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 29426894 6 36 gly N-glycosylation 930:944 arg1 serum soluble FcγRIIIb serum soluble FcγRIIIb PUBTATOR FcγRIIIb 2215 Among the six N-glycosylation sites of serum soluble FcγRIIIb, Asn45 was shown to be exclusively occupied by high-mannose-type oligosaccharides, whereas the remaining sites were solely modified by the complex-type oligosaccharides with sialic acid and fucose residues. 29426894 0 43 gly N-glycosylation 14:28 arg1 soluble Fcγ receptor IIIb soluble Fcγ receptor IIIb PUBTATOR Fcγ receptor IIIb 2215 Site-specific N-glycosylation analysis of soluble Fcγ receptor IIIb in human serum. 29426894 5 48 gly glycoproteins 901:913 arg1 the previously reported recombinant FcγRIII glycoproteins the previously reported recombinant FcγRIII glycoproteins PUBTATOR FcγRIII glycoproteins 2214 Our data indicate a distinct and common tendency of the glycoforms exhibited at each N-glycosylation site between the native and the previously reported recombinant FcγRIII glycoproteins. 29426894 3 54 gly glycoproteins 505:517 arg1 recombinant FcγRIII glycoproteins recombinant FcγRIII glycoproteins PUBTATOR FcγRIII glycoproteins 2214 Although several reports describe N-glycosylation profiles of recombinant FcγRIII glycoproteins, much remains unknown regarding their native glycoforms. 29426894 3 60 gly N-glycosylation 457:471 arg1 recombinant FcγRIII glycoproteins recombinant FcγRIII glycoproteins PUBTATOR FcγRIII glycoproteins 2214 Although several reports describe N-glycosylation profiles of recombinant FcγRIII glycoproteins, much remains unknown regarding their native glycoforms. 23632316 7 10 gly glycosylated 1161:1172 arg1 the IgG-Fc-ZP3E7 protein the IgG-Fc-ZP3E7 protein PUBTATOR IgG-Fc-ZP3E7 protein 7784 We also concluded that in the IgG-Fc-ZP3E7 protein, upon introduction of additional potential NXS/T glycosylation sites within its sequence, the original NST/S glycosylation site from the Fc region of the IgG-Fc-ZP3E7 protein is no longer glycosylated. 25094044 3 8 gly attached 576:583 arg1 UGGT1 AND glycan UGGT1 glycan PUBTATOR UGGT1 56886 The structure of glycan attached to UGGT1, however, has not been investigated. 25094044 4 22 gly glycosylation 668:680 arg1 UGGT1 UGGT1 PUBTATOR UGGT1 171129 In this study, we reveal the site of glycosylation (N269) and the glycan structures (Hex5-8HexNAc2) in UGGT1 obtained from rat (Rattus norvegicus), pig (Sus scrofa), cow (Bos taurus), and human (Homo sapiens). 25094044 0 41 gly ER-resident 50:60 arg1 uridine 5'-diphosphate-glucose ER-resident uridine 5'-diphosphate-glucose Cterm ER-resident Glycan structure and site of glycosylation in the ER-resident glycoprotein, uridine 5'-diphosphate-glucose: glycoprotein glucosyltransferases 1 from rat, porcine, bovine, and human. 25629924 0 30 gly glycosylation 14:26 arg1 secretory immunoglobulin A secretory immunoglobulin A Cterm secretory immunoglobulin A Site-specific glycosylation of secretory immunoglobulin A from human colostrum. 25629924 1 52 gly glycoprotein 125:136 arg1 Secretory immunoglobulin A Secretory immunoglobulin A Cterm Secretory immunoglobulin A Secretory immunoglobulin A (sIgA) is a major glycoprotein in milk and plays a key role in mediating immune protection of the gut mucosa. 25629924 3 89 gly glycosylation 408:420 arg1 sIgA sIgA Cterm IgA P11912 In this study, the site-specific glycosylation of sIgA isolated from human colostrum (n = 3) was analyzed using a combination of LC-MS and LC-MS/MS and in-house software (Glycopeptide Finder). 26022737 4 30 gly glycosylation 501:513 arg1 PSA PSA PUBTATOR PSA P07288 This extra glycosylation site of PSA is associated with a mutation in KLK3 genes. 27038031 4 20 gly N-glycosylation 476:490 arg1 recombinant pentameric and hexameric IgM recombinant pentameric and hexameric IgM OGER IgM P01871 In this study, the N-glycosylation of recombinant pentameric and hexameric IgM produced by the same human cell type and culture conditions was site-specifically profiled by RP-LC-CID/ETD-MS/MS using HILIC-enriched tryptic and GluC glycopeptides. 27038031 0 36 gly N-Glycosylation 14:28 arg1 Hexameric Human IgM Hexameric Human IgM OGER IgM P01871 Site-Specific N-Glycosylation of Recombinant Pentameric and Hexameric Human IgM. 29273683 5 11 part_of N230 549:552 arg1 rat CBG CBG N230 PUBTATOR SpecificSite CBG 299270 N230 We now show that mutations of conserved N-glycosylation sites at N238 in human CBG and N230 in rat CBG disrupt steroid binding. 29273683 11 13 gly glycosylation 1634:1646 arg1 the RCL the RCL OGER RCL O43598 Moreover, while glycosylation of N347 in the RCL limits these activities, N-glycans at other sites also appear to protect CBG from neutrophil elastase or chymotrypsin. 29273683 7 31 gly glycosylated 723:734 arg1 human CBG human CBG PUBTATOR CBG 866 Deglycosylation of fully glycosylated human CBG or human CBG with only one N-glycan at N238 with Endo H-reduced steroid-binding affinity, while PNGase F-mediated deglycosylation does not, indicating that steroid binding is preserved by deamidation of N238 when its N-glycan is removed. 29273683 7 51 gly Deglycosylation 698:712 arg1 human CBG human CBG PUBTATOR CBG 866 Deglycosylation of fully glycosylated human CBG or human CBG with only one N-glycan at N238 with Endo H-reduced steroid-binding affinity, while PNGase F-mediated deglycosylation does not, indicating that steroid binding is preserved by deamidation of N238 when its N-glycan is removed. 29273683 7 51 gly Deglycosylation 698:712 arg1 human CBG human CBG PUBTATOR CBG 866 Deglycosylation of fully glycosylated human CBG or human CBG with only one N-glycan at N238 with Endo H-reduced steroid-binding affinity, while PNGase F-mediated deglycosylation does not, indicating that steroid binding is preserved by deamidation of N238 when its N-glycan is removed. 29273683 5 58 part_of N238 527:530 arg1 human CBG CBG N238 PUBTATOR SpecificSite CBG 866 N238 We now show that mutations of conserved N-glycosylation sites at N238 in human CBG and N230 in rat CBG disrupt steroid binding. 29273683 3 75 gly Glycosylation 205:217 arg1 human CBG human CBG PUBTATOR CBG 866 Glycosylation of human CBG influences its steroid-binding activity, and there are N-glycosylation sites in the reactive center loops (RCLs) of human and rat CBGs. 25451932 8 69 gly N-glycosylation 978:992 arg1 corin cell surface targeting corin cell surface targeting PUBTATOR corin 10699 Moreover, N-glycosylation at Asn-697 in the scavenger receptor domain and at Asn-1022 in the protease domain is important for corin cell surface targeting and zymogen activation. 26911932 3 46 gly glycoforms 338:347 arg1 macroheterogeneous FSH glycoforms macroheterogeneous FSH glycoforms PUBTATOR FSH 14308 Recently, macroheterogeneous FSH glycoforms consisting of β-subunits that differ in N-glycan number were identified in pituitaries of several species and subsequently the recombinant human FSH glycoforms biochemically characterized. 26911932 3 114 gly glycoforms 498:507 arg1 recombinant human FSH recombinant human FSH PUBTATOR FSH 14308 Recently, macroheterogeneous FSH glycoforms consisting of β-subunits that differ in N-glycan number were identified in pituitaries of several species and subsequently the recombinant human FSH glycoforms biochemically characterized. 28759313 0 76 gly Glycosylation 0:12 arg1 DMP1 DMP1 PUBTATOR DMP1 13406 Glycosylation of DMP1 Is Essential for Chondrogenesis of Condylar Cartilage. 25242514 11 77 gly glycosylation 1731:1743 arg1 SP-A SP-A PUBTATOR SP-A Q8IWL1 SIGNIFICANCE: Our data provide evidence that the differential glycosylation of SP-A may play distinct roles in SP-A secretion, aggregation and degradation which may contribute to familial pulmonary fibrosis caused by SP-A2 mutations. 26231935 1 30 gly glycoprotein 138:149 arg1 Acetylcholinesterase Acetylcholinesterase PUBTATOR Acetylcholinesterase 43 Acetylcholinesterase (AChE; EC 3.1.1.7) is a glycoprotein possessing three conserved N-linked glycosylation sites in mammalian species, locating at 296, 381, and 495 residues of the human sequence. 26231935 2 56 gly N-glycosylation 335:349 arg1 AChE AChE PUBTATOR AChE 43 Several lines of evidence demonstrated that N-glycosylation of AChE affected the enzymatic activity, as well as its biosynthesis. 26947874 2 50 gly N-glycosylation 264:278 arg1 A1AT A1AT PUBTATOR A1AT 5265 However, the effects of an additional N-glycosylation in the unstructured region or the loop region of alpha-1 antitrypsin (A1AT) on the circulatory half-life of the protein are largely unknown. 27966990 7 25 gly deglycosylated 1146:1159 arg1 PNGase F-treated PNGase F-treated PUBTATOR PNGase 59007 MS/MS analyses of glycopeptides and deamidated, deglycosylated (PNGase F-treated) peptides from ectopically expressed VEGFR-2 in porcine aortic endothelial (PAE) cells identified N-glycans at the majority of the 17 potential N-glycosylation sites on VEGFR-2 in a site-specific manner. 27966990 0 44 gly N-Glycosylation 14:28 arg1 Endothelial Cell Receptor Tyrosine Kinase VEGFR-2 Endothelial Cell Receptor Tyrosine Kinase VEGFR-2 OGER VEGFR-2 P35968 Site-Specific N-Glycosylation of Endothelial Cell Receptor Tyrosine Kinase VEGFR-2. 27966990 4 63 gly N-glycosylation 554:568 arg1 VEGFR-2 VEGFR-2 PUBTATOR VEGFR-2 P35968 However, despite its importance, the functional role of N-glycosylation of VEGFR-2 remains poorly understood. 25628020 4 24 part_of Asn-76 821:826 arg1 thyroglobulin thyroglobulin Asn-76 PUBTATOR SpecificSite thyroglobulin 7038 Asn-76 Three of them, Asn-196 in adipocyte plasma membrane-associated protein (APMAP), Asn-91 in cluster of differentiation 166 (CD166/ALCAM), and Asn-76 in thyroglobulin, are human-specific. 25628020 4 33 part_of Asn-91 761:766 arg1 thyroglobulin thyroglobulin Asn-91 PUBTATOR SpecificSite thyroglobulin 7038 Asn-91 Three of them, Asn-196 in adipocyte plasma membrane-associated protein (APMAP), Asn-91 in cluster of differentiation 166 (CD166/ALCAM), and Asn-76 in thyroglobulin, are human-specific. 25628020 6 43 part_of thyroglobulin 1002:1014 arg1 the Asn-76 thyroglobulin the Asn-76 PUBTATOR SpecificSite thyroglobulin 7038 Asn-76 Notably, the Asn-76 of thyroglobulin might be involved in the increased production of thyroid hormones in humans, especially thyroxine (T4), because the removal of the glycan moiety from this site was reported to result in a significant decrease in T4 production. 25628020 4 73 part_of Asn-196 696:702 arg1 adipocyte plasma membrane-associated protein adipocyte plasma membrane-associated protein Asn-196 PUBTATOR SpecificSite adipocyte plasma membrane-associated protein 57136 Asn-196 Three of them, Asn-196 in adipocyte plasma membrane-associated protein (APMAP), Asn-91 in cluster of differentiation 166 (CD166/ALCAM), and Asn-76 in thyroglobulin, are human-specific. 25628020 4 73 part_of Asn-196 696:702 arg1 APMAP APMAP Asn-196 PUBTATOR SpecificSite APMAP 57136 Asn-196 Three of them, Asn-196 in adipocyte plasma membrane-associated protein (APMAP), Asn-91 in cluster of differentiation 166 (CD166/ALCAM), and Asn-76 in thyroglobulin, are human-specific. 29932112 1 1 gly glycoproteins 147:159 arg1 Pannexins Pannexins PUBTATOR Pannexins (Panx1 24145 Pannexins (Panx1, 2, 3) are channel-forming glycoproteins expressed in mammalian tissues. 29932112 9 12 gly N-glycosylation 1264:1278 arg1 Panx2 Panx2 PUBTATOR Panx2 56666 Our study indicates that N-glycosylation may be important for folding and trafficking of Panx2. 29932112 6 13 part_of Panx2 886:890 arg1 N86 Panx2 N86 PUBTATOR SpecificSite Panx2 56666 N86 Our results showed that N86 is the only N-glycosylation site of Panx2. 29932112 4 17 gly N-glycosylation 547:561 arg1 Panx2 Panx2 PUBTATOR Panx2 56666 Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1. 29932112 10 20 gly un-glycosylated 1353:1367 arg1 Panx1 Panx1 PUBTATOR Panx1 and 2 24145 We found that the un-glycosylated forms of Panx1 and 2 can readily interact, regulating their localization and potentially their channel function in cells where they are co-expressed. 29932112 6 25 gly N-glycosylation 862:876 arg1 Panx2 Panx2 PUBTATOR Panx2 56666 Our results showed that N86 is the only N-glycosylation site of Panx2. 29190644 1 0 gly glycoprotein 185:196 arg1 Human butyrylcholinesterase Human butyrylcholinesterase PUBTATOR Human butyrylcholinesterase 590 Human butyrylcholinesterase (BChE) is a glycoprotein capable of bioscavenging toxic compounds such as organophosphorus (OP) nerve agents. 29190644 5 34 gly glycoforms 888:897 arg1 monomeric human BChE glycoforms monomeric human BChE glycoforms PUBTATOR BChE 590 To investigate the effects of populating glycosylation site ASN241, monomeric human BChE glycoforms were simulated with and without site ASN241 glycosylated. 18533687 8 9 gly N-glycosylation 1305:1319 arg1 RXFP1 RXFP1 PUBTATOR RXFP1 59350 All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding. 18533687 10 28 gly N-glycosylation 1631:1645 arg1 optimal intracellular cAMP signaling optimal intracellular cAMP signaling OGER cAMP Q96JM3 In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling. 18533687 10 61 part_of RXFP1 1661:1665 arg1 Asn-303 RXFP1 Asn-303 PUBTATOR SpecificSite RXFP1 59350 Asn-303 In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling. 18533687 5 86 gly glycosylation 797:809 arg1 RXFP1 RXFP1 PUBTATOR RXFP1 59350 We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications. 28322444 1 13 gly glycosylated 198:209 arg1 The potassium ion channel Kv3.1b The potassium ion channel Kv3.1b Cterm Kv3.1b The potassium ion channel Kv3.1b is a member of a family of voltage-gated ion channels that are glycosylated in their mature form. 28322444 5 16 gly N220-glycosylated 946:962 arg1 N220-glycosylated Kv3.1b. N220-glycosylated Kv3.1b. Cterm Kv3.1b Mass spectrometry analysis revealed a complex type Hex3 HexNAc4 Fuc1 glycan as the major glycan component of the N229-glycosylated Kv3.1b protein, as opposed to a high-mannose type Man8 GlcNAc2 glycan for N220-glycosylated Kv3.1b. Taken together, these results suggest that trafficking-dependent roles of the Kv3.1b potassium channel are dependent on N229 site-specific glycosylation and N-glycan structure, and operate through a mechanism whereby specific N-glycan structures regulate cell surface expression. 28322444 3 20 gly unglycosylated 495:508 arg1 N220-glycosylated and unglycosylated Kv3.1b N220-glycosylated and unglycosylated Kv3.1b Cterm Kv3.1b Large quantities of asparagine 229 (N229)-glycosylated Kv3.1b reached the plasma membrane, whereas N220-glycosylated and unglycosylated Kv3.1b were mainly retained in the endoplasmic reticulum (ER). 28322444 3 33 gly N220-glycosylated 473:489 arg1 N220-glycosylated and unglycosylated Kv3.1b N220-glycosylated and unglycosylated Kv3.1b Cterm Kv3.1b Large quantities of asparagine 229 (N229)-glycosylated Kv3.1b reached the plasma membrane, whereas N220-glycosylated and unglycosylated Kv3.1b were mainly retained in the endoplasmic reticulum (ER). 28322444 3 51 gly -glycosylated 415:427 arg1 asparagine 229 (N229)-glycosylated Kv3.1b asparagine 229 (N229)-glycosylated Kv3.1b Cterm Kv3.1b Large quantities of asparagine 229 (N229)-glycosylated Kv3.1b reached the plasma membrane, whereas N220-glycosylated and unglycosylated Kv3.1b were mainly retained in the endoplasmic reticulum (ER). 28322444 0 63 gly N-glycosylation 53:67 arg1 the potassium channel Kv3.1b the potassium channel Kv3.1b Cterm Kv3.1b Identification and characterization of site-specific N-glycosylation in the potassium channel Kv3.1b. 23668542 9 15 gly neoglycoprotein 1290:1304 arg1 The A1AT neoglycoprotein The A1AT neoglycoprotein PUBTATOR A1AT neoglycoprotein 5265 The A1AT neoglycoprotein with an additional N-glycosylation site at position N123 exhibited a 62% increase in serum half-life. 23668542 11 32 gly neoglycoprotein 1588:1602 arg1 the recombinant A1AT neoglycoprotein the recombinant A1AT neoglycoprotein PUBTATOR A1AT neoglycoprotein 5265 The results suggest the recombinant A1AT neoglycoprotein as a serious alternative to A1AT derived from human plasma. 23668542 7 68 gly variants 994:1001 arg1 The N-glycan profile A1AT variants The N-glycan profile PUBTATOR A1AT variants 5265 The N-glycan profile of the recombinant A1AT variants was mostly composed of monofucosylated bi-, tri-, and tetraantennary complex-type N-glycans, with a tendency toward higher antennary structures compared to the wild-type. 23668542 0 92 gly neoglycoproteins 48:63 arg1 alpha 1-antitrypsin neoglycoproteins alpha 1-antitrypsin neoglycoproteins PUBTATOR alpha 1-antitrypsin neoglycoproteins 5265 Development and analysis of alpha 1-antitrypsin neoglycoproteins: the impact of additional N-glycosylation sites on serum half-life. 24018687 3 39 part_of DDR1 724:727 arg1 asparagine 211 DDR1 asparagine 211 PUBTATOR SpecificSite DDR1 780 asparagine 211 Site-directed mutational analysis of the consensus N-glycosylation sites of the DDRs revealed that mutations of asparagine 213 of DDR2 and asparagine 211 of DDR1, a conserved N-glycosylation site among vertebrate DDRs, inhibited the generation of the high-molecular-mass isoform. 24018687 3 53 part_of DDR2 697:700 arg1 asparagine 213 DDR2 asparagine 213 PUBTATOR SpecificSite DDR2 4921 asparagine 213 Site-directed mutational analysis of the consensus N-glycosylation sites of the DDRs revealed that mutations of asparagine 213 of DDR2 and asparagine 211 of DDR1, a conserved N-glycosylation site among vertebrate DDRs, inhibited the generation of the high-molecular-mass isoform. 26853155 10 66 part_of syncytin-2 1926:1935 arg1 residues 133, 312, 332 and 443 syncytin-2 residues 133, 312, 332 and 443 PUBTATOR SpecificSite syncytin-2 P60508 residues 133, 312, 332 and 443 Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2. 28630087 11 16 gly sialoglycoforms 1940:1954 arg1 the HNE sialoglycoforms the HNE sialoglycoforms PUBTATOR HNE 1991 Functionally, the paucimannosidic HNE glycoforms displayed preferential binding to human mannose binding lectin compared with the HNE sialoglycoforms, suggesting a glycoform-dependent involvement of HNE in complement activation. 28630087 12 18 gly N-glycosylated 2047:2060 arg1 α1-antitrypsin α1-antitrypsin PUBTATOR 1-antitrypsin 5265 The heavily N-glycosylated HNE protease inhibitor, α1-antitrypsin, displayed concentration-dependent complex formation and preferred glycoform-glycoform interactions with HNE. 28630087 1 25 gly N-glycosylated 170:183 arg1 Human neutrophil elastase Human neutrophil elastase PUBTATOR Human neutrophil elastase 1991 Human neutrophil elastase (HNE) is an important N-glycosylated serine protease in the innate immune system, but the structure and immune-modulating functions of HNE N-glycosylation remain undescribed. 28630087 11 30 gly glycoforms 1844:1853 arg1 the paucimannosidic HNE glycoforms the paucimannosidic HNE glycoforms PUBTATOR HNE 1991 Functionally, the paucimannosidic HNE glycoforms displayed preferential binding to human mannose binding lectin compared with the HNE sialoglycoforms, suggesting a glycoform-dependent involvement of HNE in complement activation. 28630087 10 54 gly glycosylation 1662:1674 arg1 HNE HNE PUBTATOR HNE 1991 The three glycosylation sites of HNE were located distal to the active site indicating glycan functions other than interference with HNE enzyme activity. 28630087 0 55 gly N-glycosylation 18:32 arg1 Spatiotemporally Regulated Human Neutrophil Elastase Spatiotemporally Regulated Human Neutrophil Elastase PUBTATOR Human Neutrophil Elastase 1991 Paucimannose-Rich N-glycosylation of Spatiotemporally Regulated Human Neutrophil Elastase Modulates Its Immune Functions. 28630087 2 108 gly N-glycosylation 445:459 arg1 HNE HNE PUBTATOR HNE 1991 Herein, LC-MS/MS-based glycan, glycopeptide and glycoprotein profiling were utilized to first determine the heterogeneous N-glycosylation of HNE purified from neutrophil lysates and then from isolated neutrophil granules of healthy individuals. 28630087 0 122 gly Elastase 81:88 arg1 Paucimannose-Rich N-glycosylation Human Neutrophil Elastase Paucimannose-Rich N-glycosylation PUBTATOR Human Neutrophil Elastase 1991 Paucimannose-Rich N-glycosylation of Spatiotemporally Regulated Human Neutrophil Elastase Modulates Its Immune Functions. 26784534 1 25 gly O-glycosylation 77:91 arg1 von Willebrand factor von Willebrand factor PUBTATOR von Willebrand factor 7450 BACKGROUND: O-glycosylation of von Willebrand factor (VWF) affects many of its functions; however, there is currently no information on the occupancy of the 10 putative O-glycosylation sites. 26784534 1 25 gly O-glycosylation 77:91 arg1 VWF VWF PUBTATOR VWF 7450 BACKGROUND: O-glycosylation of von Willebrand factor (VWF) affects many of its functions; however, there is currently no information on the occupancy of the 10 putative O-glycosylation sites. 28835497 2 89 gly glycoprotein 256:267 arg1 Glycoprotein K Glycoprotein K Cterm Glycoprotein K (gK Glycoprotein K (gK) is a conserved virion glycoprotein of all alphaherpesviruses that is not found in other herpesvirus subfamilies. 28835497 10 115 gly glycoprotein 2041:2052 arg1 HSV-1 glycoprotein K HSV-1 glycoprotein K Cterm HSV-1 glycoprotein K (gK These results demonstrate a critical role for the N glycosylation sites and cysteines for the structure and function of the amino terminus of gK.IMPORTANCE We have previously identified important entry and neurotropic determinants in the amino terminus of HSV-1 glycoprotein K (gK). 28747502 3 23 gly glycosylation 451:463 arg1 mouse DPP4 mouse DPP4 PUBTATOR DPP4 P27487 Previous work revealed that glycosylation of mouse DPP4 plays a role in blocking MERS-CoV infection. 27314333 4 12 gly N-glycosylated 695:708 arg1 Rspo3 Rspo3 PUBTATOR Rspo3 84870 Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain. 27314333 4 12 gly N-glycosylated 695:708 arg1 human Rspo1 human Rspo1 PUBTATOR Rspo1 284654 Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain. 27314333 10 39 gly Rspo1 1590:1594 arg1 N-glycan Rspo1 N-glycan PUBTATOR Rspo1 284654 While N-glycan of Rspo1 plays a role in its intracellular stability, it had little effect on secreted Rspo1. 27314333 6 43 part_of N137 1080:1083 arg1 Rspo1 Rspo1 N137 PUBTATOR SpecificSite Rspo1 284654 N137 Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media. 27314333 0 47 gly N-Glycosylation 0:14 arg1 Human R-Spondin 1 Human R-Spondin 1 PUBTATOR Human R-Spondin 1 284654 N-Glycosylation of Human R-Spondin 1 Is Required for Efficient Secretion and Stability but Not for Its Heparin Binding Ability. 27314333 4 50 gly N-glycosylated 789:802 arg1 Rspo2 Rspo2 PUBTATOR Rspo2 340419 Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain. 27314333 11 55 gly N-glycosylation 1736:1750 arg1 Rspo1 Rspo1 PUBTATOR Rspo1 284654 Our findings provide evidence for the critical role of N-glycosylation in the biogenesis of Rspo1. 27725718 8 24 gly hyper-glycosylated 1048:1065 arg1 In NAFLD haptoglobin and transferrin glycosylation sites In NAFLD haptoglobin and transferrin glycosylation sites PUBTATOR haptoglobin 3240 In NAFLD haptoglobin and transferrin glycosylation sites were hyper-glycosylated, a property qualifying for its use as a potential biomarker. 27725718 9 28 gly glycosylation 1159:1171 arg1 haptoglobin haptoglobin PUBTATOR haptoglobin 3240 Furthermore, we observed, that glycosylation sites of liver-originating transferrin and haptoglobin are differentially occupied under physiological conditions, a further instance not noticed in serum proteins to date. 27725718 9 28 gly glycosylation 1159:1171 arg1 liver-originating transferrin liver-originating transferrin PUBTATOR transferrin 7018 Furthermore, we observed, that glycosylation sites of liver-originating transferrin and haptoglobin are differentially occupied under physiological conditions, a further instance not noticed in serum proteins to date. 27725718 7 80 gly glycosylation 917:929 arg1 IgA1 IgA1 PUBTATOR IgA1 3493 In CDG glycosylation sites of IgG2 and IgA1 were occupied to normal levels. 27725718 7 80 gly glycosylation 917:929 arg1 IgG2 IgG2 Cterm IgG2 In CDG glycosylation sites of IgG2 and IgA1 were occupied to normal levels. 22872643 8 30 gly Notch2 1265:1270 arg1 EGF repeats Notch2 EGF repeats PUBTATOR Notch2 18129 A panel of EGF repeats from human coagulation factor 9 (FA9), mouse Notch1, and Notch2 were bacterially expressed and purified by reverse phase HPLC for use in in vitro enzyme assays. 22872643 0 32 gly notch 83:87 arg1 the epidermal growth factor-like (EGF) repeats notch the epidermal growth factor-like (EGF) repeats PUBTATOR notch 18128 Site-specific O-glucosylation of the epidermal growth factor-like (EGF) repeats of notch: efficiency of glycosylation is affected by proper folding and amino acid sequence of individual EGF repeats. 22872643 8 74 gly Notch1 1253:1258 arg1 EGF repeats Notch1 EGF repeats PUBTATOR Notch1 18128 A panel of EGF repeats from human coagulation factor 9 (FA9), mouse Notch1, and Notch2 were bacterially expressed and purified by reverse phase HPLC for use in in vitro enzyme assays. 27095603 6 43 gly glycopeptides 1108:1120 arg1 native transferrin native transferrin PUBTATOR transferrin 7018 In this technical note, the aberrant glycosylation profiles of CDG cases are presented to shed light on the MS of native transferrin and glycopeptides from the viewpoint of clinical glycoproteomics. 27095603 0 50 gly glycoforms 33:42 arg1 transferrin glycoforms transferrin glycoforms PUBTATOR transferrin 7018 Mass spectrometry of transferrin glycoforms to detect congenital disorders of glycosylation: Site-specific profiles and pitfalls. 27095603 2 67 gly glycoprotein 292:303 arg1 Transferrin Transferrin PUBTATOR Transferrin 7018 Transferrin is an 80 kDa glycoprotein and the glycoform at two N-glycosylation sites is comprised of a di-sialylated biantennary oligosaccharide as the major form and minor species with fucosylated or triantennary structures. 22688517 6 24 gly glycosylation 1145:1157 arg1 recombinant human LOX-1 recombinant human LOX-1 PUBTATOR LOX-1 4973 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 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. 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. 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. 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. 26634432 3 19 gly N-terminal 308:317 arg1 a new proteoglycan N-terminal a new proteoglycan Cterm N-terminal After glycosylation, an N-terminal fragment of DMP1 protein was identified as a new proteoglycan (DMP1-PG) in bone matrix. 26634432 0 33 gly Glycosylation 0:12 arg1 Dentin Matrix Protein 1 Dentin Matrix Protein 1 PUBTATOR Dentin Matrix Protein 1 13406 Glycosylation of Dentin Matrix Protein 1 is critical for osteogenesis. 26634432 3 56 gly protein 336:342 arg1 a new proteoglycan DMP1 protein a new proteoglycan PUBTATOR DMP1 protein 13406 After glycosylation, an N-terminal fragment of DMP1 protein was identified as a new proteoglycan (DMP1-PG) in bone matrix. 26634432 9 58 gly glycosylation 1070:1082 arg1 DMP1 DMP1 PUBTATOR DMP1 13406 These findings indicate that glycosylation of DMP1 is a key posttranslational modification process during development and that DMP1-PG functions as an indispensable proteoglycan in osteogenesis. 26776361 3 9 gly full-glycosylated 810:826 arg1 full-glycosylated EPO full-glycosylated EPO PUBTATOR EPO 2056 PEGylation with two short 750 or 2000 Da PEG units at positions 24, 38, or 83 significantly decreased unspecific aggregation and proteolytic degradation while biological activity in vitro was preserved or even increased in comparison to full-glycosylated EPO. 26776361 2 57 gly unglycosylated 482:495 arg1 recombinant unglycosylated erythropoietin recombinant unglycosylated erythropoietin PUBTATOR erythropoietin 2056 In this work we utilized the non-natural amino acid p-azidophenylalanine (pAzF) in combination with the chemoselective Staudinger-phosphite reaction to install branched PEG chains to recombinant unglycosylated erythropoietin (EPO) at each single naturally occurring glycosylation site. 26776361 2 57 gly unglycosylated 482:495 arg1 EPO EPO PUBTATOR EPO 2056 In this work we utilized the non-natural amino acid p-azidophenylalanine (pAzF) in combination with the chemoselective Staudinger-phosphite reaction to install branched PEG chains to recombinant unglycosylated erythropoietin (EPO) at each single naturally occurring glycosylation site. 23714211 15 26 gly glycosylation 2577:2589 arg1 ICAM-2 ICAM-2 PUBTATOR ICAM-2 3384 CONCLUSIONS: Reduced glycosylation of ICAM-2 significantly attenuated, but did not abolish, its ability to suppress metastatic properties of NB cells. 23714211 10 39 gly glycosylation 1639:1651 arg1 ICAM-2 ICAM-2 PUBTATOR ICAM-2 3384 METHODS: Because it is well documented that glycosylation facilitates essential steps in tumor progression and metastasis, we investigated whether the glycosylation status of ICAM-2 affected the phenotype of NB cells. 23714211 14 52 gly fully-glycosylated 2441:2458 arg1 fully-glycosylated ICAM-2 fully-glycosylated ICAM-2 PUBTATOR ICAM-2 3384 However, unlike fully-glycosylated ICAM-2, glycosylation site variants did not completely suppress disseminated tumor development. 23714211 12 55 gly fully-glycosylated 2181:2198 arg1 fully-glycosylated ICAM-2 or no ICAM-2 fully-glycosylated ICAM-2 or no ICAM-2 PUBTATOR ICAM-2 3384 RESULTS: The in vitro and in vivo phenotypes of cells expressing glycosylation site variants differed from cells expressing fully-glycosylated ICAM-2 or no ICAM-2. 23714211 9 93 gly glycosylation 1409:1421 arg1 ICAM-2 ICAM-2 PUBTATOR ICAM-2 3384 The goal of the study presented here was to determine if the glycosylation status of ICAM-2 influenced its function in neuroblastoma cells. 23714211 0 118 gly N-glycosylation 0:14 arg1 ICAM-2 ICAM-2 PUBTATOR ICAM-2 3384 N-glycosylation of ICAM-2 is required for ICAM-2-mediated complete suppression of metastatic potential of SK-N-AS neuroblastoma cells. 30135544 2 26 gly glycosylation 241:253 arg1 prion protein prion protein PUBTATOR prion protein 5621 The effects of glycosylation on prion protein (PrP) structure and function have not been thoroughly elucidated to date. 30135544 2 26 gly glycosylation 241:253 arg1 PrP PrP PUBTATOR PrP 5621 The effects of glycosylation on prion protein (PrP) structure and function have not been thoroughly elucidated to date. 30135544 3 53 gly glycosylation 400:412 arg1 human PrP human PrP PUBTATOR PrP 5621 In this study, we attempt to elucidate the effects of glycosylation on the aggregation and toxicity of human PrP. 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 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. 22355413 4 33 gly glycosylation 830:842 arg1 NA proteins NA proteins Cterm NA proteins 4758 In this study, we provided more bioinformatics and statistic evidences for further predicting the significant biological functions of glycosite migration in the host adaptation of human influenza H1N1 viruses, by employing homology modeling and in silico protein glycosylation of representative HA and NA proteins as well as amino acid variability analysis at antigenic sites of HA and NA. 22355413 4 33 gly glycosylation 830:842 arg1 NA NA Cterm NA 4758 In this study, we provided more bioinformatics and statistic evidences for further predicting the significant biological functions of glycosite migration in the host adaptation of human influenza H1N1 viruses, by employing homology modeling and in silico protein glycosylation of representative HA and NA proteins as well as amino acid variability analysis at antigenic sites of HA and NA. 28822114 5 39 gly glycosylation 704:716 arg1 DMP1 DMP1 PUBTATOR DMP1 13406 The only glycosylation site of DMP1 is serine89 (S89) in the N-terminal domain of the protein in mouse. 28822114 5 40 part_of DMP1 726:729 arg1 serine89 DMP1 serine89 PUBTATOR AminoAcid DMP1 13406 serine89 The only glycosylation site of DMP1 is serine89 (S89) in the N-terminal domain of the protein in mouse. 28822114 0 49 gly Glycosylation 0:12 arg1 dentin matrix protein 1 dentin matrix protein 1 PUBTATOR dentin matrix protein 1 13406 Glycosylation of dentin matrix protein 1 is a novel key element for astrocyte maturation and BBB integrity. 26536155 6 38 gly glycosylation 1501:1513 arg1 human IgG3 human IgG3 PUBTATOR IgG3 P01860 The approach was evaluated on glycoprotein standards and also applied to investigate the glycosylation of human IgG3 providing details on the hitherto uncharacterized glycosylation site Asn392 of the CH3 domain. 28928219 6 3 gly glycosylated 1244:1255 arg1 glycosylated Skp1 glycosylated Skp1 PUBTATOR Skp1 6500 Molecular dynamics trajectories of glycosylated Skp1 whose calculated monosaccharide relaxation kinetics and rotational correlation times agreed with the NMR data indicated that the glycan interacts with the loop connecting two α-helices of the F-box-combining site. 26420485 11 39 gly glycosylation 1477:1489 arg1 RDS function RDS function PUBTATOR RDS 19133 These data suggest that glycosylation of RDS is required for RDS function or stability in cones, a difference that may be due to extracellular versus intradiscal localization of the RDS glycan in cones versus rods. 26420485 11 39 gly glycosylation 1477:1489 arg1 RDS RDS PUBTATOR RDS 19133 These data suggest that glycosylation of RDS is required for RDS function or stability in cones, a difference that may be due to extracellular versus intradiscal localization of the RDS glycan in cones versus rods. 26420485 7 64 gly unglycosylated 972:985 arg1 the unglycosylated RDS binding partner rod outer segment membrane protein 1 the unglycosylated RDS binding partner rod outer segment membrane protein 1 PUBTATOR rod outer segment membrane protein 1 19881 Normal levels of RDS and the unglycosylated RDS binding partner rod outer segment membrane protein 1 (ROM-1) were found in N229S retinas. 26420485 7 64 gly unglycosylated 972:985 arg1 ROM-1 ROM-1 PUBTATOR ROM-1 19881 Normal levels of RDS and the unglycosylated RDS binding partner rod outer segment membrane protein 1 (ROM-1) were found in N229S retinas. 25673720 14 6 gly glycosylated 2165:2176 arg1 C C Cterm C Q9NP58 We infected mice that express different forms of glycosylated PrP(C) with three different TSE agents. 25673720 14 6 gly glycosylated 2165:2176 arg1 glycosylated PrP glycosylated PrP OGER PrP Q9NP58 We infected mice that express different forms of glycosylated PrP(C) with three different TSE agents. 25673720 10 23 gly glycosylation 1557:1569 arg1 C C Cterm C Q9NP58 These results highlight glycosylation of PrP(C) as a key factor in determining the transmission efficiency of TSEs between different species. 25673720 10 23 gly glycosylation 1557:1569 arg1 PrP PrP PUBTATOR PrP 19122 These results highlight glycosylation of PrP(C) as a key factor in determining the transmission efficiency of TSEs between different species. 25673720 0 44 gly glycosylation 4:16 arg1 PrPC PrPC PUBTATOR PrPC 19122 The glycosylation status of PrPC is a key factor in determining transmissible spongiform encephalopathy transmission between species. 25673720 6 48 gly glycosylation 938:950 arg1 C C Cterm C Q9NP58 Here, we show in vivo that glycosylation of the host PrP(C) has a significant impact on the transmission of TSE between different host species. 25673720 6 48 gly glycosylation 938:950 arg1 the host PrP the host PrP PUBTATOR PrP 19122 Here, we show in vivo that glycosylation of the host PrP(C) has a significant impact on the transmission of TSE between different host species. 25673720 13 83 gly glycosylation 2026:2038 arg1 C C Cterm C Q9NP58 PrP(C) undergoes posttranslational glycosylation, and the addition of these glycans may play a role in disease transmission. 25673720 13 83 gly glycosylation 2026:2038 arg1 PrP PrP PUBTATOR PrP 19122 PrP(C) undergoes posttranslational glycosylation, and the addition of these glycans may play a role in disease transmission. 25673720 7 106 gly glycosylated 1091:1102 arg1 C C Cterm C Q9NP58 We infected mice carrying different glycosylated forms of PrP(C) with two human agents (sCJDMM2 and vCJD) and one hamster strain (263K). 25673720 7 106 gly glycosylated 1091:1102 arg1 PrP PrP PUBTATOR PrP 19122 We infected mice carrying different glycosylated forms of PrP(C) with two human agents (sCJDMM2 and vCJD) and one hamster strain (263K). 25759508 0 41 gly O-Glycosylation 13:27 arg1 Human Immunoglobulin G3 Human Immunoglobulin G3 PUBTATOR Human Immunoglobulin G3 3502 Hinge-Region O-Glycosylation of Human Immunoglobulin G3 (IgG3). 25759508 0 41 gly O-Glycosylation 13:27 arg1 IgG3 IgG3 PUBTATOR IgG3 P01860 Hinge-Region O-Glycosylation of Human Immunoglobulin G3 (IgG3). 28970103 15 154 gly O-glycopeptides 2859:2873 arg1 the serum samples the serum samples PUBTATOR IgAN 60498 Furthermore, quantitative analysis of intact O-glycopeptides from the serum samples of IgA nephropathy (IgAN) patients and healthy donors was performed, and the results showed the potential of the strategy to discover O-glycosylation biomarkers. 20943674 8 25 gly glycosylated 1364:1375 arg1 rhLF rhLF OGER rhLF P02788 Monosaccharide composition analysis of rhLF revealed small amounts of N-glycolylneuraminic acid, which were not detected by MS. hLF and rhLF appear to be glycosylated at the same two sites: Asn138 and Asn479. 20943674 8 25 gly glycosylated 1364:1375 arg1 hLF hLF PUBTATOR hLF 3131 Monosaccharide composition analysis of rhLF revealed small amounts of N-glycolylneuraminic acid, which were not detected by MS. hLF and rhLF appear to be glycosylated at the same two sites: Asn138 and Asn479. 20943674 11 27 gly N-glycosylation 1597:1611 arg1 rhLF rhLF OGER rhLF P02788 The different N-glycosylation profile of rhLF when compared with that of hLF is in consistent with the widely held view that glycosylation is species- and tissue/cell-specific. 20943674 0 46 gly N-glycosylation 52:66 arg1 wild-type and recombinant human lactoferrin wild-type and recombinant human lactoferrin OGER lactoferrin P02788 Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle. 20943674 9 68 gly unglycosylated 1472:1485 arg1 rhLF rhLF OGER rhLF P02788 The third putative glycosylation site, at Asn624, is unglycosylated in both hLF and rhLF. 20943674 9 68 gly unglycosylated 1472:1485 arg1 hLF hLF PUBTATOR hLF 3131 The third putative glycosylation site, at Asn624, is unglycosylated in both hLF and rhLF. 20943674 6 91 gly rhLF 996:999 arg1 N-glycans rhLF N-glycans OGER rhLF P02788 However, N-glycans from rhLF are of the high mannose-, hybrid- and complex-type structures, with less N-acetylneuraminic acid and fucose. 20943674 2 96 gly N-glycosylation 369:383 arg1 rhLF rhLF OGER rhLF P02788 Here we determined the site-specific N-glycosylation profile of human lactoferrin (hLF) and recombinant human lactoferrin (rhLF) expressed in the milk of transgenic cloned cattle. 20943674 2 96 gly N-glycosylation 369:383 arg1 recombinant human lactoferrin recombinant human lactoferrin OGER lactoferrin P02788 Here we determined the site-specific N-glycosylation profile of human lactoferrin (hLF) and recombinant human lactoferrin (rhLF) expressed in the milk of transgenic cloned cattle. 20943674 2 96 gly N-glycosylation 369:383 arg1 hLF hLF PUBTATOR hLF 3131 Here we determined the site-specific N-glycosylation profile of human lactoferrin (hLF) and recombinant human lactoferrin (rhLF) expressed in the milk of transgenic cloned cattle. 20943674 2 96 gly N-glycosylation 369:383 arg1 human lactoferrin human lactoferrin OGER lactoferrin P02788 Here we determined the site-specific N-glycosylation profile of human lactoferrin (hLF) and recombinant human lactoferrin (rhLF) expressed in the milk of transgenic cloned cattle. 20943674 4 100 gly hLF 761:763 arg1 N-glycans hLF N-glycans PUBTATOR hLF 3131 N-glycans from hLF are comprised entirely of highly branched, highly sialylated and highly fucosylated complex-type structures, and many contain Lewis(x) epitopes. 26336134 2 12 gly glycoprotein 304:315 arg1 HRG HRG PUBTATOR HRG 3273 Significantly downregulated histidine-rich glycoprotein (HRG) during the dynamic stages (WB, WB7, and WB11) of neoplastic transformation of WB F344 hepatic oval-like cells was screened out by iTRAQ labeling followed by 2DLC-ESI-MS/MS analysis. 26336134 7 46 gly glycosylation 1007:1019 arg1 HRG HRG PUBTATOR HRG 3273 The glycosylation of HRG may play a key competitive role in the interaction between HRG and heparin sulfate for binding bFGF and activating the FGF receptor. 26873173 6 10 gly Hp 907:908 arg1 glycan Hp glycan Cterm Hp 3240 In this mini review, we provided a brief overview of Hp structure and biological function, discussed its glycosylation alterations in different cancers, and described the existing technologies for analyzing glycosylation site and glycan of Hp. 26873173 6 35 gly glycosylation 874:886 arg1 Hp Hp Cterm Hp 3240 In this mini review, we provided a brief overview of Hp structure and biological function, discussed its glycosylation alterations in different cancers, and described the existing technologies for analyzing glycosylation site and glycan of Hp. 26873173 0 39 gly N-glycosylation 12:26 arg1 human haptoglobin human haptoglobin PUBTATOR haptoglobin 3240 Insights on N-glycosylation of human haptoglobin and its association with cancers. 23958596 1 50 gly N-glycosylation 136:150 arg1 LPLA2 LPLA2 PUBTATOR LPLA2 23659 To understand the role of N-glycosylation of lysosomal phospholipase A2 (LPLA2), four potential N-glycosylation sites in human LPLA2 (hLPLA2) were individually modified replacing asparagine (Asn) with alanine by site-direct mutagenesis. 23958596 1 50 gly N-glycosylation 136:150 arg1 lysosomal phospholipase A2 lysosomal phospholipase A2 PUBTATOR lysosomal phospholipase A2 23659 To understand the role of N-glycosylation of lysosomal phospholipase A2 (LPLA2), four potential N-glycosylation sites in human LPLA2 (hLPLA2) were individually modified replacing asparagine (Asn) with alanine by site-direct mutagenesis. 23958596 0 52 gly N-glycosylation 8:22 arg1 human lysosomal phospholipase A2 human lysosomal phospholipase A2 PUBTATOR lysosomal phospholipase A2 23659 Role of N-glycosylation of human lysosomal phospholipase A2 for the formation of catalytically active enzyme. 23958596 10 70 gly N-glycosylation 1429:1443 arg1 LPLA2 LPLA2 PUBTATOR LPLA2 23659 These data indicate that the 99-Asn is the most critical N-glycosylation site for formation of native hLPLA2 in vivo and that the N-glycosylation of LPLA2 is crucial for biosynthesis of catalytically active hLPLA2. 20622017 0 46 gly glycosylation 26:38 arg1 renal and hepatic γ-glutamyl transpeptidase renal and hepatic γ-glutamyl transpeptidase PUBTATOR -glutamyl transpeptidase 102724197 Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue. 20622017 4 62 gly released 711:718 arg2 isolated GGT AND glycans isolated GGT glycans OGER GGT Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT. 20622017 3 72 gly released 370:377 arg2 kidney GGT AND N-glycans kidney GGT N-glycans OGER GGT The spectrum of N-glycans released from kidney GGT constituted a subset of the N-glycans identified from renal membrane glycoproteins. 26656560 9 25 gly N-glycosylation 1163:1177 arg1 TF TF Cterm TF 7018 p.N432S is a novel mutation that abolishes one N-glycosylation site of TF, while p.P589S is the polymorphism that defines the C2 isoform of TF. 27612916 7 87 gly glycan 1311:1316 arg1 the UGT2B7 enzyme UGT2B7 enzyme glycan PUBTATOR UGT2B7 enzyme 7364 The presence of an additional N-linked glycan on the UGT2B7 enzyme, likely affecting proper protein folding, resulted in a significant decrease of 49% and 40% in the formation of zidovudine and mycophenolic acid glucuronides, respectively. 27612916 6 111 gly N-glycosylation 1165:1179 arg1 endogenously produced UGT2B7 endogenously produced UGT2B7 PUBTATOR UGT2B7 7364 This amino acid change was predicted to create a putative N-glycosylation motif NX(S/T) subsequently validated upon endoglycosidase H treatment of microsomal fractions and inhibition of N-glycosylation of endogenously produced UGT2B7 with tunicamycin in human embryonic kidney (HEK293) cells. 26018173 1 8 gly glycoprotein 184:195 arg1 The human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein The human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein PUBTATOR HIV-1) envelope glycoprotein 155971 The human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer, which consists of the gp120 and gp41 subunits, is the focus of multiple strategies for vaccine development. 26018173 1 8 gly glycoprotein 184:195 arg1 Env Env PUBTATOR Env 155971 The human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer, which consists of the gp120 and gp41 subunits, is the focus of multiple strategies for vaccine development. 26018173 9 9 gly glycosylation 1730:1742 arg1 membrane-associated Env membrane-associated Env PUBTATOR Env 100616444 Additionally, we report a newly observed O-linked glycosylation site, T606, and we show that the full O-linked glycosylation profile of membrane-associated Env is similar to that of soluble gp140. 26018173 14 125 gly glycoprotein 2670:2681 arg1 the envelope glycoprotein the envelope glycoprotein PUBTATOR envelope glycoprotein 100616444 This pattern was very different from the carbohydrate profile seen for a more easily produced soluble version of the envelope glycoprotein. 26018173 8 126 gly interactions 1583:1594 arg1 native Env trimers Env trimers interactions PUBTATOR Env trimers 100616444 These site-level studies are important for understanding antibody-glycan interactions on native Env trimers. 26482295 7 60 gly glycosylate 1332:1342 arg1 human immunoglobulin G human immunoglobulin G Cterm human immunoglobulin G One notable example is D. gigas PglB, which was the only bacterial OST to glycosylate the Fc domain of human immunoglobulin G at its native 'QYNST' sequon. 23562646 13 60 gly N-glycosylation 2239:2253 arg1 hPIV-3 HN hPIV-3 HN Cterm hPIV-3 HN Taken together, these results indicated that N-glycosylation of hPIV-3 HN is critical to its receptor recognition activity, cleavage of the F protein, and fusion promotion activity, but had no influence on its interaction with the homologous F protein and NA activity. 26957414 9 64 gly glycoproteins 1166:1178 arg1 porcine thyroglobulin porcine thyroglobulin OGER thyroglobulin P01266 ISF was employed to study the glycosylation sites of three model glycoproteins, including fetuin, α1-acid glycoprotein and porcine thyroglobulin. 26957414 9 112 gly glycosylation 1131:1143 arg1 porcine thyroglobulin porcine thyroglobulin OGER thyroglobulin P01266 ISF was employed to study the glycosylation sites of three model glycoproteins, including fetuin, α1-acid glycoprotein and porcine thyroglobulin. 28327546 7 60 gly glycosylation 890:902 arg1 wild-type FVIII wild-type FVIII PUBTATOR FVIII 2157 Selected mutations also lead to partial glycosylation of N582, suggesting that rapid folding of local conformation prevents glycosylation of this site in wild-type FVIII. 28327546 3 81 gly N-glycosylation 340:354 arg1 FVIII FVIII PUBTATOR FVIII 2157 Here we characterize how hemophilia mutations near the unused N-glycosylation site of the A2 domain (N582) of FVIII affect protein conformation and intracellular trafficking. 28327546 3 82 part_of FVIII 388:392 arg1 N582 FVIII N582 PUBTATOR SpecificSite FVIII 2157 N582 Here we characterize how hemophilia mutations near the unused N-glycosylation site of the A2 domain (N582) of FVIII affect protein conformation and intracellular trafficking. 27377235 5 12 gly Glycosylation 887:899 arg1 Kv1.2 Kv1.2 Cterm Kv1.2 Glycosylation of Kv1.2 is important with respect to facilitating trafficking to the cell membrane and enhancing the stability of channels that have reached the cell membrane. 27377235 0 43 gly glycosylation 9:21 arg1 Kv1.2 voltage-gated potassium channel Kv1.2 voltage-gated potassium channel OGER voltage-gated potassium channel N-linked glycosylation of Kv1.2 voltage-gated potassium channel facilitates cell surface expression and enhances the stability of internalized channels. 27377235 2 93 gly glycosylation 463:475 arg1 Kv1.2 Kv1.2 Cterm Kv1.2 COS-7 cells expressing Kv1.2 show a crucial role of this N-linked glycosylation in the forward trafficking of Kv1.2 to the cell membrane. 25690651 7 35 gly N-glycosylated 1032:1045 arg1 hGPR109A/C19T hGPR109A/C19T PUBTATOR hGPR109A 338442 This modification is required for the normal surface expression of hGPR109A, as evidenced by the reduced surface expression of the nonglycosylated mutants, hGPR109A/N17A, and the finding that hGPR109A/C19S and hGPR109A/C19T, which are N-glycosylated at Asn(17), exhibited expression similar to the wild-type receptor. 25690651 7 35 gly N-glycosylated 1032:1045 arg1 hGPR109A/C19S hGPR109A/C19S PUBTATOR hGPR109A 338442 This modification is required for the normal surface expression of hGPR109A, as evidenced by the reduced surface expression of the nonglycosylated mutants, hGPR109A/N17A, and the finding that hGPR109A/C19S and hGPR109A/C19T, which are N-glycosylated at Asn(17), exhibited expression similar to the wild-type receptor. 21526855 5 15 gly O-glycopeptides 944:958 arg1 recombinant MUC1 recombinant MUC1 PUBTATOR MUC1 281333 The feasibility of ISD-MALDI-MS in the localization of O-glycosylation sites was demonstrated with synthetic O-glycopeptides, the tandem repeat domain of recombinant MUC1, and the natural bovine glycoproteins asialofetuin and desialylated κ-casein. 21526855 5 32 gly MUC1 1001:1004 arg1 the tandem repeat domain MUC1 the tandem repeat domain PUBTATOR MUC1 281333 The feasibility of ISD-MALDI-MS in the localization of O-glycosylation sites was demonstrated with synthetic O-glycopeptides, the tandem repeat domain of recombinant MUC1, and the natural bovine glycoproteins asialofetuin and desialylated κ-casein. 21526855 5 33 gly glycoproteins 1030:1042 arg1 asialofetuin asialofetuin PUBTATOR asialofetuin 280988 The feasibility of ISD-MALDI-MS in the localization of O-glycosylation sites was demonstrated with synthetic O-glycopeptides, the tandem repeat domain of recombinant MUC1, and the natural bovine glycoproteins asialofetuin and desialylated κ-casein. 27480168 2 9 gly glycosylated 387:398 arg1 hENT1 hENT1 OGER hENT1 Q99808 Previous work, and in silico prediction, suggest that hENT1 is glycosylated at Asn(48) in the first extracellular loop of the protein and that glycosylation plays a role in correct localization and function of hENT1. 27480168 9 23 gly glycosylation 1664:1676 arg1 hENT1 hENT1 OGER hENT1 Q99808 Based on these data we propose that glycosylation at N48 is critical for the localization, function and oligomerization of hENT1. 27480168 0 51 gly glycosylation 9:21 arg1 equilibrative nucleoside transporter 1 equilibrative nucleoside transporter 1 PUBTATOR equilibrative nucleoside transporter 1 2030 N-linked glycosylation of N48 is required for equilibrative nucleoside transporter 1 (ENT1) function. 27480168 0 51 gly glycosylation 9:21 arg1 ENT1 ENT1 PUBTATOR ENT1 2030 N-linked glycosylation of N48 is required for equilibrative nucleoside transporter 1 (ENT1) function. 