_of sites 34:38 arg1 secreted proteins proteins sites Fterm Site proteins sites Identification of N-glycosylation sites on secreted proteins of human hepatocellular carcinoma cells with a complementary proteomics approach. 28775322 3 46 part_of EGF-like 497:504 arg1 several EGF-like domains EGF several EGF-like domains OGER Site EGF P01133 domains Using several EGF-like domains and donor substrate analogs, we have determined the structures of human Protein O-glucosyltransferase 1 substrate/product complexes that provide mechanistic insight into the basis for these properties. 18467335 9 27 gly N-glycosylated 997:1010 arg2 Asn-243 PCI sites, Asn-230, Asn-243, and Asn-319 OGER PCI P05154 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 27 gly N-glycosylated 997:1010 arg2 Asn-230 PCI sites, Asn-230, Asn-243, and Asn-319 OGER PCI P05154 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 27 gly N-glycosylated 997:1010 arg2 Asn-319 PCI sites, Asn-230, Asn-243, and Asn-319 OGER PCI P05154 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 27 gly N-glycosylated 997:1010 arg2 all three potential N-glycosylation sites PCI sites, Asn-230, Asn-243, and Asn-319 OGER PCI P05154 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 27 gly N-glycosylated 997:1010 arg2 Asn-230 sites, Asn-230, Asn-243, and Asn-319 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 27 gly N-glycosylated 997:1010 arg2 Asn-319 sites, Asn-230, Asn-243, and Asn-319 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 27 gly N-glycosylated 997:1010 arg2 all three potential N-glycosylation sites sites, Asn-230, Asn-243, and Asn-319 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 27 gly N-glycosylated 997:1010 arg2 Asn-319 sites, Asn-230, Asn-243, and Asn-319 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 27 gly N-glycosylated 997:1010 arg2 all three potential N-glycosylation sites sites, Asn-230, Asn-243, and Asn-319 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 27 gly N-glycosylated 997:1010 arg2 all three potential N-glycosylation sites sites, Asn-230, Asn-243, and Asn-319 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 83 gly N-glycosylation 1035:1049 arg2 Asn-230 sites, Asn-230, Asn-243, and Asn-319 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 83 gly N-glycosylation 1035:1049 arg2 Asn-319 sites, Asn-230, Asn-243, and Asn-319 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 83 gly N-glycosylation 1035:1049 arg2 all three potential N-glycosylation sites sites, Asn-230, Asn-243, and Asn-319 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 83 gly N-glycosylation 1035:1049 arg2 Asn-319 sites, Asn-230, Asn-243, and Asn-319 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 83 gly N-glycosylation 1035:1049 arg2 all three potential N-glycosylation sites sites, Asn-230, Asn-243, and Asn-319 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 18467335 9 83 gly N-glycosylation 1035:1049 arg2 all three potential N-glycosylation sites sites, Asn-230, Asn-243, and Asn-319 sites, Asn-230, Asn-243, and Asn-319 PCI was N-glycosylated at all three potential N-glycosylation sites, Asn-230, Asn-243, and Asn-319, but a small fraction of PCI lacked the N-glycan at Asn-243. 24927598 7 39 part_of N102 1011:1014 arg1 ZIP14 ZIP14 N102 PUBTATOR SpecificSite ZIP14 23516 N102 Asparagine-linked (N-linked) glycosylation of ZIP14, particularly the glycosylation at N102, was required for efficient membrane extraction of ZIP14 and therefore is necessary for its iron sensitivity. 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. 21569239 6 32 part_of mindin 838:843 arg1 the FS domains mindin the FS domains PUBTATOR Site mindin 10417 domains Though the primary sequences of the FS domains of F-spondin and mindin are less than 36% identical, their overall structures are very similar. 21569239 6 38 part_of F-spondin 824:832 arg1 the FS domains F-spondin the FS domains PUBTATOR Site F-spondin 10418 domains Though the primary sequences of the FS domains of F-spondin and mindin are less than 36% identical, their overall structures are very similar. 19358553 4 46 part_of fetuin 1052:1057 arg1 three different sialoglycopeptides fetuin three different sialoglycopeptides Fterm Site fetuin sialoglycopeptides Similarly, precise quantitation was observed for various forms of N-glycans (free, permethylated, and fluorescence-labeled) using MS. In addition, three different sialoglycopeptides from fetuin were site-specifically profiled, and good correlation between peak intensities and relative abundances was found with only a minor loss of sialic acids (r = 0.9664, n = 5). 16497731 3 34 part_of adiponectin 489:499 arg1 Multimer composition adiponectin Multimer composition PUBTATOR Site adiponectin 9370 position Multimer composition of adiponectin appears to be regulated; however, the molecular mechanisms involved are unknown. 11285216 1 1 part_of region 183:188 arg1 the (6)F1(1)F2(2)F2 fragment region the (6)F1(1)F2(2)F2 fragment fragment The solution structure of the (6)F1(1)F2(2)F2 fragment from the gelatin-binding region of fibronectin has been determined (Protein Data Bank entry codes 1e88 and 1e8b). 11285216 1 54 part_of fibronectin 193:203 arg1 the gelatin-binding region fibronectin the gelatin-binding region PUBTATOR Site fibronectin 2335 region The solution structure of the (6)F1(1)F2(2)F2 fragment from the gelatin-binding region of fibronectin has been determined (Protein Data Bank entry codes 1e88 and 1e8b). 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 site Asn392 site Asn392 The approach was evaluated on glycoprotein standards and also applied to investigate the glycosylation of human IgG3 providing details on the hitherto uncharacterized glycosylation site Asn392 of the CH3 domain. 26536155 6 33 gly glycosylation 1579:1591 arg2 the CH3 domain domain domain The approach was evaluated on glycoprotein standards and also applied to investigate the glycosylation of human IgG3 providing details on the hitherto uncharacterized glycosylation site Asn392 of the CH3 domain. 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. 2963625 0 52 part_of H 60:60 arg1 The complete amino acid sequence factor H The complete amino acid sequence PUBTATOR Site factor H 3075 sequence The complete amino acid sequence of human complement factor H. 9342320 4 0 part_of contains 676:683 arg1 human IFN-beta AND a zinc-binding site human IFN-beta a zinc-binding site PUBTATOR Site IFN-beta P01574 site Like human IFN-alpha2b, human IFN-beta contains a zinc-binding site at the interface of the two molecules in the asymmetric unit, raising the question of functional relevance for IFN-beta dimers. 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. 3886654 6 38 part_of factor 841:846 arg1 " a "growth factor" domain factor " a "growth factor" domain Fterm Site factor domain The heavy chain of alpha-factor XIIa appears to contain four different domains including a "kringle," a "growth factor" domain, and the "type I" and "type II" domains of fibronectin. 3886654 6 68 part_of fibronectin 899:909 arg1 " a "growth factor" domain fibronectin " a "growth factor" domain PUBTATOR Site fibronectin 2335 domain The heavy chain of alpha-factor XIIa appears to contain four different domains including a "kringle," a "growth factor" domain, and the "type I" and "type II" domains of fibronectin. 3886654 6 68 part_of fibronectin 899:909 arg1 four different domains fibronectin four different domains PUBTATOR Site fibronectin 2335 domains The heavy chain of alpha-factor XIIa appears to contain four different domains including a "kringle," a "growth factor" domain, and the "type I" and "type II" domains of fibronectin. 21763278 2 25 part_of sites 241:245 arg1 human pro-BNP BNP sites PUBTATOR Site BNP 4879 sites Recent studies identified several O-glycosylation sites, including Thr-71, on human pro-BNP but the functional significance was unclear. 10639192 6 4 gly attached 712:719 arg2 Asp 301 AND high-mannose chains Asn 62 and Asp 301 high-mannose chains Asn 62 and Asp 301 It appears that high-mannose chains are attached to Asn 62 and Asp 301, while complex chains are at Asn 188. 22576872 3 8 part_of Aβ 526:527 arg1 longer Aβ peptides Aβ longer Aβ peptides PUBTATOR Site Aβ 351 peptides When one analyzes longer Aβ peptides by low-energy collision-induced dissociation tandem mass spectrometry (MS/MS), mainly long b-fragments are observed, limiting the possibility to determine variations such as amino acid variants or post-translational modifications (PTMs) within the N-terminal half of the peptide. 8617200 5 66 part_of beta1-LAP 992:1000 arg1 Cys33 LAP Cys33 OGER AminoAcid LAP P17676 Cys33 The cysteine required for the association between LTBP-1 and beta1-LAP was mapped to Cys33 of beta1-LAP. 20511397 4 10 gly sialylation 768:778 arg1 cellular and secreted apoE cellular and secreted apoE PUBTATOR apoE 348 We investigated glycosylation and sialylation of cellular and secreted apoE from primary human macrophages by one- and two-dimensional gel electrophoresis and mass spectrometry. 20511397 4 47 gly glycosylation 750:762 arg1 cellular and secreted apoE cellular and secreted apoE PUBTATOR apoE 348 We investigated glycosylation and sialylation of cellular and secreted apoE from primary human macrophages by one- and two-dimensional gel electrophoresis and mass spectrometry. 20511397 4 72 gly apoE 805:808 arg1 sialylation apoE sialylation PUBTATOR apoE 348 We investigated glycosylation and sialylation of cellular and secreted apoE from primary human macrophages by one- and two-dimensional gel electrophoresis and mass spectrometry. 21569239 10 79 part_of F-spondin 1413:1421 arg1 the F-spondin FS domain F-spondin the F-spondin FS domain PUBTATOR Site F-spondin 10418 domain The homology of its core structure to a common Ca2+- and lipid-binding C2 domain suggests that the F-spondin FS domain may be responsible for part of the membrane targeting of F-spondin in its regulation of axon development. 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). 3877053 3 31 part_of XIIa 345:348 arg1 regions factor XIIa regions Cterm Site factor XIIa P00748 regions These oligonucleotides encoded regions of beta-factor XIIa as predicted from the amino acid sequence. 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. 26146185 4 49 part_of CD6 580:582 arg1 the three SRCR domains CD6 the three SRCR domains PUBTATOR Site CD6 923 domains We have solved the X-ray crystal structures of the three SRCR domains of CD6 and two N-terminal domains of CD166. 26146185 4 47 part_of CD166 614:618 arg1 the three SRCR domains CD166 domains PUBTATOR Site CD166 214 domains We have solved the X-ray crystal structures of the three SRCR domains of CD6 and two N-terminal domains of CD166. 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. 12970363 11 17 part_of site 1668:1671 arg1 TRPC3 TRPC3 site PUBTATOR Site TRPC3 7222 site Reciprocally, engineering of an additional second glycosylated site in TRPC3 to mimic the glycosylation status in TRPC6 markedly reduced TRPC3 basal activity. 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. 12034737 0 42 part_of CXCR4 52:56 arg1 the CXCR4 amino terminus CXCR4 the CXCR4 amino terminus PUBTATOR Site CXCR4 7852 terminus The role of post-translational modifications of the CXCR4 amino terminus in stromal-derived factor 1 alpha association and HIV-1 entry. 8962717 3 53 part_of EGF-binding 567:577 arg1 the EGF-binding domain EGF the EGF-binding domain OGER Site EGF P01133 domain The latter chains were shown by chromatographic separation and mass spectrometric analysis of tryptic digests to be clustered in the EGF-binding domain. 17196528 2 3 part_of TrkA 469:472 arg1 a complete extracellular domain TrkA a complete extracellular domain PUBTATOR Site TrkA 4914 domain To define a structural basis for the high-affinity site, we have determined the three-dimensional structure of a complete extracellular domain of TrkA complexed with NGF. 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%). 16476442 0 0 part_of enzyme 76:81 arg1 the N domain enzyme the N domain Fterm Site enzyme domain Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design. 15750791 4 0 part_of Edg-1/S1P1 620:629 arg1 the N-terminal ectodomain Edg-1 the N-terminal ectodomain PUBTATOR Site Edg-1 1901 ectodomain We also demonstrated that the structure of the N-terminal ectodomain of Edg-1/S1P1 affects both its transport to the cell surface and the N-glycosylation process. 26811476 5 12 part_of UMOD 844:847 arg1 polymerization regions UMOD polymerization regions PUBTATOR Site UMOD 7369 regions Here, we report the crystal structures of polymerization regions of human UMOD and mouse ZP2, an essential sperm receptor protein that is structurally related to UMOD but forms heteropolymers. 26811476 5 59 part_of ZP2 859:861 arg1 polymerization regions ZP2 polymerization regions PUBTATOR Site ZP2 22787 regions Here, we report the crystal structures of polymerization regions of human UMOD and mouse ZP2, an essential sperm receptor protein that is structurally related to UMOD but forms heteropolymers. 18596036 9 58 part_of MBL 1808:1810 arg1 a conserved lysine MBL a conserved lysine PUBTATOR AminoAcid MBL 4153 lysine This information allows us to propose a model of the MBL-MASP-1/3 interaction, involving a major electrostatic interaction between two acidic Ca(2+) ligands of MASP-1/3 and a conserved lysine of MBL. 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. 2071582 8 84 part_of chymase 1352:1358 arg1 chymase gene-specific fragments chymase chymase gene-specific fragments PUBTATOR Site chymase P23946 fragments Amplification of chymase gene-specific fragments from hamster/human hybrid cell line DNA suggests localization of the chymase gene to human chromosome 14. 25561468 3 19 part_of β4-strands 490:499 arg1 the mature ectodomain 4 the mature ectodomain PUBTATOR Site 4 5355 ectodomain Structural studies indicated that β2- or β4-strands in the mature ectodomain (ME ICA512) form dimers in vitro. 25561468 3 50 part_of β2- 483:485 arg1 the mature ectodomain 2 the mature ectodomain PUBTATOR Site 2 27239 ectodomain Structural studies indicated that β2- or β4-strands in the mature ectodomain (ME ICA512) form dimers in vitro. 3877053 8 30 part_of fibronectin 1224:1234 arg1 regions fibronectin regions PUBTATOR Site fibronectin 2335 regions Comparison of the structure of factor XII with other proteins revealed extensive sequence identity with regions of tissue-type plasminogen activator (the epidermal growth factor-like region and the kringle region) and fibronectin (type I and type II homologies). 3877053 8 83 part_of activator 1145:1153 arg1 regions tissue-type plasminogen activator regions PUBTATOR Site tissue-type plasminogen activator 5327 regions Comparison of the structure of factor XII with other proteins revealed extensive sequence identity with regions of tissue-type plasminogen activator (the epidermal growth factor-like region and the kringle region) and fibronectin (type I and type II homologies). 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. 3353370 7 28 part_of contains 1330:1337 arg1 The amino-terminal region AND a leucine-rich sequence The amino-terminal region a leucine-rich sequence sequence The amino-terminal region of the beta chain contains a leucine-rich sequence of 24 amino acids that is similar to a sequence that occurs as seven tandem repeats in the alpha chain of GPIb and nine tandem repeats in leucine-rich alpha 2-glycoprotein. 1517205 1 13 part_of protein 341:347 arg1 Ser-53 protein Z Ser-53 Cterm SpecificSite protein Z Ser-53 We have recently discovered unusual sugar chains (xylose (Xyl)-glucose (Glc) and (Xyl)2-Glc) linked to a serine residue in the epidermal growth factor (EGF)-like domains of human and bovine clotting factors VII (Ser-52), IX (Ser-53), and protein Z (Ser-53), in addition to bovine platelet glycoprotein thrombospondin. 1517205 1 19 part_of factors 302:308 arg1 the epidermal growth factor (EGF)-like domains factors the epidermal growth factor (EGF)-like domains Fterm Site factors domains We have recently discovered unusual sugar chains (xylose (Xyl)-glucose (Glc) and (Xyl)2-Glc) linked to a serine residue in the epidermal growth factor (EGF)-like domains of human and bovine clotting factors VII (Ser-52), IX (Ser-53), and protein Z (Ser-53), in addition to bovine platelet glycoprotein thrombospondin. 1517205 1 59 part_of residue 215:221 arg1 human and bovine clotting factors VII (Ser-52), IX (Ser-53), and protein Z (Ser-53) factors residue Fterm AminoAcid factors serine residue We have recently discovered unusual sugar chains (xylose (Xyl)-glucose (Glc) and (Xyl)2-Glc) linked to a serine residue in the epidermal growth factor (EGF)-like domains of human and bovine clotting factors VII (Ser-52), IX (Ser-53), and protein Z (Ser-53), in addition to bovine platelet glycoprotein thrombospondin. 1517205 1 99 part_of factor 247:252 arg1 the epidermal growth factor (EGF)-like domains factor the epidermal growth factor (EGF)-like domains Fterm Site factor domains We have recently discovered unusual sugar chains (xylose (Xyl)-glucose (Glc) and (Xyl)2-Glc) linked to a serine residue in the epidermal growth factor (EGF)-like domains of human and bovine clotting factors VII (Ser-52), IX (Ser-53), and protein Z (Ser-53), in addition to bovine platelet glycoprotein thrombospondin. 10074346 0 33 part_of fibrin 62:67 arg1 fragments D and double-D fibrin fragments D and double-D Fterm Site fibrin fragments Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide. 19196183 4 42 gly glycopeptides 501:513 arg2 glycopeptides glycopeptides glycopeptides For the enrichment of glycopeptides, capture methods with hydrophilic affinity (HA) and hydrazide chemistry (HC) were used complementarily. 8702538 8 84 part_of motifs 1291:1296 arg1 the first or second Ig domains motifs the first or second Ig domains domains Site-directed mutagenesis of similar NC(T/S) motifs in the first or second Ig domains of the I-type lectins myelin-associated glycoprotein, and sialoadhesin did not disrupt their ability to mediate sialic acid binding. 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. 23260142 4 5 part_of HLA-DR 532:537 arg1 hydrophobic HLA-DR residues HLA hydrophobic HLA-DR residues OGER Site HLA residues Flipping of a tryptophan away from the HLA-DR1 P1 pocket enables major conformational changes that position hydrophobic HLA-DR residues into the P1 pocket. 3524673 1 49 part_of factor 109:114 arg1 The complete amino acid sequence von Willebrand factor The complete amino acid sequence PUBTATOR Site von Willebrand factor 7450 sequence The complete amino acid sequence of human von Willebrand factor (vWF) is presented. 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. 15093539 1 28 part_of receptor 199:206 arg1 the extracellular domain epidermal growth factor receptor 2 the extracellular domain PUBTATOR Site epidermal growth factor receptor 2 2064 domain We have determined the 3.2 A X-ray crystal structure of the extracellular domain of the human epidermal growth factor receptor 2 (ErbB2 or HER2) in a complex with the antigen binding fragment of pertuzumab, an anti-ErbB2 monoclonal antibody also known as 2C4 or Omnitarg. 3497398 11 5 part_of protein 1698:1704 arg1 This protein sequence protein This protein sequence Fterm Site protein sequence This protein sequence agrees completely with that deduced from the cDNA sequence reported by Lopez et al. [Lopez, J.A., Chung, D.W., Fujikawa, K., Hagen, F.S., Papayannopoulou, T. & Roth, G.J. (1987) Proc. 17065148 6 32 part_of TRPM8 1001:1005 arg1 the membrane-attached C-terminal region TRPM8 the membrane-attached C-terminal region PUBTATOR Site TRPM8 79054 region Furthermore, wild-type currents can be suppressed by expressing the membrane-attached C-terminal region of TRPM8. 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. 16732286 0 27 part_of receptor 31:38 arg1 the Tie2 receptor ectodomain Tie2 receptor the Tie2 receptor ectodomain PUBTATOR Site Tie2 receptor 7010 ectodomain Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex. 16732286 0 31 part_of Tie2 26:29 arg1 the Tie2 receptor ectodomain Tie2 receptor the Tie2 receptor ectodomain PUBTATOR Site Tie2 receptor 7010 ectodomain Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex. 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. 20879038 6 74 part_of PRP-modified 1334:1345 arg1 45 new PRP-modified residues PRP 45 new PRP-modified residues PUBTATOR Site PRP 722 residues In summary, salivary peptidome data analysis allowed the identification of 45 new PRP-modified residues, mainly due to glycosylation, phosphorylation and conversion of Gln to pyro-Glu. 3264725 0 87 part_of VIIa 72:75 arg1 Amino acid sequence factor VIIa Amino acid sequence Cterm Site factor VIIa sequence Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells. 14718370 10 38 part_of MUC5AC 1642:1647 arg1 the Cys subdomains MUC5AC the Cys subdomains PUBTATOR AminoAcid MUC5AC P98088 Cys subdomains Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs. 14718370 10 49 part_of MUC5B 1653:1657 arg1 the Cys subdomains MUC5B the Cys subdomains PUBTATOR AminoAcid MUC5B Q9HC84 Cys subdomains Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs. 14718370 10 68 part_of motifs 1703:1708 arg1 MUC5B MUC5B motifs PUBTATOR Site MUC5B Q9HC84 motifs Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs. 14718370 10 68 part_of motifs 1703:1708 arg1 MUC5AC MUC5AC motifs PUBTATOR Site MUC5AC P98088 motifs Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs. 14718370 10 68 part_of motifs 1703:1708 arg1 the Cys subdomains motifs the Cys subdomains Cys subdomains Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs. 11741940 4 2 part_of proteins 824:831 arg1 homologous domains proteins homologous domains Fterm Site proteins domains Numbering sFRP-1 cysteines sequentially from the N terminus, the five disulfide linkages in the Fz domain are 1-5, 2-4, 3-8, 6-10, and 7-9, consistent with the disulfide pattern determined for homologous domains of several other proteins. 11741940 4 112 part_of sFRP-1 605:610 arg1 sFRP-1 cysteines Numbering sFRP-1 sFRP-1 cysteines PUBTATOR AminoAcid Numbering sFRP-1 6422 cysteines Numbering sFRP-1 cysteines sequentially from the N terminus, the five disulfide linkages in the Fz domain are 1-5, 2-4, 3-8, 6-10, and 7-9, consistent with the disulfide pattern determined for homologous domains of several other proteins. 10066782 6 54 part_of motifs 947:952 arg1 known Ig superfamily domains motifs known Ig superfamily domains domains The disulfides Cys102-Cys113 and Cys146-Cys157 are consistent with known cytokine-binding domain motifs, and Cys28-Cys77 with known Ig superfamily domains. 9030779 0 65 part_of sphingomyelinase 71:86 arg1 the N-glycosylation sites acid sphingomyelinase the N-glycosylation sites PUBTATOR Site acid sphingomyelinase 6609 sites Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis. 2361960 3 39 part_of IL-5 522:525 arg1 human IL-5 cDNA sequence IL-5 human IL-5 cDNA sequence PUBTATOR Site IL-5 3567 sequence After digestion with API, we could identify all the peptides which were expected from human IL-5 cDNA sequence. 16492764 3 26 part_of GCSF-R 588:593 arg1 the cytokine receptor homologous domain GCSF-R the cytokine receptor homologous domain PUBTATOR Site GCSF-R 12986 domain The conformation of the complex is quite different from that between human GCSF and the cytokine receptor homologous domain of mouse GCSF-R, but similar to that of the IL-6/gp130 signaling complex. 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. 29374258 6 24 part_of PGAP4 1025:1029 arg1 a juxtamembrane region PGAP4 a juxtamembrane region OGER Site PGAP4 Q9BRR3 region We suggest that a juxtamembrane region of PGAP4 accommodates various GPI-anchored proteins, presenting their acceptor residue toward the catalytic center. 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. 22848655 5 16 part_of dimerization 715:726 arg1 the ligand recognition and dimerization domains dimerization the ligand recognition and dimerization domains Fterm Site dimerization domains The ectodomain of RON, containing the ligand recognition and dimerization domains, is composed of a semaphorin (Sema), Plexins-Semaphorins-Integrins domain (PSI), and four Immunoglobulins-Plexins-Transcription factor (IPT) domains. 22848655 5 63 part_of IPT 872:874 arg1 four Immunoglobulins-Plexins-Transcription factor (IPT) domains IPT four Immunoglobulins-Plexins-Transcription factor (IPT) domains OGER Site IPT Q9H3H1 domains The ectodomain of RON, containing the ligand recognition and dimerization domains, is composed of a semaphorin (Sema), Plexins-Semaphorins-Integrins domain (PSI), and four Immunoglobulins-Plexins-Transcription factor (IPT) domains. 22848655 5 71 part_of RON 672:674 arg1 The ectodomain RON The ectodomain OGER Site RON Q04912 ectodomain The ectodomain of RON, containing the ligand recognition and dimerization domains, is composed of a semaphorin (Sema), Plexins-Semaphorins-Integrins domain (PSI), and four Immunoglobulins-Plexins-Transcription factor (IPT) domains. 22848655 5 47 part_of containing 677:686 arg1 RON AND the ligand recognition and dimerization domains RON the ligand recognition and dimerization domains OGER Site RON Q04912 domains The ectodomain of RON, containing the ligand recognition and dimerization domains, is composed of a semaphorin (Sema), Plexins-Semaphorins-Integrins domain (PSI), and four Immunoglobulins-Plexins-Transcription factor (IPT) domains. 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. 26403559 1 48 part_of dipeptidylcarboxypeptidase 123:148 arg1 two active domains dipeptidylcarboxypeptidase two active domains Fterm Site dipeptidylcarboxypeptidase domains Angiotensin-I converting enzyme (ACE) is a zinc dipeptidylcarboxypeptidase with two active domains and plays a key role in the regulation of blood pressure and electrolyte homeostasis, making it the principal target in the treatment of cardiovascular disease. 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. 2129367 3 1 part_of growth 378:383 arg1 the first epidermal growth factor-like domain epidermal growth factor the first epidermal growth factor-like domain PUBTATOR Site epidermal growth factor 521832 domain In the course of the studies, we found an unknown serine derivative at position 52 in the first epidermal growth factor-like domain of factor VII. 2129367 3 40 part_of factor-like 385:395 arg1 the first epidermal growth factor-like domain epidermal growth factor the first epidermal growth factor-like domain PUBTATOR Site epidermal growth factor 521832 domain In the course of the studies, we found an unknown serine derivative at position 52 in the first epidermal growth factor-like domain of factor VII. 2129367 3 42 part_of epidermal 368:376 arg1 the first epidermal growth factor-like domain epidermal growth factor the first epidermal growth factor-like domain PUBTATOR Site epidermal growth factor 521832 domain In the course of the studies, we found an unknown serine derivative at position 52 in the first epidermal growth factor-like domain of factor VII. 2129367 3 46 part_of VII 414:416 arg1 the first epidermal growth factor-like domain factor VII the first epidermal growth factor-like domain PUBTATOR Site factor VII 2155 domain In the course of the studies, we found an unknown serine derivative at position 52 in the first epidermal growth factor-like domain of factor VII. 21908432 4 30 part_of GPIX 594:597 arg1 the GPIX ectodomain sequence GPIX the GPIX ectodomain sequence PUBTATOR Site GPIX 2815 sequence The structure of a chimera of GPIbβ(E) and 3 loops (a,b,c) taken from the GPIX ectodomain sequence was also determined. 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. 18491227 0 38 part_of E-cadherin 56:65 arg1 extracellular domain E-cadherin extracellular domain PUBTATOR Site E-cadherin 999 domain Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD. 20188224 10 76 gly glycosylation 1499:1511 arg2 the sites the sites sites The method developed was applied to progranulin (PGRN) to characterize the structures of the released glycans and to identify the sites of glycosylation. 19901337 0 39 part_of receptor-binding 50:65 arg1 NL63 respiratory coronavirus receptor-binding domain receptor NL63 respiratory coronavirus receptor-binding domain Fterm Site receptor domain Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor. 22848655 4 70 part_of kinase 638:643 arg1 the intracellular kinase domains kinase the intracellular kinase domains Fterm Site kinase domains The binding of MSP α/β heterodimer to the extracellular region of RON receptor induces receptor dimerization and activation by autophosphorylation of the intracellular kinase domains. 22848655 4 95 part_of receptor 540:547 arg1 the extracellular region RON receptor the extracellular region OGER Site RON receptor Q04912 region The binding of MSP α/β heterodimer to the extracellular region of RON receptor induces receptor dimerization and activation by autophosphorylation of the intracellular kinase domains. 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. 20696930 5 43 part_of epitope 587:593 arg1 HER2 HER2 epitope PUBTATOR Site HER2 2064 epitope Zher2 binds to a conformational epitope on HER2 that is distant from those recognized by the therapeutic antibodies trastuzumab and pertuzumab. 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. 22660477 5 13 part_of GBR2 551:554 arg1 the GBR2 ectodomain GBR2 the GBR2 ectodomain Cterm Site GBR2 ectodomain Here we demonstrate that the GBR2 ectodomain directly interacts with the GBR1 ectodomain to increase agonist affinity by selectively stabilizing the agonist-bound conformation of GBR1. 19571171 5 46 part_of addressin 1038:1046 arg1 a sulfated peripheral lymph node addressin epitope addressin a sulfated peripheral lymph node addressin epitope Fterm Site addressin epitope The N196 and N410 glycans differentially affect sulfation of two different substrates: cells that express an enzyme lacking the N410 glycan are able to sulfate the sialyl Lewis X substrate, but produce reduced levels of a sulfated peripheral lymph node addressin epitope and cells that express an enzyme lacking the N196 glycan are able to produce a sulfated peripheral lymph node addressin epitope, but are impaired in their ability to sulfate sialyl Lewis X. 19571171 5 57 part_of addressin 1166:1174 arg1 a sulfated peripheral lymph node addressin epitope addressin a sulfated peripheral lymph node addressin epitope Fterm Site addressin epitope The N196 and N410 glycans differentially affect sulfation of two different substrates: cells that express an enzyme lacking the N410 glycan are able to sulfate the sialyl Lewis X substrate, but produce reduced levels of a sulfated peripheral lymph node addressin epitope and cells that express an enzyme lacking the N196 glycan are able to produce a sulfated peripheral lymph node addressin epitope, but are impaired in their ability to sulfate sialyl Lewis X. 6333684 4 3 part_of interleukin 590:600 arg1 The entire primary sequence interleukin 2 The entire primary sequence PUBTATOR Site interleukin 2 3558 sequence The entire primary sequence of interleukin 2, including the location of the intramolecular disulfide bridge, was determined by a combination of peptide mapping and protein sequencing. 18764929 3 1 part_of SEA 530:532 arg1 sea urchin-enterokinase-agrin (SEA) domain SEA sea urchin-enterokinase-agrin (SEA) domain Cterm Site SEA O00468 domain These two subunits are generated by autoproteolysis of a monomeric precursor within a distinctive protein motif called sea urchin-enterokinase-agrin (SEA) domain, yet the purpose of this cleavage and heterodimer creation is uncertain. 18764929 3 84 part_of urchin-enterokinase-agrin 503:527 arg1 sea urchin-enterokinase-agrin (SEA) domain agrin sea urchin-enterokinase-agrin (SEA) domain OGER Site agrin O00468 domain These two subunits are generated by autoproteolysis of a monomeric precursor within a distinctive protein motif called sea urchin-enterokinase-agrin (SEA) domain, yet the purpose of this cleavage and heterodimer creation is uncertain. 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. 22588082 2 8 part_of contain 333:339 arg1 >40 human proteins AND the TSR consensus sequence >40 human proteins the TSR consensus sequence Fterm Site proteins sequence The fucose transfer is catalysed by the protein O-fucosyltransferase 2 (POFUT2) and >40 human proteins contain the TSR consensus sequence for POFUT2-dependent fucosylation. 23260142 6 1 part_of HLA-DR 784:789 arg1 HLA-DR residues HLA HLA-DR residues OGER Site HLA residues Initially, incoming peptides have access to only part of the HLA-DR groove and need to compete with HLA-DR residues for access to the P2 site and the hydrophobic P1 pocket. 3458201 0 57 part_of alpha 36:40 arg1 Amino acid sequence alpha 1B-glycoprotein Amino acid sequence PUBTATOR Site alpha 1B-glycoprotein 1 sequence Amino acid sequence of human plasma alpha 1B-glycoprotein: homology to the immunoglobulin supergene family. 3463996 4 8 part_of B 815:815 arg1 procathepsin B sequences procathepsin B procathepsin B sequences Cterm Site procathepsin B 1508 sequences A comparison of procathepsin B sequences from three species (human, mouse, and rat) reveals that the homology between the propeptides is relatively conserved with a minimum of 68% sequence identity. 3463996 4 56 part_of procathepsin 802:813 arg1 procathepsin B sequences procathepsin B procathepsin B sequences Cterm Site procathepsin B 1508 sequences A comparison of procathepsin B sequences from three species (human, mouse, and rat) reveals that the homology between the propeptides is relatively conserved with a minimum of 68% sequence identity. 8489250 2 9 gly N-glycosylation 353:367 arg2 six potential N-glycosylation sites six potential N-glycosylation sites sites Peptide peptides containing six potential N-glycosylation sites were analyzed to determine that Asn residues 9, 34, 63, 73, 96, and 116 were utilized. 8489250 2 24 gly utilized 452:459 arg2 Asn residues 9, 34, 63, 73, 96, and 116 Asn residues 9, 34, 63, 73, 96, and 116 Asn residues 9, 34, 63, 73, 96, and 116 Peptide peptides containing six potential N-glycosylation sites were analyzed to determine that Asn residues 9, 34, 63, 73, 96, and 116 were utilized. 26536155 0 54 part_of Pronase 168:174 arg1 Pronase Treated Glycopeptides Pronase Pronase Treated Glycopeptides Fterm Site Pronase Glycopeptides Site-Specific Protein N- and O-Glycosylation Analysis by a C18-Porous Graphitized Carbon-Liquid Chromatography-Electrospray Ionization Mass Spectrometry Approach Using Pronase Treated Glycopeptides. 26536155 0 89 part_of Treated 176:182 arg1 Pronase Treated Glycopeptides Treated Pronase Treated Glycopeptides Cterm Site Treated Glycopeptides Site-Specific Protein N- and O-Glycosylation Analysis by a C18-Porous Graphitized Carbon-Liquid Chromatography-Electrospray Ionization Mass Spectrometry Approach Using Pronase Treated Glycopeptides. 17542669 2 33 part_of TSHR 298:301 arg1 the TSHR extracellular domain TSHR the TSHR extracellular domain PUBTATOR Site TSHR 7253 domain DESIGN A complex of part of the TSHR extracellular domain (amino acids 1-260; TSHR260) bound to M22 Fab was prepared and purified. 15003450 4 40 part_of domain 642:647 arg1 the active site domain the active site site The structure is a homodimer with each monomer containing a (beta/alpha)8 domain with the active site and an antiparallel beta domain. 15003450 4 50 part_of domain 589:594 arg1 the active site domain the active site site The structure is a homodimer with each monomer containing a (beta/alpha)8 domain with the active site and an antiparallel beta domain. 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. 24190431 2 30 part_of vimentin 336:343 arg1 vimentin epitopes vimentin vimentin epitopes PUBTATOR Site vimentin 7431 epitopes We show how citrullinated aggrecan and vimentin epitopes bind to HLA-DRB1*04:01/04. 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. 20511397 8 28 part_of apoE 1456:1459 arg1 the C terminus apoE the C terminus PUBTATOR Site apoE 348 terminus Given the importance of the C terminus of apoE in regulating apoE solubility, stability, and lipid binding, these results may have important implications for our understanding of apoE biochemistry. 25561468 8 17 part_of NTF 1238:1240 arg1 the NTF RESP18 homology domain NTF RESP18 the NTF RESP18 homology domain PUBTATOR Site NTF RESP18 389075 domain The signal for SG sorting is located within the NTF RESP18 homology domain (RESP18-HD), whereas soluble NTF is retained in the endoplasmic reticulum. 25561468 8 57 part_of RESP18 1242:1247 arg1 the NTF RESP18 homology domain NTF RESP18 the NTF RESP18 homology domain PUBTATOR Site NTF RESP18 389075 domain The signal for SG sorting is located within the NTF RESP18 homology domain (RESP18-HD), whereas soluble NTF is retained in the endoplasmic reticulum. 3342889 2 23 part_of contains 211:218 arg1 Cathepsin H AND 230 residues Cathepsin H 230 residues PUBTATOR Site Cathepsin H 1512 residues Cathepsin H contains 230 residues and has an Mr of 25116. 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. 6203908 7 70 part_of subunit 660:666 arg1 Cys-447 subunit Cys-447 OGER SpecificSite subunit P01023 Cys-447 Cys-447 probably forms an interchain bridge with Cys-447 from another subunit. 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. 17157876 3 10 part_of CPN1 676:679 arg1 the recombinant C-terminally truncated catalytic domain CPN1 the recombinant C-terminally truncated catalytic domain PUBTATOR Site CPN1 1369 domain We have prepared and crystallized the recombinant C-terminally truncated catalytic domain of human CPN1, and have determined and refined its 2.1 A crystal structure. 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. 