21647803 8 21 gly glycans 1476:1482 arg1 bovine lactoferrin lactoferrin glycans PUBTATOR lactoferrin 280846 Our analysis identified at least 13 distinct glycans (including isomers) corresponding to five compositions at the single N-glycosylation site on bovine ribonuclease B, 59 distinct glycans at five N-glycosylation sites on bovine lactoferrin, 13 distinct glycans at one N-glycosylation site on four subclasses of human immunoglobulin G, and 20 distinct glycans at five O-glycosylation sites on bovine κ-casein. 21647803 8 50 gly glycans 1378:1384 arg1 bovine lactoferrin lactoferrin glycans PUBTATOR lactoferrin 280846 Our analysis identified at least 13 distinct glycans (including isomers) corresponding to five compositions at the single N-glycosylation site on bovine ribonuclease B, 59 distinct glycans at five N-glycosylation sites on bovine lactoferrin, 13 distinct glycans at one N-glycosylation site on four subclasses of human immunoglobulin G, and 20 distinct glycans at five O-glycosylation sites on bovine κ-casein. 21647803 8 87 gly glycans 1305:1311 arg1 bovine lactoferrin lactoferrin glycans PUBTATOR lactoferrin 280846 Our analysis identified at least 13 distinct glycans (including isomers) corresponding to five compositions at the single N-glycosylation site on bovine ribonuclease B, 59 distinct glycans at five N-glycosylation sites on bovine lactoferrin, 13 distinct glycans at one N-glycosylation site on four subclasses of human immunoglobulin G, and 20 distinct glycans at five O-glycosylation sites on bovine κ-casein. 21647803 8 88 gly glycans 1169:1175 arg1 bovine lactoferrin lactoferrin glycans PUBTATOR lactoferrin 280846 Our analysis identified at least 13 distinct glycans (including isomers) corresponding to five compositions at the single N-glycosylation site on bovine ribonuclease B, 59 distinct glycans at five N-glycosylation sites on bovine lactoferrin, 13 distinct glycans at one N-glycosylation site on four subclasses of human immunoglobulin G, and 20 distinct glycans at five O-glycosylation sites on bovine κ-casein. 26013384 0 10 part_of Ser126 59:64 arg1 Human Recombinant Erythropoietin Erythropoietin Ser126 PUBTATOR AminoAcid Erythropoietin 2056 Ser126 Structural Identification of a Non-Glycosylated Variant at Ser126 for O-Glycosylation Site from EPO BRP, Human Recombinant Erythropoietin by LC/MS Analysis. 26013384 8 12 gly O-glycosylated 997:1010 arg1 fully O-glycosylated rHu-EPO fully O-glycosylated rHu-EPO PUBTATOR EPO 2056 It is concluded that the variant peak is non-O-glycosylated rHu-EPO and the main peak is fully O-glycosylated rHu-EPO at Ser126. 26013384 8 43 gly non-O-glycosylated 943:960 arg1 non-O-glycosylated rHu-EPO non-O-glycosylated rHu-EPO PUBTATOR EPO 2056 It is concluded that the variant peak is non-O-glycosylated rHu-EPO and the main peak is fully O-glycosylated rHu-EPO at Ser126. 26013384 8 53 part_of Ser126 1023:1028 arg1 non-O-glycosylated rHu-EPO EPO Ser126 PUBTATOR AminoAcid EPO 2056 Ser126 It is concluded that the variant peak is non-O-glycosylated rHu-EPO and the main peak is fully O-glycosylated rHu-EPO at Ser126. 26013384 8 53 part_of Ser126 1023:1028 arg1 fully O-glycosylated rHu-EPO EPO Ser126 PUBTATOR AminoAcid EPO 2056 Ser126 It is concluded that the variant peak is non-O-glycosylated rHu-EPO and the main peak is fully O-glycosylated rHu-EPO at Ser126. 22750213 5 14 gly glycosylation 837:849 arg1 PRiMA PRiMA PUBTATOR PRiMA 170952 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 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 4 34 gly glycoprotein 682:693 arg1 PRiMA PRiMA PUBTATOR PRiMA 170952 PRiMA is a glycoprotein containing two putative N-linked glycosylation sites. 22750213 3 41 gly glycosylation 492:504 arg1 T T Cterm T 11423 The glycosylation of AChE(T) is known to be required for its proper assembly and trafficking; however, the role of PRiMA glycosylation in the oligomer assembly has not been revealed. 22750213 3 41 gly glycosylation 492:504 arg1 AChE AChE PUBTATOR AChE 11423 The glycosylation of AChE(T) is known to be required for its proper assembly and trafficking; however, the role of PRiMA glycosylation in the oligomer assembly has not been revealed. 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. 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. 21053369 4 75 gly glycosylation 419:431 arg1 rhIL-23r rhIL-23r OGER rhIL-23r Q5VWK5 In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides. 21053369 4 75 gly glycosylation 419:431 arg1 soluble recombinant human IL-23r soluble recombinant human IL-23r PUBTATOR IL-23r 149233 In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides. 29966421 3 28 gly glycoprotein 484:495 arg1 Bovine fetuin Bovine fetuin PUBTATOR Bovine fetuin 397585 Bovine fetuin, which harbors 3 N-glycosylation sites and a suggested half dozen O-glycosylation sites, has been used often as a model glycoprotein to test novel analytical workflows in glycoproteomics. 29966421 1 55 gly glycoprotein 168:179 arg1 alpha-2-Heremans Schmid glycoprotein alpha-2-Heremans Schmid glycoprotein PUBTATOR alpha-2-Heremans Schmid glycoprotein 197 Fetuin, also known as alpha-2-Heremans Schmid glycoprotein (AHSG), belongs to some of the most abundant glycoproteins secreted into the bloodstream. 29966421 1 55 gly glycoprotein 168:179 arg1 AHSG AHSG PUBTATOR AHSG 197 Fetuin, also known as alpha-2-Heremans Schmid glycoprotein (AHSG), belongs to some of the most abundant glycoproteins secreted into the bloodstream. 26029999 9 40 gly glycosylated 1396:1407 arg1 glycosylated CD133 glycosylated CD133 PUBTATOR CD133 8842 These data could potentially shed light on molecular regulation of CD133 by glycosylation and enhance our understanding of the utility of glycosylated CD133 as a target for cancer therapies. 26029999 4 46 gly N-glycosylation 699:713 arg1 CD133 CD133 PUBTATOR CD133 8842 Here we analyzed the exact site(s) of N-glycosylation in CD133 by mass spectrometry and found that all eight potential N-glycosylation sites of CD133 could be indeed occupied by N-glycans. 23829323 7 49 gly glycoprotein 1317:1328 arg1 haptoglobin haptoglobin PUBTATOR haptoglobin 3240 We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance. 23829323 0 63 gly microheterogeneity 40:57 arg1 haptoglobin haptoglobin PUBTATOR haptoglobin 3240 Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search. 23829323 0 104 gly N-glycosylation 24:38 arg1 haptoglobin haptoglobin PUBTATOR haptoglobin 3240 Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search. 27127844 12 35 gly unglycosylated 1559:1572 arg1 unglycosylated a4 unglycosylated a4 Cterm a4 Immunofluorescence colocalization data showed that unglycosylated a4 was mostly retained in the ER, and that plasma membrane trafficking was defective. 27127844 11 74 gly Unglycosylated 1392:1405 arg1 Unglycosylated a4 Unglycosylated a4 Cterm Unglycosylated a4 Unglycosylated a4 was degraded mostly in the proteasomal pathway, but also, in part, through the lysosomal pathway. 27127844 5 75 gly N-glycosylated 591:604 arg1 ATP6V0A4 ATP6V0A4 PUBTATOR ATP6V0A4 50617 Here we ask if human a4 (ATP6V0A4) is N-glycosylated at the predicted site, Asn489. 27127844 5 75 gly N-glycosylated 591:604 arg1 human a4 human a4 Cterm a4 Here we ask if human a4 (ATP6V0A4) is N-glycosylated at the predicted site, Asn489. 27471271 9 58 gly glycosylation 1259:1271 arg1 CEACAM1-IgV dimerization CEACAM1-IgV dimerization OGER CEACAM1 P13688 Here, we use NMR cross-correlation measurements to examine the effect of glycosylation on CEACAM1-IgV dimerization and use residual dipolar coupling (RDC) measurements to characterize the solution structure of the non-glycosylated form. 28661444 2 15 gly glycosylation 586:598 arg1 two recombinant MTB proteins two recombinant MTB proteins Cterm MTB In this work, we investigated the effect of the chemical glycosylation on two recombinant MTB proteins produced in E. coli with an additional seven-amino acid tag (recombinant Ag85B and TB10.4). 30208353 7 23 gly O-glycosylation 1206:1220 arg1 ER-α ER-α PUBTATOR ER-α 2099 We confirmed GALNT6-dependent ER-α O-glycosylation and identified O-glycosylation of S573 in an F domain of ER-α by GALNT6 through LC-MS/MS analysis. 30208353 3 74 gly O-glycosylation 555:569 arg1 ER-α ER-α PUBTATOR ER-α) 2099 Here we further report O-glycosylation of estrogen receptor alpha (ER-α) by GALNT6 and the significant role of its nuclear localization in breast cancer cells. 30208353 8 87 gly glycosylation 1334:1346 arg1 ER-α ER-α PUBTATOR ER-α 2099 We also obtained evidences showing that the glycosylation of ER-α at S573 by GALNT6 is essential for protein stability and nuclear localization of ER-α in breast cancer cells. 30208353 8 87 gly glycosylation 1334:1346 arg1 ER-α ER-α PUBTATOR ER-α 2099 We also obtained evidences showing that the glycosylation of ER-α at S573 by GALNT6 is essential for protein stability and nuclear localization of ER-α in breast cancer cells. 24872415 5 2 gly N-glycosylation 720:734 arg1 the NKG2D ligand MICA itself the NKG2D ligand MICA itself PUBTATOR MICA 100507436 Here we investigated whether direct N-glycosylation of the NKG2D ligand MICA itself is critical for cell surface expression and sought to identify the essential residues. 24468271 6 2 gly glycosylated 855:866 arg1 hIL4 hIL4 PUBTATOR form of hIL4 3565 The glycosylated form of hIL4 unexpectedly has lower biological activity and lower stability when compared to its non-glycosylated form. 24468271 6 2 gly glycosylated 855:866 arg1 The glycosylated form The glycosylated form PUBTATOR form of hIL4 3565 The glycosylated form of hIL4 unexpectedly has lower biological activity and lower stability when compared to its non-glycosylated form. 24468271 1 9 gly N-glycosylated 167:180 arg1 Secretory human interleukin 4 Secretory human interleukin 4 PUBTATOR interleukin 4 3565 Secretory human interleukin 4 (hIL4) is an N-glycosylated pleiotropic cytokine. 23891555 13 58 gly IgA1 1882:1885 arg1 the O-glycan composition IgA1 the O-glycan composition OGER IgA1 P01876 Thus identification of the O-glycan composition of IgA1 is important for a deeper understanding of the disease mechanism, biomarker discovery and validation, and implementation and monitoring of disease-specific therapies. 23891555 21 94 gly O-glycopeptides 3372:3386 arg1 IgA1 IgA1 OGER IgA1 P01876 The novelty and biological significance reside in the demonstration, for the first time, of the distribution of the most abundant isoforms of HR O-glycopeptides of IgA1. 22677411 13 88 gly glycoprotein 1819:1830 arg1 haptoglobin haptoglobin PUBTATOR haptoglobin 3240 Specific examples of site-specific glycosylation patterns of alpha-1-acid glycoprotein, haptoglobin and on a therapeutic monoclonal antibody, Infliximab are also discussed. 22677411 13 93 gly glycosylation 1780:1792 arg1 haptoglobin haptoglobin PUBTATOR haptoglobin 3240 Specific examples of site-specific glycosylation patterns of alpha-1-acid glycoprotein, haptoglobin and on a therapeutic monoclonal antibody, Infliximab are also discussed. 24334224 0 37 gly glycosylation 9:21 arg1 recombinant human granulocyte colony-stimulating factor recombinant human granulocyte colony-stimulating factor PUBTATOR granulocyte colony-stimulating factor 1440 O-linked glycosylation analysis of recombinant human granulocyte colony-stimulating factor produced in glycoengineered Pichia pastoris by liquid chromatography and mass spectrometry. 24334224 4 49 part_of found 917:921 arg2 endogenous human G-CSF AND Thr134 endogenous human G-CSF Thr134 PUBTATOR AminoAcid G-CSF 1440 Thr134 Our results demonstrated that Thr134, the equivalent O-linked glycosylation site found on endogenous human G-CSF, is the only site modified with a single mannose, allowing glycoengineered P. pastoris to be used as a viable production platform for therapeutic rhG-CSF. 24334224 2 54 gly glycosylation 489:501 arg1 rhG-CSF rhG-CSF OGER CSF Using liquid chromatography and tandem mass spectrometry techniques, we analyzed the O-linked glycosylation of recombinant human granulocyte colony-stimulating factor (rhG-CSF) derived from glycoengineered Pichia pastoris with regard to its nature, structure, occupancy, and location. 24334224 2 54 gly glycosylation 489:501 arg1 recombinant human granulocyte colony-stimulating factor recombinant human granulocyte colony-stimulating factor PUBTATOR granulocyte colony-stimulating factor 1440 Using liquid chromatography and tandem mass spectrometry techniques, we analyzed the O-linked glycosylation of recombinant human granulocyte colony-stimulating factor (rhG-CSF) derived from glycoengineered Pichia pastoris with regard to its nature, structure, occupancy, and location. 27796794 7 41 gly glycosylation 1126:1138 arg1 IgE IgE OGER IgE P01854 However, recent data demonstrate that glycosylation of IgE at the asparagine-394 site of Cε3 is necessary for IgE interaction with the high affinity IgE receptor but, surprisingly, glycosylation has no effect on IgE interaction with its low-affinity lectin receptor, CD23. 27796794 9 88 gly glycosylation 1516:1528 arg1 IgG IgG Cterm IgG Significantly more is known about the functional effects of glycosylation of IgG than for other Ig isotypes. 29268168 2 0 gly afucosylated 383:394 arg1 the afucosylated IgG the afucosylated IgG Cterm IgG Particularly, afucosylation increases the binding affinity of human IgG1 to human FcγRIIIa up to ∼20 fold, and additional galactosylation of the afucosylated IgG increases the affinity up to ∼40 fold. 29268168 5 10 gly N162-glycan 777:787 arg1 mFcγRIV FcγRIV N162-glycan PUBTATOR FcγRIV 246256 The N162-glycan in mFcγRIV was also responsible for enhancing the binding to mouse IgG with reduced fucose similar to hFcγRIIIa. 29268168 3 15 gly afucosylated 468:479 arg1 afucosylated IgG afucosylated IgG Cterm IgG The increase in affinity for afucosylated IgG has previously been shown to depend on direct carbohydrate-carbohydrate interactions between the IgG-Fc glycan with an N-linked glycan at position 162 unique to hFcγRIIIa and hFcγRIIIb. 29268168 1 40 part_of position 199:206 arg1 IgG IgG position Cterm SpecificSite IgG position N297 The binding strength between IgG and FcγR is influenced by the composition of the N-linked glycan at position N297 in the Fc-domain of IgG. 29268168 6 43 gly IgG 965:967 arg1 increased galactose IgG increased galactose Cterm IgG However, unlike hFcγRIIIa, mFcγRIV did not bind more avidly to IgG with increased galactose and reduced fucose. 29268168 6 43 gly IgG 965:967 arg1 reduced fucose IgG reduced fucose Cterm IgG However, unlike hFcγRIIIa, mFcγRIV did not bind more avidly to IgG with increased galactose and reduced fucose. 29268168 0 47 gly fucosylated 45:55 arg1 fucosylated and afucosylated IgG fucosylated and afucosylated IgG Cterm IgG Conserved FcγR- glycan discriminates between fucosylated and afucosylated IgG in humans and mice. 29268168 0 53 gly afucosylated 61:72 arg1 fucosylated and afucosylated IgG fucosylated and afucosylated IgG Cterm IgG Conserved FcγR- glycan discriminates between fucosylated and afucosylated IgG in humans and mice. 25751231 1 77 gly modified 176:183 arg3 HIV-1 gp120/gp41 AND n-linked carbohydrates HIV-1 gp120/gp41 n-linked carbohydrates PUBTATOR HIV-1 gp120 3700 BACKGROUND: HIV-1 gp120/gp41 is heavily modified by n-linked carbohydrates that play important roles either in correct folding or in shielding vulnerable viral protein surfaces from antibody recognition. 20826563 9 4 gly desialylated 1210:1221 arg1 desialylated 3N-GH desialylated 3N-GH Cterm GH The terminal half-life of 3N-GH after iv injection was 24-fold prolonged compared with wild-type GH for the pool with the most pronounced sialylation, 13-fold prolonged for the less sialylated pool, and similar to the wild-type for desialylated 3N-GH. 20826563 13 17 gly glycosylated 1647:1658 arg1 glycosylated GH glycosylated GH Cterm GH Sialic acids seem to play a pivotal role for the properties of glycosylated GH. 27161092 6 26 gly O-glycosylation 987:1001 arg1 Muc5ac Muc5ac PUBTATOR Muc5ac P98088 Our results demonstrated that the FUT2 determines the O-glycosylation pattern of Muc5ac, with Fut2 knock-out leading to a marked decrease in α1,2-fucosylated structures and increased expression of the terminal type 1 glycan structure Lewis-a. 27161092 5 78 gly O-glycosylation 786:800 arg1 Muc5ac Muc5ac PUBTATOR Muc5ac P98088 In this study we unraveled the O-glycosylation profile of Muc5ac from glycoengineered mice models lacking the FUT2 enzyme and therefore mimicking a non-secretor human phenotype. 23339644 3 36 gly glycoprotein 616:627 arg1 gp120 gp120 PUBTATOR gp120 155971 As part of our continuing effort in the analysis of glycosylation profiles of recombinant HIV-1 envelope-based immunogens, we evaluated and compared the host-cell specific glycosylation pattern of recombinant HIV-1 surface glycoprotein, gp120, derived from clade C transmitted/founder virus 1086.C expressed in Chinese hamster ovary (CHO) and human embryonic kidney containing T antigen (293T) cell lines. 23339644 3 50 gly glycosylation 565:577 arg1 gp120 gp120 PUBTATOR gp120 155971 As part of our continuing effort in the analysis of glycosylation profiles of recombinant HIV-1 envelope-based immunogens, we evaluated and compared the host-cell specific glycosylation pattern of recombinant HIV-1 surface glycoprotein, gp120, derived from clade C transmitted/founder virus 1086.C expressed in Chinese hamster ovary (CHO) and human embryonic kidney containing T antigen (293T) cell lines. 23339644 9 96 gly occupancy 1952:1960 arg1 the CHO and 293T cell-derived 1086.C gp120 the CHO and 293T cell-derived 1086.C gp120 PUBTATOR gp120 3700 Overall, glycosylation site occupancy of the CHO and 293T cell-derived 1086.C gp120 showed a high degree of similarity except for one site at N88 in the C1 region. 23339644 7 138 gly glycans 1543:1549 arg1 the CHO cell-derived 1086.C gp120 gp120 glycans PUBTATOR gp120 3700 For N-linked glycosylation, two sites (N386 and N392) in the V4 region were populated with high mannose glycans in the CHO cell-derived 1086.C gp120, while these sites had a mixture of high mannose and processed glycans in the 293T cell-derived 1086.C gp120. 23339644 7 154 gly glycans 1651:1657 arg1 the 293T cell-derived 1086.C gp120 gp120 glycans PUBTATOR gp120 3700 For N-linked glycosylation, two sites (N386 and N392) in the V4 region were populated with high mannose glycans in the CHO cell-derived 1086.C gp120, while these sites had a mixture of high mannose and processed glycans in the 293T cell-derived 1086.C gp120. 25498018 2 59 gly glycosylation 508:520 arg1 CLEC-2 CLEC-2 OGER CLEC-2 Q9P126 The two forms appear to have different ligand-binding abilities, indicating that the differential glycosylation of CLEC-2 possibly produces functionally distinct glycoforms. 23069765 2 34 gly N-glycosylated 394:407 arg1 human recombinant IL-17A human recombinant IL-17A PUBTATOR IL-17A 3605 Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag. 23069765 0 41 gly N-glycosylation 56:70 arg1 human recombinant interleukin-17A human recombinant interleukin-17A PUBTATOR interleukin-17A 3605 Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line. 23069765 1 53 gly glycosylated 222:233 arg1 The T helper cell-derived cytokine interleukin-17A The T helper cell-derived cytokine interleukin-17A PUBTATOR interleukin-17A 3605 The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa. 23069765 0 87 gly O-glycosylation 22:36 arg1 human recombinant interleukin-17A human recombinant interleukin-17A PUBTATOR interleukin-17A 3605 Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line. 23001782 5 6 gly N-glycosylated 880:893 arg1 serum-derived hSHBG serum-derived hSHBG PUBTATOR hSHBG 6462 It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively. 23001782 4 28 gly glycans 814:820 arg1 intact hSHBG hSHBG glycans PUBTATOR hSHBG 6462 MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG. 23001782 3 36 gly glycosylation 495:507 arg1 serum-derived hSHBG serum-derived hSHBG PUBTATOR hSHBG 6462 Here, we perform a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG. 23001782 1 72 gly glycoprotein 195:206 arg1 Human sex hormone binding globulin Human sex hormone binding globulin PUBTATOR Human sex hormone binding globulin 6462 Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues. 23001782 4 91 gly hSHBG 832:836 arg1 detailed glycan structures hSHBG detailed glycan structures PUBTATOR hSHBG 6462 MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG. 23001782 4 91 gly hSHBG 832:836 arg1 glycans hSHBG glycans PUBTATOR hSHBG 6462 MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG. 23001782 4 91 gly hSHBG 832:836 arg1 monosaccharide compositions hSHBG monosaccharide compositions PUBTATOR hSHBG 6462 MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG. 23001782 4 117 gly structures 766:775 arg1 intact hSHBG hSHBG structures PUBTATOR hSHBG 6462 MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG. 23001782 4 124 gly compositions 736:747 arg1 intact hSHBG hSHBG compositions PUBTATOR hSHBG 6462 MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG. 30115684 1 29 gly glycan 124:129 arg1 the envelope glycoprotein gp120 gp120 glycan PUBTATOR gp120 155971 The glycan shield on the envelope glycoprotein gp120 of human immunodeficiency virus 1 (HIV-1) has drawn immense attention as a vulnerable site for broadly neutralizing antibodies (bNAbs) and for its significant impact on host adaptive immune response to HIV-1. 24554659 2 25 gly glycoprotein 555:566 arg1 Env Env PUBTATOR Env 1490007 Here, we identify a highly conserved N-linked glycosylation site (N173 in SIV, corresponding to N160 in HIV) in the V2 region of the SIV envelope glycoprotein (Env) as a novel determinant of macrophage tropism and characterize mechanisms underlying this phenotype. 24554659 2 25 gly glycoprotein 555:566 arg1 the SIV envelope glycoprotein the SIV envelope glycoprotein PUBTATOR SIV envelope glycoprotein 1490007 Here, we identify a highly conserved N-linked glycosylation site (N173 in SIV, corresponding to N160 in HIV) in the V2 region of the SIV envelope glycoprotein (Env) as a novel determinant of macrophage tropism and characterize mechanisms underlying this phenotype. 24554659 0 54 gly glycoprotein 94:105 arg1 the simian immunodeficiency virus envelope glycoprotein the simian immunodeficiency virus envelope glycoprotein PUBTATOR envelope glycoprotein V2 1490007 Loss of a conserved N-linked glycosylation site in the simian immunodeficiency virus envelope glycoprotein V2 region enhances macrophage tropism by increasing CD4-independent cell-to-cell transmission. 24554659 12 69 gly determinant 2060:2070 arg1 N173 N173 N173 SpecificSite N173 IMPORTANCE: In this study, we identify a genetic determinant in the viral envelope (N173) that increases replication and spreading infection of SIV strains in macrophages by enhancing cell-to-cell virus transmission. 26993603 3 7 part_of GP73 560:563 arg1 Asn398 GP73 Asn398 PUBTATOR AminoAcid GP73 51280 Asn109, Asn144 and Asn398 We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398. 26993603 3 7 part_of GP73 560:563 arg1 Asn144 GP73 Asn144 PUBTATOR AminoAcid GP73 51280 Asn109, Asn144 and Asn398 We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398. 26993603 3 7 part_of GP73 560:563 arg1 Asn109 GP73 Asn109 PUBTATOR AminoAcid GP73 51280 Asn109, Asn144 and Asn398 We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398. 26993603 0 54 part_of Asn144 24:29 arg1 GP73 N-glycosylation GP73 N-glycosylation Asn144 PUBTATOR AminoAcid GP73 N-glycosylation 51280 Asn144 GP73 N-glycosylation at Asn144 reduces hepatocellular carcinoma cell motility and invasiveness. 23820512 5 39 gly glycoproteins 861:873 arg1 bovine ribonuclease B bovine ribonuclease B Cterm bovine ribonuclease B The condition to effectively collect complex and heterogeneous N-glycans was established on model glycoproteins, bovine ribonuclease B, bovine fetuin, and human serum IgG. 23820512 5 39 gly glycoproteins 861:873 arg1 human serum IgG human serum IgG Cterm IgG The condition to effectively collect complex and heterogeneous N-glycans was established on model glycoproteins, bovine ribonuclease B, bovine fetuin, and human serum IgG. 18340083 3 14 gly N-glycosylated 505:518 arg1 mouse GPIHBP1 mouse GPIHBP1 PUBTATOR GPIHBP1 68453 Here, we show that mouse GPIHBP1 is N-glycosylated at Asn-76 within the Ly-6 domain. 18340083 5 15 gly released 619:626 arg1 mouse GPIHBP1 AND The N-linked glycan mouse GPIHBP1 The N-linked glycan PUBTATOR GPIHBP1 68453 The N-linked glycan could be released from mouse GPIHBP1 with N-glycosidase F, endoglycosidase H, or endoglycosidase F1. 18340083 6 22 gly glycan 846:851 arg1 GPIHBP1 GPIHBP1 glycan PUBTATOR GPIHBP1 68453 The glycan was marginally sensitive to endoglycosidase F2 digestion but resistant to endoglycosidase F3 digestion, suggesting that the glycan on GPIHBP1 is of the oligomannose type. 18340083 8 26 gly nonglycosylated 1126:1140 arg1 a nonglycosylated GPIHBP1 a nonglycosylated GPIHBP1 PUBTATOR GPIHBP1 68453 Consistent with this finding, cells expressing a nonglycosylated GPIHBP1 lack the ability to bind LPL or chylomicrons. 18340083 4 33 gly glycosylated 576:587 arg1 Human GPIHBP1 Human GPIHBP1 PUBTATOR Human GPIHBP1 338328 Human GPIHBP1 is also glycosylated. 18340083 10 66 gly N-glycosylation 1365:1379 arg1 GPIHBP1 GPIHBP1 PUBTATOR GPIHBP1 68453 These studies demonstrate that N-glycosylation of GPIHBP1 is important for the trafficking of GPIHBP1 to the cell surface. 18340083 10 66 gly N-glycosylation 1365:1379 arg1 GPIHBP1 GPIHBP1 PUBTATOR GPIHBP1 68453 These studies demonstrate that N-glycosylation of GPIHBP1 is important for the trafficking of GPIHBP1 to the cell surface. 19610667 1 11 gly glycosylation 87:99 arg1 gp120/gp41 gp120/gp41 PUBTATOR gp120 155971 The extensive glycosylation of HIV-1 envelope proteins (Envs), gp120/gp41, is known to play an important role in evasion of host immune response by masking key neutralization epitopes and presenting the Env glycosylation as "self" to the host immune system. 22123080 3 2 gly N-glycosylation 364:378 arg1 CD82 CD82 PUBTATOR CD82 3732 However, the N-glycosylation pattern of CD82 has not been described yet. 22123080 1 31 gly glycoprotein 108:119 arg1 KAI1 KAI1 PUBTATOR KAI1 3732 The membrane glycoprotein CD82 (KAI1) has attracted increasing attention as a suppressor of cell migration, related tumor invasion, as well as metastasis. 22123080 2 62 gly glycosylation 254:266 arg1 CD82 CD82 PUBTATOR CD82 3732 The glycosylation of CD82 has been shown to be involved in a correlative cell adhesion and motility. 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. 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). 16755913 8 39 gly non-N-glycosylation 1429:1447 arg1 the modified PrP the modified PrP OGER PrP F7VJQ1 Moreover, the modified PrP with mono- and non-N-glycosylation were able to be expressed transitantly in Hela cells, which could be a useful means for studying prions. 17823199 6 52 gly N-glycosylation 1082:1096 arg1 transferrin transferrin PUBTATOR transferrin 7018 In healthy control samples, we determined 98-100% occupancy for all N-glycosylation sites of transferrin and alpha(1)-antitrypsin. 17823199 6 52 gly N-glycosylation 1082:1096 arg1 alpha(1)-antitrypsin alpha(1)-antitrypsin PUBTATOR alpha(1)-antitrypsin 5265 In healthy control samples, we determined 98-100% occupancy for all N-glycosylation sites of transferrin and alpha(1)-antitrypsin. 21338062 0 146 gly glycosylation 49:61 arg1 affinity-purified haptoglobin affinity-purified haptoglobin PUBTATOR haptoglobin 3240 Ultrasensitive characterization of site-specific glycosylation of affinity-purified haptoglobin from lung cancer patient plasma using 10 μm i.d. porous layer open tubular liquid chromatography-linear ion trap collision-induced dissociation/electron transfer dissociation mass spectrometry. 26956484 10 22 gly glycosylation 1429:1441 arg1 Orai1 Orai1 PUBTATOR Orai1 84876 In summary, the glycosylation state of Orai1 influences SOCE-mediated Ca(2+) signaling and, thus, may contribute to pathophysiological Ca(2+) signaling observed in immune disease and cancer. 26956484 5 37 gly glycosylation 743:755 arg1 Orai1 Orai1 PUBTATOR Orai1 84876 Using Western blot analysis and lectin-binding assays from various primary human cells and cancer cell lines, we found that glycosylation of Orai1 is cell type-specific. 26956484 6 49 gly glycosylation 879:891 arg1 Orai1N223A Orai1N223A PUBTATOR Orai1N223A 84876 Ca(2+) imaging experiments and patch-clamp experiments revealed that mutation of the only glycosylation site of Orai1 (Orai1N223A) enhanced SOCE in Jurkat T cells. 26956484 6 49 gly glycosylation 879:891 arg1 Orai1 Orai1 PUBTATOR Orai1 84876 Ca(2+) imaging experiments and patch-clamp experiments revealed that mutation of the only glycosylation site of Orai1 (Orai1N223A) enhanced SOCE in Jurkat T cells. 26956484 8 68 gly Orai1 1205:1209 arg1 the N-glycan Orai1 the N-glycan PUBTATOR Orai1 84876 In human mast cells, inhibition of sialyl sulfation altered the N-glycan of Orai1 (and other proteins) and increased SOCE. 26956484 0 86 gly glycosylation 19:31 arg1 Orai1 Orai1 PUBTATOR Orai1 84876 Cell type-specific glycosylation of Orai1 modulates store-operated Ca2+ entry. 26980729 5 44 gly deglycosylation 1076:1090 arg1 fully processed GC-B fully processed GC-B PUBTATOR GC-B 4882 Tunicamycin inhibition of glycosylation in the endoplasmic reticulum or mutation of the Asn-24 glycosylation site decreased GC activity, but neither inhibition of glycosylation in the Golgi by N-acetylglucosaminyltransferase I gene inactivation nor PNGase F deglycosylation of fully processed GC-B reduced GC activity. 21431619 4 53 gly glycoforms 650:659 arg1 transferrin glycoforms transferrin glycoforms PUBTATOR transferrin 7018 In some cases, these protein variants co-migrate with transferrin glycoforms, which complicates interpretation. 24338886 2 0 gly glycosylation 308:320 arg1 rhEPO rhEPO OGER rhEPO P29676 Using mass spectrometry, we characterized the N-/O-linked glycosylation of recombinant human EPO (rhEPO) produced in glycoengineered Pichia pastoris and compared with the glycosylation of Chinese hamster ovary (CHO) cell-derived rhEPO. 24338886 2 0 gly glycosylation 308:320 arg1 recombinant human EPO recombinant human EPO PUBTATOR EPO 2056 Using mass spectrometry, we characterized the N-/O-linked glycosylation of recombinant human EPO (rhEPO) produced in glycoengineered Pichia pastoris and compared with the glycosylation of Chinese hamster ovary (CHO) cell-derived rhEPO. 24338886 2 28 gly glycosylation 421:433 arg1 Chinese hamster ovary (CHO) cell-derived rhEPO Chinese hamster ovary (CHO) cell-derived rhEPO OGER rhEPO P29676 Using mass spectrometry, we characterized the N-/O-linked glycosylation of recombinant human EPO (rhEPO) produced in glycoengineered Pichia pastoris and compared with the glycosylation of Chinese hamster ovary (CHO) cell-derived rhEPO. 24338886 4 76 gly rhEPO 891:895 arg1 the N-linked glycans Pichia-produced rhEPO the N-linked glycans OGER Pichia-produced rhEPO P29676 Additionally, the N-linked glycans from Pichia-produced rhEPO were similar across all three sites. 24338886 5 93 part_of position 1013:1020 arg1 Pichia-produced rhEPO Pichia-produced rhEPO position OGER AminoAcid Pichia-produced rhEPO P29676 position Ser126 A low level of O-linked mannosylation was detected on Pichia-produced rhEPO at position Ser126, which is also the O-linked glycosylation site for endogenous human EPO and CHO-derived rhEPO. 19808681 8 20 gly unglycosylated 1169:1182 arg1 the unglycosylated Kv12.2 channels the unglycosylated Kv12.2 channels PUBTATOR Kv12.2 channels 23416 We next examined the trafficking in CHO cells to address whether the unglycosylated Kv12.2 channels are utilized in vivo. 19808681 6 21 gly N-glycosylation 733:747 arg1 Kv12.2 Kv12.2 PUBTATOR Kv12.2 23416 As an effect of N-glycosylation on the function of Kv12.2, we demonstrate that removal of sugar chains causes a depolarizing shift in the steady-state activation without a significant reduction in current amplitude. 19808681 5 53 gly N-glycosylated 610:623 arg1 Kv12.2 Kv12.2 PUBTATOR Kv12.2 23416 We show that Kv12.2 is N-glycosylated in Chinese hamster ovary (CHO) cells and in cultured neurons as well as in the mouse brain. 19808681 11 68 gly glycosylated 1552:1563 arg1 only glycosylated Kv12.2 channels only glycosylated Kv12.2 channels PUBTATOR Kv12.2 channels 23416 Our data suggest that only glycosylated Kv12.2 channels show proper voltage dependence and are utilized in vivo. 19808681 4 79 gly N-glycosylation 560:574 arg1 Kv12.2 Kv12.2 PUBTATOR Kv12.2 23416 Because glycosylation plays important roles in the folding, trafficking, and function of various Kv channels, we focused on the N-glycosylation of Kv12.2. 15331613 1 48 gly glycosylation 496:508 arg1 NGC NGC PUBTATOR NGC 29873 NGC dramatically changed its structure from a proteoglycan to a nonproteoglycan form with cerebellar development, whereas a small portion of NGC molecules existed in a nonproteoglycan form in the other areas of the mature CNS, suggesting that the CS glycosylation of NGC is developmentally regulated in the whole CNS. 27234584 7 3 gly B/MMP-9 1265:1271 arg1 N- MMP-9 N- OGER MMP-9 P14780 Validated glycobiological data on N- and O-linked oligosaccharides of gelatinase B/MMP-9 and on O-linked structures of membrane-type 1 MMP/MMP-14 indicate that in-depth research of other MMPs may yield important insights, e.g. about subcellular localizations and functions within macromolecular complexes. 27234584 7 56 gly MMP/MMP-14 1319:1328 arg1 O-linked structures MMP-14 O-linked structures OGER MMP-14 P50281 Validated glycobiological data on N- and O-linked oligosaccharides of gelatinase B/MMP-9 and on O-linked structures of membrane-type 1 MMP/MMP-14 indicate that in-depth research of other MMPs may yield important insights, e.g. about subcellular localizations and functions within macromolecular complexes. 17011210 1 101 gly glycoprotein 252:263 arg1 Human Fas ligand Human Fas ligand PUBTATOR Human Fas ligand 356 Human Fas ligand is a medically important membrane glycoprotein that induces the apoptosis of harmful cells. 29226084 6 0 gly N-glycosylation 1199:1213 arg1 GPR61 GPR61 OGER GPR61 Q9BZJ8 These results demonstrate that GPR61 is subject to N-glycosylation but suggest this is not a prerequisite for cell surface expression, although N-glycosylation of other proteins may be important for cell membrane expression of GPR61. 19369259 4 9 gly F-deglycosylated 790:805 arg1 purified and peptide N-glycosidase F-deglycosylated CD36 purified and peptide N-glycosidase F-deglycosylated CD36 OGER CD36 P16671 Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation. 22607976 3 47 gly nonglycosylated 460:474 arg1 transthyretin transthyretin PUBTATOR transthyretin 7276 We report here the cryptic N-glycosylation site as a recognition signal for unfolding of a natively nonglycosylated protein, transthyretin (TTR), involved in familial amyloidosis. 18952059 4 21 gly glycosylation 461:473 arg1 IZUMO IZUMO PUBTATOR IZUMO 73456 The expression of N204Q-IZUMO rescued the infertile phenotype of IZUMO disrupted mice, indicating glycosylation is not essential for fusion-facilitating activity of IZUMO. 18952059 6 29 gly glycosylation 755:767 arg1 IZUMO IZUMO PUBTATOR IZUMO 73456 These data suggest that glycosylation is not essential for the function of IZUMO, but has a role in protecting it from fragmentation in cauda epididymis. 18952059 3 36 gly unglycosylated 302:315 arg1 unglycosylated IZUMO unglycosylated IZUMO PUBTATOR IZUMO 73456 In the present paper, we produced transgenic mouse lines expressing unglycosylated IZUMO (N204Q-IZUMO) in Izumo1 -/- background. 18952059 3 36 gly unglycosylated 302:315 arg1 N204Q-IZUMO N204Q-IZUMO PUBTATOR -IZUMO 73456 In the present paper, we produced transgenic mouse lines expressing unglycosylated IZUMO (N204Q-IZUMO) in Izumo1 -/- background. 15527836 3 85 gly Glycosylation 451:463 arg1 the rCAT1 and hCAT1 receptors the rCAT1 and hCAT1 receptors PUBTATOR hCAT1 receptors 6541 Glycosylation of the rCAT1 and hCAT1 receptors inhibits ecotropic MLV infection of CAT1-expressing cells, but that of the mCAT1 does not afford the cells this protection. 15527836 9 92 gly glycosylation 1459:1471 arg1 the wild-type rCAT1 the wild-type rCAT1 PUBTATOR rCAT1 25648 An amino acid substitution in the glycosylation site of the wild-type rCAT1 conferred higher infection susceptibility, but that of the rCAT1 mutant 1 did not. 28920453 4 19 gly O-glycans 623:631 arg1 rhEPOs rhEPOs O-glycans Cterm rhEPOs We developed selective and sensitive method to profile native O-glycans on rhEPOs. 28920453 1 35 gly Glycosylation 139:151 arg1 rhEPOs rhEPOs Cterm rhEPOs AIM: Glycosylation of recombinant human erythropoietins (rhEPOs) is significantly associated with drug's quality and potency. 28920453 1 35 gly Glycosylation 139:151 arg1 recombinant human erythropoietins recombinant human erythropoietins Cterm erythropoietins AIM: Glycosylation of recombinant human erythropoietins (rhEPOs) is significantly associated with drug's quality and potency. 18330979 3 57 gly glycosylation 572:584 arg1 Env Env PUBTATOR Env 100616444 Thus, characterizing glycosylation patterns of Env and native virions and correlating glycosylation profiles with infectivity and Env immunogenicity are necessary first steps in designing effective immunogens. 18330979 3 91 gly glycosylation 637:649 arg1 Env Env PUBTATOR Env 100616444 Thus, characterizing glycosylation patterns of Env and native virions and correlating glycosylation profiles with infectivity and Env immunogenicity are necessary first steps in designing effective immunogens. 18330979 7 92 gly glycosylation 1433:1445 arg1 Env Env PUBTATOR Env 155971 Thus, these techniques can be used to (1) define glycosylation profiles of recombinant Env proteins and Env on mature virions, (2) define specific carbohydrate moieties at each glycosylation site, and (3) determine the role of certain carbohydrates in HIV-1 infectivity and in modulation of Env immunogenicity. 18330979 7 92 gly glycosylation 1433:1445 arg1 recombinant Env proteins recombinant Env proteins PUBTATOR Env proteins 155971 Thus, these techniques can be used to (1) define glycosylation profiles of recombinant Env proteins and Env on mature virions, (2) define specific carbohydrate moieties at each glycosylation site, and (3) determine the role of certain carbohydrates in HIV-1 infectivity and in modulation of Env immunogenicity. 29944110 8 31 part_of HA1 1157:1159 arg1 HA1 position N158 HA1 HA1 position N158 PUBTATOR SpecificSite HA1 23526 position N158 We found that clade 3C.2a viruses, possessing an additional potential glycosylation site at HA1 position N158, were poorly recognized by some of the mAbs, but other residues, notably at position 159, also affected antibody binding. 29944110 9 61 part_of HA1 1432:1434 arg1 residue 158 HA1 residue 158 PUBTATOR SpecificSite HA1 23526 residue 158 Through a mass spectrometric (MS) analysis of HA, the glycosylated sites of HA1 were established and we determined that residue 158 of HA1 was glycosylated and so modified a neutralization-sensitive epitope. 29944110 9 65 gly glycosylated 1440:1451 arg1 HA1 HA1 PUBTATOR HA1 23526 Through a mass spectrometric (MS) analysis of HA, the glycosylated sites of HA1 were established and we determined that residue 158 of HA1 was glycosylated and so modified a neutralization-sensitive epitope. 29944110 9 70 gly glycosylated 1351:1362 arg1 HA1 HA1 PUBTATOR HA1 23526 Through a mass spectrometric (MS) analysis of HA, the glycosylated sites of HA1 were established and we determined that residue 158 of HA1 was glycosylated and so modified a neutralization-sensitive epitope. 26683050 3 9 gly glycosylation 525:537 arg1 48 paired CSF and serum samples 48 paired CSF and serum samples OGER CSF METHODS: We applied mass spectrometry of tryptic Fc glycopeptides to analyze IgG Fc glycosylation (sialylation, galactosylation, fucosylation, and bisecting N-acetylglucosamine (GlcNAc)) in 48 paired CSF and serum samples from adult patients with MS or a first demyelinating event highly suggestive of MS (designated as MS cases), and from healthy volunteers and patients with other non-inflammatory diseases (control group). 26683050 10 37 gly afucosylation 1510:1522 arg1 CSF CSF OGER CSF Third, hypothesis-free regression analysis revealed that alterations of afucosylation and bisecting GlcNAc in CSF from MS cases peaked 2-3 months after the last relapse. 26683050 10 45 gly afucosylation 1510:1522 arg1 CSF CSF afucosylation OGER CSF Third, hypothesis-free regression analysis revealed that alterations of afucosylation and bisecting GlcNAc in CSF from MS cases peaked 2-3 months after the last relapse. 26683050 2 110 gly glycosylation 376:388 arg1 CSF CSF OGER CSF Intrathecal production of IgG, especially IgG1, is a hallmark of multiple sclerosis (MS), but nothing is known about IgG Fc glycosylation in MS and in cerebrospinal fluid (CSF) in general. 26683050 10 111 gly GlcNAc 1538:1543 arg1 CSF CSF GlcNAc OGER CSF Third, hypothesis-free regression analysis revealed that alterations of afucosylation and bisecting GlcNAc in CSF from MS cases peaked 2-3 months after the last relapse. 23925152 1 18 gly glycoprotein 158:169 arg1 HIV-1 envelope glycoprotein gp120 HIV-1 envelope glycoprotein gp120 PUBTATOR envelope glycoprotein gp120 155971 The third variable region (V3) of HIV-1 envelope glycoprotein gp120 plays a key role in determination of viral coreceptor usage (tropism). 29632412 3 19 gly GlcNAc 962:967 arg1 murine IgGs IgG GlcNAc Cterm IgG By analyzing the IgG glycome composition of 95 CC strains, we made several important observations: (i) glycome variation between mouse strains was higher than between individual humans, despite all mice having the same environmental influences; (ii) five genetic loci were found to be associated with murine IgG glycosylation; (iii) variants outside traditional glycosylation site motifs affected glycome variation; (iv) bisecting N-acetylglucosamine (GlcNAc) was produced by several strains although most previous studies have reported the absence of glycans containing the bisecting GlcNAc on murine IgGs; and (v) common laboratory mouse strains are not optimal animal models for studying effects of glycosylation on IgG function. 29632412 3 35 gly glycosylation 1079:1091 arg1 IgG function IgG function Cterm IgG By analyzing the IgG glycome composition of 95 CC strains, we made several important observations: (i) glycome variation between mouse strains was higher than between individual humans, despite all mice having the same environmental influences; (ii) five genetic loci were found to be associated with murine IgG glycosylation; (iii) variants outside traditional glycosylation site motifs affected glycome variation; (iv) bisecting N-acetylglucosamine (GlcNAc) was produced by several strains although most previous studies have reported the absence of glycans containing the bisecting GlcNAc on murine IgGs; and (v) common laboratory mouse strains are not optimal animal models for studying effects of glycosylation on IgG function. 12538726 9 32 gly N-glycosylated 1350:1363 arg1 rNCC rNCC PUBTATOR rNCC 54300 Thus, we have demonstrated that rNCC is N-glycosylated in vivo at two sites, that glycosylation is essential for efficient function and surface expression of the cotransporter, and that the elimination of glycosylation allows much greater access of thiazide diuretics to their binding site. 18416605 4 3 gly glycosylation 843:855 arg1 PrP PrP OGER PrP Q9NP58 Moreover we have shown that brain material from mice infected with TSE that have only unglycosylated PrP(Sc) is capable of transmitting infection to wild-type mice, demonstrating that glycosylation of PrP is not essential for establishing infection within a host or for transmitting TSE infectivity to a new host. 18416605 2 19 gly glycosylation 459:471 arg1 PrP PrP OGER PrP Q9NP58 To address the hypothesis that glycosylation of host PrP is a major factor influencing TSE infection, we have inoculated gene-targeted transgenic mice that have restricted N-linked glycosylation of PrP with three TSE strains. 18416605 3 29 gly unglycosylated 560:573 arg1 only unglycosylated PrP only unglycosylated PrP OGER PrP Q9NP58 We have uniquely demonstrated that mice expressing only unglycosylated PrP can sustain a TSE infection, despite altered cellular location of the host PrP. 18416605 2 32 gly glycosylation 309:321 arg1 host PrP host PrP OGER PrP Q9NP58 To address the hypothesis that glycosylation of host PrP is a major factor influencing TSE infection, we have inoculated gene-targeted transgenic mice that have restricted N-linked glycosylation of PrP with three TSE strains. 18416605 5 46 gly glycosylation 1141:1153 arg1 host PrP host PrP OGER PrP Q9NP58 We have further dissected the requirement of each glycosylation site and have shown that different TSE strains have dramatically different requirements for each of the glycosylation sites of host PrP, and moreover, we have shown that the host PrP has a major role in determining the glycosylation state of de novo generated PrP(Sc). 18416605 5 58 gly glycosylation 1256:1268 arg1 Sc Sc Cterm Sc Q9NP58 We have further dissected the requirement of each glycosylation site and have shown that different TSE strains have dramatically different requirements for each of the glycosylation sites of host PrP, and moreover, we have shown that the host PrP has a major role in determining the glycosylation state of de novo generated PrP(Sc). 18416605 5 58 gly glycosylation 1256:1268 arg1 de novo generated PrP de novo generated PrP OGER PrP Q9NP58 We have further dissected the requirement of each glycosylation site and have shown that different TSE strains have dramatically different requirements for each of the glycosylation sites of host PrP, and moreover, we have shown that the host PrP has a major role in determining the glycosylation state of de novo generated PrP(Sc). 22577028 2 48 gly glycoprotein 477:488 arg1 HA HA Cterm HA 23526 HA is a surface glycoprotein of the influenza virus that plays a key role in viral infectivity and pathogenesis. 26620227 3 44 part_of proSP-B 418:424 arg1 Asn129 SP-B Asn129 OGER AminoAcid SP-B P07988 Asn129 The SNP causes an altered N-linked glycosylation modification at Asn129 of proSP-B, e.g. the C allele with this glycosylation site but not in the T allele. 21752569 2 9 gly attached 384:391 arg2 Human IgA1 AND The glycans Human IgA1 The glycans PUBTATOR Human IgA1 P01876 The glycans attached to Human IgA1 were removed from their attachment sites by an array of enzymes. 21752569 1 50 gly glycoprotein 328:339 arg1 Human IgA1 Human IgA1 PUBTATOR Human IgA1 P01876 Human IgA1 was used as a model glycoprotein to demonstrate this technique. 21752569 0 54 gly deglycosylation 63:77 arg1 Human IgA1 Human IgA1 PUBTATOR Human IgA1 P01876 Glycosylation characterization of Human IgA1 with differential deglycosylation by UPLC-ESI TOF MS. Differential deglycosylation was introduced as an effective technique to characterize glycosylation in glycoprotein containing both N-linked and O-linked glycans at both protein and peptide levels. 27938679 1 23 gly glycoproteins 283:295 arg1 TM TM Cterm TM The bovine leukaemia virus (BLV) envelope protein (Env) is synthesized as a polyprotein precursor (gp72) proteolytically cleaved into the mature surface (SU) and transmembrane (TM) glycoproteins. 30158294 6 11 part_of site 877:880 arg1 SERINC5 SERINC5 site PUBTATOR SpecificSite SERINC5 256987 site, N294 Sequence alignment of SERINC family proteins led us to identify a conserved N-glycosylation site, N294, in SERINC5. 30158294 14 21 gly glycosylated 2296:2307 arg1 SERINC5 SERINC5 PUBTATOR SERINC5 256987 Here we show that SERINC5 is a glycosylated protein and that N-glycosylation is important for its steady state expression. 30158294 16 37 gly N-glycosylation 2481:2495 arg1 SERINC5 SERINC5 PUBTATOR SERINC5 256987 Nonetheless, N-glycosylation per se is neither required for the ability of SERINC5 to inhibit HIV-1 infectivity nor for its sensitivity to antagonism by Nef. 30158294 0 50 gly N-glycosylated 3:16 arg1 An N-glycosylated form An N-glycosylated form PUBTATOR N-Glycosylated Form of SERINC5 256987 An N-glycosylated form of SERINC5 is specifically incorporated into HIV-1 virions. 30158294 0 50 gly N-glycosylated 3:16 arg1 SERINC5 SERINC5 PUBTATOR N-Glycosylated Form of SERINC5 256987 An N-glycosylated form of SERINC5 is specifically incorporated into HIV-1 virions. 30158294 5 61 gly modified 626:633 arg1 virion-associated SERINC5 AND N-linked, complex glycans virion-associated SERINC5 N-linked, complex glycans PUBTATOR SERINC5 256987 We used various glycosidases to establish that virion-associated SERINC5 is modified by N-linked, complex glycans, whereas the majority of SERINC5 in cells is of relatively low molecular weight and is modified by high-mannose glycans. 30158294 11 88 gly non-glycosylated 1726:1741 arg1 non-glycosylated SERINC5 non-glycosylated SERINC5 PUBTATOR SERINC5 256987 We conclude that although not required for restrictive-activity or Nef-sensitivity, N-linked glycosylation is important for maintaining the steady-state expression of SERINC5 and that non-glycosylated SERINC5 is likely subjected to a quality-control mechanism that induces its proteasomal degradation.IMPORTANCE SERINC5 is a member of a family of multi-pass transmembrane proteins that inhibit the infectivity of retroviruses including HIV-1. 30158294 8 95 gly N-glycosylation 1108:1122 arg1 SERINC5 SERINC5 PUBTATOR SERINC5 256987 Our results demonstrate that N294 is the major site of N-glycosylation in SERINC5. 21535396 12 1 gly Non-glycosylated 1573:1588 arg1 Non-glycosylated TF Non-glycosylated TF Cterm Non-glycosylated TF 2152 Non-glycosylated TF is also capable of supporting FVIIa cleavage of PAR2 and PAR2-dependent p44/42 MAPK activation. 21535396 11 68 gly non-glycosylated 1459:1474 arg1 A fully non-glycosylated TF A fully non-glycosylated TF Cterm TF 2152 A fully non-glycosylated TF is shown to bind FVIIa and interact with FX with the same efficiency as that of wild-type TF. 21535396 0 85 gly Glycosylation 0:12 arg1 tissue factor tissue factor PUBTATOR tissue factor 2152 Glycosylation of tissue factor is not essential for its transport or functions. 25389233 9 74 gly IgG 1438:1440 arg1 the glycan IgG the glycan Cterm IgG We studied associations of the glycan of complexed IgG and disease activity according to the physician's global assessment of disease activity and the systemic lupus erythematosus disease activity index 2000 documented at the moment of blood taking. 25389233 6 119 gly glycosylation 901:913 arg1 complexed random IgG complexed random IgG Cterm IgG The levels and type of glycosylation of complexed random IgG was measured with lectin enzyme-immunosorbent assays. 20470225 1 24 gly glycosylation 123:135 arg1 Mucin1 Mucin1 PUBTATOR Mucin1 4582 Mucin1 (MUC1) with altered glycosylation behaves as an antigen unique to adenocarcinomas (ADCs). 20470225 1 24 gly glycosylation 123:135 arg1 MUC1 MUC1 PUBTATOR MUC1 4582 Mucin1 (MUC1) with altered glycosylation behaves as an antigen unique to adenocarcinomas (ADCs). 21264968 4 27 gly glycosylated 1611:1622 arg1 densely glycosylated MUC4 densely glycosylated MUC4 PUBTATOR MUC4 4585 In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15. 21264968 6 74 part_of MUC4 2024:2027 arg1 Thr10 MUC4 Thr10 PUBTATOR AminoAcid MUC4 4585 Thr10 The solution structures determined by NMR spectroscopic studies elicited that the preferential introduction of α-GalNAc at Thr10 of MUC4 stabilizes specifically a β-like extended backbone structure at this area, whereas other synthetic models with a single α-GalNAc residue at Thr1, Thr6, or Thr15 did not exhibit any converged three-dimensional structure at the proximal peptide moiety. 21264968 3 84 gly glycoproteins 1252:1264 arg1 human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly) human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly) PUBTATOR mucin glycoproteins 100508689 An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly). 21264968 3 84 gly glycoproteins 1252:1264 arg1 MUC5AC MUC5AC PUBTATOR MUC5AC 4586 An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly). 21264968 3 84 gly glycoproteins 1252:1264 arg1 MUC4 MUC4 PUBTATOR MUC4 4585 An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly). 21264968 7 89 gly glycosylation 2369:2381 arg1 MUC5AC MUC5AC PUBTATOR MUC5AC 4586 Such conformational impact on the underlying peptides was proved to be remarkable in the glycosylation at the consecutive Thr residues of MUC5AC. 21264968 5 95 gly MUC5AC 1826:1831 arg1 four α-GalNAc residues MUC5AC four α-GalNAc residues PUBTATOR MUC5AC 4586 On the contrary, O-glycosylation of naked MUC5AC peptide occurred predominantly at consecutive Thr residues and led to MUC5AC with four α-GalNAc residues at Thr2, Thr3, Thr7, and Thr8. 21264968 3 128 gly glycoproteins 1252:1264 arg1 the tandem repeats mucin glycoproteins the tandem repeats PUBTATOR mucin glycoproteins 100508689 An electron-capture dissociation device in a linear radio-frequency quadrupole ion trap (RFQ-ECD) combined with a time-of-flight (TOF) mass spectrometer was employed for the identification of Thr/Ser residues occupied by α-GalNAc branching among multiple and potential O-glycosylation sites in the tandem repeats of human mucin glycoproteins MUC4 (Thr-Ser-Ser-Ala-Ser-Thr-Gly-His-Ala-Thr-Pro-Leu-Pro-Val-Thr-Asp) and MUC5AC (Pro-Thr-Thr-Val-Gly-Ser-Thr-Thr-Val-Gly). 15616123 2 30 gly glycosylation 356:368 arg1 apoB100 apoB100 PUBTATOR apoB100 338 In the present study, a site-specific glycosylation analysis of apoB100 was carried out using reversed-phase high-performance liquid chromatography coupled with electrospray ionization tandem mass spectrometry (LC/ESI MS/MS). 15616123 0 37 gly glycosylation 14:26 arg1 human apolipoprotein B100 human apolipoprotein B100 PUBTATOR apolipoprotein B100 338 Site-specific glycosylation analysis of human apolipoprotein B100 using LC/ESI MS/MS. 22245433 5 14 gly glycosylation 855:867 arg1 COX-2 COX-2 PUBTATOR COX-2 5743 Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors. 22245433 0 17 gly Glycosylation 0:12 arg1 COX-2 COX-2 PUBTATOR COX-2 5743 Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors. 22245433 0 17 gly Glycosylation 0:12 arg1 human cyclooxygenase-2 human cyclooxygenase-2 PUBTATOR cyclooxygenase-2 5743 Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors. 25485983 0 10 part_of antithrombin 84:95 arg1 N135 antithrombin N135 PUBTATOR SpecificSite antithrombin 462 N135 Increased N-glycosylation efficiency by generation of an aromatic sequon on N135 of antithrombin. 25485983 4 16 gly glycosylation 615:627 arg1 antithrombin antithrombin PUBTATOR antithrombin 462 We evaluated the effect of the aromatic sequon in this defective glycosylation site of antithrombin, despite of being located in a loop between the helix D and the strand 2A. 25485983 1 41 gly glycosylation 114:126 arg1 antithrombin antithrombin PUBTATOR antithrombin 462 The inefficient glycosylation of consensus sequence on N135 in antithrombin explains the two glycoforms of this key anticoagulant serpin found in plasma: α and β, with four and three N-glycans, respectively. 14658030 0 82 gly N-glycosylation 18:32 arg1 the murine neural cell adhesion molecule NCAM the murine neural cell adhesion molecule NCAM PUBTATOR NCAM 17967 Identification of N-glycosylation sites of the murine neural cell adhesion molecule NCAM by MALDI-TOF and MALDI-FTICR mass spectrometry. 23661698 8 6 part_of EphA2 1196:1200 arg1 Lys-136 EphA2 Lys-136 PUBTATOR SpecificSite EphA2 1969 Asp-78 and Lys-136 Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136. 23661698 8 6 part_of EphA2 1196:1200 arg1 Asp-78 EphA2 Asp-78 PUBTATOR SpecificSite EphA2 1969 Asp-78 and Lys-136 Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136. 23661698 8 6 gly EphA2 1196:1200 arg1 the ligand's carbohydrates EphA2 the ligand's carbohydrates PUBTATOR EphA2 1969 Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136. 23661698 2 23 part_of ephrin-A1 368:376 arg1 the Asn-26 ephrin-A1 the Asn-26 PUBTATOR SpecificSite ephrin-A1 1942 Asn-26 The crystal structure of the ligand-receptor complex revealed a glycosylation on the Asn-26 of ephrin-A1. 23661698 6 44 gly deglycosylated 911:924 arg1 deglycosylated ephrin-A1 deglycosylated ephrin-A1 PUBTATOR ephrin-A1 1942 Data obtained by surface plasmon resonance confirms that deglycosylated ephrin-A1 does not bind EphA2 with high affinity. 23661698 4 48 gly deglycosylated 518:531 arg1 Ephrin-A1 Ephrin-A1 PUBTATOR Ephrin-A1 1942 Ephrin-A1 was enzymatically deglycosylated, and its activity was evaluated in several assays using glioblastoma (GBM) cells and recombinant EphA2. 23661698 5 50 gly deglycosylated 651:664 arg1 deglycosylated ephrin-A1 deglycosylated ephrin-A1 PUBTATOR ephrin-A1 1942 We found that deglycosylated ephrin-A1 does not efficiently induce EphA2 receptor internalization and degradation, and does not activate the downstream signaling pathways involved in cell migration and proliferation. 23661698 9 52 gly glycosylation 1255:1267 arg1 ephrin-A1 ephrin-A1 PUBTATOR ephrin-A1 1942 These findings suggest that the glycosylation on ephrin-A1 plays a critical role in the binding and activation of the EphA2 receptor. 28694069 5 70 gly Aglycosylated 882:894 arg1 N297D/S298A-IYG N297D/S298A-IYG PUBTATOR D/S298A- 6531 Aglycosylated constructs N297D/S298T (DTT)-K326I/A327Y/L328G (IYG) and N297D/S298A-IYG optimally drove tumor cell phagocytosis. 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. 23028207 2 46 gly N-glycosylation 221:235 arg1 human serum alpha-2-macroglobulin human serum alpha-2-macroglobulin PUBTATOR alpha-2-macroglobulin 2 Herein, the detailed N-glycosylation pattern of human serum alpha-2-macroglobulin was studied using an integrative approach, including permethylation of N-glycans, collision induced dissociation (CID) and electron transfer dissociation (ETD) of chymotryptic N-glycopeptides, and partial deglycosylation of chymotryptic N-glycopeptides with endo-β-N-acetylglucosaminidase F3 (Endo F3). 19276077 10 33 gly N-glycosylation 1762:1776 arg1 the alpha5 subunit the alpha5 subunit OGER subunit 3678 These results, taken together, strongly suggest that N-glycosylation of site-4 on the alpha5 subunit is the most important site for its biological functions. 19276077 1 45 gly N-glycans 226:234 arg1 the integrin alpha5 subunit integrin alpha5 subunit N-glycans PUBTATOR integrin alpha5 subunit 3678 Recently we reported that N-glycans on the beta-propeller domain of the integrin alpha5 subunit (S-3,4,5) are essential for alpha5beta1 heterodimerization, expression, and cell adhesion. 25327667 0 54 gly glycosylation 33:45 arg1 prostate specific antigen prostate specific antigen PUBTATOR prostate specific antigen 354 Glycoproteomics: identifying the glycosylation of prostate specific antigen at normal and high isoelectric points by LC-MS/MS. 10913840 2 14 gly unglycosylated 402:415 arg1 rFuc-TIV rFuc-TIV PUBTATOR form of rFuc-TIV 60670 When one member of this family, rFuc-TIV, is expressed in bacteria, the unglycosylated form of rFuc-TIV has no detectable enzymatic activity. 10913840 2 14 gly unglycosylated 402:415 arg1 the unglycosylated form the unglycosylated form PUBTATOR form of rFuc-TIV 60670 When one member of this family, rFuc-TIV, is expressed in bacteria, the unglycosylated form of rFuc-TIV has no detectable enzymatic activity. 10913840 3 26 gly N-glycosylation 490:504 arg1 rFuc-TIV rFuc-TIV PUBTATOR rFuc-TIV 60670 The two potential N-glycosylation sites of rFuc-TIV were mutated to determine site occupancy and the effect of site occupancy on enzyme activity and targeting of this enzyme. 10913840 0 45 gly occupancy 21:29 arg1 rat alpha-1,3-fucosyltransferase IV rat alpha-1,3-fucosyltransferase IV OGER fucosyltransferase IV Q62994 N-glycosylation site occupancy of rat alpha-1,3-fucosyltransferase IV and the effect of glycosylation on enzymatic activity. 12490395 6 7 gly glycosylation 1070:1082 arg1 xcCAT1 xcCAT1 Cterm xcCAT1 114246 We found that xcCAT1 expressed in Chinese hamster ovary (CHO) cells undergoes less glycosylation than rCAT1 and that the expression of xcCAT1 rendered the CHO cells more susceptible to infection with Moloney MLV. 27489265 1 32 gly glycoprotein 144:155 arg1 Env Env PUBTATOR Env 155971 The envelope glycoprotein (Env) is the major target for HIV-1 broadly neutralizing antibodies (bNAbs). 27489265 1 32 gly glycoprotein 144:155 arg1 The envelope glycoprotein The envelope glycoprotein PUBTATOR envelope glycoprotein 155971 The envelope glycoprotein (Env) is the major target for HIV-1 broadly neutralizing antibodies (bNAbs). 27489265 11 94 gly glycoprotein 1802:1813 arg1 The HIV-1 Env glycoprotein The HIV-1 Env glycoprotein PUBTATOR Env glycoprotein 155971 The HIV-1 Env glycoprotein presents a dense patchwork of host cell-derived N-linked glycans. 27489265 2 105 gly glycosylation 362:374 arg1 Env Env PUBTATOR Env 100616444 One of the mechanisms that HIV has evolved to escape the host's immune response is to mask conserved epitopes on Env with dense glycosylation. 16938437 0 40 gly N-glycosylation 0:14 arg1 human nicastrin human nicastrin PUBTATOR nicastrin 23385 N-glycosylation of human nicastrin is required for interaction with the lectins from the secretory pathway calnexin and ERGIC-53. 22238065 8 13 gly aglycosylated 1720:1732 arg1 aglycosylated H10-Mut aglycosylated H10-Mut OGER H10-Mut P22033 In the case of aglycosylated H10-Mut, more than 95% of the heavy chain was cleaved, confirming the pivotal role of the sugar moiety in protein stability. 23005037 4 1 gly non-glycosylated 678:693 arg1 non-glycosylated prokaryotic CD147 non-glycosylated prokaryotic CD147 PUBTATOR CD147 682 Moreover, native glycosylated CD147 existed exclusively as oligomers in solution and directly stimulated MMP production more efficiently than non-glycosylated prokaryotic CD147. 23005037 9 41 gly N-glycosylation 1456:1470 arg1 CD147 CD147 PUBTATOR CD147 682 The present study reveals the important role of N-glycosylation of CD147 in its biological function and implied that targeting aberrant β1,6-branching of N-glycans on CD147 would be valuable for the development of novel therapeutic modalities against carcinoma. 23005037 3 48 gly N-glycosylated 437:450 arg1 the purified native CD147 the purified native CD147 PUBTATOR CD147 682 In the present study, mass spectrum analysis demonstrated that the purified native CD147 from human lung cancer tissue was N-glycosylated and contained a series of high-mannose and complex-type N-linked glycan structures. 23005037 4 62 gly glycosylated 553:564 arg1 native glycosylated CD147 native glycosylated CD147 PUBTATOR CD147 682 Moreover, native glycosylated CD147 existed exclusively as oligomers in solution and directly stimulated MMP production more efficiently than non-glycosylated prokaryotic CD147. 12867358 2 30 gly N-glycosylation 336:350 arg1 hNaSi-1 hNaSi-1 PUBTATOR hNaSi-1 6561 In this study, the location and functional role of the N-glycosylation site of hNaSi-1 were studied using antifusion protein antibodies. 12867358 0 50 gly N-glycosylation 19:33 arg1 hNaSi-1 hNaSi-1 PUBTATOR hNaSi-1 6561 Mutagenesis of the N-glycosylation site of hNaSi-1 reduces transport activity. 17899080 2 26 gly glycoproteins 318:330 arg1 factor VIII factor VIII PUBTATOR factor VIII 2157 This should allow efficient secretion of glycoproteins such as factor VIII (FVIII) whose secretion is negatively affected by BiP interaction. 29587225 1 7 gly glycoprotein 186:197 arg1 Recombinant human erythropoietin Recombinant human erythropoietin PUBTATOR erythropoietin 2056 Recombinant human erythropoietin (EPO) is a therapeutic glycoprotein widely used for treating anemia. 29587225 3 51 gly sialylation 439:449 arg1 EPO conformation EPO conformation PUBTATOR EPO 2056 Nonetheless, a detailed understanding of the effects of sialylation on EPO conformation and dynamics is still lacking. 29274340 3 27 gly glycosylation 708:720 arg1 rhGAA rhGAA OGER rhGAA Q6P7A9 This study investigated M6P glycosylation on rhGAA using liquid chromatography (LC)-electrospray ionization (ESI)-high-energy collisional dissociation (HCD) tandem mass spectrometry (MS/MS). 29274340 2 40 gly glycosylation 453:465 arg1 rhGAA rhGAA OGER rhGAA Q6P7A9 Mannose-6-phosphate (M6P) glycosylation on rhGAA is a key factor influencing lysosomal enzyme targeting and the efficacy of enzyme replacement therapy (ERT); however, its complex structure and relatively small quantity still remain to be characterized. 29274340 2 60 gly glycosylation 453:465 arg1 rhGAA rhGAA glycosylation OGER rhGAA Q6P7A9 Mannose-6-phosphate (M6P) glycosylation on rhGAA is a key factor influencing lysosomal enzyme targeting and the efficacy of enzyme replacement therapy (ERT); however, its complex structure and relatively small quantity still remain to be characterized. 29274340 4 84 gly released 883:890 arg1 rhGAA AND The glycans rhGAA The glycans OGER rhGAA Q6P7A9 The glycans released from rhGAA were labeled with procainamide to improve mass ionization efficiency and the sensitivity of MS/MS. 15009203 0 41 gly N- 0:1 arg1 granulocyte-macrophage colony-stimulating factor granulocyte-macrophage colony-stimulating factor N- PUBTATOR granulocyte-macrophage colony-stimulating factor 1437 N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line. 15009203 0 109 gly carbohydrates 16:28 arg1 granulocyte-macrophage colony-stimulating factor granulocyte-macrophage colony-stimulating factor carbohydrates PUBTATOR granulocyte-macrophage colony-stimulating factor 1437 N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line. 21248038 1 18 gly glycosylation 325:337 arg1 gp120 gp120 PUBTATOR gp120 3700 The broadly neutralizing human monoclonal antibody 2G12 binds to a carbohydrate-dependent epitope involving three major potential N-linked glycosylation sites (PNGS) of gp120 (N295, N332, and N392). 17715132 5 1 gly glycosylated 694:705 arg1 Pannexin1 Pannexin1 PUBTATOR Pannexin1 24145 We show for the first time that Pannexin1 is glycosylated at Asn-254 and that this residue is important for plasma membrane targeting. 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. 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. 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. 25220145 11 2 gly CF-glycosylation 1863:1878 arg1 AFP-L3 AFP-L3 OGER AFP Q12899 For example, the CF-glycosylation of an α-fetoprotein isoform (AFP-L3) was approved as a biomarker of hepatocellular carcinoma (HCC). 25499076 5 45 gly present 859:865 arg1 native, pituitary G-hPRL AND the N-glycan structures native, pituitary G-hPRL the N-glycan structures PUBTATOR hPRL 5617 The main objective of this study was to determine the N-glycan structures present in native, pituitary G-hPRL and compare them with those present in the recombinant hormone. 25499076 0 79 gly glycosylated 105:116 arg1 recombinant and pituitary glycosylated human prolactin recombinant and pituitary glycosylated human prolactin PUBTATOR prolactin 5617 N-glycoprofiling analysis in a simple glycoprotein model: a comparison between recombinant and pituitary glycosylated human prolactin. 17599380 3 20 part_of HIV 326:328 arg1 Asp 386 HIV Env variant Asp 386 PUBTATOR SpecificSite HIV Env variant 100616444 Asp 386 Here, we identify an HIV Env variant in the V4 region of gp120, Asp 386 (D386), that eliminates an N-linked glycosylation site at position 386, enhances viral replication in macrophages, and is present at a higher frequency in AIDS patients with HIV-associated dementia (HAD) compared with non-HAD patients. 17599380 3 70 part_of Env 330:332 arg1 Asp 386 HIV Env variant Asp 386 PUBTATOR SpecificSite HIV Env variant 100616444 Asp 386 Here, we identify an HIV Env variant in the V4 region of gp120, Asp 386 (D386), that eliminates an N-linked glycosylation site at position 386, enhances viral replication in macrophages, and is present at a higher frequency in AIDS patients with HIV-associated dementia (HAD) compared with non-HAD patients. 20936810 0 77 gly glycosylation 40:52 arg1 Pin WW folding kinetics Pin WW folding kinetics PUBTATOR Pin 8655 Context-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics. 15247302 0 42 gly glycosylation 25:37 arg1 the beta2-adrenergic receptor the beta2-adrenergic receptor OGER beta2-adrenergic receptor P07550 A primate-dominant third glycosylation site of the beta2-adrenergic receptor routes receptors to degradation during agonist regulation. 29980609 5 14 gly glycoproteins 951:963 arg1 AICL glycoproteins AICL glycoproteins PUBTATOR AICL glycoproteins 9976 Cys87 residing within the C-type lectin-like domain not only ensures stable homodimerization of AICL glycoproteins by disulfide bonding, but Cys87 is also required for efficient cell surface expression of AICL homodimers and essential for AICL-NKp80 interaction. 29980609 1 17 gly glycoproteins 123:135 arg1 AICL glycoproteins AICL glycoproteins PUBTATOR AICL glycoproteins 9976 AICL glycoproteins are cognate activation-induced ligands of the C-type lectin-like receptor NKp80, which is expressed on virtually all mature human NK cells, and NKp80-AICL interaction stimulates NK cell effector functions such as cytotoxicity and cytokine secretion. 29980609 4 26 gly glycoproteins 755:767 arg1 AICL glycoproteins AICL glycoproteins PUBTATOR AICL glycoproteins 9976 In this study, we characterize molecular determinants of AICL glycoproteins that cause intracellular retention, thereby controlling AICL surface expression. 29980609 4 30 gly glycoproteins 755:767 arg1 molecular determinants AICL glycoproteins molecular determinants PUBTATOR AICL glycoproteins 9976 In this study, we characterize molecular determinants of AICL glycoproteins that cause intracellular retention, thereby controlling AICL surface expression. 23263199 0 45 gly N-glycosylations 0:15 arg1 human α1,3-fucosyltransferase IX human α1,3-fucosyltransferase IX PUBTATOR fucosyltransferase IX 10690 N-glycosylations of human α1,3-fucosyltransferase IX are required for full enzyme activity. 26869352 11 29 gly fucosylated 1824:1834 arg1 fucosylated haptoglobin fucosylated haptoglobin PUBTATOR haptoglobin 3240 These data suggest that the original tissue/cell producing fucosylated haptoglobin is different in each cancer type and linkage of fucosylation might be a clue of primary lesion, thereby enabling a differential diagnosis between gastroenterological cancers and non-gastroenterological cancers. 26869352 2 61 gly N-glycans 365:373 arg1 haptoglobin haptoglobin N-glycans PUBTATOR haptoglobin 3240 Previously, we reported that fucosylated N-glycans on haptoglobin in the sera of patients with pancreatic cancer were increased by lectin-ELISA and mass spectrometry analyses. 26869352 3 80 gly fucosylated 524:534 arg1 fucosylated haptoglobin fucosylated haptoglobin PUBTATOR haptoglobin 3240 However, an increase in fucosylated haptoglobin has been reported in various types of cancer. 26869352 8 88 gly released 1379:1386 arg1 haptoglobin AND N-glycan alditols haptoglobin N-glycan alditols PUBTATOR haptoglobin 3240 We next analyzed N-glycan alditols released from haptoglobin using graphitized carbon column LC-ESI MS to identify the linkage of fucosylation. 23991039 10 49 gly CD4bs 1628:1632 arg1 glycans CD4 glycans PUBTATOR CD4 920 High-resolution analyses of trimeric Env that show the orientation of glycans and polymorphic elements of the CD4bs that affect binding to antibodies like 1F7 are desirable to understand how to promote immunogenicity of more conserved elements of the CD4bs. 24884609 6 1 gly N-glycoforms 998:1009 arg1 ITIH4 N-glycoforms ITIH4 N-glycoforms PUBTATOR ITIH4 3700 Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms. 24884609 10 23 gly O-glycoforms 1413:1424 arg1 isoform-specific ITIH4 O-glycoforms isoform-specific ITIH4 O-glycoforms PUBTATOR ITIH4 3700 We also identified isoform-specific ITIH4 O-glycoforms and documented that utilization of O-glycosylation sites on ITIH4 differed between the cell line and serum. 24884609 3 41 gly glycosylation 443:455 arg1 recombinant and serum-derived ITIH4 recombinant and serum-derived ITIH4 PUBTATOR ITIH4 3700 In this study, we aimed to characterize glycosylation of recombinant and serum-derived ITIH4 using analytical mass spectrometry. 24884609 5 68 part_of ITIH4 665:669 arg1 N81 ITIH4 N81 PUBTATOR SpecificSite ITIH4 3700 N81, N207, N517, and N577 First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water. 24884609 5 68 part_of ITIH4 665:669 arg1 N517 ITIH4 N517 PUBTATOR SpecificSite ITIH4 3700 N81, N207, N517, and N577 First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water. 24884609 5 68 part_of ITIH4 665:669 arg1 N577 ITIH4 N577 PUBTATOR SpecificSite ITIH4 3700 N81, N207, N517, and N577 First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water. 24884609 5 68 part_of ITIH4 665:669 arg1 N207 ITIH4 N207 PUBTATOR SpecificSite ITIH4 3700 N81, N207, N517, and N577 First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water. 24884609 1 70 gly glycoprotein 167:178 arg1 Inter-alpha-trypsin inhibitor heavy chain H4 Inter-alpha-trypsin inhibitor heavy chain H4 PUBTATOR Inter-alpha-trypsin inhibitor heavy chain H4 3700 Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum. 26296369 5 67 gly CD69 1094:1097 arg1 the N-glycan composition CD69 the N-glycan composition PUBTATOR CD69 969 In agreement, the glycomics analysis determines the glycosylation site and the N-glycan composition of CD69, and terminal removal of sialic acid from that N-linked glycans reverses the generation of forkhead box P3-positive Treg cells (23.21%; P < 0.05). 26296369 5 84 gly glycosylation 1043:1055 arg1 CD69 CD69 PUBTATOR CD69 969 In agreement, the glycomics analysis determines the glycosylation site and the N-glycan composition of CD69, and terminal removal of sialic acid from that N-linked glycans reverses the generation of forkhead box P3-positive Treg cells (23.21%; P < 0.05). 20053750 4 34 gly glycan 836:841 arg1 hPIV-3 HN hPIV-3 HN glycan Cterm hPIV-3 HN 4758 Sequence analysis and superposition of the NDV and hPIV-3 HN dimer structures revealed that, similar to what was seen in hPIV-1, the N-linked glycan at residue 523 on hPIV-3 HN may cover a second receptor-binding site. 20053750 0 66 gly hemagglutinin-neuraminidase 67:93 arg1 N-linked glycan neuraminidase N-linked glycan PUBTATOR neuraminidase 4758 N-linked glycan at residue 523 of human parainfluenza virus type 3 hemagglutinin-neuraminidase masks a second receptor-binding site. 26944735 4 68 part_of BMP-1 872:876 arg1 the vicinal disulfide linkage C185-C186 BMP-1 the vicinal disulfide linkage C185-C186 PUBTATOR SiteSequence BMP-1 649 C185-C186 Ten disulfide linkages of BMP-1, including the vicinal disulfide linkage C185-C186 could be unambiguously identified. 14715137 5 1 part_of synaptotagmin 927:939 arg1 the C(2) domains synaptotagmin 7 the C(2) domains PUBTATOR SpecificSite synaptotagmin 7 9066 C(2) domains In addition to the intraluminal N-glycosylation site, the cytoplasmic C(2) domains of synaptotagmin 1 were required for correct targeting but could be functionally replaced by the C(2) domains of synaptotagmin 7. 14715137 5 21 part_of synaptotagmin 817:829 arg1 the cytoplasmic C(2) domains synaptotagmin 1 the cytoplasmic C(2) domains PUBTATOR SpecificSite synaptotagmin 1 6857 C(2) domains In addition to the intraluminal N-glycosylation site, the cytoplasmic C(2) domains of synaptotagmin 1 were required for correct targeting but could be functionally replaced by the C(2) domains of synaptotagmin 7. 14715137 0 25 gly N-glycosylation 0:14 arg1 synaptotagmin 1 synaptotagmin 1 PUBTATOR synaptotagmin 1 6857 N-glycosylation is essential for vesicular targeting of synaptotagmin 1. 14715137 3 35 gly N-glycosylation 434:448 arg1 synaptotagmin 1 synaptotagmin 1 PUBTATOR synaptotagmin 1 6857 Conversely, mutation of the N-terminal N-glycosylation site of synaptotagmin 1 redirects synaptotagmin 1 from vesicles to the plasma membrane. 14715137 6 45 gly N-glycosylation 985:999 arg1 synaptotagmin 1 synaptotagmin 1 PUBTATOR synaptotagmin 1 6857 Our data suggest that the intravesicular N-glycosylation site of synaptotagmin 1 collaborates with its cytoplasmic C(2) domains in directing synaptotagmin 1 to synaptic vesicles via a novel N-glycosylation-dependent mechanism. 25614955 7 25 gly glycoprotein 1238:1249 arg1 the glycoprotein G the glycoprotein G OGER glycoprotein G P07996 In addition, sequence analysis of the glycoprotein G identified an amino acid substitution (I338→T338) unique to the IMDRV-13 within antigenic sites III (330-338), this mutation also leads to an additional potential N-glycosylation site (N336), which may represent a useful model to study relationship of N-glycosylation in G protein and specific properties such as pathogenicity or host adaption of RABV. 25614955 7 66 gly N-glycosylation 1505:1519 arg1 G protein G protein OGER G protein In addition, sequence analysis of the glycoprotein G identified an amino acid substitution (I338→T338) unique to the IMDRV-13 within antigenic sites III (330-338), this mutation also leads to an additional potential N-glycosylation site (N336), which may represent a useful model to study relationship of N-glycosylation in G protein and specific properties such as pathogenicity or host adaption of RABV. 19284292 2 23 gly polysialylation 406:420 arg1 NCAM NCAM PUBTATOR NCAM 4684 Examples of the latter are found in the formation of the mannose-6-phosphate receptor ligand on lysosomal hydrolases, and in polysialylation of NCAM, which are regulated via conformational signal patches on the protein. 19284292 2 45 gly NCAM 425:428 arg1 polysialylation NCAM polysialylation PUBTATOR NCAM 4684 Examples of the latter are found in the formation of the mannose-6-phosphate receptor ligand on lysosomal hydrolases, and in polysialylation of NCAM, which are regulated via conformational signal patches on the protein. 27641734 16 29 gly N-glycosylation 2981:2995 arg1 CD97 CD97 PUBTATOR CD97 976 A comparison of the HeLa binding affinities of PNGase F-digested, GPS-mutated and N-glycosylation-mutated CD97 samples revealed diverse findings, suggesting that the functions of CD97 ECD were complex, and various technologies for function validation should be utilized to avoid single-approach bias when investigating N-glycosylation and auto-proteolysis of CD97. 27641734 10 86 gly N-glycosylation 1795:1809 arg1 CD97 EGF1-5 isoform CD97 EGF1-5 isoform PUBTATOR CD97 EGF1-5 isoform 976 N-glycosylation affected the auto-proteolysis of CD97 EGF1-5 isoform in a similar way as the other previously reported CD97 isoforms. 27641734 19 148 gly N-glycosylation 3486:3500 arg1 HeLa cell attachment HeLa cell attachment OGER HeLa P0DMC3 Finally, the GAIN and EGF domains are also important for CD97-HeLa adhesion, whereas N-glycosylation of the CD97 GAIN domain and GPS auto-proteolysis are not required for HeLa cell attachment. 27641734 11 150 gly deglycosylated 1950:1963 arg1 WT and deglycosylated CD97ECD WT and deglycosylated CD97ECD PUBTATOR CD97 976 SAXS data for WT and deglycosylated CD97ECD revealed a spatula-like shape with GAIN and EGF domains constituting the body and handle, respectively. 12706347 4 9 part_of asparagine 691:700 arg1 NTPDase3 NTPDase3 asparagine PUBTATOR SpecificSite NTPDase3 956 sites, asparagine 81 Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases. 16368742 0 76 gly Glycosylation 0:12 arg1 the osmoresponsive transient receptor potential channel TRPV4 the osmoresponsive transient receptor potential channel TRPV4 PUBTATOR TRPV4 59341 Glycosylation of the osmoresponsive transient receptor potential channel TRPV4 on Asn-651 influences membrane trafficking. 16368742 5 83 part_of TRPV4 974:978 arg1 Residue N651 TRPV4 Residue N651 PUBTATOR SpecificSite TRPV4 59341 N651 Residue N651 of TRPV4 is immediately adjacent to the pore-forming loop. 26701645 4 10 gly N-glycosylated 663:676 arg1 tyrosinase tyrosinase PUBTATOR tyrosinase 7299 By LC-MS/MS analysis of human tyrosinase expressed in a melanoma cell, we show that all seven sites of tyrosinase are at least partially N-glycosylated. 26701645 3 55 gly glycosylated 456:467 arg1 tyrosinase tyrosinase PUBTATOR tyrosinase 7299 Here, we investigate the processing of tyrosinase, a multiple glycosylated tumor antigen overexpressed in human malignant melanoma. 20622883 6 52 gly N46-glycosylation 903:919 arg1 pre-BCR function pre-BCR function PUBTATOR BCR 613 When tested in the context of the BCR, muHC with a mutant N46 showed normal function, which indicated that N46-glycosylation is specifically required for pre-BCR function. 15616124 6 12 gly N-glycosylation 908:922 arg1 FVII FVII Cterm FVII 2155 Immediately after pulse, most labeled intracellular FVII had one N-glycan, but during a 1-h chase, the vast majority was processed into FVII with two N-glycans, demonstrating posttranslational N-glycosylation of FVII. 15616124 4 68 gly FVII 541:544 arg1 one and two N-glycans FVII one and two N-glycans Cterm FVII 2155 Pulse-chase labeled intracellular FVII migrated as two bands corresponding to FVII with one and two N-glycans, respectively. 15616124 6 79 gly FVII 851:854 arg1 two N-glycans FVII two N-glycans Cterm FVII 2155 Immediately after pulse, most labeled intracellular FVII had one N-glycan, but during a 1-h chase, the vast majority was processed into FVII with two N-glycans, demonstrating posttranslational N-glycosylation of FVII. 15616124 2 83 gly N-glycosylation 312:326 arg1 FVII FVII Cterm FVII 2155 In the present study, however, we demonstrate posttranslational N-glycosylation of recombinant human coagulation factor VII (FVII) in CHO-K1 and 293A cells. 15616124 2 83 gly N-glycosylation 312:326 arg1 recombinant human coagulation factor VII recombinant human coagulation factor VII PUBTATOR coagulation factor VII 2155 In the present study, however, we demonstrate posttranslational N-glycosylation of recombinant human coagulation factor VII (FVII) in CHO-K1 and 293A cells. 11439087 11 8 gly N-glycosylation 1428:1442 arg1 sBST-1 sBST-1 Cterm sBST-1 683 We conclude that N-glycosylation of sBST-1 facilitates the folding of the nascent polypeptide chain into a conformation that is conductive for intracellular transport and enzymic activity. 11439087 8 49 part_of sBST-1 1133:1138 arg1 N1-N4 sBST-1 N1-N4 Cterm SiteSequence sBST-1 683 N1-N4 Site-directed mutagenesis was performed to generate sBST-1 mutants (N1-N4), each preserving a single N-glycosylation site. 14749323 6 4 part_of site 931:934 arg1 mOAT1 mOAT1 site PUBTATOR SpecificSite mOAT1 18399 site Asp-39 We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated. 14749323 8 5 gly glycosylation 1484:1496 arg1 OAT function OAT function OGER OAT P04181 Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function. 14749323 4 67 gly glycosylation 629:641 arg1 mOAT1 function mOAT1 function PUBTATOR mOAT1 18399 274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function. 14749323 11 82 gly glycosylation 2054:2066 arg1 OAT1 OAT1 PUBTATOR OAT1 9356 This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family. 14749323 10 96 gly glycosylation 1816:1828 arg1 OAT1 function OAT1 function PUBTATOR OAT1 9356 In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane. 24533768 4 54 gly glycans 569:575 arg1 Asn-297 Asn-297 Asn-297 SpecificSite Asn-297 The native glycans on Asn-297 of antibodies were enzymatically remodeled in vitro using galactosyl and sialyltransferases to introduce terminal sialic acids. 17055129 0 57 gly N-glycosylation 15:29 arg1 hepatitis C virus envelope protein E2 hepatitis C virus envelope protein E2 Cterm E2 Engineering of N-glycosylation of hepatitis C virus envelope protein E2 enhances T cell responses for DNA immunization. 28336547 0 24 gly Glycans 0:6 arg1 the intestinal peptide transporter PEPT1 PEPT1 Glycans PUBTATOR PEPT1 56643 Glycans in the intestinal peptide transporter PEPT1 contribute to function and protect from proteolysis. 28336547 2 90 gly glycosylated 361:372 arg1 the proton-coupled oligopeptide transporter 1 the proton-coupled oligopeptide transporter 1 PUBTATOR proton-coupled oligopeptide transporter 1 56643 We recently demonstrated that the proton-coupled oligopeptide transporter 1 (PEPT1) in the intestine is glycosylated at six asparagine residues (N50, N406, N439, N510, N515, and N532). 28336547 2 90 gly glycosylated 361:372 arg1 PEPT1 PEPT1 PUBTATOR PEPT1 56643 We recently demonstrated that the proton-coupled oligopeptide transporter 1 (PEPT1) in the intestine is glycosylated at six asparagine residues (N50, N406, N439, N510, N515, and N532). 28336547 8 104 gly glycosylation 1567:1579 arg1 PEPT1 PEPT1 PUBTATOR PEPT1 56643 In addition, our experiments provide strong evidence that glycosylation of PEPT1 confers resistance against proteolytic cleavage by proteinase K, whereas a remarkable intrinsic stability against trypsin, even in the absence of N-linked glycans, was detected.NEW & NOTEWORTHY This study highlights the role of N50-linked glycans in modulating the bidirectional transport activity of the murine peptide transporter PEPT1. 20805301 5 12 gly glycosylation 689:701 arg1 CYP2W1 CYP2W1 PUBTATOR CYP2W1 54905 Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells. 20805301 5 69 part_of CYP2W1 711:716 arg1 Asn177 CYP2W1 Asn177 PUBTATOR AminoAcid CYP2W1 54905 Asn177 Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells. 23613470 7 9 gly modified 995:1002 arg1 Wnt11 AND high-mannose(Asn90)- Wnt11 high-mannose(Asn90)- PUBTATOR Wnt11 7481 Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298). 23613470 7 9 gly modified 995:1002 arg3 Wnt11 AND high-mannose/hybrid(Asn300)-type glycans Wnt11 high-mannose/hybrid(Asn300)-type glycans PUBTATOR Wnt11 7481 Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298). 23613470 7 40 gly modified 1117:1124 arg1 Wnt3a AND two high-mannose-type glycans Wnt3a two high-mannose-type glycans PUBTATOR Wnt3a 89780 Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298). 23613470 9 66 gly glycosylation 1399:1411 arg1 Wnt11 Wnt11 PUBTATOR Wnt11 7481 By the fusion of the Asn40 glycosylation site of Wnt11, Wnt3a was secreted apically. 15039521 5 29 gly glycosylation 648:660 arg1 M-sAg M-sAg OGER sAg Q9UBF6 In in vitro translation assays, the mutation Thr to Asn at aa 5 significantly impaired glycosylation of M-sAg. 19249803 10 41 gly glycan 1330:1335 arg1 the WNV E protein protein can glycan OGER protein can P35658 Together these data suggest that loss of the glycan at aa154 on the WNV E protein can severely restrict viral spread in the mosquito vector. 29755357 8 17 gly N-glycosylation 1473:1487 arg1 LCN2 LCN2 PUBTATOR LCN2 3934 In sum, our data indicate that the N-glycosylation of LCN2 is not required for proper secretion and exosome cargo recruitment in different cell types, but might be relevant to increase overall solubility. 29755357 6 33 gly non-glycosylated 1066:1081 arg1 the non-glycosylated LCN2 variants the non-glycosylated LCN2 variants PUBTATOR LCN2 variants 3934 Moreover, both the glycosylated and the non-glycosylated LCN2 variants are equally targeted to exosomes, demonstrating that this post-translational modification is not necessary for proper trafficking of LCN2 into these membranous extracellular vesicles. 29755357 0 38 gly N-Glycosylation 0:14 arg1 Lipocalin 2 Lipocalin 2 PUBTATOR Lipocalin 2 3934 N-Glycosylation of Lipocalin 2 Is Not Required for Secretion or Exosome Targeting. 9884403 1 0 gly N-glycosylation 93:107 arg1 human Tamm-Horsfall glycoprotein human Tamm-Horsfall glycoprotein OGER Tamm-Horsfall glycoprotein P07911 The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry. 9884403 0 15 gly glycoprotein 75:86 arg1 human Tamm-Horsfall glycoprotein human Tamm-Horsfall glycoprotein OGER Tamm-Horsfall glycoprotein P07911 Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein. 9884403 6 39 gly glycoprotein 1322:1333 arg1 native human Tamm-Horsfall glycoprotein native human Tamm-Horsfall glycoprotein OGER Tamm-Horsfall glycoprotein P07911 Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant. 9884403 1 45 gly glycoprotein 138:149 arg1 human Tamm-Horsfall glycoprotein human Tamm-Horsfall glycoprotein OGER Tamm-Horsfall glycoprotein P07911 The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry. 9884403 0 67 gly glycosylation 38:50 arg1 human Tamm-Horsfall glycoprotein human Tamm-Horsfall glycoprotein OGER Tamm-Horsfall glycoprotein P07911 Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein. 24798328 7 23 gly man 1159:1161 arg1 LDLR LDLR man PUBTATOR LDLR 3949 The glycosites in linker regions of LDLR class A repeats are conserved in LDLR from man to Xenopus and found in other homologous receptors. 20332087 3 30 gly MPO 470:472 arg1 the N-glycan composition MPO the N-glycan composition PUBTATOR MPO 4353 Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated. 20332087 3 48 gly MPO 517:519 arg1 the N-glycan composition MPO the N-glycan composition PUBTATOR MPO 4353 Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated. 17496250 11 1 gly O-glycosylated 1382:1395 arg1 IGFBP-5 IGFBP-5 PUBTATOR IGFBP-5 3488 IGFBP-5 was heterogeneously O-glycosylated mainly by sialylated core 1 type glycans. 19088065 12 35 gly sialylation 1587:1597 arg1 KLK6 KLK6 Cterm KLK6 Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma. 19088065 10 62 gly modified 1329:1336 arg3 ovarian cancer-derived KLK6 AND alpha2-6-linked sialic acid ovarian cancer-derived KLK6 alpha2-6-linked sialic acid Cterm KLK6 Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid. 19088065 12 85 gly KLK6 1602:1605 arg1 the extensive and almost exclusive sialylation KLK6 the extensive and almost exclusive sialylation Cterm KLK6 Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma. 26687240 2 50 gly glycosylated 188:199 arg1 IgE IgE PUBTATOR IgE P01854 IgE is the most heavily glycosylated antibody, but in comparison to other antibodies little is known about its glycan structure function relationships. 29867209 7 40 gly glycosylated 1013:1024 arg1 active glycosylated EPO active glycosylated EPO PUBTATOR EPO 2056 Therefore we present an alternative method for the synthesis of active glycosylated EPO with an engineered O-glycosylation site by combining eukaryotic cell-free protein synthesis and site-directed incorporation of non-canonical amino acids with subsequent chemoselective modifications. 18829751 0 79 gly Glycosylation 0:12 arg1 gp41 gp41 Cterm gp41 Glycosylation of gp41 of simian immunodeficiency virus shields epitopes that can be targets for neutralizing antibodies. 12731887 0 35 gly glycosylation 2:14 arg1 p67 p67 PUBTATOR p67 64370 A glycosylation site, 60SGTS63, of p67 is required for its ability to regulate the phosphorylation and activity of eukaryotic initiation factor 2alpha. 28708860 3 12 gly N-glycosylation 462:476 arg1 NA NA PUBTATOR NA 4758 The purpose of this paper is to explore the relations between charged amino acids, N-glycosylation and epitopes in hemagglutinin (HA) and neuraminidase (NA). 28708860 3 12 gly N-glycosylation 462:476 arg1 neuraminidase neuraminidase PUBTATOR neuraminidase 4758 The purpose of this paper is to explore the relations between charged amino acids, N-glycosylation and epitopes in hemagglutinin (HA) and neuraminidase (NA). 20153530 1 1 gly oligosaccharides 170:185 arg1 native human C9 C9 oligosaccharides PUBTATOR C9 117512 The two N-linked oligosaccharides in native human C9 were deleted by site-specific mutagenesis. 20153530 4 9 gly glycosylated 530:541 arg1 human C9 human C9 PUBTATOR C9 117512 This glycosylated form of human C9 was as active as the native protein suggesting that the glycan chain remains on the external side of the membrane and that translocation of this hairpin is not required for membrane anchoring. 20153530 7 65 gly glycosylated 1130:1141 arg1 this glycosylated C9 this glycosylated C9 PUBTATOR C9 117512 Again, this glycosylated C9 was as active as native C9 and could be induced to polymerize by heating or incubation with metal ions. 8429003 3 0 gly oligosaccharides 626:641 arg1 rat sCD4 sCD4 oligosaccharides PUBTATOR sCD4 499358 The most obvious differences between the rat and human sCD4 oligosaccharides were the greater abundance of oligomannose and hybrid oligosaccharides on rat sCD4 and the presence of oligosaccharides carrying a terminal alpha-galactose residue on human sCD4. 8429003 3 24 gly residue 728:734 arg1 human sCD4 sCD4 residue PUBTATOR sCD4 79966 The most obvious differences between the rat and human sCD4 oligosaccharides were the greater abundance of oligomannose and hybrid oligosaccharides on rat sCD4 and the presence of oligosaccharides carrying a terminal alpha-galactose residue on human sCD4. 8429003 0 39 gly glycosylation 14:26 arg1 recombinant rat and human soluble CD4 variants recombinant rat and human soluble CD4 variants PUBTATOR CD4 variants 920 Site-specific glycosylation of recombinant rat and human soluble CD4 variants expressed in Chinese hamster ovary cells. 8429003 6 59 part_of Asn159 1280:1285 arg1 rat sCD4 sCD4 Asn159 PUBTATOR AminoAcid sCD4 499358 Asn159 The glycosylation at the conserved site at Asn270 of rat sCD4 was identical to that seen for the equivalent site in human sCD4, and the oligomannose and hybrid structures were restricted to the nonconserved site at Asn159 in rat sCD4. 8429003 6 65 part_of sCD4 1122:1125 arg1 Asn270 sCD4 Asn270 PUBTATOR AminoAcid sCD4 499358 Asn270 The glycosylation at the conserved site at Asn270 of rat sCD4 was identical to that seen for the equivalent site in human sCD4, and the oligomannose and hybrid structures were restricted to the nonconserved site at Asn159 in rat sCD4. 18381078 1 8 gly glycoprotein 175:186 arg1 metalloprotease 10 metalloprotease 10 PUBTATOR A disintegrin and metalloprotease 10 102 A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins. 18381078 1 8 gly glycoprotein 175:186 arg1 A disintegrin A disintegrin PUBTATOR A disintegrin and metalloprotease 10 102 A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins. 23530120 2 21 gly glycoprotein 394:405 arg1 Env Env PUBTATOR Env 100616444 Neutralizing antibodies against the evolutionarily conserved CD4-binding site (CD4-BS) on the HIV envelope glycoprotein (Env) are capable of inhibiting infection of diverse HIV strains, and have been isolated from HIV-infected individuals. 23530120 2 21 gly glycoprotein 394:405 arg1 the HIV envelope glycoprotein the HIV envelope glycoprotein PUBTATOR V envelope glycoprotein 100616444 Neutralizing antibodies against the evolutionarily conserved CD4-binding site (CD4-BS) on the HIV envelope glycoprotein (Env) are capable of inhibiting infection of diverse HIV strains, and have been isolated from HIV-infected individuals. 22187327 1 5 gly glycoprotein 196:207 arg1 Intercellular adhesion molecule-5 Intercellular adhesion molecule-5 PUBTATOR Intercellular adhesion molecule-5 15898 Intercellular adhesion molecule-5 (ICAM-5, telencephalin) is a dendritically polarized type I membrane glycoprotein, and promotes dendritic filopodia formation. 22187327 2 7 gly ICAM-5 309:314 arg1 the N-glycan structures ICAM-5 the N-glycan structures PUBTATOR ICAM-5 15898 Although we have determined the N-glycan structures of ICAM-5 in a previous report, their function is unknown. 22187327 3 17 gly ICAM-5 519:524 arg1 the N-glycans ICAM-5 the N-glycans PUBTATOR ICAM-5 15898 Here, we produced fifteen ICAM-5 gene constructs, in which each potential N-glycosylation site was mutated, to elucidate the function of the N-glycans of ICAM-5, and observed the effects of transfection of them on a neuronal cell line, Neuro-2a (N2a). 26968544 8 34 gly dystrophin-glycoprotein 1606:1628 arg1 overall dystrophin-glycoprotein complex function overall dystrophin-glycoprotein complex function OGER dystrophin P11532 Therefore, appropriate glycosylation of δ-sarcoglycan may also be necessary for proper δ-sarcoglycan function and overall dystrophin-glycoprotein complex function. 26968544 1 49 gly dystrophin-glycoprotein 198:220 arg1 dystrophin-glycoprotein dystrophin-glycoprotein OGER dystrophin P11530 Delta-sarcoglycan is a component of the sarcoglycan subcomplex within the dystrophin-glycoprotein complex located at the plasma membrane of muscle cells. 26968544 4 83 gly dystrophin-glycoprotein 876:898 arg1 the dystrophin-glycoprotein complex the dystrophin-glycoprotein complex OGER dystrophin P11530 This study demonstrates that DCM mutant δ-sarcoglycans can be stably expressed in adult rat cardiac myocytes and traffic similarly to wild-type δ-sarcoglycan to the plasma membrane, without perturbing assembly of the dystrophin-glycoprotein complex. 26968544 9 89 gly dystrophin-glycoprotein 1750:1772 arg1 dystrophin-glycoprotein dystrophin-glycoprotein OGER dystrophin P11532 These studies demonstrate that DCM mutations in δ-sarcoglycan can exert a dominant negative effect on dystrophin-glycoprotein complex function leading to myocardial mechanical instability that may underlie the pathogenesis of δ-sarcoglycan-associated DCM. 11390601 3 42 part_of gp120 845:849 arg1 N301 gp120 N301 PUBTATOR SpecificSite gp120 3700 N301 Of the glycosylation sites that were evaluated, those proximal to the V1/V2 loops (N135, N141, N156, N160) and the V3 loops (N301) of gp120 were functionally critical. 27798666 0 48 gly Neuropilin-1 68:79 arg1 A Novel Physiological Glycosaminoglycan-Deficient Splice Variant Neuropilin-1 A Novel Physiological Glycosaminoglycan-Deficient Splice Variant PUBTATOR Neuropilin-1 8829 A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1 Is Anti-Tumorigenic In Vitro and In Vivo. 17222411 0 29 gly glycosylation 11:23 arg1 human podoplanin human podoplanin OGER podoplanin Q86YL7 Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor. 17222411 1 36 gly sialoglycoprotein 140:156 arg1 Podoplanin Podoplanin OGER Podoplanin Q86YL7 Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation. 17222411 2 47 part_of Thr52 299:303 arg1 human podoplanin podoplanin Thr52 OGER AminoAcid podoplanin Q86YL7 domain, and Thr52 Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity. 25567004 3 33 gly hyper-glycosylated 752:769 arg1 BSG BSG PUBTATOR BSG 12215 Recombinant low-glycosylated secreted BHc products (BSK) were also immunologically inert, similar to hyper-glycosylated BHc products (BSG), although deglycosylation restored their immunological activities. 25567004 5 37 gly non-glycosylated 1078:1093 arg1 mBHc mBHc PUBTATOR mBHc 192285 Notably, a non-glycosylated secreted homogeneous BHc isoform (mBHc), which we successfully prepared after deleting the pro-peptide and removing its single potential glycosylation site, was immunologically active and could confer effective protective immunity, similarly to non-glycosylated rBHc. 25567004 5 37 gly non-glycosylated 1078:1093 arg1 a non-glycosylated secreted homogeneous BHc isoform a non-glycosylated secreted homogeneous BHc isoform PUBTATOR BHc isoform 192285 Notably, a non-glycosylated secreted homogeneous BHc isoform (mBHc), which we successfully prepared after deleting the pro-peptide and removing its single potential glycosylation site, was immunologically active and could confer effective protective immunity, similarly to non-glycosylated rBHc. 25567004 5 40 gly non-glycosylated 1340:1355 arg1 non-glycosylated rBHc non-glycosylated rBHc PUBTATOR BHc 192285 Notably, a non-glycosylated secreted homogeneous BHc isoform (mBHc), which we successfully prepared after deleting the pro-peptide and removing its single potential glycosylation site, was immunologically active and could confer effective protective immunity, similarly to non-glycosylated rBHc. 25567004 6 48 gly non-glycosylated 1394:1409 arg1 a non-glycosylated secreted BHc isoform a non-glycosylated secreted BHc isoform PUBTATOR BHc isoform 192285 In summary, we conclude that a non-glycosylated secreted BHc isoform can be prepared in yeast by deleting the pro-peptide of the α-factor signal and mutating its single potential glycosylation site. 25567004 3 50 gly low-glycosylated 663:678 arg1 BSK BSK PUBTATOR BSK 450219 Recombinant low-glycosylated secreted BHc products (BSK) were also immunologically inert, similar to hyper-glycosylated BHc products (BSG), although deglycosylation restored their immunological activities. 25567004 4 90 gly deglycosylated 871:884 arg1 deglycosylated proBHc deglycosylated proBHc PUBTATOR BHc 192285 Unexpectedly, deglycosylated proBHc contained an unexpected pro-peptide of an α-factor signal and fortuitous N-linked glycosylation sites in the non-cleaved pro-peptide sequences, but not in the BHc sequences. 17986444 6 5 gly glycosylation 896:908 arg1 polySia-NCAM polySia-NCAM PUBTATOR polySia-NCAM 17967 Our results revealed an identical glycosylation and almost complete polysialylation of N-glycosylation sites 5 and 6 in polySia-NCAM irrespective of the enzyme present. 17986444 6 13 gly polysialylation 930:944 arg1 polySia-NCAM polySia-NCAM PUBTATOR polySia-NCAM 17967 Our results revealed an identical glycosylation and almost complete polysialylation of N-glycosylation sites 5 and 6 in polySia-NCAM irrespective of the enzyme present. 17986444 0 31 gly molecule 79:86 arg1 the polysialylation neural cell adhesion molecule the polysialylation PUBTATOR neural cell adhesion molecule 17967 Enzyme-dependent variations in the polysialylation of the neural cell adhesion molecule (NCAM) in vivo. 17986444 0 72 gly polysialylation 35:49 arg1 the neural cell adhesion molecule the neural cell adhesion molecule PUBTATOR neural cell adhesion molecule 17967 Enzyme-dependent variations in the polysialylation of the neural cell adhesion molecule (NCAM) in vivo. 17986444 0 72 gly polysialylation 35:49 arg1 NCAM NCAM PUBTATOR NCAM 17967 Enzyme-dependent variations in the polysialylation of the neural cell adhesion molecule (NCAM) in vivo. 17986444 4 82 gly NCAM 718:721 arg1 polysialylation NCAM polysialylation PUBTATOR NCAM 17967 Using mutant mice, lacking either enzyme, we now assessed in vivo the contribution of ST8SiaII and ST8SiaIV to polysialylation of NCAM. 17986444 4 83 gly polysialylation 699:713 arg1 NCAM NCAM PUBTATOR NCAM 17967 Using mutant mice, lacking either enzyme, we now assessed in vivo the contribution of ST8SiaII and ST8SiaIV to polysialylation of NCAM. 17986444 6 91 gly polysialylation 930:944 arg1 polySia-NCAM polySia-NCAM polysialylation PUBTATOR polySia-NCAM 17967 Our results revealed an identical glycosylation and almost complete polysialylation of N-glycosylation sites 5 and 6 in polySia-NCAM irrespective of the enzyme present. 