18065761 7 34 part_of TSPN-1 1334:1339 arg1 the TSPN-1 domain TSPN-1 the TSPN-1 domain Cterm Site TSPN-1 domain The formation of cis and trans dimers of the TSPN-1 domain with relatively short segments of heparin further enhances the ability of TSP-1 to participate in high affinity binding to glycosaminoglycans. 30765605 3 40 part_of β2 469:470 arg1 The immunoglobulin domain 2 The immunoglobulin domain PUBTATOR Site 2 23545 domain The immunoglobulin domain of β2 interacts with the shoulder of the pore domain through a disulfide bond. 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. 25826155 4 55 part_of LLT1 590:593 arg1 the ectodomain LLT1 the ectodomain PUBTATOR Site LLT1 29121 ectodomain Here, we report the crystal structure of the ectodomain of LLT1. 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. 26811476 7 23 part_of glycoproteins 1285:1297 arg1 the sequence glycoproteins the sequence Fterm Site glycoproteins sequence This arrangement is required for filament formation and is directed by an ordered ZP-N/ZP-C linker that is not observed in ZP2 but is conserved in the sequence of deafness/Crohn's disease-associated homopolymeric glycoproteins α-tectorin (TECTA) and glycoprotein 2 (GP2). 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. 19528533 3 60 part_of region 688:693 arg1 a negatively charged residue region a negatively charged residue residue ZPI has an unusual shutter region with a negatively charged residue buried within the hydrophobic core of the molecule. 19528533 3 12 part_of has 665:667 arg1 ZPI AND an unusual shutter region ZPI an unusual shutter region PUBTATOR Site ZPI 51156 region ZPI has an unusual shutter region with a negatively charged residue buried within the hydrophobic core of the molecule. 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. 20944746 5 24 part_of domain 881:886 arg1 a single immunoglobulin-like domain domain a single immunoglobulin-like domain domain The pre-Tα chain comprised a single immunoglobulin-like domain that is structurally distinct from the constant (C) domain of the TCR α-chain; nevertheless, the mode of association between pre-Tα and TCRβ mirrored that mediated by the Cα-Cβ domains of the αβTCR. 20944746 5 72 part_of α-chain 899:905 arg1 the constant (C) domain TCR α- the constant (C) domain PUBTATOR Site TCR α- 28695 domain The pre-Tα chain comprised a single immunoglobulin-like domain that is structurally distinct from the constant (C) domain of the TCR α-chain; nevertheless, the mode of association between pre-Tα and TCRβ mirrored that mediated by the Cα-Cβ domains of the αβTCR. 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. 9722584 4 12 part_of has 492:494 arg1 The protein AND a putative signal peptide The protein a putative signal peptide Fterm Site protein peptide The protein has a putative signal peptide of 21 amino acids, and is a proform of two polypeptides. 22601780 5 58 part_of EGF 583:585 arg1 its 3 EGF domains 3 EGF its 3 EGF domains OGER Site 3 EGF P01133 domains We report the crystal structure of its 3 EGF domains. 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. 21138434 0 20 part_of subunit 75:81 arg1 N-glycosylated residues subunit N-glycosylated residues Fterm Site subunit residues The identification of N-glycosylated residues of the human 5-HT3B receptor subunit: importance for cell membrane expression. 3458201 6 13 part_of 1B 782:783 arg1 several domains alpha 1B several domains PUBTATOR Site alpha 1B 1 domains However, several domains of alpha 1B, especially the third, show statistically significant homology to variable regions of certain immunoglobulin light and heavy chains. 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. 18691975 4 51 part_of ICAM-5 682:687 arg1 the N-terminal two domains ICAM-5 the N-terminal two domains PUBTATOR Site ICAM-5 Q9UMF0 domains We describe the crystal structure of an engineered high-affinity I domain from the integrin alpha(L)beta(2) (LFA-1) alpha subunit in complex with the N-terminal two domains of ICAM-5, an adhesion molecule expressed in telencephalic neurons. 18691975 4 54 part_of subunit 628:634 arg1 an engineered high-affinity I domain subunit an engineered high-affinity I domain Fterm Site subunit domain We describe the crystal structure of an engineered high-affinity I domain from the integrin alpha(L)beta(2) (LFA-1) alpha subunit in complex with the N-terminal two domains of ICAM-5, an adhesion molecule expressed in telencephalic neurons. 15173186 12 22 part_of Toll-like 1842:1850 arg1 Toll-like receptor 2 glycosylation sites Toll-like receptor 2 Toll-like receptor 2 glycosylation sites PUBTATOR Site Toll-like receptor 2 7097 sites The remaining Toll-like receptor 2 glycosylation sites also contribute to efficient protein secretion, albeit to a lesser degree. 15173186 12 81 part_of receptor 1852:1859 arg1 Toll-like receptor 2 glycosylation sites Toll-like receptor 2 Toll-like receptor 2 glycosylation sites PUBTATOR Site Toll-like receptor 2 7097 sites The remaining Toll-like receptor 2 glycosylation sites also contribute to efficient protein secretion, albeit to a lesser degree. 22387313 3 26 part_of containing 497:506 arg1 DPP10 AND eight predicted N-glycosylation sites DPP10 eight predicted N-glycosylation sites PUBTATOR Site DPP10 57628 sites DPP10 is a glycoprotein containing eight predicted N-glycosylation sites in the extracellular domain. 22387313 3 26 part_of containing 497:506 arg1 a glycoprotein AND eight predicted N-glycosylation sites a glycoprotein eight predicted N-glycosylation sites Fterm Site glycoprotein sites DPP10 is a glycoprotein containing eight predicted N-glycosylation sites in the extracellular domain. 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. 21148085 5 12 part_of VEGFR-2 749:755 arg1 VEGFR-2 interacting residues VEGFR-2 VEGFR-2 interacting residues PUBTATOR Site VEGFR-2 3791 residues Comparison of the VEGF-D and VEGF-C structures shows similar extended N-terminal helices, conserved overall folds, and VEGFR-2 interacting residues. 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. 14699159 5 58 part_of p90ATF6 1119:1125 arg1 the carboxyl terminus p90ATF6 the carboxyl terminus Cterm Site p90ATF6 22926 terminus By mutating a single amino acid within the N-linked glycosylation site closest to the carboxyl terminus of p90ATF6, we recreated ATF6(f). 21056543 6 7 gly Thr20 1101:1105 arg1 NeuAcGalGalNAc Thr20 NeuAcGalGalNAc Thr20 Furthermore, we have provided experimental evidence that PCI in both individuals is O-glycosylated on Thr20 with a core type 1 O-glycan, which is mostly NeuAcGalGalNAc. 21056543 6 7 gly Thr20 1101:1105 arg1 a core type 1 O-glycan Thr20 a core type 1 O-glycan Thr20 Furthermore, we have provided experimental evidence that PCI in both individuals is O-glycosylated on Thr20 with a core type 1 O-glycan, which is mostly NeuAcGalGalNAc. 21056543 6 15 gly O-glycosylated 1083:1096 arg1 PCI Thr20 PCI Thr20 Furthermore, we have provided experimental evidence that PCI in both individuals is O-glycosylated on Thr20 with a core type 1 O-glycan, which is mostly NeuAcGalGalNAc. 21056543 6 15 gly O-glycosylated 1083:1096 arg1 Thr20 Thr20 Thr20 Furthermore, we have provided experimental evidence that PCI in both individuals is O-glycosylated on Thr20 with a core type 1 O-glycan, which is mostly NeuAcGalGalNAc. 21056543 6 15 gly O-glycosylated 1083:1096 arg1 Thr20 Thr20 PCI Thr20 Furthermore, we have provided experimental evidence that PCI in both individuals is O-glycosylated on Thr20 with a core type 1 O-glycan, which is mostly NeuAcGalGalNAc. 11741940 1 101 part_of contains 239:246 arg1 Secreted Frizzled-related protein-1 AND an N-terminal domain Secreted Frizzled-related protein-1 domain PUBTATOR Site Secreted Frizzled-related protein-1 6422 domain Secreted Frizzled-related protein-1 (sFRP-1), a soluble protein that binds to Wnts and modulates Wnt signaling, contains an N-terminal domain homologous to the putative Wnt-binding site of Frizzled (Fz domain) and a C-terminal heparin-binding domain with weak homology to netrin. 11741940 1 101 part_of contains 239:246 arg1 a soluble protein AND an N-terminal domain protein domain Fterm Site protein domain Secreted Frizzled-related protein-1 (sFRP-1), a soluble protein that binds to Wnts and modulates Wnt signaling, contains an N-terminal domain homologous to the putative Wnt-binding site of Frizzled (Fz domain) and a C-terminal heparin-binding domain with weak homology to netrin. 11741940 1 101 part_of contains 239:246 arg1 sFRP-1 AND an N-terminal domain sFRP-1 domain PUBTATOR Site sFRP-1 6422 domain Secreted Frizzled-related protein-1 (sFRP-1), a soluble protein that binds to Wnts and modulates Wnt signaling, contains an N-terminal domain homologous to the putative Wnt-binding site of Frizzled (Fz domain) and a C-terminal heparin-binding domain with weak homology to netrin. 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. 21763278 8 47 part_of contained 840:848 arg1 recombinant pro-BNP AND recombinant pro-BNP recombinant pro-BNP recombinant pro-BNP 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. 28668641 1 3 part_of glycoprotein 128:139 arg1 three predicted glycosylation sites glycoprotein three predicted glycosylation sites Fterm Site glycoprotein sites Vaspin is a glycoprotein with three predicted glycosylation sites at asparagine residues located in proximity to the reactive center loop and close to domains that play important roles in conformational changes underlying serpin function. 18491227 2 26 part_of sites 352:356 arg1 E-cadherin E-cadherin sites PUBTATOR Site E-cadherin 999 sites In a previous study, we demonstrated that all of four potential N-glycosylation sites in E-cadherin are occupied by N-glycans in human breast carcinoma cells in vivo and the elimination of N-glycan at Asn-633 dramatically affected E-cadherin expression and made it degraded. 23139753 3 39 part_of WFDC 349:352 arg1 a conserved WFDC domain WFDC a conserved WFDC domain Cterm Site WFDC domain A WFDC protein has a conserved WFDC domain of 50 amino acids with eight conserved cystine residue. 23139753 3 30 part_of has 333:335 arg1 A WFDC protein AND a conserved WFDC domain A WFDC protein a conserved WFDC domain Fterm Site protein domain A WFDC protein has a conserved WFDC domain of 50 amino acids with eight conserved cystine residue. 29581294 5 42 part_of hLOXL2 731:736 arg1 the copper-binding site hLOXL2 the copper-binding site OGER Site hLOXL2 Q9Y4K0 site Unexpectedly, the copper-binding site of hLOXL2 is occupied by zinc, which blocks LTQ generation and the enzymatic activity of hLOXL2 in our in vitro assay. 9748270 2 5 part_of XVII 143:146 arg1 The cDNA sequence XVII The cDNA sequence Cterm Site XVII sequence The cDNA sequence of human collagen XVII predicts an unusual type II transmembrane protein, but a biochemical characterization of this structure has not been accomplished yet. 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. 3463996 5 65 part_of sequences 1014:1022 arg1 the propeptide sequences the propeptide propeptide In particular, two conserved sequences in the propeptide that may be functionally significant include a potential glycosylation site and the presence of a single cysteine at position 59. 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 Ser-61 a tetrasaccharide O-fucosidically Ser-61 We now have evidence of another modification in the first EGF-like domain of human factor IX, which proved to be a tetrasaccharide O-fucosidically linked to Ser-61. 24121512 4 9 part_of AE1 955:957 arg1 the cytosolic domain AE1 the cytosolic domain PUBTATOR Site AE1 6521 domain Introduction of single and double mutations at the equivalent arginine (Arg(283)) and at an interacting glutamate (Glu(85)) in the cytosolic domain of human AE1 (cdAE1) had no effect on the cell surface expression or the transport activity of AE1 expressed in HEK-293 cells. 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. 21138434 4 17 part_of sequences 901:909 arg1 the h5-HT3B subunit 5-HT3B subunit sequences PUBTATOR Site 5-HT3B subunit 9177 sequences Disruption of each consensus N-glycosylation sequences in the h5-HT3B subunit (N31S, N75S, N117S, N147S and N182S) resulted in a reduced molecular weight (by ∼ 2-4 kDa) of each mutant when expressed by HEK293 cells stably expressing the h5-HT3A subunit. 16445295 7 61 gly attached 1108:1115 arg1 Asn22 AND the glycan Asn22 the glycan Asn22 Four of the glycans, Asn51, Asn63, Asn86, and Asn219 displayed microheterogeneity, while the glycan attached to Asn22 appeared to be homogeneous. 22718755 8 49 part_of ALK1 1148:1151 arg1 the extracellular domains ALK1 the extracellular domains PUBTATOR Site ALK1 94 domains We also report the crystal structure of a fully assembled ternary complex of BMP9 with the extracellular domains of ALK1 and ActRIIB. 22718755 8 52 part_of ActRIIB 1157:1163 arg1 the extracellular domains ActRIIB the extracellular domains PUBTATOR Site ActRIIB 93 domains We also report the crystal structure of a fully assembled ternary complex of BMP9 with the extracellular domains of ALK1 and ActRIIB. 21569239 3 9 part_of found 518:522 arg2 amphiF-spondin AND The FS domain amphiF-spondin The FS domain Fterm Site amphiF-spondin 10418 domain The FS domain is found in F-spondins, mindins, M-spondin and amphiF-spondin. 21569239 3 9 part_of found 518:522 arg2 M-spondin AND The FS domain M-spondin The FS domain PUBTATOR Site M-spondin 10417 domain The FS domain is found in F-spondins, mindins, M-spondin and amphiF-spondin. 8670172 9 96 part_of Asn-18 1358:1363 arg1 CD59u CD59u Asn-18 Cterm SpecificSite CD59u P13987 Asn-18 The N-linked carbohydrate side chain of CD59u (at Asn-18) also displayed considerable heterogeneity. 29666272 1 27 gly Asn-linked 127:136 arg1 Asn-linked oligosaccharides Asn Asn-linked oligosaccharides Asn Asn-linked oligosaccharides are extensively modified during transit through the secretory pathway, first by trimming of the nascent glycan chains and subsequently by initiating and extending multiple oligosaccharide branches from the trimannosyl glycan core. 15628971 1 82 part_of position 183:190 arg1 chondroitin chondroitin position Fterm Site chondroitin position 4 C4ST-1 (chondroitin 4-sulphotransferase-1) transfers sulphate to position 4 of N-acetylgalactosamine in chondroitin. 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. 27349982 2 3 part_of ASM 369:371 arg1 the ASM polypeptide ASM the ASM polypeptide PUBTATOR Site ASM 6609 polypeptide While other lysosomal sphingolipid hydrolases require a saposin activator protein for full activity, the ASM polypeptide incorporates a built-in N-terminal saposin domain and does not require an external activator protein. 21805521 8 109 part_of huDKK1 1558:1563 arg1 the huDKK1 N-terminal domain huDKK1 the huDKK1 N-terminal domain Cterm Site huDKK1 22943 domain The five disulfide bonds within the huDKK1 N-terminal domain are unique to the DKK family proteins; there are no exact matches in disulfide positioning when compared to other known disulfide clusters. 17157876 2 85 part_of CPN1 563:566 arg1 a 48 to 55 kDa catalytic (CPN1) domain CPN1 a 48 to 55 kDa catalytic (CPN1) domain PUBTATOR Site CPN1 1369 domain Normally, CPN circulates in blood plasma as a hetero-tetramer consisting of two 83 kDa (CPN2) domains each flanked by a 48 to 55 kDa catalytic (CPN1) domain. 8172892 6 50 gly alpha-D4 993:1000 arg1 Component sugar and sialic acid analyses AP alpha Component sugar and sialic acid analyses PUBTATOR AP alpha 2028 Component sugar and sialic acid analyses of AP alpha-D4 and AP alpha-D5 revealed that they contained 1 mol each of N-acetyl-D-galactosamine (GalNAc), D-galactose (Gal), and sialic acid. 8172892 6 95 gly alpha-D5 1009:1016 arg1 Component sugar and sialic acid analyses AP alpha Component sugar and sialic acid analyses PUBTATOR AP alpha 2028 Component sugar and sialic acid analyses of AP alpha-D4 and AP alpha-D5 revealed that they contained 1 mol each of N-acetyl-D-galactosamine (GalNAc), D-galactose (Gal), and sialic acid. 11533490 2 14 part_of receptor 417:424 arg1 the extracellular domain NP receptor the extracellular domain PUBTATOR Site NP receptor 4883 domain We report the hormone-binding thermodynamics and crystal structures at 2.9 and 2.0 angstroms, respectively, of the extracellular domain of the unliganded human NP receptor (NPR-C) and its complex with CNP, a 22-amino acid NP. 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). 6203908 4 24 part_of contain 209:215 arg1 The identical subunits AND 1451 amino acid residues The identical subunits 1451 amino acid residues OGER Site subunits P01023 residues The identical subunits contain 1451 amino acid residues. 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. 8617200 6 3 part_of LTBP-1 1028:1033 arg1 The N-terminal region LTBP-1 The N-terminal region PUBTATOR Site LTBP-1 4052 region The N-terminal region of LTBP-1 consisting of the first 400 amino acids was found to associate covalently with the ECM. 9689040 1 12 part_of fibrinogen-420 142:155 arg1 a recombinant alphaEC domain fibrinogen a recombinant alphaEC domain PUBTATOR Site fibrinogen 2244 domain The crystal structure of a recombinant alphaEC domain from human fibrinogen-420 has been determined at a resolution of 2.1 A. 8069634 13 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. 2226832 1 25 part_of CAP37 208:212 arg1 the amino acid sequence CAP37 the amino acid sequence PUBTATOR Site CAP37 566 sequence We report the amino acid sequence of CAP37, a human neutrophil granule protein with antibacterial and monocyte-specific chemotactic activity. 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. 16445295 10 54 part_of contains 1373:1380 arg1 TAFI AND eight cysteine residues TAFI eight cysteine residues PUBTATOR AminoAcid TAFI 1361 cysteine residues TAFI contains eight cysteine residues, of which two, Cys69 and Cys383, are not involved in disulfides and contain free sulfhydryl groups. 10419520 7 61 part_of S2P 1074:1076 arg1 S2P face the cytosol S2P S2P face the cytosol OGER Site S2P O43462 face Both the NH(2) and COOH termini of S2P face the cytosol. 12527193 8 61 part_of have 1162:1165 arg1 Mouse and human CRB3 AND identical intracellular domains CRB3 domains PUBTATOR Site CRB3 92359 domains Mouse and human CRB3 have identical intracellular domains but divergent extracellular domains except for a conserved N-glycosylation site. 20693656 1 40 part_of phosphatase 206:216 arg1 the functional sites phosphatase the functional sites Fterm Site phosphatase sites In order to gain deeper insights into the functional sites of human placental alkaline phosphatase, the structures of the enzyme with the putative regulators L-Phe, pNPP and 5'-AMP [Llinas et al. (2005), J. Mol. 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. 17286803 9 24 part_of CLN3 1209:1212 arg1 cytoplasmic tails CLN3 cytoplasmic tails OGER Site CLN3 Q13286 tails Alteration of the spacing between the transmembrane domain and the CAAX motif or the substitution of the entire C-terminal domain of CLN3 with cytoplasmic tails of mannose 6-phosphate receptors have demonstrated the importance of the C-terminal domain of proper length and composition for exit of the endoplasmic reticulum. 17286803 9 40 part_of CLN3 1209:1212 arg1 the entire C-terminal domain CLN3 the entire C-terminal domain OGER Site CLN3 Q13286 domain Alteration of the spacing between the transmembrane domain and the CAAX motif or the substitution of the entire C-terminal domain of CLN3 with cytoplasmic tails of mannose 6-phosphate receptors have demonstrated the importance of the C-terminal domain of proper length and composition for exit of the endoplasmic reticulum. 23695682 6 16 part_of IL-17A 861:866 arg1 the second, symmetry-related receptor site IL-17A the second, symmetry-related receptor site PUBTATOR Site IL-17A Q16552 site Binding to IL-17RA at one side of the IL-17A molecule induces a conformational change in the second, symmetry-related receptor site of IL-17A. 23695682 6 32 part_of receptor 844:851 arg1 the second, symmetry-related receptor site receptor the second, symmetry-related receptor site Fterm Site receptor site Binding to IL-17RA at one side of the IL-17A molecule induces a conformational change in the second, symmetry-related receptor site of IL-17A. 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. 8636209 9 31 part_of gamma 1147:1151 arg1 the TM domain CD3 gamma the TM domain PUBTATOR Site CD3 gamma 917 domain Site-directed mutagenesis of the acidic amino acid in the TM domain of CD3 gamma demonstrated that this residue is involved in TCR assembly probably by binding to Ti beta. 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). 20505120 4 34 part_of EphA2 476:480 arg1 the complete EphA2 ectodomain EphA2 the complete EphA2 ectodomain PUBTATOR Site EphA2 1969 ectodomain Here we present high-resolution structures of the complete EphA2 ectodomain and complexes with ephrin-A1 and A5 as the base unit of an Eph cluster. 21525977 3 29 part_of NPC1L1 438:443 arg1 the N-terminal domain NPC1L1 the N-terminal domain PUBTATOR Site NPC1L1 29881 domain PRINCIPAL FINDINGS Here we present the 2.8 Å crystal structure of the N-terminal domain (NTD) of NPC1L1 in the absence of cholesterol. 19880749 3 45 part_of ADAMTS13 455:462 arg1 an exosite-containing human ADAMTS13 fragment ADAMTS13 an exosite-containing human ADAMTS13 fragment PUBTATOR Site ADAMTS13 11093 fragment Here, we determined 2 crystal structures of ADAMTS13-DTCS (residues 287-685), an exosite-containing human ADAMTS13 fragment, at 2.6-A and 2.8-A resolution. 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. 10022822 3 26 part_of type-1 523:528 arg1 the thyroglobulin type-1 domains thyroglobulin type-1 the thyroglobulin type-1 domains OGER Site thyroglobulin type-1 P01266 domains The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L. 10022822 3 42 part_of thyroglobulin 509:521 arg1 the thyroglobulin type-1 domains thyroglobulin type-1 the thyroglobulin type-1 domains OGER Site thyroglobulin type-1 P01266 domains The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L. 10022822 3 43 part_of p41 476:478 arg1 the p41 fragment structure of the p41 the p41 fragment Cterm Site structure of the p41 fragment The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L. 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. 23756652 3 25 part_of furin-like 521:530 arg1 two adjacent furin-like cysteine-rich domains furin two adjacent furin-like cysteine-rich domains OGER Site furin P09958 domains Here we report the complex structure of the LGR4 extracellular domain (ECD) with the RSPO1 N-terminal fragment (RSPO1-2F) containing two adjacent furin-like cysteine-rich domains (FU-CRDs). 23756652 3 27 part_of RSPO1 460:464 arg1 the RSPO1 N-terminal fragment RSPO1 the RSPO1 N-terminal fragment PUBTATOR Site RSPO1 284654 fragment Here we report the complex structure of the LGR4 extracellular domain (ECD) with the RSPO1 N-terminal fragment (RSPO1-2F) containing two adjacent furin-like cysteine-rich domains (FU-CRDs). 23756652 3 40 part_of containing 497:506 arg1 the RSPO1 N-terminal fragment AND two adjacent furin-like cysteine-rich domains RSPO1 domains OGER Site RSPO1 Q2MKA7 domains Here we report the complex structure of the LGR4 extracellular domain (ECD) with the RSPO1 N-terminal fragment (RSPO1-2F) containing two adjacent furin-like cysteine-rich domains (FU-CRDs). 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. 10066782 0 17 part_of receptor 106:113 arg1 the extracellular domain interleukin-6 receptor the extracellular domain PUBTATOR Site interleukin-6 receptor 3570 domain Disulfide bond structure and N-glycosylation sites of the extracellular domain of the human interleukin-6 receptor. 18420026 0 105 part_of glycoprotein 28:39 arg1 a single N-glycosylation site glycoprotein a single N-glycosylation site Fterm Site glycoprotein site Nectin-like molecule 1 is a glycoprotein with a single N-glycosylation site at N290KS which influences its adhesion activity. 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. 19805286 0 70 part_of anhydrase 81:89 arg1 the catalytic domain carbonic anhydrase IX the catalytic domain PUBTATOR Site carbonic anhydrase IX 768 domain Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX. 2775232 8 99 part_of domains 1616:1622 arg1 beta-subunits beta-subunits domains Fterm Site beta-subunits domains Some of the general features of the structure of GPIIb, such as the existence of distinct domains in the alpha- and beta-subunits, as well as the identification of well-defined points in its external topography, are discussed. 15863501 3 76 part_of sPLA 512:515 arg1 C-terminal domains sPLA(2)-III C-terminal domains PUBTATOR Site sPLA(2)-III 50487 domains In several if not all cell types, the N- and C-terminal domains of sPLA(2)-III were proteolytically removed, leading to the production of the form containing only the sPLA(2) domain, which could be further N-glycosylated at two consensus sites. 19153605 8 21 part_of mindin 886:891 arg1 The mindin FS domain mindin FS The mindin FS domain PUBTATOR Site mindin FS 10417 domain The mindin FS domain therefore represents a new integrin ligand. 19153605 8 50 part_of FS 893:894 arg1 The mindin FS domain mindin FS The mindin FS domain PUBTATOR Site mindin FS 10417 domain The mindin FS domain therefore represents a new integrin ligand. 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. 18065761 8 11 part_of TSPN-1 1524:1529 arg1 TSPN-1 domains TSPN-1 TSPN-1 domains Cterm Site TSPN-1 domains Dimer formation may also involve TSPN-1 domains from two separate TSP-1 molecules. 24374484 4 43 part_of enzyme 793:798 arg1 the entire extracellular domain enzyme the entire extracellular domain Fterm Site enzyme domain In this article, we report the expression, purification, and the crystallographic structure of the entire extracellular domain of this enzyme. 18559974 1 43 part_of fibrinolysis 149:160 arg1 a pro-metallocarboxypeptidase Thrombin-activatable fibrinolysis inhibitor a pro-metallocarboxypeptidase PUBTATOR AminoAcid Thrombin-activatable fibrinolysis inhibitor 1361 pro Thrombin-activatable fibrinolysis inhibitor (TAFI) is a pro-metallocarboxypeptidase that can be proteolytically activated (TAFIa). 18559974 1 47 part_of Thrombin-activatable 128:147 arg1 a pro-metallocarboxypeptidase Thrombin-activatable fibrinolysis inhibitor a pro-metallocarboxypeptidase PUBTATOR AminoAcid Thrombin-activatable fibrinolysis inhibitor 1361 pro Thrombin-activatable fibrinolysis inhibitor (TAFI) is a pro-metallocarboxypeptidase that can be proteolytically activated (TAFIa). 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. 22576872 0 18 part_of β 110:110 arg1 endogenous fragments amyloid β endogenous fragments PUBTATOR Site amyloid β 351 fragments An online nano-LC-ESI-FTICR-MS method for comprehensive characterization of endogenous fragments from amyloid β and amyloid precursor protein in human and cat cerebrospinal fluid. 22576872 0 89 part_of protein 134:140 arg1 endogenous fragments amyloid precursor protein endogenous fragments PUBTATOR Site amyloid precursor protein 351 fragments An online nano-LC-ESI-FTICR-MS method for comprehensive characterization of endogenous fragments from amyloid β and amyloid precursor protein in human and cat cerebrospinal fluid. 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. 16815919 7 70 part_of PLAP 1283:1286 arg1 the calcium-binding site PLAP the calcium-binding site PUBTATOR Site PLAP 250 site The use of the flexible and polarizable force-field TCPEp (topological and classical polarization effects for proteins) predicts that calcium or strontium has similar interaction energies at the calcium-binding site of PLAP. 11152692 11 64 part_of contains 1231:1238 arg1 The protein AND an N-glycosylation site protein site Fterm Site protein site The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54). 19901337 4 15 part_of receptor-binding 566:581 arg1 NL63-CoV spike protein receptor-binding domain receptor NL63-CoV spike protein receptor-binding domain Fterm Site receptor domain We determined the crystal structure of NL63-CoV spike protein receptor-binding domain (RBD) complexed with human ACE2. 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. 9883900 4 33 part_of IGFBP-5 574:580 arg1 Different fragments IGFBP-5 Different fragments PUBTATOR Site IGFBP-5 3488 fragments Different fragments of IGFBP-5 with molecular sizes from 12 to 25 kDa were identified. 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. 15385547 5 1 part_of contain 807:813 arg1 SPP AND a type I signal anchor sequence SPP a type I signal anchor sequence PUBTATOR Site SPP 81502 sequence Whereas SPPL2a, -2b, and -2c contain a signal sequence, SPP and SPPL3 contain a type I signal anchor sequence for initiation of protein translocation and membrane insertion. 15385547 5 1 part_of contain 807:813 arg1 SPPL3 AND a type I signal anchor sequence SPPL3 a type I signal anchor sequence PUBTATOR Site SPPL3 121665 sequence Whereas SPPL2a, -2b, and -2c contain a signal sequence, SPP and SPPL3 contain a type I signal anchor sequence for initiation of protein translocation and membrane insertion. 15385547 5 32 part_of contain 766:772 arg1 -2b AND a signal sequence Whereas SPPL2a, -2b, and -2c sequence PUBTATOR Site Whereas SPPL2a, -2b, and -2c 84888 sequence Whereas SPPL2a, -2b, and -2c contain a signal sequence, SPP and SPPL3 contain a type I signal anchor sequence for initiation of protein translocation and membrane insertion. 15385547 5 32 part_of contain 766:772 arg1 -2c AND a signal sequence Whereas SPPL2a, -2b, and -2c sequence PUBTATOR Site Whereas SPPL2a, -2b, and -2c 84888 sequence Whereas SPPL2a, -2b, and -2c contain a signal sequence, SPP and SPPL3 contain a type I signal anchor sequence for initiation of protein translocation and membrane insertion. 15385547 5 32 part_of contain 766:772 arg1 -2c AND a signal sequence Whereas SPPL2a, -2b, and -2c sequence PUBTATOR Site Whereas SPPL2a, -2b, and -2c 84888 sequence Whereas SPPL2a, -2b, and -2c contain a signal sequence, SPP and SPPL3 contain a type I signal anchor sequence for initiation of protein translocation and membrane insertion. 1472036 0 7 part_of receptor 110:117 arg1 the extracellular domain insulin receptor the extracellular domain OGER Site insulin receptor P06213 domain Identification of a disulfide bridge connecting the alpha-subunits of the extracellular domain of the insulin receptor. 19528533 6 6 part_of FXa 1348:1350 arg1 the gamma-carboxy-glutamic acid-containing domains FXa the gamma-carboxy-glutamic acid-containing domains PUBTATOR Site FXa 2159 domains As modeled in this study, the gamma-carboxy-glutamic acid-containing domains of PZ and FXa enable them to bind to the same phospholipid surfaces on platelet and other membranes, with optimal proximity for the inhibition of FXa by the complexed ZPI. 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 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. 9535843 2 53 part_of proteins 358:365 arg1 the amino acid sequence proteins the amino acid sequence Fterm Site proteins sequence Kyte-Doolittle analysis of the amino acid sequence of Trp proteins identifies seven hydrophobic regions (H1-H7) with potential of forming transmembrane segments. 16362042 7 62 part_of Gas6 991:994 arg1 Only the minor Gas6 binding site Gas6 Only the minor Gas6 binding site PUBTATOR Site Gas6 2621 site Only the minor Gas6 binding site is highly conserved in the other Axl family receptors, Sky/Tyro3 and Mer. 3877053 7 92 part_of XII 889:891 arg1 the predicted amino acid sequence factor XII the predicted amino acid sequence PUBTATOR Site factor XII P00748 sequence Within the predicted amino acid sequence of factor XII, we have identified three peptide bonds that are cleaved by kallikrein during the formation of beta-factor XIIa. 9030779 6 8 gly N-glycosylation 801:815 arg2 the two C-terminal N-glycosylation sites the two C-terminal N-glycosylation sites sites However, removal of the two C-terminal N-glycosylation sites inhibits the formation of mature enzyme. 20534510 4 41 part_of PDGFRbeta 674:682 arg1 the first three Ig domains PDGFRbeta the first three Ig domains PUBTATOR Site PDGFRbeta 5159 domains We also present the structure of the complex between PDGF-B and the first three Ig domains of PDGFRbeta, showing that two PDGF-B protomers clamp PDGFRbeta at their dimerization seam. 17018531 5 36 gly utilized 952:959 arg2 Asn-116 Asn-116 Asn-116 Mass spectrometric analysis revealed that of the three potential N-linked glycosylation sites present in the mature protein, Asn-19 is not utilized; Asn-39 is linked to an endoglycosidase H (Endo H)-sensitive oligosaccharide, and Asn-116 is variably utilized, either being unmodified or linked to Endo H-sensitive or Endo H-resistant oligosaccharides. 17018531 5 58 gly utilized 841:848 arg2 Asn-19 Asn-19 Asn-19 Mass spectrometric analysis revealed that of the three potential N-linked glycosylation sites present in the mature protein, Asn-19 is not utilized; Asn-39 is linked to an endoglycosidase H (Endo H)-sensitive oligosaccharide, and Asn-116 is variably utilized, either being unmodified or linked to Endo H-sensitive or Endo H-resistant oligosaccharides. 17018531 5 92 gly glycosylation 776:788 arg2 the three potential N-linked glycosylation sites the three potential N-linked glycosylation sites sites Mass spectrometric analysis revealed that of the three potential N-linked glycosylation sites present in the mature protein, Asn-19 is not utilized; Asn-39 is linked to an endoglycosidase H (Endo H)-sensitive oligosaccharide, and Asn-116 is variably utilized, either being unmodified or linked to Endo H-sensitive or Endo H-resistant oligosaccharides. 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. 30301806 5 51 part_of NAAA 877:880 arg1 the otherwise buried active site NAAA the otherwise buried active site PUBTATOR Site NAAA 27163 site Self-proteolysis exposes the otherwise buried active site of NAAA to allow catalysis. 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. 22848655 7 2 part_of Sema-PSI 1096:1103 arg1 RON Sema-PSI domains RON Sema-PSI RON Sema-PSI domains OGER Site RON Sema-PSI Q04912 domains Here, we report the structure of RON Sema-PSI domains at 1.85 Å resolution. 22848655 7 56 part_of RON 1092:1094 arg1 RON Sema-PSI domains RON Sema-PSI RON Sema-PSI domains OGER Site RON Sema-PSI Q04912 domains Here, we report the structure of RON Sema-PSI domains at 1.85 Å resolution. 7574684 0 39 part_of trkB 46:49 arg1 Extracellular domain trkB Extracellular domain PUBTATOR Site trkB 4915 domain Extracellular domain of neurotrophin receptor trkB: disulfide structure, N-glycosylation sites, and ligand binding. 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. 3550808 1 18 part_of elastase 101:108 arg1 The complete amino acid sequence neutrophil elastase The complete amino acid sequence PUBTATOR Site neutrophil elastase 1991 sequence The complete amino acid sequence of human neutrophil elastase has been determined. 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. 14718370 1 51 part_of protein 152:158 arg1 this highly conserved protein domain protein this highly conserved protein domain Fterm Site protein domain We expressed recombinant Cys subdomains in COS-7 cells to examine the role of this highly conserved protein domain in mucin biosynthesis. 18930737 11 24 part_of PIP 1489:1491 arg1 alpha1-alpha2 domains PIP alpha1-alpha2 domains PUBTATOR Site PIP 5304 domains On the perpendicular interface involving alpha1-alpha2 domains of ZAG and a loop of PIP, another salt bridge is formed. 18930737 11 76 part_of ZAG 1471:1473 arg1 alpha1-alpha2 domains ZAG alpha1-alpha2 domains PUBTATOR Site ZAG 563 domains On the perpendicular interface involving alpha1-alpha2 domains of ZAG and a loop of PIP, another salt bridge is formed. 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. 22333914 0 20 part_of novel 2:6 arg1 A novel evolutionarily conserved domain l A novel evolutionarily conserved domain PUBTATOR Site l 23218 domain A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis. 22333914 0 29 part_of conserved 23:31 arg1 A novel evolutionarily conserved domain d A novel evolutionarily conserved domain PUBTATOR Site d 23218 domain A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis. 21569239 4 5 part_of human 623:627 arg1 human F-spondin FS domain F-spondin human F-spondin FS domain PUBTATOR Site F-spondin 10418 domain RESULTS: We present the crystal structure of human F-spondin FS domain at 1.95Å resolution. 21569239 4 55 part_of F-spondin 629:637 arg1 human F-spondin FS domain F-spondin human F-spondin FS domain PUBTATOR Site F-spondin 10418 domain RESULTS: We present the crystal structure of human F-spondin FS domain at 1.95Å resolution. 8702538 6 81 part_of CD22 1059:1062 arg1 the first immunoglobulin domain CD22 the first immunoglobulin domain OGER Site CD22 P20273 domain We show that mutation of a single potential N-linked glycosylation site in the first immunoglobulin domain of CD22 completely abrogates ligand recognition. 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. 17989695 3 27 part_of Nrp2 541:544 arg1 Nrp2 fragments Nrp2 Nrp2 fragments PUBTATOR Site Nrp2 8828 fragments We report several crystal structures of Nrp1 and Nrp2 fragments alone and in complex with antibodies that selectively block either semaphorin or vascular endothelial growth factor (VEGF) binding. 8939990 3 23 part_of mac25 403:407 arg1 the human mac25 propeptide mac25 the human mac25 propeptide PUBTATOR Site mac25 3490 propeptide The deduced amino acid sequence of the human mac25 propeptide shares a 20-25% identity to human insulin-like growth factor-binding proteins (IGFBPs), suggesting that mac25 could be another member of the IGFBP family. 