16227249 9 72 gly glycosylated 1116:1127 arg1 prM prM Cterm prM RVPs or virions bearing combinations of glycosylated and nonglycosylated forms of prM and E could infect mammalian, avian, and mosquito cells (BHK-21, QT6, and C6/36, respectively). 16227249 9 75 gly nonglycosylated 1133:1147 arg1 prM prM Cterm prM RVPs or virions bearing combinations of glycosylated and nonglycosylated forms of prM and E could infect mammalian, avian, and mosquito cells (BHK-21, QT6, and C6/36, respectively). 24799124 7 17 gly ceruloplasmin 1559:1571 arg1 core-fucosylation ceruloplasmin core-fucosylation PUBTATOR ceruloplasmin 1356 However, in HBV- or HCV-related liver diseases, no significant site-specific change in core-fucosylation of ceruloplasmin was observed between HCC and cirrhosis. 24799124 1 18 gly ceruloplasmin 212:224 arg1 core-fucosylation ceruloplasmin core-fucosylation PUBTATOR ceruloplasmin 1356 A mass spectrometry-based methodology has been developed to study changes in core-fucosylation of serum ceruloplasmin that are site-specific between cirrhosis and hepatocellular carcinoma (HCC). 24799124 7 20 gly core-fucosylation 1538:1554 arg1 ceruloplasmin ceruloplasmin PUBTATOR ceruloplasmin 1356 However, in HBV- or HCV-related liver diseases, no significant site-specific change in core-fucosylation of ceruloplasmin was observed between HCC and cirrhosis. 24799124 0 43 gly ceruloplasmin 49:61 arg1 Mass-selected site-specific core-fucosylation ceruloplasmin Mass-selected site-specific core-fucosylation PUBTATOR ceruloplasmin 1356 Mass-selected site-specific core-fucosylation of ceruloplasmin in alcohol-related hepatocellular carcinoma. 24799124 1 48 gly core-fucosylation 185:201 arg1 serum ceruloplasmin serum ceruloplasmin PUBTATOR ceruloplasmin 1356 A mass spectrometry-based methodology has been developed to study changes in core-fucosylation of serum ceruloplasmin that are site-specific between cirrhosis and hepatocellular carcinoma (HCC). 24799124 0 50 gly core-fucosylation 28:44 arg1 ceruloplasmin ceruloplasmin PUBTATOR ceruloplasmin 1356 Mass-selected site-specific core-fucosylation of ceruloplasmin in alcohol-related hepatocellular carcinoma. 27604319 4 0 gly glycosylation 713:725 arg1 gp120 gp120 PUBTATOR gp120 Q14624 Knowing the site-specific glycosylation of gp120 can facilitate the rational design of glycopeptide antigens for HIV vaccine development. 27604319 1 35 gly glycoprotein 148:159 arg1 SU SU Cterm SU Q14624 The surface envelope glycoprotein (SU) of Human immunodeficiency virus type 1 (HIV-1), gp120(SU) plays an essential role in virus binding to target CD4+ T-cells and is a major vaccine target. 27604319 1 35 gly glycoprotein 148:159 arg1 The surface envelope glycoprotein The surface envelope glycoprotein PUBTATOR envelope glycoprotein 155971 The surface envelope glycoprotein (SU) of Human immunodeficiency virus type 1 (HIV-1), gp120(SU) plays an essential role in virus binding to target CD4+ T-cells and is a major vaccine target. 27604319 5 62 gly glycosylation 949:961 arg1 gp120 gp120 PUBTATOR gp120 Q14624 While most prior studies have focused on glycan analysis of recombinant forms of gp120, here we report the first systematic glycosylation site analysis of gp120 derived from virions produced by infected T lymphoid cells and show that a single site is exclusively substituted with complex glycans. 18941134 3 67 gly N-glycosylated 932:945 arg1 the highly abundant lactotransferrin the highly abundant lactotransferrin PUBTATOR lactotransferrin 17002 The predominance of Lewis X/Y along with Neu5Acalpha2-6 sialylation was found to be a salient feature of the ULF glycome, and several other protein carriers were additionally identified including the highly abundant lactotransferrin, which is N-glycosylated at two sites, both with a similar range of highly fucosylated N-glycans. 15113920 1 2 gly glycoproteins 173:185 arg1 Gn Gn Cterm Gn The membrane glycoproteins Gn and Gc of Hantaan virus (HTNV) (family Bunyaviridae) are modified by N-linked glycosylation. 15113920 7 21 gly chain 1143:1147 arg1 residue N134 residue N134 residue N134 SpecificSite residue N134 The oligosaccharide chain on residue N134 was found to be crucial for protein folding, whereas single mutations at the other glycosylation sites were better tolerated. 26059044 0 0 gly interleukin-22 82:95 arg1 the atypical N-glycan composition interleukin-22 the atypical N-glycan composition PUBTATOR interleukin-22 50616 The N-glycan on Asn54 affects the atypical N-glycan composition of plant-produced interleukin-22, but does not influence its activity. 26059044 0 4 gly N-glycan 4:11 arg1 Asn54 Asn54 Asn54 AminoAcid Asn54 The N-glycan on Asn54 affects the atypical N-glycan composition of plant-produced interleukin-22, but does not influence its activity. 26059044 10 9 gly glycoproteins 1597:1609 arg1 IL-22 IL-22 PUBTATOR IL-22 50616 Altogether, our data demonstrate that plants offer an excellent tool to investigate the role of N-glycosylation on folding and activity of recombinant glycoproteins, such as IL-22. 26059044 6 12 gly N-glycans 861:869 arg1 IL-22 IL-22 N-glycans PUBTATOR IL-22 50616 Surprisingly, upon engineering of human-like N-glycans on IL-22 by co-expressing mouse FUT8 in ΔXT/FT plants a strong reduction in Lewis A was observed. 26059044 9 20 gly IL-22 1367:1371 arg1 the atypical N-glycan composition IL-22 the atypical N-glycan composition PUBTATOR IL-22 50616 However, we do show that the presence of a N-glycan on Asn54 contributes to the atypical N-glycan composition of plant-produced IL-22 and influences the N-glycan composition of N-glycans on other positions. 17522223 2 1 gly sites 361:365 arg1 gp120 gp120 sites PUBTATOR gp120 3700 Here, we delineate the N-linked glycosylation (N-glycan) sites in gp120 that contribute to optimal DC-SIGN binding. 12022871 8 4 gly glycosylated 1241:1252 arg1 Human TGH Human TGH PUBTATOR Human TGH 1066 Human TGH was glycosylated in the insect cells. 17606981 3 13 gly acid 351:354 arg1 CD45 CD45 acid PUBTATOR CD45 5788 For example, loss of sialic acid from core 1 O-glycans on T-cell surface glycoproteins CD45, CD43 and CD8, detected with peanut agglutinin (PNA), is a hallmark of immature thymocytes and activated peripheral T cells. 17606981 3 13 gly acid 351:354 arg1 CD43 CD43 acid OGER CD43 P16150 For example, loss of sialic acid from core 1 O-glycans on T-cell surface glycoproteins CD45, CD43 and CD8, detected with peanut agglutinin (PNA), is a hallmark of immature thymocytes and activated peripheral T cells. 17606981 3 30 gly glycoproteins 396:408 arg1 CD45 CD45 PUBTATOR CD45 5788 For example, loss of sialic acid from core 1 O-glycans on T-cell surface glycoproteins CD45, CD43 and CD8, detected with peanut agglutinin (PNA), is a hallmark of immature thymocytes and activated peripheral T cells. 17606981 3 30 gly glycoproteins 396:408 arg1 CD43 CD43 OGER CD43 P16150 For example, loss of sialic acid from core 1 O-glycans on T-cell surface glycoproteins CD45, CD43 and CD8, detected with peanut agglutinin (PNA), is a hallmark of immature thymocytes and activated peripheral T cells. 17606981 0 47 gly glycosylation 59:71 arg1 CD45 CD45 PUBTATOR CD45 5788 T-cell activation results in microheterogeneous changes in glycosylation of CD45. 26015261 8 16 gly glycosylation 1502:1514 arg1 afucosylated anti-CS1 mAb afucosylated anti-CS1 mAb OGER CS1 O94985 Our results indicate that Fc glycosylation is critical for in vivo efficacy and afucosylated anti-CS1 mAb expressed in glycoengineered Pichia pastoris shows a better in vivo efficacy in tumor regression when compared to fucosylated anti-CS1 mAb expressed in HEK293 cells. 12901863 3 10 gly glycosylated 455:466 arg1 The human ABCC6 The human ABCC6 PUBTATOR ABCC6 368 The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells. 12901863 0 26 gly N-glycosylation 29:43 arg1 human ABCC6 human ABCC6 PUBTATOR ABCC6 368 Subcellular localization and N-glycosylation of human ABCC6, expressed in MDCKII cells. 29759137 6 3 gly IgG4 596:599 arg1 sialylation IgG4 sialylation OGER IgG4 P01861 Galactosylation and sialylation of IgG4 also differed significantly. 29759137 3 9 gly glycosylation 307:319 arg1 serum IgG serum IgG Cterm IgG Therefore, the glycosylation pattern of serum IgG is well characterized. 29759137 6 10 gly sialylation 581:591 arg1 IgG4 IgG4 OGER IgG4 P01861 Galactosylation and sialylation of IgG4 also differed significantly. 29759137 2 30 gly glycosylation 199:211 arg1 IgG IgG Cterm IgG Changes in glycosylation of IgG occur in many autoimmune diseases but also in physiological conditions. 29759137 4 40 gly glycosylation 407:419 arg1 IgG IgG Cterm IgG However, limited data is available on the glycosylation pattern of IgG in cerebrospinal fluid (CSF) compared to serum. 14693913 0 56 gly glycosylation 36:48 arg1 recombinant human bile salt-stimulated lipase recombinant human bile salt-stimulated lipase OGER bile salt-stimulated lipase P19835 Characterization of N- and O-linked glycosylation of recombinant human bile salt-stimulated lipase secreted by Pichia pastoris. 10839980 0 53 gly bis-glycosylated 74:89 arg1 bis-glycosylated human lysozyme bis-glycosylated human lysozyme PUBTATOR lysozyme 4069 Glycosylation-site-selective synthesis of N-acetyl-lactosamine repeats in bis-glycosylated human lysozyme. 29470411 9 17 gly Hypoglycosylation 1015:1031 arg1 both CaV2.1 subunits both CaV2.1 subunits PUBTATOR CaV2.1 subunits 773 Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia. 29470411 10 52 part_of α1A 1250:1252 arg1 Unoccupied N-glycosylation site N283 1A Unoccupied N-glycosylation site N283 PUBTATOR SpecificSite 1A 773 site N283 Unoccupied N-glycosylation site N283 at α1A contributes to a gain-of-function by lessening CaV2.1 inactivation. 29470411 13 58 gly N-glycosylation 1559:1573 arg1 PMM2-CDG PMM2-CDG PUBTATOR PMM2 5373 Aberrant CaV2.1 N-glycosylation as a novel pathomechanism in PMM2-CDG opens new therapeutic possibilities. 15342690 2 16 gly glycosylated 469:480 arg1 EL EL PUBTATOR EL 9388 Reduction in molecular mass of EL after treatment with glycosidases and after treatment of EL-expressing cells with the glycosylation inhibitor tunicamycin demonstrated that EL is a glycosylated protein. 15342690 0 53 gly glycosylation 17:29 arg1 endothelial lipase endothelial lipase PUBTATOR endothelial lipase 9388 Role of N-linked glycosylation in the secretion and activity of endothelial lipase. 26348848 6 16 gly glycosylated 1127:1138 arg1 Kv3.1b Kv3.1b PUBTATOR Kv3 29731 Based on particle analysis of EGFP-Kv proteins in the adhered membrane, glycosylated forms of Kv3.1a, Kv1.1, and Kv3.1b had differences in the number, size or density of Kv protein clusters in the cell membrane of neurites and cell body of B35 cells. 26348848 2 49 gly occupancy 359:367 arg1 Kv3.1b Kv3.1b PUBTATOR Kv3 29731 Recently, we showed that N-glycosylation site occupancy of Kv3.1b modulated its placement in the cell body and neurites of a neuronal-derived cell line, B35 neuroblastoma cells. 26348848 5 53 gly Kv3.1a 938:943 arg1 N-glycans Kv3 N-glycans PUBTATOR Kv3 29731 Total internal reflection fluorescence microscopy images revealed that N-glycans of Kv3.1a contributed to its placement in the cell membrane while N-glycans had no effect on the distribution of Kv1.1. 26348848 11 111 gly N-glycosylation 2012:2026 arg1 Kv3.1a Kv3.1a PUBTATOR Kv3 29731 Our study demonstrates that N-glycosylation of Kv3.1a, like Kv3.1b, provides a mechanism for the distribution of these proteins to the cell body and outgrowths and thereby can generate different voltage-dependent conductances in these membranes. 26348848 8 119 gly Kv3.1a 1502:1507 arg1 complex N-glycans Kv3 complex N-glycans PUBTATOR Kv3 29731 Cell dissociation assays revealed that cell-cell adhesion was increased by the presence of complex N-glycans of Kv3.1a, like Kv3.1b, whereas cell adhesion was similar in the oligomannose and unglycosylated Kv1.1 subunit containing B35 cells. 14759610 5 18 gly N-glycosylation 795:809 arg1 mutant yeast protein disulfide isomerase mutant yeast protein disulfide isomerase OGER protein disulfide isomerase P07237 The scFv proteins recognized NCS/T and N-glycosylation site of mutant yeast protein disulfide isomerase when they were in their native but not denatured state. 12527108 0 44 gly N-glycosylation 0:14 arg1 recombinant human fucosyltransferase III recombinant human fucosyltransferase III PUBTATOR fucosyltransferase III 2525 N-glycosylation of recombinant human fucosyltransferase III is required for its in vivo folding in mammalian and insect cells. 12773316 2 37 gly determinants 210:221 arg1 K-ATPase gastric H,K-ATPase determinants OGER gastric H,K-ATPase To identify such determinants in the gastric H,K-ATPase, fusion proteins of yellow fluorescent protein (YFP) and the gastric H,K-ATPase beta-subunit (YFP-beta) and cyan fluorescent protein (CFP) and the gastric H,K-ATPase alpha-subunit (CFP-alpha) were expressed in HEK-293 cells. 12773316 2 37 gly determinants 210:221 arg1 the gastric H gastric H,K-ATPase determinants OGER gastric H,K-ATPase To identify such determinants in the gastric H,K-ATPase, fusion proteins of yellow fluorescent protein (YFP) and the gastric H,K-ATPase beta-subunit (YFP-beta) and cyan fluorescent protein (CFP) and the gastric H,K-ATPase alpha-subunit (CFP-alpha) were expressed in HEK-293 cells. 12773316 2 37 gly determinants 210:221 arg1 the gastric H gastric H,K-ATPase beta-subunit (YFP-beta determinants PUBTATOR gastric H,K-ATPase beta-subunit (YFP-beta 496 To identify such determinants in the gastric H,K-ATPase, fusion proteins of yellow fluorescent protein (YFP) and the gastric H,K-ATPase beta-subunit (YFP-beta) and cyan fluorescent protein (CFP) and the gastric H,K-ATPase alpha-subunit (CFP-alpha) were expressed in HEK-293 cells. 16274239 3 24 gly glycosylated 627:638 arg1 N579Q N579Q PUBTATOR EGFR (N579Q) 13649 To characterize the subpopulation of receptors not glycosylated at N(579), we established a 32D cell line expressing a point mutant of the EGFR (N579Q), which cannot be glycosylated at this position. 16274239 1 57 part_of receptor 186:193 arg1 N epidermal growth factor receptor N PUBTATOR SpecificSite epidermal growth factor receptor 13649 N(579) We have investigated functional effects of glycosylation at N(579) of the epidermal growth factor receptor (EGFR). 16274239 1 57 part_of receptor 186:193 arg1 579 epidermal growth factor receptor 579 PUBTATOR SpecificSite epidermal growth factor receptor 13649 N(579) We have investigated functional effects of glycosylation at N(579) of the epidermal growth factor receptor (EGFR). 16274239 0 63 part_of receptor 78:85 arg1 Asn-579 epidermal growth factor receptor Asn-579 PUBTATOR SpecificSite epidermal growth factor receptor 13649 Asn-579 Functional effects of glycosylation at Asn-579 of the epidermal growth factor receptor. 17623277 6 67 gly monosaccharides 635:649 arg1 mosquito DCE DCE monosaccharides PUBTATOR DCE 1718 Results showed that N-acetyl D-glucosamine and D-mannose are the major monosaccharides and L-fucose, D-xylose, and D-arabinose are the minor ones in mosquito DCE. 16212939 4 55 part_of IL-1ra 822:827 arg1 Asn84 IL-1ra Asn84 PUBTATOR AminoAcid IL-1ra 3557 Asn84 The mutation of potential N-glycosylation site, by substituting Gln for either Asn7 of N-terminal 24 amino acids of hIL-1beta (Asn7Gln) or Asn84 of IL-1ra (Asn84Gln), resulted in a dramatic reduction of rhG-CSF secretion efficiency. 16212939 4 55 part_of IL-1ra 822:827 arg1 Asn7 IL-1ra Asn7 PUBTATOR AminoAcid IL-1ra 3557 Asn7 The mutation of potential N-glycosylation site, by substituting Gln for either Asn7 of N-terminal 24 amino acids of hIL-1beta (Asn7Gln) or Asn84 of IL-1ra (Asn84Gln), resulted in a dramatic reduction of rhG-CSF secretion efficiency. 14691230 3 0 gly glycosylation 628:640 arg1 DPPIV DPPIV PUBTATOR DPPIV 1803 Crystallographic studies on DPPIV reveal clear N-linked glycosylation of nine Asn residues in DPPIV. 14691230 11 11 gly glycosylation 1665:1677 arg1 ADA binding ADA binding OGER ADA P00813 Our studies indicate that glycosylation of DPPIV is not required for ADA binding. 14691230 11 11 gly glycosylation 1665:1677 arg1 DPPIV DPPIV PUBTATOR DPPIV 1803 Our studies indicate that glycosylation of DPPIV is not required for ADA binding. 14691230 0 35 gly glycosylation 9:21 arg1 dipeptidyl peptidase IV dipeptidyl peptidase IV PUBTATOR dipeptidyl peptidase IV 1803 N-linked glycosylation of dipeptidyl peptidase IV (CD26): effects on enzyme activity, homodimer formation, and adenosine deaminase binding. 14691230 0 35 gly glycosylation 9:21 arg1 CD26 CD26 PUBTATOR CD26 1803 N-linked glycosylation of dipeptidyl peptidase IV (CD26): effects on enzyme activity, homodimer formation, and adenosine deaminase binding. 14691230 6 37 gly glycosylation 1065:1077 arg1 DPPIV DPPIV PUBTATOR DPPIV 1803 Crystallographic and biochemical data demonstrate that N-linked glycosylation of DPPIV does not contribute significantly to its peptidase activity. 14691230 12 50 gly glycosylation 1806:1818 arg1 DPPIV DPPIV PUBTATOR DPPIV 1803 Taken together, these data indicate that in contrast to the generally accepted view, glycosylation of DPPIV is not a prerequisite for catalysis, dimerization, or ADA binding. 14691230 10 54 gly glycosylated 1515:1526 arg1 DPPIV DPPIV PUBTATOR DPPIV 1803 ADA binds to the highly glycosylated beta-propeller domain of DPPIV, but the impact of glycosylation on binding had not previously been determined. 14691230 2 81 gly glycosylation 433:445 arg1 DPPIV DPPIV PUBTATOR DPPIV 1803 It has been generally accepted that glycosylation of DPPIV and of other transmembrane dipeptidyl peptidases is a prerequisite for enzyme activity and correct protein folding. 14691230 2 81 gly glycosylation 433:445 arg1 other transmembrane dipeptidyl peptidases other transmembrane dipeptidyl peptidases OGER peptidases P28838 It has been generally accepted that glycosylation of DPPIV and of other transmembrane dipeptidyl peptidases is a prerequisite for enzyme activity and correct protein folding. 25707740 4 12 gly glycoprotein 452:463 arg1 hCG hCG OGER hCG Specific to humans, hCG is a complex glycoprotein composed of two glycosylated subunits. 25707740 18 23 gly glycoforms 2053:2062 arg1 hCG hCG OGER hCG Depending on its source of production, glycoforms of hCG display different biological activities and functions that are essential for pregnancy outcome. 25707740 10 50 gly hyperglycosylated 1323:1339 arg1 hCG-H hCG-H OGER hCG The invasive extravillous trophoblast also secretes hCG, and in particular like choriocarcinoma cells, hyperglycosylated forms of hCG (hCG-H). 25707740 10 50 gly hyperglycosylated 1323:1339 arg1 hCG hCG OGER hCG The invasive extravillous trophoblast also secretes hCG, and in particular like choriocarcinoma cells, hyperglycosylated forms of hCG (hCG-H). 25707740 16 71 gly glycosylated 1824:1835 arg1 Other abnormally glycosylated hCG Other abnormally glycosylated hCG OGER hCG Other abnormally glycosylated hCG are described in aneuploidies. 27834568 5 0 gly glycan 771:776 arg1 H-CDR2 CDR2 glycan PUBTATOR CDR2 1039 We show that an N-linked complex-type Fab glycan in H-CDR2 of 37E1B5 is directly involved in the inhibition of latent TGF-β activation. 20378933 9 69 gly desialylation 1394:1406 arg1 the increased IgA binding the increased IgA binding OGER IgA P11912 Furthermore, increased IgA binding was also observed on desialylated FcalphaR after neuraminidase treatment and desialylation of N58 contributed most to the increased IgA binding. 20378933 7 84 gly deglycosylation 1007:1021 arg1 IgA binding IgA binding OGER IgA P11912 Flow cytometry analysis of IgA binding to CHO cells transfected with mutated FcalphaR showed that deglycosylation of FcalphaR at individual N44, N120, N156, N165 or N177 site did not affect IgA binding but deglycosylation at N58 resulted in marked increase of IgA binding. 12626422 6 7 gly glycoforms 1235:1244 arg1 alpha1-antitrypsin alpha1-antitrypsin PUBTATOR alpha1-antitrypsin 5265 It was found that asparagine 46 was always glycosylated and that asparagine 83 was never glycosylated in the underglycosylated glycoforms of alpha1-antitrypsin. 12626422 5 22 gly underglycosylated 947:963 arg1 alpha1-antitrypsin alpha1-antitrypsin PUBTATOR alpha1-antitrypsin 5265 The state of glycosylation of the three asparagine residues was analyzed in all the underglycosylated forms of alpha1-antitrypsin by peptide mass fingerprinting using matrix-assisted laser desorption ionization time-of-flight mass spectrometry. 12626422 0 36 gly underglycosylation 4:21 arg1 plasma alpha 1-antitrypsin plasma alpha 1-antitrypsin PUBTATOR alpha 1-antitrypsin 5265 The underglycosylation of plasma alpha 1-antitrypsin in congenital disorders of glycosylation type I is not random. 12626422 6 54 gly underglycosylated 1217:1233 arg1 alpha1-antitrypsin alpha1-antitrypsin PUBTATOR alpha1-antitrypsin 5265 It was found that asparagine 46 was always glycosylated and that asparagine 83 was never glycosylated in the underglycosylated glycoforms of alpha1-antitrypsin. 12626422 4 64 gly glycosylated 757:768 arg1 alpha1-antitrypsin alpha1-antitrypsin PUBTATOR alpha1-antitrypsin 5265 Human plasma alpha1-antitrypsin is normally fully glycosylated at three asparagine residues (46, 83, and 247), but un-, mono-, di-, and fully glycosylated forms of alpha1-antitrypsin were detected by 2D PAGE in the plasma from patients with CDG-I. 12626422 7 67 gly underglycosylated 1379:1395 arg1 alpha1-antitrypsin alpha1-antitrypsin PUBTATOR alpha1-antitrypsin 5265 This showed that the asparagine residues are preferentially glycosylated in the order 46>247>83 in the mature underglycosylated forms of alpha1-antitrypsin found in plasma. 12626422 4 70 gly glycosylated 665:676 arg1 Human plasma alpha1-antitrypsin Human plasma alpha1-antitrypsin PUBTATOR alpha1-antitrypsin 5265 Human plasma alpha1-antitrypsin is normally fully glycosylated at three asparagine residues (46, 83, and 247), but un-, mono-, di-, and fully glycosylated forms of alpha1-antitrypsin were detected by 2D PAGE in the plasma from patients with CDG-I. 23316195 0 23 gly glycosylation 42:54 arg1 PTX3 functions PTX3 functions PUBTATOR PTX3 5806 The "sweet" side of a long pentraxin: how glycosylation affects PTX3 functions in innate immunity and inflammation. 18815274 9 9 gly glycosylated 1250:1261 arg1 SV2A SV2A PUBTATOR SV2A 64051 Together, the data reported here demonstrate that glycosylated SV2A and SV2B act in conjunction with gangliosides to mediate the entry of BoNT/E into neurons. 9030779 0 59 gly N-glycosylation 35:49 arg1 human acid sphingomyelinase human acid sphingomyelinase PUBTATOR acid sphingomyelinase 6609 Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis. 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. 28531887 11 35 gly N-glycosylation 1425:1439 arg1 MT4-MMP MT4-MMP PUBTATOR MT4-MMP 4326 Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP. 28531887 11 45 part_of MT4-MMP 1449:1455 arg1 Asn318 MT4-MMP Asn318 PUBTATOR AminoAcid MT4-MMP 4326 Asn318 Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP. 23776650 8 2 gly glycosylation 1037:1049 arg1 the DCIR the DCIR PUBTATOR DCIR 50856 Nevertheless, altering the glycosylation status of the DCIR expressing cell or mutating the N-glycosylation site of DCIR itself did not increase glycan binding. 23776650 3 21 gly Immunoreceptor 447:460 arg1 glycan specificity Dendritic Cell Immunoreceptor glycan specificity OGER Dendritic Cell Immunoreceptor Q9UMR7 Little is known on the glycan specificity and ligands of the Dendritic Cell Immunoreceptor (DCIR), the only classical C-type lectin that contains an intracellular immunoreceptor tyrosine-based inhibitory motif (ITIM). 23776650 8 41 gly N-glycosylation 1102:1116 arg1 DCIR itself DCIR itself PUBTATOR DCIR 50856 Nevertheless, altering the glycosylation status of the DCIR expressing cell or mutating the N-glycosylation site of DCIR itself did not increase glycan binding. 23776650 7 42 gly present 936:942 arg1 purified DCIR AND the glycans purified DCIR the glycans PUBTATOR DCIR 50856 Removing or truncating the glycans present on purified DCIR increased the affinity for DCIR-binding glycans. 23776650 10 61 gly glycosylation 1388:1400 arg1 DCIR DCIR PUBTATOR DCIR 50856 These results show that glycan binding to DCIR is influenced by the glycosylation of the CRD region in DCIR and that interaction with its ligands result in signaling via its ITIM motif. 10211957 1 19 gly glycoproteins 237:249 arg1 E1 E1 Cterm E1 The hepatitis C virus (HCV) genome encodes two membrane-associated envelope glycoproteins (E1 and E2), which are released from the viral polyprotein precursor by host signal peptidase cleavages. 10211957 3 30 gly glycoproteins 482:494 arg1 E1 E1 Cterm E1 HCV glycoproteins, E1 and E2, are heavily modified by N-linked glycosylation. 10211957 0 56 gly glycosylation 16:28 arg1 hepatitis C virus (HCV) glycoprotein E1 hepatitis C virus (HCV) glycoprotein E1 Cterm E1 Analysis of the glycosylation sites of hepatitis C virus (HCV) glycoprotein E1 and the influence of E1 glycans on the formation of the HCV glycoprotein complex. 10211957 4 82 gly glycosylation 673:685 arg1 HCV glycoprotein E1 HCV glycoprotein E1 Cterm E1 A recent study has revealed that upon partial deglycosylation with endoglycosidase H only four of the five potential glycosylation sites of HCV glycoprotein E1 are utilized. 11258925 3 28 gly glycosylation 348:360 arg1 recombinant COX-2 recombinant COX-2 PUBTATOR COX-2 4513 This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa. 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. 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. 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. 11251288 11 97 gly glycosylated 2326:2337 arg1 Erythropoietin Erythropoietin PUBTATOR Erythropoietin 2056 CONCLUSIONS: Erythropoietin expressed in E. coli bearing specific Asn-->Cys mutations at natural glycosylation sites can be glycosylated using beta-N-glycosyl iodoacetamides even in the presence of two disulfide bonds. 11251288 6 104 gly glycoprotein 1192:1203 arg1 the glycoprotein hormone erythropoietin the glycoprotein hormone erythropoietin PUBTATOR erythropoietin 2056 Here, we have shown that the approach can be applied to the glycoprotein hormone erythropoietin, an important therapeutic glycoprotein with three sites of N-glycosylation that are essential for in vivo biological activity. 11251288 0 108 gly glycoforms 94:103 arg1 human erythropoietin human erythropoietin PUBTATOR erythropoietin 2056 Selective in vitro glycosylation of recombinant proteins: semi-synthesis of novel homogeneous glycoforms of human erythropoietin. 16125194 6 8 gly non-glycosylated 1250:1265 arg1 The non-glycosylated recombinant cathepsin B The non-glycosylated recombinant cathepsin B OGER cathepsin B P07858 The non-glycosylated recombinant cathepsin B migrated as a single band of 39 kDa on SDS-PAGE. 16125194 5 13 gly non-glycosylated 1128:1143 arg1 a non-glycosylated mutant form a non-glycosylated mutant form OGER form of cathepsin B P07858 To avoid this non-specific reactivity, a non-glycosylated mutant form of cathepsin B, engineered by disrupting its potential glycosylation site, was produced. 16125194 5 13 gly non-glycosylated 1128:1143 arg1 cathepsin B cathepsin B OGER form of cathepsin B P07858 To avoid this non-specific reactivity, a non-glycosylated mutant form of cathepsin B, engineered by disrupting its potential glycosylation site, was produced. 16125194 3 69 gly glycosylated 721:732 arg1 recombinant wild-type cathepsin B recombinant wild-type cathepsin B OGER cathepsin B P07858 However, when produced in P. pastoris we found that recombinant wild-type cathepsin B was preferentially secreted as a heterogeneously glycosylated molecule that migrated at 39 kDa, 41 kDa and a smear of >50 kDa on SDS-PAGE, and was susceptible to treatment with Endo H and PGNase F. 11015576 1 1 gly glycoprotein 151:162 arg1 Fibroblast growth factor receptor 3 Fibroblast growth factor receptor 3 PUBTATOR Fibroblast growth factor receptor 3 2261 Fibroblast growth factor receptor 3 (FGFR3) is a glycoprotein that belongs to the family of tyrosine kinase receptors. 11093789 5 6 gly residues 960:967 arg1 20 20 20 SpecificSite Asn(20) Using ligand cross-linking studies in stable mutants expressed in Balb 3T3 cells, all four potential extracellular sites were glycosylated with carbohydrate residues of approximately 13 kDa on Asn(5), 10 kDa on Asn(20), 5 kDa on Asn(24), and 9 kDa on Asn(191). 11093789 5 6 gly residues 960:967 arg1 Asn Asn Asn SpecificSite Asn(24) Using ligand cross-linking studies in stable mutants expressed in Balb 3T3 cells, all four potential extracellular sites were glycosylated with carbohydrate residues of approximately 13 kDa on Asn(5), 10 kDa on Asn(20), 5 kDa on Asn(24), and 9 kDa on Asn(191). 11093789 5 6 gly residues 960:967 arg1 24 24 24 SpecificSite Asn(24) Using ligand cross-linking studies in stable mutants expressed in Balb 3T3 cells, all four potential extracellular sites were glycosylated with carbohydrate residues of approximately 13 kDa on Asn(5), 10 kDa on Asn(20), 5 kDa on Asn(24), and 9 kDa on Asn(191). 11093789 5 6 gly residues 960:967 arg1 Asn Asn Asn SpecificSite Asn(191) Using ligand cross-linking studies in stable mutants expressed in Balb 3T3 cells, all four potential extracellular sites were glycosylated with carbohydrate residues of approximately 13 kDa on Asn(5), 10 kDa on Asn(20), 5 kDa on Asn(24), and 9 kDa on Asn(191). 11093789 5 6 gly residues 960:967 arg1 Asn Asn Asn SpecificSite Asn(5) Using ligand cross-linking studies in stable mutants expressed in Balb 3T3 cells, all four potential extracellular sites were glycosylated with carbohydrate residues of approximately 13 kDa on Asn(5), 10 kDa on Asn(20), 5 kDa on Asn(24), and 9 kDa on Asn(191). 11093789 5 6 gly residues 960:967 arg1 191 191 191 SpecificSite Asn(191) Using ligand cross-linking studies in stable mutants expressed in Balb 3T3 cells, all four potential extracellular sites were glycosylated with carbohydrate residues of approximately 13 kDa on Asn(5), 10 kDa on Asn(20), 5 kDa on Asn(24), and 9 kDa on Asn(191). 11093789 5 6 gly residues 960:967 arg1 5 5 5 SpecificSite Asn(5) Using ligand cross-linking studies in stable mutants expressed in Balb 3T3 cells, all four potential extracellular sites were glycosylated with carbohydrate residues of approximately 13 kDa on Asn(5), 10 kDa on Asn(20), 5 kDa on Asn(24), and 9 kDa on Asn(191). 11093789 5 6 gly residues 960:967 arg1 Asn Asn Asn SpecificSite Asn(20) Using ligand cross-linking studies in stable mutants expressed in Balb 3T3 cells, all four potential extracellular sites were glycosylated with carbohydrate residues of approximately 13 kDa on Asn(5), 10 kDa on Asn(20), 5 kDa on Asn(24), and 9 kDa on Asn(191). 11093789 0 102 gly Glycosylation 0:12 arg1 the gastrin-releasing peptide receptor the gastrin-releasing peptide receptor PUBTATOR gastrin-releasing peptide receptor 14829 Glycosylation of the gastrin-releasing peptide receptor and its effect on expression, G protein coupling, and receptor modulatory processes. 8806496 0 66 gly glycosylation 28:40 arg1 the yellow fever virus NS1 protein the yellow fever virus NS1 protein PUBTATOR NS1 protein 10625 Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: effects on virus replication and mouse neurovirulence. 30213862 0 43 gly CD16a 0:4 arg1 oligomannose-type N-glycans CD16a oligomannose-type N-glycans PUBTATOR CD16a 2214 CD16a with oligomannose-type N-glycans is the only "low affinity" Fc γ receptor that binds the IgG crystallizable fragment with high affinity in vitro. 23319596 10 10 gly hLOXL2 1578:1583 arg1 the N-glycan at Asn-644 hLOXL2 the N-glycan at Asn-644 PUBTATOR hLOXL2 4017 These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain. 21750110 1 52 gly N-glycosylation 189:203 arg1 seipin/BSCL2 seipin/BSCL2 PUBTATOR BSCL2 14705 Heterozygosity for mutations (N88S and P90L) in the N-glycosylation site of seipin/BSCL2 is associated with the autosomal dominant motor neuron diseases, spastic paraplegia 17 and distal hereditary motor neuropathy type V, referred to as 'seipinopathies'. 8870657 1 3 gly glycoprotein 164:175 arg1 Human lactoferrin Human lactoferrin OGER Human lactoferrin P02788 Human lactoferrin (hLF) is a glycoprotein involved in the host defence against infection and excessive inflammation. 8870657 12 4 gly unglycosylated 1428:1441 arg1 unglycosylated hLF unglycosylated hLF PUBTATOR hLF 3131 The pronounced degradation of unglycosylated hLF in supernatant after mutation at all three glycosylation sites (Asn138/479/624 mutant) but not after mutation at both Asn138 and Asn479 suggests that an altered conformation rather than the lack of glycosylation has rendered the Asn138/479/624 mutant susceptible to intra- and/or extra-cellular degradation. 8870657 9 11 gly glycosylation 1115:1127 arg1 natural hLF natural hLF PUBTATOR hLF 3131 29% and 40% of Asn479 and Asn138/479 mutant molecules respectively, which indicates that glycosylation at Asn624 in natural hLF might be limited by glycosylation at Asn479. 8870657 10 39 gly unglycosylated 1230:1243 arg1 unglycosylated hLF unglycosylated hLF PUBTATOR hLF 3131 The presence in supernatant of unglycosylated hLF (approx. 8870657 5 48 gly glycosylation 751:763 arg1 hLF hLF PUBTATOR hLF 3131 Comparative SDS/PAGE analyses of rhLF, mutated rhLF and human-milk-derived (natural) hLF led us to propose that glycosylation of hLF occurs at two sites (at Asn138 and Asn479) in approx. 8870657 11 58 gly glycosylation 1327:1339 arg1 hLF hLF PUBTATOR hLF 3131 60% of the total) after mutations of Asn138 and Asn479 suggests that glycosylation of hLF is not an absolute requirement for its secretion. 23808883 5 18 gly sialylated 765:774 arg1 sialylated IgGs sialylated IgGs Cterm IgGs In contrast, it has been shown that sialylated IgGs are responsible for anti-inflammatory effects of intravenous immunoglobulin (IVIG; purified IgG from pooled human plasma), which is administered at high doses (2 g/kg) for the systemic treatment of autoimmune patients. 23808883 8 36 gly sialylated 1465:1474 arg1 antigen-specific galactosylated and sialylated IgGs antigen-specific galactosylated and sialylated IgGs Cterm IgGs Therefore, antigen-specific galactosylated and sialylated IgGs may be a promising therapeutic tool for re-establishing tolerance against defined (self-) antigens in autoimmune or allergic patients. 23808883 6 55 gly sialylated 1211:1220 arg1 immunosuppressive galactosylated and sialylated IgGs immunosuppressive galactosylated and sialylated IgGs Cterm IgGs It has become increasingly evident that pro-inflammatory immune responses, such as autoimmune reactions, primarily induce antigen-specific G0 IgGs, whereas tolerance induces immunosuppressive galactosylated and sialylated IgGs. 23808883 7 71 gly glycosylated 1275:1286 arg1 differentially glycosylated IgGs differentially glycosylated IgGs Cterm IgGs Under physiological conditions, differentially glycosylated IgGs mediate their pro- or anti-inflammatory effector functions obviously as immune complexes (IC) in an antigen-specific manner. 17015441 4 29 gly glycosylated 573:584 arg1 Unmodified TRPM8 Unmodified TRPM8 PUBTATOR Unmodified TRPM8 Q7Z2W7 Unmodified TRPM8 migrates with an apparent mass of 129 kDa and can be glycosylated in Chinese hamster ovary cells to give glycoproteins with apparent masses of 136 and 147 kDa. 17015441 1 47 gly glycosylation 118:130 arg1 mouse TRPM8 mouse TRPM8 PUBTATOR TRPM8 Q7Z2W7 We have investigated the glycosylation, disulfide bonding, and subunit structure of mouse TRPM8. 21673010 7 57 gly hormone 1015:1021 arg1 two N-glycan sites growth hormone two N-glycan sites PUBTATOR growth hormone 81668 For this purpose, rat growth hormone (rGH) with two N-glycan sites (rGH-2N) inserted into the rGH portion (NAS and NFT) was fused to green fluorescent protein (GFP) and expressed in MDCK cells. 28935113 9 64 gly oligosaccharides 1532:1547 arg1 the HIV envelope glycoprotein gp120 gp120 oligosaccharides PUBTATOR gp120 155971 The target described here is the HIV broadly neutralizing monoclonal antibody 2G12; 2G12 binds to cluster of high-mannose oligosaccharides on the HIV envelope glycoprotein gp120; and glycopeptides that mimic this epitope may be useful in HIV vaccine applications. 22122935 1 27 gly glycoforms 271:280 arg1 rhEPO rhEPO OGER rhEPO P29676 Capillary electrophoresis electrospray-mass spectrometry was used to detect and characterize the great variety of O- and N-glycopeptide glycoforms of recombinant human erythropoietin (rhEPO) using an orthogonal accelerating time-of-flight mass spectrometer to obtain their exact molecular masses (CE-TOF-MS). 22122935 1 27 gly glycoforms 271:280 arg1 recombinant human erythropoietin recombinant human erythropoietin PUBTATOR erythropoietin 2056 Capillary electrophoresis electrospray-mass spectrometry was used to detect and characterize the great variety of O- and N-glycopeptide glycoforms of recombinant human erythropoietin (rhEPO) using an orthogonal accelerating time-of-flight mass spectrometer to obtain their exact molecular masses (CE-TOF-MS). 17634239 0 24 gly modifications 16:28 arg1 gp120 gp120 modifications PUBTATOR gp120 155971 N-linked glycan modifications in gp120 of human immunodeficiency virus type 1 subtype C render partial sensitivity to 2G12 antibody neutralization. 20506028 3 29 gly nonglycosylated 476:490 arg1 NG-hChM-I NG-hChM-I PUBTATOR hChM-I 11061 We generated a nonglycosylated recombinant human ChM-I (NG-hChM-I) and compared its bioactivity with that of the glycosylated form of human ChM-I (G-hChM-I) expressed in Chinese hamster ovary cells in vitro. 20506028 3 29 gly nonglycosylated 476:490 arg1 a nonglycosylated recombinant human ChM-I a nonglycosylated recombinant human ChM-I PUBTATOR ChM-I 11061 We generated a nonglycosylated recombinant human ChM-I (NG-hChM-I) and compared its bioactivity with that of the glycosylated form of human ChM-I (G-hChM-I) expressed in Chinese hamster ovary cells in vitro. 20506028 3 44 gly glycosylated 574:585 arg1 G-hChM-I G-hChM-I PUBTATOR hChM-I 11061 We generated a nonglycosylated recombinant human ChM-I (NG-hChM-I) and compared its bioactivity with that of the glycosylated form of human ChM-I (G-hChM-I) expressed in Chinese hamster ovary cells in vitro. 20506028 3 44 gly glycosylated 574:585 arg1 human ChM-I human ChM-I PUBTATOR ChM-I 11061 We generated a nonglycosylated recombinant human ChM-I (NG-hChM-I) and compared its bioactivity with that of the glycosylated form of human ChM-I (G-hChM-I) expressed in Chinese hamster ovary cells in vitro. 20506028 1 48 gly glycoprotein 114:125 arg1 Chondromodulin-I Chondromodulin-I PUBTATOR Chondromodulin-I 11061 Chondromodulin-I (ChM-I) is a 25-kDa glycoprotein that specifically localizes in the extracellular matrix of cartilage and negatively regulates angiogenesis. 20506028 0 65 gly glycosylated 25:36 arg1 chondromodulin-I chondromodulin-I PUBTATOR chondromodulin-I 11061 A functional role of the glycosylated N-terminal domain of chondromodulin-I. 28303575 10 7 gly n-glycosylation 1220:1234 arg1 Dectin-1 Dectin-1 PUBTATOR Dectin-1 64581 We show here that n-glycosylation of Dectin-1 is crucial for its cell surface expression and consequently signal transduction. 18707900 0 10 gly N-glycosylation 51:65 arg1 recombinant IgGs recombinant IgGs Cterm IgGs Comparison of LC and LC/MS methods for quantifying N-glycosylation in recombinant IgGs. 12356334 5 10 gly glycosylation 780:792 arg1 the SP-B variant the SP-B variant PUBTATOR SP-B variant 6439 The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile). 12356334 6 36 gly glycosylated 982:993 arg1 the C allele SP-B variant the C allele SP-B variant PUBTATOR SP-B variant 6439 To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies. 11595658 0 38 gly N-glycosylation 0:14 arg1 CRF receptor type 1 CRF receptor type 1 PUBTATOR CRF receptor type 1 1394 N-glycosylation of CRF receptor type 1 is important for its ligand-specific interaction. 12175915 7 66 gly deglycosylated 1516:1529 arg1 deglycosylated RFC-Gln deglycosylated RFC-Gln PUBTATOR SpecificSite RFC 6573 Insertion of a consensus N-glycosylation site [NX(S/T)] into putative loops 5/6, 8/9, and 9/10 of deglycosylated RFC-Gln(58) had minimal effects on MTX transport. 12175915 7 80 part_of RFC-Gln 1531:1537 arg1 deglycosylated RFC-Gln RFC deglycosylated RFC-Gln PUBTATOR SpecificSite RFC 6573 Gln(58) Insertion of a consensus N-glycosylation site [NX(S/T)] into putative loops 5/6, 8/9, and 9/10 of deglycosylated RFC-Gln(58) had minimal effects on MTX transport. 22407978 0 15 gly aglycosylated 61:73 arg1 aglycosylated immunoglobulin G1 aglycosylated immunoglobulin G1 Cterm immunoglobulin G1 Avidity confers FcγR binding and immune effector function to aglycosylated immunoglobulin G1. 22407978 7 64 gly aglycosylated 1221:1233 arg1 aglycosylated IgGs aglycosylated IgGs Cterm IgGs We show here that under in vitro conditions, which allowed avidity binding, aglycosylated IgGs can bind to one of the FcγRs, FcγRI, and mediate effector functions. 20067810 3 14 gly glycosylated 539:550 arg1 glycosylated hPRL glycosylated hPRL PUBTATOR hPRL 5617 Although the biological activity of glycosylated hPRL (G-hPRL) has been found to be approximately 4-fold lower than that of hPRL, its physiological function is not yet well defined. 20067810 3 14 gly glycosylated 539:550 arg1 G-hPRL G-hPRL PUBTATOR hPRL 5617 Although the biological activity of glycosylated hPRL (G-hPRL) has been found to be approximately 4-fold lower than that of hPRL, its physiological function is not yet well defined. 20067810 0 73 gly glycosylated 60:71 arg1 G-hPRL G-hPRL PUBTATOR hPRL 5617 Synthesis, purification and characterization of recombinant glycosylated human prolactin (G-hPRL) secreted by cycloheximide-treated CHO cells. 20067810 0 73 gly glycosylated 60:71 arg1 recombinant glycosylated human prolactin recombinant glycosylated human prolactin PUBTATOR prolactin 5617 Synthesis, purification and characterization of recombinant glycosylated human prolactin (G-hPRL) secreted by cycloheximide-treated CHO cells. 24632142 5 32 gly glycosylated 913:924 arg1 recombinantly-expressed human aspartoacylase recombinantly-expressed human aspartoacylase OGER aspartoacylase P45381 A more extensive study specifically designed to resolve this discrepancy has now shown that recombinantly-expressed human aspartoacylase is not glycosylated, but is still fully functional and stable even when produced from a bacterial expression system. 9925876 13 23 gly glycosylation 1672:1684 arg1 HERG HERG PUBTATOR HERG 3757 Taken together, these results strongly suggest that N-linked glycosylation is required for surface membrane expression of HERG. 17671839 9 53 gly glycosylations 1398:1411 arg1 GP5 GP5 PUBTATOR GP5 P40197 It indicated that glycosylations of GP5 at residues N30, N33, N44 and N51 are critical for induction of neutralizing antibodies. 15823038 5 13 gly glycosylation 858:870 arg1 LRP folding LRP folding PUBTATOR LRP 4035 The roles of N-linked glycosylation and the lectin chaperone, calnexin, in LRP folding were further dissected using LRP minireceptors that carry mutations at individual glycosylation sites. 21196036 0 15 gly glycoprotein 76:87 arg1 goat oviduct-specific glycoprotein goat oviduct-specific glycoprotein OGER oviduct-specific glycoprotein Q12889 Purification, sequence characterization and effect of goat oviduct-specific glycoprotein on in vitro embryo development. 21196036 1 34 gly glycoprotein 138:149 arg1 oviductin oviductin OGER oviductin Q12889 Oviduct-specific glycoprotein (oviductin) plays an important role during fertilization and early embryonic development. 21196036 1 34 gly glycoprotein 138:149 arg1 Oviduct-specific glycoprotein Oviduct-specific glycoprotein OGER Oviduct-specific glycoprotein Q12889 Oviduct-specific glycoprotein (oviductin) plays an important role during fertilization and early embryonic development. 9442070 3 15 gly glycosylation 479:491 arg1 IgA1 IgA1 OGER IgA1 P01876 In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants. 9442070 13 46 gly Fc 2176:2177 arg1 sialylation IgA1 Fc sialylation OGER IgA1 Fc P01876 The accessibility of the Cα 2 N-glycans provides an explanation for the increased sialylation and galactosylation of IgA1 Fc over that of IgG Fc N-glycans, which are confined in the space between the two Cγ 2 domains. 9442070 2 52 gly glycosylation 316:328 arg1 IgG IgG Cterm IgG In contrast to IgA1, the glycosylation of IgG has been well characterized, and its interaction with various Fc receptors (Fc Rs) has been well studied. 9442070 0 60 gly glycosylation 4:16 arg1 human serum IgA1 human serum IgA1 OGER IgA1 P01876 The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions. 9442070 5 66 gly N-glycans 825:833 arg1 IgA1 IgA1 N-glycans OGER IgA1 P01876 Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid. 9442070 7 68 gly attached 1128:1135 arg1 recombinant IgA1 AND the N-glycans recombinant IgA1 the N-glycans OGER IgA1 P01876 Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures. 9442070 5 77 gly IgA1 838:841 arg1 the N-glycans IgA1 the N-glycans OGER IgA1 P01876 Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid. 9442070 13 93 gly sialylation 2136:2146 arg1 IgA1 Fc IgA1 Fc OGER IgA1 Fc P01876 The accessibility of the Cα 2 N-glycans provides an explanation for the increased sialylation and galactosylation of IgA1 Fc over that of IgG Fc N-glycans, which are confined in the space between the two Cγ 2 domains. 9442070 12 117 gly N-glycans 1984:1992 arg1 IgA1 Fc IgA1 Fc N-glycans OGER IgA1 Fc P01876 As a consequence of both the primary sequence and S-S bond pattern, the N-glycans in IgA1 Fc are not confined within the inter-α-chain space. 21172408 1 3 gly glycoprotein 179:190 arg1 Tissue factor Tissue factor PUBTATOR Tissue factor 2152 BACKGROUND: Tissue factor (TF) is a single polypeptide integral membrane glycoprotein composed of 263 residues and is essential to life in its role as the initiator of blood coagulation. 21172408 0 74 gly factor 98:103 arg1 carbohydrates tissue factor carbohydrates OGER tissue factor P13726 Differences in the fractional abundances of carbohydrates of natural and recombinant human tissue factor. 21172408 8 81 gly glycosylation 964:976 arg1 the natural placental TF the natural placental TF Cterm TF 2152 Carbohydrate fractional abundance at Asn11 revealed that glycosylation in the natural placental TF is much more prevalent (~76%) than in the recombinant protein (~20%). 10970800 10 73 gly glycosylation 1381:1393 arg1 the EP3beta receptor the EP3beta receptor PUBTATOR EP3beta receptor 64184 Therefore, glycosylation of the EP3beta receptor seems not to be necessary for correct folding of the receptor protein but for the efficient transport of the receptor protein to the plasma membrane. 10970800 0 83 gly N-glycosylation 15:29 arg1 the prostaglandin E2 receptor EP3beta the prostaglandin E2 receptor EP3beta PUBTATOR EP3beta 64184 Requirement of N-glycosylation of the prostaglandin E2 receptor EP3beta for correct sorting to the plasma membrane but not for correct folding. 10191272 6 74 gly N-glycosylation 1580:1594 arg1 the AT1 receptor expression the AT1 receptor expression Cterm AT1 These results demonstrate that N-glycosylation is required for the AT1 receptor expression. 10905635 2 59 gly N-glycosylation 300:314 arg1 the mouse beta1,3galactosyltransferase the mouse beta1,3galactosyltransferase OGER beta1,3galactosyltransferase Q9NS00 Here we examined the occupancy and relevance for the activity and intracellular trafficking of the only potential N-glycosylation site of the mouse beta1,3galactosyltransferase (Gal-T2 or GA1/GM1/GD1b synthase) in Gal-T2 cDNA transfected CHO-K1 cells. 24806200 0 62 gly glycoprotein 96:107 arg1 glycoprotein hormones glycoprotein hormones PUBTATOR chorionic gonadotropin (hCG) glycoprotein 93659 Chemical synthesis of the β-subunit of human luteinizing (hLH) and chorionic gonadotropin (hCG) glycoprotein hormones. 17082223 8 41 gly Bsep 1644:1647 arg1 one glycan Bsep one glycan PUBTATOR Bsep 83569 To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans. 17082223 1 67 gly glycosylation 185:197 arg1 the bile salt export pump [Bsep the bile salt export pump [Bsep OGER bile salt export pump O70127 The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)]. 15341529 5 71 gly glycosylation 726:738 arg1 the mOR-EG the mOR-EG PUBTATOR mOR-EG 117004 Disruption of the N-terminal glycosylation site of the mOR-EG completely impaired its membrane trafficking to the cell surface. 27177499 17 34 gly glycoforms 2377:2386 arg1 hCG hCG OGER hCG Depending on its source of production, glycoforms of hCG display different biological activities and functions that are essential for pregnancy outcome. 27177499 10 83 gly hyperglycosylated 1500:1516 arg1 hCG-H hCG-H OGER hCG The invasive extravillous trophoblast (iEVT) also secretes hCG, and in particular hyperglycosylated forms of hCG (hCG-H) also produced by choriocarcinoma cells. 27177499 10 83 gly hyperglycosylated 1500:1516 arg1 hCG hCG OGER hCG The invasive extravillous trophoblast (iEVT) also secretes hCG, and in particular hyperglycosylated forms of hCG (hCG-H) also produced by choriocarcinoma cells. 27177499 4 84 gly glycoprotein 575:586 arg1 hCG hCG OGER hCG Specific to humans, hCG is a complex glycoprotein composed of two highly glycosylated subunits. 10218949 2 19 gly glycosylated 492:503 arg1 the endogenous AT1-R the endogenous AT1-R PUBTATOR AT1-R 24180 All three asparagine residues (Asn4, Asn176, Asn188) contained within consensus sites for N-linked glycosylation could be glycosylated in Cos-7 cells and appeared to be glycosylated on the endogenous AT1-R in bovine adrenal glomerulosa cells. 10218949 0 49 gly glycosylation 9:21 arg1 optimal AT1a angiotensin receptor expression optimal AT1a angiotensin receptor expression PUBTATOR AT1a angiotensin 24180 N-linked glycosylation is required for optimal AT1a angiotensin receptor expression in COS-7 cells. 10218949 0 49 gly glycosylation 9:21 arg1 optimal AT1a angiotensin receptor expression optimal AT1a angiotensin receptor expression PUBTATOR AT1a angiotensin 24180 N-linked glycosylation is required for optimal AT1a angiotensin receptor expression in COS-7 cells. 23527852 1 10 gly glycoprotein 175:186 arg1 Apolipoprotein-CIII Apolipoprotein-CIII PUBTATOR Apolipoprotein-CIII 345 Apolipoprotein-CIII (apoCIII) is an abundant blood glycoprotein associated with lipoprotein particles. 23527852 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. 12527303 8 37 gly glycosylated 1385:1396 arg1 "wild-type" glycosylated IgG1-Fc "wild-type" glycosylated IgG1-Fc OGER IgG1 P01857 To investigate the influence of individual sugar (monosaccharide) residues of the oligosaccharide on the structure and function of IgG-Fc we have compared the structure of "wild-type" glycosylated IgG1-Fc with that of four glycoforms bearing consecutively truncated oligosaccharides. 12527303 0 45 gly glycoforms 36:45 arg1 human IgG-Fc glycoforms human IgG-Fc glycoforms Cterm IgG Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. 12527303 4 62 gly glycosylation 562:574 arg1 IgG-Fc IgG-Fc Cterm IgG It is established that glycosylation of IgG-Fc is essential for recognition and activation of these ligands. 9455905 2 41 gly glycosylation 519:531 arg1 human von Willebrand factor human von Willebrand factor PUBTATOR von Willebrand factor 7450 Previously, we demonstrated that the in vivo O-glycosylation of a sequence derived from a known glycosylation site of human von Willebrand factor (PHMAQVTVGPGL) was markedly reduced when charged residues were substituted at position -1 and +3 relative to the single threonine. 9455905 2 41 gly glycosylation 519:531 arg1 PHMAQVTVGPGL PHMAQVTVGPGL Cterm PHMAQVTVGPGL 7450 Previously, we demonstrated that the in vivo O-glycosylation of a sequence derived from a known glycosylation site of human von Willebrand factor (PHMAQVTVGPGL) was markedly reduced when charged residues were substituted at position -1 and +3 relative to the single threonine. 11559807 0 76 gly determinants 10:21 arg1 the coronavirus receptor aminopeptidase N aminopeptidase N determinants PUBTATOR aminopeptidase N 290 Molecular determinants of species specificity in the coronavirus receptor aminopeptidase N (CD13): influence of N-linked glycosylation. 11559807 0 76 gly determinants 10:21 arg1 CD13 CD13 determinants PUBTATOR CD13 290 Molecular determinants of species specificity in the coronavirus receptor aminopeptidase N (CD13): influence of N-linked glycosylation. 15183061 4 12 gly N-glycosylated 563:576 arg1 non-N-glycosylated or N-glycosylated CXCR4 non-N-glycosylated or N-glycosylated CXCR4 PUBTATOR N-glycosylated CXCR4 7852 Similar results were observed in binding studies using non-N-glycosylated or N-glycosylated CXCR4 expressed on cells. 15183061 2 40 gly glycosylation 221:233 arg1 CXCR4 CXCR4 PUBTATOR CXCR4 7852 We investigated the role of N-linked glycosylation in the N-terminus of CXCR4 in binding to HIV-1 gp120 envelope glycoproteins. 15183061 4 69 gly non-N-glycosylated 541:558 arg1 non-N-glycosylated or N-glycosylated CXCR4 non-N-glycosylated or N-glycosylated CXCR4 PUBTATOR N-glycosylated CXCR4 7852 Similar results were observed in binding studies using non-N-glycosylated or N-glycosylated CXCR4 expressed on cells. 9620884 1 15 gly glycoprotein 160:171 arg1 Human alpha-galactosidase A Human alpha-galactosidase A PUBTATOR Human alpha-galactosidase A 2717 Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. 2456913 8 0 part_of beta-subunits 1077:1089 arg1 Asn23 TSH beta Asn23 PUBTATOR AminoAcid TSH beta 7252 Asn23 The processing at Asn23 of TSH beta-subunits was slower than that at Asn56 or Asn82 of alpha-subunits. 2456913 0 27 gly glycosylation 75:87 arg1 mouse thyrotropin mouse thyrotropin OGER thyrotropin Rates of processing of the high mannose oligosaccharide units at the three glycosylation sites of mouse thyrotropin and the two sites of free alpha-subunits. 2456913 1 55 gly glycosylation 250:262 arg1 mouse TSH mouse TSH OGER TSH We have determined the structures of high mannose (Man) oligosaccharide units at individual glycosylation sites of mouse TSH. 2456913 10 74 gly glycosylation 1384:1396 arg1 TSH TSH OGER TSH The present study demonstrates that the early processing of oligosaccharides differs at the individual glycosylation sites of TSH and free alpha-subunits, perhaps because of local conformational differences. 9832151 7 37 gly unglycosylated 1178:1191 arg1 the unglycosylated form the unglycosylated form PUBTATOR form of rVMAT1 25693 It is interesting that in contrast to plasma-membrane neurotransmitter transporters, the unglycosylated form of rVMAT1 distributed in the cell as the wild-type protein. 9832151 7 37 gly unglycosylated 1178:1191 arg1 rVMAT1 rVMAT1 PUBTATOR form of rVMAT1 25693 It is interesting that in contrast to plasma-membrane neurotransmitter transporters, the unglycosylated form of rVMAT1 distributed in the cell as the wild-type protein. 9832151 1 43 gly N-glycosylation 180:194 arg1 rVMAT1 rVMAT1 PUBTATOR rVMAT1 25693 The role of N-glycosylation in the expression, ligand recognition, activity, and intracellular localization of a rat vesicular monoamine transporter (rVMAT1) was investigated. 9832151 1 43 gly N-glycosylation 180:194 arg1 a rat vesicular monoamine transporter a rat vesicular monoamine transporter OGER monoamine transporter Q01827 The role of N-glycosylation in the expression, ligand recognition, activity, and intracellular localization of a rat vesicular monoamine transporter (rVMAT1) was investigated. 9832151 0 76 gly Glycosylation 0:12 arg1 a vesicular monoamine transporter a vesicular monoamine transporter OGER monoamine transporter Q01827 Glycosylation of a vesicular monoamine transporter: a mutation in a conserved proline residue affects the activity, glycosylation, and localization of the transporter. 8509412 3 26 gly glycosylation 402:414 arg1 the human transferrin receptor the human transferrin receptor PUBTATOR transferrin receptor 7018 The effect of asparagine-linked glycosylation on the processing and cell surface localization of the human transferrin receptor is examined here by site-directed mutagenesis. 8509412 10 57 gly unglycosylated 1537:1550 arg1 the unglycosylated mutated transferrin receptor the unglycosylated mutated transferrin receptor PUBTATOR transferrin receptor 7018 Addition of a new glycosylation site in the C-terminal region of the unglycosylated mutated transferrin receptor restores the cell surface localization and the transferrin binding of the transferrin receptor, indicating that glycosylation in this region is critical for the correct transport of this receptor to the cell surface. 23422691 4 0 gly glycosylated 643:654 arg1 glycosylated VEGF glycosylated VEGF PUBTATOR VEGF 7422 The pre region of the mating factor α1 (MFα1) signal sequence was found to perform better than the entire MFα1 prepro signal sequence in secreting glycosylated VEGF. 23422691 2 15 gly glycoprotein 274:285 arg1 VEGF VEGF PUBTATOR VEGF 7422 VEGF is a homodimeric glycoprotein that contains one N-glycosylation site. 23422691 8 60 gly non-glycosylated 1172:1187 arg1 non-glycosylated VEGF non-glycosylated VEGF PUBTATOR VEGF 7422 Furthermore, substitution of asparagine at the VEGF glycosylation site with lysine or glutamic acid increased secretion of non-glycosylated VEGF, a finding not previously reported. 10191360 6 5 gly chains 906:911 arg1 Kv1.1 and Kv1.2 but not Kv1.4 channels Kv1.4 channels chains PUBTATOR Kv1.4 channels 3739 The extent of processing of N-linked chains on Kv1.1 and Kv1.2 but not Kv1.4 channels expressed in transfected cells differs from that seen for native brain channels, reflecting the different efficiencies of transport of K+ channel polypeptides from the endoplasmic reticulum to the Golgi apparatus. 10191360 4 10 gly N-glycosylated 634:647 arg1 Kv2.1 Kv2.1 PUBTATOR Kv2.1 3745 Kv2.1, which has a consensus site in the second extracellular interhelical domain, is not N-glycosylated. 10191360 3 86 gly N-glycosylated 483:496 arg1 Kv1.1 Kv1.1 PUBTATOR Kv1.1 3736 We find that in brain Kv1.1, Kv1.2 and Kv1.4, which have a single consensus glycosylation site in the first extracellular interhelical domain, are N-glycosylated with sialic acid-rich oligosaccharide chains. 10191360 3 86 gly N-glycosylated 483:496 arg1 Kv1.2 Kv1.2 PUBTATOR Kv1.2 3737 We find that in brain Kv1.1, Kv1.2 and Kv1.4, which have a single consensus glycosylation site in the first extracellular interhelical domain, are N-glycosylated with sialic acid-rich oligosaccharide chains. 10191360 3 86 gly N-glycosylated 483:496 arg1 Kv1.4 Kv1.4 PUBTATOR Kv1.4 3739 We find that in brain Kv1.1, Kv1.2 and Kv1.4, which have a single consensus glycosylation site in the first extracellular interhelical domain, are N-glycosylated with sialic acid-rich oligosaccharide chains. 25213400 1 0 gly glycoprotein 56:67 arg1 Human P0 Human P0 Cterm Human P0 Human P0 is the main myelin glycoprotein of the peripheral nervous system. 25213400 3 21 part_of Asn 286:288 arg1 MOG MOG Asn PUBTATOR SpecificSite MOG 4340 Asn(31) Other myelin glycoproteins, also with a single glycosylation site (PMP22 at Asn(36) , MOG at Asn(31) ), bind only one glycan. 25213400 3 73 part_of Asn 269:271 arg1 PMP22 PMP22 Asn PUBTATOR SpecificSite PMP22 5376 Asn(36) Other myelin glycoproteins, also with a single glycosylation site (PMP22 at Asn(36) , MOG at Asn(31) ), bind only one glycan. 25213400 6 80 gly linked 581:586 arg1 MOG AND the glycans MOG the glycans PUBTATOR MOG 4340 Here we review and analyze all published data on the physicochemical structure of the glycans linked to P0, PMP22, MOG, and MAG. 25213400 6 80 gly linked 581:586 arg1 P0 AND the glycans P0 the glycans Cterm P0 Here we review and analyze all published data on the physicochemical structure of the glycans linked to P0, PMP22, MOG, and MAG. 25213400 6 80 gly linked 581:586 arg1 PMP22 AND the glycans PMP22 the glycans PUBTATOR PMP22 5376 Here we review and analyze all published data on the physicochemical structure of the glycans linked to P0, PMP22, MOG, and MAG. 27339457 1 64 gly glycoprotein 160:171 arg1 Fibulin-4 Fibulin-4 PUBTATOR Fibulin-4 30008 Fibulin-4 is a 60kDa calcium binding glycoprotein that has an important role in development and integrity of extracellular matrices. 23776238 3 8 gly glycoprotein 598:609 arg1 B-cell maturation antigen B-cell maturation antigen PUBTATOR B-cell maturation antigen 608 The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42. 23776238 0 42 gly modified 29:36 arg3 B-cell maturation antigen AND a single N-glycan chain B-cell maturation antigen a single N-glycan chain PUBTATOR B-cell maturation antigen 608 B-cell maturation antigen is modified by a single N-glycan chain that modulates ligand binding and surface retention. 23776238 4 55 gly N-glycosylation 729:743 arg1 BCMA BCMA PUBTATOR BCMA 608 We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection. 12438611 7 62 gly sugars 1363:1368 arg1 gp120 gp120 sugars OGER gp120 Q14624 To further guide our efforts in mapping the DC-SIGN binding sites on gp120, we used two well-characterized HIV inhibitory agents (2G12 monoclonal antibody and cyanovirin) that bind to high-mannose sugars on gp120. 18203712 1 18 gly N-glycosylated 102:115 arg1 Cyclooxygenases Cyclooxygenases PUBTATOR Cyclooxygenases (COX-1 4512 Cyclooxygenases (COX-1 and COX-2) are N-glycosylated, endoplasmic reticulum-resident, integral membrane proteins that catalyze the committed step in prostanoid synthesis. 23341449 3 48 gly NCAM 433:436 arg1 the first fibronectin type III repeat NCAM the first fibronectin type III repeat PUBTATOR NCAM 4684 Previous work demonstrated that the first fibronectin type III repeat (FN1) of NCAM is required for polyST recognition and the polysialylation of the N-glycans on the adjacent Ig5 domain. 23341449 6 64 gly N-glycans 1013:1021 arg1 NCAM NCAM N-glycans PUBTATOR NCAM 4684 Specifically, two basic OCAM Ig5 residues (Lys and Arg) found near asparagines equivalent to those carrying the polysialylated N-glycans in NCAM substantially decrease or eliminate polysialylation when used to replace the smaller and more neutral residues (Ser and Asn) in analogous positions in NCAM Ig5. 16567801 8 19 gly proteins 1697:1704 arg1 The drastically different carbohydrate processing UPIb proteins The drastically different carbohydrate processing PUBTATOR UPIb proteins 7348 The drastically different carbohydrate processing of the UPIa and UPIb proteins, two closely related members of the tetraspanin family, may reflect differences in their folding and masking due to their interactions with their associated proteins, UPII and UPIIIa, respectively. 16567801 1 30 gly glycoprotein 193:204 arg1 mouse uroplakin (UP) Ia mouse uroplakin (UP) Ia PUBTATOR uroplakin (UP) Ia 109637 Although it has been shown that mouse uroplakin (UP) Ia, a major glycoprotein of urothelial apical surface, can serve as the receptor for the FimH lectin adhesin of type 1-fimbriated Escherichia coli, the organism that causes a great majority of urinary tract infections, the glycan structure of this native receptor was unknown. 16567801 5 34 gly UPIb 1326:1329 arg1 most terminally exposed glycans UPIb most terminally exposed glycans PUBTATOR UPIb 22268 In contrast, our results indicate that most terminally exposed glycans of mouse UPIb are non-mannose residues, thus explaining the failure of FimH to bind to this UPIb. 16567801 5 34 gly UPIb 1326:1329 arg1 non-mannose residues UPIb non-mannose residues PUBTATOR UPIb 22268 In contrast, our results indicate that most terminally exposed glycans of mouse UPIb are non-mannose residues, thus explaining the failure of FimH to bind to this UPIb. 27574189 2 17 gly ADAMTS13 254:261 arg1 the glycan composition ADAMTS13 the glycan composition PUBTATOR ADAMTS13 11093 Here, we studied the glycan composition of plasma-derived ADAMTS13. 27574189 0 25 gly glycans 18:24 arg1 plasma-derived ADAMTS13 ADAMTS13 glycans PUBTATOR ADAMTS13 11093 Identification of glycans on plasma-derived ADAMTS13. 26858738 7 28 gly O-glycans 1438:1446 arg1 plant-produced IgA1 IgA1 O-glycans PUBTATOR IgA1 P01876 By co-expression of enzymes required for initiation and elongation of human O-glycosylation it was possible to generate disialylated mucin-type core 1 O-glycans on plant-produced IgA1. 26858738 8 76 gly IgA1 1582:1585 arg1 defined human-type N- IgA1 defined human-type N- PUBTATOR IgA1 P01876 Our data demonstrate that ΔXT/FT N. benthamiana plants can be engineered toward the production of recombinant IgA1 with defined human-type N- and O-linked glycans. 26858738 8 76 gly IgA1 1582:1585 arg1 O-linked glycans IgA1 O-linked glycans PUBTATOR IgA1 P01876 Our data demonstrate that ΔXT/FT N. benthamiana plants can be engineered toward the production of recombinant IgA1 with defined human-type N- and O-linked glycans. 26858738 0 88 gly IgA1 51:54 arg1 O-Glycans IgA1 O-Glycans PUBTATOR IgA1 P01876 Transient Glyco-Engineering to Produce Recombinant IgA1 with Defined N- and O-Glycans in Plants. 26858738 0 88 gly IgA1 51:54 arg1 N- IgA1 N- PUBTATOR IgA1 P01876 Transient Glyco-Engineering to Produce Recombinant IgA1 with Defined N- and O-Glycans in Plants. 8702538 10 29 gly glycoproteins 1714:1726 arg1 the CD22 and CD33 glycoproteins the CD22 and CD33 glycoproteins PUBTATOR CD33 glycoproteins 945 These observations suggest that a single N-linked glycosylation site located at a similar position in the CD22 and CD33 glycoproteins is critical for regulating ligand recognition by both receptors. 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. 8307000 12 24 part_of GS-tPA 2480:2485 arg1 Asn117 tPA Asn117 OGER AminoAcid tPA P00750 Asn117 The relative amounts of complex-type glycans at Asn117 of GS-tPA correlated with the degree of carbohydrate substitution of Asn58. 8307000 8 46 part_of GS-tPA 1623:1628 arg1 Asn117 tPA Asn117 OGER AminoAcid tPA P00750 Asn117 In contrast, Asn117 of GS-tPA carried only small amounts (about 25%) of high-mannose and hybrid-type species and predominantly complex-type sugar chains (about 75%) which were partially incomplete and mostly devoid of fucose. 8307000 4 107 part_of YN-tPA 1366:1371 arg1 Asn117 tPA Asn117 OGER AminoAcid tPA P00750 Asn117 The results revealed that Asn117 of YN-tPA carried exclusively high-mannose-type glycans with five to nine mannose residues similar to wild-type tPA expressed in this cell line [Pfeiffer, G., Schmidt, M., Strube, K.-H. 8307000 0 118 gly Glycosylation 0:12 arg1 two recombinant human uterine tissue plasminogen activator variants two recombinant human uterine tissue plasminogen activator variants PUBTATOR tissue plasminogen activator variants P00750 Glycosylation of two recombinant human uterine tissue plasminogen activator variants carrying an additional N-glycosylation site in the epidermal-growth-factor-like domain. 23326351 5 52 gly gp120 965:969 arg1 the glycan-rich outer domain gp120 the glycan-rich outer domain PUBTATOR gp120 3700 The sera contained different neutralizing activities dependent on C3 and V5, C3 and V4, or V4 regions located on the glycan-rich outer domain of gp120. 16834341 7 2 part_of hFSH 964:967 arg1 Asn52 hFSH Asn52 OGER AminoAcid hFSH Asn52 Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site. 16834341 6 27 part_of hFSH 872:875 arg1 Asn7 hFSH Asn7 OGER AminoAcid hFSH Asn7 For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms. 16834341 3 33 gly glycopeptides 370:382 arg1 human pituitary follicle stimulating hormone human pituitary follicle stimulating hormone Cterm follicle stimulating hormone In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing. 7780197 6 35 part_of found 886:890 arg2 the TfR AND Asn-727 the TfR Asn-727 PUBTATOR SpecificSite TfR 7037 Asn-727 Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing. 7780197 0 45 gly glycosylation 13:25 arg1 human transferrin receptor human transferrin receptor PUBTATOR transferrin receptor 7037 The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide. 9365923 1 34 gly glycoprotein 157:168 arg1 Human alpha-lactalbumin Human alpha-lactalbumin PUBTATOR Human alpha-lactalbumin 3906 Human alpha-lactalbumin has not been described as a glycoprotein, despite the fact that several alpha-lactalbumins of both ruminant and nonruminant species are known to be glycosylated. 9365923 3 37 gly glycosylated 436:447 arg1 human alpha-lactalbumin human alpha-lactalbumin PUBTATOR alpha-lactalbumin 3906 We have found that human alpha-lactalbumin is glycosylated and the glycosylation site has been determined by protein sequencing and mass spectrometry. 11278567 1 3 gly glycoprotein 227:238 arg1 gp120 gp120 PUBTATOR gp120 155971 The variable V1V2 and V3 regions of the human immunodeficiency virus type-1 (HIV-1) envelope glycoprotein (gp120) can influence viral coreceptor usage. 11278567 0 12 gly CXCR4 104:108 arg1 a major determinant CXCR4 a major determinant PUBTATOR CXCR4 7852 N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization. 11278567 0 28 gly CCR5 95:98 arg1 a major determinant CCR5 a major determinant PUBTATOR CCR5 1234 N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization. 27773655 1 17 gly glycoprotein 205:216 arg1 Lactase phlorizin-hydrolase Lactase phlorizin-hydrolase PUBTATOR Lactase phlorizin-hydrolase 3938 Lactase phlorizin-hydrolase (LPH) is a membrane anchored type I glycoprotein of the intestinal epithelium that is composed of four homologous structural domains. 2082620 2 45 gly N-glycosylation 353:367 arg1 HIV-1 gp120 HIV-1 gp120 PUBTATOR gp120 155971 To address the possible role of N-glycosylation of HIV-1 gp120 in binding CD4, we mutated different conserved N-glycosylation site Asn-residues in the vicinity of the putative CD4 binding site, as single mutations or in combinations. 10764840 3 44 gly rHuEpo 542:547 arg1 the glycan chains rHuEpo the glycan chains Cterm rHuEpo 2056 The structure of the glycan chains of this rHuEpo slightly differ of those of the urinary human Epo (uHuEpo), considered as the natural Epo molecule. 10764840 0 49 gly N-glycosylation 8:22 arg1 a recombinant human erythropoietin a recombinant human erythropoietin PUBTATOR erythropoietin 2056 Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties. 14985108 3 35 gly glycosylated 423:434 arg1 gONC gONC Cterm ONC (gONC We employed the Pichia pastoris expression system to produce recombinant glycosylated ONC (gONC) protein. 14985108 3 35 gly glycosylated 423:434 arg1 glycosylated ONC glycosylated ONC Cterm ONC (gONC We employed the Pichia pastoris expression system to produce recombinant glycosylated ONC (gONC) protein. 21980282 0 78 gly glycoproteins 55:67 arg1 HIV-1 B clade envelope glycoproteins HIV-1 B clade envelope glycoproteins PUBTATOR envelope glycoproteins 155971 Recurrent signature patterns in HIV-1 B clade envelope glycoproteins associated with either early or chronic infections. 16096263 1 25 gly glycoprotein 208:219 arg1 Anion exchanger 1 Anion exchanger 1 PUBTATOR Anion exchanger 1 (AE1, or Band 3 6521 Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane. 11226831 0 23 gly Glycosylation 0:12 arg1 the murine estrogen receptor-alpha the murine estrogen receptor-alpha PUBTATOR estrogen receptor 13982 Glycosylation of the murine estrogen receptor-alpha. 3219367 5 9 gly glycosylation 593:605 arg1 human recombinant erythropoietin human recombinant erythropoietin PUBTATOR erythropoietin 2056 In order to examine the extent to which protein structure influences glycosylation, we have analyzed the saccharide structures at each glycosylation site (Asn24, Asn38, Asn83, and Ser126) of human recombinant erythropoietin. 3219367 0 35 gly glycosylation 14:26 arg1 human recombinant erythropoietin human recombinant erythropoietin PUBTATOR erythropoietin 2056 Site-specific glycosylation of human recombinant erythropoietin: analysis of glycopeptides or peptides at each glycosylation site by fast atom bombardment mass spectrometry. 8639654 11 107 gly N-glycosylation 2147:2161 arg1 the human VIP 1 receptor the human VIP 1 receptor PUBTATOR VIP 1 receptor 7432 These studies highlight the functional importance of the N-glycosylation of the human VIP 1 receptor which belongs to a new subfamily of seven membrane-spanning receptors. 21153780 8 30 gly glycosylated 1046:1057 arg1 Casein kinase II Casein kinase II OGER Casein kinase II Our computational study predicted that B cell epitope 1 was Casein kinase II phosphorylated (site No. 31) and glycosylated (site No. 29). 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. 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). 10677208 0 30 gly N-glycosylation 55:69 arg1 LTBP-1 LTBP-1 OGER LTBP-1 Q14766 Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells. 20209506 5 17 gly N-glycosylation 1213:1227 arg1 beta2-GPI beta2-GPI PUBTATOR GPI 350 A total of 23 glycan structures, including sialylated bi- and tri-antennary complex type glycans, were characterized at three N-glycosylation sites, namely Asn-143, Asn-174 and Asn-234, of beta2-GPI. 20209506 3 21 gly beta2-glycoprotein 607:624 arg1 human beta2-glycoprotein I human beta2-glycoprotein I PUBTATOR beta2-glycoprotein I 350 The glycopeptide analysis workflow was applied to human beta2-glycoprotein I (beta2-GPI, apolipoprotein H), which contains multiple N-glycosylation sites. 20209506 0 48 gly glycopeptides 47:59 arg1 beta2-glycoprotein I beta2-glycoprotein I PUBTATOR beta2-glycoprotein I 350 Characterization of sialylated and fucosylated glycopeptides of beta2-glycoprotein I by a combination of HILIC LC and MALDI MS/MS. 20209506 5 87 part_of beta2-GPI 1276:1284 arg1 Asn-234 GPI Asn-234 PUBTATOR SpecificSite GPI 350 Asn-143, Asn-174 and Asn-234 A total of 23 glycan structures, including sialylated bi- and tri-antennary complex type glycans, were characterized at three N-glycosylation sites, namely Asn-143, Asn-174 and Asn-234, of beta2-GPI. 20209506 5 87 part_of beta2-GPI 1276:1284 arg1 Asn-174 GPI Asn-174 PUBTATOR SpecificSite GPI 350 Asn-143, Asn-174 and Asn-234 A total of 23 glycan structures, including sialylated bi- and tri-antennary complex type glycans, were characterized at three N-glycosylation sites, namely Asn-143, Asn-174 and Asn-234, of beta2-GPI. 20209506 5 87 part_of beta2-GPI 1276:1284 arg1 Asn-143 GPI Asn-143 PUBTATOR SpecificSite GPI 350 Asn-143, Asn-174 and Asn-234 A total of 23 glycan structures, including sialylated bi- and tri-antennary complex type glycans, were characterized at three N-glycosylation sites, namely Asn-143, Asn-174 and Asn-234, of beta2-GPI. 20209506 0 100 gly beta2-glycoprotein 64:81 arg1 beta2-glycoprotein I beta2-glycoprotein I PUBTATOR beta2-glycoprotein I 350 Characterization of sialylated and fucosylated glycopeptides of beta2-glycoprotein I by a combination of HILIC LC and MALDI MS/MS. 20848033 3 23 gly glycoforms 407:416 arg1 distinct CD52 glycoforms distinct CD52 glycoforms PUBTATOR CD52 1043 To facilitate functional and immunological studies of distinct CD52 glycoforms, we report in this paper the first chemoenzymatic synthesis of homogeneous CD52 glycoforms carrying both N- and O-glycans. 20848033 3 45 gly glycoforms 498:507 arg1 homogeneous CD52 glycoforms homogeneous CD52 glycoforms PUBTATOR CD52 1043 To facilitate functional and immunological studies of distinct CD52 glycoforms, we report in this paper the first chemoenzymatic synthesis of homogeneous CD52 glycoforms carrying both N- and O-glycans. 20848033 6 69 gly glycoforms 1218:1227 arg1 various homogeneous CD52 glycoforms various homogeneous CD52 glycoforms PUBTATOR CD52 1043 This chemoenzymatic approach is highly convergent and permits easy construction of various homogeneous CD52 glycoforms from a common polypeptide precursor. 23527023 6 40 gly diglycosylated 1447:1460 arg1 the diglycosylated PrP the diglycosylated PrP PUBTATOR PrP Q9NP58 Furthermore, PrP(V180I) with a typical glycoform profile from cultured cells generates detectable PrP(res) that also contains the diglycosylated PrP in addition to mono- and unglycosylated forms upon PK-treatment. 23527023 4 53 gly diglycosylated 957:970 arg1 the diglycosylated PrP the diglycosylated PrP OGER PrP Q9NP58 Remarkably, the absence of the diglycosylated PrP(res) species in both fCJD(V180I) and VPSPr is likewise attributable to the absence of PrP(res) glycosylated at the first N-linked glycosylation site at residue 181, as in fCJD(T183A). 23527023 5 73 gly glycosylation 1223:1235 arg1 monoglycosylated (mono181) PrP monoglycosylated (mono181) PrP PUBTATOR PrP Q9NP58 In contrast to fCJD(T183A), both VPSPr and fCJD(V180I) exhibit glycosylation at residue 181 on di- and monoglycosylated (mono181) PrP prior to PK-treatment. 23527023 5 91 gly monoglycosylated 1263:1278 arg1 monoglycosylated (mono181) PrP monoglycosylated (mono181) PrP PUBTATOR PrP Q9NP58 In contrast to fCJD(T183A), both VPSPr and fCJD(V180I) exhibit glycosylation at residue 181 on di- and monoglycosylated (mono181) PrP prior to PK-treatment. 9694881 11 12 gly deglycosylated 1226:1239 arg1 This deglycosylated recombinant human angiotensinogen This deglycosylated recombinant human angiotensinogen PUBTATOR angiotensinogen 183 This deglycosylated recombinant human angiotensinogen could be of value for x-ray crystallography studies. 9694881 1 41 gly glycoprotein 125:136 arg1 Human angiotensinogen Human angiotensinogen PUBTATOR Human angiotensinogen 183 Human angiotensinogen, the specific substrate of renin, is a heterogeneous glycoprotein constitutively secreted by the liver. 8573180 7 33 gly glycosylation 1164:1176 arg1 GLUT4 GLUT4 PUBTATOR GLUT4 25139 Thus, in the physiologically relevant adipose cell, glycosylation of GLUT4 appears to play an important functional role. 12930842 6 54 gly IFN-alpha 882:890 arg1 IFN-alpha(psi2) transcripts IFN-alpha IFN-alpha(psi2) transcripts PUBTATOR IFN-alpha 111654 IFN-alpha(psi2) transcripts are the most abundant IFN-alpha transcripts detected in several mouse organs in the absence of viral infection. 27743357 1 9 gly N-glycosylation 188:202 arg1 IgG IgG Cterm IgG This chapter contains a nanoscale liquid chromatography-mass spectrometry method for the glycoform profiling of the conserved Fc N-glycosylation site of monoclonal and polyclonal immunoglobulin G (IgG). 27743357 1 9 gly N-glycosylation 188:202 arg1 immunoglobulin G immunoglobulin G Cterm immunoglobulin G This chapter contains a nanoscale liquid chromatography-mass spectrometry method for the glycoform profiling of the conserved Fc N-glycosylation site of monoclonal and polyclonal immunoglobulin G (IgG). 8286855 4 7 part_of Ser23 661:665 arg1 GpA GpA Ser23 PUBTATOR AminoAcid GpA 2993 Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA. 8286855 4 13 part_of Ser15 654:658 arg1 GpA GpA Ser15 PUBTATOR AminoAcid GpA 2993 Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA. 8286855 4 18 part_of Ser14 647:651 arg1 GpA GpA Ser14 PUBTATOR AminoAcid GpA 2993 Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA. 8286855 4 25 part_of Ser1 641:644 arg1 GpA GpA Ser1 PUBTATOR AminoAcid GpA 2993 Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA. 8286855 2 38 gly O-glycosylation 328:342 arg1 GpA GpA PUBTATOR GpA 2993 We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site. 8286855 1 46 gly sialoglycoprotein 144:160 arg1 glycophorin A glycophorin A PUBTATOR glycophorin A 2993 The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens. 8286855 9 49 gly glycosylation 1234:1246 arg1 GpA GpA PUBTATOR GpA 2993 These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA. 8286855 4 63 part_of Thr58 678:682 arg1 GpA GpA Thr58 PUBTATOR AminoAcid GpA 2993 Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA. 8286855 4 69 part_of Thr28 668:672 arg1 GpA GpA Thr28 PUBTATOR AminoAcid GpA 2993 Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA. 7613486 1 29 gly glycosylation 193:205 arg1 the insulin receptor the insulin receptor PUBTATOR insulin receptor 3643 Asparagine-linked glycosylation of the insulin receptor is required for complete biosynthesis and acquisition of function. 10099545 3 97 gly glycosylation 539:551 arg1 IFN-gamma IFN-gamma PUBTATOR IFN-gamma 3458 To investigate the relationship between metabolism and glycosylation site occupancy, we studied the glycosylation of recombinant human interferon-gamma (IFN-gamma) produced in continuous culture of Chinese hamster ovary cells. 10099545 3 97 gly glycosylation 539:551 arg1 recombinant human interferon-gamma recombinant human interferon-gamma PUBTATOR interferon-gamma P01579 To investigate the relationship between metabolism and glycosylation site occupancy, we studied the glycosylation of recombinant human interferon-gamma (IFN-gamma) produced in continuous culture of Chinese hamster ovary cells. 27957769 12 15 gly structures 2334:2343 arg1 MUC1 MUC1 structures OGER MUC1 P15941 All antibody sera show high reactivity to the tumor-associated saccharide structures on MUC1. 16622833 1 46 gly glycoprotein 140:151 arg1 Human alpha1-antitrypsin Human alpha1-antitrypsin PUBTATOR Human alpha1-antitrypsin 5265 Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes. 16622833 2 52 gly N-glycosylation 245:259 arg1 A1PI A1PI PUBTATOR A1PI 5265 The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI. 16622833 5 66 gly acids 733:737 arg1 glycosylation site N107 glycosylation site N107 glycosylation site N107 SpecificSite site N107 The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI. 16622833 5 74 gly antennae 707:714 arg1 glycosylation site N107 glycosylation site N107 glycosylation site N107 SpecificSite site N107 The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI. 8496193 1 0 gly glycosylation 132:144 arg1 procathepsin L procathepsin L OGER procathepsin L P06797 The role of glycosylation in the synthesis, transport, and localization of procathepsin L has been analyzed. 8496193 4 2 gly glycosylation 625:637 arg1 procathepsin L trafficking procathepsin L trafficking OGER procathepsin L P06797 To study the role of glycosylation in procathepsin L trafficking, we constructed a cDNA in which the codon for Asn-204 was mutated to encode Gln. 8496193 4 2 gly glycosylation 625:637 arg1 procathepsin L trafficking procathepsin L trafficking OGER procathepsin L P06797 To study the role of glycosylation in procathepsin L trafficking, we constructed a cDNA in which the codon for Asn-204 was mutated to encode Gln. 8496193 8 30 gly glycosylated 1239:1250 arg1 glycosylated procathepsin L glycosylated procathepsin L OGER procathepsin L P06797 Nonglycosylated and endogenous glycosylated procathepsin L were secreted by NIH 3T3 cells with identical kinetics. 8496193 9 40 gly acceptor 1406:1413 arg1 procathepsin L procathepsin L acceptor OGER procathepsin L P06797 These studies therefore confirm that Asn-204 is the normal functional carbohydrate acceptor in procathepsin L and that carbohydrate in wild-type procathepsin L serves predominantly as a lysosomal targeting signal, with little or no role in protein folding or stability. 8496193 11 47 gly glycosylation 1942:1954 arg1 procathepsin L procathepsin L OGER procathepsin L P06797 In experiments with a second mutant, the glycosylation signal at Asn-251, which normally is not utilized, was capable of serving as a carbohydrate acceptor, suggesting that there is normally a structural impediment to glycosylation at Asn-251 in procathepsin L. 8496193 9 53 gly carbohydrate 1442:1453 arg1 wild-type procathepsin L procathepsin L carbohydrate OGER procathepsin L P06797 These studies therefore confirm that Asn-204 is the normal functional carbohydrate acceptor in procathepsin L and that carbohydrate in wild-type procathepsin L serves predominantly as a lysosomal targeting signal, with little or no role in protein folding or stability. 8496193 5 68 gly nonglycosylated 822:836 arg1 a completely nonglycosylated form a completely nonglycosylated form OGER form of procathepsin L P06797 When this mutated cDNA was transfected into NIH 3T3 cells, a completely nonglycosylated form of procathepsin L was expressed. 8496193 5 68 gly nonglycosylated 822:836 arg1 procathepsin L procathepsin L OGER form of procathepsin L P06797 When this mutated cDNA was transfected into NIH 3T3 cells, a completely nonglycosylated form of procathepsin L was expressed. 10889209 6 0 gly glycosylated 1021:1032 arg1 GIRK4 GIRK4 PUBTATOR GIRK4 3762 This finding may partly account for the reason that GIRK4 is not glycosylated at Asn(132), either as a homomer or when coexpressed with GIRK1. 10889209 8 6 gly N-glycosylation 1526:1540 arg1 ROMK1 ROMK1 PUBTATOR ROMK1 3758 Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol. 10889209 8 14 gly N-glycosylation 1301:1315 arg1 GIRK1 GIRK1 PUBTATOR GIRK1 3760 Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol. 10889209 0 43 gly Glycosylation 0:12 arg1 GIRK1 GIRK1 PUBTATOR GIRK1 3760 Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function. 10889209 0 50 part_of Asn117 46:51 arg1 ROMK1 ROMK1 Asn117 PUBTATOR AminoAcid ROMK1 3758 Asn117 Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function. 10889209 4 55 gly glycosylated 655:666 arg1 GIRK1 GIRK1 PUBTATOR GIRK1 3760 Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132). 10889209 4 68 gly glycosylated 703:714 arg1 GIRK4 GIRK4 PUBTATOR GIRK4 3762 Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132). 8364023 8 41 part_of LCAT 1217:1220 arg1 Asn20-->Thr LCAT Asn20-->Thr PUBTATOR AminoAcid LCAT 3931 Asn20 The amount secreted, specific activity, and Vmax of LCAT (Asn20-->Thr) were similar to those of the wild-type LCAT. 8364023 0 53 gly N-glycosylation 44:58 arg1 human lecithin:cholesterol acyltransferase human lecithin:cholesterol acyltransferase PUBTATOR lecithin:cholesterol acyltransferase 3931 Effects of site-directed mutagenesis on the N-glycosylation sites of human lecithin:cholesterol acyltransferase. 9804815 10 9 gly glycosylation 1518:1530 arg1 MUC1 MUC1 PUBTATOR MUC1 4582 The function of GalNAc-T4 complements other GalNAc-transferases in O-glycosylation of MUC1 showing that glycosylation of MUC1 is a highly ordered process and changes in the repertoire or topology of GalNAc-transferases will result in altered pattern of O-glycan attachments. 9804815 6 19 gly glycoprotein 1117:1128 arg1 P-selectin glycoprotein ligand-1 P-selectin glycoprotein ligand-1 PUBTATOR P-selectin glycoprotein ligand-1 6404 Furthermore, GalNAc-T4 showed the best kinetic properties with an O-glycosylation site in the P-selectin glycoprotein ligand-1 molecule. 9804815 10 41 gly O-glycosylation 1481:1495 arg1 MUC1 MUC1 PUBTATOR MUC1 4582 The function of GalNAc-T4 complements other GalNAc-transferases in O-glycosylation of MUC1 showing that glycosylation of MUC1 is a highly ordered process and changes in the repertoire or topology of GalNAc-transferases will result in altered pattern of O-glycan attachments. 9210490 3 12 gly N-glycosylation 402:416 arg1 DPPIV DPPIV PUBTATOR DPPIV 25253 To investigate the role of N-glycosylation in the function of DPPIV, three of its asparagine residues were separately converted to glutamine by site-directed mutagenesis. 9210490 1 13 gly N-glycosylated 234:247 arg1 Dipeptidyl peptidase IV Dipeptidyl peptidase IV PUBTATOR Dipeptidyl peptidase IV 25253 Dipeptidyl peptidase IV (DPPIV, CD26) is an N-glycosylated type II plasma membrane protein. 9210490 0 48 gly N-glycosylation 16:30 arg1 the membrane glycoprotein dipeptidylpeptidase IV the membrane glycoprotein dipeptidylpeptidase IV PUBTATOR dipeptidylpeptidase IV 25253 Domain-specific N-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity and protein folding. 9210490 0 48 gly N-glycosylation 16:30 arg1 CD26 CD26 PUBTATOR CD26 25253 Domain-specific N-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity and protein folding. 2886334 0 13 gly Thy-1 109:113 arg1 Tissue-specific N-glycosylation, site-specific oligosaccharide patterns Thy-1 Tissue-specific N-glycosylation, site-specific oligosaccharide patterns PUBTATOR Thy-1 24832 Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1. 2886334 1 35 gly glycosylation 277:289 arg1 the cell surface glycoprotein Thy-1 the cell surface glycoprotein Thy-1 PUBTATOR Thy-1 24832 To examine the extent to which protein structure and tissue-type influence glycosylation, we have determined the oligosaccharide structures at each of the three glycosylation sites (Asn-23, 74 and 98) of the cell surface glycoprotein Thy-1 isolated from rat brain and thymus. 20371379 6 10 gly glycosylation 692:704 arg1 the recombinant protein the recombinant protein OGER protein, it P35900 In order to overcome non-native glycosylation of the recombinant protein, it was necessary to delete a glycosylation site. 3192519 9 17 gly glycosylation 1391:1403 arg1 apoCIII apoCIII PUBTATOR apoCIII 345 These findings suggest that the intracellular glycosylation of apoCIII is not required for its intracellular transport and secretion. 3192519 1 27 gly glycosylation 65:77 arg1 ApoCIII secretion ApoCIII secretion PUBTATOR ApoCIII 345 O-linked glycosylation is not required for ApoCIII secretion and lipid binding. 3192519 0 45 gly glycosylation 19:31 arg1 human ApoCIII human ApoCIII PUBTATOR ApoCIII 345 Mutagenesis of the glycosylation site of human ApoCIII. 9241750 0 119 gly glycosylation 23:35 arg1 HPS HPS OGER HPS Q08830 The effect of N-linked glycosylation on molecular weight, thrombin cleavage, and functional activity of human protein S. Human protein S (HPS) has three potential N-linked glycosylation sites at Asn458, 468, 489. 9241750 0 119 gly glycosylation 23:35 arg1 thrombin cleavage thrombin cleavage PUBTATOR thrombin 2147 The effect of N-linked glycosylation on molecular weight, thrombin cleavage, and functional activity of human protein S. Human protein S (HPS) has three potential N-linked glycosylation sites at Asn458, 468, 489. 8325864 2 31 gly N-glycosylation 134:148 arg1 human acid beta-glucosidase human acid beta-glucosidase OGER acid beta-glucosidase P04062 The five potential N-glycosylation sites (sequons) of human acid beta-glucosidase were individually mutated to determine site occupancy and the effect of site occupancy on selected catalytic and stability properties of this enzyme. 10940860 3 23 gly occupancy 472:480 arg1 t-PA t-PA OGER t-PA P00750 In this report, the site occupancy of t-PA is shown to increase gradually over the course of batch and fed-batch CHO cultures. 10940860 0 78 gly glycosylation 45:57 arg1 CHO-produced tissue-type plasminogen activator CHO-produced tissue-type plasminogen activator OGER tissue-type plasminogen activator P00750 Multiple cell culture factors can affect the glycosylation of Asn-184 in CHO-produced tissue-type plasminogen activator. 16331960 5 0 gly nonglycosylated 1028:1042 arg1 rhTf-NG rhTf-NG OGER rhTf P12346 The observed peptide fragmentation profile showed that the C-lobe of recombinant full-length nonglycosylated transferrin (rhTf-NG) appeared to be preferentially cleaved, while cleavage of the N-lobe was restricted to the N-terminal and link sequence regions. 16331960 5 0 gly nonglycosylated 1028:1042 arg1 recombinant full-length nonglycosylated transferrin recombinant full-length nonglycosylated transferrin PUBTATOR transferrin 7018 The observed peptide fragmentation profile showed that the C-lobe of recombinant full-length nonglycosylated transferrin (rhTf-NG) appeared to be preferentially cleaved, while cleavage of the N-lobe was restricted to the N-terminal and link sequence regions. 16331960 9 42 gly glycoforms 1827:1836 arg1 the different transferrin glycoforms the different transferrin glycoforms PUBTATOR transferrin 7018 After fragmentation, a range of peptides representing previously cryptic epitopes were identified as potential candidates for an immunological approach to differentiate between the different transferrin glycoforms. 16331960 3 68 gly nonglycosylated 607:621 arg1 normal glycosylated and nonglycosylated recombinant human transferrin normal glycosylated and nonglycosylated recombinant human transferrin PUBTATOR transferrin 7018 Differential susceptibility to proteolysis by chymotrypsin was demonstrated for normal glycosylated and nonglycosylated recombinant human transferrin, using reverse-phase (RP) HPLC, matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry, and LC-tandem mass spectrometry (MS/MS). 16331960 3 71 gly glycosylated 590:601 arg1 normal glycosylated and nonglycosylated recombinant human transferrin normal glycosylated and nonglycosylated recombinant human transferrin PUBTATOR transferrin 7018 Differential susceptibility to proteolysis by chymotrypsin was demonstrated for normal glycosylated and nonglycosylated recombinant human transferrin, using reverse-phase (RP) HPLC, matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry, and LC-tandem mass spectrometry (MS/MS). 16331960 0 81 gly glycoforms 43:52 arg1 transferrin glycoforms transferrin glycoforms PUBTATOR transferrin 7018 Differential susceptibility of transferrin glycoforms to chymotrypsin: a proteomics approach to the detection of carbohydrate-deficient transferrin. 10413465 6 23 part_of apoE4 1298:1302 arg1 position 158 apoE4 position 158 PUBTATOR SpecificSite apoE4 348 cysteine at position 158 In contrast, introduction of cysteine at position 158 of apoE4 (Arg112, Cys158) increased the SDS-stable binding of apoE to Abeta to the levels similar to those observed in apoE2. 10413465 5 42 gly O-glycosylation 1142:1156 arg1 Thr194-Ala Thr194-Ala Cterm Thr194-Ala 348 This analysis showed that a mutation in the O-glycosylation site of apoE2 (Thr194-Ala) did not affect the SDS-stable binding of apoE to Abeta. 10413465 5 42 gly O-glycosylation 1142:1156 arg1 apoE2 apoE2 PUBTATOR apoE2 348 This analysis showed that a mutation in the O-glycosylation site of apoE2 (Thr194-Ala) did not affect the SDS-stable binding of apoE to Abeta. 18642129 1 6 gly glycoprotein 141:152 arg1 Factor VII Factor VII OGER Factor VII P08709 Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX. 18642129 5 14 gly O-glycosylation 692:706 arg1 pd-FVII pd-FVII OGER FVII P08709 N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques. 18642129 12 16 part_of position 1702:1709 arg1 the light chain chain position OGER SpecificSite chain P08709 position Ser(60) and Ser(52) Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively. 18642129 7 20 gly N-glycosylated 1081:1094 arg1 light chain light chain OGER chain P08709 LC-ESIMS/MS analysis revealed that both light chain and heavy chain were N-glycosylated mainly by A2S2 but also by triantennary sialylated glycans. 18642129 7 20 gly N-glycosylated 1081:1094 arg1 heavy chain heavy chain OGER chain P08709 LC-ESIMS/MS analysis revealed that both light chain and heavy chain were N-glycosylated mainly by A2S2 but also by triantennary sialylated glycans. 18642129 6 30 gly glycoprotein 912:923 arg1 FVII FVII OGER FVII P08709 A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans. 18642129 0 75 gly VII 93:95 arg1 O-glycans coagulation factor VII O-glycans OGER coagulation factor VII P08709 Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII. 18642129 0 75 gly VII 93:95 arg1 N- coagulation factor VII N- OGER coagulation factor VII P08709 Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII. 18642129 12 83 gly O-glycosylated 1665:1678 arg1 FVII FVII OGER FVII P08709 Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively. 18642129 12 83 gly O-glycosylated 1665:1678 arg1 the light chain the light chain OGER chain P08709 Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively. 18642129 5 84 gly heterogeneity 732:744 arg1 pd-FVII pd-FVII OGER FVII P08709 N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques. 18642129 4 93 gly FVII 604:607 arg1 N- FVII N- OGER FVII P08709 Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site. 1331508 8 59 gly attached 1223:1230 arg1 human PVR AND sugar moieties human PVR sugar moieties PUBTATOR PVR 5817 These results suggest that domain 1 of the monkey receptor also harbors the binding site for poliovirus and that sugar moieties possibly attached to this domain of human PVR are dispensable for the virus-receptor interaction. 7613477 1 31 gly glycosylation 289:301 arg1 human lecithin human lecithin PUBTATOR lecithin:cholesterol acyltransferase 3931 Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS). 7613477 5 51 part_of LCAT 1156:1159 arg1 Asn272 LCAT Asn272 PUBTATOR AminoAcid LCAT 3931 Asn20, Asn84, Asn272, and Asn384 All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures. 7613477 5 51 part_of LCAT 1156:1159 arg1 Asn384 LCAT Asn384 PUBTATOR AminoAcid LCAT 3931 Asn20, Asn84, Asn272, and Asn384 All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures. 7613477 5 51 part_of LCAT 1156:1159 arg1 Asn84 LCAT Asn84 PUBTATOR AminoAcid LCAT 3931 Asn20, Asn84, Asn272, and Asn384 All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures. 7613477 0 59 gly glycosylation 63:75 arg1 apolipoprotein D apolipoprotein D PUBTATOR apolipoprotein D 347 Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion. 7613477 0 59 gly glycosylation 63:75 arg1 lecithin:cholesterol acyltransferase lecithin:cholesterol acyltransferase PUBTATOR lecithin:cholesterol acyltransferase 3931 Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion. 7613477 5 101 gly glycosylation 1098:1110 arg1 LCAT LCAT PUBTATOR LCAT 3931 All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures. 7613477 3 117 gly glycopeptides 793:805 arg1 LCAT LCAT PUBTATOR LCAT 3931 In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides. 1456441 9 23 gly N-glycosylation 1336:1350 arg1 h-STF h-STF Cterm h-STF 7018 Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15. 8288048 0 66 gly glycosylation 40:52 arg1 the insulin receptor alpha-subunit the insulin receptor alpha-subunit OGER subunit 3643 Mutational analysis of the NH2-terminal glycosylation sites of the insulin receptor alpha-subunit. 8435067 6 32 gly alpha-glucosidase 862:878 arg1 the oligosaccharide side chains lysosomal alpha-glucosidase the oligosaccharide side chains PUBTATOR lysosomal alpha-glucosidase 2548 Evidence is presented that at least two of the oligosaccharide side chains of human lysosomal alpha-glucosidase are phosphorylated. 1567356 11 28 gly glycosylation 1641:1653 arg1 OMD OMD OGER OMD Q99983 The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD. 2242757 0 40 gly Glycosylation 0:12 arg1 IgG IgG Cterm IgG Glycosylation of IgG, immune complexes and IgG subclasses in the MRL-lpr/lpr mouse model of rheumatoid arthritis. 8347587 12 4 gly glycosylation 1406:1418 arg1 the insulin receptor the insulin receptor PUBTATOR insulin receptor P01308 Thus, glycosylation of the first four N-linked glycosylation sites of the insulin receptor is necessary for the proper processing and intracellular transport of the receptor. 8347587 14 49 gly glycosylation 1716:1728 arg1 the insulin receptor the insulin receptor PUBTATOR insulin receptor P01308 Therefore, N-linked glycosylation of the insulin receptor at specific sites has multiple distinctive roles. 8347587 12 57 gly glycosylation 1365:1377 arg1 the insulin receptor the insulin receptor PUBTATOR insulin receptor P01308 Thus, glycosylation of the first four N-linked glycosylation sites of the insulin receptor is necessary for the proper processing and intracellular transport of the receptor. 7829269 3 9 gly aglycosylated 777:789 arg1 The resultant aglycosylated chimeric LL2 The resultant aglycosylated chimeric LL2 PUBTATOR LL2 633295 The resultant aglycosylated chimeric LL2 exhibited a similar Raji cell binding affinity to that of the glycosylated form. 10099468 2 39 gly N-glycosylation 482:496 arg1 secreted recombinant IFN-gamma secreted recombinant IFN-gamma Cterm IFN-gamma During establishment of the culture, the N-glycosylation of secreted recombinant IFN-gamma was monitored by capillary electrophoresis of intact IFN-gamma proteins and by HPLC analysis of released N-glycans. 7904345 2 4 gly presence 199:206 arg1 rat sCD4 AND identical oligosaccharides rat sCD4 identical oligosaccharides PUBTATOR sCD4 499358 The presence of identical oligosaccharides at the conserved glycosylation site in domain 3 of rat and human sCD4 and the greater abundance of oligomannose and hybrid type glycans at the non-conserved glycosylation site of rat sCD4 clearly indicate that the protein structure influences oligosaccharide processing. 7904345 2 4 gly presence 199:206 arg2 rat sCD4 AND hybrid type glycans rat sCD4 the conserved glycosylation site hybrid type glycans PUBTATOR sCD4 499358 site The presence of identical oligosaccharides at the conserved glycosylation site in domain 3 of rat and human sCD4 and the greater abundance of oligomannose and hybrid type glycans at the non-conserved glycosylation site of rat sCD4 clearly indicate that the protein structure influences oligosaccharide processing. 7904345 0 35 gly Glycosylation 0:12 arg1 CD4 CD4 PUBTATOR CD4 24932 Glycosylation of CD4 and Thy-1. 7904345 0 35 gly Glycosylation 0:12 arg1 Thy-1 Thy-1 PUBTATOR Thy-1 24832 Glycosylation of CD4 and Thy-1. 7904345 2 68 gly glycosylation 395:407 arg1 rat sCD4 rat sCD4 PUBTATOR sCD4 499358 The presence of identical oligosaccharides at the conserved glycosylation site in domain 3 of rat and human sCD4 and the greater abundance of oligomannose and hybrid type glycans at the non-conserved glycosylation site of rat sCD4 clearly indicate that the protein structure influences oligosaccharide processing. 7765932 1 5 gly occupancy 178:186 arg1 recombinant human prolactin recombinant human prolactin PUBTATOR prolactin 5617 The relationship between synthesis and N-linked glycosylation site occupancy of recombinant human prolactin produced from C127 cells was studied with the aid of a battery of protein synthesis inhibitors. 