17157876 4 92 part_of transthyretin 938:950 arg1 an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain transthyretin an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain OGER Site transthyretin P02766 domain The structural analysis reveals that CPN1 has a pear-like shape, consisting of a 319 residue N-terminal catalytic domain and an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain, more resembling CPD-2 than CPM. 17157876 4 96 part_of TT 953:954 arg1 an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain TT an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain Cterm Site TT P02766 domain The structural analysis reveals that CPN1 has a pear-like shape, consisting of a 319 residue N-terminal catalytic domain and an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain, more resembling CPD-2 than CPM. 27391701 9 42 part_of protein 1555:1561 arg1 short protein binding regions protein short protein binding regions Fterm Site protein regions Accordingly, IDPs were highly enriched in short protein binding regions called Molecular Recognition Features (MoRFs). 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. 2141278 5 6 part_of plasmin-cleavage 1348:1363 arg1 the other plasmin-cleavage fragments plasmin the other plasmin-cleavage fragments PUBTATOR Site plasmin 5340 fragments As measured by equilibrium dialysis, native alpha 2, like the other plasmin-cleavage fragments, did not retain the ability of intact C1-s to bind Ca2+. 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. 8489250 2 34 part_of Peptide 311:317 arg1 Peptide peptides Peptide Peptide peptides OGER Site Peptide peptides Peptide peptides containing six potential N-glycosylation sites were analyzed to determine that Asn residues 9, 34, 63, 73, 96, and 116 were utilized. 8489250 2 4 part_of containing 328:337 arg1 Peptide peptides AND six potential N-glycosylation sites Peptide peptides six potential N-glycosylation sites sites Peptide peptides containing six potential N-glycosylation sites were analyzed to determine that Asn residues 9, 34, 63, 73, 96, and 116 were utilized. 21606496 4 38 part_of 2B4 509:511 arg1 the extracellular domain 2B4 the extracellular domain OGER Site 2B4 Q9BZW8 domain Using a recombinant fusion protein of the extracellular domain of 2B4, we demonstrate that N-linked glycosylation of 2B4 is essential for the binding to its ligand CD48. 21768335 4 23 gly glycosylated 676:687 arg1 a glycosylated Fcγ receptor a glycosylated Fcγ receptor Cterm Fcγ In this study, the crystal structures of a glycosylated Fcγ receptor complexed with either afucosylated or fucosylated Fc were determined allowing a detailed, molecular understanding of the regulatory role of Fc-oligosaccharide core fucosylation in improving ADCC. 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. 12408961 3 44 part_of protein 394:400 arg1 protein sequences protein protein sequences Fterm Site protein sequences The predicted human and mouse protein sequences exhibit 35% identity with CREG protein. 9023546 0 33 part_of EGF 109:111 arg1 EGF domains EGF EGF domains PUBTATOR Site EGF 1950 domains Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains. 19196183 10 9 gly glycoproteins 1381:1393 arg1 the glycoproteins the glycoproteins Fterm glycoproteins Among the glycoproteins identified, alpha-fetoprotein, CD44 and laminin have been reported to be implicated in HCC and its metastasis. 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. 3877053 9 109 part_of region 1355:1360 arg1 factor XII factor XII region PUBTATOR Site factor XII P00748 region As the type II region of fibronectin contains a collagen-binding site, the homologous region in factor XII may be responsible for the binding of factor XII to collagen. 3877053 9 110 part_of fibronectin 1294:1304 arg1 the type II region fibronectin the type II region PUBTATOR Site fibronectin 2335 region As the type II region of fibronectin contains a collagen-binding site, the homologous region in factor XII may be responsible for the binding of factor XII to collagen. 3877053 9 72 part_of contains 1306:1313 arg1 the type II region AND a collagen-binding site the type II region a collagen-binding site site As the type II region of fibronectin contains a collagen-binding site, the homologous region in factor XII may be responsible for the binding of factor XII to collagen. 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. 9501084 1 47 part_of BM-40 223:227 arg1 The extracellular calcium-binding domain BM-40 The extracellular calcium-binding domain PUBTATOR Site BM-40 6678 domain The extracellular calcium-binding domain (positions 138-286) of the matrix protein BM-40 possesses a binding epitope of moderate affinity for several collagen types. 9501084 1 47 part_of BM-40 223:227 arg1 positions 138-286 BM-40 positions 138-286 PUBTATOR Site BM-40 6678 positions 138 The extracellular calcium-binding domain (positions 138-286) of the matrix protein BM-40 possesses a binding epitope of moderate affinity for several collagen types. 9501084 1 57 part_of possesses 229:237 arg1 the matrix protein BM-40 AND a binding epitope BM-40 epitope PUBTATOR Site BM-40 6678 epitope The extracellular calcium-binding domain (positions 138-286) of the matrix protein BM-40 possesses a binding epitope of moderate affinity for several collagen types. 1993171 10 9 part_of IL-4 1236:1239 arg1 the third and fifth cysteines IL-4 the third and fifth cysteines PUBTATOR AminoAcid IL-4 3565 cysteines Sequence analysis of the peptides containing the third and fifth cysteines of human IL-4 also demonstrated that only one of the potential N-glycosylation sites is used by C127 mammary tumor cells. 1993171 10 29 part_of containing 1186:1195 arg1 the peptides AND the third and fifth cysteines the peptides the third and fifth cysteines cysteines Sequence analysis of the peptides containing the third and fifth cysteines of human IL-4 also demonstrated that only one of the potential N-glycosylation sites is used by C127 mammary tumor cells. 29632068 4 11 part_of domain 664:669 arg1 a region domain a region region We previously demonstrated that substrate specificity resides in a region of ∼150 residues in the Tram-Lag-CLN8 domain. 29632068 4 27 part_of Tram-Lag-CLN8 650:662 arg1 the Tram-Lag-CLN8 domain Tram the Tram-Lag-CLN8 domain OGER Site Tram Q86XR7 domain We previously demonstrated that substrate specificity resides in a region of ∼150 residues in the Tram-Lag-CLN8 domain. 29632068 4 39 part_of region 619:624 arg1 the Tram-Lag-CLN8 domain region the Tram-Lag-CLN8 domain domain We previously demonstrated that substrate specificity resides in a region of ∼150 residues in the Tram-Lag-CLN8 domain. 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. 20534510 2 9 part_of region 333:338 arg1 their prodomain sequences region their prodomain sequences sequences We show that PDGFs share a conserved region in their prodomain sequences which can remain noncovalently associated with the mature cystine-knot growth factor domain after processing. 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). 12888274 7 38 part_of A 1058:1058 arg1 the active site arylsulfatase A the active site PUBTATOR Site arylsulfatase A 410 site The metal ion present in the active site of arylsulfatase A isolated from human placenta is Ca(2+) and not Mg(2+) as was found in the structure of the recombinant enzyme. 19252480 9 61 part_of residues 1481:1488 arg1 MD-2 MD-2 residues PUBTATOR AminoAcid MD-2 23643 residues in This structural shift allows phosphate groups of LPS to contribute to receptor multimerization by forming ionic interactions with a cluster of positively charged residues in TLR4 and MD-2. 19252480 9 61 part_of residues 1481:1488 arg1 TLR4 TLR4 residues PUBTATOR AminoAcid TLR4 7099 residues in This structural shift allows phosphate groups of LPS to contribute to receptor multimerization by forming ionic interactions with a cluster of positively charged residues in TLR4 and MD-2. 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. 22344443 4 1 part_of receptor 683:690 arg1 the transmembrane region receptor the transmembrane region Fterm Site receptor region Access is gained by ligands entering laterally between helices I and VII within the transmembrane region of the receptor. 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. 15099525 2 47 part_of ICAM-1 263:268 arg1 an entire ICAM-1 extracellular fragment ICAM-1 an entire ICAM-1 extracellular fragment PUBTATOR Site ICAM-1 3383 fragment Combined with the previously known N-terminal two-domain structure (D1D2), a model of an entire ICAM-1 extracellular fragment has been constructed. 17558413 2 13 part_of sites 259:263 arg1 proteins proteins sites Fterm Site proteins sites We describe a subtractive strategy to determine the sites of tyrosine O-sulfation in proteins. 17558413 2 39 part_of proteins 292:299 arg1 the sites proteins the sites Fterm Site proteins sites We describe a subtractive strategy to determine the sites of tyrosine O-sulfation in proteins. 1463457 5 20 gly N-glycosylation 909:923 arg2 13 potential N-glycosylation sites 13 potential N-glycosylation sites sites The predicted sequence has 552 amino acids with a leader peptide of 36 amino acids and contains 13 potential N-glycosylation sites, of which it is likely that 10 are used. 15657036 7 48 part_of containing 758:767 arg1 a calcium-binding protein AND an N-terminal (residues 86-168) and a C-terminal (residues 178-374) protease-resistant domain a calcium-binding protein an N-terminal (residues 86-168) and a C-terminal (residues 178-374) protease-resistant domain Fterm Site protein domain FGE is a calcium-binding protein containing an N-terminal (residues 86-168) and a C-terminal (residues 178-374) protease-resistant domain. 15657036 7 48 part_of containing 758:767 arg1 FGE AND an N-terminal (residues 86-168) and a C-terminal (residues 178-374) protease-resistant domain FGE an N-terminal (residues 86-168) and a C-terminal (residues 178-374) protease-resistant domain PUBTATOR Site FGE 285362 domain FGE is a calcium-binding protein containing an N-terminal (residues 86-168) and a C-terminal (residues 178-374) protease-resistant domain. 15809306 4 29 part_of Known 557:561 arg1 Known DPPIV dipeptides Known DPPIV Known DPPIV dipeptides PUBTATOR Site Known DPPIV 1803 dipeptides Known DPPIV dipeptides are cleaved by FAPalpha with an approximately 100-fold decrease in catalytic efficiency compared with DPPIV. 15809306 4 41 part_of DPPIV 563:567 arg1 Known DPPIV dipeptides Known DPPIV Known DPPIV dipeptides PUBTATOR Site Known DPPIV 1803 dipeptides Known DPPIV dipeptides are cleaved by FAPalpha with an approximately 100-fold decrease in catalytic efficiency compared with DPPIV. 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 Tyr10 Unexpectedly, we also identified a series of 27 glycopeptides, the Aβ1-X series, where X was 20 (DAEFRHDSGYEVHHQKLVFF), 19, 18, 17, 16, and 15, which were all uniquely glycosylated on Tyr10. 21712440 5 46 gly glycopeptides 1133:1145 arg2 27 glycopeptides 27 glycopeptides glycopeptides Unexpectedly, we also identified a series of 27 glycopeptides, the Aβ1-X series, where X was 20 (DAEFRHDSGYEVHHQKLVFF), 19, 18, 17, 16, and 15, which were all uniquely glycosylated on Tyr10. 11706042 3 10 part_of TLR4 500:503 arg1 the amino-terminal ectodomain TLR4 the amino-terminal ectodomain PUBTATOR Site TLR4 7099 ectodomain We demonstrate that MD-2 contains 2 N-glycosylated sites at positions Asn(26) and Asn(114), whereas the amino-terminal ectodomain of human TLR4 contains 9 N-linked glycosylation sites. 11706042 3 65 part_of contains 386:393 arg1 MD-2 AND 2 N-glycosylated sites MD-2 2 N-glycosylated sites PUBTATOR Site MD-2 23643 sites We demonstrate that MD-2 contains 2 N-glycosylated sites at positions Asn(26) and Asn(114), whereas the amino-terminal ectodomain of human TLR4 contains 9 N-linked glycosylation sites. 11706042 3 51 part_of contains 505:512 arg1 human TLR4 AND 9 N-linked glycosylation sites human TLR4 9 N-linked glycosylation sites PUBTATOR Site TLR4 7099 sites We demonstrate that MD-2 contains 2 N-glycosylated sites at positions Asn(26) and Asn(114), whereas the amino-terminal ectodomain of human TLR4 contains 9 N-linked glycosylation sites. 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. 26146185 2 1 part_of receptor 324:331 arg1 the N-terminal immunoglobulin superfamily (IgSF) domain receptor the N-terminal immunoglobulin superfamily (IgSF) domain Fterm Site receptor domain The membrane proximal domain of CD6 binds the N-terminal immunoglobulin superfamily (IgSF) domain of another cell surface receptor, CD166, which also engages in homophilic interactions. 26146185 2 41 part_of CD6 234:236 arg1 The membrane proximal domain CD6 The membrane proximal domain PUBTATOR Site CD6 923 domain The membrane proximal domain of CD6 binds the N-terminal immunoglobulin superfamily (IgSF) domain of another cell surface receptor, CD166, which also engages in homophilic interactions. 11081633 3 5 part_of EGF 614:616 arg1 the lectin and EGF (LE) domains EGF the lectin and EGF (LE) domains OGER Site EGF P01133 domains Here, we report crystal structures of human P- and E-selectin constructs containing the lectin and EGF (LE) domains co-complexed with SLe(X). 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. 12144777 6 8 part_of urease 1096:1101 arg1 the catalytic domain urease the catalytic domain Fterm Site urease domain The barrel and active-site architectures utilizing catalytic metal ions exhibit unexpected similarities to those of the murine adenosine deaminase and the catalytic domain of the bacterial urease. 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. 12906826 3 8 part_of beta 499:502 arg1 two domains alpha/beta hydrolase fold, and a beta two domains PUBTATOR Site alpha/beta hydrolase fold, and a beta 351 domains 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 8 part_of beta 499:502 arg1 a beta propeller domain alpha/beta hydrolase fold, and a beta a beta propeller domain PUBTATOR Site alpha/beta hydrolase fold, and a beta 351 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. 25765764 7 2 part_of LRIG1-3Ig 1067:1075 arg1 the LRIG1-3Ig domains LRIG1 the LRIG1-3Ig domains PUBTATOR Site LRIG1 Q96JA1 domains Similarly, neither the soluble LRIG1-LRR nor the LRIG1-3Ig domains nor the full-length LRIG1 co-expressed in HEK293 cells inhibited ligand-stimulated activation of cell-surface EGFR. 16476442 4 16 part_of sACE 715:718 arg1 the N domain ACE the N domain PUBTATOR Site ACE 1636 domain Previously we determined the structure of testis ACE (C domain); here we present the crystal structure of the N domain of sACE (both in the presence and absence of the antihypertensive drug lisinopril) in order to aid the understanding of how these two domains differ in specificity and function. 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. 11533490 4 7 part_of dimer 736:740 arg1 the membrane-proximal domains dimer the membrane-proximal domains Fterm Site dimer domains Hormone binding induces a 20 angstrom closure between the membrane-proximal domains of the dimer. 3524673 0 37 part_of factor 44:49 arg1 Amino acid sequence von Willebrand factor Amino acid sequence PUBTATOR Site von Willebrand factor 7450 sequence Amino acid sequence of human von Willebrand factor. 12970363 10 5 gly glycosylation 1397:1409 arg2 the e2 glycosylation site the e2 glycosylation site site Elimination of the e2 glycosylation site, missing in the monoglycosylated TRPC3, was sufficient to convert the tightly receptor-regulated TRPC6 into a constitutively active channel, displaying functional characteristics of TRPC3. 12970363 10 21 gly monoglycosylated 1432:1447 arg1 the monoglycosylated TRPC3 the monoglycosylated TRPC3 PUBTATOR TRPC3 7222 Elimination of the e2 glycosylation site, missing in the monoglycosylated TRPC3, was sufficient to convert the tightly receptor-regulated TRPC6 into a constitutively active channel, displaying functional characteristics of TRPC3. 18596036 0 25 part_of MASP-1/3 55:62 arg1 the CUB1-EGF-CUB2 domain MASP-1/3 the CUB1-EGF-CUB2 domain PUBTATOR Site MASP-1/3 5648 domain Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins. 18596036 0 36 part_of CUB1-EGF-CUB2 25:37 arg1 the CUB1-EGF-CUB2 domain EGF the CUB1-EGF-CUB2 domain PUBTATOR Site EGF 1950 domain Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins. 3123586 2 27 part_of apoC-III 194:201 arg1 The apoC-III polypeptide apoC-III The apoC-III polypeptide PUBTATOR Site apoC-III 345 polypeptide The apoC-III polypeptide contains a carbohydrate chain containing galactosamine, galactose, and sialic acid attached in O-linkage to a threonine residue at position 74. 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. 19737401 8 57 part_of BST-2 1136:1140 arg1 the BST-2 extracellular domain BST-2 the BST-2 extracellular domain PUBTATOR Site BST-2 684 domain Analysis of single, double, or triple cysteine mutants revealed that any one of three cysteine residues present in the BST-2 extracellular domain was sufficient for BST-2 dimerization, for inhibition of virus release, and sensitivity to Vpu. 12878160 9 48 part_of VIPL 1153:1156 arg1 the cytoplasmic tail VIPL the cytoplasmic tail PUBTATOR Site VIPL Q9H0V9 tail Like VIP36, the cytoplasmic tail of VIPL terminates in the sequence KRFY, a motif characteristic for proteins recycling between the ER and ERGIC/cis-Golgi. 1451807 1 0 gly O-glycosylation 65:79 arg2 Thr7 Thr7 Thr7 Variable O-glycosylation at Thr7, proteolytic processing, and allelic variation. 22660477 0 14 part_of GBR2 91:94 arg1 the extracellular domain GBR2 the extracellular domain Cterm Site GBR2 domain Structure and functional interaction of the extracellular domain of human GABA(B) receptor GBR2. 22664871 3 9 part_of N-terminal 489:498 arg1 the N-terminal fragment N-terminal the N-terminal fragment Cterm Site N-terminal fragment In this article, we report the 2.7-Å crystal structure of human RANKL trimer in complex with the N-terminal fragment of human OPG containing four cysteine-rich TNFR homologous domains (OPG-CRD). 22664871 3 44 part_of OPG 518:520 arg1 the N-terminal fragment OPG the N-terminal fragment PUBTATOR Site OPG 4982 fragment In this article, we report the 2.7-Å crystal structure of human RANKL trimer in complex with the N-terminal fragment of human OPG containing four cysteine-rich TNFR homologous domains (OPG-CRD). 22664871 3 12 part_of containing 522:531 arg1 human OPG AND four cysteine-rich TNFR homologous domains human OPG four cysteine-rich TNFR homologous domains PUBTATOR Site OPG 4982 domains In this article, we report the 2.7-Å crystal structure of human RANKL trimer in complex with the N-terminal fragment of human OPG containing four cysteine-rich TNFR homologous domains (OPG-CRD). 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. 15350125 0 39 part_of transporter 137:147 arg1 the extracellular binding domains apical sodium-dependent bile acid transporter the extracellular binding domains PUBTATOR Site apical sodium-dependent bile acid transporter 6555 domains Topology scanning and putative three-dimensional structure of the extracellular binding domains of the apical sodium-dependent bile acid transporter (SLC10A2). 21676880 4 19 gly glycosylation 811:823 arg1 the post-translational site the post-translational site site Mutations that ablate the co-translational site concomitantly reduce glycosylation at the post-translational site, resulting in unglycosylated KCNE1 subunits that cannot reach the cell surface with their cognate K(+) channel. 21676880 4 34 gly unglycosylated 870:883 arg1 unglycosylated KCNE1 subunits unglycosylated KCNE1 subunits PUBTATOR KCNE1 subunits 3753 Mutations that ablate the co-translational site concomitantly reduce glycosylation at the post-translational site, resulting in unglycosylated KCNE1 subunits that cannot reach the cell surface with their cognate K(+) channel. 20944746 9 2 part_of β-chain 1781:1787 arg1 both the V and C domains TCR β- both the V and C domains PUBTATOR Site TCR β- 28695 domains Accordingly, we provide a mechanism of pre-TCR self-association that allows the pre-Tα chain to simultaneously 'sample' the correct folding of both the V and C domains of any TCR β-chain, regardless of its ultimate specificity, which represents a critical checkpoint in T-cell development. 15809306 7 59 part_of Ala 1037:1039 arg1 FAPalpha FAPalpha Ala PUBTATOR SpecificSite FAPalpha 2191 Ala(657) Ala(657) in FAPalpha, instead of Asp(663) as in DP-PIV, reduces the acidity in this pocket, and this change could explain the lower affinity for N-terminal amines by FAPalpha. 1993171 10 3 gly used 1315:1318 arg2 the potential N-glycosylation sites the potential N-glycosylation sites sites Sequence analysis of the peptides containing the third and fifth cysteines of human IL-4 also demonstrated that only one of the potential N-glycosylation sites is used by C127 mammary tumor cells. 1993171 10 46 gly N-glycosylation 1290:1304 arg2 the potential N-glycosylation sites the potential N-glycosylation sites sites Sequence analysis of the peptides containing the third and fifth cysteines of human IL-4 also demonstrated that only one of the potential N-glycosylation sites is used by C127 mammary tumor cells. 16107205 3 21 gly glycosylation 708:720 arg1 Asn-243 Asn-243 Asn-243 Human DNase X, ectopically expressed in HeLa S3 cells, is located in the ER (endoplasmic reticulum) and is modified by an N-linked glycosylation at Asn-243. 11741940 6 81 part_of sFRP-1 1131:1136 arg1 an NTR-type domain sFRP-1 domain PUBTATOR Site sFRP-1 6422 domain This latter set of assignments provides experimental verification of one of the disulfide patterns proposed for netrin (NTR) modules and thereby supports the prediction that the C-terminal heparin-binding domain of sFRP-1 is an NTR-type domain. 9153399 6 9 part_of residue 1035:1041 arg1 fibronectin fibronectin residue PUBTATOR AminoAcid fibronectin 2335 aspartic acid residue The glutamic acid residue at position 37 is critical for LFA-1 binding and is proposed to coordinate the Mg2+ ion in the I domain; this Glu 37 is surrounded by a relatively flat recognition surface and lies in a beta-strand, whereas the critical aspartic acid residue in VCAM-1 and fibronectin lie in protruding loops. 9153399 6 9 part_of residue 1035:1041 arg1 VCAM-1 VCAM-1 residue PUBTATOR AminoAcid VCAM-1 7412 aspartic acid residue The glutamic acid residue at position 37 is critical for LFA-1 binding and is proposed to coordinate the Mg2+ ion in the I domain; this Glu 37 is surrounded by a relatively flat recognition surface and lies in a beta-strand, whereas the critical aspartic acid residue in VCAM-1 and fibronectin lie in protruding loops. 23050552 3 16 part_of contain 346:352 arg1 The beta and gamma subunits AND one N-glycosylation site The beta and gamma subunits one N-glycosylation site Fterm Site subunits site The beta and gamma subunits each contain one N-glycosylation site, each of which is occupied by a biantennary N-glycan. 22128166 5 25 part_of TIM 767:769 arg1 a catalytic TIM barrel domain TIM a catalytic TIM barrel domain OGER Site TIM Q9UNS1 domain Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. 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 Asn62 All components are N-glycosylated at Asn62; N-glycosylation does not contribute to heterogeneity. 12214108 3 9 part_of protein 414:420 arg1 residue 183 protein residue 183 Fterm SpecificSite protein residue 183 One pathogenic mutation, Thr to Ala at residue 183 of the human prion protein, blocks addition of the first glycan to the Asp residue 181. 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. 23050552 5 32 part_of fibrinogen 551:560 arg1 proteinase K-generated fibrinogen glycopeptides K-generated fibrinogen proteinase K-generated fibrinogen glycopeptides PUBTATOR Site K-generated fibrinogen 2244 glycopeptides Here, we make use of tryptic- and proteinase K-generated fibrinogen glycopeptides for the detailed analysis of the protein's O-glycosylation by combining information obtained from both one- and two-dimensional nanoLC-ESI-ion trap (IT)-MS approaches. 23050552 5 35 part_of K-generated 539:549 arg1 proteinase K-generated fibrinogen glycopeptides K-generated fibrinogen proteinase K-generated fibrinogen glycopeptides PUBTATOR Site K-generated fibrinogen 2244 glycopeptides Here, we make use of tryptic- and proteinase K-generated fibrinogen glycopeptides for the detailed analysis of the protein's O-glycosylation by combining information obtained from both one- and two-dimensional nanoLC-ESI-ion trap (IT)-MS approaches. 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. 7918467 7 32 part_of apoA-II 810:816 arg1 Cys6 apoA-II Cys6 PUBTATOR AminoAcid apoA-II 336 Cys6 Using a combination of manual Edman degradations and mass spectrometric analysis on a purified cluster of chymotryptic fragments, we identified an intramolecular disulfide bridge between Cys8 and Cys114 and an intermolecular bridge between Cys116 of apoD and Cys6 of apoA-II. 7918467 7 21 part_of apoD 793:796 arg1 Cys114 apoD Cys8 and Cys114 PUBTATOR AminoAcid apoD 347 Cys8 and Cys114 Using a combination of manual Edman degradations and mass spectrometric analysis on a purified cluster of chymotryptic fragments, we identified an intramolecular disulfide bridge between Cys8 and Cys114 and an intermolecular bridge between Cys116 of apoD and Cys6 of apoA-II. 22285761 9 63 part_of uPAR 1437:1440 arg1 uPAR DI-DII domains uPAR uPAR DI-DII domains PUBTATOR Site uPAR Q03405 domains The domain boundary between uPAR DI-DII domains is more flexible than the DII-DIII domain boundary. 3542030 11 14 part_of receptors 1461:1469 arg1 the cDNA-derived sequences receptors the cDNA-derived sequences Fterm Site receptors sequences The protein shows no homology either with the cDNA-derived sequences of the estrogen and glucocorticoid receptors found by others to be homologous with each other or with any other protein sequence in the 1986 data base. 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. 28011641 2 19 part_of Ca2+ 372:375 arg1 the Ca2+ coordination site Ca2 the Ca2+ coordination site OGER Site Ca2 P00918 site Crystal structures of P- and E-selectin suggest a two-state model in which ligand binding to the lectin domain closes loop 83-89 around the Ca2+ coordination site, enabling Glu-88 to engage Ca2+ and fucose. 25765764 2 46 part_of LRIG1 333:337 arg1 The two LRIG1 domains LRIG1 The two LRIG1 domains PUBTATOR Site LRIG1 Q96JA1 domains The two LRIG1 domains crystallised so that we have been able to determine the three-dimensional structures at 2.3Å resolution. 3542030 1 9 part_of protein 129:135 arg1 The amino acid sequence steroid binding protein The amino acid sequence PUBTATOR Site steroid binding protein 8991 sequence The amino acid sequence of the sex steroid binding protein (SBP) from human plasma has been determined. 26536155 5 15 gly glycoproteins 1218:1230 arg1 Pronase treated glycoproteins Pronase treated glycoproteins Fterm glycoproteins Here, we describe a universal workflow for site-specific N- and O-glycopeptide analysis of Pronase treated glycoproteins with integrated, sequential C18 reverse phase and porous graphitized carbon-LC-ESI-QTOF-MS/MS employing a combination of lower- and enhanced-energy collision-induced dissociation. 26536155 5 55 gly O-glycopeptide 1175:1188 arg2 O-glycopeptide analysis O-glycopeptide analysis O-glycopeptide Here, we describe a universal workflow for site-specific N- and O-glycopeptide analysis of Pronase treated glycoproteins with integrated, sequential C18 reverse phase and porous graphitized carbon-LC-ESI-QTOF-MS/MS employing a combination of lower- and enhanced-energy collision-induced dissociation. 12888562 8 43 gly glycosylated 1500:1511 arg1 the Cys399 the Cys399 Cys399 Neither the Cys399 nor Asn443 mutants were fully glycosylated, and both were retained in the endoplasmic reticulum. 12906826 2 7 part_of DPP-IV 318:323 arg1 the ectodomain DPP-IV the ectodomain PUBTATOR Site DPP-IV 1803 ectodomain We expressed and purified the ectodomain of human DPP-IV in Pichia pastoris and determined the X-ray structure at 2.1 A resolution. 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. 20145116 6 20 part_of VEGFR-2 840:846 arg1 the VEGFR-2 high-affinity-binding site VEGFR the VEGFR-2 high-affinity-binding site PUBTATOR Site VEGFR 3791 site Here we present the crystal structure of VEGF-C bound to the VEGFR-2 high-affinity-binding site, which consists of immunoglobulin homology domains D2 and D3. 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. 16732286 2 10 part_of Tie2 273:276 arg1 the Tie2 ligand-binding region Tie2 the Tie2 ligand-binding region PUBTATOR Site Tie2 7010 region Here we present the crystal structures of the Tie2 ligand-binding region alone and in complex with Ang2. 31959827 0 78 part_of IgA1 32:35 arg1 the IgA1 hinge region IgA1 the IgA1 hinge region PUBTATOR Site IgA1 P01876 region Analysis of O-glycoforms of the IgA1 hinge region by sequential deglycosylation. 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. 24121512 5 82 part_of AE1 1109:1111 arg1 the membrane domain AE1 the membrane domain PUBTATOR Site AE1 6521 domain In addition, the membrane domain of AE1 (mdAE1) efficiently mediated anion transport. 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. 3163150 0 26 part_of kallikrein--amino 14:30 arg1 Human urinary kallikrein--amino acid sequence kallikrein Human urinary kallikrein--amino acid sequence PUBTATOR Site kallikrein 9622 sequence Human urinary kallikrein--amino acid sequence and carbohydrate attachment sites. 1517205 2 62 part_of EGF-like 479:486 arg1 the first EGF-like domain EGF the first EGF-like domain OGER Site EGF P01133 domain We now have evidence of another modification in the first EGF-like domain of human factor IX, which proved to be a tetrasaccharide O-fucosidically linked to Ser-61. 1517205 2 77 part_of IX 511:512 arg1 the first EGF-like domain factor IX the first EGF-like domain OGER Site factor IX P00740 domain We now have evidence of another modification in the first EGF-like domain of human factor IX, which proved to be a tetrasaccharide O-fucosidically linked to Ser-61. 9153399 5 35 part_of ICAM-2 767:772 arg1 the extracellular region ICAM-2 the extracellular region PUBTATOR Site ICAM-2 3384 region Here we present the crystal structure of the extracellular region of ICAM-2. 2226832 0 31 part_of CAP37 23:27 arg1 Amino acid sequence CAP37 Amino acid sequence PUBTATOR Site CAP37 566 sequence Amino acid sequence of CAP37, a human neutrophil granule-derived antibacterial and monocyte-specific chemotactic glycoprotein structurally similar to neutrophil elastase. 22041449 7 8 part_of Ca 1285:1286 arg1 a Ca(2+) binding site Ca(2 a Ca(2+) binding site OGER Site Ca(2 P00918 site The structure reveals an overall architecture similar to that of laminin α chain LN domains but includes significant differences including a Ca(2+) binding site in the LN domain. 9539702 7 29 part_of ICAM-1 1300:1305 arg1 previously described I set domains ICAM-1 previously described I set domains PUBTATOR Site ICAM-1 3383 domains A subdivision of the intermediate (I) set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set. 9539702 7 29 part_of ICAM-1 1300:1305 arg1 domain 1 ICAM-1 domain 1 PUBTATOR Site ICAM-1 3383 domain A subdivision of the intermediate (I) set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set. 9539702 7 36 part_of ICAM-2 1391:1396 arg1 domain 2 ICAM-2 domain 2 PUBTATOR Site ICAM-2 3384 domain A subdivision of the intermediate (I) set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set. 9539702 7 38 part_of molecule-1 1426:1435 arg1 domain 2 vascular cell adhesion molecule-1 domain 2 PUBTATOR Site vascular cell adhesion molecule-1 7412 domain A subdivision of the intermediate (I) set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set. 9539702 7 72 part_of ICAM-1 1383:1388 arg1 domain 2 ICAM-1 domain 2 PUBTATOR Site ICAM-1 3383 domain A subdivision of the intermediate (I) set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set. 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. 22809326 11 2 part_of LAMP-2 1356:1361 arg1 the glycosylated luminal regions LAMP-2 the glycosylated luminal regions PUBTATOR Site LAMP-2 P13473 regions Computational models of the glycosylated luminal regions of LAMP-1 and LAMP-2 indicate that the proteins adopt a compact conformation in close proximity to the lysosomal membrane. 22809326 11 6 part_of LAMP-1 1345:1350 arg1 the glycosylated luminal regions LAMP-1 the glycosylated luminal regions PUBTATOR Site LAMP-1 3916 regions Computational models of the glycosylated luminal regions of LAMP-1 and LAMP-2 indicate that the proteins adopt a compact conformation in close proximity to the lysosomal membrane. 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. 24121512 3 45 part_of NBCe1 619:623 arg1 the cytosolic domain NBCe1 the cytosolic domain OGER Site NBCe1 Q9Y6R1 domain Mutation of a conserved arginine residue (R298S) in the cytosolic domain of NBCe1 (SLC4A4) is linked to proximal renal tubular acidosis and results in impaired transport function, suggesting that the cytosolic domain plays a role in substrate permeation. 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 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). 27033522 4 31 part_of Myc 602:604 arg1 Myc epitope Myc Myc epitope PUBTATOR Site Myc 4609 epitope To test if PEBP4 is secreted, we made constructs with Myc epitope at the amino (N) terminus or carboxyl (C) terminus to mask the signal sequence or keep it free, respectively. 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. 21199866 7 67 part_of ABCB6 1001:1005 arg1 The amino terminus ABCB6 The amino terminus PUBTATOR Site ABCB6 10058 terminus The amino terminus of ABCB6 has an additional highly conserved ER luminal cysteine (Cys-26). 21199866 7 31 part_of has 1007:1009 arg1 The amino terminus AND Cys-26 The amino terminus Cys-26 Cys-26 The amino terminus of ABCB6 has an additional highly conserved ER luminal cysteine (Cys-26). 21199866 7 31 part_of has 1007:1009 arg1 The amino terminus AND an additional highly conserved ER luminal cysteine The amino terminus an additional highly conserved ER luminal cysteine cysteine The amino terminus of ABCB6 has an additional highly conserved ER luminal cysteine (Cys-26). 25053408 4 69 part_of PCFT 682:685 arg1 the PCFT substrate binding domain PCFT the PCFT substrate binding domain PUBTATOR Site PCFT 113235 domain By structural homology to other solute carriers, TMD2 may form part of the PCFT substrate binding domain. 1544894 0 5 part_of XII 81:83 arg1 the first epidermal growth factor domain factor XII the first epidermal growth factor domain OGER Site factor XII P00748 domain O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system. 1544894 0 28 part_of C. 101:102 arg1 protein C. Epidermal growth factor (EGF) domains protein C protein C. Epidermal growth factor (EGF) domains OGER Site protein C P02810 domains O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system. 1544894 0 30 part_of protein 93:99 arg1 protein C. Epidermal growth factor (EGF) domains protein C protein C. Epidermal growth factor (EGF) domains OGER Site protein C P02810 domains O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system. 1544894 0 47 part_of factor 121:126 arg1 protein C. Epidermal growth factor (EGF) domains Epidermal growth factor protein C. Epidermal growth factor (EGF) domains PUBTATOR Site Epidermal growth factor 1950 domains O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system. 1544894 0 60 part_of found 146:150 arg2 many proteins AND the first epidermal growth factor domain many proteins the first epidermal growth factor domain Fterm Site proteins domain O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system. 1544894 0 60 part_of found 146:150 arg2 many proteins AND protein C. Epidermal growth factor (EGF) domains many proteins protein C. Epidermal growth factor (EGF) domains Fterm Site proteins domains O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system. 1544894 0 61 part_of factor 57:62 arg1 the first epidermal growth factor domain factor the first epidermal growth factor domain Fterm Site factor domain O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. Epidermal growth factor (EGF) domains are found in many proteins, particularly those of the coagulation/fibrinolytic system. 8757293 9 29 part_of PR3 1477:1479 arg1 The linear antigenic sites PR3 The linear antigenic sites PUBTATOR Site PR3 5657 sites The linear antigenic sites of PR3 reported to react with Wegener's granulomatosis autoantibodies occur in regions of the three-dimensional structure that may implicate the inactive pro-form of the enzyme in the pathogenesis of the disease. 20145116 13 54 part_of VEGFR-2 1656:1662 arg1 VEGFR-2 residues VEGFR-2 VEGFR-2 residues PUBTATOR Site VEGFR-2 3791 residues This biochemical analysis, together with our structural data, defined VEGFR-2 residues critical for the binding of VEGF-A and VEGF-C. 18930737 6 41 gly N-glycosylation 858:872 arg2 Asn77 Asn77 Asn77 The amino acid sequence of PIP contains one potential N-glycosylation site at Asn77, and the same is found glycosylated with four sugar residues. 18930737 6 41 gly N-glycosylation 858:872 arg2 one potential N-glycosylation site one potential N-glycosylation site site The amino acid sequence of PIP contains one potential N-glycosylation site at Asn77, and the same is found glycosylated with four sugar residues. 1517205 0 16 gly linked 55:60 arg1 serine 61 AND a tetrasaccharide serine 61 a tetrasaccharide serine 61 Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue. 1517205 0 64 gly has 16:18 arg1 Human factor IX AND a tetrasaccharide Human factor IX a tetrasaccharide OGER factor IX P00740 Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue. 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. 