7765932 0 16 gly occupancy 69:77 arg1 recombinant human prolactin recombinant human prolactin PUBTATOR prolactin 5617 The effect of protein synthesis inhibitors on the glycosylation site occupancy of recombinant human prolactin. 7559469 3 8 gly osteonectin 452:462 arg1 oligosaccharide chain structures osteonectin oligosaccharide chain structures PUBTATOR osteonectin 282077 After removal of oligosaccharide chain structures from tHON, bovine bone osteonectin (BBON) and human platelet osteonectin (HPON) by N-glycanase, their ability to bind to type V collagen is increased, and HPON affinity to collagen V is the same as that of BBON. 7559469 8 13 part_of residue 1756:1762 arg1 wild-type osteonectin osteonectin residue PUBTATOR SpecificSite osteonectin 282077 residue 71 These data suggest that only the position 99 glycosylation site (Asn99-X-Thr101) in tHON is important in the reduction of binding of osteonectin to collagen V. Consistent with the binding data is the observation that both the N71Q and T73A mutant proteins migrate on SDS-polyacrylamide gel electrophoresis gels identically to wild-type tHON, suggesting that there is little or no N-glycosylation of residue 71 in wild-type osteonectin. 7559469 3 45 gly osteonectin 414:424 arg1 oligosaccharide chain structures osteonectin oligosaccharide chain structures PUBTATOR osteonectin 282077 After removal of oligosaccharide chain structures from tHON, bovine bone osteonectin (BBON) and human platelet osteonectin (HPON) by N-glycanase, their ability to bind to type V collagen is increased, and HPON affinity to collagen V is the same as that of BBON. 7559469 4 61 gly glycosylation 627:639 arg1 osteonectin osteonectin PUBTATOR osteonectin 282077 These data suggest that glycosylation of osteonectin has a direct or regulatory effect on osteonectin binding to collagen V and that the increase in tHON binding upon removal of carbohydrate is the result of a loss of a down-regulation site or direct interference of the carbohydrate at the binding site. 7559469 3 76 gly tHON 396:399 arg1 oligosaccharide chain structures tHON oligosaccharide chain structures Cterm tHON 282077 After removal of oligosaccharide chain structures from tHON, bovine bone osteonectin (BBON) and human platelet osteonectin (HPON) by N-glycanase, their ability to bind to type V collagen is increased, and HPON affinity to collagen V is the same as that of BBON. 23894062 8 94 part_of NOG 1130:1132 arg1 NOG-N54 NOG NOG-N54 PUBTATOR SpecificSite NOG 9241 N54 We showed a SOST peptide (SOST-S146, with homology to a bacterial glycotransferase peptide) binds to a NOG peptide (NOG-N54), which contains a N-glycosylation site. 8180202 8 9 gly glycosylation 1333:1345 arg1 CBG CBG PUBTATOR CBG 866 As we have previously found, glycosylation at Asn238 is essential for the production of CBG with steroid-binding activity, but when the mutant containing only one oligosaccharide at this position was enzymatically deglycosylated, its steroid-binding activity was unaltered. 8180202 0 42 gly Glycosylation 0:12 arg1 human corticosteroid-binding globulin human corticosteroid-binding globulin PUBTATOR corticosteroid-binding globulin 866 Glycosylation of human corticosteroid-binding globulin. 8180202 7 60 gly glycosylation 1224:1236 arg1 recombinant CBG recombinant CBG PUBTATOR CBG 866 Thus, the glycosylation of recombinant CBG appears to resemble that of natural human CBG. 26618514 7 9 gly sialylated 1031:1040 arg1 sialylated IgG sialylated IgG Cterm IgG In contrast, sialylated IgG reduced the phagocytosis by monocytes of SNEC. 26618514 6 18 gly non-sialylated 897:910 arg1 non-sialylated anti-SNEC IgG non-sialylated anti-SNEC IgG Cterm anti-SNEC Ig In functional ex-vivo phagocytosis studies, non-sialylated anti-SNEC IgG directed SNEC preferentially into PMN but did not change their cytokine secretion profiles. 26618514 5 32 gly IgG 693:695 arg1 the sialylation status IgG the sialylation status Cterm IgG Analysing the sialylation status of affinity-purified anti-histone IgG in patients with systemic lupus erythematosus (SLE), we demonstrated that the anti-histone IgG was contained preferentially in the non-sialylated fraction. 26618514 2 48 gly sialylation 231:241 arg1 IgG IgG Cterm IgG Glycan sialylation is critical for structure and for certain effector functions of IgG. 26618514 8 66 gly sialylated 1107:1116 arg1 the sialylated anti-SNEC IgG the sialylated anti-SNEC IgG Cterm anti-SNEC Ig Moreover, the sialylated anti-SNEC IgG was not simply anti-inflammatory, but switched the cytokine secretion profiles from interleukin (IL)-6/IL-8 to tumour necrosis factor (TNF)-α/IL-1β. 26618514 5 71 gly sialylation 640:650 arg1 affinity-purified anti-histone IgG affinity-purified anti-histone IgG Cterm IgG Analysing the sialylation status of affinity-purified anti-histone IgG in patients with systemic lupus erythematosus (SLE), we demonstrated that the anti-histone IgG was contained preferentially in the non-sialylated fraction. 10196694 6 12 gly N-glycosylation 1085:1099 arg1 saposin B saposin B Cterm saposin B The mutation involves a highly conserved amino acidic residue and abolishes the only N-glycosylation site of saposin B. 8603082 0 59 gly glycosylation 148:160 arg1 MCT1 function MCT1 function PUBTATOR MCT1 P53985 Cloning and sequencing of the monocarboxylate transporter from mouse Ehrlich Lettré tumour cell confirms its identity as MCT1 and demonstrates that glycosylation is not required for MCT1 function. 26415233 1 13 gly N-glycosylated 159:172 arg1 nascent immature N-glycosylated 110kDa TrkA nascent immature N-glycosylated 110kDa TrkA PUBTATOR TrkA 4914 In human SH-SY5Y neuroblastoma (NB) cells, nascent immature N-glycosylated 110kDa TrkA moves rapidly from the endoplasmic reticulum (ER) to the Golgi Network (GN), where it matures into the 140kDa receptor prior to being transported to the cell surface, creating GN and cell surface pools of inactive receptor maintained below the spontaneous activation threshold by a full compliment of inhibitory domains and endogenous PTPases. 20338479 3 13 gly sialylated 507:516 arg1 sialylated integrin beta1 sialylated integrin beta1 PUBTATOR integrin beta1 3688 METHODS AND MATERIALS: We performed Western blotting and lectin affinity assay to analyze the expression and level of sialylated integrin beta1. 20338479 8 18 gly beta1 1099:1103 arg1 sialylation integrin beta1 sialylation PUBTATOR integrin beta1 3688 When sialylation of integrin beta1 was targeted with a sulfonamide chalcone compound, inhibition of radiation-induced sialylation of integrin beta1 and inhibition of radiation-induced adhesion and migration occurred. 20338479 5 19 gly beta1 711:715 arg1 sialylation integrin beta1 sialylation PUBTATOR integrin beta1 3688 RESULTS: IR increased sialylation of integrin beta1 responsible for its increased protein stability and adhesion and migration of colon cancer cells. 20338479 8 28 gly sialylation 1188:1198 arg1 integrin beta1 integrin beta1 PUBTATOR integrin beta1 3688 When sialylation of integrin beta1 was targeted with a sulfonamide chalcone compound, inhibition of radiation-induced sialylation of integrin beta1 and inhibition of radiation-induced adhesion and migration occurred. 20338479 0 39 gly beta1 24:28 arg1 Sialylation integrin beta1 Sialylation PUBTATOR integrin beta1 3688 Sialylation of integrin beta1 is involved in radiation-induced adhesion and migration in human colon cancer cells. 20338479 8 42 gly sialylation 1075:1085 arg1 integrin beta1 integrin beta1 PUBTATOR integrin beta1 3688 When sialylation of integrin beta1 was targeted with a sulfonamide chalcone compound, inhibition of radiation-induced sialylation of integrin beta1 and inhibition of radiation-induced adhesion and migration occurred. 20338479 5 70 gly sialylation 687:697 arg1 integrin beta1 integrin beta1 PUBTATOR integrin beta1 3688 RESULTS: IR increased sialylation of integrin beta1 responsible for its increased protein stability and adhesion and migration of colon cancer cells. 20338479 8 81 gly beta1 1212:1216 arg1 radiation-induced sialylation integrin beta1 radiation-induced sialylation PUBTATOR integrin beta1 3688 When sialylation of integrin beta1 was targeted with a sulfonamide chalcone compound, inhibition of radiation-induced sialylation of integrin beta1 and inhibition of radiation-induced adhesion and migration occurred. 19527756 7 38 gly O-glycosylation 1205:1219 arg1 rhGCSF rhGCSF OGER rhGCSF P09919 Mutagenesis of the O-glycosylation site of rhGCSF (Thr(133) to Leu(133)) showed a single peak on bioanalyzer, which overlapped with the peak obtained for a non-glycosylated rhGCSF. 19527756 0 53 gly O-glycosylated 32:45 arg1 O-glycosylated recombinant human granulocyte colony stimulating factor O-glycosylated recombinant human granulocyte colony stimulating factor PUBTATOR granulocyte colony stimulating factor 1440 Over expression and analysis of O-glycosylated recombinant human granulocyte colony stimulating factor in Pichia pastoris using Agilent 2100 Bioanalyzer. 19527756 7 76 gly non-glycosylated 1342:1357 arg1 a non-glycosylated rhGCSF a non-glycosylated rhGCSF OGER rhGCSF P09919 Mutagenesis of the O-glycosylation site of rhGCSF (Thr(133) to Leu(133)) showed a single peak on bioanalyzer, which overlapped with the peak obtained for a non-glycosylated rhGCSF. 9287313 4 24 gly glycoforms 758:767 arg1 human CD69 glycoforms human CD69 glycoforms PUBTATOR CD69 969 In the current report we show that human CD69 glycoforms are generated before the egress of CD69 proteins from the endoplasmic reticulum to the Golgi and are synthesized under conditions where Golgi processing is inhibited, effectively ruling out the possibility that CD69 heterogeneity results from the differential processing of a single glycosylation site in the Golgi complex. 10471296 9 4 gly glycosylation 1430:1442 arg1 factor V factor V OGER factor V P12259 These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes. 21569239 0 76 gly glycosylated 35:46 arg1 F-spondin F-spondin PUBTATOR F-spondin 10418 The structure of the Ca²+-binding, glycosylated F-spondin domain of F-spondin - A C2-domain variant in an extracellular matrix protein. 17960575 8 30 gly N-glycosylation 1155:1169 arg1 TRFE TRFE PUBTATOR TRFE 7018 Disialylated diantennary glycans were observed in glycopeptides of both N-glycosylation sites of TRFE. 17960575 8 35 gly glycopeptides 1133:1145 arg1 TRFE TRFE PUBTATOR TRFE 7018 Disialylated diantennary glycans were observed in glycopeptides of both N-glycosylation sites of TRFE. 17960575 5 36 gly N-glycosylation 656:670 arg1 FETUA FETUA PUBTATOR FETUA 197 Glycopeptides derived from all three N-glycosylation sites of FETUA were observed, and the corresponding CID spectra proved the respective glycans to be oligosaccharides of the triantennary complex type. 9295302 2 15 gly phosphoglycoprotein 205:223 arg1 Multidrug resistance protein Multidrug resistance protein PUBTATOR Multidrug resistance protein 4363 Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents. 9295302 6 39 gly deglycosylation 887:901 arg1 intact MRP intact MRP PUBTATOR MRP 4363 Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP. 7849028 6 30 gly glycosylation 737:749 arg1 rat p62 rat p62 PUBTATOR p62 117268 Localization of the sites of O-linked GlcNAc glycosylation of rat p62 was performed by a combination of deletion analysis of in vitro translation products and by immunoprecipitation of [14C]GlcNAc-labeled proteolytic fragments. 7849028 3 58 gly Glycosylation 282:294 arg1 p62 p62 PUBTATOR p62 117268 Glycosylation of the major rat nuclear pore glycoprotein, p62, was examined in vitro using recombinant p62 as a substrate. 7849028 6 60 gly p62 758:760 arg1 O-linked GlcNAc glycosylation p62 O-linked GlcNAc glycosylation PUBTATOR p62 117268 Localization of the sites of O-linked GlcNAc glycosylation of rat p62 was performed by a combination of deletion analysis of in vitro translation products and by immunoprecipitation of [14C]GlcNAc-labeled proteolytic fragments. 7849028 3 102 gly glycoprotein 326:337 arg1 p62 p62 PUBTATOR p62 117268 Glycosylation of the major rat nuclear pore glycoprotein, p62, was examined in vitro using recombinant p62 as a substrate. 9126611 8 66 gly hCox-2 1546:1551 arg1 N-linked oligosaccharide profiling hCox-2 N-linked oligosaccharide profiling PUBTATOR hCox-2 4513 N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6. 10998266 1 31 gly heterogeneity 418:430 arg1 EPO EPO heterogeneity PUBTATOR EPO 2056 High-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) and liquid chromatography with tandem mass spectrometry (LC/MS/MS) were applied to the analysis of the site-specific carbohydrate heterogeneity in erythropoietin (EPO) used as a model of the sialylated glycoprotein. 10998266 1 31 gly heterogeneity 418:430 arg1 erythropoietin erythropoietin heterogeneity PUBTATOR erythropoietin 2056 High-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) and liquid chromatography with tandem mass spectrometry (LC/MS/MS) were applied to the analysis of the site-specific carbohydrate heterogeneity in erythropoietin (EPO) used as a model of the sialylated glycoprotein. 10998266 0 70 gly heterogeneity 161:173 arg1 erythropoietin erythropoietin heterogeneity PUBTATOR erythropoietin 2056 Application of liquid chromatography/mass spectrometry and liquid chromatography with tandem mass spectrometry to the analysis of the site-specific carbohydrate heterogeneity in erythropoietin. 10998266 2 73 gly released 535:542 arg1 recombinant human EPO AND N-linked oligosaccharides recombinant human EPO N-linked oligosaccharides PUBTATOR EPO 2056 N-linked oligosaccharides were released from recombinant human EPO expressed in Chinese hamster ovary cells enzymatically and reduced with NaBH(4). 10998266 3 84 gly EPO 698:700 arg1 Many different sialylated oligosaccharides EPO Many different sialylated oligosaccharides PUBTATOR EPO 2056 Many different sialylated oligosaccharides of EPO were separated and characterized by LC/MS equipped with a graphitized carbon column (GCC). 8941718 7 76 gly deglycosylation 1238:1252 arg1 normal LAL normal LAL PUBTATOR LAL 3988 Furthermore, deglycosylation of normal LAL reduced the acid hydrolase activity towards both tri-oleyl glycerol and cholesteryl oleate by 50%, strongly suggesting that N-linked carbohydrate residues are important for optimal catalytic activity. 1318404 1 20 gly glycoprotein 184:195 arg1 SU (gp70) SU (gp70) Cterm SU The role of the N-linked glycosylation sites in the major envelope glycoprotein, SU (gp70), of Moloney murine leukemia virus has been examined. 15199058 0 80 part_of E 50:50 arg1 Lys-352 immunoglobulin E Lys-352 PUBTATOR SpecificSite immunoglobulin E P01854 Lys-352 The importance of Lys-352 of human immunoglobulin E in FcepsilonRII/CD23 recognition. 17050611 0 5 gly Pradimicin 0:9 arg1 a carbohydrate-binding nonpeptidic lead compound Pradimicin A a carbohydrate-binding nonpeptidic lead compound Cterm Pradimicin A Pradimicin A, a carbohydrate-binding nonpeptidic lead compound for treatment of infections with viruses with highly glycosylated envelopes, such as human immunodeficiency virus. 17050611 1 6 gly Pradimicin 178:187 arg1 a low-molecular-weight (molecular weight, 838) carbohydrate binding agent Pradimicin A (PRM-A a low-molecular-weight (molecular weight, 838) carbohydrate binding agent Cterm Pradimicin A (PRM-A Pradimicin A (PRM-A), an antifungal nonpeptidic benzonaphtacenequinone antibiotic, is a low-molecular-weight (molecular weight, 838) carbohydrate binding agent (CBA) endowed with a selective inhibitory activity against human immunodeficiency virus (HIV). 2033065 12 56 gly glycosylation 2171:2183 arg1 HPC HPC OGER HPC P11498 Overall, our studies demonstrate that glycosylation at different sites in HPC affects distinct properties of this complex protein. 2033065 0 110 gly Glycosylation 0:12 arg1 human protein C human protein C OGER protein C P02810 Glycosylation of human protein C affects its secretion, processing, functional activities, and activation by thrombin. 1840295 9 43 gly tPA 1197:1199 arg1 sugars tPA sugars PUBTATOR tPA P00750 In the dMM-treated sample, type I tPA (with sugars at sites 117, 184 and 448) was found to have 2- to 3-fold increased catalytic activity and an affinity for lysine which was greater than that of type I from untreated preparations, but less than that of control type II tPA (containing sugar only at sites 117 and 448). 1457969 8 18 gly hTSH 1609:1612 arg1 the N-glycans hTSH the N-glycans OGER hTSH Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland. 1457969 5 43 gly present 877:883 arg1 hTSH AND The N-glycans hTSH The N-glycans OGER hTSH The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc. 1457969 5 43 gly present 877:883 arg2 hTSH AND diantennary complex-type structures hTSH diantennary complex-type structures OGER hTSH The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc. 1457969 2 72 gly glycosylated 414:425 arg1 hTSH beta hTSH beta PUBTATOR hTSH beta 7252 Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23). 1457969 2 85 gly glycosylated 364:375 arg1 hTSH alpha hTSH alpha PUBTATOR hTSH alpha 1081 Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23). 1457969 4 89 gly liberated 648:656 arg1 intact hTSH beta AND The oligosaccharides intact hTSH beta The oligosaccharides PUBTATOR hTSH beta 7252 The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis. 11038011 10 73 gly glycosylation 1975:1987 arg1 vasopressin vasopressin PUBTATOR vasopressin 551 Our data suggest that 1) intact neurophysin is not indispensable for vasopressin expression, although an altered structure of neurophysin significantly affects the secretion of the hormone; 2) the pathogenesis of diabetes insipidus with the two naturally-occurring mutations found in the rat (Brattleboro rat) and human (familial central diabetes insipidus) seem to be different; and 3) glycosylation of the carboxy-terminal glycopeptide is not essential for the expression of vasopressin. 15100290 2 13 gly carbohydrate 261:272 arg1 CDR2 2 (CDR2 carbohydrate OGER 2 (CDR2 P97817 We have studied a murine anti-alpha(1-->6) dextran V(H) that contains a carbohydrate in complementarity-determining region 2 (CDR2). 15100290 5 29 gly present 628:634 arg2 CDR1 AND another carbohydrate CDR1 another carbohydrate PUBTATOR CDR1 1038 Also, when another carbohydrate was present in CDR1, CDR2, or CDR3 of the L chain, the V(H) CDR2 glycan remained high mannose. 15100290 5 29 gly present 628:634 arg1 CDR2 AND another carbohydrate CDR2 another carbohydrate OGER CDR2 P97817 Also, when another carbohydrate was present in CDR1, CDR2, or CDR3 of the L chain, the V(H) CDR2 glycan remained high mannose. 15100290 5 29 gly present 628:634 arg1 CDR3 AND another carbohydrate CDR3 another carbohydrate PUBTATOR CDR3 8163 Also, when another carbohydrate was present in CDR1, CDR2, or CDR3 of the L chain, the V(H) CDR2 glycan remained high mannose. 15100290 5 46 gly present 628:634 arg2 CDR1 AND another carbohydrate CDR1 another carbohydrate PUBTATOR CDR1 1038 Also, when another carbohydrate was present in CDR1, CDR2, or CDR3 of the L chain, the V(H) CDR2 glycan remained high mannose. 15100290 5 46 gly present 628:634 arg1 CDR2 AND another carbohydrate CDR2 another carbohydrate OGER CDR2 P97817 Also, when another carbohydrate was present in CDR1, CDR2, or CDR3 of the L chain, the V(H) CDR2 glycan remained high mannose. 15100290 5 46 gly present 628:634 arg1 CDR3 AND another carbohydrate CDR3 another carbohydrate PUBTATOR CDR3 8163 Also, when another carbohydrate was present in CDR1, CDR2, or CDR3 of the L chain, the V(H) CDR2 glycan remained high mannose. 12765790 1 22 gly Polysialylated 77:90 arg1 NCAM NCAM PUBTATOR NCAM 17967 Polysialylated neural cell adhesion molecule (NCAM) was immunoaffinity-purified from the brains of newborn calves. 12765790 5 43 gly NCAM 994:997 arg1 PSA-N-glycans NCAM PSA-N-glycans PUBTATOR NCAM 17967 Non-PSA/HNK1-glycans were assigned to glycosylation site 2, whereas PSA-N-glycans of bovine NCAM had been already previously shown to be restricted to glycosylation sites 5 and 6 (Glycobiology 12 (2002) 47). 12765790 0 49 gly polysialylated 56:69 arg1 bovine polysialylated NCAM bovine polysialylated NCAM PUBTATOR NCAM 17967 Localization of defined carbohydrate epitopes in bovine polysialylated NCAM. 27506355 11 60 gly glycoprotein 1365:1376 arg1 human transferrin human transferrin PUBTATOR transferrin 7018 We validated our method using a standard glycoprotein, human transferrin, and evaluated its potential to be used in site-specific glycosylation profiling of glycoprotein datasets from LC-MS/MS. 27506355 12 66 gly N-glycosylation 1610:1624 arg1 recombinant human acetylcholinesterase recombinant human acetylcholinesterase PUBTATOR acetylcholinesterase 43 In addition, we further applied our method to reveal, for the first time, the site-specific N-glycosylation profile of recombinant human acetylcholinesterase expressed in HEK293 cells. 8207403 1 34 gly glycoprotein 225:236 arg1 gp41 gp41 Cterm gp41 The transmembrane envelope glycoprotein (gp41) of human immunodeficiency virus type 1 possesses four consensus sites (Asn-X-Ser/Thr) for the incorporation of N-linked sugars situated on the extracellular domain of the molecule. 1421757 1 30 gly glycoprotein 121:132 arg1 The human transferrin receptor The human transferrin receptor PUBTATOR transferrin receptor 7018 The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites. 1421757 0 32 gly glycosylation 31:43 arg1 the human transferrin receptor the human transferrin receptor PUBTATOR transferrin receptor 7037 Identification of the O-linked glycosylation site of the human transferrin receptor. 8027066 6 75 gly glycosylation 1311:1323 arg1 the IR beta subunit the IR beta subunit Cterm IR beta subunit 3643 These data provide evidence for (i) glycosylation of each N-linked glycosylation site of the IR beta subunit, (ii) absence of correlation between internalization and transmembrane signaling, and (iii) a major role for oligosaccharide side chain(s) located close to the cell membrane in IR activation and transmembrane signaling. 8027066 6 93 gly glycosylation 1280:1292 arg1 the IR beta subunit the IR beta subunit Cterm IR beta subunit 3643 These data provide evidence for (i) glycosylation of each N-linked glycosylation site of the IR beta subunit, (ii) absence of correlation between internalization and transmembrane signaling, and (iii) a major role for oligosaccharide side chain(s) located close to the cell membrane in IR activation and transmembrane signaling. 9201996 2 29 gly N-acetylgalactosaminyl 469:490 arg1 O-GalNAcT N-acetylgalactosaminyl O-GalNAcT Cterm N-acetylgalactosaminyl To determine the shortest motif sequence required for high level mucin-type O-glycosylation, we prepared more than 100 synthetic peptides and assayed in vitro O-GalNAc transfer to serine or threonine in these peptides using a bovine colostrum UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyl transferase (O-GalNAcT). 9705240 0 43 gly glycosylation 23:35 arg1 biotinidase biotinidase PUBTATOR biotinidase 686 Mutation in a putative glycosylation site (N489T) of biotinidase in the only known Japanese child with biotinidase deficiency. 8349699 10 4 gly N-glycosylation 1444:1458 arg1 PGH synthase-1 PGH synthase-1 PUBTATOR PGH synthase-1 19224 Assuming that the N-glycosylation sites of PGH synthase-1 are on the luminal side of the endoplasmic reticulum (ER), and that the site of tryptic cleavage of ovine PGH synthase-1 (Arg277) is on the cytoplasmic side of the ER, we propose that both the NH2 and COOH termini of PGH synthase-1 are located in the lumen of the ER and that there are two transmembrane domains located between Asn144 and Arg277 and between Arg277 and Asn410, respectively. 8349699 6 16 gly glycosylation 850:862 arg1 ovine PGH synthase-1 ovine PGH synthase-1 PUBTATOR PGH synthase-1 19224 N-Glycosylation consensus sequences corresponding to the three glycosylation sites of ovine PGH synthase-1 are conserved in the deduced amino acid sequences of PGH synthases-2. 8349699 10 17 part_of PGH 1590:1592 arg1 Arg277 PGH synthase-1 Arg277 PUBTATOR AminoAcid PGH synthase-1 19224 Arg277 Assuming that the N-glycosylation sites of PGH synthase-1 are on the luminal side of the endoplasmic reticulum (ER), and that the site of tryptic cleavage of ovine PGH synthase-1 (Arg277) is on the cytoplasmic side of the ER, we propose that both the NH2 and COOH termini of PGH synthase-1 are located in the lumen of the ER and that there are two transmembrane domains located between Asn144 and Arg277 and between Arg277 and Asn410, respectively. 8349699 9 31 gly glycosylation 1351:1363 arg1 PGH synthase-2 PGH synthase-2 PUBTATOR PGH synthase-2 19225 Glycosylation of PGH synthase-2 is necessary for expression of enzyme activity, but glycosylation of PGH synthase-2 at Asn580 per se does not affect activity. 8349699 7 45 gly N-glycosylation 1047:1061 arg1 murine PGH synthase-2 murine PGH synthase-2 PUBTATOR PGH synthase-2 19225 Using site-directed mutagenesis, we determined that there is an additional site of N-glycosylation in murine PGH synthase-2 located at Asn580. 8349699 9 70 gly Glycosylation 1267:1279 arg1 PGH synthase-2 PGH synthase-2 PUBTATOR PGH synthase-2 19225 Glycosylation of PGH synthase-2 is necessary for expression of enzyme activity, but glycosylation of PGH synthase-2 at Asn580 per se does not affect activity. 8349699 3 99 gly Glycosylation 349:361 arg1 PGH synthase-1 PGH synthase-1 PUBTATOR PGH synthase-1 19224 Glycosylation of PGH synthase-1 at Asn410 and at either Asn68 or Asn144 was required for expression of both the cyclooxygenase and the peroxidase activities of the enzyme. 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 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. 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. 7755594 1 0 gly glycoprotein 158:169 arg1 Human interferon-gamma Human interferon-gamma PUBTATOR Human interferon-gamma 3458 Human interferon-gamma (IFN-gamma) is a secretory, dimeric glycoprotein that forms a compact globular structure with potential N-linked glycosylation sites at Asn-25 and Asn-97 on the surface of the dimer. 7755594 7 16 gly Unglycosylated 1073:1086 arg1 Unglycosylated recombinant IFN-gamma proteins Unglycosylated recombinant IFN-gamma proteins PUBTATOR IFN-gamma proteins 25712 Unglycosylated recombinant IFN-gamma proteins (from Escherichia coli and baculovirus) and N25Q IFN-gamma were sensitive to crude granulocyte protease, purified elastase, cathepsin G and plasmin degradation. 7755594 0 23 gly N-glycosylation 0:14 arg1 human interferon-gamma human interferon-gamma PUBTATOR interferon-gamma 3458 N-glycosylation of human interferon-gamma: glycans at Asn-25 are critical for protease resistance. 7755594 8 32 gly glycosylated 1286:1297 arg1 Fully glycosylated nIFN-gamma Fully glycosylated nIFN-gamma Cterm nIFN-gamma 25712 Fully glycosylated nIFN-gamma and baculovirus Wt and N97Q IFN-gamma showed full or partial resistance to these proteases. 7755594 10 51 gly glycosylation 1557:1569 arg1 rIFN-gamma rIFN-gamma PUBTATOR rIFN-gamma 25712 Whether the differential glycosylation of n- and recombinant IFN-gamma (rIFN-gamma) is reflected in their biological activities in tissues or their clinical applicability is not known. 7755594 10 51 gly glycosylation 1557:1569 arg1 recombinant IFN-gamma recombinant IFN-gamma PUBTATOR IFN-gamma 3458 Whether the differential glycosylation of n- and recombinant IFN-gamma (rIFN-gamma) is reflected in their biological activities in tissues or their clinical applicability is not known. 7755594 6 80 part_of Asn-25 1018:1023 arg1 IFN-gamma IFN-gamma Asn-25 PUBTATOR SpecificSite IFN-gamma 3458 Asn-25 The glycan residues of IFN-gamma, especially at Asn-25, play an important role in protease resistance. 7755594 6 86 gly IFN-gamma 993:1001 arg1 The glycan residues IFN-gamma The glycan residues PUBTATOR IFN-gamma 3458 The glycan residues of IFN-gamma, especially at Asn-25, play an important role in protease resistance. 8301235 3 77 gly glycoprotein 439:450 arg1 Human HL Human HL PUBTATOR Human HL 3280 Human HL is a glycoprotein and its predicted amino acid sequence contains four putative N-linked glycosylation sites at Asn residues 20, 56, 340, and 375. 8185569 5 23 gly glycosylation 808:820 arg1 the TSHR the TSHR PUBTATOR TSHR 7253 These results might suggest a real difference in glycosylation of the TSHR among species. 8185569 0 39 gly glycosylation 23:35 arg1 the thyrotropin receptor the thyrotropin receptor PUBTATOR thyrotropin receptor 7253 Possible difference in glycosylation of the thyrotropin receptor among species. 16372382 2 57 gly hormone 410:416 arg1 the N-linked oligosaccharides thyroid-stimulating hormone the N-linked oligosaccharides Cterm thyroid-stimulating hormone In this paper we report the first detailed structural characterization of the N-linked oligosaccharides of recombinant human thyroid-stimulating hormone (rhTSH). 10995221 4 9 gly glycosylated 662:673 arg1 UGT2B15 UGT2B15 PUBTATOR UGT2B15 7366 Endoglycosidase H digestion of the human and monkey UGT2B proteins demonstrates that only UGT2B7, UGT2B15, UGT2B17, and UGT2B20 are glycosylated. 10995221 4 9 gly glycosylated 662:673 arg1 UGT2B7 UGT2B7 PUBTATOR UGT2B7 7364 Endoglycosidase H digestion of the human and monkey UGT2B proteins demonstrates that only UGT2B7, UGT2B15, UGT2B17, and UGT2B20 are glycosylated. 10995221 4 9 gly glycosylated 662:673 arg1 UGT2B17 UGT2B17 PUBTATOR UGT2B17 7367 Endoglycosidase H digestion of the human and monkey UGT2B proteins demonstrates that only UGT2B7, UGT2B15, UGT2B17, and UGT2B20 are glycosylated. 10995221 4 9 gly glycosylated 662:673 arg1 UGT2B20 UGT2B20 Cterm UGT2B20 Endoglycosidase H digestion of the human and monkey UGT2B proteins demonstrates that only UGT2B7, UGT2B15, UGT2B17, and UGT2B20 are glycosylated. 12954207 9 28 gly glycoprotein 1537:1548 arg1 Envelope glycoprotein oligomers Envelope glycoprotein oligomers PUBTATOR Envelope glycoprotein 100616444 Envelope glycoprotein oligomers on the cell surface derived from the V3 glycan-deficient virus were better recognized by a CD4BS antibody and a V3 loop antibody than were the wild-type glycoproteins. 12954207 0 39 gly deglycosylation 26:40 arg1 HIV-1 gp120 HIV-1 gp120 PUBTATOR HIV-1 gp120 155971 Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition. 12954207 1 48 gly glycoprotein 184:195 arg1 gp120 gp120 PUBTATOR gp120 155971 The human immunodeficiency virus (HIV-1) exterior envelope glycoprotein, gp120, mediates receptor binding and is the major target for neutralizing antibodies. 12954207 1 48 gly glycoprotein 184:195 arg1 The human immunodeficiency virus (HIV-1) exterior envelope glycoprotein The human immunodeficiency virus (HIV-1) exterior envelope glycoprotein PUBTATOR envelope glycoprotein 155971 The human immunodeficiency virus (HIV-1) exterior envelope glycoprotein, gp120, mediates receptor binding and is the major target for neutralizing antibodies. 17640971 3 8 gly O-glycosylation 640:654 arg1 CD52 CD52 PUBTATOR CD52 1043 Although the amount of posttranslational modification is already remarkable for such a small polypeptide, O-glycosylation of CD52 has additionally been implicated by several studies, but never rigorously characterized. 17640971 0 79 gly glycoforms 43:52 arg1 CD52 CD52 PUBTATOR CD52 1043 The sperm agglutination antigen-1 (SAGA-1) glycoforms of CD52 are O-glycosylated. 15582650 8 73 gly glycosylation 1633:1645 arg1 modified HIV Env proteins modified HIV Env proteins PUBTATOR HIV Env proteins 100616444 Our study suggests that modified HIV Env proteins with reduced glycosylation in domains surrounding the CD4 binding site or variable loop-deleted mutants expose important neutralizing epitopes at higher levels than wild type and may provide novel vaccine immunogens. 7980452 1 24 gly glycoprotein 146:157 arg1 Human interferon-gamma Human interferon-gamma PUBTATOR Human interferon-gamma 3458 Human interferon-gamma (IFN-gamma) is a secretory glycoprotein, which has two potential N-linked glycosylation sites at positions Asn-25 and Asn-97 of its 143 amino acid long mature polypeptide chain. 7980452 0 86 gly N-glycosylation 8:22 arg1 human interferon-gamma human interferon-gamma PUBTATOR interferon-gamma 3458 Role of N-glycosylation in the synthesis, dimerization and secretion of human interferon-gamma. 8382971 3 16 gly glycosylation 533:545 arg1 tPA-6P tPA-6P OGER tPA P00750 tPA-6 is composed of kringle-2 and the serine protease domains and, like ntPA, cells expressing tPA-6 process it into two glycoforms: the monoglycosylated tPA-6-primary (tPA-6P, type II) with N-linked glycosylation at Asn-448 in the serine protease domain and diglycosylated tPA-6-variant (tPA-6V, type I) with glycosylation at Asn-448 and at Asn-184 in kringle-2. 8382971 3 16 gly glycosylation 533:545 arg1 the monoglycosylated tPA-6-primary the monoglycosylated tPA-6-primary OGER tPA P00750 tPA-6 is composed of kringle-2 and the serine protease domains and, like ntPA, cells expressing tPA-6 process it into two glycoforms: the monoglycosylated tPA-6-primary (tPA-6P, type II) with N-linked glycosylation at Asn-448 in the serine protease domain and diglycosylated tPA-6-variant (tPA-6V, type I) with glycosylation at Asn-448 and at Asn-184 in kringle-2. 8382971 3 20 part_of Asn-448 550:556 arg1 diglycosylated tPA-6-variant tPA Asn-448 OGER SpecificSite tPA P00750 Asn-448 tPA-6 is composed of kringle-2 and the serine protease domains and, like ntPA, cells expressing tPA-6 process it into two glycoforms: the monoglycosylated tPA-6-primary (tPA-6P, type II) with N-linked glycosylation at Asn-448 in the serine protease domain and diglycosylated tPA-6-variant (tPA-6V, type I) with glycosylation at Asn-448 and at Asn-184 in kringle-2. 8382971 3 34 gly monoglycosylated 470:485 arg1 tPA-6P tPA-6P OGER tPA P00750 tPA-6 is composed of kringle-2 and the serine protease domains and, like ntPA, cells expressing tPA-6 process it into two glycoforms: the monoglycosylated tPA-6-primary (tPA-6P, type II) with N-linked glycosylation at Asn-448 in the serine protease domain and diglycosylated tPA-6-variant (tPA-6V, type I) with glycosylation at Asn-448 and at Asn-184 in kringle-2. 8382971 3 34 gly monoglycosylated 470:485 arg1 the monoglycosylated tPA-6-primary the monoglycosylated tPA-6-primary OGER tPA P00750 tPA-6 is composed of kringle-2 and the serine protease domains and, like ntPA, cells expressing tPA-6 process it into two glycoforms: the monoglycosylated tPA-6-primary (tPA-6P, type II) with N-linked glycosylation at Asn-448 in the serine protease domain and diglycosylated tPA-6-variant (tPA-6V, type I) with glycosylation at Asn-448 and at Asn-184 in kringle-2. 8382971 0 44 gly glycosylation 8:20 arg1 a modified human tissue plasminogen activator a modified human tissue plasminogen activator PUBTATOR tissue plasminogen activator P00750 Kringle glycosylation in a modified human tissue plasminogen activator improves functional properties. 8382971 3 61 gly diglycosylated 592:605 arg1 diglycosylated tPA-6-variant diglycosylated tPA-6-variant OGER tPA P00750 tPA-6 is composed of kringle-2 and the serine protease domains and, like ntPA, cells expressing tPA-6 process it into two glycoforms: the monoglycosylated tPA-6-primary (tPA-6P, type II) with N-linked glycosylation at Asn-448 in the serine protease domain and diglycosylated tPA-6-variant (tPA-6V, type I) with glycosylation at Asn-448 and at Asn-184 in kringle-2. 24931470 1 11 gly glycoprotein 71:82 arg1 Env Env PUBTATOR Env 100616444 The HIV envelope glycoprotein (Env) trimer undergoes receptor-induced conformational changes that drive fusion of the viral and cellular membranes. 24931470 1 11 gly glycoprotein 71:82 arg1 HIV envelope glycoprotein HIV envelope glycoprotein PUBTATOR HIV envelope glycoprotein 155971 The HIV envelope glycoprotein (Env) trimer undergoes receptor-induced conformational changes that drive fusion of the viral and cellular membranes. 24931470 3 41 gly CD4-bound 468:476 arg1 their glycan composition CD4 their glycan composition PUBTATOR CD4 920 Here, we use hydrogen-deuterium exchange and oxidative labeling to gain a more precise understanding of the unliganded and CD4-bound forms of soluble Env trimers (SOSIP.664), including their glycan composition. 24931470 3 43 gly trimers 499:505 arg1 their glycan composition Env trimers their glycan composition PUBTATOR Env trimers 100616444 Here, we use hydrogen-deuterium exchange and oxidative labeling to gain a more precise understanding of the unliganded and CD4-bound forms of soluble Env trimers (SOSIP.664), including their glycan composition. 12097564 7 44 gly glycosylated 1034:1045 arg1 terminally glycosylated Env terminally glycosylated Env PUBTATOR Env 100616444 We furthermore observed a preference for binding to terminally glycosylated Env over core-glycosylated Env precursor in IPs, suggesting that the epitope is at least partially conformational and dependent on glycosylation. 12097564 7 51 gly core-glycosylated 1056:1072 arg1 core-glycosylated Env precursor core-glycosylated Env precursor PUBTATOR Env precursor 100616444 We furthermore observed a preference for binding to terminally glycosylated Env over core-glycosylated Env precursor in IPs, suggesting that the epitope is at least partially conformational and dependent on glycosylation. 8419363 0 43 gly Glycosylation 0:12 arg1 human corticosteroid-binding globulin human corticosteroid-binding globulin PUBTATOR corticosteroid-binding globulin 866 Glycosylation of human corticosteroid-binding globulin at aspargine 238 is necessary for steroid binding. 8419363 1 57 gly glycoprotein 162:173 arg1 Human corticosteroid binding-globulin Human corticosteroid binding-globulin PUBTATOR Human corticosteroid binding-globulin 866 Human corticosteroid binding-globulin (CBG) is a plasma glycoprotein that binds and regulates the biological activity of glucocorticoids and progesterone. 9581553 1 77 gly glycosylation 197:209 arg1 FR FR Cterm FR In a previous study with inhibitors of N-glycosylation, it was proposed that core glycosylation of the folate receptor (FR) is required for the proper folding of the protein [Luhrs (1991) Blood 77, 1171-1180]. 2477364 15 110 gly glycosylation 2051:2063 arg1 hCG assembly hCG assembly PUBTATOR hCG 93659 Because glycosylation at this site is essential for hCG assembly and signal transduction, these data imply a critical link between the site-specific processing and hormone function. 24780636 2 18 gly glycoforms 191:200 arg1 Transferrin glycoforms Transferrin glycoforms PUBTATOR Transferrin 7018 Transferrin glycoforms Tf-1 and Tf-2, previously identified in human cerebrospinal fluid, are defined as the lower and upper bands in gel electrophoresis, respectively. 24780636 5 84 gly sTf 845:847 arg1 the N-glycans sTf the N-glycans Cterm sTf 7018 Mass spectrometric analyses confirmed that Tf-2 is modified with disialylated biantennary glycans at both of the two N-glycosylation sites, which are similar to the N-glycans of sTf. 2737288 0 9 gly glycosylation 41:53 arg1 human pancreatic elastase 1 human pancreatic elastase 1 PUBTATOR pancreatic elastase 1 1990 Localization and characterization of the glycosylation site of human pancreatic elastase 1. 12388686 5 26 gly O-glycosylated 1063:1076 arg1 DAF DAF OGER DAF P08174 Through the use of site-directed mutagenesis to eliminate the single N-linked glycosylation site of DAF and of a chimeric receptor protein in which the O-glycosylated domain of DAF was replaced by a region of the HLA-B44 molecule, a role in EV70 binding for the sialic acid residues of DAF was excluded, suggesting the existence of at least one additional, sialylated EV70-binding factor at the cell surface. 12388686 5 38 gly DAF 1197:1199 arg1 the sialic acid residues DAF the sialic acid residues OGER DAF P08174 Through the use of site-directed mutagenesis to eliminate the single N-linked glycosylation site of DAF and of a chimeric receptor protein in which the O-glycosylated domain of DAF was replaced by a region of the HLA-B44 molecule, a role in EV70 binding for the sialic acid residues of DAF was excluded, suggesting the existence of at least one additional, sialylated EV70-binding factor at the cell surface. 12388686 5 52 gly glycosylation 989:1001 arg1 DAF DAF OGER DAF P08174 Through the use of site-directed mutagenesis to eliminate the single N-linked glycosylation site of DAF and of a chimeric receptor protein in which the O-glycosylated domain of DAF was replaced by a region of the HLA-B44 molecule, a role in EV70 binding for the sialic acid residues of DAF was excluded, suggesting the existence of at least one additional, sialylated EV70-binding factor at the cell surface. 12388686 6 86 gly glycosylation 1477:1489 arg1 EV70 binding EV70 binding Cterm EV70 Treatment of cells with metabolic inhibitors of glycosylation excluded a role for the N-linked oligosaccharides of glycoproteins but suggested that O-linked glycosylation is important for EV70 binding. 9757569 1 7 part_of angiotensinogen 165:179 arg1 Ser14 angiotensinogen Ser14 PUBTATOR AminoAcid angiotensinogen P01019 Ser14 A mutant angiotensinogen, S14N, in which Ser14 of ovine angiotensinogen was replaced by Asn to form a N-glycosylation site, was produced in CHO cells. 9757569 0 10 part_of residue 32:38 arg1 ovine angiotensinogen angiotensinogen residue PUBTATOR AminoAcid angiotensinogen 183 residue at position 14 Effects of glycosylation of the residue at position 14 in ovine angiotensinogen on the human renin reaction. 9757569 0 23 gly glycosylation 11:23 arg1 the human renin reaction the human renin reaction PUBTATOR renin 5972 Effects of glycosylation of the residue at position 14 in ovine angiotensinogen on the human renin reaction. 9757569 2 26 gly glycosylated 391:402 arg1 S14N angiotensinogen S14N angiotensinogen PUBTATOR S14N angiotensinogen P01019 The molecular weight was about 3,000 larger than that of wild-type ovine angiotensinogen, indicating that S14N angiotensinogen was glycosylated at Asn14. 25541284 0 28 gly glycoprotein 89:100 arg1 myelin oligodendrocyte glycoprotein myelin oligodendrocyte glycoprotein PUBTATOR myelin oligodendrocyte glycoprotein 4340 The role of N-glycan in folding, trafficking and pathogenicity of myelin oligodendrocyte glycoprotein (MOG). 25541284 0 28 gly glycoprotein 89:100 arg1 MOG MOG PUBTATOR MOG 4340 The role of N-glycan in folding, trafficking and pathogenicity of myelin oligodendrocyte glycoprotein (MOG). 25541284 1 42 gly glycoprotein 132:143 arg1 MOG MOG PUBTATOR MOG 4340 Myelin oligodendrocyte glycoprotein (MOG) is a type I integral membrane protein that is expressed in the central nervous system. 25541284 1 42 gly glycoprotein 132:143 arg1 Myelin oligodendrocyte glycoprotein Myelin oligodendrocyte glycoprotein PUBTATOR Myelin oligodendrocyte glycoprotein 4340 Myelin oligodendrocyte glycoprotein (MOG) is a type I integral membrane protein that is expressed in the central nervous system. 2341397 0 14 gly glycoforms 57:66 arg1 nonspecific cross-reacting antigen nonspecific cross-reacting antigen PUBTATOR nonspecific cross-reacting antigen 1084 Sequence and glycosylation site identity of two distinct glycoforms of nonspecific cross-reacting antigen as demonstrated by sequence analysis and fast atom bombardment mass spectrometry. 2341397 5 44 gly glycosylated 1130:1141 arg1 NCA NCA PUBTATOR NCA 1089 This approach showed that TEX and NCA were identical with respect to primary sequence and provided direct evidence that 11 of the 12 predicted asparagine-linked glycosylation sites were glycosylated in both TEX and NCA. 2341397 2 52 gly glycoforms 393:402 arg1 NCA NCA PUBTATOR NCA 1089 Two glycoforms of NCA were purified from a single liver metastasis of a colonic carcinoma and characterized with respect to their primary sequence and position of glycosylation sites. 19874459 11 8 gly glycosylation 1624:1636 arg1 VWF functions VWF functions PUBTATOR VWF 7450 In conjunction with current models explaining VWF activity, knowledge of the complete O-glycome will facilitate research aimed at providing a better understanding of the influence of glycosylation on VWF functions. 19874459 9 22 gly present 1294:1300 arg1 VWF AND Eighteen O-glycan structures VWF Eighteen O-glycan structures PUBTATOR VWF 7450 Eighteen O-glycan structures including both core 1 and core 2 structures are now demonstrated to be present on VWF. 19874459 9 22 gly present 1294:1300 arg2 VWF AND core 2 VWF core 2 PUBTATOR VWF 7450 Eighteen O-glycan structures including both core 1 and core 2 structures are now demonstrated to be present on VWF. 19874459 9 22 gly present 1294:1300 arg2 VWF AND core 1 VWF core 1 PUBTATOR VWF 7450 Eighteen O-glycan structures including both core 1 and core 2 structures are now demonstrated to be present on VWF. 19874459 9 83 gly present 1294:1300 arg1 VWF AND Eighteen O-glycan structures VWF Eighteen O-glycan structures PUBTATOR VWF 7450 Eighteen O-glycan structures including both core 1 and core 2 structures are now demonstrated to be present on VWF. 19874459 9 83 gly present 1294:1300 arg2 VWF AND core 2 VWF core 2 PUBTATOR VWF 7450 Eighteen O-glycan structures including both core 1 and core 2 structures are now demonstrated to be present on VWF. 19874459 9 83 gly present 1294:1300 arg2 VWF AND core 1 VWF core 1 PUBTATOR VWF 7450 Eighteen O-glycan structures including both core 1 and core 2 structures are now demonstrated to be present on VWF. 8601595 0 33 gly Glycosylation 0:12 arg1 CD44 CD44 PUBTATOR CD44 960 Glycosylation of CD44 is implicated in CD44-mediated cell adhesion to hyaluronan. 8601595 8 40 gly glycosylation 1726:1738 arg1 CD44 CD44 PUBTATOR CD44 960 Taken together, these observations indicate that changes in glycosylation of CD44 can have profound effects on its interaction with hyaluronic acid and suggest that glycosylation may provide an important regulatory mechanism of CD44 function. 8601595 2 56 gly glycosylation 234:246 arg1 CD44-hyaluronate interaction CD44-hyaluronate interaction PUBTATOR CD44 960 In the present work we examine the role of N-linked glycosylation and Ser-Gly motifs in regulating CD44-hyaluronate interaction. 10397812 0 55 gly glycosylation 33:45 arg1 recombinant IFN-gamma recombinant IFN-gamma PUBTATOR IFN-gamma 3458 Constraints on the transport and glycosylation of recombinant IFN-gamma in Chinese hamster ovary and insect cells. 10397812 2 67 gly N-glycosylation 265:279 arg1 recombinant human IFN-gamma recombinant human IFN-gamma PUBTATOR IFN-gamma 3458 Detailed analysis of the N-glycosylation of recombinant human IFN-gamma by matrix-assisted laser-desorption mass spectrometry showed that the protein secreted by Chinese hamster ovary and baculovirus-infected insect Sf9 cells was associated with complex sialylated or truncated tri-mannosyl core glycans, respectively. 2113054 6 5 gly glycosylation 1171:1183 arg1 sCD4 sCD4 PUBTATOR sCD4 499358 The role of glycosylation in the expression of sCD4 was investigated by mutagenesis of the constructs to remove each of the two N-linked glycosylation sites in turn and both together. 11380948 0 4 gly glycosylation 58:70 arg1 CD16 CD16 PUBTATOR IIIB (CD16 2214 Evidence for a novel polymorphism affecting both N-linked glycosylation and ligand binding of the IgG receptor IIIB (CD16). 11380948 0 4 gly glycosylation 58:70 arg1 the IgG receptor IIIB the IgG receptor IIIB PUBTATOR IIIB (CD16 2214 Evidence for a novel polymorphism affecting both N-linked glycosylation and ligand binding of the IgG receptor IIIB (CD16). 9140729 3 108 gly carbohydrates 433:445 arg1 Asn-30 Asn-30 Asn-30 SpecificSite Asn-30 Since this antibody possesses N-linked carbohydrates on Asn-30 of VH region, which seems to be very close to an antigen-binding site, influence of these carbohydrates on antigen-binding was investigated. 8884270 1 50 gly glycoprotein 145:156 arg1 Fibrillin-1 Fibrillin-1 PUBTATOR Fibrillin-1 2200 Fibrillin-1 is a large cysteine-rich glycoprotein of the 10-nm microfibrils in the extracellular matrix. 16669630 8 47 gly Deglycosylation 1254:1268 arg1 aspartoacylase aspartoacylase OGER aspartoacylase P45381 Deglycosylation of aspartoacylase or mutation at the glycosylation site causes decreased enzyme stability and diminished catalytic activity. 19947664 5 10 gly glycoforms 912:921 arg1 rt-PA rt-PA Cterm rt-PA P00750 In this work, we applied LC-MS with state-of-the-art instrumentation to the characterization of glycoforms of rt-PA. 19947664 1 77 gly glycoprotein 245:256 arg1 Recombinant tissue plasminogen activator Recombinant tissue plasminogen activator OGER Recombinant tissue plasminogen activator P00750 Recombinant tissue plasminogen activator (rt-PA) is a well-characterized glycoprotein with a great deal of published information on its structure, post-translational modifications, and O- and N-glycosylation. 8379944 1 4 gly glycoprotein 195:206 arg1 Lecithin:cholesterol acyltransferase Lecithin:cholesterol acyltransferase PUBTATOR Lecithin:cholesterol acyltransferase 3931 Lecithin:cholesterol acyltransferase (LCAT; phosphatidylcholine-sterol acyltransferase, EC 2.3.1.43) is a glycoprotein which is responsible for the formation of cholesteryl ester in plasma. 8379944 11 66 gly unglycosylated 1550:1563 arg1 the unglycosylated LCAT the unglycosylated LCAT PUBTATOR LCAT 3931 The amount of the unglycosylated LCAT secreted into the culture medium was less than 10% of the wild-type level and the specific activity of this enzyme was decreased to 5% of that of the wild type. 1402806 7 10 gly glycosylation 1182:1194 arg1 the M protein the M protein OGER M protein P54296 Indeed, the glycosylation of the M protein was not inhibited in the presence of tunicamycin, which is indicative of O-glycosylation, as previously reported for BCV and murine hepatitis virus. 25755023 2 53 gly glycoprotein 360:371 arg1 the tumor-associated MUC4 glycoprotein the tumor-associated MUC4 glycoprotein PUBTATOR MUC4 glycoprotein Q99102 Although several strategies have been developed to explore anti-tumor vaccines based on MUC1 glycopeptides, only few studies have focused on vaccines directed against the tumor-associated MUC4 glycoprotein. 25755023 4 59 gly glycosylation 511:523 arg1 MUC4 MUC4 PUBTATOR MUC4 Q99102 The aberrant glycosylation of MUC4 in tumor cells results in an exposure of its peptide backbone and the formation of tumor-associated glycopeptide antigens. 25755023 0 62 gly glycoprotein 62:73 arg1 the tumor-associated MUC4 glycoprotein the tumor-associated MUC4 glycoprotein PUBTATOR MUC4 glycoprotein Q99102 Antibody induction directed against the tumor-associated MUC4 glycoprotein. 9597548 5 34 gly presence 900:907 arg1 this human IgM AND oligosaccharides this human IgM oligosaccharides OGER IgM P01871 Of note is the presence in this human IgM of oligosaccharides containing N-glycolylneuraminic acid and N-acetylneuraminic acid in the ratio of 98:2 as determined using anion-exchange chromatography. 