15728350 2 3 part_of ICAM-3 317:322 arg1 the ICAM-3 N-terminal domain structure of the ICAM-3 N-terminal the ICAM-3 N-terminal domain PUBTATOR Site structure of the ICAM-3 N-terminal 3385 domain We report a 1.65-A-resolution crystal structure of the ICAM-3 N-terminal domain (D1) in complex with the inserted domain, the ligand-binding domain of alphaLbeta2. 15728350 2 5 part_of N-terminal 324:333 arg1 the ICAM-3 N-terminal domain structure of the ICAM-3 N-terminal the ICAM-3 N-terminal domain PUBTATOR Site structure of the ICAM-3 N-terminal 3385 domain We report a 1.65-A-resolution crystal structure of the ICAM-3 N-terminal domain (D1) in complex with the inserted domain, the ligand-binding domain of alphaLbeta2. 3264725 6 106 part_of found 1243:1247 arg2 human plasma factor VIIa AND the 10 N-terminally located glutamic acid residues human plasma factor VIIa the 10 N-terminally located glutamic acid residues Cterm AminoAcid factor VIIa glutamic acid residues In human plasma factor VIIa, the 10 N-terminally located glutamic acid residues were found to be fully gamma-carboxylated whereas 9 full and 1 partial gamma-carboxylated residues were found in the corresponding positions of the recombinant factor VIIa molecule. 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 sites, Asn175 Of the three potential N-linked glycosylation sites, Asn175 was not glycosylated, whereas Asn88 was completely glycosylated, and Asn51 was partially glycosylated. 11080501 7 71 gly glycosylation 1443:1455 arg2 the three potential N-linked glycosylation sites the three potential N-linked glycosylation sites sites, Asn175 Of the three potential N-linked glycosylation sites, Asn175 was not glycosylated, whereas Asn88 was completely glycosylated, and Asn51 was partially glycosylated. 11080501 7 78 gly glycosylated 1560:1571 arg1 Asn51 Asn51 Asn51 Of the three potential N-linked glycosylation sites, Asn175 was not glycosylated, whereas Asn88 was completely glycosylated, and Asn51 was partially glycosylated. 11080501 7 97 gly glycosylated 1522:1533 arg1 Asn88 Asn88 Asn88 Of the three potential N-linked glycosylation sites, Asn175 was not glycosylated, whereas Asn88 was completely glycosylated, and Asn51 was partially glycosylated. 17400922 0 35 part_of ephrin-A5 31:39 arg1 the human ephrin-A5 ectodomain ephrin-A5 the human ephrin-A5 ectodomain PUBTATOR Site ephrin-A5 1946 ectodomain Crystal structure of the human ephrin-A5 ectodomain. 19153605 0 27 part_of F-spondin 17:25 arg1 the F-spondin domain structure of the F-spondin the F-spondin domain PUBTATOR Site structure of the F-spondin 10418 domain Structure of the F-spondin domain of mindin, an integrin ligand and pattern recognition molecule. 19153605 0 43 part_of mindin 37:42 arg1 the F-spondin domain mindin the F-spondin domain PUBTATOR Site mindin 10417 domain Structure of the F-spondin domain of mindin, an integrin ligand and pattern recognition molecule. 8702538 10 0 part_of position 1684:1691 arg1 the CD22 and CD33 glycoproteins CD33 glycoproteins position OGER Site CD33 glycoproteins P20138 position These observations suggest that a single N-linked glycosylation site located at a similar position in the CD22 and CD33 glycoproteins is critical for regulating ligand recognition by both receptors. 10756055 2 57 part_of sites 379:383 arg1 CXCR4 CXCR4 sites PUBTATOR Site CXCR4 7852 sites Here we report on the unexpected observation that the removal of the N-linked glycosylation sites in CXCR4 potentially allows the protein to serve as a universal coreceptor for both X4 and R5 laboratory-adapted and primary HIV-1 strains. 9628725 5 32 part_of beta-chain 905:914 arg1 the beta-chain domain beta-chain the beta-chain domain Fterm Site beta-chain domain Additionally, we have found that the beta-chain domain, like its gamma-chain counterpart, binds calcium. 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. 15738388 4 55 part_of cystatins 602:610 arg1 two topologically equivalent subdomains cystatins two topologically equivalent subdomains OGER Site cystatins P01036 subdomains Human latexin consists of two topologically equivalent subdomains, reminiscent of cystatins, consisting of an alpha-helix enveloped by a curved beta-sheet. 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. 16905106 6 12 part_of OX40L 804:808 arg1 the interfacial residues OX40L the interfacial residues PUBTATOR Site OX40L 7292 residues Site-directed changes of the interfacial residues of OX40L suggest this interface lacks a single "hot spot" and that instead, binding energy is dispersed over at least two distinct areas. 12646248 4 37 part_of protease 576:583 arg1 a serine protease domain protease a serine protease domain Fterm Site protease domain The molecule consists of a unique eight-bladed beta-propeller domain in the N-terminal region and a serine protease domain in the C-terminal region. 12646248 4 19 part_of domain 585:590 arg1 the C-terminal region region region The molecule consists of a unique eight-bladed beta-propeller domain in the N-terminal region and a serine protease domain in the C-terminal region. 12646248 4 36 part_of domain 531:536 arg1 the C-terminal region region region The molecule consists of a unique eight-bladed beta-propeller domain in the N-terminal region and a serine protease domain in the C-terminal region. 1472036 3 24 part_of containing 675:684 arg1 the peptide AND Cys524 the peptide Cys524 Cys524 The peptides containing Cys435 and Cys468 appeared in the same fraction, indicating that these two form a disulfide bond, and in another fraction we found the sequence of the peptide containing Cys524. 1472036 3 3 part_of containing 505:514 arg1 The peptides AND Cys468 Cys435 and Cys468 Cys435 and Cys468 The peptides containing Cys435 and Cys468 appeared in the same fraction, indicating that these two form a disulfide bond, and in another fraction we found the sequence of the peptide containing Cys524. 15385547 6 26 part_of contain 974:980 arg1 the transmembrane regions AND the catalytic residues the transmembrane regions the catalytic residues residues The hydrophilic loops joining the transmembrane regions, which contain the catalytic residues, are facing the exoplasm. 15961631 0 20 part_of receptor 37:44 arg1 human toll-like receptor 3 (TLR3) ectodomain toll-like receptor 3 human toll-like receptor 3 (TLR3) ectodomain PUBTATOR Site toll-like receptor 3 7098 ectodomain Crystal structure of human toll-like receptor 3 (TLR3) ectodomain. 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 Asn73 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. 22451694 0 26 part_of α5β1 21:24 arg1 α5β1 integrin ectodomain structure of α5 α5β1 integrin ectodomain Cterm Site structure of α5 ectodomain Crystal structure of α5β1 integrin ectodomain: atomic details of the fibronectin receptor. 3342889 4 6 part_of cathepsin 499:507 arg1 the propeptide cathepsin H the propeptide PUBTATOR Site cathepsin H 1512 propeptide The glycosylated mini chain is a proteolytic fragment of the propeptide of cathepsin H. Human cathepsin L has 217 amino acid residues and an Mr of 23720. 3342889 4 44 part_of has 530:532 arg1 Human cathepsin L AND 217 amino acid residues Human cathepsin L 217 amino acid residues PUBTATOR Site cathepsin L 1514 residues The glycosylated mini chain is a proteolytic fragment of the propeptide of cathepsin H. Human cathepsin L has 217 amino acid residues and an Mr of 23720. 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. 20145116 3 69 part_of receptor 512:519 arg1 the intracellular tyrosine kinase domain receptor the intracellular tyrosine kinase domain Fterm Site receptor domain Dimerization initiates transmembrane signaling, which activates the intracellular tyrosine kinase domain of the receptor. 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. 3886654 2 72 part_of XIIa 424:427 arg1 the previously determined sequence factor XIIa the previously determined sequence Cterm Site factor XIIa sequence Combining this sequence with the previously determined sequence of beta-factor XIIa (Fujikawa, K., and McMullen, B. A. (1983) J. Biol. 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. 11866528 5 17 part_of BST-1 617:621 arg1 the extracellular region BST-1 the extracellular region PUBTATOR Site BST-1 683 region We determined the crystal structures of the extracellular region of human BST-1 at atomic resolution in the free form and in complexes with five substrate analogues: nicotinamide, NMN, ATPgammaS, ethenoNADP, and ethenoNAD. 9539702 1 17 part_of 190-residue 122:132 arg1 a 190-residue fragment structure of a 190 a 190-residue fragment OGER Site structure of a 190 O95602 fragment The 3.0-A structure of a 190-residue fragment of intercellular adhesion molecule-1 (ICAM-1, CD54) reveals two tandem Ig-superfamily (IgSF) domains. 9539702 1 20 part_of molecule-1 169:178 arg1 a 190-residue fragment intercellular adhesion molecule-1 a 190-residue fragment PUBTATOR Site intercellular adhesion molecule-1 3383 fragment The 3.0-A structure of a 190-residue fragment of intercellular adhesion molecule-1 (ICAM-1, CD54) reveals two tandem Ig-superfamily (IgSF) domains. 25601083 3 20 part_of Fic 526:528 arg1 a Fic (filamentation induced by cAMP) domain Fic a Fic (filamentation induced by cAMP) domain Cterm Site Fic domain A family of enzymes, defined by the presence of a Fic (filamentation induced by cAMP) domain, catalyzes this adenylylation reaction. 22351761 3 24 part_of containing 572:581 arg1 a stable α-helical domain AND 14 conserved Cys residues a stable α-helical domain 14 conserved Cys residues Cys residues Glypican core proteins consist of a stable α-helical domain containing 14 conserved Cys residues followed by a glycosaminoglycan attachment domain that becomes exclusively substituted with heparan sulfate (HS) and presumably adopts a random coil conformation. 23056909 5 24 part_of ACE 1021:1023 arg1 the carboxy-terminal domain ACE the carboxy-terminal domain OGER Site ACE P12821 domain Moreover, Ang II showed selective competitive inhibition of the carboxy-terminal domain of human somatic ACE providing evidence for a regulatory role in the human renin-angiotensin system (RAS). 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). 9023546 4 72 part_of peptides 468:475 arg1 sequences peptides sequences sequences Synthetic peptides with sequences taken from five proteins previously shown to contain O-linked fucose (Harris and Spellman, 1993; Glycobiology, 3, 219-224) did not serve as efficient acceptor substrates. 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 N196, N410, and N428 We determined that glycans are added at three of four potential N-linked glycosylation sites: N196, N410, and N428. 19571171 3 66 gly three 470:474 arg1 N196 N196, N410, and N428 N196, N410, and N428 We determined that glycans are added at three of four potential N-linked glycosylation sites: N196, N410, and N428. 19571171 3 66 gly three 470:474 arg1 N196 N196, N410, and N428 N196, N410, and N428 We determined that glycans are added at three of four potential N-linked glycosylation sites: N196, N410, and N428. 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. 16445295 13 74 part_of TAFI 1844:1847 arg1 the TAFI amino acid sequence TAFI the TAFI amino acid sequence PUBTATOR Site TAFI 1361 sequence LC-MS/MS analyses covering more than 90% of the TAFI amino acid sequence revealed no additional modifications. 11741940 7 25 part_of protein 1470:1476 arg1 the Fz domain protein the Fz domain Fterm Site protein domain Interestingly, two subsets of sFRPs appear to have alternate disulfide linkage patterns compared with sFRP-1, one of which involves the loss of a disulfide due to deletion of a single cysteine from the NTR module, whereas the remaining cysteine may pair with a new cysteine introduced in the Fz domain of the protein. 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. 18585350 1 49 part_of amyloid-beta 219:230 arg1 cerebral amyloid-beta (Abeta) peptide deposition amyloid-beta cerebral amyloid-beta (Abeta) peptide deposition PUBTATOR Site amyloid-beta 351 position Alzheimer's disease (AD) is a genetically heterogeneous disorder characterized by early hippocampal atrophy and cerebral amyloid-beta (Abeta) peptide deposition. 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). 2071582 2 18 part_of preproenzyme 196:207 arg1 a 226-amino acid catalytic domain enzyme a 226-amino acid catalytic domain Fterm Site enzyme domain The protein-coding exons reveal a preproenzyme with a 19-amino acid signal peptide, an acidic 2-amino acid propeptide, and a 226-amino acid catalytic domain. 2071582 2 18 part_of preproenzyme 196:207 arg1 a 19-amino acid signal peptide enzyme a 19-amino acid signal peptide Fterm Site enzyme peptide The protein-coding exons reveal a preproenzyme with a 19-amino acid signal peptide, an acidic 2-amino acid propeptide, and a 226-amino acid catalytic domain. 2071582 2 18 part_of preproenzyme 196:207 arg1 an acidic 2-amino acid propeptide enzyme an acidic 2-amino acid propeptide Fterm Site enzyme propeptide The protein-coding exons reveal a preproenzyme with a 19-amino acid signal peptide, an acidic 2-amino acid propeptide, and a 226-amino acid catalytic domain. 18420026 7 26 gly glycosylation 1694:1706 arg2 the glycosylation site mutation the glycosylation site mutation site Cell aggregation assay further showed there was an increased adhesion activity after the glycosylation site mutation of NECL1 molecule. 22041449 6 17 part_of G2 1047:1048 arg1 the LN domain netrin G2 domain and domain PUBTATOR Site netrin G2 Q96CW9 domain and domain We determined the crystal structure for a fragment comprising the LN domain and domain LE1 of netrin G2 by sulfur single-wavelength anomalous diffraction phasing and refined it to 1.8 Å resolution. 22809326 14 79 part_of LAMP-2 1835:1840 arg1 the LAMP-1 and LAMP-2 luminal regions LAMP-2 the LAMP-1 and LAMP-2 luminal regions PUBTATOR LAMP-2 P13473 Insights into the structure of the lysosomal glycoprotein coat were obtained by computational models of the LAMP-1 and LAMP-2 luminal regions. 22809326 14 99 part_of LAMP-1 1824:1829 arg1 the LAMP-1 and LAMP-2 luminal regions LAMP-1 the LAMP-1 and LAMP-2 luminal regions PUBTATOR LAMP-1 3916 Insights into the structure of the lysosomal glycoprotein coat were obtained by computational models of the LAMP-1 and LAMP-2 luminal regions. 7682553 7 25 part_of bikunin 1152:1158 arg1 Ser10 bikunin Ser10 PUBTATOR AminoAcid bikunin 259 Ser10 Biochemical and mass spectrometric analysis of the peptides containing the cross-link indicate that it is mediated by a chondroitin-4-sulfate chain that originates from a typical O-glycosidic link to Ser10 of bikunin. 9030779 4 58 gly used 628:631 arg2 these sites these sites sites Evidence is presented that five of these sites are used. 11152678 1 1 part_of neurotrophic 186:197 arg1 pro-BDNF brain-derived neurotrophic factor precursor pro-BDNF PUBTATOR AminoAcid brain-derived neurotrophic factor precursor 627 pro We examined the biosynthesis and post-translational processing of the brain-derived neurotrophic factor precursor (pro-BDNF) in cells infected with a pro-BDNF-encoding vaccinia virus. 11152678 1 3 part_of factor 199:204 arg1 pro-BDNF brain-derived neurotrophic factor precursor pro-BDNF PUBTATOR AminoAcid brain-derived neurotrophic factor precursor 627 pro We examined the biosynthesis and post-translational processing of the brain-derived neurotrophic factor precursor (pro-BDNF) in cells infected with a pro-BDNF-encoding vaccinia virus. 11152678 1 51 part_of brain-derived 172:184 arg1 pro-BDNF brain-derived neurotrophic factor precursor pro-BDNF PUBTATOR AminoAcid brain-derived neurotrophic factor precursor 627 pro We examined the biosynthesis and post-translational processing of the brain-derived neurotrophic factor precursor (pro-BDNF) in cells infected with a pro-BDNF-encoding vaccinia virus. 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 Ser-2730 A single chondroitin 6-sulfate oligosaccharide unit Ser-2730 A single chondroitin 6-sulfate oligosaccharide unit at Ser-2730 of human thyroglobulin enhances hormone formation and limits proteolytic accessibility at the carboxyl terminus. 9722584 8 14 part_of NTPPHase 1114:1121 arg1 the NTPPHase region NTPPHase the NTPPHase region Fterm Site NTPPHase region In the precursor protein the NTPPHase region is immediately preceded by a tetrapeptide conforming to a furin proteinase cleavage consensus sequence. 9722584 8 55 part_of furin 1188:1192 arg1 a furin proteinase cleavage consensus sequence furin a furin proteinase cleavage consensus sequence OGER Site furin P09958 sequence In the precursor protein the NTPPHase region is immediately preceded by a tetrapeptide conforming to a furin proteinase cleavage consensus sequence. 20145116 9 8 part_of VEGFR-2 1236:1242 arg1 VEGFR-2 subdomains D2 and D3 VEGFR-2 VEGFR-2 subdomains D2 and D3 PUBTATOR Site VEGFR-2 3791 subdomains Our structure shows that two of these loops in VEGF-C bind to VEGFR-2 subdomains D2 and D3, while one interacts primarily with D3. 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. 19805286 6 17 part_of IX 870:871 arg1 two catalytic domains CA IX two catalytic domains PUBTATOR Site CA IX 768 domains Thus, two catalytic domains of CA IX associate to form a dimer, which is stabilized by the formation of an intermolecular disulfide bond. 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. 19153605 7 35 part_of FS 798:799 arg1 the FS domain FS the FS domain Cterm Site FS 10418 domain We demonstrated that the FS domain mediates integrin binding and identified the binding site by mutagenesis. 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. 19651138 0 25 part_of GluR2 25:29 arg1 the GluR2 amino-terminal domain GluR2 the GluR2 amino-terminal domain PUBTATOR Site GluR2 2891 domain Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors. 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). 15014436 3 40 part_of TSP-1 373:377 arg1 a cell-binding TSP-1 fragment TSP a cell-binding TSP-1 fragment PUBTATOR Site TSP 7057 fragment The crystal structure of a cell-binding TSP-1 fragment, spanning three T3 repeats and the CTD, reveals a compact assembly. 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. 17139081 7 45 part_of enzymes 1185:1191 arg1 the active-site residues enzymes the active-site residues Fterm Site enzymes residues Comparison of the structure of acid-beta-glucosidase with that of xylanase, a bacterial enzyme from a closely related protein family, demonstrates a close correspondence between the active-site residues of the two enzymes. 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. 20877282 3 87 part_of plexin 569:574 arg1 the plexin ectodomain plexin the plexin ectodomain Fterm Site plexin ectodomain In the absence of any structural information on the plexin ectodomain or its interaction with semaphorins the extracellular specificity and mechanism controlling plexin signalling has remained unresolved. 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. 21569239 2 3 part_of F-spondin 339:347 arg1 FS domain F-spondin domain PUBTATOR Site F-spondin 10418 domain The reelin_N domain and the F-spondin domain (FS domain) comprise a proteolytic fragment that interacts with the cell membrane and guides the projection of commissural axons to floor plate. 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. 21269602 3 52 part_of VE-cadherin 497:507 arg1 mammalian-produced VE-cadherin ectodomains VE-cadherin mammalian-produced VE-cadherin ectodomains PUBTATOR Site VE-cadherin 1003 ectodomains Here we report studies of mammalian-produced VE-cadherin ectodomains suggesting that, like other classical cadherins, VE-cadherin forms adhesive trans dimers between monomers located on opposing cell surfaces. 1569071 10 57 part_of IGF-II 1980:1985 arg1 the Ser66-Lys88 endoprotease-generated E domain peptides IGF-II the Ser66-Lys88 endoprotease-generated E domain peptides PUBTATOR Site IGF-II P01344 peptides When the Ser66-Lys88 endoprotease-generated E domain peptides from pI5.1 and 5.4 high Mr IGF-II were treated with the glycosidases, they had relative mobility changes during sodium dodecyl sulfate-polyacrylamide gel electrophoresis that were similar to those of the intact precursors. 21908432 6 20 part_of GPIbβ 822:826 arg1 residue Tyr106 GPIbβ, residue Tyr106 PUBTATOR AminoAcid GPIbβ, 2811 residue Tyr106 Central to this interface is residue Tyr106 from GPIbβ, which inserts into a pocket generated by 2 loops (b,c) from GPIX. 16186819 0 30 part_of thrombospondin-2 56:71 arg1 the calcium-rich signature domain thrombospondin-2 the calcium-rich signature domain PUBTATOR Site thrombospondin-2 7058 domain Structure of the calcium-rich signature domain of human thrombospondin-2. 1517205 3 42 part_of containing 605:614 arg1 Two large peptides AND positions 44-63 Two large peptides positions 44-63 positions 44 Two large peptides containing Ser-61 (positions 44-63), named hIX-GP1 and hIX-GP2, were first isolated from the lysyl endopeptidase-digest of human factor IX, by reversed-phase high performance liquid chromatography (HPLC). 1517205 3 42 part_of containing 605:614 arg1 Two large peptides AND Ser-61 Two large peptides Ser-61 Ser-61 Two large peptides containing Ser-61 (positions 44-63), named hIX-GP1 and hIX-GP2, were first isolated from the lysyl endopeptidase-digest of human factor IX, by reversed-phase high performance liquid chromatography (HPLC). 9722584 6 36 part_of has 905:907 arg1 CILP AND six putative N-glycosylation sites CILP six putative N-glycosylation sites PUBTATOR Site CILP 8483 sites CILP has 30 cysteines and six putative N-glycosylation sites. 9722584 6 36 part_of has 905:907 arg1 CILP AND 30 cysteines CILP 30 cysteines PUBTATOR AminoAcid CILP 8483 cysteines CILP has 30 cysteines and six putative N-glycosylation sites. 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. 22664871 5 14 part_of OPG-CRD 774:780 arg1 the CRD3 domain OPG the CRD3 domain PUBTATOR Site OPG 4982 domain A loop from the CRD3 domain of OPG-CRD inserts into the shallow groove of RANKL, providing the major binding determinant that is further confirmed by affinity measurement and osteoclast differentiation assay. 10419520 13 74 part_of S2P 1706:1708 arg1 the active site S2P the active site OGER Site S2P O43462 site The hydrophobicity of these sequences suggests that the active site of S2P is located within the membrane in an ideal position to cleave its target, a Leu-Cys bond in the first transmembrane helix of SREBPs. 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. 19561611 4 3 part_of HHIP 500:503 arg1 the human HHIP ectodomain HHIP the human HHIP ectodomain PUBTATOR Site HHIP Q96QV1 ectodomain We have solved a series of crystal structures for the human HHIP ectodomain and Desert hedgehog (DHH) in isolation, as well as HHIP in complex with DHH (HHIP-DHH) and Sonic hedgehog (Shh) (HHIP-Shh), with and without Ca2+. 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. 23878260 4 47 part_of VEGFR-3 795:801 arg1 VEGFR-3 domains D1-2 VEGFR-3 VEGFR-3 domains D1-2 PUBTATOR Site VEGFR-3 2324 domains Here we analyzed the crystal structures of VEGF-C in complex with VEGFR-3 domains D1-2 and of the VEGFR-3 D4-5 homodimer. 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. 6333684 0 42 part_of interleukin 65:75 arg1 Amino acid sequence interleukin 2 Amino acid sequence PUBTATOR Site interleukin 2 3558 sequence Amino acid sequence and post-translational modification of human interleukin 2. 15606899 1 32 part_of enzyme 323:328 arg1 the C-terminal cytosolic tail enzyme the C-terminal cytosolic tail Fterm Site enzyme tail Using a yeast two-hybrid system, we screened a human brain cDNA library for possible interacting proteins with the C-terminal cytosolic tail of the beta-secretase beta-amyloid protein converting enzyme (BACE)1. 15606899 1 37 part_of proteins 225:232 arg1 the C-terminal cytosolic tail proteins the C-terminal cytosolic tail Fterm Site proteins tail Using a yeast two-hybrid system, we screened a human brain cDNA library for possible interacting proteins with the C-terminal cytosolic tail of the beta-secretase beta-amyloid protein converting enzyme (BACE)1. 23695682 7 9 part_of receptor 952:959 arg1 a different receptor polypeptide receptor a different receptor polypeptide Fterm Site receptor polypeptide This change favors, and is sufficient to account for, the selection of a different receptor polypeptide to complete the cytokine-receptor complex. 9883900 7 16 part_of IGFBP-5 943:949 arg1 the central IGFBP-5 region IGFBP-5 the central IGFBP-5 region PUBTATOR Site IGFBP-5 3488 region In addition, a smaller fragment with Mr 2722 of the central IGFBP-5 region was purified and showed the sequence HTRISELKAEAVKKDRRKKLTQS (residues 121-143) indicating plasma proteolysis of IGFBP-5 C-terminal to amino acids Lys-120, Ser-143, Lys-144, and Arg-188. 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 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. 15173186 9 2 part_of located 1363:1369 arg2 other human Toll-like receptors AND consensus glycosylation sites other human Toll-like receptors consensus glycosylation sites Fterm Site receptors sites We have also analyzed where consensus glycosylation sites are located in the extracellular domains of other human Toll-like receptors. 15173186 9 85 part_of receptors 1425:1433 arg1 the extracellular domains receptors the extracellular domains Fterm Site receptors domains We have also analyzed where consensus glycosylation sites are located in the extracellular domains of other human Toll-like receptors. 28011641 6 13 part_of L-selectin 825:834 arg1 the lectin and EGF domains L-selectin the lectin and EGF domains PUBTATOR Site L-selectin 6402 domains Here we report the structure of the lectin and EGF domains of L-selectin bound to a fucose mimetic; that is, a terminal mannose on an N-glycan attached to a symmetry-related molecule. 28011641 6 32 part_of EGF 810:812 arg1 the lectin and EGF domains EGF the lectin and EGF domains OGER Site EGF P01133 domains Here we report the structure of the lectin and EGF domains of L-selectin bound to a fucose mimetic; that is, a terminal mannose on an N-glycan attached to a symmetry-related molecule. 9023546 2 85 part_of EGF 331:333 arg1 EGF domains EGF EGF domains PUBTATOR Site EGF 1950 domains The enzyme catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in EGF domains. 22601780 11 2 part_of EGF 1161:1163 arg1 EGF domain sequences EGF EGF domain sequences OGER Site EGF P01133 sequences A database search for EGF domain sequences shows that this RGD finger is likely an evolutionary insertion and unique to the EGF domain of Del-1 and its homologue milk fat globule-EGF 8. 22601780 11 11 part_of Del-1 1277:1281 arg1 the EGF domain Del-1 the EGF domain PUBTATOR Site Del-1 10085 domain A database search for EGF domain sequences shows that this RGD finger is likely an evolutionary insertion and unique to the EGF domain of Del-1 and its homologue milk fat globule-EGF 8. 22601780 11 28 part_of EGF 1263:1265 arg1 the EGF domain EGF the EGF domain OGER Site EGF P01133 domain A database search for EGF domain sequences shows that this RGD finger is likely an evolutionary insertion and unique to the EGF domain of Del-1 and its homologue milk fat globule-EGF 8. 22601780 11 45 part_of globule-EGF 1310:1320 arg1 the EGF domain EGF 8 the EGF domain OGER Site EGF 8 P01133 domain A database search for EGF domain sequences shows that this RGD finger is likely an evolutionary insertion and unique to the EGF domain of Del-1 and its homologue milk fat globule-EGF 8. 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. 22664871 6 7 part_of RANKL 1168:1172 arg1 important interacting residues RANKL important interacting residues PUBTATOR Site RANKL 21943 residues These results, together with a previously reported mouse RANKL/RANK complex structure, reveal that OPG exerts its decoy receptor function by directly blocking the accessibilities of important interacting residues of RANKL for RANK recognition. 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. 15532026 9 14 part_of site 1591:1594 arg1 the gamma subunit subunit site OGER Site subunit Q9UJJ9 site These data suggest that the loss of the used glycosylation site in the gamma subunit may affect the intracellular localization of GNPTAG and the overall efficiency of M6P formation. 22333914 3 16 part_of overall 698:704 arg1 the overall GAIN domain l GAIN the overall GAIN domain PUBTATOR Site l GAIN 23218 domain Crystal structures of GAIN domains from two distantly related cell-adhesion GPCRs revealed a conserved novel fold in which the GPS motif forms five β-strands that are tightly integrated into the overall GAIN domain. 22333914 3 21 part_of GAIN 706:709 arg1 the overall GAIN domain l GAIN the overall GAIN domain PUBTATOR Site l GAIN 23218 domain Crystal structures of GAIN domains from two distantly related cell-adhesion GPCRs revealed a conserved novel fold in which the GPS motif forms five β-strands that are tightly integrated into the overall GAIN domain. 22333914 3 44 part_of GPS 630:632 arg1 the GPS motif GPS the GPS motif OGER Site GPS motif Crystal structures of GAIN domains from two distantly related cell-adhesion GPCRs revealed a conserved novel fold in which the GPS motif forms five β-strands that are tightly integrated into the overall GAIN domain. 16186819 4 22 part_of THBS2 533:537 arg1 The THBS2 signature domain THBS2 The THBS2 signature domain PUBTATOR Site THBS2 7058 domain The THBS2 signature domain is stabilized by these interactions and by a network of 30 bound Ca(2+) ions and 18 disulfide bonds. 2226832 4 28 gly glycosylated 480:491 arg2 all three sites all three sites sites Some species of CAP37 are glycosylated at all three sites; some at Asn-114 alone, others at Asn-114 and Asn-110 or Asn-145. 2226832 4 35 gly sites 506:510 arg1 Asn-145 Asn-145 Asn-145 Some species of CAP37 are glycosylated at all three sites; some at Asn-114 alone, others at Asn-114 and Asn-110 or Asn-145. 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. 10201933 4 63 part_of GPI-anchor 704:713 arg1 the GPI-anchor motif GPI the GPI-anchor motif OGER Site GPI P06744 motif The 1998-base pairs of the open reading frame of the cloned cDNA encoded a protein of 666 amino acids (aa), including the 46 aa of the signal peptide and the 19 aa of the GPI-anchor motif. 18491227 0 34 gly Unglycosylation 0:14 arg2 Asn-633 Asn-633 Asn-633 Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD. 2013294 6 17 gly Asn77 623:627 arg1 A single N-glycosidic carbohydrate moiety Asn77 A single N-glycosidic carbohydrate moiety Asn77 A single N-glycosidic carbohydrate moiety is located at Asn77. 2013294 6 29 gly located 612:618 arg1 Asn77 AND A single N-glycosidic carbohydrate moiety Asn77 A single N-glycosidic carbohydrate moiety Asn77 A single N-glycosidic carbohydrate moiety is located at Asn77. 17503783 3 42 part_of EGF-like 766:773 arg1 a novel, EGF-like domain EGF a novel, EGF-like domain OGER Site EGF P01133 domain The crystal structure reveals a molecule composed of two closely associated domains: a catalytic domain that adopts a distorted (beta/alpha)8 barrel resembling that of bee venom hyaluronidase, and a novel, EGF-like domain, characteristic of involvement in protein-protein interactions and regulatory processes. 17503783 3 42 part_of EGF-like 766:773 arg1 two closely associated domains EGF two closely associated domains OGER Site EGF P01133 domains The crystal structure reveals a molecule composed of two closely associated domains: a catalytic domain that adopts a distorted (beta/alpha)8 barrel resembling that of bee venom hyaluronidase, and a novel, EGF-like domain, characteristic of involvement in protein-protein interactions and regulatory processes. 16040958 7 13 gly Asn 1499:1501 arg1 the N-linked carbohydrate Asn(3) the N-linked carbohydrate Asn(3) Therefore, the interaction of C1INH with gram-negative bacterial LPS is dependent both on the N-linked carbohydrate at Asn(3) and on the positively charged residues within the amino-terminal domain. 15173186 0 74 part_of sites 28:32 arg1 human toll-like receptor 2 toll-like receptor 2 sites PUBTATOR Site toll-like receptor 2 7097 sites Four N-linked glycosylation sites in human toll-like receptor 2 cooperate to direct efficient biosynthesis and secretion. 22041449 3 13 part_of laminin 509:515 arg1 three laminin epidermal growth factor-like (LE) domains laminin three laminin epidermal growth factor-like (LE) domains OGER Site laminin domains Netrin G proteins share a common multi-domain architecture comprising a laminin N-terminal (LN) domain followed by three laminin epidermal growth factor-like (LE) domains and a C' region containing a glycosylphosphatidylinositol anchor. 22041449 3 32 part_of laminin 460:466 arg1 a laminin N-terminal (LN) domain laminin a laminin N-terminal (LN) domain OGER Site laminin domain Netrin G proteins share a common multi-domain architecture comprising a laminin N-terminal (LN) domain followed by three laminin epidermal growth factor-like (LE) domains and a C' region containing a glycosylphosphatidylinositol anchor. 21712440 9 62 gly sialylated 1687:1696 arg1 sialylated O-glycans sialylated O-glycans APP/Aβ sialylated O-glycans, including that of a Tyr residue, the first in a mammalian protein, may modulate APP processing, inhibiting the amyloidogenic pathway associated with AD. 2277032 3 52 part_of enzyme 572:577 arg1 the 27th residue enzyme the 27th residue Fterm Site enzyme residue The N-terminal amino acid sequence up to the 27th residue of the enzyme was similar to that of pancreatic deoxyribonuclease I from bovine and other species. 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. 21569239 9 26 part_of F-spondin 1224:1232 arg1 the F-spondin FS domain structure of the F-spondin the F-spondin FS domain PUBTATOR Site structure of the F-spondin 10418 domain CONCLUSION: The structure of the F-spondin FS domain completes the structural studies of the multiple-domain ECM molecule. 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. 18596036 3 13 part_of MASP-1/3 449:456 arg1 the CUB(1)-EGF-CUB(2) domain MASP-1/3 the CUB(1)-EGF-CUB(2) domain PUBTATOR Site MASP-1/3 5648 domain The x-ray structure of the CUB(1)-EGF-CUB(2) domain of human MASP-1/3, responsible for interaction of MASP-1 and -3 with their partner proteins mannan-binding lectin (MBL) and ficolins, was solved to a resolution of 2.3A(.) 18596036 3 42 part_of -EGF-CUB 421:428 arg1 the CUB(1)-EGF-CUB(2) domain EGF the CUB(1)-EGF-CUB(2) domain PUBTATOR Site EGF 1950 domain The x-ray structure of the CUB(1)-EGF-CUB(2) domain of human MASP-1/3, responsible for interaction of MASP-1 and -3 with their partner proteins mannan-binding lectin (MBL) and ficolins, was solved to a resolution of 2.3A(.) 16422668 11 43 part_of Yvo 1629:1631 arg1 the Yvo antigen-binding site Yvo the Yvo antigen-binding site Cterm Site Yvo P01871 site An atypical serine, arginine and glutamate motif is located in the middle of the Yvo antigen-binding site and displays an overall geometry that mimics the classical serine, histidine and aspartate catalytic triad of serine proteases. 1556128 7 56 part_of HB-EGF 1055:1060 arg1 the mature HB-EGF polypeptide HB-EGF the mature HB-EGF polypeptide PUBTATOR Site HB-EGF 1839 polypeptide Microsequencing of tryptic fragments indicated that the mature HB-EGF polypeptide can contain at least 86 of the 208 amino acids predicted by nucleotide sequence to be the HB-EGF precursor molecule. 21752865 4 58 part_of bears 784:788 arg1 BRI2 AND the consensus sequence BRI2 the consensus sequence PUBTATOR Site BRI2 9445 sequence In support, bioinformatics analysis indicated that BRI2 bears the consensus sequence Asn-Thr-Ser (residues 170-173) and could be N-glycosylated at Asn170. 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. 15965977 7 64 part_of EGF 1402:1404 arg1 the EGF core ectodomain EGF the EGF core ectodomain PUBTATOR Site EGF 13645 ectodomain It is expressed as two forms with different lengths, forms dimers and interacts with TGF-alpha ligands through a luminal interaction with the EGF core ectodomain. 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. 22040171 2 33 part_of NAAA 322:325 arg1 the NAAA pro-enzyme NAAA the NAAA pro-enzyme PUBTATOR AminoAcid NAAA 27163 pro We developed a HEK293 cell line stably expressing the NAAA pro-enzyme (zymogen) and a single step chromatographic purification of the protein from the media. 7681597 2 1 gly glycosylated 382:393 arg1 two serine residues two serine residues serine residues Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure. 7681597 2 20 gly residues 345:352 arg1 two serine residues two serine residues serine residues Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure. 7681597 2 46 gly glycosylated 420:431 arg1 two serine residues two serine residues serine residues Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure. 7681597 2 54 gly glycopeptides 306:318 arg2 the glycopeptides the glycopeptides glycopeptides Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure. 7681597 2 1 gly glycosylated 382:393 arg1 Ser-14 Ser-14 and Ser-15 Ser-14 and Ser-15 Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure. 7681597 2 20 gly residues 345:352 arg1 Ser-14 Ser-14 and Ser-15 Ser-14 and Ser-15 Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure. 7681597 2 46 gly glycosylated 420:431 arg1 Thr-17 Thr-17 and Ser-19 Thr-17 and Ser-19 Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure. 7681597 2 46 gly glycosylated 420:431 arg1 Ser-14 Ser-14 and Ser-15 Ser-14 and Ser-15 Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure. 9572875 5 23 part_of IGFBP-6 884:890 arg1 Glycosylation sites IGFBP-6 Glycosylation sites PUBTATOR Site IGFBP-6 3489 sites Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography. 9572875 5 23 part_of IGFBP-6 884:890 arg1 Thr146 IGFBP-6 Thr126, Ser144, Thr145, Thr146, and Ser152 PUBTATOR AminoAcid IGFBP-6 3489 Thr126, Ser144, Thr145, Thr146, and Ser152 Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography. 