24196967 7 57 gly glycosylation 1081:1093 arg1 ROM1 ROM1 PUBTATOR ROM1 6094 Peripherin, but not ROM1, is glycosylated and we examined the glycosylation site and glycan composition of ROM1 by liquid chromatographic tandem mass spectrometry. 24196967 7 58 gly ROM1 1126:1129 arg1 glycan composition ROM1 glycan composition PUBTATOR ROM1 6094 Peripherin, but not ROM1, is glycosylated and we examined the glycosylation site and glycan composition of ROM1 by liquid chromatographic tandem mass spectrometry. 24196967 7 76 gly glycosylated 1048:1059 arg1 ROM1 ROM1 PUBTATOR ROM1 6094 Peripherin, but not ROM1, is glycosylated and we examined the glycosylation site and glycan composition of ROM1 by liquid chromatographic tandem mass spectrometry. 24196967 7 76 gly glycosylated 1048:1059 arg1 Peripherin Peripherin PUBTATOR Peripherin 5630 Peripherin, but not ROM1, is glycosylated and we examined the glycosylation site and glycan composition of ROM1 by liquid chromatographic tandem mass spectrometry. 16227292 10 51 gly glycans 1538:1544 arg1 Gc Gc glycans Cterm Gc The viability of these recombinant viruses and analysis of growth kinetics indicates that the glycans on Gc are not essential for BUN replication, but they do contribute to the efficiency of virus infection. 16227292 1 55 gly glycoproteins 142:154 arg1 Gc Gc Cterm Gc The membrane glycoproteins (Gn and Gc) of Bunyamwera virus (BUN, family Bunyaviridae) contain three potential sites for the attachment of N-linked glycans: one site (N60) on Gn and two (N624 and N1169) on Gc. 16227292 7 83 gly glycans 1148:1154 arg1 N1169 N1169 N1169 SpecificSite N1169 In contrast, mutant Gc proteins lacking glycans on either N624 or N1169, or both sites, were able to target to the Golgi. 16227292 7 83 gly glycans 1148:1154 arg1 N624 N624 N624 SpecificSite N624 In contrast, mutant Gc proteins lacking glycans on either N624 or N1169, or both sites, were able to target to the Golgi. 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. 16720579 1 30 gly glycoprotein 273:284 arg1 purified chondroitin 6-sulfotransferase-1 purified chondroitin 6-sulfotransferase-1 OGER chondroitin 6-sulfotransferase Q7LGC8 We have shown previously that purified chondroitin 6-sulfotransferase-1 (C6ST-1) was a glycoprotein abundant in N-linked oligosaccharides and could sulfate both chondroitin (C6ST activity) and keratan sulfate (KSST activity); however, functional roles of the N-glycans have remained unclear. 16720579 2 59 gly attached 537:544 arg1 C6ST-1 AND N-glycans C6ST-1 N-glycans OGER C6ST-1 Q7LGC8 In the present study, we show essential roles of N-glycans attached to C6ST-1 in the generation of the active enzyme and in its KSST activity. 16720579 0 73 gly oligosaccharides 9:24 arg1 chondroitin 6-sulfotransferase-1 chondroitin 6-sulfotransferase oligosaccharides OGER chondroitin 6-sulfotransferase Q7LGC8 N-linked oligosaccharides on chondroitin 6-sulfotransferase-1 are required for production of the active enzyme, Golgi localization, and sulfotransferase activity toward keratan sulfate. 16720579 4 83 gly C6ST-1 801:806 arg1 N-glycans C6ST-1 N-glycans OGER C6ST-1 Q7LGC8 A nearly complete removal of N-glycans of the recombinant C6ST-1 by peptide N-glycosidase F increased the C6ST activity but decreased the KSST activity. 9291187 9 36 gly N-glycoprotein 1398:1411 arg1 human 11beta-HSD2 human 11beta-HSD2 PUBTATOR 11beta-HSD2 3291 We conclude that human 11beta-HSD2 is not a N-glycoprotein and N-glycosylation is not essential for the expression of enzyme activity. 9291187 0 39 gly N-glycosylation 0:14 arg1 11beta-hydroxysteroid dehydrogenase type 2 11beta-hydroxysteroid dehydrogenase type 2 OGER 11beta-hydroxysteroid dehydrogenase type 2 P80365 N-glycosylation is not essential for enzyme activity of 11beta-hydroxysteroid dehydrogenase type 2. 15147907 2 0 gly presence 333:340 arg2 the human complement serum glycoprotein C3 AND such monoglucosylated N-glycans the human complement serum glycoprotein C3 such monoglucosylated N-glycans Cterm C3 We report here the presence of such monoglucosylated N-glycans on the human complement serum glycoprotein C3. 15147907 0 4 gly glycans 17:23 arg1 the secreted human complement component C3 C3 glycans Cterm C3 Monoglucosylated glycans in the secreted human complement component C3: implications for protein biosynthesis and structure. 7559653 7 36 gly non-glycosylated 1634:1649 arg1 the non-glycosylated PAF receptor the non-glycosylated PAF receptor PUBTATOR PAF receptor 9768 The binding affinity for PAF is not significantly effected by the presence or location of the carbohydrate, and variations in cell surface expression have little influence on signal transduction, as the non-glycosylated PAF receptor is equally effective for activation of phospholipase C as the native molecule. 7999071 0 14 gly glycosylation 98:110 arg1 human lipoprotein lipase human lipoprotein lipase PUBTATOR lipoprotein lipase 4023 A naturally occurring mutation at the second base of codon asparagine 43 in the proposed N-linked glycosylation site of human lipoprotein lipase: in vivo evidence that asparagine 43 is essential for catalysis and secretion. 11428934 0 12 gly glycoprotein 71:82 arg1 human myelin oligodendrocyte glycoprotein human myelin oligodendrocyte glycoprotein PUBTATOR myelin oligodendrocyte glycoprotein 4340 Conformational analysis of a glycosylated human myelin oligodendrocyte glycoprotein peptide epitope able to detect antibody response in multiple sclerosis. 11428934 1 68 gly glycoprotein 179:190 arg1 MOG MOG PUBTATOR MOG 4340 Myelin oligodendrocyte glycoprotein (MOG), a minor myelin component, is an important central nervous system specific target autoantigen for primary demyelination in autoimmune diseases such as multiple sclerosis (MS). 11428934 1 68 gly glycoprotein 179:190 arg1 Myelin oligodendrocyte glycoprotein Myelin oligodendrocyte glycoprotein PUBTATOR Myelin oligodendrocyte glycoprotein 4340 Myelin oligodendrocyte glycoprotein (MOG), a minor myelin component, is an important central nervous system specific target autoantigen for primary demyelination in autoimmune diseases such as multiple sclerosis (MS). 20208072 5 9 gly glycosylation 989:1001 arg1 human GRP78 human GRP78 PUBTATOR GRP78 3309 Moreover, deletion of the C-terminal ER retention motif in GRP78 alters its cell surface presentation in a dose-dependent manner; however, mutation of the putative O-linked glycosylation site Thr(648) of human GRP78 is without effect. 20208072 5 30 part_of GRP78 1026:1030 arg1 the putative O-linked glycosylation site Thr(648) GRP78 the putative O-linked glycosylation site Thr(648) PUBTATOR SpecificSite GRP78 3309 site Thr(648) Moreover, deletion of the C-terminal ER retention motif in GRP78 alters its cell surface presentation in a dose-dependent manner; however, mutation of the putative O-linked glycosylation site Thr(648) of human GRP78 is without effect. 8286753 2 69 part_of Thr 392:394 arg1 the TfR TfR Thr PUBTATOR SpecificSite TfR 7037 Thr 104 The function of the single O-linked oligosaccharide near the transmembrane domain of the TfR at amino acid Thr 104 is unknown. 8543840 10 104 gly glycosylated 1407:1418 arg1 env protein env protein PUBTATOR env protein 100616444 Thus, the naturally processed form of an env epitope containing an N-linked glycosylation site is derived from env protein that is not glycosylated at the relevant asparagine during biosynthesis. 8407981 2 26 gly glycosylated 215:226 arg1 arom arom PUBTATOR cytochrome P-450(arom) 55010 It was found that cytochrome P-450(arom) purified from human placenta microsomes is glycosylated, and the sugar chain was cleaved with endoglycosidase H (Endo H). 8407981 2 26 gly glycosylated 215:226 arg1 cytochrome P-450 cytochrome P-450 PUBTATOR cytochrome P-450(arom) 55010 It was found that cytochrome P-450(arom) purified from human placenta microsomes is glycosylated, and the sugar chain was cleaved with endoglycosidase H (Endo H). 8407981 3 30 gly glycosylation 303:315 arg1 P-450 P-450 PUBTATOR P-450(arom) 55010 The core glycosylation of P-450(arom) was examined with two heterologous expression systems, cultured insect cells and in vitro translation system. 8407981 3 30 gly glycosylation 303:315 arg1 arom arom PUBTATOR P-450(arom) 55010 The core glycosylation of P-450(arom) was examined with two heterologous expression systems, cultured insect cells and in vitro translation system. 8407981 4 34 gly glycosylated 500:511 arg1 The P-450(arom) protein The P-450(arom) protein PUBTATOR P-450(arom) protein 55010 The P-450(arom) protein expressed in the insect cells was glycosylated, and the sugar chain was sensitive to Endo H. 8407981 0 51 gly glycosylation 5:17 arg1 arom arom PUBTATOR cytochrome P-450(arom) 55010 Core glycosylation of cytochrome P-450(arom). 8407981 0 51 gly glycosylation 5:17 arg1 cytochrome P-450 cytochrome P-450 PUBTATOR cytochrome P-450(arom) 55010 Core glycosylation of cytochrome P-450(arom). 15113889 1 33 gly glycoprotein 209:220 arg1 G G OGER glycoprotein (G P07996 We developed a rational approach to identify a site in the vesicular stomatitis virus (VSV) glycoprotein (G) that is exposed on the protein surface and tolerant of foreign epitope insertion. 15113889 1 33 gly glycoprotein 209:220 arg1 the vesicular stomatitis virus (VSV) glycoprotein the vesicular stomatitis virus (VSV) glycoprotein OGER glycoprotein (G P07996 We developed a rational approach to identify a site in the vesicular stomatitis virus (VSV) glycoprotein (G) that is exposed on the protein surface and tolerant of foreign epitope insertion. 10712595 6 53 gly glycosylated 1104:1115 arg1 the minor human isoform beta-antithrombin the minor human isoform beta-antithrombin PUBTATOR antithrombin 462 The high heparin binding affinity of the salmon inhibitor, Kd of 2.2 and 48 nM at I = 0.15 and 0.3, respectively, is very similar to that of the minor human isoform beta-antithrombin, which is not glycosylated at Asn135. 10712595 7 59 gly glycosylation 1329:1341 arg1 human antithrombin human antithrombin PUBTATOR antithrombin 462 Furthermore, the invariant third-position Ser137 at this glycosylation site of mammalian and chicken antithrombins is substituted by Thr in the salmon, a replacement that has been shown to induce full glycosylation in human antithrombin. 10712595 3 110 part_of antithrombin 473:484 arg1 Asn135 antithrombin Asn135 PUBTATOR AminoAcid antithrombin 462 Asn135 Due to a single nucleotide replacement, Asn135 of the antithrombin in higher vertebrates is substituted by Asp in the salmon homolog. 1535241 1 55 gly glycoprotein 225:236 arg1 The proto-oncogene Wnt-1 The proto-oncogene Wnt-1 PUBTATOR proto-oncogene Wnt-1 22408 The proto-oncogene Wnt-1 encodes a cysteine-rich, secretory glycoprotein implicated in virus-induced mouse mammary cancer and intercellular signaling during vertebrate neural development. 14736728 3 39 gly glycosylation 582:594 arg1 the CLN2 protein the CLN2 protein PUBTATOR CLN2 protein 1200 We introduced the p.Asn286Ser mutation into the wild-type CLN2 cDNA and performed transient expression analysis to determine the effect on the catalytic activity, intracellular targeting, and glycosylation of the CLN2 protein. 6604728 1 61 gly glycoprotein 163:174 arg1 The H-2Kk glycoprotein The H-2Kk glycoprotein PUBTATOR H-2Kk glycoprotein 14972 The H-2Kk glycoprotein has been isolated by monoclonal antibody affinity chromatography, and an analysis of the asparagine-linked oligosaccharides present at the two major glycosylation sites has been performed. 1446688 0 9 gly N-glycosylation 61:75 arg1 human interleukin-6 human interleukin-6 PUBTATOR interleukin-6 3569 Improvement in the heterogeneous N-termini and the defective N-glycosylation of human interleukin-6 by genetic engineering. 2110456 4 55 gly Deglycosylation 436:450 arg1 purified acid beta-glucosidase purified acid beta-glucosidase PUBTATOR acid beta-glucosidase 2629 Deglycosylation of purified acid beta-glucosidase from human placenta with N-Glycanase under native conditions resulted in the removal of an accessible oligosaccharide chain from a single site with no effect on activity, whereas complete deglycosylation resulted in proportionate loss of activity. 15555933 1 15 gly glycoprotein 165:176 arg1 Alpha-Fetoprotein Alpha-Fetoprotein PUBTATOR Alpha-Fetoprotein 174 Alpha-Fetoprotein (AFP) is a 68 kDa glycoprotein expressed at high levels by the fetal liver and yolk with transcription repressed to very low levels after birth. 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. 16873272 1 62 gly glycoprotein 114:125 arg1 Env Env Cterm Env P40189 The foamy virus (FV) glycoprotein precursor gp130(Env) undergoes a highly unusual biosynthesis, resulting in the generation of three particle-associated, mature subunits, leader peptide (LP), surface (SU), and transmembrane (TM). 27266248 3 8 gly unglycosylated 379:392 arg1 unglycosylated rhAFPO unglycosylated rhAFPO Cterm rhAFPO 174 A/rhAFP0, which produces unglycosylated rhAFPO and secretes it to the culture medium, has been constructed. 12235182 1 3 gly glycosylation 155:167 arg1 apolipoprotein B apolipoprotein B PUBTATOR apolipoprotein B 54225 We determined the role of N-linked glycosylation of apolipoprotein B (apoB) in the assembly and secretion of lipoproteins using transfected rat hepatoma McA-RH7777 cells expressing human apoB-17, apoB-37, and apoB-50, three apoB variants with different ability to recruit neutral lipids. 12235182 1 3 gly glycosylation 155:167 arg1 apoB apoB PUBTATOR apoB 54225 We determined the role of N-linked glycosylation of apolipoprotein B (apoB) in the assembly and secretion of lipoproteins using transfected rat hepatoma McA-RH7777 cells expressing human apoB-17, apoB-37, and apoB-50, three apoB variants with different ability to recruit neutral lipids. 22354962 6 51 gly HGF-β 1020:1024 arg1 the mannose receptor HGF the mannose receptor OGER HGF P14210 Mass spectrometric detection of the ligand receptor complex revealed that the binding site of HGF-β was the mannose receptor (MR). 14711516 6 3 gly Recombinant 1003:1013 arg1 GlcNAc Recombinant Thy-1 GlcNAc PUBTATOR Recombinant Thy-1 P04216 Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5). 14711516 6 3 gly Recombinant 1003:1013 arg1 2 Recombinant Thy-1 2 PUBTATOR Recombinant Thy-1 P04216 Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5). 14711516 6 3 gly Recombinant 1003:1013 arg1 Man Recombinant Thy-1 Man PUBTATOR Recombinant Thy-1 P04216 Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5). 14711516 6 3 gly Recombinant 1003:1013 arg1 5 Recombinant Thy-1 5 PUBTATOR Recombinant Thy-1 P04216 Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5). 14711516 4 4 gly N-glycosylation 752:766 arg1 recombinant chicken Thy-1 recombinant chicken Thy-1 PUBTATOR Thy-1 P04216 The disulfide linkage pattern and glycoform distribution on each N-glycosylation site of recombinant chicken Thy-1 from both cell lines were determined by a combination of amino-terminal sequencing and mass spectrometry. 14711516 6 6 part_of Thy-1 1015:1019 arg1 asparagine 60 Recombinant Thy-1 asparagine 60 PUBTATOR SpecificSite Recombinant Thy-1 P04216 asparagine 60 Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5). 14711516 6 41 gly oligosaccharides 1097:1112 arg1 asparagine 23 and 100 asparagine 23 and 100 asparagine 23 and 100 SpecificSite asparagine 23 and 100 Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5). 14711516 6 41 gly oligosaccharides 1097:1112 arg1 100 100 100 SpecificSite asparagine 23 and 100 Recombinant Thy-1 from Lec1 cells contained (GlcNAc)(2)(Man)(5) on asparagine 60, whereas the oligosaccharides on asparagine 23 and 100 contained approximately 80% (GlcNAc)(2)(Man)(4) and approximately 20% (GlcNAc)(2)(Man)(5). 21270153 7 60 gly glycosylation 1371:1383 arg1 the PiT1 receptor the PiT1 receptor PUBTATOR PiT1 receptor 18736 N-linked glycosylation of the receptors was not found to mediate resistance of receptor-expressing BHK cells to GALV or XMRV, as shown by tunicamycin treatment and mutation of the specific glycosylation site of the PiT1 receptor. 12883358 7 50 gly O-glycosylation 1249:1263 arg1 CD44s CD44s PUBTATOR CD44s 960 Furthermore, we observed that changes in N- and O-glycosylation of CD44s could modulate its cleavage. 1385399 7 4 gly N-glycosylation 1276:1290 arg1 human CD2 adhesion functions human CD2 adhesion functions PUBTATOR CD2 914 Thus, N-glycosylation is essential for human CD2 adhesion functions. 1385399 4 10 gly deglycosylated 605:618 arg1 deglycosylated soluble recombinant CD2 deglycosylated soluble recombinant CD2 PUBTATOR CD2 914 Analysis of deglycosylated soluble recombinant CD2 as well as a mutant transmembrane CD2 molecule containing a single Asn65-Gln65 substitution demonstrates that neither deglycosylated CD2 nor the mutant CD2 transmembrane receptor binds CD58 or monoclonal antibodies directed at native CD2 adhesion domain epitopes. 1385399 4 13 gly deglycosylated 762:775 arg1 deglycosylated CD2 deglycosylated CD2 PUBTATOR CD2 914 Analysis of deglycosylated soluble recombinant CD2 as well as a mutant transmembrane CD2 molecule containing a single Asn65-Gln65 substitution demonstrates that neither deglycosylated CD2 nor the mutant CD2 transmembrane receptor binds CD58 or monoclonal antibodies directed at native CD2 adhesion domain epitopes. 1385399 0 44 gly N-glycosylation 0:14 arg1 human CD2 immunoadhesion functions human CD2 immunoadhesion functions PUBTATOR CD2 914 N-glycosylation is required for human CD2 immunoadhesion functions. 21672516 7 38 gly N-glycosylated 1010:1023 arg1 Podnl Podnl Cterm Podnl When Podnl was transfected into osteoblastic cells, the protein with N-glycosylation was detected mainly in the cultured medium, indicating that Podnl is a secreted N-glycosylated protein. 9063619 6 15 gly glycosylation 1002:1014 arg1 IgG IgG Cterm IgG Examples include protein-specific glycosylation within the immunoglobulins and immunoglobulin superfamily and site-specific processing in ribonuclease, Thy-1, IgG, tissue plasminogen activator, and influenza A hemagglutinin. 9063619 6 15 gly glycosylation 1002:1014 arg1 Thy-1 Thy-1 PUBTATOR Thy-1 7070 Examples include protein-specific glycosylation within the immunoglobulins and immunoglobulin superfamily and site-specific processing in ribonuclease, Thy-1, IgG, tissue plasminogen activator, and influenza A hemagglutinin. 16253890 0 43 gly gp120 25:29 arg1 the glycans gp120 the glycans PUBTATOR gp120 3700 Targeting the glycans of gp120: a novel approach aimed at the Achilles heel of HIV. 17095532 4 26 gly deglycosylated 755:768 arg1 deglycosylated Cit s 1 deglycosylated Cit s 1 PUBTATOR Cit s 1 11113 These reagents also inhibited the interaction of Cit s 1 with patients' sera, thus underlining the critical role of glycosylation in the recognition of this protein by patients' IgE and extending previous data showing that deglycosylated Cit s 1 does not possess IgE epitopes. 17095532 0 74 gly glycosylated 52:63 arg1 the glycosylated orange allergen Cit s 1 the glycosylated orange allergen Cit s 1 PUBTATOR Cit s 1 11113 Molecular and immunological characterization of the glycosylated orange allergen Cit s 1. 7914890 0 34 gly Glycosylation 0:12 arg1 arylsulfatase A arylsulfatase A PUBTATOR arylsulfatase A 410 Glycosylation and phosphorylation of arylsulfatase A. 7914890 1 56 gly glycosylation 58:70 arg1 the lysosomal enzyme arylsulfatase A the lysosomal enzyme arylsulfatase A PUBTATOR arylsulfatase A 410 The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing. 8019599 4 1 gly glycosylated 560:571 arg1 both glycosylated and unglycosylated b3 both glycosylated and unglycosylated b3 Cterm b3 443978 Similar amounts of cleavage were observed with both glycosylated and unglycosylated b3. 8019599 4 3 gly unglycosylated 577:590 arg1 both glycosylated and unglycosylated b3 both glycosylated and unglycosylated b3 Cterm b3 443978 Similar amounts of cleavage were observed with both glycosylated and unglycosylated b3. 8019599 5 40 gly glycosylated 701:712 arg1 either glycosylated or unglycosylated b3 either glycosylated or unglycosylated b3 Cterm b3 443978 Greater cleavage of b3 was obtained when human red cell glycophorin A (GPA) was co-expressed with either glycosylated or unglycosylated b3. 8019599 5 44 gly unglycosylated 717:730 arg1 either glycosylated or unglycosylated b3 either glycosylated or unglycosylated b3 Cterm b3 443978 Greater cleavage of b3 was obtained when human red cell glycophorin A (GPA) was co-expressed with either glycosylated or unglycosylated b3. 8019599 8 52 gly glycosylation 1127:1139 arg1 functional b3 functional b3 Cterm b3 443978 We suggest that glycosylation is not essential for the expression of functional b3 in oocytes, but may play a role in enabling the protein to acquire its correct folding with the highest anion transport activity. 8019599 6 62 gly unglycosylated 789:802 arg1 either glycosylated or unglycosylated b3 either glycosylated or unglycosylated b3 Cterm b3 443978 The co-expression of GPA with either glycosylated or unglycosylated b3 increased the stilbene disulphonate-sensitive chloride transport into oocytes at low cRNA concentrations. 8019599 6 64 gly glycosylated 773:784 arg1 either glycosylated or unglycosylated b3 either glycosylated or unglycosylated b3 Cterm b3 443978 The co-expression of GPA with either glycosylated or unglycosylated b3 increased the stilbene disulphonate-sensitive chloride transport into oocytes at low cRNA concentrations. 1367433 6 16 part_of t-PA 1238:1241 arg1 asn 117 t-PA asn 117 PUBTATOR SpecificSite t-PA 18791 asn 117 We found that with one exception, all mutant activators lack the high mannose glycan found at asn 117 of native t-PA. 1367433 3 48 gly glycoprotein 672:683 arg1 tissue-type plasminogen activator tissue-type plasminogen activator PUBTATOR tissue-type plasminogen activator 18791 In order to gain insight into the processing mechanisms, we studied the glycan pattern of a panel of related molecules constructed by insertion, duplication or deletion of the domains encoded by the cDNA of a fibrinolytic glycoprotein, tissue-type plasminogen activator (t-PA). 8638940 11 37 gly glycosylation 1851:1863 arg1 the beta-subunit the beta-subunit OGER subunit P20933 The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase. 8638940 0 76 gly Glycosylation 0:12 arg1 lysosomal glycosylasparaginase lysosomal glycosylasparaginase OGER glycosylasparaginase P20933 Glycosylation and phosphorylation of lysosomal glycosylasparaginase. 10318794 7 22 gly glycoprotein 1216:1227 arg1 wild-type G6PT wild-type G6PT PUBTATOR G6PT 2538 Whereas wild-type G6PT is not a glycoprotein, both T53N and S55N mutants are glycosylated, strongly supporting the ten-helical model for G6PT. 12139935 1 78 gly glycosylated 152:163 arg1 beta(2)-Glycoprotein I beta(2)-Glycoprotein I PUBTATOR beta(2)-Glycoprotein I 350 beta(2)-Glycoprotein I (beta(2)GPI) is a highly glycosylated phospholipid-binding plasma protein comprised of four complement control protein (CCP) domains and a distinct fifth domain. 12139935 0 79 gly -glycoprotein 46:58 arg1 human and bovine beta(2)-glycoprotein I human and bovine beta(2)-glycoprotein I PUBTATOR beta(2)-glycoprotein I 281006 Solution structure of human and bovine beta(2)-glycoprotein I revealed by small-angle X-ray scattering. 12223479 4 34 gly glycosylation 681:693 arg1 the beta4 subunit the beta4 subunit PUBTATOR beta4 subunit 10717 We investigated here the N-linked glycosylation of the beta4 subunit and its effect on the modulation of the hSlo alpha subunit. 12223479 9 58 gly Glycosylation 1480:1492 arg1 the beta4 subunit the beta4 subunit PUBTATOR beta4 subunit 10717 Glycosylation of the beta4 subunit is not required for its binding to the hSlo channel alpha subunit. 12223479 7 88 gly residues 1076:1083 arg1 beta4 beta4 residues PUBTATOR beta4 10717 Enzymatic deglycosylation or mutation of the N-linked glycosylation residues in beta4 converts it to a single lower molecular weight band, even in the presence of the hSlo alpha subunit, suggesting that the beta4 subunit can be present as an immature, core glycosylated form and a mature, highly glycosylated form. 12223479 12 107 gly glycosylation 2013:2025 arg1 its auxiliary beta4 subunit its auxiliary beta4 subunit PUBTATOR beta4 subunit 10717 Taken together, these data show that the pore-forming alpha subunit of the hSlo channel promotes N-linked glycosylation of its auxiliary beta4 subunit, and this in turn influences the modulation of the channel by the beta4 subunit. 9574531 1 15 part_of DRA 171:173 arg1 Pro96-->Ser DRA Pro96-->Ser PUBTATOR AminoAcid DRA 1811 Pro96 The HLA-DR hemizygous B lymphoblastoid cell line, 10.24.6, has a DRA mutation (Pro96-->Ser) that creates a novel glycosylation site at Asn94. 9574531 0 43 gly glycosylation 6:18 arg1 HLA-DRalpha HLA-DRalpha OGER HLA Novel glycosylation of HLA-DRalpha disrupts antigen presentation without altering endosomal localization. 19706343 6 1 gly sialylation 1065:1075 arg1 Asn-143 Asn-143 Asn-143 SpecificSite Asn-143 It revealed significant differences in the extent of sialylation and branching of glycans at Asn-143. 19706343 6 7 gly branching 1081:1089 arg1 Asn-143 Asn-143 Asn-143 SpecificSite Asn-143 It revealed significant differences in the extent of sialylation and branching of glycans at Asn-143. 19706343 9 12 gly units 1519:1523 arg1 Asn-143 Asn-143 Asn-143 SpecificSite Asn-143 These data indicate that some APS patients have beta2GPI molecules with a reduced number of negatively charged sialic acid units in the glycan structure at Asn-143. 19706343 11 43 gly beta2GPI 1953:1960 arg1 site-specific glycan profiles beta2GPI site-specific glycan profiles PUBTATOR beta2GPI 350 Thus, our study suggests a link between site-specific glycan profiles of beta2GPI and the pathology of antiphospholipid syndrome. 19706343 0 50 gly beta-2-glycoprotein 26:44 arg1 beta-2-glycoprotein I beta-2-glycoprotein I OGER beta-2-glycoprotein I P02749 Glycopeptide profiling of beta-2-glycoprotein I by mass spectrometry reveals attenuated sialylation in patients with antiphospholipid syndrome. 19706343 1 68 gly Beta2-glycoprotein 144:161 arg1 Beta2-glycoprotein I Beta2-glycoprotein I PUBTATOR Beta2-glycoprotein I 350 Beta2-glycoprotein I (beta2GPI) is a five-domain protein associated with the antiphospholipid syndrome (APS), however, its normal biological function is yet to be defined. 19706343 2 103 gly N-glycosylated 328:341 arg1 beta2GPI beta2GPI PUBTATOR beta2GPI 350 beta2GPI is N-glycosylated at several asparagine residues and the glycan moiety conjugated to residue 143 has been proposed to interact with the Gly40-Arg43 motif of beta2GPI. 9254044 1 23 gly glycoprotein 213:224 arg1 Glucosidase II Glucosidase II OGER Glucosidase II Glucosidase II is an ER resident glycoprotein involved in the processing of N-linked glycans and probably a component of the ER quality control of glycoproteins. 8443586 0 8 gly glycosylation 70:82 arg1 tissue plasminogen activator tissue plasminogen activator OGER tissue plasminogen activator P00750 Pro to Gly (P219G) in a silent glycosylation site results in complete glycosylation in tissue plasminogen activator. 20663928 3 15 gly glycoprotein 719:730 arg1 Trop-2 Trop-2 PUBTATOR Trop-2 4070 To enhance its potency and targeted tumor therapy, we describe the generation of a novel IgG-based immunotoxin, designated 2L-Rap(Q)-hRS7, comprising Rap(Q), a mutant Rap with the putative N-glycosylation site removed, and hRS7, an internalizing, humanized antibody against Trop-2, a cell surface glycoprotein overexpressed in variety of epithelial cancers. 23909558 7 58 gly O-glycosylated 1044:1057 arg1 erythropoietin erythropoietin PUBTATOR erythropoietin 2056 By implementing the rules into an algorithm to score potential assignments against ETD-MS/MS data, we applied the method to glycopeptides generated from various O-glycosylated proteins including mucin, erythropoietin, fetuin, and an HIV envelope protein, 1086.C gp120. 23909558 7 58 gly O-glycosylated 1044:1057 arg1 mucin mucin PUBTATOR mucin 100508689 By implementing the rules into an algorithm to score potential assignments against ETD-MS/MS data, we applied the method to glycopeptides generated from various O-glycosylated proteins including mucin, erythropoietin, fetuin, and an HIV envelope protein, 1086.C gp120. 18955570 5 49 gly glycosylation 961:973 arg1 GM-CSF-Ralpha GM-CSF-Ralpha PUBTATOR GM-CSF-Ralpha 1438 The other, a point mutation in the paternal X chromosome allele encoding a G174R substitution, altered an N-linked glycosylation site within the cytokine binding domain and glycosylation of GM-CSF-Ralpha, severely reducing GM-CSF binding, receptor signaling, and GM-CSF-dependent functions in primary myeloid cells. 11222739 9 7 part_of hFSH 1478:1481 arg1 hFSH residues 62-73 hFSH hFSH residues 62-73 OGER SpecificSite hFSH residues 62-73 These differences include conformational changes and/or differential distributions of polar or charged residues in loops L3beta (hFSH residues 62-73), the cystine noose, or determinant loop (residues 87-94), and the carboxy-terminal loop (residues 94-104). 9557657 11 28 gly N-glycosylation 2333:2347 arg1 havcr-1 havcr-1 PUBTATOR havcr-1 Q96D42 These results indicate that the Cys-rich region of havcr-1 and its first N-glycosylation site are required for binding of protective MAb 190/4 and HAV receptor function. 9557657 6 32 gly N-glycosylated 1412:1425 arg1 havcr-1 havcr-1 PUBTATOR havcr-1 26762 Treatment of AGMK and cr5 cell extracts with peptide-N-glycosidase F resulted in the collapse of the havcr-1-specific bands into a single band of 56 kDa, which indicated that different N-glycosylated forms of havcr-1 were expressed in these cells. 9557657 3 66 gly glycoprotein 642:653 arg1 The havcr-1 glycoprotein The havcr-1 glycoprotein PUBTATOR havcr-1 glycoprotein 26762 The havcr-1 glycoprotein contains four putative N-glycosylation sites, two in the Cys-rich region and two in the TSP-rich region. 10731668 5 44 gly glycosylation 815:827 arg1 CHO sEGFR CHO sEGFR PUBTATOR CHO sEGFR P00533 The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified. 8780172 5 66 gly nonglycosylated 809:823 arg1 nonglycosylated VEGF/VPF nonglycosylated VEGF/VPF PUBTATOR VEGF 281572 Specifically unaddressed to date is the concern that nonglycosylated VEGF/VPF may be less stable, and therefore characterized by a shorter half-life, reducing its utility for therapeutic angiogenesis. 8780172 4 81 gly glycosylation 640:652 arg1 VEGF/VPF VEGF/VPF PUBTATOR VEGF 281572 The extent to which glycosylation of the 75 asparagine site affects the angiogenic properties of VEGF/VPF has not been studied in vivo. 2328698 3 36 gly nonglycosylated 421:435 arg1 a nonsecreted nonglycosylated rPLP-B protein a nonsecreted nonglycosylated rPLP-B protein PUBTATOR rPLP-B protein 24657 The mol wt of a nonsecreted nonglycosylated rPLP-B protein would be 27,145 based on the mRNA sequence. 2328698 10 48 gly 1-glycoprotein 1386:1399 arg1 human pregnancy-specific beta 1-glycoprotein human pregnancy-specific beta 1-glycoprotein PUBTATOR pregnancy-specific beta 1-glycoprotein 653492 The rPLP-B antiserum showed no cross-reactivity with proteins identified using antisera against rPLP-A, rPL-II, or human pregnancy-specific beta 1-glycoprotein. 27048837 9 22 gly glycosylation 1088:1100 arg1 the protein the protein OGER protein can P35658 Post translational glycosylation of the protein can also be identified. 27048837 1 24 gly glycoprotein 183:194 arg1 Apolipoprotein E Apolipoprotein E PUBTATOR Apolipoprotein E 348 BACKGROUND: Apolipoprotein E (Apo E) is a glycoprotein which acts as a ligand facilitating the uptake of lipids. 7529232 3 11 gly glycosylation 396:408 arg1 the cell-cell recognition molecule CD2 the cell-cell recognition molecule CD2 PUBTATOR CD2 914 In this study a systematic analysis of the effect of glycosylation on the ligand-binding properties of the cell-cell recognition molecule CD2, which consists of two IgSF domains, was undertaken. 7529232 5 35 gly glycosylated 927:938 arg1 fully glycosylated hsCD2 fully glycosylated hsCD2 Cterm hsCD2 914 The ligand and antibody binding properties of this form of hsCD2 were indistinguishable from those of fully glycosylated hsCD2 as determined by surface plasmon resonance analyses. 7529232 4 61 gly CD2 562:564 arg1 single N-acetylglucosamine residues CD2 single N-acetylglucosamine residues PUBTATOR CD2 914 A form of human soluble CD2 (hsCD2) with single N-acetylglucosamine residues at each glycosylation site was produced by inhibiting glucosidase I with N-butyldeoxynojirimycin during expression in Chinese hamster ovary cells and digesting the expressed hsCD2 with endoglycosidase H. 12706379 15 44 gly TSHR 2161:2164 arg1 an important determinant TSHR an important determinant PUBTATOR TSHR P16473 Changes in some critical residues raise questions about variation in function: thus S281 is conserved in all mammals and an important determinant of negative agonist function of TSHR is replaced by R in Sea Bass. 6651835 3 11 part_of IgM 407:409 arg1 Asn 563 IgM Asn 563 OGER SpecificSite IgM P01872 Asn 563 Amino acid and carbohydrate analyses show that Asn 563 of murine IgM is glycosylated only about 44% of the time. 6651835 0 18 gly glycosylation 11:23 arg1 mouse immunoglobulin M. Mouse immunoglobulin IgM mouse immunoglobulin M. Mouse immunoglobulin IgM OGER IgM P01872 Incomplete glycosylation of Asn 563 in mouse immunoglobulin M. Mouse immunoglobulin IgM was prepared from MOPC 104E ascites fluid and [3H]-mannose labeled tumor cells. 21111695 3 42 gly glycosylated 686:697 arg1 annexin A2 annexin A2 PUBTATOR annexin A2 12306 Results of western blot analysis showed that about 36 kDa make specific antibodies appeared specific antibodies in antiserum of immune mice, whereas the best immune effects became visible at the induction time of 48 h. Analyses of 2-dimensional electrophoresis identified the specific antigen was annexin A2, which was a glycosylated protein that contained a glycosylation site, closely related to oncogenesis, cancer development, invasion and metastasis. 10861210 5 15 part_of AE1 819:821 arg1 N555 AE1 N555 PUBTATOR SpecificSite AE1 6521 N555 Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1. 10861210 1 29 gly N-glycosylated 367:380 arg1 AE2 AE2 PUBTATOR AE2 6522 The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop. 10861210 1 29 gly N-glycosylated 367:380 arg1 AE3 AE3 PUBTATOR AE3 6508 The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop. 7711052 6 9 gly plasminogen 1451:1461 arg1 the N-linked sugar plasminogen the N-linked sugar OGER plasminogen P00747 Additionally, in fibrinolysis, within a ternary complex of fibrin, plasminogen and tissue plasminogen activator, the N-linked sugar of plasminogen hinders the initial interaction with tissue plasminogen activator (i.e., it alters Km). 7711052 5 28 part_of Asn-288 1009:1015 arg1 plasminogen plasminogen Asn-288 OGER SpecificSite plasminogen P00747 Asn-288 The N-linked sugar on plasminogen (at Asn-288) within kringle 3 reduces the rate of the beta- to alpha-conformational change, modulates the transport of plasminogen into the extravascular compartment, decreases plasminogen binding to U937 cells and downregulates the activation of plasminogen by both urokinase and tissue plasminogen activator. 7711052 7 51 gly presence 1555:1562 arg2 tissue plasminogen activator AND an N-linked glycan tissue plasminogen activator the kringle 2 domain an N-linked glycan OGER tissue plasminogen activator P00750 domain The presence of an N-linked glycan (at Asn-184) in the kringle 2 domain of tissue plasminogen activator hinders the rearrangement of this ternary complex, decreasing the turnover rate (Kcat). 7711052 5 69 gly sugar 984:988 arg1 plasminogen plasminogen sugar OGER plasminogen P00747 The N-linked sugar on plasminogen (at Asn-288) within kringle 3 reduces the rate of the beta- to alpha-conformational change, modulates the transport of plasminogen into the extravascular compartment, decreases plasminogen binding to U937 cells and downregulates the activation of plasminogen by both urokinase and tissue plasminogen activator. 7475306 0 44 gly env 58:60 arg1 Glycosylation-dependent peptide antigenic determinants env gp46 Glycosylation-dependent peptide antigenic determinants PUBTATOR env gp46 1491939 Glycosylation-dependent peptide antigenic determinants of env gp46 HTLV-1. 2189790 0 33 gly N-glycosylated 13:26 arg1 N-glycosylated human recombinant interleukin-1 alpha N-glycosylated human recombinant interleukin-1 alpha PUBTATOR interleukin-1 alpha 3552 Secretion of N-glycosylated human recombinant interleukin-1 alpha in Saccharomyces cerevisiae. 12877809 11 35 gly glycosylation 1788:1800 arg1 the tree shrew CETP the tree shrew CETP PUBTATOR CETP P11597 CONCLUSION: The possible glycosylation in the tree shrew CETP may be involved in the molecular mechanism of its insusceptibility to atherosclerosis. 12877809 10 103 part_of Asn342 1579:1584 arg1 the tree shrew CETP protein CETP protein Asn342 PUBTATOR AminoAcid CETP protein P11597 Asn342 There is a deletion of an N-linked glycosylation site at Asn342 in the tree shrew CETP protein that may participate in the removal of peripheral cholesterol and cholesteryl ester by increasing its activity of transferring cholesteryl ester. 2745457 0 79 gly glycosylated 36:47 arg1 beta nerve growth factor beta nerve growth factor PUBTATOR form of beta nerve growth factor 18049 Isolation and characterization of a glycosylated form of beta nerve growth factor in mouse submandibular glands. 2745457 0 79 gly glycosylated 36:47 arg1 a glycosylated form a glycosylated form PUBTATOR form of beta nerve growth factor 18049 Isolation and characterization of a glycosylated form of beta nerve growth factor in mouse submandibular glands. 9774483 11 15 gly NCAM 1950:1953 arg1 polysialylation NCAM polysialylation PUBTATOR NCAM 4684 These results suggest that polysialylation of NCAM is influenced by the difference between PST and STX in their preference for N-glycosylation sites on NCAM. 9774483 1 20 gly acid 186:189 arg1 NCAM NCAM acid PUBTATOR NCAM 4684 PST and STX are polysialyltransferases that form polysialic acid in the neural cell adhesion molecule (NCAM), and these two polysialyltransferases often exist together in the same tissues. 9774483 1 20 gly acid 186:189 arg1 neural cell adhesion molecule neural cell adhesion molecule acid PUBTATOR neural cell adhesion molecule 4684 PST and STX are polysialyltransferases that form polysialic acid in the neural cell adhesion molecule (NCAM), and these two polysialyltransferases often exist together in the same tissues. 9774483 5 22 gly acid 996:999 arg1 NCAM.Fc NCAM acid PUBTATOR NCAM 4684 PST and STX were found to add polysialic acid on NCAM.Fc molecules sialylated by alpha-2,3- or alpha-2,6-linkage in vitro, but not on NCAM.Fc lacking either sialic acid. 9774483 12 31 gly polysialylated 2109:2122 arg1 polysialylated NCAM polysialylated NCAM PUBTATOR NCAM 4684 The results also suggest that PST and STX form polysialylated NCAM in a synergistic manner. 9774483 0 41 gly polysialylation 29:43 arg1 the neural cell adhesion molecule the neural cell adhesion molecule PUBTATOR neural cell adhesion molecule 4684 Differential and cooperative polysialylation of the neural cell adhesion molecule by two polysialyltransferases, PST and STX. 9774483 11 45 gly polysialylation 1931:1945 arg1 NCAM NCAM PUBTATOR NCAM 4684 These results suggest that polysialylation of NCAM is influenced by the difference between PST and STX in their preference for N-glycosylation sites on NCAM. 9774483 2 49 gly NCAM 541:544 arg1 polysialylation NCAM polysialylation PUBTATOR NCAM 4684 To determine the individual and combined roles of PST and STX in polysialic acid synthesis, in the present study we asked if PST and STX differ in the acceptor requirement and if PST and STX act together in polysialylation of NCAM. 9774483 2 63 gly polysialylation 522:536 arg1 NCAM NCAM PUBTATOR NCAM 4684 To determine the individual and combined roles of PST and STX in polysialic acid synthesis, in the present study we asked if PST and STX differ in the acceptor requirement and if PST and STX act together in polysialylation of NCAM. 9774483 0 67 gly molecule 73:80 arg1 Differential and cooperative polysialylation neural cell adhesion molecule Differential and cooperative polysialylation PUBTATOR neural cell adhesion molecule 4684 Differential and cooperative polysialylation of the neural cell adhesion molecule by two polysialyltransferases, PST and STX. 9774483 6 69 gly structures 1221:1230 arg1 NCAM NCAM structures PUBTATOR NCAM 4684 These results indicate that both PST and STX have relatively broad specificity on N-glycan core structures in NCAM and no remarkable difference exists between PST and STX for the requirement of core structures and sialic acid attached to the N-glycans of NCAM. 9774483 10 72 gly acid 1868:1871 arg1 NCAM NCAM acid PUBTATOR NCAM 4684 Moreover, a mixture of PST and STX more efficiently synthesized polysialic acid on NCAM than PST or STX alone. 9774483 10 72 gly acid 1868:1871 arg1 STX STX acid PUBTATOR STX 8128 Moreover, a mixture of PST and STX more efficiently synthesized polysialic acid on NCAM than PST or STX alone. 9774483 6 78 gly NCAM 1380:1383 arg1 the N-glycans NCAM the N-glycans PUBTATOR NCAM 4684 These results indicate that both PST and STX have relatively broad specificity on N-glycan core structures in NCAM and no remarkable difference exists between PST and STX for the requirement of core structures and sialic acid attached to the N-glycans of NCAM. 9774483 3 87 gly attached 659:666 arg1 NCAM AND N-glycans NCAM N-glycans PUBTATOR NCAM 4684 We first examined whether PST and STX differ in the requirement of sialic acid and core structures of N-glycans attached to NCAM. 12087059 5 0 gly nonglycosylated 1012:1026 arg1 nonglycosylated Edg-1 nonglycosylated Edg-1 PUBTATOR Edg-1 1901 Although there was no difference in ligand binding ability and ligand-induced MAP kinase activation in the wild-type and mutant receptors, nonglycosylated Edg-1 was much less responsive for ligand-induced internalization. 12087059 6 2 gly N-glycosylated 1359:1372 arg1 N-glycosylated Edg-1 N-glycosylated Edg-1 PUBTATOR Edg-1 1901 Unlike the wild-type receptor, which was associated with the caveolae, nonglycosylated N30D-Edg-1 was dispersed broadly in the membrane fractions separated by sucrose density gradient centrifugation, suggesting that internalization and microdomain localization of N-glycosylated Edg-1 might be related. 12087059 3 5 gly nonglycosylated 663:677 arg1 N30D-Edg-1 N30D-Edg-1 PUBTATOR Edg-1 1901 We found for the first time that Edg-1 is glycosylated in its amino-terminal extracellular portion, and further identified the specific glycosylation site as asparagine 30 by creating a nonglycosylated mutant of Edg-1 (N30D-Edg-1) and transfecting it into cell lines. 12087059 3 13 gly glycosylated 519:530 arg1 Edg-1 Edg-1 PUBTATOR Edg-1 1901 We found for the first time that Edg-1 is glycosylated in its amino-terminal extracellular portion, and further identified the specific glycosylation site as asparagine 30 by creating a nonglycosylated mutant of Edg-1 (N30D-Edg-1) and transfecting it into cell lines. 12087059 6 24 gly nonglycosylated 1166:1180 arg1 nonglycosylated N30D-Edg-1 nonglycosylated N30D-Edg-1 PUBTATOR Edg-1 1901 Unlike the wild-type receptor, which was associated with the caveolae, nonglycosylated N30D-Edg-1 was dispersed broadly in the membrane fractions separated by sucrose density gradient centrifugation, suggesting that internalization and microdomain localization of N-glycosylated Edg-1 might be related. 12087059 0 43 gly Edg-1 46:50 arg1 N-glycans Edg-1 N-glycans PUBTATOR Edg-1 1901 N-glycans of sphingosine 1-phosphate receptor Edg-1 regulate ligand-induced receptor internalization. 12087059 7 58 gly N-glycosylated 1469:1482 arg1 the N-glycosylated Edg-1 the N-glycosylated Edg-1 PUBTATOR Edg-1 1901 Although the precise molecular mechanism of the internalization of the N-glycosylated Edg-1 localized in the microdomain remains to be examined, the present study suggested that the presence of N-linked glycan in the receptor may play a regulatory role in the receptor dynamics in ligand-stimulated mammalian cells. 19916043 5 51 part_of residue 600:606 arg1 the VP7 VP7 residue PUBTATOR SpecificSite VP7 3773131 residue 67 Similar to other human group C rotaviruses, one N-glycosylation site was predicted at amino acid residue 67 on the VP7 of strain GUP188. 1331083 5 13 part_of D 1348:1348 arg1 residues 265-319 cathepsin D, residues 265-319 PUBTATOR SpecificSite cathepsin D, 1509 lysine 203 and residues 265-319 Similar results were obtained for oligosaccharides at homologous sites on a pepsinogen/cathepsin D chimera containing only lysine 203 and residues 265-319 of cathepsin D, although the absolute levels of phosphorylation were lower. 16927286 4 77 gly glycoprotein 570:581 arg1 G G OGER glycoprotein (G P07996 Therefore, we analyzed viral attachment glycoprotein (G) gene sequences from 106 RSV subgroup A isolates collected in New Zealand between 1967 and 2003, and 38 subgroup B viruses collected between 1984 and 2004. 16927286 4 77 gly glycoprotein 570:581 arg1 attachment glycoprotein attachment glycoprotein OGER glycoprotein (G P07996 Therefore, we analyzed viral attachment glycoprotein (G) gene sequences from 106 RSV subgroup A isolates collected in New Zealand between 1967 and 2003, and 38 subgroup B viruses collected between 1984 and 2004. 10497235 9 50 gly glycosylation 1196:1208 arg1 triadin 1 triadin 1 OGER triadin Q13061 The glycosylation site of triadin 1 was localized to asparagine residue 75, and its bitopic arrangement in the membrane was confirmed. 10497235 7 60 gly glycosylated 943:954 arg1 triadin 1 triadin 1 OGER triadin Q13061 The 40-kDa mobility form was shown to correspond to the glycosylated form of triadin 1, not a distinct triadin 2 isoform as previously hypothesized. 21345964 2 31 gly glycoproteins 297:309 arg1 gE gE Cterm gE The two VZV glycoproteins gE and gI form a heterodimer that mediates efficient cell-to-cell spread. 10419504 4 46 gly N-glycosylated 613:626 arg1 NPC1 NPC1 PUBTATOR NPC1 O15118 Tunicamycin treatment resulted in a 140-kDa protein, the deduced size of NPC1, suggesting that NPC1 is N-glycosylated. 10419504 10 68 gly glycoprotein 1418:1429 arg1 NPC1 NPC1 PUBTATOR NPC1 O15118 We conclude that NPC1 is a glycoprotein that must have an intact sterol-sensing domain and leucine zipper motif for cholesterol-mobilizing activity. 8163463 4 0 gly glycosylated 737:748 arg1 kainate receptor subunits kainate receptor subunits OGER subunits 2898 In this study we have shown that both AMPA receptor subunits (GluR1-4) and kainate receptor subunits (GluR6/7) are glycosylated in adult rat brain; however, the kainate receptor subunits are glycosylated to a greater extent. 8163463 4 0 gly glycosylated 737:748 arg1 GluR1-4 GluR1-4 PUBTATOR GluR1 50592 In this study we have shown that both AMPA receptor subunits (GluR1-4) and kainate receptor subunits (GluR6/7) are glycosylated in adult rat brain; however, the kainate receptor subunits are glycosylated to a greater extent. 8163463 4 0 gly glycosylated 737:748 arg1 GluR6/7 GluR6/7 PUBTATOR GluR6 54257 In this study we have shown that both AMPA receptor subunits (GluR1-4) and kainate receptor subunits (GluR6/7) are glycosylated in adult rat brain; however, the kainate receptor subunits are glycosylated to a greater extent. 8163463 4 0 gly glycosylated 737:748 arg1 both AMPA receptor subunits both AMPA receptor subunits OGER AMPA receptor subunits P19493 In this study we have shown that both AMPA receptor subunits (GluR1-4) and kainate receptor subunits (GluR6/7) are glycosylated in adult rat brain; however, the kainate receptor subunits are glycosylated to a greater extent. 8163463 4 76 gly glycosylated 813:824 arg1 the kainate receptor subunits the kainate receptor subunits OGER subunits 2898 In this study we have shown that both AMPA receptor subunits (GluR1-4) and kainate receptor subunits (GluR6/7) are glycosylated in adult rat brain; however, the kainate receptor subunits are glycosylated to a greater extent. 19035324 4 7 gly N-glycosylation 601:615 arg1 HA2 HA2 OGER HA2 HA had highly conservative N-glycosylation site at position 11, 23, 87 and 276 sites of HA1, and two more at position 154 and 213 sites of HA2. 19035324 4 7 gly N-glycosylation 601:615 arg1 HA1 HA1 OGER HA1 HA had highly conservative N-glycosylation site at position 11, 23, 87 and 276 sites of HA1, and two more at position 154 and 213 sites of HA2. 9820138 1 30 gly glycosylated 203:214 arg1 prM prM Cterm prM The three flavivirus glycoproteins prM, E and NS1 are formed by post-translational cleavage and are glycosylated by the addition of N-linked glycans. 9820138 1 30 gly glycosylated 203:214 arg1 NS1 NS1 PUBTATOR NS1 10625 The three flavivirus glycoproteins prM, E and NS1 are formed by post-translational cleavage and are glycosylated by the addition of N-linked glycans. 9820138 1 34 gly glycoproteins 124:136 arg1 prM prM Cterm prM The three flavivirus glycoproteins prM, E and NS1 are formed by post-translational cleavage and are glycosylated by the addition of N-linked glycans. 9820138 1 34 gly glycoproteins 124:136 arg1 NS1 NS1 PUBTATOR NS1 10625 The three flavivirus glycoproteins prM, E and NS1 are formed by post-translational cleavage and are glycosylated by the addition of N-linked glycans. 12755619 2 18 gly glycoprotein 362:373 arg1 GCDFP-15/PIP GCDFP-15/PIP PUBTATOR PIP 5304 GCDFP-15/PIP is also identified as gp17 and/or seminal actin-binding protein (SABP) from seminal vesicles and as extraparotid glycoprotein (EP-GP) from salivary glands. 11361003 11 20 gly TfR 2050:2052 arg1 the N-linked carbohydrates TfR the N-linked carbohydrates PUBTATOR TfR 7037 Since the receptor did not exhibit detectable changes in the CD spectrum of the deglycosylated receptor, it can be concluded that the N-linked carbohydrates of the mature, fully processed TfR are not essential for transferrin binding and conformational stability. 11361003 10 48 gly deglycosylated 1842:1855 arg1 deglycosylated TfR deglycosylated TfR PUBTATOR TfR 7037 To assess changes in the secondary structure of the receptor, circular dichroic spectra were recorded from TfR at pH 5.0, from heat pretreated receptor and from deglycosylated TfR. 11361003 9 49 gly desialylated 1563:1574 arg1 all desialylated and N-deglycosylated TfR variants all desialylated and N-deglycosylated TfR variants PUBTATOR TfR variants 7037 In contrast to the parameters described above, all desialylated and N-deglycosylated TfR variants had exactly the same transferrin binding properties as the native TfR. 11361003 9 53 gly N-deglycosylated 1580:1595 arg1 all desialylated and N-deglycosylated TfR variants all desialylated and N-deglycosylated TfR variants PUBTATOR TfR variants 7037 In contrast to the parameters described above, all desialylated and N-deglycosylated TfR variants had exactly the same transferrin binding properties as the native TfR. 11361003 1 76 gly O-glycosylated 135:148 arg1 The transferrin receptor The transferrin receptor PUBTATOR transferrin receptor 7037 The transferrin receptor (TfR) is a N- and O-glycosylated transmembrane protein mediating the cellular iron uptake by binding and internalization of diferric transferrin. 