9572875 5 23 part_of IGFBP-6 884:890 arg1 Thr126 IGFBP-6 Thr126, Ser144, Thr145, Thr146, and Ser152 PUBTATOR AminoAcid IGFBP-6 3489 Thr126, Ser144, Thr145, Thr146, and Ser152 Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography. 9572875 5 23 part_of IGFBP-6 884:890 arg1 Ser144 IGFBP-6 Thr126, Ser144, Thr145, Thr146, and Ser152 PUBTATOR AminoAcid IGFBP-6 3489 Thr126, Ser144, Thr145, Thr146, and Ser152 Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography. 9572875 5 23 part_of IGFBP-6 884:890 arg1 Ser152 IGFBP-6 Thr126, Ser144, Thr145, Thr146, and Ser152 PUBTATOR AminoAcid IGFBP-6 3489 Thr126, Ser144, Thr145, Thr146, and Ser152 Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography. 9572875 5 23 part_of IGFBP-6 884:890 arg1 Thr126 IGFBP-6 Thr126, Ser144, Thr145, Thr146, and Ser152 PUBTATOR AminoAcid IGFBP-6 3489 Thr126, Ser144, Thr145, Thr146, and Ser152 Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography. 9572875 5 23 part_of IGFBP-6 884:890 arg1 Ser144 IGFBP-6 Thr126, Ser144, Thr145, Thr146, and Ser152 PUBTATOR AminoAcid IGFBP-6 3489 Thr126, Ser144, Thr145, Thr146, and Ser152 Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography. 9572875 5 23 part_of IGFBP-6 884:890 arg1 Ser152 IGFBP-6 Thr126, Ser144, Thr145, Thr146, and Ser152 PUBTATOR AminoAcid IGFBP-6 3489 Thr126, Ser144, Thr145, Thr146, and Ser152 Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography. 9572875 5 23 part_of IGFBP-6 884:890 arg1 Ser144 IGFBP-6 Thr126, Ser144, Thr145, Thr146, and Ser152 PUBTATOR AminoAcid IGFBP-6 3489 Thr126, Ser144, Thr145, Thr146, and Ser152 Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography. 9572875 5 23 part_of IGFBP-6 884:890 arg1 Ser152 IGFBP-6 Thr126, Ser144, Thr145, Thr146, and Ser152 PUBTATOR AminoAcid IGFBP-6 3489 Thr126, Ser144, Thr145, Thr146, and Ser152 Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography. 9572875 5 23 part_of IGFBP-6 884:890 arg1 Ser152 IGFBP-6 Thr126, Ser144, Thr145, Thr146, and Ser152 PUBTATOR AminoAcid IGFBP-6 3489 Thr126, Ser144, Thr145, Thr146, and Ser152 Glycosylation sites of IGFBP-6 were identified as Thr126, Ser144, Thr145, Thr146, and Ser152 by using a combination of ESMS and Edman sequencing of tryptic fragments separated by reverse-phase high-pressure liquid chromatography. 20823119 5 74 part_of residues 743:750 arg1 the HR HR residues Cterm AminoAcid HR serine and threonine residues However, locating and characterizing the entire range of O-glycan attachment sites are analytically challenging due to the clustered serine and threonine residues in the HR of IgA1 heavy chain. 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)). 17614963 8 41 part_of fibronectin 1526:1536 arg1 juvenile-specific fibronectin fragments fibronectin juvenile-specific fibronectin fragments PUBTATOR Site fibronectin 2335 fragments This is the first report on the identification and characterization of juvenile-specific fibronectin fragments excreted into urine. 12970363 6 1 part_of motifs 906:911 arg1 TRPC6 TRPC6 motifs PUBTATOR Site TRPC6 7225 motifs Two NX(S/T) motifs in TRPC6 were mutated (Asn to Gln) by in vitro mutagenesis to delete one or both extracellular N-linked glycosylation sites. 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. 1569071 11 62 part_of IGF-II 2258:2263 arg1 the E domain peptide IGF-II the E domain peptide PUBTATOR Site IGF-II P01344 peptide Finally, the association of O-linked oligosaccharide with the E domain peptide of IGF-II was confirmed by demonstrating the specificity of binding of the Ser66-Lys88 asialoglycopeptide to jackfruit lectin. 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. 21827946 3 6 part_of VEGFR2 475:480 arg1 VEGFR2 domain 3 VEGFR2 VEGFR2 domain 3 OGER Site VEGFR2 P35968 domain The two Fab fragments bind at opposite ends of VEGFR2 domain 3; 1121B directly blocks VEGF binding, whereas 6.64 may prevent receptor dimerization by perturbing the domain 3:domain 4 interface. 21827946 3 17 part_of Fab 436:438 arg1 The two Fab fragments Fab The two Fab fragments PUBTATOR Site Fab 2187 fragments The two Fab fragments bind at opposite ends of VEGFR2 domain 3; 1121B directly blocks VEGF binding, whereas 6.64 may prevent receptor dimerization by perturbing the domain 3:domain 4 interface. 16895906 2 10 gly sialylated 286:295 arg1 sialylated glycans sialylated glycans The CD33-related siglecs show complex recognition patterns for sialylated glycans. 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. 6785754 1 75 part_of Fc-like 109:115 arg1 an Fc-like fragment Fc-like an Fc-like fragment Cterm Site Fc-like fragment The complete amino acid sequence of an Fc-like fragment designated Fc delta (t) and obtained by limited proteolysis with trypsin of an intact myeloma IgD protein (NIG-65) has been determined. 11152692 1 21 gly leucine-rich 70:81 arg1 the leucine-rich repeat protein family leucine the leucine-rich repeat protein family leucine a novel member of the leucine-rich repeat protein family closely related to decorin and biglycan. 2498325 8 7 part_of Apolipoprotein 1176:1189 arg1 Gly196----Ser Apolipoprotein E Gly196----Ser PUBTATOR AminoAcid Apolipoprotein E 348 Ser Apolipoprotein E(Thr194----Asn,Gly196----Ser), which introduces a potential site for N-glycosylation at position 194, was secreted with a higher apparent molecular weight than native, O-glycosylated apoE. 2775232 3 5 part_of residue 750:756 arg1 GPIIb GPIIb residue PUBTATOR AminoAcid GPIIb 3674 cysteine residue It could be established that each cysteine residue in GPIIb, beginning at alpha-Cys-56, is disulphide-bonded to its nearest neighbour in the amino acid sequence. 24190431 1 14 part_of susceptibility 228:241 arg1 the shared susceptibility epitope us the shared susceptibility epitope PUBTATOR Site us 3123 epitope Rheumatoid arthritis (RA) is strongly associated with the human leukocyte antigen (HLA)-DRB1 locus that possesses the shared susceptibility epitope (SE) and the citrullination of self-antigens. 24190431 1 67 part_of possesses 207:215 arg1 the human leukocyte antigen (HLA)-DRB1 locus AND the shared susceptibility epitope the human leukocyte antigen (HLA)-DRB1 locus the shared susceptibility epitope PUBTATOR Site us 3123 epitope Rheumatoid arthritis (RA) is strongly associated with the human leukocyte antigen (HLA)-DRB1 locus that possesses the shared susceptibility epitope (SE) and the citrullination of self-antigens. 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. 17924658 0 74 part_of gamma-glutamyltranspeptidase 106:133 arg1 glycosylation sites gamma-glutamyltranspeptidase glycosylation sites PUBTATOR Site gamma-glutamyltranspeptidase 102724197 sites Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human gamma-glutamyltranspeptidase. 8962717 0 18 part_of receptor 98:105 arg1 the extracellular domain epidermal growth factor receptor the extracellular domain PUBTATOR Site epidermal growth factor receptor P00533 domain Analysis of the glycosylation patterns of the extracellular domain of the epidermal growth factor receptor expressed in Chinese hamster ovary fibroblasts. 2361960 5 1 gly glycosylated 822:833 arg1 Thr-3 Thr-3 and Asn-28 Thr-3 and Asn-28 In addition, we concluded that Thr-3 and Asn-28 were glycosylated. 20044576 1 23 part_of laminin-G 217:225 arg1 laminin-G domains laminin laminin-G domains OGER Site laminin domains Alpha-dystroglycan (alpha-DG) is a cell-surface glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains and certain arenaviruses. 20044576 1 42 part_of containing 206:215 arg1 both extracellular matrix proteins AND laminin-G domains both extracellular matrix proteins laminin-G domains Fterm Site proteins domains Alpha-dystroglycan (alpha-DG) is a cell-surface glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains and certain arenaviruses. 28060820 2 20 part_of sIL-6R 619:624 arg1 all O- and N-glycosylation sites sIL all O- and N-glycosylation sites OGER Site 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. 21712440 1 2 part_of Aβ 266:267 arg1 shorter aggregating amyloid β (Aβ)-peptides Aβ) shorter aggregating amyloid β (Aβ)-peptides PUBTATOR Site Aβ) 351 -peptides The proteolytic processing of human amyloid precursor protein (APP) into shorter aggregating amyloid β (Aβ)-peptides, e.g., Aβ1-42, is considered a critical step in the pathogenesis of Alzheimer's disease (AD). 21712440 1 53 part_of amyloid 255:261 arg1 shorter aggregating amyloid β (Aβ)-peptides amyloid β shorter aggregating amyloid β (Aβ)-peptides PUBTATOR Site amyloid β 351 -peptides The proteolytic processing of human amyloid precursor protein (APP) into shorter aggregating amyloid β (Aβ)-peptides, e.g., Aβ1-42, is considered a critical step in the pathogenesis of Alzheimer's disease (AD). 21712440 1 102 part_of β 263:263 arg1 shorter aggregating amyloid β (Aβ)-peptides amyloid β shorter aggregating amyloid β (Aβ)-peptides PUBTATOR Site amyloid β 351 -peptides The proteolytic processing of human amyloid precursor protein (APP) into shorter aggregating amyloid β (Aβ)-peptides, e.g., Aβ1-42, is considered a critical step in the pathogenesis of Alzheimer's disease (AD). 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. 3542030 0 75 part_of protein 47:53 arg1 Amino acid sequence steroid binding protein Amino acid sequence PUBTATOR Site steroid binding protein 8991 sequence Amino acid sequence of the sex steroid binding protein of human blood plasma. 9023546 3 35 part_of EGF-1 388:392 arg1 recombinant human factor VII EGF-1 domain factor VII EGF recombinant human factor VII EGF-1 domain OGER Site factor VII EGF P08709 domain The assay uses recombinant human factor VII EGF-1 domain as acceptor substrate and GDP-fucose as donor substrate. 9023546 3 77 part_of VII 384:386 arg1 recombinant human factor VII EGF-1 domain factor VII EGF recombinant human factor VII EGF-1 domain OGER Site factor VII EGF P08709 domain The assay uses recombinant human factor VII EGF-1 domain as acceptor substrate and GDP-fucose as donor substrate. 9501084 0 20 part_of form 107:110 arg1 the collagen-binding epitope form of BM-40 the collagen-binding epitope PUBTATOR Site form of BM-40 6678 epitope Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin. 20145116 7 32 part_of receptor 1015:1022 arg1 left-handed twisted receptor domains receptor left-handed twisted receptor domains Fterm Site receptor domains This structure reveals a symmetrical 22 complex, in which left-handed twisted receptor domains wrap around the 2-fold axis of VEGF-C. 10644446 7 47 part_of contain 1046:1052 arg1 ANGPTL3 AND the characteristic calcium binding motif ANGPTL3 the characteristic calcium binding motif PUBTATOR Site ANGPTL3 30924 motif ANGPTL3 also does not contain the characteristic calcium binding motif found in the other angiopoietins. 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. 23756651 2 21 part_of RNF43 357:361 arg1 RNF43 ectodomains RNF43 RNF43 ectodomains PUBTATOR Site RNF43 54894 ectodomains The structure of RSPO1 bound to both LGR5 and RNF43 ectodomains confirms their physical linkage. 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. 3542989 0 24 part_of cholinesterase 44:57 arg1 Complete amino acid sequence cholinesterase Complete amino acid sequence PUBTATOR Site cholinesterase 534616 sequence Complete amino acid sequence of human serum cholinesterase. 21712440 2 66 part_of APP/Aβ 506:511 arg1 released APP/Aβ glycopeptides APP/Aβ released APP/Aβ glycopeptides PUBTATOR Site APP/Aβ 351 glycopeptides Although APP is a well-known membrane glycoprotein carrying both N- and O-glycans, nothing is known about the occurrence of released APP/Aβ glycopeptides in cerebrospinal fluid (CSF). 1472036 2 9 part_of receptor 375:382 arg1 the soluble extracellular domain insulin receptor the soluble extracellular domain OGER Site insulin receptor P06213 domain We have digested the soluble extracellular domain of the insulin receptor with succinylated trypsin, partially separated the resulting peptides, and sequenced a number of fractions. 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. 18420026 6 9 part_of glycoprotein 1539:1550 arg1 a single glycosylation site glycoprotein a single glycosylation site Fterm Site glycoprotein site Based on the results of N-Glycosidase F treatment with human fetal brain tissue and lysates from transient transfection with human wild-type or glycosylation site mutant NECL1 in 293ET cells, we demonstrated that human NECL1 is an N-linked glycoprotein with a single glycosylation site at position N290KS. 22483115 4 32 part_of Fab 576:578 arg1 the Fab fragment Fab the Fab fragment PUBTATOR Site Fab 2187 fragment The crystal structure of the monomeric DDR1 extracellular region bound to the Fab fragment of mAb 3E3 reveals that the collagen-binding discoidin (DS) domain is tightly associated with the following DS-like domain, which contains the epitopes of all mAbs. 22483115 4 38 part_of DDR1 537:540 arg1 the monomeric DDR1 extracellular region DDR1 the monomeric DDR1 extracellular region PUBTATOR Site DDR1 780 region The crystal structure of the monomeric DDR1 extracellular region bound to the Fab fragment of mAb 3E3 reveals that the collagen-binding discoidin (DS) domain is tightly associated with the following DS-like domain, which contains the epitopes of all mAbs. 22483115 4 11 part_of contains 719:726 arg1 the following DS-like domain AND the epitopes the following DS-like domain the epitopes epitopes The crystal structure of the monomeric DDR1 extracellular region bound to the Fab fragment of mAb 3E3 reveals that the collagen-binding discoidin (DS) domain is tightly associated with the following DS-like domain, which contains the epitopes of all mAbs. 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. 19153605 5 12 part_of FS 587:588 arg1 the FS domain structure of the FS the FS domain Cterm Site structure of the FS 10418 domain We determined the structure of the FS domain at 1.8-A resolution. 19303388 3 17 part_of protein 605:611 arg1 a peptide myelin basic protein a peptide PUBTATOR Site myelin basic protein 17196 peptide We show that a microbial peptide, common to several major classes of bacteria, can induce MS-like disease in humanized mice by crossreacting with a T cell receptor (TCR) that also recognizes a peptide from myelin basic protein, a candidate MS autoantigen. 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. 22848655 11 114 part_of Sema 1587:1590 arg1 the Sema domain Sema the Sema domain PUBTATOR Site Sema 57556 domain The RON Sema-PSI crystal packing generates a homodimer with interface formed by the Sema domain. 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) Thr(226) Thr(226) We demonstrated that GalNAc-T2 glycosylation of Thr(226) in a peptide with the RAPR(224)↓TT processing site blocks in vitro furin cleavage. 20837471 7 71 gly Thr 1228:1230 arg1 GalNAc-T2 glycosylation Thr(226) GalNAc-T2 glycosylation Thr(226) We demonstrated that GalNAc-T2 glycosylation of Thr(226) in a peptide with the RAPR(224)↓TT processing site blocks in vitro furin cleavage. 20837471 7 63 gly glycosylation 1211:1223 arg1 a peptide peptide a peptide Site peptide We demonstrated that GalNAc-T2 glycosylation of Thr(226) in a peptide with the RAPR(224)↓TT processing site blocks in vitro furin cleavage. 22333914 4 48 part_of extracellular 804:816 arg1 the only extracellular domain r the only extracellular domain PUBTATOR Site r 151 domain The GAIN domain is evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. 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. 3497398 2 1 part_of von 336:338 arg1 the von Willebrand factor-binding domain von Willebrand factor the von Willebrand factor-binding domain OGER Site von Willebrand factor P04275 domain This includes the complete sequence of the amino-terminal tryptic fragment of 290 residues comprising the von Willebrand factor-binding domain. 3497398 2 47 part_of Willebrand 340:349 arg1 the von Willebrand factor-binding domain von Willebrand factor the von Willebrand factor-binding domain OGER Site von Willebrand factor P04275 domain This includes the complete sequence of the amino-terminal tryptic fragment of 290 residues comprising the von Willebrand factor-binding domain. 3497398 2 96 part_of factor-binding 351:364 arg1 the von Willebrand factor-binding domain von Willebrand factor the von Willebrand factor-binding domain OGER Site von Willebrand factor P04275 domain This includes the complete sequence of the amino-terminal tryptic fragment of 290 residues comprising the von Willebrand factor-binding domain. 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. 23050552 9 69 part_of regions 1167:1173 arg1 human fibrinogen fibrinogen regions PUBTATOR Site fibrinogen 2244 regions Moreover, we describe seven novel O-glycosylation regions in human fibrinogen, all occupied by a monosialylated T-antigen. 21733844 5 35 gly Nonglycosylated 679:693 arg1 Nonglycosylated protein Nonglycosylated protein Fterm protein Nonglycosylated protein was isolated using both glycan affinity chromatography and through mutating asparagine 133 to a glutamine. 2721499 3 2 part_of contains 557:564 arg1 The precursor AND six N-linked glycosylation sites The precursor six N-linked glycosylation sites Fterm Site precursor sites The precursor is preceded by a signal sequence for vectorial export and contains six N-linked glycosylation sites distributed equally between the two chains of the structure. 17614963 0 31 part_of fibronectin 24:34 arg1 novel fibronectin fragments fibronectin novel fibronectin fragments PUBTATOR Site fibronectin 2335 fragments Identification of novel fibronectin fragments detected specifically in juvenile urine. 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. 3542989 4 8 part_of terminus 452:459 arg1 the 198th residue terminus the 198th residue residue The active site serine is the 198th residue from the amino terminus. 3542989 4 8 part_of terminus 452:459 arg1 The active site serine terminus The active site serine serine The active site serine is the 198th residue from the amino terminus. 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. 22579623 4 5 part_of sites 697:701 arg1 TLR3ecd at sites TLR3 sites PUBTATOR Site TLR3 7098 sites In contrast, Fab12 and Fab1068 bind TLR3ecd at sites distinct from the N- and C-terminal regions that interact with dsRNA and do not inhibit minimal SU formation with short dsRNA. 22579623 4 9 part_of TLR3ecd 686:692 arg1 TLR3ecd at sites TLR3 TLR3ecd at sites PUBTATOR Site TLR3 7098 sites In contrast, Fab12 and Fab1068 bind TLR3ecd at sites distinct from the N- and C-terminal regions that interact with dsRNA and do not inhibit minimal SU formation with short dsRNA. 8757293 5 38 part_of sites 835:839 arg1 the related proteinase proteinase sites PUBTATOR Site proteinase 100616101 sites In general, the substrate binding sites, S4 to S3', are more polar than comparable sites in the related proteinase, human leukocyte elastase. 8757293 5 38 part_of sites 835:839 arg1 human leukocyte elastase human leukocyte elastase sites OGER Site human leukocyte elastase P08246 sites In general, the substrate binding sites, S4 to S3', are more polar than comparable sites in the related proteinase, human leukocyte elastase. 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. 17286803 10 56 part_of CLN3 1489:1492 arg1 different cytoplasmic domains CLN3 different cytoplasmic domains OGER Site CLN3 Q13286 domains The data suggest that co-operative signal structures in different cytoplasmic domains of CLN3 are required for efficient sorting and for transport to the lysosome. 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 Thr194 the carbohydrate moiety Thr194 Sequence analysis and amino sugar analysis of this peptide derived from asialo-, monosialo-, or disialo-apoE indicated that the carbohydrate moiety is attached only to Thr194 in monosialo- and disialo-apoE and that asialo-apoE is not glycosylated. 9572875 8 58 part_of positions 1343:1351 arg1 IGFBP-6 IGFBP-6 positions PUBTATOR Site IGFBP-6 3489 positions Native disulfide bond positions in IGFBP-6 were localized by means of observed disulfide-linked tryptic fragments, revealing that there are two disulfide-linked subdomains within each of the N- and C-terminal regions and confirming a previous suggestion that the latter regions are not interconnected. 20511397 5 58 part_of Thr 1037:1039 arg1 both cellular and secreted apoE apoE Thr PUBTATOR SpecificSite apoE 348 Thr(194) Our results identify eight different glycoforms with (HexNAc)(2)-Hex(2)-(NeuAc)(2) being the most complex glycan detected on Thr(194) in both cellular and secreted apoE. 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. 19153605 4 11 part_of F-spondin 479:487 arg1 an N-terminal F-spondin (FS) domain N-terminal F-spondin an N-terminal F-spondin (FS) domain PUBTATOR Site N-terminal F-spondin 10418 domain Mindin comprises an N-terminal F-spondin (FS) domain and C-terminal thrombospondin type 1 repeat (TSR). 19153605 4 16 part_of N-terminal 468:477 arg1 an N-terminal F-spondin (FS) domain N-terminal F-spondin an N-terminal F-spondin (FS) domain PUBTATOR Site N-terminal F-spondin 10418 domain Mindin comprises an N-terminal F-spondin (FS) domain and C-terminal thrombospondin type 1 repeat (TSR). 19153605 4 19 part_of FS 490:491 arg1 an N-terminal F-spondin (FS) domain FS an N-terminal F-spondin (FS) domain Cterm Site FS 10418 domain Mindin comprises an N-terminal F-spondin (FS) domain and C-terminal thrombospondin type 1 repeat (TSR). 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. 22848655 8 6 part_of Sema 1139:1142 arg1 RON Sema domain RON Sema RON Sema domain OGER Site RON Sema Q04912 domain RON Sema domain adopts a seven-bladed β-propeller fold, followed by disulfide bond rich, cysteine-knot PSI motif. 22848655 8 61 part_of RON 1135:1137 arg1 RON Sema domain RON Sema RON Sema domain OGER Site RON Sema Q04912 domain RON Sema domain adopts a seven-bladed β-propeller fold, followed by disulfide bond rich, cysteine-knot PSI motif. 22576872 2 42 part_of Endogenous 324:333 arg1 Endogenous Aβ peptides Endogenous Aβ Endogenous Aβ peptides PUBTATOR Site Endogenous Aβ 351 peptides Endogenous Aβ peptides reflect the APP processing, and greater knowledge of different APP degradation pathways is important to understand the mechanism underlying AD pathology. 22576872 2 77 part_of Aβ 335:336 arg1 Endogenous Aβ peptides Endogenous Aβ Endogenous Aβ peptides PUBTATOR Site Endogenous Aβ 351 peptides Endogenous Aβ peptides reflect the APP processing, and greater knowledge of different APP degradation pathways is important to understand the mechanism underlying AD pathology. 2579379 2 38 part_of alpha 320:324 arg1 22 amino acid residues alpha chain residues PUBTATOR Site alpha chain 2217 residues The encoded precursor molecule contains a signal peptide of 22 amino acid residues, the beta chain (645 residues), and the alpha chain (992 residues). 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. 10644446 6 12 part_of contains 817:824 arg1 ANGPTL3 AND the four conserved cysteines ANGPTL3 the four conserved cysteines PUBTATOR AminoAcid ANGPTL3 30924 cysteines ANGPTL3 contains the four conserved cysteines implicated in the intramolecular disulfide bonds within the FHD, but it does not contain two other cysteines that are found within the FHD of angiopoietins 1, 2, and 4. 22940367 5 7 part_of GALNS 797:801 arg1 The active site GALNS The active site PUBTATOR Site GALNS 2588 site The active site of GALNS is a large, positively charged trench suitable for binding polyanionic substrates such as keratan sulfate and chondroitin-6-sulfate. 28775322 6 2 part_of receptors 1391:1399 arg1 the EGF-like domains receptors the EGF-like domains Fterm Site receptors domains Finally, we show that Protein O-glucosyltransferase 1 has co-evolved with EGF-like domains of the type found in Notch.POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors. 28775322 6 20 part_of EGF-like 1217:1224 arg1 EGF-like domains EGF EGF-like domains OGER Site EGF P01133 domains Finally, we show that Protein O-glucosyltransferase 1 has co-evolved with EGF-like domains of the type found in Notch.POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors. 28775322 6 24 part_of EGF-like 1345:1352 arg1 the EGF-like domains EGF the EGF-like domains OGER Site EGF P01133 domains Finally, we show that Protein O-glucosyltransferase 1 has co-evolved with EGF-like domains of the type found in Notch.POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors. 28775322 6 52 part_of Notch 1365:1369 arg1 the EGF-like domains Notch the EGF-like domains PUBTATOR Site Notch 31293 domains Finally, we show that Protein O-glucosyltransferase 1 has co-evolved with EGF-like domains of the type found in Notch.POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors. 8702538 0 51 gly glycosylation 18:30 arg2 A single N-linked glycosylation site A single N-linked glycosylation site site A single N-linked glycosylation site is implicated in the regulation of ligand recognition by the I-type lectins CD22 and CD33. 33203861 5 3 part_of Ca2+ 647:650 arg1 a Ca2+ binding site Ca2 a Ca2+ binding site OGER Site Ca2 P00918 site A Na+ ion-binding site, reminiscent of a Ca2+ binding site in Cav channels, is identified in the unique EEKE selectivity filter. 33203861 5 30 part_of channels 672:679 arg1 A Na+ ion-binding site Cav channels A Na+ ion-binding site PUBTATOR Site Cav channels 858 site A Na+ ion-binding site, reminiscent of a Ca2+ binding site in Cav channels, is identified in the unique EEKE selectivity filter. 33203861 5 51 part_of site 660:663 arg1 Cav channels Cav channels site PUBTATOR Site Cav channels 858 site A Na+ ion-binding site, reminiscent of a Ca2+ binding site in Cav channels, is identified in the unique EEKE selectivity filter. 18703501 8 44 gly glycosylation 1520:1532 arg2 Thr(78) Thr(78) Thr(78) Parallel experiments on a recombinant protein obtained by a mammalian cell expression system demonstrated the occurrence of an additional O-linked glycosylation site (Thr(78)) and characterized the nature of the oligosaccharide structures. 18703501 8 44 gly glycosylation 1520:1532 arg2 an additional O-linked glycosylation site an additional O-linked glycosylation site site Parallel experiments on a recombinant protein obtained by a mammalian cell expression system demonstrated the occurrence of an additional O-linked glycosylation site (Thr(78)) and characterized the nature of the oligosaccharide structures. 3264725 2 54 part_of factor 440:445 arg1 10 gamma-carboxylated, N-terminally located glutamic acid residues factor VIIa 10 gamma-carboxylated, N-terminally located glutamic acid residues Cterm AminoAcid factor VIIa glutamic acid residues Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues. 3264725 2 54 part_of factor 440:445 arg1 1 beta-hydroxylated aspartic acid residue factor VIIa 1 beta-hydroxylated aspartic acid residue Cterm AminoAcid factor VIIa aspartic acid residue Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues. 3264725 2 54 part_of factor 440:445 arg1 2 N-glycosylated asparagine residues factor VIIa 2 N-glycosylated asparagine residues Cterm AminoAcid factor VIIa asparagine residues Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues. 3264725 2 113 part_of VIIa 447:450 arg1 10 gamma-carboxylated, N-terminally located glutamic acid residues factor VIIa 10 gamma-carboxylated, N-terminally located glutamic acid residues Cterm AminoAcid factor VIIa glutamic acid residues Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues. 3264725 2 113 part_of VIIa 447:450 arg1 1 beta-hydroxylated aspartic acid residue factor VIIa 1 beta-hydroxylated aspartic acid residue Cterm AminoAcid factor VIIa aspartic acid residue Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues. 3264725 2 113 part_of VIIa 447:450 arg1 2 N-glycosylated asparagine residues factor VIIa 2 N-glycosylated asparagine residues Cterm AminoAcid factor VIIa asparagine residues Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues. 8576151 11 64 part_of collagenase-3 1859:1871 arg1 the active site sequence collagenase-3 the active site sequence PUBTATOR Site collagenase-3 4322 sequence Unlike these collagenases, gelatin and the peptide substrates Mea-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 and Mca-Pro-Cha-Gly-Nva-His-Ala-Dpa-NH2 were efficiently hydrolyzed as well, as would be predicted from the similarities between the active site sequence of collagenase-3 (MMP-13) and the gelatinases A and B. Active collagenase-3 was inhibited in a 1:1 stoichiometric fashion by the tissue inhibitors of metalloproteinases, TIMP-1, TIMP-2, and TIMP-3. 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 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. 18768470 7 29 part_of FSTL3 1395:1399 arg1 the N-terminal domain FSTL3 the N-terminal domain PUBTATOR Site FSTL3 10272 domain Therefore, both structural and biochemical evidence support a significant interaction of the N-terminal domain of FSTL3 with activin A. 11502179 1 4 part_of receptor 175:182 arg1 The amino-terminal ectodomain TSH receptor The amino-terminal ectodomain PUBTATOR Site TSH receptor 7253 ectodomain The amino-terminal ectodomain of the human TSH receptor has been expressed at the surface of CHO cells as a glycosylphosphatidylinositol-anchored molecule containing a 10-residue histidine tag close to its C terminus. 11953431 5 44 part_of amidotransferase 740:755 arg1 the class I glutamine amidotransferase domains amidotransferase the class I glutamine amidotransferase domains Fterm Site amidotransferase domains The topology is very similar to that of the class I glutamine amidotransferase domains, with the only major differences consisting of extensions in four loops and at the C terminus. 30069874 1 49 part_of receptor 138:145 arg1 Ly6/urokinase-type plasminogen activator receptor (uPAR) (LU) domain Ly6/urokinase-type plasminogen activator receptor Ly6/urokinase-type plasminogen activator receptor (uPAR) (LU) domain PUBTATOR Site Ly6/urokinase-type plasminogen activator receptor 5329 domain Ly6/urokinase-type plasminogen activator receptor (uPAR) (LU) domain containing 6 (LYPD6) is a Wnt signaling enhancer that promotes phosphorylation of the Wnt coreceptor low density lipoprotein receptor-related protein 6 (LRP6). 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. 20145116 2 35 part_of receptors 280:288 arg1 The extracellular domain VEGF receptors The extracellular domain PUBTATOR Site VEGF receptors P15692 domain The extracellular domain of VEGF receptors consists of seven immunoglobulin homology domains, which, upon ligand binding, promote receptor dimerization. 8617200 3 1 part_of LTBP-1 645:650 arg1 various fragments LTBP-1 various fragments PUBTATOR Site LTBP-1 4052 fragments The association of beta1-LAP with LTBP-1 was characterized at the molecular level with an expression system in mammalian cells, where TGF-beta1 and various fragments of LTBP-1 were co-expressed and secreted with the aid of a signal peptide synthesized to the LTBP-1 constructs. 17503783 4 38 part_of EGF-like 920:927 arg1 this unique EGF-like domain EGF this unique EGF-like domain OGER Site EGF P01133 domain The structure shows that the fold of this unique EGF-like domain is intact in four alternative splice-variants, whereas the catalytic domain is likely to be unfolded. 21047790 3 38 part_of neurofascin 457:467 arg1 The four N-terminal Ig-like domains neurofascin The four N-terminal Ig-like domains PUBTATOR Site neurofascin 23114 domains The four N-terminal Ig-like domains of neurofascin form a horseshoe shape, akin to several other immunoglobulin superfamily cell adhesion molecules such as hemolin, axonin, and Dscam. 22750213 4 4 part_of containing 695:704 arg1 PRiMA AND two putative N-linked glycosylation sites PRiMA two putative N-linked glycosylation sites PUBTATOR Site PRiMA 170952 sites PRiMA is a glycoprotein containing two putative N-linked glycosylation sites. 22750213 4 4 part_of containing 695:704 arg1 a glycoprotein AND two putative N-linked glycosylation sites a glycoprotein two putative N-linked glycosylation sites Fterm Site glycoprotein sites PRiMA is a glycoprotein containing two putative N-linked glycosylation sites. 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. 3524673 10 15 part_of site 1018:1021 arg1 fibronectin fibronectin site PUBTATOR Site fibronectin 2335 site The protein also contains the tetrapeptide sequence Arg-Gly-Asp-Ser (at residues 1744-1747), which may be a cell attachment site, as in fibronectin. 3524673 10 57 part_of contains 911:918 arg1 The protein AND the tetrapeptide sequence Arg-Gly-Asp-Ser The protein the tetrapeptide sequence Arg-Gly-Asp-Ser Fterm Site protein Arg-Gly-Asp-Ser The protein also contains the tetrapeptide sequence Arg-Gly-Asp-Ser (at residues 1744-1747), which may be a cell attachment site, as in fibronectin. 3524673 10 57 part_of contains 911:918 arg1 The protein AND a cell attachment site The protein a cell attachment site Fterm Site protein site The protein also contains the tetrapeptide sequence Arg-Gly-Asp-Ser (at residues 1744-1747), which may be a cell attachment site, as in fibronectin. 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. 7681597 1 30 part_of GPA-1 265:269 arg1 the glycopeptides GPA the glycopeptides OGER Site GPA P02724 glycopeptides Glycophorin A was digested with glycoprotease (Pasteurella haemolytica) and the digest was fractionated by a combination of high-pressure column chromatographies to produce the glycopeptides GPA-1 to GPA-6. 22235133 6 19 part_of IL-21R 886:891 arg1 the WSXWS motif IL-21R the WSXWS motif PUBTATOR Site IL-21R 50615 motif Here, we present the crystal structure of IL-21 bound to IL-21R and reveal that the WSXWS motif of IL-21R is C-mannosylated at the first tryptophan. 17196528 1 20 part_of NGF 253:255 arg1 a "high-affinity" NGF binding site NGF a "high-affinity" NGF binding site OGER Site NGF P01138 site Nerve growth factor engages two structurally distinct transmembrane receptors, TrkA and p75, which have been proposed to create a "high-affinity" NGF binding site through formation of a ternary TrkA/NGF/p75 complex. 7574684 2 62 part_of trkB 503:506 arg1 the extracellular domain trkB the extracellular domain PUBTATOR Site trkB 4915 domain The extracellular domain contains 398 amino acids and has a molecular weight of 60.6 kDa according to laser desorption mass spectrometry, indicating that the extracellular domain of trkB contains 33.3% carbohydrate moieties. 26146185 1 14 part_of receptor 163:170 arg1 three scavenger receptor cysteine rich (SRCR) domains receptor three scavenger receptor cysteine rich (SRCR) domains Fterm Site receptor domains CD6 is a transmembrane protein with an extracellular region containing three scavenger receptor cysteine rich (SRCR) domains. 26146185 1 19 part_of protein 99:105 arg1 an extracellular region protein an extracellular region Fterm Site protein region CD6 is a transmembrane protein with an extracellular region containing three scavenger receptor cysteine rich (SRCR) domains. 26146185 1 16 part_of containing 136:145 arg1 an extracellular region AND three scavenger receptor cysteine rich (SRCR) domains an extracellular region three scavenger receptor cysteine rich (SRCR) domains domains CD6 is a transmembrane protein with an extracellular region containing three scavenger receptor cysteine rich (SRCR) domains. 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. 17803912 3 23 part_of TLR4 355:358 arg1 the full-length ectodomain TLR4 the full-length ectodomain PUBTATOR Site TLR4 21898 ectodomain We determined the structure of the full-length ectodomain of the mouse TLR4 and MD-2 complex. 21615908 4 28 part_of 2.5-kbp 548:554 arg1 A 2.5-kbp genomic sequence fragment kbp A 2.5-kbp genomic sequence fragment OGER Site kbp Q6ZPU9 fragment A 2.5-kbp genomic sequence fragment upstream of the coding sequence is sufficient to drive and regulate fibin expression through stimulation by glucocorticoids, activators of the protein kinase C signalling pathways and manganese ions. 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. 3571235 4 9 part_of sialoglycoprotein 624:640 arg1 the hydrophobic region sialoglycoprotein the hydrophobic region Fterm Site sialoglycoprotein region The amino acid sequence of the intramembranous domain (residues 36-71) of glycophorin B was determined and found to be similar to that of the hydrophobic region of the major sialoglycoprotein (glycophorin A). 3571235 4 18 part_of B 536:536 arg1 the intramembranous domain glycophorin B the intramembranous domain PUBTATOR Site glycophorin B 2994 domain The amino acid sequence of the intramembranous domain (residues 36-71) of glycophorin B was determined and found to be similar to that of the hydrophobic region of the major sialoglycoprotein (glycophorin A). 3571235 4 18 part_of B 536:536 arg1 residues 36-71 glycophorin B residues 36-71 PUBTATOR SpecificSite glycophorin B 2994 residues 36-71 The amino acid sequence of the intramembranous domain (residues 36-71) of glycophorin B was determined and found to be similar to that of the hydrophobic region of the major sialoglycoprotein (glycophorin A). 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. 9023546 5 14 part_of EGF 716:718 arg1 complete EGF domains EGF complete EGF domains PUBTATOR Site EGF 1950 domains These synthetic peptides did not compromise complete EGF domains and did not contain all six cysteine residues that define the EGF structure. 9023546 5 30 part_of contain 740:746 arg1 These synthetic peptides AND all six cysteine residues These synthetic peptides all six cysteine residues cysteine residues These synthetic peptides did not compromise complete EGF domains and did not contain all six cysteine residues that define the EGF structure. 4742735 2 8 part_of immunoglobulin 288:301 arg1 the constant regions immunoglobulin the constant regions Fterm Site immunoglobulin regions The homology of the constant regions of immunoglobulin micro, gamma, alpha, and epsilon heavy chains reveals evolutionary relationships and suggests that two genes code for each heavy chain. 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. 30140003 4 12 part_of GnT-V 534:538 arg1 human GnT-V luminal domain GnT-V human GnT-V luminal domain PUBTATOR Site GnT-V 4249 domain Here, we report crystal structures of human GnT-V luminal domain with a substrate analog. 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. 22344443 3 3 part_of receptor 561:568 arg1 amino terminus receptor amino terminus Fterm Site receptor terminus Extracellular access to the binding pocket is occluded by the amino terminus and extracellular loops of the receptor. 10644446 5 9 part_of 455-acid 713:720 arg1 a 455-acid polypeptide 455-acid a 455-acid polypeptide Cterm Site 455-acid polypeptide Murine ANGPTL3 is a 455-acid polypeptide encoded by seven exons on mouse chromosome 4, spanning about 11 kb of DNA. 10644446 5 27 part_of Murine 693:698 arg1 a 455-acid polypeptide Murine ANGPTL3 a 455-acid polypeptide PUBTATOR Site Murine ANGPTL3 30924 polypeptide Murine ANGPTL3 is a 455-acid polypeptide encoded by seven exons on mouse chromosome 4, spanning about 11 kb of DNA. 3497398 10 66 part_of contains 1528:1535 arg1 The determined sequence AND residues 29-193 The determined sequence residues 29-193 residues 29-193 The determined sequence of the alpha chain of glycoprotein Ib contains a region (residues 29-193) with seven repeats, which is indicative of gene duplication and is highly homologous to human leucine-rich alpha 2-glycoprotein. 3497398 10 66 part_of contains 1528:1535 arg1 The determined sequence AND a region The determined sequence a region region The determined sequence of the alpha chain of glycoprotein Ib contains a region (residues 29-193) with seven repeats, which is indicative of gene duplication and is highly homologous to human leucine-rich alpha 2-glycoprotein. 9748270 3 67 part_of XVII 345:348 arg1 recombinant collagen XVII fragments XVII recombinant collagen XVII fragments Cterm Site XVII fragments Using domain-specific antibodies against recombinant collagen XVII fragments, we identified two molecular forms of the collagen in human skin and epithelial cells. 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. 22579623 2 33 part_of Fab 412:414 arg1 three neutralizing Fab fragments Fab three neutralizing Fab fragments PUBTATOR Site Fab 2187 fragments We report the crystal structure of human TLR3 ectodomain (TLR3ecd) in a quaternary complex with three neutralizing Fab fragments. 22579623 2 58 part_of TLR3 338:341 arg1 human TLR3 ectodomain TLR3 human TLR3 ectodomain PUBTATOR Site TLR3 7098 ectodomain We report the crystal structure of human TLR3 ectodomain (TLR3ecd) in a quaternary complex with three neutralizing Fab fragments. 28753425 5 0 part_of vasopressin-2 944:956 arg1 the phosphorylated vasopressin-2 receptor tail vasopressin-2 receptor the phosphorylated vasopressin-2 receptor tail PUBTATOR Site vasopressin-2 receptor 554 tail These two phospho-residues, together with E341, form an extensive network of electrostatic interactions with three positively charged pockets in arrestin in a mode that resembles binding of the phosphorylated vasopressin-2 receptor tail to β-arrestin-1. 28753425 5 12 part_of receptor 958:965 arg1 the phosphorylated vasopressin-2 receptor tail vasopressin-2 receptor the phosphorylated vasopressin-2 receptor tail PUBTATOR Site vasopressin-2 receptor 554 tail These two phospho-residues, together with E341, form an extensive network of electrostatic interactions with three positively charged pockets in arrestin in a mode that resembles binding of the phosphorylated vasopressin-2 receptor tail to β-arrestin-1. 22660477 6 22 part_of GBR2 747:750 arg1 the GBR2 ectodomain structure of the GBR2 the GBR2 ectodomain Cterm Site structure of the GBR2 ectodomain We present the crystal structure of the GBR2 ectodomain, which reveals a polar heterodimeric interface. 1400872 3 22 part_of SHBG 685:688 arg1 the SHBG polypeptide SHBG the SHBG polypeptide PUBTATOR Site SHBG P04278 polypeptide Sequence analysis of these exons revealed a point mutation encoding an amino acid substitution (Asp --> Asn) at residue 327 in the SHBG polypeptide, and the same mutation was identified in three siblings who also appear to be homozygous for this trait. 16732286 3 1 part_of factor 472:477 arg1 the three epidermal growth factor domains factor the three epidermal growth factor domains Fterm Site factor domains In contrast to prediction, Tie2 contains not two but three immunoglobulin (Ig) domains, which fold together with the three epidermal growth factor domains into a compact, arrowhead-shaped structure. 16732286 3 13 part_of contains 364:371 arg1 Tie2 AND not two but three immunoglobulin (Ig) domains Tie2 not two but three immunoglobulin (Ig) domains PUBTATOR Site Tie2 7010 domains In contrast to prediction, Tie2 contains not two but three immunoglobulin (Ig) domains, which fold together with the three epidermal growth factor domains into a compact, arrowhead-shaped structure. 31959827 2 23 part_of IgA1 226:229 arg1 IgA1 hinge region IgA1 IgA1 hinge region PUBTATOR Site IgA1 P01876 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. 28775322 2 12 part_of EGF-like 339:346 arg1 folded EGF-like domains EGF folded EGF-like domains OGER Site EGF P01133 domains Protein O-glucosyltransferase 1 shows specificity for folded EGF-like domains, it can only glycosylate serine residues in the C1XSXPC2 motif, and it possesses an uncommon dual donor substrate specificity. 2668275 6 70 part_of STS 715:717 arg1 most, if not all, sequences STS most, if not all, sequences OGER Site STS P08842 sequences The resistance of STS toward proteinase K after translocation into microsomes suggests that most, if not all, sequences of STS are exposed at the luminal side of microsomes. 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. 23846701 9 62 part_of HC 1095:1096 arg1 β-domains HC β-domains PUBTATOR Site HC 6947 β-domains In addition, the α- and β-domains of HC form several unique interdomain contacts and have a higher shape complementarity than those of intrinsic factor and transcobalamin. 10821832 1 10 part_of reductase 471:479 arg1 the sterol-sensing domains 3-hydroxy-3-methylglutaryl-coenzyme A reductase the sterol-sensing domains PUBTATOR Site 3-hydroxy-3-methylglutaryl-coenzyme A reductase 3156 domains The Niemann-Pick C1 (NPC1) protein is predicted to be a polytopic glycoprotein, and it contains a region with extensive homology to the sterol-sensing domains (SSD) of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-R) and sterol regulatory element binding protein cleavage-activating protein (SCAP). 10821832 1 12 part_of protein 555:561 arg1 the sterol-sensing domains sterol regulatory element binding protein cleavage-activating protein the sterol-sensing domains PUBTATOR Site sterol regulatory element binding protein cleavage-activating protein 22937 domains The Niemann-Pick C1 (NPC1) protein is predicted to be a polytopic glycoprotein, and it contains a region with extensive homology to the sterol-sensing domains (SSD) of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-R) and sterol regulatory element binding protein cleavage-activating protein (SCAP). 17157876 0 29 part_of kininase 51:58 arg1 the human carboxypeptidase N (kininase I) catalytic domain kininase I the human carboxypeptidase N (kininase I) catalytic domain PUBTATOR Site kininase I 1369 domain Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain. 17157876 0 49 part_of N 48:48 arg1 the human carboxypeptidase N (kininase I) catalytic domain carboxypeptidase N the human carboxypeptidase N (kininase I) catalytic domain PUBTATOR Site carboxypeptidase N 1369 domain Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain. 17157876 0 97 part_of carboxypeptidase 31:46 arg1 the human carboxypeptidase N (kininase I) catalytic domain carboxypeptidase N the human carboxypeptidase N (kininase I) catalytic domain PUBTATOR Site carboxypeptidase N 1369 domain Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain. 3458201 5 16 part_of has 714:716 arg1 alpha 1B AND a unique amino acid sequence alpha 1B a unique amino acid sequence PUBTATOR Site alpha 1B 1 sequence alpha 1B has a unique amino acid sequence. 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. 3524673 9 0 part_of factor 792:797 arg1 The sequence von Willebrand factor The sequence PUBTATOR Site von Willebrand factor 7450 sequence The sequence of von Willebrand factor includes several regions bearing evidence of internal gene duplication of ancestral sequences. 22041449 4 16 part_of contains 703:710 arg1 the LN domain region AND the binding site the LN domain region the binding site site Here, we use deletion analysis to show that the LN domain region of netrin Gs contains the binding site for NGLs to which they bind with 1:1 stoichiometry and sub-micromolar affinity. 24927598 7 26 gly glycosylation 953:965 arg1 ZIP14 ZIP14 PUBTATOR ZIP14 23516 Asparagine-linked (N-linked) glycosylation of ZIP14, particularly the glycosylation at N102, was required for efficient membrane extraction of ZIP14 and therefore is necessary for its iron sensitivity. 24927598 7 49 gly glycosylation 994:1006 arg2 N102 N102 N102 Asparagine-linked (N-linked) glycosylation of ZIP14, particularly the glycosylation at N102, was required for efficient membrane extraction of ZIP14 and therefore is necessary for its iron sensitivity. 9689040 7 16 part_of fibrinogen 921:930 arg1 gamma-chain carboxyl domains fibrinogen gamma-chain carboxyl domains PUBTATOR Site fibrinogen 2244 domains Comparison with structures of the beta- and gamma-chain carboxyl domains of human fibrinogen revealed that the binding cleft is essentially neutral and should not bind Gly-Pro-Arg or Gly-His-Arg peptides of the sort bound by those other domains. 18508581 6 17 gly glycosylation 804:816 arg2 asparagine198 asparagine198 asparagine198 We show that glycosylation at asparagine198 is crucial for protein stability. 11502179 10 60 part_of receptor 1530:1537 arg1 the soluble ectodomain TSH receptor the soluble ectodomain PUBTATOR Site TSH receptor 7253 ectodomain Contrary to all currently available assays, the soluble ectodomain of the TSH receptor purified in a functionally competent conformation allows direct studies of its interactions with TSH and autoantibodies and opens the way to structural studies. 2498325 7 68 part_of Apolipoprotein 945:958 arg1 Thr194----Ala Apolipoprotein E Thr194----Ala PUBTATOR AminoAcid Apolipoprotein E 348 Thr194 Apolipoprotein E(Thr194----Ala) was secreted exclusively as the asialo isoform, confirming that Thr194 is the site of carbohydrate attachment in these cells and indicating that glycosylation of apoE is not essential for secretion. 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. 1710976 12 12 part_of Peptide 1287:1293 arg1 Peptide Asn-Gly-Ser Peptide Peptide Asn-Gly-Ser OGER Site Peptide Asn-Gly-Ser Peptide Asn-Gly-Ser (residues 427-429) is the most probable candidate for glycosylation; literature data suggests that deamidation occurs in the stretch Glu-Asn-Gly-Lys-Asp (residues 364-368) and Asn-Gly-Asn-Cys (residues 474-477). 1710976 12 12 part_of Peptide 1287:1293 arg1 residues 427-429 Peptide residues 427-429 OGER SpecificSite Peptide residues 427-429 Peptide Asn-Gly-Ser (residues 427-429) is the most probable candidate for glycosylation; literature data suggests that deamidation occurs in the stretch Glu-Asn-Gly-Lys-Asp (residues 364-368) and Asn-Gly-Asn-Cys (residues 474-477). 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 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. 18065761 6 52 part_of TSPN-1 1152:1157 arg1 several TSPN-1 domains TSPN-1 several TSPN-1 domains Cterm Site TSPN-1 domains The ability of several TSPN-1 domains to bind to glycosaminoglycans simultaneously probably increases the affinity of binding through multivalent interactions. 18467335 12 69 part_of PCI 1565:1567 arg1 the N-terminal region PCI the N-terminal region OGER Site PCI P05154 region These results thus demonstrate that the N-linked glycans and the N-terminal region of blood-derived PCI in different ways affect the cofactor-enhanced rates of thrombin inhibition and provide information on the mechanisms by which this may be achieved. 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. 12122212 3 10 part_of CD21 410:413 arg1 the CD21 SCR1-SCR2 fragment structure of the CD21 the CD21 SCR1-SCR2 fragment Cterm Site structure of the CD21 1380 fragment Here we present the crystal structure of the CD21 SCR1-SCR2 fragment in the absence of ligand and demonstrate that it is able to bind EBV. 12122212 3 55 part_of SCR1-SCR2 415:423 arg1 the CD21 SCR1-SCR2 fragment SCR2 the CD21 SCR1-SCR2 fragment PUBTATOR Site SCR2 5937 fragment Here we present the crystal structure of the CD21 SCR1-SCR2 fragment in the absence of ligand and demonstrate that it is able to bind EBV. 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. 22809326 7 23 part_of DC-LAMP 957:963 arg1 the conserved domain DC-LAMP the conserved domain PUBTATOR Site DC-LAMP 27074 domain RESULTS: The crystal structure of the conserved domain of human DC-LAMP was solved. 2141278 3 52 part_of EGF-like 708:715 arg1 the epidermal growth factor-like (EGF-like) region EGF the epidermal growth factor-like (EGF-like) region OGER Site EGF P01133 region Fragment alpha 2, which comprised the epidermal growth factor-like (EGF-like) region of C1-s, was heterogeneous, starting at serine 97 or phenylalanine 105 and ending at lysine 195. 2141278 3 60 part_of factor-like 695:705 arg1 the epidermal growth factor-like (EGF-like) region factor the epidermal growth factor-like (EGF-like) region Fterm Site factor region Fragment alpha 2, which comprised the epidermal growth factor-like (EGF-like) region of C1-s, was heterogeneous, starting at serine 97 or phenylalanine 105 and ending at lysine 195. 2141278 3 66 part_of C1-s 728:731 arg1 the epidermal growth factor-like (EGF-like) region C1-s the epidermal growth factor-like (EGF-like) region PUBTATOR Site C1-s 716 region Fragment alpha 2, which comprised the epidermal growth factor-like (EGF-like) region of C1-s, was heterogeneous, starting at serine 97 or phenylalanine 105 and ending at lysine 195. 20934432 6 45 part_of IFN 765:767 arg1 the IFN site IFN the IFN site PUBTATOR Site IFN 3439 site The ligand-receptor interface includes helix A, loop AB, and helix F on the IFN site, as well as loops primarily from the N-terminal domain and inter-domain hinge region of IFN-λR1. 20934432 6 53 part_of IFN-λR1 862:868 arg1 inter-domain hinge region IFN-λR1 inter-domain hinge region PUBTATOR Site IFN-λR1 163702 region The ligand-receptor interface includes helix A, loop AB, and helix F on the IFN site, as well as loops primarily from the N-terminal domain and inter-domain hinge region of IFN-λR1. 20934432 6 53 part_of IFN-λR1 862:868 arg1 the N-terminal domain IFN-λR1 the N-terminal domain PUBTATOR Site IFN-λR1 163702 domain The ligand-receptor interface includes helix A, loop AB, and helix F on the IFN site, as well as loops primarily from the N-terminal domain and inter-domain hinge region of IFN-λR1. 19571171 0 8 gly N-glycosylation 11:25 arg1 GlcNAc-6-sulfotransferase 1 GlcNAc-6-sulfotransferase 1 Fterm GlcNAc-6-sulfotransferase 1 Effects of N-glycosylation on the activity and localization of GlcNAc-6-sulfotransferase 1. 12600216 7 7 gly N-glycosylation 1153:1167 arg2 N-glycosylation sites N-glycosylation sites sites In this study, we have determined which of the connecting loops are exposed to the extracellular milieu using two different methods: accessibility of substituted cysteine residues and insertion of N-glycosylation sites. 20511397 5 39 gly detected 1025:1032 arg1 194 AND the most complex glycan Thr(194) the most complex glycan Thr(194) Our results identify eight different glycoforms with (HexNAc)(2)-Hex(2)-(NeuAc)(2) being the most complex glycan detected on Thr(194) in both cellular and secreted apoE. 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. 19004833 3 7 part_of residues 440:447 arg1 DS-epimerase 1 DS-epimerase 1 residues OGER AminoAcid DS-epimerase 1 Q9UL01 residues in We have identified the catalytic site and three putative catalytic residues in DS-epimerase 1, His-205, Tyr-261, and His-450, by tertiary structure modeling and amino acid conservation to heparinase II. 19004833 3 63 part_of site 406:409 arg1 DS-epimerase 1 DS-epimerase 1 site OGER Site DS-epimerase 1 Q9UL01 site We have identified the catalytic site and three putative catalytic residues in DS-epimerase 1, His-205, Tyr-261, and His-450, by tertiary structure modeling and amino acid conservation to heparinase II. 20877282 4 48 part_of PLXNB1 868:873 arg1 semaphorin ectodomains PLXNB1 semaphorin ectodomains OGER Site PLXNB1 O43157 ectodomains Here we present crystal structures of cognate complexes of the semaphorin-binding regions of plexins B1 and A2 with semaphorin ectodomains (human PLXNB1(1-2)-SEMA4D(ecto) and murine PlxnA2(1-4)-Sema6A(ecto)), plus unliganded structures of PlxnA2(1-4) and Sema6A(ecto). 20877282 4 51 part_of semaphorin 838:847 arg1 semaphorin ectodomains semaphorin semaphorin ectodomains Fterm Site semaphorin ectodomains Here we present crystal structures of cognate complexes of the semaphorin-binding regions of plexins B1 and A2 with semaphorin ectodomains (human PLXNB1(1-2)-SEMA4D(ecto) and murine PlxnA2(1-4)-Sema6A(ecto)), plus unliganded structures of PlxnA2(1-4) and Sema6A(ecto). 20877282 4 54 part_of PlxnA2 904:909 arg1 semaphorin ectodomains PlxnA2 semaphorin ectodomains OGER Site PlxnA2 O75051 ectodomains Here we present crystal structures of cognate complexes of the semaphorin-binding regions of plexins B1 and A2 with semaphorin ectodomains (human PLXNB1(1-2)-SEMA4D(ecto) and murine PlxnA2(1-4)-Sema6A(ecto)), plus unliganded structures of PlxnA2(1-4) and Sema6A(ecto). 20877282 4 88 part_of semaphorin-binding 785:802 arg1 the semaphorin-binding regions semaphorin the semaphorin-binding regions Fterm Site semaphorin regions Here we present crystal structures of cognate complexes of the semaphorin-binding regions of plexins B1 and A2 with semaphorin ectodomains (human PLXNB1(1-2)-SEMA4D(ecto) and murine PlxnA2(1-4)-Sema6A(ecto)), plus unliganded structures of PlxnA2(1-4) and Sema6A(ecto). 19563754 4 8 part_of NPC1 464:467 arg1 the N-terminal domain NPC1 the N-terminal domain PUBTATOR Site NPC1 O15118 domain Here, we describe high-resolution structures of the N-terminal domain (NTD) of NPC1 and complexes with cholesterol and 25-hydroxycholesterol. 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. 34074792 1 76 part_of protein 246:252 arg1 intrinsically disordered protein regions protein intrinsically disordered protein regions Fterm Site protein regions The role of biomolecular condensates in regulating biological function and the importance of dynamic interactions involving intrinsically disordered protein regions (IDRs) in their assembly are increasingly appreciated. 9883900 0 22 part_of protein-5 118:126 arg1 circulating 13-kDa C-terminal fragments protein-5 circulating 13-kDa C-terminal fragments Fterm Site protein-5 fragments Isolation and characterization of circulating 13-kDa C-terminal fragments of human insulin-like growth factor binding protein-5. 7574684 1 22 part_of trkB 173:176 arg1 An extracellular domain trkB An extracellular domain PUBTATOR Site trkB 4915 domain An extracellular domain of a human neurotrophin receptor trkB was expressed in Chinese hamster ovary cells and isolated as a glycoprotein possessing binding activity for brain-derived neurotrophic factor. 19122660 2 12 part_of factor-beta 409:419 arg1 the prodomain factor-beta the prodomain Fterm Site factor-beta prodomain Binding competition studies suggest that additional binding sites, for example, for the prodomain of nerve growth factor-beta, are present in the tunnel and that competition for binding relates to the restricted space inside the propeller. 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. 8962717 1 25 part_of receptor 251:258 arg1 The extracellular domain receptor The extracellular domain Fterm Site receptor domain The extracellular domain (621 N-terminal amino acids) of the p170 epidermal growth factor (EGF) receptor has eleven consensus N-linked glycosylation sites. 8962717 1 16 part_of has 260:262 arg1 the p170 epidermal growth factor (EGF) receptor AND eleven consensus N-linked glycosylation sites receptor sites Fterm Site receptor sites The extracellular domain (621 N-terminal amino acids) of the p170 epidermal growth factor (EGF) receptor has eleven consensus N-linked glycosylation sites. 24226769 0 65 gly glycosylates 28:39 arg1 Notch Notch PUBTATOR Notch 100037842 The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type and laterality. 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. 22483115 0 7 part_of Fab 89:91 arg1 an inhibitory Fab fragment Fab an inhibitory Fab fragment PUBTATOR Site Fab 2187 fragment Structure of the discoidin domain receptor 1 extracellular region bound to an inhibitory Fab fragment reveals features important for signaling. 22483115 0 31 part_of receptor 34:41 arg1 the discoidin domain receptor 1 extracellular region receptor 1 the discoidin domain receptor 1 extracellular region Fterm Site receptor 1 780 region Structure of the discoidin domain receptor 1 extracellular region bound to an inhibitory Fab fragment reveals features important for signaling. 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. 10871631 3 87 part_of A 593:593 arg1 the C terminus torsin A the C terminus PUBTATOR Site torsin A 1861 terminus The deletion in DYT1 associated with torsion dystonia results in the loss of one of a pair of glutamic acid residues residing near the C terminus of torsin A (DeltaE-torsin A). 17715132 0 15 part_of contain 19:25 arg1 Pannexin1 channels AND a glycosylation site Pannexin1 channels a glycosylation site PUBTATOR Site Pannexin1 channels 24145 site Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane. 20188224 8 28 gly deglycosylated 1157:1170 arg1 deglycosylated protein deglycosylated protein Fterm protein In-gel tryptic digestion was further applied to the gel pieces containing deglycosylated protein, for N-glycosylation site determination. 22020283 4 25 part_of HLA 1090:1092 arg1 an 'innate HLA sensor' domain HLA an 'innate HLA sensor' domain OGER Site HLA domain First, the D0 domain, a distinguishing feature of the KIR3D family, extended towards β2-microglobulin and abutted a region of the HLA molecule with limited polymorphism, thereby acting as an 'innate HLA sensor' domain. 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. 10022822 6 54 part_of p41 924:926 arg1 the p41 fragment p41 the p41 fragment Cterm Site p41 fragment The wedge shape and three-loop arrangement of the p41 fragment bound to the active site cleft of cathepsin L are reminiscent of the inhibitory edge of cystatins, thus demonstrating the first example of convergent evolution observed in cysteine protease inhibitors. 26274980 6 63 part_of nCG 1749:1751 arg1 nCG Asn71-glycosylation nCG nCG Asn71-glycosylation Cterm AminoAcid nCG 1511 Asn71 Importantly, this study now facilitates investigation of the functional role of nCG Asn71-glycosylation. 19836338 2 70 part_of EphA4 332:336 arg1 the EphA4 ligand binding domain structure of the EphA4 the EphA4 ligand binding domain PUBTATOR Site structure of the EphA4 2043 domain We have solved the crystal structure of the EphA4 ligand binding domain alone and in complex with (1) ephrinB2 and (2) ephrinA2. 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. 15657036 10 44 part_of sequence 1159:1166 arg1 The first two cysteine residues sequence The first two cysteine residues cysteine residues The first two cysteine residues are located in the sequence preceding the N-terminal protease-resistant domain. 16169851 5 13 part_of HVEM 588:591 arg1 the N-terminal cysteine-rich domain HVEM the N-terminal cysteine-rich domain PUBTATOR Site HVEM 8764 domain This structure shows that BTLA binds the N-terminal cysteine-rich domain of HVEM and employs a unique binding surface compared with other CD28-like receptors. 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. 10419520 1 11 part_of proteins 261:268 arg1 the NH(2)-terminal domains proteins the NH(2)-terminal domains Fterm Site proteins domains In sterol-depleted mammalian cells, a two-step proteolytic process releases the NH(2)-terminal domains of sterol regulatory element-binding proteins (SREBPs) from membranes of the endoplasmic reticulum (ER). 3840370 5 41 part_of protein 832:838 arg1 the sequence protein the sequence Fterm Site protein sequence The plasmid clones isolated allowed the unambiguous determination of 1717 nucleotides of cDNA sequence between the codon for the 32nd amino acid in the sequence of C4b-binding protein and the 164th nucleotide in the 3' non-translated region. 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. 28377511 3 19 part_of receptors 588:596 arg1 the cysteine-rich domain FZD receptors the cysteine-rich domain PUBTATOR Site FZD receptors 7855 domain Despite the progress in biochemical understanding of Wnt-FZD receptor interactions, the molecular basis for recognition of Wnt cis-unsaturated fatty acyl groups by the cysteine-rich domain (CRD) of FZD receptors remains elusive. 3353370 9 72 part_of protein 1958:1964 arg1 the carboxyl terminus protein the carboxyl terminus Fterm Site protein terminus The amino-terminal region of the beta chain of GPIb is followed by a transmembrane segment of 25 amino acids and an intracellular segment of 34 amino acids at the carboxyl terminus of the protein. 18467335 7 84 gly epitopes 894:901 arg1 Fucose residues epitopes Fucose residues epitopes Fucose residues were identified both on the core GlcNAc and as parts of sialyl-Le(a/x) epitopes. 10769135 0 46 part_of alpha-amylase 40:52 arg1 the human pancreatic alpha-amylase active site pancreatic alpha-amylase the human pancreatic alpha-amylase active site PUBTATOR Site pancreatic alpha-amylase 279 site Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques. 10769135 0 90 part_of pancreatic 29:38 arg1 the human pancreatic alpha-amylase active site pancreatic alpha-amylase the human pancreatic alpha-amylase active site PUBTATOR Site pancreatic alpha-amylase 279 site Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques. 15662415 3 17 part_of receptor 430:437 arg1 the extracellular hormone-binding domain receptor the extracellular hormone-binding domain Fterm Site receptor domain We present here the 2.9-A-resolution structure of a partially deglycosylated complex of human FSH bound to the extracellular hormone-binding domain of its receptor (FSHR(HB)). 6203908 13 58 part_of 2-macroglobulin 1383:1397 arg1 sequences alpha 2-macroglobulin sequences PUBTATOR Site alpha 2-macroglobulin P01023 sequences A comparison of stretches of sequences from alpha 2-macroglobulin with partial sequence data for complement components C3 and C4 indicates that these proteins are evolutionary related. 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. 10419520 10 53 part_of S2P 1308:1310 arg1 The HEIGH sequence S2P The HEIGH sequence OGER Site S2P O43462 sequence The HEIGH sequence of S2P, which contains two potential zinc-coordinating residues, is contained within a long hydrophobic segment. 10419520 10 27 part_of contains 1319:1326 arg1 The HEIGH sequence AND two potential zinc-coordinating residues The HEIGH sequence two potential zinc-coordinating residues residues The HEIGH sequence of S2P, which contains two potential zinc-coordinating residues, is contained within a long hydrophobic segment. 29374258 4 28 part_of contains 665:672 arg1 PGAP4 AND three transmembrane domains PGAP4 three transmembrane domains OGER Site PGAP4 Q9BRR3 domains Furthermore, we demonstrate that PGAP4, in contrast to known Golgi glycosyltransferases, is not a single-pass membrane protein but contains three transmembrane domains, including a tandem transmembrane domain insertion into its glycosyltransferase-A fold as indicated by comparative modeling. 29374258 4 28 part_of contains 665:672 arg1 a single-pass membrane protein AND three transmembrane domains a single-pass membrane protein three transmembrane domains Fterm Site protein domains Furthermore, we demonstrate that PGAP4, in contrast to known Golgi glycosyltransferases, is not a single-pass membrane protein but contains three transmembrane domains, including a tandem transmembrane domain insertion into its glycosyltransferase-A fold as indicated by comparative modeling. 28165004 6 7 part_of PD-1 779:782 arg1 the IgV domain PD-1 the IgV domain PUBTATOR Site PD-1 P18621 domain Structural and functional analyses unexpectedly reveal an N-terminal loop outside the IgV domain of PD-1. 18065761 2 1 part_of heparin-binding 371:385 arg1 the high affinity heparin-binding domain heparin the high affinity heparin-binding domain Fterm Site heparin domain We have previously determined the structure of the high affinity heparin-binding domain of TSP-1, designated TSPN-1, in association with the synthetic heparin, Arixtra. 18065761 2 31 part_of TSP-1 397:401 arg1 the high affinity heparin-binding domain TSP-1 the high affinity heparin-binding domain PUBTATOR Site TSP-1 7057 domain We have previously determined the structure of the high affinity heparin-binding domain of TSP-1, designated TSPN-1, in association with the synthetic heparin, Arixtra. 22333914 2 24 part_of ∼320-residue 423:434 arg1 a much larger ∼320-residue domain r ∼320-residue a much larger ∼320-residue domain PUBTATOR Site r ∼320-residue 23218 domain Here, we show that unexpectedly the ∼40-residue GPS motif represents an integral part of a much larger ∼320-residue domain that we termed GPCR-Autoproteolysis INducing (GAIN) domain. 22333914 2 28 part_of GPS 368:370 arg1 unexpectedly the ∼40-residue GPS motif GPS unexpectedly the ∼40-residue GPS motif OGER Site GPS motif Here, we show that unexpectedly the ∼40-residue GPS motif represents an integral part of a much larger ∼320-residue domain that we termed GPCR-Autoproteolysis INducing (GAIN) domain. 22333914 2 35 part_of GPCR-Autoproteolysis 458:477 arg1 GPCR-Autoproteolysis INducing (GAIN) domain d GPCR GPCR-Autoproteolysis INducing (GAIN) domain PUBTATOR Site d GPCR 23218 domain Here, we show that unexpectedly the ∼40-residue GPS motif represents an integral part of a much larger ∼320-residue domain that we termed GPCR-Autoproteolysis INducing (GAIN) domain. 22333914 2 41 part_of larger 416:421 arg1 a much larger ∼320-residue domain l a much larger ∼320-residue domain PUBTATOR Site l 23218 domain Here, we show that unexpectedly the ∼40-residue GPS motif represents an integral part of a much larger ∼320-residue domain that we termed GPCR-Autoproteolysis INducing (GAIN) domain. 24121512 6 21 part_of cdAE1 1228:1232 arg1 55-356 cdAE1 55-356 Cterm SpecificSite cdAE1 6521 residues 55-356 A 2.1-Å resolution crystal structure of cdΔ54AE1 (residues 55-356 of cdAE1) lacking the amino-terminal and carboxyl-terminal disordered regions, produced at physiological pH, revealed an extensive hydrogen-bonded network involving Arg(283) and Glu(85). 12526797 2 13 part_of ICAM-1 366:371 arg1 Glu-34 ICAM-1 Glu-34 PUBTATOR SpecificSite ICAM-1 3383 Glu-34 The I domain Mg2+ directly coordinates Glu-34 of ICAM-1, and a dramatic swing of I domain residue Glu-241 enables a critical salt bridge. 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. 20877282 7 13 part_of semaphorin 1694:1703 arg1 the amino-terminal seven-bladed β-propeller (sema) domains semaphorin the amino-terminal seven-bladed β-propeller (sema) domains Fterm Site semaphorin domains Furthermore, the shared generic architecture of the complexes, formed through conserved contacts of the amino-terminal seven-bladed β-propeller (sema) domains of both semaphorin and plexin, suggests that a common mode of interaction triggers all semaphorin-plexin based signalling, while distinct insertions within or between blades of the sema domains determine binding specificity. 20877282 7 52 part_of plexin 1709:1714 arg1 the amino-terminal seven-bladed β-propeller (sema) domains plexin the amino-terminal seven-bladed β-propeller (sema) domains Fterm Site plexin domains Furthermore, the shared generic architecture of the complexes, formed through conserved contacts of the amino-terminal seven-bladed β-propeller (sema) domains of both semaphorin and plexin, suggests that a common mode of interaction triggers all semaphorin-plexin based signalling, while distinct insertions within or between blades of the sema domains determine binding specificity. 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. 18070108 10 3 part_of BMP-6 1500:1504 arg1 the binding epitope BMP-6 the binding epitope PUBTATOR Site BMP-6 654 epitope 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. 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. 16754968 2 0 part_of region 544:549 arg1 position region position position A minor improvement in resolution has resulted in improved electron-density maps, which have given a clearer indication of the position and stabilization of the key residues Tyr15, Phe79, Tyr347, His349, Ile350 and Tyr403 in the elbow region between domain 1 and domain 4 of the dimer-related molecule. 2141278 0 8 part_of factor 95:100 arg1 the epidermal growth factor homology region factor the epidermal growth factor homology region Fterm Site factor region Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region. 2141278 0 63 part_of C1-s 58:61 arg1 a fragment C1-s a fragment PUBTATOR Site C1-s 716 fragment Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region. 2141278 0 2 part_of containing 63:72 arg1 C1-s AND the epidermal growth factor homology region C1-s the epidermal growth factor homology region PUBTATOR Site C1-s 716 region Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region. 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. 23878260 3 53 part_of VEGFRs 489:494 arg1 The extracellular domain VEGFRs The extracellular domain PUBTATOR Site VEGFRs 2324 domain The extracellular domain of VEGFRs consists of seven Ig homology domains; domains 1-3 (D1-3) are responsible for ligand binding, and the membrane-proximal domains 4-7 (D4-7) are involved in structural rearrangements essential for receptor dimerization and activation. 18491227 3 52 gly N-glycosylation 628:642 arg1 Asn-633 Asn-633 Asn-633 In this study we investigated the molecular mechanism of E-cadherin, which lacks N-glycosylation at Asn-633 (M4), degradation and the role of the N-glycan at Asn-633 in E-cadherin folding. 19520913 3 20 part_of LDLR 598:601 arg1 its cytoplasmic domain LDLR its cytoplasmic domain PUBTATOR Site LDLR 16835 domain LXR inhibits the LDL receptor (LDLR) pathway through transcriptional induction of Idol (inducible degrader of the LDLR), an E3 ubiquitin ligase that triggers ubiquitination of the LDLR on its cytoplasmic domain, thereby targeting it for degradation. 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 Asn-86 The results demonstrate that only Asn-86 is glycosylated. 15687489 5 28 part_of FGE 633:635 arg1 the FGE recognition motif FGE the FGE recognition motif PUBTATOR Site FGE 285362 motif pFGE binds a sulfatase-derived peptide bearing the FGE recognition motif, but it lacks formylglycine-generating activity. 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. 3571235 5 26 part_of C 741:741 arg1 the hydrophobic domain glycophorin C the hydrophobic domain PUBTATOR Site glycophorin C 2995 domain The amino acid sequence of the hydrophobic domain (residues 49-88) of glycophorin C, that was also determined, agreed completely with the structure recently deduced from cDNA sequencing. 3571235 5 26 part_of C 741:741 arg1 residues 49-88 glycophorin C residues 49-88 PUBTATOR SpecificSite glycophorin C 2995 residues 49-88 The amino acid sequence of the hydrophobic domain (residues 49-88) of glycophorin C, that was also determined, agreed completely with the structure recently deduced from cDNA sequencing. 28402104 5 2 gly glycosylated 956:967 arg1 the predicted glycosylation sites the predicted glycosylation sites sites Further analysis revealed that green cone opsin exists as a dimer in both dark (inactive) and bleached (active) states, and that the predicted glycosylation sites at N32 and N34 are indeed glycosylated. 28402104 5 89 gly glycosylation 910:922 arg2 the predicted glycosylation sites the predicted glycosylation sites sites Further analysis revealed that green cone opsin exists as a dimer in both dark (inactive) and bleached (active) states, and that the predicted glycosylation sites at N32 and N34 are indeed glycosylated. 28402104 5 89 gly glycosylation 910:922 arg2 N32 N32 and N34 N32 and N34 Further analysis revealed that green cone opsin exists as a dimer in both dark (inactive) and bleached (active) states, and that the predicted glycosylation sites at N32 and N34 are indeed glycosylated. 14699159 9 69 gly glycosylation 1805:1817 arg1 p90ATF6 p90ATF6 Cterm p90ATF6 22926 Because accumulation of underglycosylated proteins in the ER is a potent inducer for the UPR, these studies uncover a novel mechanism whereby the glycosylation status of p90ATF6 can serve as a sensor for ER homeostasis, resulting in ATF6 activation to trigger the UPR. 14699159 9 80 gly underglycosylated 1683:1699 arg1 underglycosylated proteins underglycosylated proteins Fterm proteins Because accumulation of underglycosylated proteins in the ER is a potent inducer for the UPR, these studies uncover a novel mechanism whereby the glycosylation status of p90ATF6 can serve as a sensor for ER homeostasis, resulting in ATF6 activation to trigger the UPR. 2277032 2 9 gly glycoprotein 391:402 arg1 The enzyme The enzyme Fterm enzyme The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule. 2277032 2 9 gly glycoprotein 391:402 arg1 a glycoprotein a glycoprotein Fterm glycoprotein The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule. 2277032 2 51 gly containing 405:414 arg1 The enzyme AND 10 mannose The enzyme 10 mannose Fterm enzyme The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule. 2277032 2 51 gly containing 405:414 arg1 The enzyme AND 2 sialic acid residues The enzyme 2 sialic acid residues Fterm enzyme The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule. 2277032 2 51 gly containing 405:414 arg1 The enzyme AND 1 fucose The enzyme 1 fucose Fterm enzyme The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule. 2277032 2 51 gly containing 405:414 arg1 The enzyme AND 7 galactose The enzyme 7 galactose Fterm enzyme The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule. 2277032 2 51 gly containing 405:414 arg1 The enzyme AND 6 glucosamine The enzyme 6 glucosamine Fterm enzyme The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule. 2277032 2 51 gly containing 405:414 arg1 a glycoprotein AND 10 mannose a glycoprotein 10 mannose Fterm glycoprotein The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule. 2277032 2 51 gly containing 405:414 arg1 a glycoprotein AND 2 sialic acid residues a glycoprotein 2 sialic acid residues Fterm glycoprotein The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule. 2277032 2 51 gly containing 405:414 arg1 a glycoprotein AND 1 fucose a glycoprotein 1 fucose Fterm glycoprotein The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule. 2277032 2 51 gly containing 405:414 arg1 a glycoprotein AND 7 galactose a glycoprotein 7 galactose Fterm glycoprotein The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule. 2277032 2 51 gly containing 405:414 arg1 a glycoprotein AND 6 glucosamine a glycoprotein 6 glucosamine Fterm glycoprotein The enzyme was found to be a glycoprotein, containing 1 fucose, 7 galactose, 10 mannose, 6 glucosamine, and 2 sialic acid residues per molecule. 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. 3353370 0 115 part_of containing 92:101 arg1 both transmembrane proteins AND a leucine-rich amino acid sequence both transmembrane proteins a leucine-rich amino acid sequence Fterm Site proteins sequence The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence. 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. 26146185 6 43 part_of sites 733:737 arg1 CD166 CD166 sites PUBTATOR Site CD166 214 sites We characterized the binding sites on CD6 and CD166 and showed that a SNP in CD6 causes glycosylation that hinders the CD6/CD166 interaction. 26146185 6 43 part_of sites 733:737 arg1 CD6 CD6 sites PUBTATOR Site CD6 923 sites We characterized the binding sites on CD6 and CD166 and showed that a SNP in CD6 causes glycosylation that hinders the CD6/CD166 interaction. 22848655 0 33 part_of kinase 86:91 arg1 the Sema-PSI extracellular domain kinase the Sema-PSI extracellular domain Fterm Site kinase domain Crystal structure of the Sema-PSI extracellular domain of human RON receptor tyrosine kinase. 22848655 0 46 part_of Sema-PSI 25:32 arg1 the Sema-PSI extracellular domain structure of the Sema the Sema-PSI extracellular domain Cterm Site structure of the Sema 57556 domain Crystal structure of the Sema-PSI extracellular domain of human RON receptor tyrosine kinase. 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. 18657508 4 7 part_of SIRPgamma 730:738 arg1 the N-terminal domains SIRPgamma the N-terminal domains PUBTATOR Site SIRPgamma 55423 domains We have also determined structures of the N-terminal domains of SIRPbeta, SIRPbeta(2), and SIRPgamma; proteins that are closely related to SIRPalpha but bind CD47 with negligible or reduced affinity. 18657508 4 36 part_of SIRPbeta 703:710 arg1 the N-terminal domains SIRPbeta the N-terminal domains PUBTATOR Site SIRPbeta 140885 domains We have also determined structures of the N-terminal domains of SIRPbeta, SIRPbeta(2), and SIRPgamma; proteins that are closely related to SIRPalpha but bind CD47 with negligible or reduced affinity. 18657508 4 45 part_of SIRPbeta 713:720 arg1 the N-terminal domains SIRPbeta the N-terminal domains PUBTATOR Site SIRPbeta 140885 domains We have also determined structures of the N-terminal domains of SIRPbeta, SIRPbeta(2), and SIRPgamma; proteins that are closely related to SIRPalpha but bind CD47 with negligible or reduced affinity. 4055801 9 40 part_of C9b 1179:1181 arg1 The C9a and C9b polypeptide regions C9b The C9a and C9b polypeptide regions Cterm Site C9b regions The C9a and C9b polypeptide regions have been mapped on poly(C9) by immunoelectron microscopy. 4055801 9 56 part_of polypeptide 1183:1193 arg1 The C9a and C9b polypeptide regions polypeptide The C9a and C9b polypeptide regions Fterm Site polypeptide regions The C9a and C9b polypeptide regions have been mapped on poly(C9) by immunoelectron microscopy. 9883900 3 26 part_of IGFBP-5 395:401 arg1 IGFBP-5 peptides IGFBP-5 IGFBP-5 peptides PUBTATOR Site IGFBP-5 3488 peptides Identification of IGFBP-5 peptides in the fractions of our peptide bank generated from hemofiltrate was performed by their immunoreactivity and their capacity to bind IGF-I. 2013294 4 10 part_of SABP 311:314 arg1 The complete amino acid sequence SABP The complete amino acid sequence PUBTATOR Site SABP 5304 sequence The complete amino acid sequence of SABP was determined with the aid of fragments generated by trypsin, Staphylococcus aureus V8 protease and pepsin. 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. 10978165 5 10 part_of HCC-1 522:526 arg1 two distinct HCC-1 peptides HCC-1 two distinct HCC-1 peptides PUBTATOR Site HCC-1 Q14498 peptides Western blot analysis of human plasma extracts revealed a HCC-1 immunoreactive double band at 8-10 kDa indicating the presence of two distinct HCC-1 peptides. 29632068 6 57 part_of CerS2 1033:1037 arg1 11 residues CerS2 11 residues PUBTATOR Site CerS2 29956 residues The specificity of a chimeric protein, CerS5(299-309→CerS2), based on the backbone of CerS5 (which generates C16-ceramide), but containing 11 residues from CerS2 (which generates C22-C24-ceramides), was altered such that it generated C22-C24 and other ceramides. 29632068 6 61 part_of containing 1005:1014 arg1 CerS5 AND 11 residues CerS5 11 residues PUBTATOR Site CerS5 91012 residues The specificity of a chimeric protein, CerS5(299-309→CerS2), based on the backbone of CerS5 (which generates C16-ceramide), but containing 11 residues from CerS2 (which generates C22-C24-ceramides), was altered such that it generated C22-C24 and other ceramides. 3542989 1 28 part_of cholinesterase 108:121 arg1 The complete amino acid sequence cholinesterase The complete amino acid sequence PUBTATOR Site cholinesterase 534616 sequence The complete amino acid sequence of human serum cholinesterase (choline esterase II (unspecific), EC 3.1.1.8) was determined by Edman degradation of purified peptides. 21515415 3 34 part_of containing 365:374 arg1 six variants AND serine six variants serine Fterm AminoAcid variants serine To study the impact of these sites on PLTP secretion and activity, six variants containing serine to alanine point mutations were prepared by site-directed mutagenesis and expressed in Chinese hamster ovary Flp-In cells. 8636209 3 99 part_of gamma 390:394 arg1 the extracellular (EC), transmembrane (TM), and cytoplasmic (CY) domain CD3 gamma the extracellular (EC), transmembrane (TM), and cytoplasmic (CY) domain PUBTATOR Site CD3 gamma 917 domain In this study we examined the role of the extracellular (EC), transmembrane (TM), and cytoplasmic (CY) domain of CD3 gamma in assembly and cell surface expression of the complete TCR in human T cells. 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. 27551080 0 0 part_of NPC1 69:72 arg1 NPC1 middle lumenal domain structure of NPC1 NPC1 middle lumenal domain PUBTATOR Site structure of NPC1 4864 domain Clues to the mechanism of cholesterol transfer from the structure of NPC1 middle lumenal domain bound to NPC2. 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. 19467646 9 10 part_of BDNF 1194:1197 arg1 the glycosylated pro-form BDNF the glycosylated pro-form PUBTATOR AminoAcid BDNF 627 pro Treatment with N-glycanase and plasmin reduced the size of the higher molecular weight bands, confirming the glycosylated pro-form of BDNF. 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. 16679516 0 25 part_of thyroglobulin 73:85 arg1 Ser-2730 thyroglobulin Ser-2730 PUBTATOR SpecificSite 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. 23756652 5 31 part_of RSPO1 735:739 arg1 Both the FU-CRD1 and FU-CRD2 domains RSPO1 Both the FU-CRD1 and FU-CRD2 domains PUBTATOR Site RSPO1 Q2MKA7 domains Both the FU-CRD1 and FU-CRD2 domains of RSPO1 contribute to LGR4 interaction, and binding and cellular assays identified critical RSPO1 residues for its biological activities. 23756652 5 32 part_of RSPO1 825:829 arg1 critical RSPO1 residues RSPO1 critical RSPO1 residues PUBTATOR Site RSPO1 Q2MKA7 residues Both the FU-CRD1 and FU-CRD2 domains of RSPO1 contribute to LGR4 interaction, and binding and cellular assays identified critical RSPO1 residues for its biological activities. 23756652 5 45 part_of FU-CRD1 704:710 arg1 Both the FU-CRD1 and FU-CRD2 domains CRD1 Both the FU-CRD1 and FU-CRD2 domains PUBTATOR Site CRD1 1319 domains Both the FU-CRD1 and FU-CRD2 domains of RSPO1 contribute to LGR4 interaction, and binding and cellular assays identified critical RSPO1 residues for its biological activities. 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. 18234225 4 84 part_of enzyme 787:792 arg1 both S1 and S1' sites enzyme both S1 and S1' sites Fterm Site enzyme sites In this article, we have extended structural characterization of GCPII to its S1 site by using dipeptide-based inhibitors that interact with both S1 and S1' sites of the enzyme. 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. 16492764 2 0 part_of GCSF 449:452 arg1 the Ig-like domains GCSF the Ig-like domains PUBTATOR Site GCSF 1440 domains The GCSF:GCSF-R complex formed a 2:2 stoichiometry by means of a cross-over interaction between the Ig-like domains of GCSF-R and GCSF. 16492764 2 14 part_of GCSF-R 438:443 arg1 the Ig-like domains GCSF-R the Ig-like domains PUBTATOR Site GCSF-R 1441 domains The GCSF:GCSF-R complex formed a 2:2 stoichiometry by means of a cross-over interaction between the Ig-like domains of GCSF-R and GCSF. 9689040 0 33 part_of fibrinogen-420 61:74 arg1 a recombinant alphaEC domain fibrinogen a recombinant alphaEC domain PUBTATOR Site fibrinogen 2244 domain Crystal structure of a recombinant alphaEC domain from human fibrinogen-420. 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. 21676880 0 47 part_of KCNE1 59:63 arg1 type I transmembrane KCNE1 peptides KCNE1 type I transmembrane KCNE1 peptides PUBTATOR Site KCNE1 3753 peptides Post-translational N-glycosylation of type I transmembrane KCNE1 peptides: implications for membrane protein biogenesis and disease. 21569239 0 25 part_of F-spondin 68:76 arg1 the Ca²+-binding, glycosylated F-spondin domain F-spondin the Ca²+-binding, glycosylated F-spondin domain PUBTATOR Site F-spondin 10418 domain The structure of the Ca²+-binding, glycosylated F-spondin domain of F-spondin - A C2-domain variant in an extracellular matrix protein. 21569239 0 44 part_of F-spondin 48:56 arg1 the Ca²+-binding, glycosylated F-spondin domain F-spondin the Ca²+-binding, glycosylated F-spondin domain PUBTATOR Site F-spondin 10418 domain The structure of the Ca²+-binding, glycosylated F-spondin domain of F-spondin - A C2-domain variant in an extracellular matrix protein. 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. 22351761 8 77 part_of containing 1413:1422 arg1 glypican-1 AND the HS attachment domain glypican-1 the HS attachment domain PUBTATOR Site glypican-1 2817 domain No additional electron density was observed for crystals of glypican-1 containing the HS attachment domain, and CD spectra of the two protein species were highly similar. 30559189 2 28 part_of protein 274:280 arg1 a three-fingered LU domain protein domain Fterm Site protein domain The LPL within capillaries is bound to GPIHBP1, an endothelial cell protein with a three-fingered LU domain and an N-terminal intrinsically disordered acidic domain. 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. 22511793 6 0 part_of protein 1125:1131 arg1 a highly glycosylated luminal domain protein a highly glycosylated luminal domain Fterm Site protein domain By differential membrane extraction and sequential mutagenesis of potential N-glycosylation sites, we identified TMEM106B as a type 2 integral membrane protein with a highly glycosylated luminal domain. 10419520 9 33 part_of S2P 1212:1214 arg1 the long hydrophilic sequences S2P the long hydrophilic sequences OGER Site S2P O43462 sequences All three of the long hydrophilic sequences of S2P can be glycosylated, indicating that they all project into the lumen. 28775322 4 54 part_of EGF-like 795:802 arg1 folded EGF-like domains EGF folded EGF-like domains OGER Site EGF P01133 domains Notably, we show that Protein O-glucosyltransferase 1's requirement for folded EGF-like domains also leads to its serine specificity and that two distinct local conformational states are likely responsible for its ability to transfer both glucose and xylose. 20823119 7 22 part_of IgA1 1156:1159 arg1 IgA1 HR fragments IgA1 HR IgA1 HR fragments PUBTATOR Site IgA1 HR P01876 fragments 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. 20823119 7 73 part_of HR 1161:1162 arg1 IgA1 HR fragments IgA1 HR IgA1 HR fragments PUBTATOR Site IgA1 HR P01876 fragments 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. 6785754 2 10 part_of contains 275:282 arg1 The fragment AND 226 amino acid residues The fragment 226 amino acid residues residues The fragment contains 226 amino acid residues and has a molecular weight of 32,000 per monomeric unit. 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. 1472036 4 21 part_of receptor 763:770 arg1 the extracellular domain insulin receptor the extracellular domain OGER Site insulin receptor P06213 domain Since it has been shown that the extracellular domain of the insulin receptor has no free thiols and since no other sequences containing cysteine were found in these fractions, we conclude that Cys524 forms a disulfide bond to the Cys524 in the other alpha-subunit. 1472036 4 25 part_of Cys524 925:930 arg1 the other alpha-subunit subunit Cys524 OGER AminoAcid subunit P06213 Cys524 Since it has been shown that the extracellular domain of the insulin receptor has no free thiols and since no other sequences containing cysteine were found in these fractions, we conclude that Cys524 forms a disulfide bond to the Cys524 in the other alpha-subunit. 1472036 4 35 part_of containing 820:829 arg1 no other sequences AND cysteine no other sequences cysteine cysteine Since it has been shown that the extracellular domain of the insulin receptor has no free thiols and since no other sequences containing cysteine were found in these fractions, we conclude that Cys524 forms a disulfide bond to the Cys524 in the other alpha-subunit. 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. 3497398 6 55 part_of Ib 942:943 arg1 This region Ib This region Cterm Site Ib region This region of glycoprotein Ib is largely hydrophobic and contains only two N-linked and one O-linked carbohydrate chains. 29899144 0 66 part_of domain 20:25 arg1 GPIHBP1 GPIHBP1 domain PUBTATOR Site GPIHBP1 338328 domain A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase. 22660477 7 23 part_of subunits 868:875 arg1 GBR1 residues subunits GBR1 residues Fterm Site subunits residues We also identify specific heterodimer contacts from both subunits, and GBR1 residues involved in ligand recognition. 8636209 11 33 part_of gamma 1459:1463 arg1 TM domain CD3 gamma TM domain PUBTATOR Site CD3 gamma 917 domain In conclusion, this study demonstrated that specific TCR interaction sites exist in both the EC and TM domain of CD3 gamma. 8636209 11 97 part_of TCR 1395:1397 arg1 specific TCR interaction sites TCR specific TCR interaction sites PUBTATOR Site TCR 6962 sites In conclusion, this study demonstrated that specific TCR interaction sites exist in both the EC and TM domain of CD3 gamma. 19276170 0 0 part_of protein 77:83 arg1 the signature domain cartilage oligomeric matrix protein the signature domain OGER Site cartilage oligomeric matrix protein P49747 domain The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding. 11080501 5 44 part_of thyroglobulin 1178:1190 arg1 the thyroglobulin type 1A domain thyroglobulin the thyroglobulin type 1A domain OGER Site thyroglobulin P01266 domain The next three disulfide linkages are Cys7-Cys8, Cys9-Cys10, and Cys11-Cys12, consistent with the recently determined disulfide pattern of the thyroglobulin type 1A domain of insulin-like growth factor-binding proteins 1 and 6. 11080501 5 59 part_of proteins 1245:1252 arg1 the thyroglobulin type 1A domain proteins 1 the thyroglobulin type 1A domain Fterm Site proteins 1 domain The next three disulfide linkages are Cys7-Cys8, Cys9-Cys10, and Cys11-Cys12, consistent with the recently determined disulfide pattern of the thyroglobulin type 1A domain of insulin-like growth factor-binding proteins 1 and 6. 8702538 9 35 part_of CD33 1546:1549 arg1 the first Ig domain CD33 the first Ig domain OGER Site CD33 P20138 domain In contrast, mutation of a NCS motif in the first Ig domain of the I-type lectin CD33 unmasked its sialic acid binding activity. 8702538 9 73 part_of NCS 1492:1494 arg1 a NCS motif NCS a NCS motif OGER Site NCS motif In contrast, mutation of a NCS motif in the first Ig domain of the I-type lectin CD33 unmasked its sialic acid binding activity. 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. 21205830 3 45 part_of Nixin 672:676 arg1 the Nixin RING domain Nixin the Nixin RING domain PUBTATOR Site Nixin 148066 domain Ectopic expression of wild type Nixin induced a dramatic down-regulation of the ER-localized chaperone calnexin that was prevented by inactivation of the Nixin RING domain. 19153605 10 29 part_of FS 1152:1153 arg1 the FS and TSR domains FS the FS and TSR domains Cterm Site FS 10418 domains Through these dual interactions, the FS and TSR domains of mindin promote activation of both adaptive and innate immune responses. 19153605 10 55 part_of mindin 1174:1179 arg1 the FS and TSR domains mindin the FS and TSR domains PUBTATOR Site mindin 10417 domains Through these dual interactions, the FS and TSR domains of mindin promote activation of both adaptive and innate immune responses. 19004833 0 46 part_of DS-epimerase 37:48 arg1 the active site DS-epimerase 1 the active site OGER Site DS-epimerase 1 Q9UL01 site Identification of the active site of DS-epimerase 1 and requirement of N-glycosylation for enzyme function. 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. 6510521 4 38 part_of CB1-CB4 577:583 arg1 Fragments Fragments CB1 Fragments PUBTATOR Fragments CB1 1268 Fragments CB1-CB4 include 5 sites, where hexosamine oligosaccharides are attached (positions 1,41,164,217 and probably 223). 29899144 3 12 part_of GPIHBP1 504:510 arg1 The N-terminal domain GPIHBP1 The N-terminal domain PUBTATOR Site GPIHBP1 338328 domain The N-terminal domain of GPIHBP1, an intrinsically disordered region (IDR) rich in acidic residues, is important for stabilizing LPL's catalytic domain against spontaneous and ANGPTL4-catalyzed unfolding. 19880749 0 48 part_of ADAMTS13 50:57 arg1 the noncatalytic domains ADAMTS13 the noncatalytic domains PUBTATOR Site ADAMTS13 11093 domains Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple discontinuous exosites for von Willebrand factor. 1544894 2 40 part_of EGF 461:463 arg1 two EGF domains EGF two EGF domains PUBTATOR Site EGF 1950 domains Factor XII and protein C each contain two EGF domains; in both proteins, the EGF domain nearest the N terminus has a threonine residue in a position homologous to that which is fucosylated in t-PA. 1544894 2 57 part_of EGF 496:498 arg1 the EGF domain EGF the EGF domain PUBTATOR Site EGF 1950 domain Factor XII and protein C each contain two EGF domains; in both proteins, the EGF domain nearest the N terminus has a threonine residue in a position homologous to that which is fucosylated in t-PA. 1544894 2 49 part_of contain 449:455 arg1 Factor XII AND two EGF domains Factor XII two EGF domains OGER Site Factor XII P00748 domains Factor XII and protein C each contain two EGF domains; in both proteins, the EGF domain nearest the N terminus has a threonine residue in a position homologous to that which is fucosylated in t-PA. 1544894 2 49 part_of contain 449:455 arg1 protein C AND two EGF domains protein C two EGF domains OGER Site protein C P02810 domains Factor XII and protein C each contain two EGF domains; in both proteins, the EGF domain nearest the N terminus has a threonine residue in a position homologous to that which is fucosylated in t-PA. 3342889 6 52 part_of cathepsins 808:817 arg1 known sequences cathepsins H known sequences OGER Site cathepsins H P25774 sequences The fragments were aligned by comparison with known sequences of cathepsins H and L from other species. 18070108 8 23 part_of BMP-6 1248:1252 arg1 Asn73 BMP-6 Asn73 PUBTATOR AminoAcid 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. 18070108 8 59 part_of receptors 1196:1204 arg1 different ectodomains receptors different ectodomains Fterm Site receptors ectodomains 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. 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. 3497398 0 54 part_of Willebrand 31:40 arg1 the von Willebrand factor-binding domain von Willebrand factor the von Willebrand factor-binding domain OGER Site von Willebrand factor P04275 domain Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib. 3497398 0 80 part_of Ib 98:99 arg1 the von Willebrand factor-binding domain Ib the von Willebrand factor-binding domain Cterm Site Ib domain Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib. 3497398 0 90 part_of von 27:29 arg1 the von Willebrand factor-binding domain von Willebrand factor the von Willebrand factor-binding domain OGER Site von Willebrand factor P04275 domain Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib. 3497398 0 93 part_of factor-binding 42:55 arg1 the von Willebrand factor-binding domain von Willebrand factor the von Willebrand factor-binding domain OGER Site von Willebrand factor P04275 domain Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib. 25765764 4 9 part_of LRIG1-LRR 574:582 arg1 The LRIG1-LRR domain LRIG1 The LRIG1-LRR domain PUBTATOR Site LRIG1 Q96JA1 domain The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric. 25765764 4 9 part_of LRIG1-LRR 574:582 arg1 the LRIG1-LRR-1Ig fragment LRIG1 the LRIG1-LRR-1Ig fragment PUBTATOR Site LRIG1 Q96JA1 fragment The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric. 25765764 4 19 part_of LRIG1-3Ig 660:668 arg1 the LRIG1-3Ig domain LRIG1 the LRIG1-3Ig domain PUBTATOR Site LRIG1 Q96JA1 domain The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric. 25765764 4 45 part_of LRIG1-LRR-1Ig 599:611 arg1 The LRIG1-LRR domain LRIG1 The LRIG1-LRR domain PUBTATOR Site LRIG1 Q96JA1 domain The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric. 25765764 4 45 part_of LRIG1-LRR-1Ig 599:611 arg1 the LRIG1-LRR-1Ig fragment LRIG1 the LRIG1-LRR-1Ig fragment PUBTATOR Site LRIG1 Q96JA1 fragment The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric. 19880749 7 9 part_of VWF-binding 957:967 arg1 3 VWF-binding exosites 3 VWF 3 VWF-binding exosites PUBTATOR Site 3 VWF 7450 exosites We identified 3 VWF-binding exosites on the linearly aligned discontinuous surfaces of the D, C(A), and S domains traversing the W-shaped molecule. 21763278 2 55 gly O-glycosylation 225:239 arg2 Thr-71 Thr-71 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. 21676880 5 53 part_of KCNE1 1089:1093 arg1 the KCNE1 post-translational site KCNE1 the KCNE1 post-translational site PUBTATOR Site KCNE1 3753 site This long range inhibition is highly specific for post-translational N-glycosylation because mutagenic conversion of the KCNE1 post-translational site into a co-translational site restored both monoglycosylation and anterograde trafficking. 9030779 3 67 gly N-glycosylation 471:485 arg2 Each N-glycosylation site Each N-glycosylation site site Each N-glycosylation site was modified by site-directed mutagenesis and subsequently expressed in COS-1 cells. 8172892 0 89 part_of IX 35:36 arg1 Activation peptide factor IX Activation peptide OGER Site factor IX P00740 peptide Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to threonine residues at 159 and 169. 10066782 2 46 part_of fibronectin-type 438:453 arg1 two fibronectin-type III (FN III) domains fibronectin two fibronectin-type III (FN III) domains OGER Site fibronectin P02751 domains The extracellular "soluble" part of the IL-6R (sIL-6R) consists of three domains: an amino-terminal Ig-like domain and two fibronectin-type III (FN III) domains. 22750213 5 17 part_of PRiMA 859:863 arg1 the asparagine-43 PRiMA the asparagine-43 PUBTATOR SpecificSite PRiMA 170952 asparagine-43 By using site-directed mutagenesis, the asparagine-43 was identified to be the N-linked glycosylation site of PRiMA. 22750213 5 17 part_of PRiMA 859:863 arg1 the N-linked glycosylation site PRiMA the N-linked glycosylation site PUBTATOR Site PRiMA 170952 site By using site-directed mutagenesis, the asparagine-43 was identified to be the N-linked glycosylation site of PRiMA. 3163150 1 38 part_of kallikrein 122:131 arg1 The amino acid sequence kallikrein The amino acid sequence PUBTATOR Site kallikrein 9622 sequence The amino acid sequence of human urinary kallikrein was determined by protein-chemical methods. 15378069 2 29 part_of head 263:266 arg1 the ectodomain head the ectodomain ectodomain Integrin alpha and beta subunits form a head and two long legs in the ectodomain and span the membrane. 22688517 6 59 part_of LOX-1 1185:1189 arg1 one potential glycosylation site LOX-1 one potential glycosylation site PUBTATOR Site LOX-1 4973 site With this approach, one potential glycosylation site of recombinant human LOX-1 on Asn(139) is readily identified and found to carry heterogeneous complex type N-glycans. 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. 20826823 2 19 part_of contains 356:363 arg1 ACE AND two domains ACE domains PUBTATOR Site ACE P12821 domains ACE contains two domains, the N and C domains, both of which are heavily glycosylated. 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. 26859324 8 10 part_of enzyme 1627:1632 arg1 the membrane-binding domain enzyme the membrane-binding domain Fterm Site enzyme domain We also observe differential acetylation of COX-2 purified in various detergent systems and nanodiscs, indicating that detergent and lipid binding within the membrane-binding domain of the enzyme alters the rate of the acetylation reaction in vitro. 16036915 4 2 part_of containing 731:740 arg1 Wild type ELOVL4 AND an endoplasmic reticulum retention sequence Wild type ELOVL4 an endoplasmic reticulum retention sequence PUBTATOR Site ELOVL4 6785 sequence Wild type ELOVL4 containing an endoplasmic reticulum retention sequence was localized to the endoplasmic reticulum as expected. 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. 3840370 2 34 part_of protein 379:385 arg1 The entire amino acid sequence protein can The entire amino acid sequence OGER Site protein can P35658 sequence The entire amino acid sequence of the C4b-binding protein can be predicted from this study of the cloned cDNA when allied to a previous sequence study at the protein level [Chung, Gagnon & Reid (1985) Mol. 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. 20696930 3 22 part_of HER2 413:416 arg1 The 58 amino acid residue HER2 The 58 amino acid residue PUBTATOR Site HER2 2064 residue The 58 amino acid residue Zher2 affibody molecule was previously engineered as a high-affinity binder of HER2. 20427278 0 75 gly glycosylation 52:64 arg1 the amyloid precursor protein the amyloid precursor protein OGER amyloid precursor protein P05067 The novel membrane protein TMEM59 modulates complex glycosylation, cell surface expression, and secretion of the amyloid precursor protein. 8172892 9 19 part_of IX 1547:1548 arg1 the activation peptide factor IX the activation peptide OGER Site factor IX P00740 peptide From these results, it was concluded that a part of the activation peptide of human factor IX in circulating blood has tri- and tetrasaccharides O-glycosidically linked to the threonine residues at 159 and 169. 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. 27316455 5 42 part_of ATG9A 706:710 arg1 the C-terminal region ATG9A the C-terminal region PUBTATOR Site ATG9A 79065 region In addition, we found that substitution of the L(711)YM(713) sequence (located in the C-terminal region of ATG9A) by alanine residues severely impaired its transport through the Golgi apparatus. 20534510 5 46 part_of PDGF 843:846 arg1 the PDGF propeptides PDGF the PDGF propeptides OGER Site PDGF propeptides The PDGF-B:PDGFRbeta interface is predominantly hydrophobic, and PDGFRs and the PDGF propeptides occupy overlapping positions on mature PDGFs, rationalizing the need of propeptides by PDGFs to cover functionally important hydrophobic surfaces during secretion. 10022822 4 5 part_of p41 629:631 arg1 the p41 fragment structure of the p41 the p41 fragment Cterm Site structure of the p41 fragment The structure of the p41 fragment demonstrates a novel fold, consisting of two subdomains, each stabilized by disulfide bridges. 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. 16186819 2 12 part_of THBS2 308:312 arg1 the glycosylated signature domain THBS2 the glycosylated signature domain PUBTATOR Site THBS2 7058 domain Here, we describe the 2.6-A-resolution crystal structure of the glycosylated signature domain of human THBS2, which includes three epidermal growth factor-like modules, 13 aspartate-rich repeats and a lectin-like module. 18657508 3 1 part_of CD47 513:516 arg1 The unusual and convoluted interacting face CD47 The unusual and convoluted interacting face OGER Site CD47 Q08722 face The unusual and convoluted interacting face of CD47, comprising the N terminus and loops at the end of the domain, intercalates with the corresponding regions in SIRPalpha. 18657508 3 21 part_of regions 617:623 arg1 SIRPalpha SIRPalpha regions PUBTATOR Site SIRPalpha 140885 regions The unusual and convoluted interacting face of CD47, comprising the N terminus and loops at the end of the domain, intercalates with the corresponding regions in SIRPalpha. 16763549 3 40 gly NRP1 501:504 arg1 proteoglycan NRP1 proteoglycan OGER NRP1 O14786 Here we show that a substantial fraction of NRP1 is proteoglycan modified with either heparan sulfate or chondroitin sulfate on a single conserved Ser. 16763549 3 44 gly proteoglycan 509:520 arg1 a single conserved Ser a single conserved Ser a single conserved Ser AminoAcid Ser Here we show that a substantial fraction of NRP1 is proteoglycan modified with either heparan sulfate or chondroitin sulfate on a single conserved Ser. 7477400 3 25 gly glycoproteins 599:611 arg1 class II histocompatibility glycoproteins class II histocompatibility glycoproteins Fterm glycoproteins The structure shows that the CLIP fragment binds to DR3 in a way almost identical to that in which antigenic peptides bind class II histocompatibility glycoproteins. 17157876 7 55 part_of sites 1591:1595 arg1 the membrane-anchored CPM CPM sites OGER Site CPM P14384 sites Three Thr residues at the distal TT edge of CPN1 are O-linked to N-acetyl glucosamine sugars; equivalent sites in the membrane-anchored CPM are occupied by basic residues probably involved in membrane interaction. 16445295 6 5 part_of found 972:976 arg1 an unglycosylated variant AND Asn219 an unglycosylated variant Asn219 Fterm AminoAcid variant Asn219 Asn219 was also found in an unglycosylated variant. 21712440 7 4 gly glycosylation 1498:1510 arg1 the Aβ1-38/40/42 isoforms the Aβ1-38/40/42 isoforms 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. 9233787 0 36 part_of domains 76:82 arg1 BM-40 BM-40 domains OGER Site BM-40 P09486 domains Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40. 9233787 0 45 part_of follistatin-like 31:46 arg1 follistatin-like and EF-hand calcium-binding domains follistatin follistatin-like and EF-hand calcium-binding domains OGER Site follistatin P19883 domains Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40. 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-. 3463996 3 64 part_of residues 691:698 arg1 mature (single chain) cathepsin B cathepsin B residues PUBTATOR AminoAcid cathepsin B 1508 residues in The nucleotide sequences predict that the primary structure of preprocathepsin B contains 339 amino acids organized as follows: a 17-residue NH2-terminal prepeptide sequence followed by a 62-residue propeptide region, 254 residues in mature (single chain) cathepsin B, and a 6-residue extension at the COOH terminus. 3463996 3 90 part_of terminus 776:783 arg1 254 residues terminus 254 residues residues in The nucleotide sequences predict that the primary structure of preprocathepsin B contains 339 amino acids organized as follows: a 17-residue NH2-terminal prepeptide sequence followed by a 62-residue propeptide region, 254 residues in mature (single chain) cathepsin B, and a 6-residue extension at the COOH terminus. 3463996 3 90 part_of terminus 776:783 arg1 a 62-residue propeptide region terminus a 62-residue propeptide region region The nucleotide sequences predict that the primary structure of preprocathepsin B contains 339 amino acids organized as follows: a 17-residue NH2-terminal prepeptide sequence followed by a 62-residue propeptide region, 254 residues in mature (single chain) cathepsin B, and a 6-residue extension at the COOH terminus. 21569239 8 34 part_of found 1130:1134 arg2 mindin AND The integrin-binding motif mindin The integrin-binding motif PUBTATOR Site mindin 10417 motif The integrin-binding motif found in mindin is not conserved in the F-spondin FS domain. 21569239 8 51 part_of F-spondin 1170:1178 arg1 the F-spondin FS domain F-spondin the F-spondin FS domain PUBTATOR F-spondin 10418 The integrin-binding motif found in mindin is not conserved in the F-spondin FS domain. 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. 3877053 5 5 part_of XII 662:664 arg1 the complete amino acid sequence factor XII the complete amino acid sequence OGER Site factor XII P00748 sequence DNA sequence analysis of these overlapping clones showed that they contained DNA coding for part of an amino-terminal extension, the complete amino acid sequence of plasma factor XII, a TGA stop codon, a 3' untranslated region of 150 nucleotides, and a poly(A)+ tail. 3877053 5 5 part_of XII 662:664 arg1 tail factor XII tail OGER Site factor XII P00748 tail DNA sequence analysis of these overlapping clones showed that they contained DNA coding for part of an amino-terminal extension, the complete amino acid sequence of plasma factor XII, a TGA stop codon, a 3' untranslated region of 150 nucleotides, and a poly(A)+ tail. 3877053 5 5 part_of XII 662:664 arg1 a 3' untranslated region factor XII a 3' untranslated region OGER Site factor XII P00748 region DNA sequence analysis of these overlapping clones showed that they contained DNA coding for part of an amino-terminal extension, the complete amino acid sequence of plasma factor XII, a TGA stop codon, a 3' untranslated region of 150 nucleotides, and a poly(A)+ tail. 12391027 3 47 part_of contains 597:604 arg1 The front face AND the "recognition" face The front face the "recognition" face face The front face of the TSR contains a right-handed spiral, positively charged groove that might be the "recognition" face, mediating interactions with various ligands. 10978165 7 6 gly position 768:775 arg1 the disaccharide N-acetylgalactosamine galactose position 7 the disaccharide N-acetylgalactosamine galactose position 7 Glycosylated HCC-1 exhibits a molecular mass of 9621 Da due to O-glycosylation at position 7 (Ser-7) with two N-acetylneuraminic acids and the disaccharide N-acetylgalactosamine galactose. 10978165 7 49 gly O-glycosylation 749:763 arg2 position 7 position 7 position 7 Glycosylated HCC-1 exhibits a molecular mass of 9621 Da due to O-glycosylation at position 7 (Ser-7) with two N-acetylneuraminic acids and the disaccharide N-acetylgalactosamine galactose. 10978165 7 49 gly O-glycosylation 749:763 arg2 Ser-7 Ser-7 Ser-7 Glycosylated HCC-1 exhibits a molecular mass of 9621 Da due to O-glycosylation at position 7 (Ser-7) with two N-acetylneuraminic acids and the disaccharide N-acetylgalactosamine galactose. 24338010 4 1 part_of NPP4 879:882 arg1 the corresponding region NPP4 the corresponding region PUBTATOR Site NPP4 22875 region Comparative structural analysis reveals a tripartite lysine claw in NPP1 that stabilizes the terminal phosphate of ATP, whereas the corresponding region of NPP4 contains features that hinder this binding orientation, thereby inhibiting ATP hydrolysis. 28753425 3 41 part_of rhodopsin 559:567 arg1 the phosphorylated C terminus rhodopsin the phosphorylated C terminus PUBTATOR Site rhodopsin 6010 terminus Here, we report an X-ray free electron laser (XFEL) crystal structure of the rhodopsin-arrestin complex, in which the phosphorylated C terminus of rhodopsin forms an extended intermolecular β sheet with the N-terminal β strands of arrestin. 9501082 8 0 part_of alpha6 1107:1112 arg1 RGD peptide alpha2 and alpha6 subunits RGD peptide PUBTATOR Site alpha2 and alpha6 subunits 170589 peptide Adhesion to M2BP was inhibited by antibodies to integrin beta1 subunits but not to alpha2 and alpha6 subunits, RGD peptide or lactose. 9501082 8 7 part_of alpha2 1096:1101 arg1 RGD peptide alpha2 and alpha6 subunits RGD peptide PUBTATOR Site alpha2 and alpha6 subunits 170589 peptide Adhesion to M2BP was inhibited by antibodies to integrin beta1 subunits but not to alpha2 and alpha6 subunits, RGD peptide or lactose. 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. 17558413 6 17 part_of sites 1043:1047 arg1 mouse lumican lumican sites OGER Site lumican P51885 sites Using this methodology we identified the sites and the order of sulfation of several peptides mediated by purified human tyrosylprotein sulfotransferases (TPSTs), and unambiguously determined the tyrosine sulfation sites in mouse lumican and human vitronectin. 17558413 6 17 part_of sites 1043:1047 arg1 human vitronectin vitronectin sites PUBTATOR Site vitronectin 7448 sites Using this methodology we identified the sites and the order of sulfation of several peptides mediated by purified human tyrosylprotein sulfotransferases (TPSTs), and unambiguously determined the tyrosine sulfation sites in mouse lumican and human vitronectin. 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. 11080501 8 3 part_of thyroglobulin 1757:1769 arg1 GA733 type 2 motif thyroglobulin GA733 type 2 motif OGER Site thyroglobulin P01266 motif These data show that the extracellular domain of the GA733-2 antigen consists of three distinct domains; a novel cysteine-rich N-terminal domain (GA733 type 1 motif), a cysteine-rich thyroglobulin type 1A domain (GA733 type 2 motif), and a unique nonglycosylated domain without cysteines (GA733 type 3 motif). 11080501 8 3 part_of thyroglobulin 1757:1769 arg1 a cysteine-rich thyroglobulin type 1A domain thyroglobulin a cysteine-rich thyroglobulin type 1A domain OGER Site thyroglobulin P01266 domain These data show that the extracellular domain of the GA733-2 antigen consists of three distinct domains; a novel cysteine-rich N-terminal domain (GA733 type 1 motif), a cysteine-rich thyroglobulin type 1A domain (GA733 type 2 motif), and a unique nonglycosylated domain without cysteines (GA733 type 3 motif). 11080501 8 3 part_of thyroglobulin 1757:1769 arg1 three distinct domains thyroglobulin three distinct domains OGER Site thyroglobulin P01266 domains These data show that the extracellular domain of the GA733-2 antigen consists of three distinct domains; a novel cysteine-rich N-terminal domain (GA733 type 1 motif), a cysteine-rich thyroglobulin type 1A domain (GA733 type 2 motif), and a unique nonglycosylated domain without cysteines (GA733 type 3 motif). 22235133 7 13 part_of IL-21R 1062:1067 arg1 the extracellular domain IL-21R the extracellular domain PUBTATOR Site IL-21R 50615 domain We furthermore demonstrate that a sugar chain bridges the two fibronectin domains that constitute the extracellular domain of IL-21R and anchors at the WSXWS motif through an extensive hydrogen bonding network, including mannosylation. 22235133 7 42 part_of fibronectin 998:1008 arg1 the two fibronectin domains fibronectin the two fibronectin domains OGER Site fibronectin P02751 domains We furthermore demonstrate that a sugar chain bridges the two fibronectin domains that constitute the extracellular domain of IL-21R and anchors at the WSXWS motif through an extensive hydrogen bonding network, including mannosylation. 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. 11406581 6 19 part_of IgG 882:884 arg1 the hinge region IgG the hinge region Cterm Site IgG region In addition, we show that the secreted streptococcal cysteine proteinase SpeB cleaves IgG in the hinge region in a papain-like manner. 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. 12667445 2 17 part_of receptor 401:408 arg1 the extracellular domain receptor the extracellular domain Fterm Site receptor domain Here we report the crystal structure of BMP7 in complex with the extracellular domain (ECD) of the activin type II receptor. 18227435 5 36 gly O-glycosylated 873:886 arg2 Thr10 Thr10 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. 16362042 3 3 part_of Gas6 480:483 arg1 the first laminin G-like domain Gas6 the first laminin G-like domain PUBTATOR Site Gas6 2621 domain The crystal structure at 3.3 A resolution of a minimal human Gas6/Axl complex reveals an assembly of 2:2 stoichiometry, in which the two immunoglobulin-like domains of the Axl ectodomain are crosslinked by the first laminin G-like domain of Gas6, with no direct Axl/Axl or Gas6/Gas6 contacts. 16362042 3 10 part_of laminin 455:461 arg1 the first laminin G-like domain laminin the first laminin G-like domain OGER Site laminin domain The crystal structure at 3.3 A resolution of a minimal human Gas6/Axl complex reveals an assembly of 2:2 stoichiometry, in which the two immunoglobulin-like domains of the Axl ectodomain are crosslinked by the first laminin G-like domain of Gas6, with no direct Axl/Axl or Gas6/Gas6 contacts. 16362042 3 13 part_of Axl 411:413 arg1 the Axl ectodomain Axl the Axl ectodomain PUBTATOR Site Axl 558 ectodomain The crystal structure at 3.3 A resolution of a minimal human Gas6/Axl complex reveals an assembly of 2:2 stoichiometry, in which the two immunoglobulin-like domains of the Axl ectodomain are crosslinked by the first laminin G-like domain of Gas6, with no direct Axl/Axl or Gas6/Gas6 contacts. 1533633 2 3 part_of sites 313:317 arg1 the alpha-subunit subunit sites OGER Site subunit P06865 sites We have identified the sites of N-linked glycosylation and oligosaccharide phosphorylation on the alpha-subunit of beta-hexosaminidase and have determined the influence of the oligosaccharides on the folding and transport of the enzyme. 20188224 11 66 part_of PGRN 1558:1561 arg1 four out of five potential PGRN N-glycosylation consensus sites PGRN four out of five potential PGRN N-glycosylation consensus sites PUBTATOR Site PGRN 2896 sites Glycosylation of four out of five potential PGRN N-glycosylation consensus sites was demonstrated (the final one remains undetermined), with one of the four observed to be partially occupied. 7574684 6 24 part_of trkB 1033:1036 arg1 the soluble domain trkB the soluble domain PUBTATOR Site trkB 4915 domain Among 12 potential N-linked glycosylation sites proposed in the soluble domain of trkB, 10 sites are actually glycosylated. 22809326 0 31 part_of protein 82:88 arg1 the conserved domain protein the conserved domain Fterm Site protein domain Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx. 2013294 1 53 gly glycoprotein 118:129 arg1 Secretory actin-binding protein Secretory actin-binding protein PUBTATOR Secretory actin-binding protein 5304 Secretory actin-binding protein (SABP), a glycoprotein from human seminal plasma, was isolated according to Akiyama and Kimura [Akiyama, K. & Kimura, H. (1990) Biochim. 2013294 1 53 gly glycoprotein 118:129 arg1 a glycoprotein a glycoprotein Fterm glycoprotein Secretory actin-binding protein (SABP), a glycoprotein from human seminal plasma, was isolated according to Akiyama and Kimura [Akiyama, K. & Kimura, H. (1990) Biochim. 8670172 5 88 part_of Asn-77 888:893 arg1 a GPI-anchor GPI Asn-77 OGER SpecificSite GPI P06744 Asn-77 Mass analysis of the isolated C-terminal peptide (T9) indicated that a GPI-anchor (at Asn-77) without an inositol-associated phospholipid was present in soluble CD59u. 20188224 3 65 part_of containing 403:412 arg1 PGRN AND five N-glycosylation consensus sequons PGRN five N-glycosylation consensus sequons PUBTATOR PGRN 2896 PGRN is a glycoprotein, containing five N-glycosylation consensus sequons, three of which fall within granulin domains. 20188224 3 65 part_of containing 403:412 arg1 a glycoprotein AND five N-glycosylation consensus sequons a glycoprotein five N-glycosylation consensus sequons Fterm glycoprotein PGRN is a glycoprotein, containing five N-glycosylation consensus sequons, three of which fall within granulin domains. 9539703 4 68 part_of ICAM-1 647:652 arg1 the two amino-terminal domains ICAM-1 the two amino-terminal domains PUBTATOR Site ICAM-1 3383 domains The three-dimensional atomic structure of the two amino-terminal domains (D1 and D2) of ICAM-1 has been determined to 2.2-A resolution and fitted into a cryoelectron microscopy reconstruction of a rhinovirus-ICAM-1 complex. 21389326 4 50 part_of Flt3 915:918 arg1 extracellular domain 3 Flt3 extracellular domain 3 PUBTATOR Site Flt3 2322 domain FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions. 9233787 8 52 part_of site 1185:1188 arg1 follistatin follistatin site OGER Site follistatin P19883 site This hairpin is likely to act as a rigid spacer in proteins containing tandemly repeated FS domains, such as follistatin and agrin, and forms the heparin-binding site in follistatin. 9233787 8 54 part_of containing 1083:1092 arg1 follistatin AND tandemly repeated FS domains follistatin tandemly repeated FS domains OGER Site follistatin P19883 domains This hairpin is likely to act as a rigid spacer in proteins containing tandemly repeated FS domains, such as follistatin and agrin, and forms the heparin-binding site in follistatin. 9233787 8 54 part_of containing 1083:1092 arg1 proteins AND tandemly repeated FS domains proteins tandemly repeated FS domains Fterm Site proteins domains This hairpin is likely to act as a rigid spacer in proteins containing tandemly repeated FS domains, such as follistatin and agrin, and forms the heparin-binding site in follistatin. 9233787 8 54 part_of containing 1083:1092 arg1 agrin AND tandemly repeated FS domains agrin tandemly repeated FS domains PUBTATOR Site agrin 375790 domains This hairpin is likely to act as a rigid spacer in proteins containing tandemly repeated FS domains, such as follistatin and agrin, and forms the heparin-binding site in follistatin. 21908432 3 45 gly leucine-rich 442:453 arg1 a single leucine-rich repeat leucine a single leucine-rich repeat leucine We have crystallized the GPIbβ ectodomain (GPIbβ(E)) and determined the structure to show a single leucine-rich repeat with N- and C-terminal disulphide-bonded capping regions. 18657508 2 28 part_of alpha 447:451 arg1 the N-terminal ligand-binding domain signal regulatory protein alpha the N-terminal ligand-binding domain PUBTATOR Site signal regulatory protein alpha 140885 domain We describe the high-resolution X-ray crystallographic structures of the immunoglobulin superfamily domain of CD47 alone and in complex with the N-terminal ligand-binding domain of signal regulatory protein alpha (SIRPalpha). 18657508 2 38 part_of CD47 350:353 arg1 the immunoglobulin superfamily domain CD47 the immunoglobulin superfamily domain OGER Site CD47 Q08722 domain We describe the high-resolution X-ray crystallographic structures of the immunoglobulin superfamily domain of CD47 alone and in complex with the N-terminal ligand-binding domain of signal regulatory protein alpha (SIRPalpha). 12144777 4 42 part_of site 468:471 arg1 the (alpha/beta)(8) barrel subunits subunits site OGER Site subunits 1800 site The active site in each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is composed of binuclear zinc ions bridged by the Glu125 side-chain located at the bottom of the barrel, and it faces toward the microvillar membrane of a kidney tubule. 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. 25765764 0 20 part_of LRIG1 0:4 arg1 LRIG1 extracellular domain LRIG1 LRIG1 extracellular domain PUBTATOR Site LRIG1 26018 domain LRIG1 extracellular domain: structure and function analysis. 21676880 3 30 part_of has 548:550 arg1 KCNE1 AND two distinct N-glycosylation sites KCNE1 two distinct N-glycosylation sites PUBTATOR Site KCNE1 3753 sites We show that KCNE1 has two distinct N-glycosylation sites: a typical co-translational site and a consensus site ∼20 residues away that unexpectedly acquires N-glycans after protein synthesis (post-translational). 21676880 3 30 part_of has 548:550 arg1 KCNE1 AND a consensus site KCNE1 site PUBTATOR Site KCNE1 3753 site We show that KCNE1 has two distinct N-glycosylation sites: a typical co-translational site and a consensus site ∼20 residues away that unexpectedly acquires N-glycans after protein synthesis (post-translational). 25385546 3 8 part_of RPTPσ 540:544 arg1 the RPTPσ extracellular region RPTPσ the RPTPσ extracellular region PUBTATOR Site RPTPσ 5802 region Here, we report crystallographic, electron microscopic and small-angle X-ray scattering analyses, which reveal sufficient inter-domain flexibility in the RPTPσ extracellular region for interaction with both cis (same cell) and trans (opposite cell) ligands. 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. 1533633 4 77 part_of sites 744:748 arg1 the alpha-subunit subunit sites OGER Site subunit P06865 sites By expression of the mutant cDNAs in COS-1 cells, each of the three glycosylation sites on the alpha-subunit was found to be modified by an oligosaccharide. 9233787 2 32 part_of follistatin-like 272:287 arg1 a follistatin-like (FS) domain follistatin a follistatin-like (FS) domain OGER Site follistatin P19883 domain Apart from an acidic N-terminal segment, BM-40 consists of a follistatin-like (FS) domain and an EF-hand calcium-binding (EC) domain. 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. 17542669 5 68 part_of 2,500 687:691 arg1 2 large (2,500 A(2) OGER SpecificSite large (2,500 Q8N3Y3 A(2) The interface buried in the complex is large (2,500 A(2)) and an extensive network of ionic, polar, and hydrophobic bonding is involved in the interaction. 3542030 6 55 part_of terminus 776:783 arg1 an additional leucine terminus an additional leucine leucine 24, 815] have an additional leucine at the amino terminus, making a total of 373 residues in the chain. 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. 10022822 7 47 part_of enzymes 1254:1260 arg1 the R-domain enzymes the R-domain Fterm Site enzymes R-domain However, the different fold of the p41 fragment results in additional contacts with the top of the R-domain of the enzymes, which defines the specificity-determining S2 and S1' substrate-binding sites. 10022822 7 70 part_of p41 1174:1176 arg1 the p41 fragment p41 the p41 fragment Cterm Site p41 fragment However, the different fold of the p41 fragment results in additional contacts with the top of the R-domain of the enzymes, which defines the specificity-determining S2 and S1' substrate-binding sites. 19252480 6 49 part_of TLR4 946:949 arg1 the conserved phenylalanines TLR4 the conserved phenylalanines PUBTATOR AminoAcid TLR4 7099 phenylalanines Five of the six lipid chains of LPS are buried deep inside the pocket and the remaining chain is exposed to the surface of MD-2, forming a hydrophobic interaction with the conserved phenylalanines of TLR4. 1544894 4 50 part_of containing 768:777 arg1 peptides AND these sites peptides these sites sites We isolated peptides containing these sites to determine, primarily by mass spectrometric analysis, the presence of O-linked fucose and/or beta-hydroxyaspartate. 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. 28661582 4 9 part_of tyrosinase 948:957 arg1 the tyrosinase subdomain tyrosinase the tyrosinase subdomain OGER Site tyrosinase P14679 subdomain In addition, the structures reveal for the first time that the Cys-rich subdomain, which is unique to vertebrate melanogenic proteins, has an epidermal growth factor-like fold and is tightly associated with the tyrosinase subdomain. 12620237 2 2 part_of EGF 372:374 arg1 the 621 amino acid EGF receptor extracellular region EGF the 621 amino acid EGF receptor extracellular region PUBTATOR Site EGF 1950 region EGF activates its receptor by inducing dimerization of the 621 amino acid EGF receptor extracellular region. 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. 9767079 6 37 part_of terminus 1080:1087 arg1 a hemagglutinin (HA) epitope terminus a hemagglutinin (HA) epitope epitope Wild-type and Gln58-RFCs containing a hemagglutinin (HA) epitope at the carboxyl terminus were similarly functional and, by immunofluorescence staining with rhodamine-conjugated anti-HA antibody, were localized to plasma membranes. 18768590 6 26 part_of WNK3 969:972 arg1 The kinase domain WNK3 The kinase domain PUBTATOR Site WNK3 Q9BYP7 domain The kinase domain of WNK3 alone was sufficient to increase TRPV5-mediated Ca2+ transport, and the positive regulatory effect was abolished by the kinase-inactive D294A mutation in WNK3, indicating a kinase-dependent mechanism. 20223216 4 20 part_of receptor 649:656 arg1 peripheral receptor residues receptor peripheral receptor residues Fterm Site receptor residues While retaining a similar mode of IL-13 binding to its related signaling receptor, IL-13Ralpha1, IL-13Ralpha2 uses peripheral receptor residues unused in the IL-13/IL-13Ralpha1 complex to generate a larger and more complementary interface for IL-13. 15173186 11 75 part_of receptor 1640:1647 arg1 Toll-like receptor 2 extracellular domain Toll-like receptor 2 Toll-like receptor 2 extracellular domain PUBTATOR Site Toll-like receptor 2 7097 domain Using site-directed mutagenesis, we have found that in Toll-like receptor 2 extracellular domain all four predicted glycosylation sites are substituted, although one site is inefficiently core-glycosylated and its removal drastically affects secretion. 10821832 4 60 part_of contains 986:993 arg1 this glycoprotein AND 13 transmembrane domains this glycoprotein 13 transmembrane domains Fterm Site glycoprotein domains Our data indicate that this glycoprotein contains 13 transmembrane domains, 3 large and 4 small luminal loops, 6 small cytoplasmic loops, and a cytoplasmic tail. 10821832 4 60 part_of contains 986:993 arg1 this glycoprotein AND a cytoplasmic tail this glycoprotein a cytoplasmic tail Fterm Site glycoprotein tail Our data indicate that this glycoprotein contains 13 transmembrane domains, 3 large and 4 small luminal loops, 6 small cytoplasmic loops, and a cytoplasmic tail. 21827946 2 7 part_of Fab 260:262 arg1 the 1121B Fab fragment 1121B Fab the 1121B Fab fragment PUBTATOR Site 1121B Fab 2187 fragment We have determined the structure of the 1121B Fab fragment in complex with domain 3 of VEGFR2, as well as the structure of a different neutralizing anti-VEGFR2 antibody, 6.64, also in complex with VEGFR2 domain 3. 21827946 2 9 part_of 1121B 254:258 arg1 the 1121B Fab fragment 1121B Fab the 1121B Fab fragment PUBTATOR Site 1121B Fab 2187 fragment We have determined the structure of the 1121B Fab fragment in complex with domain 3 of VEGFR2, as well as the structure of a different neutralizing anti-VEGFR2 antibody, 6.64, also in complex with VEGFR2 domain 3. 21827946 2 18 part_of VEGFR2 301:306 arg1 domain 3 VEGFR2 domain 3 PUBTATOR Site VEGFR2 3791 domain We have determined the structure of the 1121B Fab fragment in complex with domain 3 of VEGFR2, as well as the structure of a different neutralizing anti-VEGFR2 antibody, 6.64, also in complex with VEGFR2 domain 3. 21827946 2 22 part_of VEGFR2 411:416 arg1 VEGFR2 domain 3 VEGFR2 VEGFR2 domain 3 OGER Site VEGFR2 P35968 domain We have determined the structure of the 1121B Fab fragment in complex with domain 3 of VEGFR2, as well as the structure of a different neutralizing anti-VEGFR2 antibody, 6.64, also in complex with VEGFR2 domain 3. 27768895 5 34 part_of PKD2 759:762 arg1 The extracellular domain PKD2 The extracellular domain PUBTATOR Site PKD2 Q13563 domain The extracellular domain of PKD2, a hotspot for ADPKD pathogenic mutations, contributes to channel assembly and strategically interacts with the transmembrane core, likely serving as a physical substrate for extracellular stimuli to allosterically gate the channel. 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). 2141278 4 56 part_of C1-r 1223:1226 arg1 the homologous position C1-r the homologous position PUBTATOR Site C1-r 715 position This fragment was reduced and alkylated and then digested with elastase, and three peptides covering positions 131-135, 131-139, and 131-140 were characterized by amino acid analysis, Edman degradation, and mass spectrometry, showing that position 134 of C1-s is occupied partly by an asparagine (47%) and partly by an erythro-beta-hydroxyasparagine, in contrast with the homologous position (150) of C1-r which only contains erythro-beta-hydroxyasparagine. 2141278 4 61 part_of C1-s 1077:1080 arg1 position 134 C1-s position 134 PUBTATOR Site C1-s 716 position 134 This fragment was reduced and alkylated and then digested with elastase, and three peptides covering positions 131-135, 131-139, and 131-140 were characterized by amino acid analysis, Edman degradation, and mass spectrometry, showing that position 134 of C1-s is occupied partly by an asparagine (47%) and partly by an erythro-beta-hydroxyasparagine, in contrast with the homologous position (150) of C1-r which only contains erythro-beta-hydroxyasparagine. 11707436 7 23 part_of GAG 1501:1503 arg1 sulfated GAG fragments GAG sulfated GAG fragments Cterm Site GAG fragments In vitro, recombinant Hex S was highly active on water-soluble and amphiphilic glycoconjugates including artificial substrates, sulfated GAG fragments, and the sulfated glycosphingolipid SM2. 2737288 0 5 part_of elastase 80:87 arg1 the glycosylation site pancreatic elastase 1 the glycosylation site PUBTATOR Site pancreatic elastase 1 1990 site Localization and characterization of the glycosylation site of human pancreatic elastase 1. 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 Asn Asn SpecificSite Asn(172) Analysis of glycosylation sites showed that sFRP-1 contains a relatively large carbohydrate moiety on Asn(172) (approximately 2.8 kDa), whereas Asn(262), the second potential N-linked glycosylation site, is not modified. 11741940 8 32 gly moiety 1571:1576 arg1 172 172 172 SpecificSite Asn(172) Analysis of glycosylation sites showed that sFRP-1 contains a relatively large carbohydrate moiety on Asn(172) (approximately 2.8 kDa), whereas Asn(262), the second potential N-linked glycosylation site, is not modified. 11741940 8 42 gly glycosylation 1491:1503 arg2 glycosylation sites glycosylation sites sites Analysis of glycosylation sites showed that sFRP-1 contains a relatively large carbohydrate moiety on Asn(172) (approximately 2.8 kDa), whereas Asn(262), the second potential N-linked glycosylation site, is not modified. 11741940 8 100 gly glycosylation 1663:1675 arg2 Asn Asn Asn(262) Analysis of glycosylation sites showed that sFRP-1 contains a relatively large carbohydrate moiety on Asn(172) (approximately 2.8 kDa), whereas Asn(262), the second potential N-linked glycosylation site, is not modified. 11741940 8 100 gly glycosylation 1663:1675 arg2 the second potential N-linked glycosylation site the second potential N-linked glycosylation site site Analysis of glycosylation sites showed that sFRP-1 contains a relatively large carbohydrate moiety on Asn(172) (approximately 2.8 kDa), whereas Asn(262), the second potential N-linked glycosylation site, is not modified. 11741940 8 87 gly contains 1530:1537 arg1 sFRP-1 AND a relatively large carbohydrate moiety sFRP-1 a relatively large carbohydrate moiety PUBTATOR sFRP-1 6422 Analysis of glycosylation sites showed that sFRP-1 contains a relatively large carbohydrate moiety on Asn(172) (approximately 2.8 kDa), whereas Asn(262), the second potential N-linked glycosylation site, is not modified. 24036510 3 16 part_of fibronectin-like 501:516 arg1 a fibronectin-like domain fibronectin domain PUBTATOR Site fibronectin 2335 domain IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain. 24036510 3 39 part_of TIM 426:428 arg1 a TIM barrel domain TIM domain PUBTATOR Site TIM 7984 domain IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain. 24036510 3 39 part_of TIM 426:428 arg1 a fibronectin-like domain TIM domain PUBTATOR Site TIM 7984 domain IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain. 24036510 3 39 part_of TIM 426:428 arg1 a fibronectin-like domain TIM domain PUBTATOR Site TIM 7984 domain IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain. 24036510 3 0 part_of containing 444:453 arg1 a TIM barrel domain AND the catalytic site site site IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain. 24036510 3 0 part_of containing 444:453 arg1 a fibronectin-like domain AND the catalytic site site site IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain. 24036510 3 0 part_of containing 444:453 arg1 a fibronectin-like domain AND the catalytic site site site IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain. 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. 9883900 9 61 part_of IGFBP-5 1272:1278 arg1 C-terminal IGFBP-5 fragments IGFBP-5 C-terminal IGFBP-5 fragments PUBTATOR Site IGFBP-5 3488 fragments Fractions containing C-terminal IGFBP-5 fragments revealed significant IGF-I binding properties. 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. 2963625 1 0 part_of protein 138:144 arg1 The complete amino acid sequence protein The complete amino acid sequence Fterm Site protein sequence The complete amino acid sequence of the human complement system regulatory protein, factor H, has been derived from sequencing three overlapping cDNA clones. 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. 22809326 13 63 part_of proteins 1666:1673 arg1 The conserved luminal domain proteins The conserved luminal domain Fterm Site proteins domain CONCLUSION: The conserved luminal domain of lysosome-associated membrane proteins forms a previously unknown β-prism fold. 9233787 5 19 part_of BM-40 676:680 arg1 one face BM-40 one face OGER Site BM-40 P09486 face Residues implicated in cell binding, inhibition of cell spreading and disassembly of focal adhesions cluster on one face of BM-40, opposite the binding epitope for collagens and the N-linked carbohydrate. 2361960 1 11 gly glycosylation 212:224 arg2 glycosylation sites glycosylation sites sites The complete peptide map of purified recombinant human interleukin 5 (rhIL-5) was determined to verify its primary structure, glycosylation sites, and disulfide bonding structure. 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. 8636209 4 16 part_of gamma 527:531 arg1 the EC domain CD3 gamma the EC domain PUBTATOR Site CD3 gamma 917 domain A computer model indicated that the EC domain of CD3 gamma folds as an Ig domain. 28775322 7 59 part_of EGF-like 1487:1494 arg1 3 different EGF-like domains EGF 3 different EGF-like domains OGER Site EGF P01133 domains Here the authors report the structure of human POGLUT1 in complexes with 3 different EGF-like domains and donor substrates and shed light on the enzyme's substrate specificity and catalytic mechanism. 19901337 5 1 part_of receptor-binding 743:758 arg1 3 discontinuous receptor-binding motifs receptor 3 discontinuous receptor-binding motifs Fterm Site receptor motifs NL63-CoV RBD has a novel beta-sandwich core structure consisting of 2 layers of beta-sheets, presenting 3 discontinuous receptor-binding motifs (RBMs) to bind ACE2. 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. 29794134 3 60 part_of apo-WT 596:601 arg1 the extracellular ligand-binding domains apo the extracellular ligand-binding domains OGER Site apo Q8N6M6 domains Here, we report three high-resolution structures of the extracellular ligand-binding domains (ECDs) of R47H TREM2, apo-WT, and phosphatidylserine (PS)-bound WT TREM2 at 1.8, 2.2, and 2.2 Å, respectively. 29794134 3 67 part_of TREM2 641:645 arg1 the extracellular ligand-binding domains WT TREM2 the extracellular ligand-binding domains PUBTATOR Site WT TREM2 54209 domains Here, we report three high-resolution structures of the extracellular ligand-binding domains (ECDs) of R47H TREM2, apo-WT, and phosphatidylserine (PS)-bound WT TREM2 at 1.8, 2.2, and 2.2 Å, respectively. 29794134 3 69 part_of TREM2 589:593 arg1 the extracellular ligand-binding domains TREM2 the extracellular ligand-binding domains PUBTATOR Site TREM2 54209 domains Here, we report three high-resolution structures of the extracellular ligand-binding domains (ECDs) of R47H TREM2, apo-WT, and phosphatidylserine (PS)-bound WT TREM2 at 1.8, 2.2, and 2.2 Å, respectively. 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. 22041449 0 60 part_of G2 57:58 arg1 the ligand binding domain netrin G2 the ligand binding domain OGER Site netrin G2 Q96CW9 domain Crystal structure of the ligand binding domain of netrin G2. 22023369 3 40 gly sFcγRIIIa 568:576 arg1 the two N-glycans FcγRIIIa the two N-glycans PUBTATOR FcγRIIIa 2214 The crystal structure shows that one of the two N-glycans of sFcγRIIIa mediates the interaction with nonfucosylated Fc, thereby stabilizing the complex. 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. 1463457 5 8 part_of contains 887:894 arg1 The predicted sequence AND 13 potential N-glycosylation sites The predicted sequence 13 potential N-glycosylation sites sites The predicted sequence has 552 amino acids with a leader peptide of 36 amino acids and contains 13 potential N-glycosylation sites, of which it is likely that 10 are used. 1533633 4 1 gly glycosylation 730:742 arg2 the three glycosylation sites the three glycosylation sites sites By expression of the mutant cDNAs in COS-1 cells, each of the three glycosylation sites on the alpha-subunit was found to be modified by an oligosaccharide. 1533633 4 31 gly modified 787:794 arg1 the three glycosylation sites AND an oligosaccharide the three glycosylation sites an oligosaccharide sites By expression of the mutant cDNAs in COS-1 cells, each of the three glycosylation sites on the alpha-subunit was found to be modified by an oligosaccharide. 24226769 7 72 part_of NOTCH1 919:924 arg1 human NOTCH1 peptides NOTCH1 human NOTCH1 peptides PUBTATOR Site NOTCH1 100037842 peptides GALNT11 O-glycosylates human NOTCH1 peptides in vitro, thereby supporting a mechanism of Notch activation either by increasing ADAM17-mediated ectodomain shedding of the Notch receptor or by modification of specific EGF repeats. 8962717 7 72 part_of proteins 1225:1232 arg1 consensus glycosylation sites proteins consensus glycosylation sites Fterm Site proteins sites The large hydrodynamic mass of these oligosaccharides could influence ligand binding, an effect which is likely to vary with the difference in consensus glycosylation sites of proteins related to p170 i.e. p185erbB2/neu, p180erbB3 and p180erbB4. 21269602 5 18 part_of VE-cadherin 842:852 arg1 the VE-cadherin EC1-2 adhesive region structure of the VE-cadherin EC1-2 the VE-cadherin EC1-2 adhesive region PUBTATOR Site structure of the VE-cadherin EC1-2 1003 region We also present the 2.1-Å-resolution crystal structure of the VE-cadherin EC1-2 adhesive region, which reveals homodimerization via the strand-swap mechanism common to classical cadherins. 21269602 5 23 part_of EC1-2 854:858 arg1 the VE-cadherin EC1-2 adhesive region structure of the VE-cadherin EC1-2 the VE-cadherin EC1-2 adhesive region PUBTATOR Site structure of the VE-cadherin EC1-2 1003 region We also present the 2.1-Å-resolution crystal structure of the VE-cadherin EC1-2 adhesive region, which reveals homodimerization via the strand-swap mechanism common to classical cadherins. 19901337 6 35 part_of ACE2 895:898 arg1 common ACE2 regions ACE2 common ACE2 regions PUBTATOR Site ACE2 59272 regions NL63-CoV and SARS-CoV have no structural homology in RBD cores or RBMs; yet the 2 viruses recognize common ACE2 regions, largely because of a "virus-binding hotspot" on ACE2. 14699159 2 11 part_of contains 413:420 arg1 a 90-kDa ER transmembrane protein AND three evolutionarily conserved N-linked glycosylation sites a 90-kDa ER transmembrane protein three evolutionarily conserved N-linked glycosylation sites Fterm Site protein sites ATF6, a 90-kDa ER transmembrane protein, contains three evolutionarily conserved N-linked glycosylation sites within its carboxyl luminal domain. 14699159 2 11 part_of contains 413:420 arg1 ATF6 AND three evolutionarily conserved N-linked glycosylation sites ATF6 three evolutionarily conserved N-linked glycosylation sites PUBTATOR Site ATF6 22926 sites ATF6, a 90-kDa ER transmembrane protein, contains three evolutionarily conserved N-linked glycosylation sites within its carboxyl luminal domain. 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. 28775322 1 22 part_of EGF-like 216:223 arg1 Notch epidermal growth factor-like (EGF-like) domains EGF Notch epidermal growth factor-like (EGF-like) domains OGER Site EGF P01133 domains Protein O-glucosyltransferase 1/Rumi-mediated glucosylation of Notch epidermal growth factor-like (EGF-like) domains plays an important role in Notch signaling. 28775322 1 66 part_of Notch 180:184 arg1 Notch epidermal growth factor-like (EGF-like) domains Notch Notch epidermal growth factor-like (EGF-like) domains PUBTATOR Site Notch 31293 domains Protein O-glucosyltransferase 1/Rumi-mediated glucosylation of Notch epidermal growth factor-like (EGF-like) domains plays an important role in Notch signaling. 22601780 4 30 part_of EGF 469:471 arg1 the second EGF domain EGF the second EGF domain OGER Site EGF P01133 domain An Arg-Gly-Asp (RGD) motif in the second EGF domain (EGF2) mediates adhesion by endothelial cells and phagocytes. 22601780 4 42 part_of motif 449:453 arg1 the second EGF domain motif the second EGF domain domain An Arg-Gly-Asp (RGD) motif in the second EGF domain (EGF2) mediates adhesion by endothelial cells and phagocytes. 18234225 3 68 part_of enzyme 609:614 arg1 the S1' site enzyme the S1' site Fterm Site enzyme site Crystal structures of GCPII in complex with various ligands have provided insight into the binding of these ligands, particularly to the S1' site of the enzyme. 1472036 1 17 part_of alpha-subunits 243:256 arg1 the region subunits the region OGER Site subunits P06213 region The alpha 2 beta 2 structure of the insulin receptor has previously been shown to involve one disulfide bridge between the alpha-subunits in the region containing Cys435, Cys468 and Cys524. 1472036 1 5 part_of containing 272:281 arg1 the region AND Cys468 Cys435, Cys468 and Cys524 Cys435, Cys468 and Cys524 The alpha 2 beta 2 structure of the insulin receptor has previously been shown to involve one disulfide bridge between the alpha-subunits in the region containing Cys435, Cys468 and Cys524. 1472036 1 5 part_of containing 272:281 arg1 the region AND Cys435 Cys435, Cys468 and Cys524 Cys435, Cys468 and Cys524 The alpha 2 beta 2 structure of the insulin receptor has previously been shown to involve one disulfide bridge between the alpha-subunits in the region containing Cys435, Cys468 and Cys524. 1472036 1 5 part_of containing 272:281 arg1 the region AND Cys435 Cys435, Cys468 and Cys524 Cys435, Cys468 and Cys524 The alpha 2 beta 2 structure of the insulin receptor has previously been shown to involve one disulfide bridge between the alpha-subunits in the region containing Cys435, Cys468 and Cys524. 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. 10769135 1 14 part_of alpha-amylase 200:212 arg1 the active site region pancreatic alpha-amylase the active site region PUBTATOR Site pancreatic alpha-amylase 279 region We report a multifaceted study of the active site region of human pancreatic alpha-amylase. 18768470 6 57 part_of FSTL3 1184:1188 arg1 the FSTL3 N-terminal domain FSTL3 the FSTL3 N-terminal domain PUBTATOR Site FSTL3 10272 domain Furthermore, binding studies revealed that replacing the FSTL3 N-terminal domain with the corresponding FS domain considerably lowers activin A affinity. 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. 19683538 5 49 part_of enzyme 1000:1005 arg1 the active site enzyme the active site Fterm Site enzyme site To investigate the binding specificity and catalytic mechanism of the human alpha-NAGAL enzyme, we determined three crystallographic complexes with different catalytic products bound in the active site of the enzyme. 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 Asn-18 Asn-18 SpecificSite Asn-18 The N-linked carbohydrate side chain of CD59u (at Asn-18) also displayed considerable heterogeneity. 8670172 9 92 gly CD59u 1348:1352 arg1 The N-linked carbohydrate side chain CD59u The N-linked carbohydrate side chain 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 Asn-18 The N-linked carbohydrate side chain Asn-18 The N-linked carbohydrate side chain of CD59u (at Asn-18) also displayed considerable heterogeneity. 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. 2668275 11 75 part_of STS 1416:1418 arg1 the two luminal domains STS the two luminal domains OGER Site STS P08842 domains The stability of STS in lysosomes may be related to the high homology of the two luminal domains of STS with the lysosomal sulfatases, arylsulfatase A, and arylsulfatase B. 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. 18703501 4 10 part_of IX 775:776 arg1 the small transmembrane and intracytoplasmic regions CA IX the small transmembrane and intracytoplasmic regions PUBTATOR Site CA IX 768 regions The produced proteins lacked the small transmembrane and intracytoplasmic regions of CA IX. 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. 19838198 3 34 part_of IL-17RA 543:549 arg1 two fibronectin-type domains IL-17RA two fibronectin-type domains OGER Site IL-17RA Q96F46 domains The mechanism of complex formation was unique for cytokines and involved the engagement of IL-17 by two fibronectin-type domains of IL-17RA in a groove between the IL-17 homodimer interface. 19838198 3 41 part_of fibronectin-type 515:530 arg1 two fibronectin-type domains fibronectin two fibronectin-type domains OGER Site fibronectin P02751 domains The mechanism of complex formation was unique for cytokines and involved the engagement of IL-17 by two fibronectin-type domains of IL-17RA in a groove between the IL-17 homodimer interface. 8702538 5 83 part_of sites 855:859 arg1 CD22 CD22 sites OGER Site CD22 P20273 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. 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.