7813575 4 19 gly glycosylation 714:726 arg1 tissue-type plasminogen activator tissue-type plasminogen activator PUBTATOR tissue-type plasminogen activator 25692 The mannose glycosylation site on the kringle 1 of tissue-type plasminogen activator is modified to yield a compound with a longer half-life in the blood than native tissue-type plasminogen activator. 7813575 4 93 gly activator 777:785 arg1 The mannose glycosylation site tissue-type plasminogen activator The mannose glycosylation site PUBTATOR tissue-type plasminogen activator 25692 The mannose glycosylation site on the kringle 1 of tissue-type plasminogen activator is modified to yield a compound with a longer half-life in the blood than native tissue-type plasminogen activator. 14695241 2 11 part_of Asn357 312:317 arg1 factor V factor V Asn357 OGER AminoAcid factor V P12259 Asn357 This mutation creates an additional potential N-linked glycosylation site (Asn-X-Ser/Thr) in factor V (FV) at Asn357 that could interfere with secretion and/or protein interactions. 14695241 2 11 part_of Asn357 312:317 arg1 FV FV Asn357 Cterm AminoAcid FV P12259 Asn357 This mutation creates an additional potential N-linked glycosylation site (Asn-X-Ser/Thr) in factor V (FV) at Asn357 that could interfere with secretion and/or protein interactions. 10413093 1 52 part_of gp120 226:230 arg1 N306 gp120 N306 PUBTATOR SpecificSite gp120 155971 N306 We have previously shown that an N-glycosylation site of N306 of HIV-1 gp120 is not necessary for the HIV-1 infectivity but protects HIV-1 from neutralising antibodies. 18636497 2 30 gly sialylation 410:420 arg1 human interferon-gamma human interferon-gamma PUBTATOR interferon-gamma 3458 This study reports site- and branch-specific differences in sialylation of human interferon-gamma (IFN-gamma) derived from Chinese hamster ovary (CHO) cell culture. 18636497 2 30 gly sialylation 410:420 arg1 IFN-gamma IFN-gamma PUBTATOR IFN-gamma 3458 This study reports site- and branch-specific differences in sialylation of human interferon-gamma (IFN-gamma) derived from Chinese hamster ovary (CHO) cell culture. 18636497 2 37 gly interferon-gamma 431:446 arg1 sialylation interferon-gamma sialylation PUBTATOR interferon-gamma 3458 This study reports site- and branch-specific differences in sialylation of human interferon-gamma (IFN-gamma) derived from Chinese hamster ovary (CHO) cell culture. 18636497 0 45 gly sialylation 26:36 arg1 recombinant human interferon-gamma recombinant human interferon-gamma PUBTATOR interferon-gamma 3458 Site- and branch-specific sialylation of recombinant human interferon-gamma in Chinese hamster ovary cell culture. 18636497 0 92 gly interferon-gamma 59:74 arg1 branch-specific sialylation interferon-gamma branch-specific sialylation PUBTATOR interferon-gamma 3458 Site- and branch-specific sialylation of recombinant human interferon-gamma in Chinese hamster ovary cell culture. 9690810 0 49 gly glycoprotein 61:72 arg1 full-length mouse platelet glycoprotein IX full-length mouse platelet glycoprotein IX PUBTATOR platelet glycoprotein IX 54368 Characterization of cDNA encoding full-length mouse platelet glycoprotein IX. 21698149 3 2 part_of env 546:548 arg1 the env V1-C4 env the env V1-C4 PUBTATOR SiteSequence env 155971 V1-C4 In this study we investigate the genetic properties of the env V1-C4 of HIV-1B soon after transmission to Trinidadian heterosexuals. 21698149 7 44 part_of env 1235:1237 arg1 the env V1-C4 env the env V1-C4 PUBTATOR SiteSequence env 155971 V1-C4 Signature amino acids within the constant domains of the env V1-C4 were identified for heterosexually transmitted HIV-1B from Trinidad relative to HIV-1B globally. 21698149 5 56 part_of env 860:862 arg1 the env V1-C4 env the env V1-C4 PUBTATOR SiteSequence env 155971 V1-C4 METHODOLOGY/PRINCIPAL FINDINGS: Quasispecies sampling was performed on the env V1-C4 of HIV-1B strains soon after transmission to heterosexual Trinidadians in a cohort of seroconverters. 18585921 1 5 gly glycoprotein 132:143 arg1 Seipin Seipin PUBTATOR Seipin 26580 Seipin, which is encoded by the BSCL2 gene, is a glycoprotein of unknown biochemical function that is associated with dominant hereditary motor neuron diseases. 18585921 2 7 gly N-glycosylation 261:275 arg1 seipin seipin PUBTATOR seipin 26580 Mutations in the N-glycosylation site of seipin are associated with the disease states and result in accumulation of unfolded protein in the endoplasmic reticulum (ER), leading to the unfolded protein response (UPR) and cell death, suggesting that these diseases are tightly associated with ER stress. 10551860 4 6 part_of 74-122 619:624 arg1 ovine PGHS-1 PGHS-1 74-122 PUBTATOR SpecificSite PGHS-1 5742 residues 74-122 X-ray crystallographic studies have led to the hypothesis that PGHS-1 and -2 associate with only one face of the membrane bilayer through a novel, monotopic membrane binding domain (MBD) that is comprised of four short, consecutive, amphipathic alpha-helices (helices A-D) that include residues 74-122 in ovine PGHS-1 (oPGHS-1) and residues 59-108 in human PGHS-2 (hPGHS-2). 10551860 4 54 part_of residues 610:617 arg1 hPGHS-2 hPGHS-2 residues PUBTATOR SpecificSite hPGHS-2 5743 residues 74-122 X-ray crystallographic studies have led to the hypothesis that PGHS-1 and -2 associate with only one face of the membrane bilayer through a novel, monotopic membrane binding domain (MBD) that is comprised of four short, consecutive, amphipathic alpha-helices (helices A-D) that include residues 74-122 in ovine PGHS-1 (oPGHS-1) and residues 59-108 in human PGHS-2 (hPGHS-2). 10551860 4 54 part_of residues 610:617 arg1 human PGHS-2 PGHS-2 residues PUBTATOR SpecificSite PGHS-2 5743 residues 74-122 X-ray crystallographic studies have led to the hypothesis that PGHS-1 and -2 associate with only one face of the membrane bilayer through a novel, monotopic membrane binding domain (MBD) that is comprised of four short, consecutive, amphipathic alpha-helices (helices A-D) that include residues 74-122 in ovine PGHS-1 (oPGHS-1) and residues 59-108 in human PGHS-2 (hPGHS-2). 10551860 4 92 part_of residues 656:663 arg1 hPGHS-2 hPGHS-2 residues PUBTATOR SpecificSite hPGHS-2 5743 residues 59-108 X-ray crystallographic studies have led to the hypothesis that PGHS-1 and -2 associate with only one face of the membrane bilayer through a novel, monotopic membrane binding domain (MBD) that is comprised of four short, consecutive, amphipathic alpha-helices (helices A-D) that include residues 74-122 in ovine PGHS-1 (oPGHS-1) and residues 59-108 in human PGHS-2 (hPGHS-2). 10551860 4 92 part_of residues 656:663 arg1 human PGHS-2 PGHS-2 residues PUBTATOR SpecificSite PGHS-2 5743 residues 59-108 X-ray crystallographic studies have led to the hypothesis that PGHS-1 and -2 associate with only one face of the membrane bilayer through a novel, monotopic membrane binding domain (MBD) that is comprised of four short, consecutive, amphipathic alpha-helices (helices A-D) that include residues 74-122 in ovine PGHS-1 (oPGHS-1) and residues 59-108 in human PGHS-2 (hPGHS-2). 9169007 1 3 gly glycoforms 166:175 arg1 recombinant antithrombin recombinant antithrombin PUBTATOR antithrombin 462 Two major glycoforms of recombinant antithrombin which differ 10-fold in their affinity for the effector glycosaminoglycan, heparin, were previously shown to be expressed in BHK or CHO mammalian cell lines (I. Björk, et al., 1992, Biochem. 9169007 7 5 part_of antithrombin 1124:1135 arg1 Asn 155 antithrombin Asn 155 PUBTATOR SpecificSite antithrombin 462 Asn 155 These results demonstrate that heterogeneous glycosylation of Asn 155 of recombinant antithrombin is responsible for generating the low heparin affinity glycoform. 9169007 11 11 gly antithrombin 2012:2023 arg1 all carbohydrate chains antithrombin all carbohydrate chains PUBTATOR antithrombin 462 These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin. 9169007 6 51 gly variants 782:789 arg1 Heparin-agarose chromatography antithrombin variants Heparin-agarose chromatography PUBTATOR antithrombin variants 462 Heparin-agarose chromatography of the four antithrombin variants revealed that Gln 96, Gln 135, and Gln 192 variants still displayed the two functional heparin-affinity forms previously observed with the wild-type inhibitor, whereas the Gln 155 variant showed only a single functional high heparin affinity form. 9169007 0 100 gly antithrombin 56:67 arg1 individual carbohydrate chains antithrombin individual carbohydrate chains PUBTATOR antithrombin 462 Effect of individual carbohydrate chains of recombinant antithrombin on heparin affinity and on the generation of glycoforms differing in heparin affinity. 10024532 1 16 gly IgG 179:181 arg1 The variable-domain-attached oligosaccharide side chains IgG The variable-domain-attached oligosaccharide side chains Cterm IgG The variable-domain-attached oligosaccharide side chains of a human IgG produced by a human-human-mouse heterohybridoma were analysed. 10024532 0 47 gly IgG 62:64 arg1 Variable domain-linked oligosaccharides IgG Variable domain-linked oligosaccharides Cterm IgG Variable domain-linked oligosaccharides of a human monoclonal IgG: structure and influence on antigen binding. 6935656 5 24 gly glycosylated 936:947 arg1 gp70 gp70 Cterm gp70 The observed differences in gel electrophoretic mobilities and glycopeptide profiles of the respective glycosylated envelope gene cleavage products (gp70) may be accounted for by the presence of an additional oligosaccharide chain on the gp70 of the GIX- virus. 6935656 7 72 gly present 1365:1371 arg1 gp70 AND this oligosaccharide chain gp70 this oligosaccharide chain Cterm gp70 These results suggest that the GIX- virus codes for an extra glycosylation site relative to the GIX+ virus, and this oligosaccharide chain is present both on the envelope gene precursor (Prenv) and on the major cleavage product (gp70). 6935656 5 107 gly presence 1016:1023 arg1 the gp70 AND an additional oligosaccharide chain the gp70 an additional oligosaccharide chain Cterm gp70 The observed differences in gel electrophoretic mobilities and glycopeptide profiles of the respective glycosylated envelope gene cleavage products (gp70) may be accounted for by the presence of an additional oligosaccharide chain on the gp70 of the GIX- virus. 10471642 0 5 gly N-glycosylation 200:214 arg1 transferrin transferrin PUBTATOR transferrin 7018 Microheterogeneity of serum glycoproteins in patients with chronic alcohol abuse compared with carbohydrate-deficient glycoprotein syndrome type I. BACKGROUND: Chronic alcohol abuse alters the normal N-glycosylation of transferrin, producing the carbohydrate-deficient transferrin isoforms. 10471642 4 88 gly N-glycosylation 847:861 arg1 transferrin transferrin PUBTATOR transferrin 7018 A specific antibody directed against the amino acid sequence surrounding the N-432 N-glycosylation site of transferrin was prepared (SZ-350 antibody). 10383441 0 0 gly I 83:83 arg1 mannose phosphorylation DNase I mannose phosphorylation PUBTATOR DNase I 13419 Identification of amino acids that modulate mannose phosphorylation of mouse DNase I, a secretory glycoprotein. 10383441 1 9 gly glycoprotein 162:173 arg1 bovine DNase I bovine DNase I PUBTATOR DNase I 282217 We have reported that bovine DNase I, a secretory glycoprotein, acquires mannose 6-phosphate residues on 12.6% of its Asn-linked oligosaccharides when expressed in COS-1 cells and that the extent of phosphorylation increases to 79.2% when lysines are placed at positions 27 and 74 of the mature protein (Nishikawa, A., Gregory, W. , Frenz, J., Cacia, J., and Kornfeld, S. (1997) J. Biol. 10383441 0 36 gly glycoprotein 98:109 arg1 mouse DNase I mouse DNase I PUBTATOR DNase I 13419 Identification of amino acids that modulate mannose phosphorylation of mouse DNase I, a secretory glycoprotein. 10828943 10 71 gly glycosylation 1656:1668 arg1 SP-A SP-A PUBTATOR SP-A 24773 The glycosylation site of SP-A was located at the side of each subunit, suggesting that the covalently linked carbohydrate moiety probably occupies the spaces between the adjacent globular domains, a location that would not sterically interfere with ligand binding. 18077336 7 2 gly glycosylated 984:995 arg1 A mutant MRAP A mutant MRAP PUBTATOR MRAP Q8TCY5 A mutant MRAP with potential glycosylation sites on both sides of the membrane was singly but not doubly glycosylated, suggesting that MRAP is not monotopic. 18077336 10 15 gly glycosylated 1418:1429 arg1 the MC2 receptor the MC2 receptor OGER MC2 receptor P33032 In the absence of MRAP, MC2 receptor was trapped in the endoplasmic reticulum, but with MRAP, the MC2 receptor was glycosylated and localized on the plasma membrane, where it signaled in response to ACTH. 16823988 11 11 gly glycosylation 1503:1515 arg1 alpha1-antitrypsin alpha1-antitrypsin OGER alpha1-antitrypsin P01009 Changes in glycosylation sites in cancer serum are also observed by glycopeptide mapping using microLC-ESI-TOF-MS where the N83 glycosylation of alpha1-antitrypsin is down regulated. 12766998 6 82 gly glycoproteins 1277:1289 arg1 the HCV3a-Gla glycoproteins the HCV3a-Gla glycoproteins OGER Gla glycoproteins P06280 However, neither conformational E2 antibodies nor antibodies raised against E1 were able to detect the HCV3a-Gla glycoproteins. 11231274 5 8 gly siglec-8 953:960 arg1 the glycan composition siglec-8 the glycan composition OGER siglec-8 Q9NYZ4 To determine any differences in the glycan composition of siglec-5, siglec-7 and siglec-8 that may modify their function, we released and characterized the N-linked oligosaccharide distribution in these three glycoproteins. 11231274 0 14 gly oligosaccharides 45:60 arg1 siglec-7 siglec-7 oligosaccharides OGER siglec-7 Q9Y286 A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition. 11231274 0 14 gly oligosaccharides 45:60 arg1 siglec-5 siglec-5 oligosaccharides OGER siglec-5 O15389 A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition. 11231274 0 14 gly oligosaccharides 45:60 arg1 siglec-8 siglec-8 oligosaccharides OGER siglec-8 Q9NYZ4 A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition. 11231274 6 26 gly released 1302:1309 arg1 siglec-8 AND the carbohydrate mixture siglec-8 the carbohydrate mixture OGER siglec-8 Q9NYZ4 The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans. 11231274 5 30 gly siglec-7 940:947 arg1 the glycan composition siglec-7 the glycan composition OGER siglec-7 Q9Y286 To determine any differences in the glycan composition of siglec-5, siglec-7 and siglec-8 that may modify their function, we released and characterized the N-linked oligosaccharide distribution in these three glycoproteins. 11231274 6 48 gly siglec-7 1131:1138 arg1 The glycan pools siglec-7 The glycan pools OGER siglec-7 Q9Y286 The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans. 11231274 2 60 gly glycoprotein 446:457 arg1 myelin-associated glycoprotein myelin-associated glycoprotein PUBTATOR myelin-associated glycoprotein P20916 In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned. 11231274 5 65 gly siglec-5 930:937 arg1 the glycan composition siglec-5 the glycan composition OGER siglec-5 O15389 To determine any differences in the glycan composition of siglec-5, siglec-7 and siglec-8 that may modify their function, we released and characterized the N-linked oligosaccharide distribution in these three glycoproteins. 11231274 6 74 gly siglec-5 1118:1125 arg1 The glycan pools siglec-5 The glycan pools OGER siglec-5 O15389 The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans. 10749666 4 8 gly glycosylation 699:711 arg1 SERP-1 secretion SERP-1 secretion PUBTATOR SERP-1 27230 In the present study, examination of SERP-1 glycosylation-site mutants showed that the N-linked glycosylation of Asn(172) was essential for SERP-1 secretion, whereas mutation of Asn(99) decreased secretion efficiency, indicating that N-linked glycosylation plays an essential role in the processing and trafficking of SERP-1. 10749666 7 28 gly SERP-1 1590:1595 arg1 viral sialylation SERP-1 viral sialylation PUBTATOR SERP-1 27230 Rather, the role of viral sialylation of SERP-1 likely relates to masking antigenicity or targeting SERP-1 to specific sites of action in vivo. 10749666 6 78 gly SERP-1 1294:1299 arg1 Sialylation SERP-1 Sialylation PUBTATOR SERP-1 27230 Sialylation of SERP-1 by the MST3N gene product creates a uniquely charged species of secreted SERP-1 that is distinct from SERP-1 produced from other eukaryotic expression systems, though this has no apparent effect upon the kinetics of in vitro proteinase inhibition. 10749666 7 80 gly sialylation 1575:1585 arg1 SERP-1 SERP-1 PUBTATOR SERP-1 27230 Rather, the role of viral sialylation of SERP-1 likely relates to masking antigenicity or targeting SERP-1 to specific sites of action in vivo. 9116048 5 39 gly C5a 805:807 arg1 a 6 histidine tag C5a a 6 histidine tag PUBTATOR C5a 362119 Recombinant rat C5a with a 6 histidine tag at the N-terminus was expressed in bacteria, purified and renatured. 8344280 0 63 gly glycoprotein 50:61 arg1 human interleukin 2 glycoprotein variants human interleukin 2 glycoprotein variants PUBTATOR interleukin 2 glycoprotein 3558 Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus-infected Sf21 cells. 9435448 13 15 gly chain 2269:2273 arg1 hSHBG hSHBG chain PUBTATOR hSHBG 6462 This study demonstrated that an additional carbohydrate chain on hSHBG decreases the clearance rate of this protein. 9435448 0 55 gly globulin 34:41 arg1 an additional carbohydrate chain sex hormone-binding globulin an additional carbohydrate chain PUBTATOR sex hormone-binding globulin 100009224 Human variant sex hormone-binding globulin (SHBG) with an additional carbohydrate chain has a reduced clearance rate in rabbit. 1370483 1 7 gly glycoprotein 149:160 arg1 Surfactant protein D Surfactant protein D PUBTATOR Surfactant protein D 25350 Surfactant protein D (SP-D) is a carbohydrate-binding glycoprotein containing a collagen-like domain that is synthesized by alveolar type II epithelial cells. 1370483 1 11 gly Surfactant 95:104 arg1 a carbohydrate-binding glycoprotein Surfactant protein D a carbohydrate-binding glycoprotein PUBTATOR Surfactant protein D 25350 Surfactant protein D (SP-D) is a carbohydrate-binding glycoprotein containing a collagen-like domain that is synthesized by alveolar type II epithelial cells. 1370483 1 46 gly protein 106:112 arg1 a carbohydrate-binding glycoprotein Surfactant protein D a carbohydrate-binding glycoprotein PUBTATOR Surfactant protein D 25350 Surfactant protein D (SP-D) is a carbohydrate-binding glycoprotein containing a collagen-like domain that is synthesized by alveolar type II epithelial cells. 20512925 7 3 gly Glycosylation 928:940 arg1 RAGE RAGE PUBTATOR RAGE Q15109 Glycosylation of RAGE and maximum binding sites for S100A12 on RAGE are also cell type dependent. 20512925 0 5 gly N-glycans 13:21 arg1 RAGE RAGE N-glycans PUBTATOR RAGE 177 Carboxylated N-glycans on RAGE promote S100A12 binding and signaling. 20512925 6 6 gly modified 816:823 arg1 RAGE AND complex glycans RAGE complex glycans PUBTATOR RAGE Q15109 When expressed in mammalian cells, RAGE is modified by complex glycans predominantly at the first glycosylation site (N25IT) that retains S100A12 binding. 20512925 3 23 gly glycans 396:402 arg1 RAGE RAGE glycans PUBTATOR RAGE Q15109 We earlier showed that carboxylated glycans on the V-domain of RAGE promote the binding of HMGB1 and S100A8/A9. 20512925 8 40 gly non-glycosylated 1204:1219 arg1 non-glycosylated sRAGE non-glycosylated sRAGE OGER RAGE 177 Carboxylated glycan-enriched population of RAGE forms higher order multimeric complexes with S100A12, and this ability to multimerize is reduced upon deglycosylation or by using non-glycosylated sRAGE expressed in E. coli. 20512925 8 50 gly RAGE 1069:1072 arg1 Carboxylated glycan-enriched population RAGE Carboxylated glycan-enriched population PUBTATOR RAGE Q15109 Carboxylated glycan-enriched population of RAGE forms higher order multimeric complexes with S100A12, and this ability to multimerize is reduced upon deglycosylation or by using non-glycosylated sRAGE expressed in E. coli. 20512925 10 57 gly N-glycans 1432:1440 arg1 RAGE RAGE N-glycans PUBTATOR RAGE Q15109 These results demonstrate that carboxylated N-glycans on RAGE enhance binding potential and promote receptor clustering and subsequent signaling events following oligomeric S100A12 binding. 26977294 9 47 gly fucosylation 1358:1369 arg1 Fab-TNF α interactions Fab-TNF α interactions PUBTATOR Fab-TNF α 7124 While fucosylation does not affect Fab-TNF α interactions, we found that in the absence of fucosylation the Fc-mAb domain and Fcγ RIIIA are closer and new strong interactions are established between G129 of the receptor and S301 of the Chimera 2 Fc mAb; new polar interactions are also established between the Chimera 2 Fc residues Y299, N300, and S301 and the Fcγ RIIIA residues K128, G129, R130, and R155. 26977294 9 47 gly fucosylation 1358:1369 arg1 Fab-TNF α interactions Fab-TNF α interactions PUBTATOR Fab-TNF α 7124 While fucosylation does not affect Fab-TNF α interactions, we found that in the absence of fucosylation the Fc-mAb domain and Fcγ RIIIA are closer and new strong interactions are established between G129 of the receptor and S301 of the Chimera 2 Fc mAb; new polar interactions are also established between the Chimera 2 Fc residues Y299, N300, and S301 and the Fcγ RIIIA residues K128, G129, R130, and R155. 26977294 10 73 gly fucosylated 1820:1830 arg1 the fucosylated mAbs the fucosylated mAbs PUBTATOR mAbs 72935 These data help to explain the reduced ADCC observed in the fucosylated mAbs suggesting the specific AA residues involved in binding interactions. 12440958 1 70 gly receptor 193:200 arg1 the first two short consensus repeats complement receptor (CR) 2 the first two short consensus repeats PUBTATOR complement receptor (CR) 2 1380 Using X-ray crystallography, we have determined the structure of the first two short consensus repeats (SCRs) of human complement receptor (CR) 2 in complex with C3d. 10424400 10 30 gly glycosylated 1782:1793 arg1 the additionally glycosylated SHBG the additionally glycosylated SHBG PUBTATOR SHBG 6462 This observation suggests the existence of a close link between the estrogen-dependence of breast cancer and the additionally glycosylated SHBG, further supporting a critical role of the protein in the neoplasm. 2721453 11 0 gly oligosaccharides 2265:2280 arg1 secreted TSH TSH oligosaccharides OGER TSH This suggests that the probability of sialylation or sulfation at a second site on these oligosaccharides is similar to that at the first and that anionic oligosaccharides in secreted TSH and free alpha are distributed binomially with regard to sialic acid and sulfate residues. 2721453 3 58 gly subunit 508:514 arg1 Oligosaccharides subunit Oligosaccharides OGER subunit Oligosaccharides from each subunit displayed a distinct anion exchange HPLC profile due to a specific pattern of sialylation and sulfation. 2721453 2 107 gly alpha 381:385 arg1 oligosaccharides TSH alpha oligosaccharides PUBTATOR TSH alpha 12640 By dual metabolic labeling with [35S]sulfate and [3H]mannose, we have characterized oligosaccharides from secreted TSH alpha, TSH beta, and free alpha-subunits released from the apoprotein by enzymatic deglycosylation. 11557028 12 30 gly glycosylated 1824:1835 arg1 hLAT1 hLAT1 PUBTATOR hLAT1 8140 Finally, in in vitro translation, we show that hLAT1 is not a glycosylated protein even though an N-glycosylation site has been predicted in its extracellular loop, consistent with the property of the classical 4F2 light chain. 18085777 2 13 gly glycoform 277:285 arg1 monocyte chemotactic protein-3 monocyte chemotactic protein-3 PUBTATOR monocyte chemotactic protein-3 6354 We have examined the synthesis of a single glycoform of monocyte chemotactic protein-3 (MCP-3), a CC-chemokine that consists of 76 amino acids and one N-glycosylation site. 18085777 2 13 gly glycoform 277:285 arg1 MCP-3 MCP-3 PUBTATOR MCP-3 6354 We have examined the synthesis of a single glycoform of monocyte chemotactic protein-3 (MCP-3), a CC-chemokine that consists of 76 amino acids and one N-glycosylation site. 8352759 0 34 gly VIII 32:35 arg1 human structure of the factor VIII human PUBTATOR structure of the factor VIII 2157 Primary structure of the factor VIII binding domain of human, porcine and rabbit von Willebrand factor. 8352759 0 37 gly factor 25:30 arg1 human structure of the factor VIII human PUBTATOR structure of the factor VIII 2157 Primary structure of the factor VIII binding domain of human, porcine and rabbit von Willebrand factor. 9578495 1 7 gly choriogonadotropin 158:175 arg1 the N-linked oligosaccharide choriogonadotropin the N-linked oligosaccharide OGER choriogonadotropin Several studies indicate that in human choriogonadotropin the N-linked oligosaccharide at position 52 of the alpha-subunit is important for bioactivity. 9578495 5 11 gly choriogonadotropin 693:710 arg1 the alpha52 oligosaccharide choriogonadotropin the alpha52 oligosaccharide OGER choriogonadotropin Therefore, we conclude that the alpha52 oligosaccharide of choriogonadotropin is not involved in signal transduction, but in the stability of the heterodimer. 9578495 0 22 gly deglycosylated 10:23 arg1 Partially deglycosylated human choriogonadotropin Partially deglycosylated human choriogonadotropin OGER choriogonadotropin Partially deglycosylated human choriogonadotropin, stabilized by intersubunit disulfide bonds, shows full bioactivity. 15538777 9 38 gly beta2-glycoprotein 2089:2106 arg1 beta2-glycoprotein I beta2-glycoprotein I OGER beta2-glycoprotein I P02749 The strategy, isolation of glycopeptides followed by MS(n) analysis, efficiently characterized the structures of beta2-glycoprotein I with four N-glycosylation sites and was applied to an analysis of total serum glycoproteins. 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 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. 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. 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. 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. 22279061 0 37 gly SREC-I 13:18 arg1 N-glycans SREC-I N-glycans OGER SREC-I Q14162 N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability. 22279061 12 38 gly SREC-I 1794:1799 arg1 Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans SREC-I Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans OGER SREC-I Q14162 These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis. 7688818 1 69 gly glycoproteins 127:139 arg1 E2 E2 Cterm E2 Sindbis virus glycoproteins E1 and E2 undergo a conformational alteration during early virus-cell interaction at the cell surface (D. Flynn, W. J. Meyer, J. M. MacKenzie, Jr., and R. E. Johnston, J. Virol. 7688818 1 69 gly glycoproteins 127:139 arg1 E1 E1 Cterm E1 Sindbis virus glycoproteins E1 and E2 undergo a conformational alteration during early virus-cell interaction at the cell surface (D. Flynn, W. J. Meyer, J. M. MacKenzie, Jr., and R. E. Johnston, J. Virol. 7688818 11 119 part_of E2 1788:1789 arg1 E2 residues 200 to 202 E2 E2 residues 200 to 202 Cterm SpecificSite E2 residues 200 One of the transitional epitopes identified (E2 residues 200 to 202) lies in the E2 190-216 region, which harbors two major neutralization sites, E2a and E2b, and an N-linked glycosylation site at E2 196. 7642555 2 4 gly modified 337:344 arg1 c-Myc AND O-linked N-acetylglucosamine c-Myc O-linked N-acetylglucosamine PUBTATOR c-Myc 4609 Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc. 7642555 2 4 gly modified 337:344 arg1 c-Myc AND O-GlcNAc c-Myc O-GlcNAc PUBTATOR c-Myc 4609 Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc. 7642555 9 10 gly c-Myc 1120:1124 arg1 the major O-GlcNAc glycosylation site c-Myc the major O-GlcNAc glycosylation site PUBTATOR c-Myc 4609 These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc. 7642555 9 10 part_of c-Myc 1120:1124 arg1 threonine 58 c-Myc threonine 58 PUBTATOR SpecificSite c-Myc 4609 threonine 58 These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc. 7642555 6 17 gly s 607:607 arg1 c-Myc c-Myc s PUBTATOR c-Myc 4609 In this paper, we identified the O-GlcNAc attachment site(s) on c-Myc. 7642555 0 52 gly glycosylated 9:20 arg1 c-Myc c-Myc PUBTATOR c-Myc 4609 c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas. 7642555 9 63 gly glycosylation 1098:1110 arg1 c-Myc c-Myc PUBTATOR c-Myc 4609 These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc. 25643797 5 8 part_of residues 964:971 arg1 HA1 HA1 residues PUBTATOR SpecificSite HA1 23526 residues 295-297 Most of the isolates in lineage h9.4.2.5 lost one potential glycosylation site at residues 200-202, and had an additional one at residues 295-297 in HA1. 19050247 6 25 gly IgG1 1190:1193 arg1 oligosaccharide chains IgG1 oligosaccharide chains Cterm IgG1 Differences in the glycan composition were observed when we analyzed oligosaccharide chains from anaphylactic or non-anaphylactic IgG1, mainly the presence of more sialic acid and fucose residues in anaphylactic molecules. 19050247 7 74 gly residues 1344:1351 arg1 anaphylactic IgG1 IgG1 residues Cterm IgG1 Interestingly, the enzymatic removal of terminal sialic acid residues in anaphylactic IgG1 resulted in loss of the ability to trigger mast cell degranulation and in vivo anaphylactic reaction, similarly to the deglycosylated IgG1 Ab. 26641950 3 39 gly glycosylation 711:723 arg1 recombinant human interferon-β1 recombinant human interferon-β1 PUBTATOR interferon-β1 3456 Here, we report on capillary zone electrophoresis (CZE) coupled via a commercial CESI sheathless interface to an Orbitrap ELITE MS for the intact analysis of recombinant human interferon-β1 (Avonex, rhIFN-β1), a biopharmaceutical with complex glycosylation at a single N-linked site. 8554050 7 20 gly glycoprotein 1132:1143 arg1 II-1 II-1 Cterm II-1 The Po protein and a glycoprotein (II-1) are encoded in the PRB4 gene, and both proteins are absent in the presence of a mutation in the PRB4M PO- allele that contains a single nt change (G--C) at the +1 invariant position of the intron 3 5'donor splice site. 8554050 3 86 gly glycoprotein 459:470 arg1 The Con1 glycoprotein The Con1 glycoprotein PUBTATOR Con1 glycoprotein P02812 The Con1 glycoprotein is encoded in exon 3 of a PRB2 allele (PRB2L CON1+) with a potential N-linked glycosylation site. 26056814 3 1 gly A/California/07/09 679:696 arg1 The glycan-binding selectivity A/California/07/09 HAs The glycan-binding selectivity OGER A/California/07/09 HAs Q92839 The glycan-binding selectivity of three A/California/07/09 vaccine production strains, and purified recombinant A/California/07/09 HAs harboring these mutations was examined via a solid-phase ELISA assay. 8126562 11 49 gly glycosylation 1788:1800 arg1 Kv1.1 Kv1.1 PUBTATOR Kv1.1 16485 Together these results suggest (1) heteromeric assembly of Shaker-like channels is cotranslational, and (2) N207 glycosylation of Kv1.1 occurs but is not required for subunit assembly, transport, or function. 9249051 0 23 gly glycosylated 54:65 arg1 glycosylated recombinant human granulocyte-colony-stimulating factor glycosylated recombinant human granulocyte-colony-stimulating factor PUBTATOR granulocyte-colony-stimulating factor 1440 NMR investigations of the role of the sugar moiety in glycosylated recombinant human granulocyte-colony-stimulating factor. 10698685 6 12 gly glycosylated 846:857 arg1 Recombinant HFARP Recombinant HFARP PUBTATOR HFARP 51129 Recombinant HFARP expressed in COS-7 cells is secreted and glycosylated. 9020858 3 6 gly O-glycosylated 510:523 arg1 LAP LAP PUBTATOR LAP P11117 All TNAPs proved to be N-glycosylated, and only the liver isoform (LAP) is not O-glycosylated. 9020858 9 38 gly deglycosylation 1314:1328 arg1 GPI-linked APs GPI-linked APs OGER APs O14492 With regard to the oligomeric state of alkaline phosphatase (AP) isoforms, the dimer/tetramer equilibrium is dependent on the deglycosylation of glycosyl-phosphatidylinositol(GPI)-free APs, but not GPI-linked APs. 9020858 9 38 gly deglycosylation 1314:1328 arg1 glycosyl-phosphatidylinositol(GPI)-free APs glycosyl-phosphatidylinositol(GPI)-free APs OGER APs O14492 With regard to the oligomeric state of alkaline phosphatase (AP) isoforms, the dimer/tetramer equilibrium is dependent on the deglycosylation of glycosyl-phosphatidylinositol(GPI)-free APs, but not GPI-linked APs. 9020858 3 60 gly N-glycosylated 454:467 arg1 All TNAPs All TNAPs OGER APs All TNAPs proved to be N-glycosylated, and only the liver isoform (LAP) is not O-glycosylated. 28443077 1 38 gly N-glycosylation 452:466 arg1 HA HA Cterm (HA) Increasing evidence suggests that the antigenic change occasionally occurred concomitant with the alterations of the N-glycosylation site profile and hemagglutination activity of the virion surface protein hemagglutinin (HA). 1988041 13 5 part_of serine-194 1954:1963 arg1 human milk BAL BAL serine-194 PUBTATOR SpecificSite BAL P19835 serine-194 These chemical studies established that the active site of human milk BAL is located at serine-194, the N-glycosylation site is present at asparagine-187, the O-glycosylation region is in the 16 repeating units near the C-terminus, and the heparin binding domain is in the N-terminal region. 8437218 4 48 gly glycosylation 1154:1166 arg1 SFFVAP-L env SFFVAP-L env PUBTATOR SFFVAP-L env 30816 Mutants carrying Asn-->Asp mutations at each of the two consensus signals for N-linked glycosylation in the N-terminal domain of SFFVAP-L env (gs1 and gs2), the gs1-2- double mutant, and the gs0 quadruple mutant (mutated at all four signals utilized for N-linked glycosylation in SFFVAP-L env) were made. 2154881 0 23 gly glycoprotein 68:79 arg1 HSV-1 glycoprotein D. Herpes simplex virus HSV-1 glycoprotein D. Herpes simplex virus PUBTATOR HSV-1 glycoprotein D 2532 Antigenic and functional analysis of a neutralization site of HSV-1 glycoprotein D. Herpes simplex virus glycoprotein D is a component of the virion envelope and appears to be involved in attachment, penetration, and cell fusion. 2154881 0 48 gly glycoprotein 105:116 arg1 HSV-1 glycoprotein D. Herpes simplex virus glycoprotein D HSV-1 glycoprotein D. Herpes simplex virus glycoprotein D PUBTATOR glycoprotein D 2532 Antigenic and functional analysis of a neutralization site of HSV-1 glycoprotein D. Herpes simplex virus glycoprotein D is a component of the virion envelope and appears to be involved in attachment, penetration, and cell fusion. 21637915 2 45 gly glycosylated 238:249 arg1 Emmprin Emmprin PUBTATOR Emmprin 682 Emmprin is a glycosylated transmembrane protein containing two immunoglobulin (Ig) domains that is expressed in carcinoma cells and stimulates MMP production by adjacent stromal cells. 2503511 5 43 gly rt-PA 1121:1125 arg1 the total carbohydrate content rt-PA the total carbohydrate content Cterm rt-PA P00750 High mannose oligosaccharides were found to account for 38% of the total carbohydrate content of rt-PA and consisted of Man5GlcNAc2, Man6GlcNAc2, and Man7GlcNAc2 in the ratio 1.8:1.7:1. 2503511 2 56 gly rt-PA 442:446 arg1 the Asn-linked oligosaccharides rt-PA the Asn-linked oligosaccharides Cterm rt-PA P00750 In this study, the structures of the Asn-linked oligosaccharides of Chinese hamster ovary-expressed rt-PA have been elucidated. 2503511 0 66 gly activator 52:60 arg1 Carbohydrate structures tissue plasminogen activator Carbohydrate structures PUBTATOR tissue plasminogen activator P00750 Carbohydrate structures of human tissue plasminogen activator expressed in Chinese hamster ovary cells. 2503511 6 81 gly rt-PA 1298:1302 arg1 the carbohydrate rt-PA the carbohydrate Cterm rt-PA P00750 Two hybrid oligosaccharides were identified and accounted for 3% of the carbohydrate of rt-PA. 8982862 1 36 gly glycoprotein 250:261 arg1 Vitronectin Vitronectin PUBTATOR Vitronectin 7448 Vitronectin is a multifunctional glycoprotein regulating the fibrinolysis, complement, and coagulation systems in plasma, besides exhibiting cell-spreading activity. 1371468 2 15 part_of MEL-14 539:544 arg1 Leu-8 gp90 MEL Leu-8 OGER SpecificSite gp90 MEL P14151 Leu-8 Here we tested the cross-reactivity of four anti-human peripheral lymph node homing receptor (LECAM-1) (also known as LAM-1, LEC-CAM-1, Leu-8, TQ-1, or human equivalent of gp90 MEL-14) antibodies on bovine lymphocytes. 10406958 10 112 gly D 1621:1621 arg1 the sugar moiety saposin D the sugar moiety Cterm saposin D The analysis of the sugar moiety of saposin D revealed that the single N-glycosylation site present in the molecule is mainly modified by high-mannose-type structures varying from two to six hexose residues. 15867500 1 8 gly attached 231:238 arg1 glycoprotein gp120 AND high mannose carbohydrate groups glycoprotein gp120 high mannose carbohydrate groups PUBTATOR gp120 3700 Many clade C isolates of HIV-1 do not react with monoclonal antibody (MAb) 2G12, a broad-ranging human neutralizing MAb that recognizes high mannose carbohydrate groups attached to glycoprotein gp120. 6148073 1 24 gly glycoprotein 218:229 arg1 purified mouse thymocyte Thy-1 glycoprotein purified mouse thymocyte Thy-1 glycoprotein OGER Thy-1 glycoprotein P01831 Four glycopeptides (I, IIA, IIB, III) with different oligosaccharide structures were isolated from purified mouse thymocyte Thy-1 glycoprotein. 6148073 0 28 gly glycoprotein 74:85 arg1 mouse thymocyte Thy-1 glycoprotein mouse thymocyte Thy-1 glycoprotein OGER Thy-1 glycoprotein P01831 Partial characterization of the oligosaccharides of mouse thymocyte Thy-1 glycoprotein. 6148073 10 55 gly glycoprotein 1659:1670 arg1 the previously reported carbohydrate heterogeneity Thy-1 glycoprotein the previously reported carbohydrate heterogeneity OGER Thy-1 glycoprotein P01831 The results presented explain the previously reported carbohydrate heterogeneity of thymocyte Thy-1 glycoprotein. 6148073 0 65 gly glycoprotein 74:85 arg1 the oligosaccharides Thy-1 glycoprotein the oligosaccharides OGER Thy-1 glycoprotein P01831 Partial characterization of the oligosaccharides of mouse thymocyte Thy-1 glycoprotein. 6148073 10 70 gly glycoprotein 1659:1670 arg1 thymocyte Thy-1 glycoprotein thymocyte Thy-1 glycoprotein OGER Thy-1 glycoprotein P01831 The results presented explain the previously reported carbohydrate heterogeneity of thymocyte Thy-1 glycoprotein. 6148073 10 75 gly heterogeneity 1626:1638 arg1 thymocyte Thy-1 glycoprotein thymocyte Thy-1 glycoprotein OGER Thy-1 glycoprotein P01831 The results presented explain the previously reported carbohydrate heterogeneity of thymocyte Thy-1 glycoprotein. 25499264 2 52 gly gp120 440:444 arg1 multiple N-linked glycans envelope glycoprotein gp120 multiple N-linked glycans PUBTATOR envelope glycoprotein gp120 Q14624 The development of phenotypic resistance to CBAs by the virus is accompanied by the deletion of multiple N-linked glycans of the surface envelope glycoprotein gp120. 25499264 3 62 gly N-glycan 465:472 arg1 the transmembrane envelope glycoprotein gp41 envelope glycoprotein gp41 N-glycan PUBTATOR envelope glycoprotein gp41 100616444 Recently, also an N-glycan on the transmembrane envelope glycoprotein gp41 was shown to be deleted during CBA resistance development. 25499264 4 96 gly glycoprotein 754:765 arg1 envelope glycoprotein incorporation envelope glycoprotein incorporation PUBTATOR envelope glycoprotein 100616444 RESULTS: We generated HIV-1 mutants lacking gp41 N-glycans and determined the influence of these glycan deletions on the viral phenotype (infectivity, CD4 binding, envelope glycoprotein incorporation in the viral particle and on the transfected cell, virus capture by DC-SIGN(+) cells and transmission of DC-SIGN-captured virions to CD4(+) T-lymphocytes) and on the phenotypic susceptibility of HIV-1 to a selection of CBAs. 25499264 3 112 gly glycoprotein 504:515 arg1 the transmembrane envelope glycoprotein gp41 the transmembrane envelope glycoprotein gp41 PUBTATOR envelope glycoprotein gp41 100616444 Recently, also an N-glycan on the transmembrane envelope glycoprotein gp41 was shown to be deleted during CBA resistance development. 25499264 2 128 gly glycoprotein 427:438 arg1 the surface envelope glycoprotein gp120 the surface envelope glycoprotein gp120 PUBTATOR envelope glycoprotein gp120 Q14624 The development of phenotypic resistance to CBAs by the virus is accompanied by the deletion of multiple N-linked glycans of the surface envelope glycoprotein gp120. 2451667 5 8 gly glycans 776:782 arg1 the anchored form form of hCG-alpha glycans PUBTATOR form of hCG-alpha 1113 The two asparagine-linked glycans on the anchored form of hCG-alpha were large and heterogeneous when compared to those on the secretory form. 22239659 5 60 gly N-glycoproteins 1013:1027 arg1 hemopexin hemopexin PUBTATOR hemopexin 3263 Application of the workflow to human haptoglobin and hemopexin, two microheterogeneous N-glycoproteins, identified a total of 57 distinct site-specific glycoforms in the case of haptoglobin and 14 site-specific glycoforms of hemopexin. 22239659 5 72 gly glycoforms 1137:1146 arg1 hemopexin hemopexin PUBTATOR hemopexin 3263 Application of the workflow to human haptoglobin and hemopexin, two microheterogeneous N-glycoproteins, identified a total of 57 distinct site-specific glycoforms in the case of haptoglobin and 14 site-specific glycoforms of hemopexin. 9758750 10 2 gly glycosylation 1679:1691 arg1 sG-CSFr sG-CSFr Cterm sG-CSFr Q99062 These results show that while glycosylation of sG-CSFr is not necessary for ligand binding, it appears to be crucial in folding and export from the cell. 10584881 2 19 gly glycoforms 385:394 arg1 AFP AFP PUBTATOR AFP 174 However, there exist glycoforms of AFP which may be more specific for particular tumours. 10584881 4 34 gly AFP 816:818 arg1 the glycan structures AFP the glycan structures PUBTATOR AFP 174 We report here the application of fluorescence labelling, sequential exoglycosidase digestion, high-performance liquid chromatography and matrix-assisted laser desorption ionization in time-of-flight mass spectrometry, to determine the glycan structures of purified serum AFP from patients with HCC and NSGCT. 10584881 0 35 gly alpha-fetoprotein 28:44 arg1 Glycan composition alpha-fetoprotein Glycan composition PUBTATOR alpha-fetoprotein 174 Glycan composition of serum alpha-fetoprotein in patients with hepatocellular carcinoma and non-seminomatous germ cell tumour. 2747653 6 13 gly glycosylated 1107:1118 arg1 The 74K albumin The 74K albumin PUBTATOR 74K albumin 24186 The 74K albumin (unlike the 68K albumin) is glycosylated; a point mutation converting Lys256 to Asn introduces an N-linked glycosylation site that is similar to one found in the sequence of mammalian alpha-fetoproteins. 10682309 12 44 gly non-glycosylated 1874:1889 arg1 non-glycosylated SAP-B non-glycosylated SAP-B OGER SAP O60880 Feeding studies with non-glycosylated SAP-precursor, generating non-glycosylated SAP-B, showed that the loss of the carbohydrate chain reduced the intracellular activity of the protein significantly. 10682309 0 45 gly non-glycosylated 2:17 arg1 SAP-B SAP-B OGER SAP O60880 A non-glycosylated and functionally deficient mutant (N215H) of the sphingolipid activator protein B (SAP-B) in a novel case of metachromatic leukodystrophy (MLD). 10682309 12 49 gly non-glycosylated 1831:1846 arg1 non-glycosylated SAP-precursor non-glycosylated SAP-precursor OGER SAP O60880 Feeding studies with non-glycosylated SAP-precursor, generating non-glycosylated SAP-B, showed that the loss of the carbohydrate chain reduced the intracellular activity of the protein significantly. 10682309 8 59 gly glycosylation 1335:1347 arg1 SAP-B SAP-B OGER SAP O60880 A 643A > C transversion results in the exchange of asparagine 215 to histidine and eliminates the single glycosylation site of SAP-B. 10682309 11 76 gly deglycosylated 1766:1779 arg1 the wild-type SAP-B the wild-type SAP-B OGER SAP O60880 SAP-B in the patient's cells was found to be slightly less stable than the protein in normal cells and corresponded in size to the deglycosylated form of the wild-type SAP-B. 7685965 7 47 gly deglycosylation 1118:1132 arg1 HA1 HA1 OGER HA1 More extensive deglycosylation of HA1 had a differential effect on the clones, allowing one to proliferate but not the other. 9658108 2 27 gly glycoprotein 433:444 arg1 havcr-1 havcr-1 OGER havcr-1 Q96D42 The HAVcr-1 cDNA codes for havcr-1, a 451-amino-acid class I integral-membrane mucin-like glycoprotein of unknown natural function. 17927214 2 17 gly CI-MPR 529:534 arg1 two high-affinity Man-6-P binding sites CI-MPR two high-affinity Man-6-P binding sites PUBTATOR CI-MPR 3482 Previous studies have mapped two high-affinity Man-6-P binding sites of the CI-MPR to domains 1-3 and 9 and one low-affinity site to domain 5 within its 15-domain extracytoplasmic region. 17927214 3 77 gly CI-MPR 846:851 arg1 Man-6-P binding CI-MPR Man-6-P binding PUBTATOR CI-MPR 3482 A structure-based sequence alignment predicts that domain 5 contains the four conserved residues (Gln, Arg, Glu, Tyr) identified as essential for Man-6-P binding by the CD-MPR and domains 1-3 and 9 of the CI-MPR. 7781780 1 4 part_of erythropoietin 285:298 arg1 Asn-24 erythropoietin Asn-24 PUBTATOR SpecificSite erythropoietin 2056 Asn-24 A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site. 7781780 1 7 gly glycosylation 234:246 arg1 recombinant human erythropoietin recombinant human erythropoietin PUBTATOR erythropoietin 2056 A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site. 7781780 0 29 gly erythropoietin 119:132 arg1 a mannose-6-phosphate containing oligomannosidic N-glycan erythropoietin a mannose-6-phosphate containing oligomannosidic N-glycan PUBTATOR erythropoietin 2056 Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells. 9398598 1 54 gly glycoprotein 135:146 arg1 CD4 CD4 PUBTATOR CD4 12504 CD4 is a membrane glycoprotein on T lymphocytes that binds to the same peptide:major histocompatibility complex (MHC) class II molecules recognized by the antigen-specific T cell receptor (TcR). 26333807 3 47 gly glycosylation 387:399 arg1 Tf Tf PUBTATOR Tf 7018 We present a Tf variant affecting the second glycosylation site of Tf and the complications it causes in diagnosing alcoholism. 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 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. 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 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. 10103002 6 4 gly carbohydrate 1135:1146 arg1 gp42 gp42 Cterm gp42 A single N-glycosylation site present in chicken gp42 is conserved among all five of these proteins: carbohydrate analysis of gp42 revealed the presence of a complex type glycan chain at this site. 10103002 3 21 gly glycoprotein 550:561 arg1 gp42 gp42 Cterm gp42 By using a DNA probe amplified with degenerative primers derived from the protein's partial amino acid sequences, a cDNA clone encoding the egg-envelope 42-kDa glycoprotein (gp42) was isolated from a hen's ovary cDNA library. 1647209 8 39 gly glycosylated 1291:1302 arg1 CHO cell-derived IFN-omega 1 CHO cell-derived IFN-omega 1 PUBTATOR IFN-omega 1 3467 Upon treatment with peptide:N-glycosidase F, both bands were shifted to lower molecular masses (20.5 and 18.5 kDa), indicating that CHO cell-derived IFN-omega 1 is glycosylated; Asn-78 was identified as the glycosylation site. 1899031 0 20 part_of plasminogen 74:84 arg1 asparagine-289 plasminogen asparagine-289 PUBTATOR SpecificSite plasminogen 5340 asparagine-289 Oligosaccharide structures present on asparagine-289 of recombinant human plasminogen expressed in a Chinese hamster ovary cell line. 22209231 2 29 gly glycans 420:426 arg1 gp120 gp120 glycans PUBTATOR gp120 155971 The lectins griffithsin (GRFT), cyanovirin-N (CV-N) and scytovirin (SVN) inhibit HIV-1 infection by binding to mannose-rich glycans on gp120. 21380457 2 16 gly haptoglobin 247:257 arg1 glycan changes haptoglobin glycan changes PUBTATOR haptoglobin 3240 Many studies have reported glycan changes of haptoglobin in diseases such as breast cancer and pancreatic cancer. 21380457 1 41 gly glycoprotein 109:120 arg1 Human haptoglobin Human haptoglobin PUBTATOR Human haptoglobin 3240 Human haptoglobin is a serum glycoprotein secreted by the liver with four potential N-glycosylation sites on its β chain. 10858228 5 46 gly glycoprotein 838:849 arg1 gp15 gp15 Cterm gp15 We have cloned and sequenced a gene designated Cpgp40/15 that encodes gp40 as well as gp15, an antigenically distinct, surface glycoprotein also implicated in C. parvum-host cell interactions. 10858228 3 70 gly glycoprotein 395:406 arg1 gp40 gp40 OGER gp40 P09564 In this study we have shown that gp40, a mucin-like glycoprotein, is localized to the surface and apical region of invasive stages of the parasite and is shed from its surface. 10858228 0 71 gly glycoproteins 75:87 arg1 gp15 gp15 Cterm gp15 Molecular cloning and expression of a gene encoding Cryptosporidium parvum glycoproteins gp40 and gp15. 10858228 0 71 gly glycoproteins 75:87 arg1 gp40 gp40 OGER gp40 P09564 Molecular cloning and expression of a gene encoding Cryptosporidium parvum glycoproteins gp40 and gp15. 10374967 0 10 gly glycoprotein 58:69 arg1 glycoprotein H glycoprotein H Cterm herpesvirus-6 glycoprotein H N- and C-terminal external domains of human herpesvirus-6 glycoprotein H affect a fusion-associated conformation mediated by glycoprotein L binding the N terminus. 10374967 0 45 gly glycoprotein 125:136 arg1 glycoprotein L glycoprotein L Cterm glycoprotein L N- and C-terminal external domains of human herpesvirus-6 glycoprotein H affect a fusion-associated conformation mediated by glycoprotein L binding the N terminus. 19753315 14 13 gly glycoprotein 1696:1707 arg1 WT CLRN1 WT CLRN1 PUBTATOR WT CLRN1 P58418 CONCLUSIONS: WT CLRN1 is a glycoprotein localized to the plasma membrane in transfected BHK-21 cells. 19753315 7 68 gly N-glycosylation 762:776 arg1 CLRN1 CLRN1 PUBTATOR CLRN1 P58418 The N-glycosylation status of CLRN1 was studied by using the N-glycosidase F (PNGase F) enzyme and western blotting. 7922031 7 25 gly sugars 1155:1160 arg1 the beta-subunit subunit sugars OGER subunit P0DN86 The carboxy-terminal peptide of the beta-subunit, which is rich in O-linked sugars, is disordered. 7559574 0 23 gly oligosaccharides 31:46 arg1 phosphacan phosphacan oligosaccharides PUBTATOR phosphacan 5803 Complex-type asparagine-linked oligosaccharides on phosphacan and protein-tyrosine phosphatase-zeta/beta mediate their binding to neural cell adhesion molecules and tenascin. 3004936 9 38 gly glycosylated 1497:1508 arg1 a glycosylated MUP protein a glycosylated MUP protein PUBTATOR MUP protein 381531 We show here that mouse urine does indeed contain a glycosylated MUP protein with those properties, presumably the product of the gene that corresponds to pMUP15. 9820620 7 0 part_of Asn 1380:1382 arg1 hGH-V hGH-V Asn PUBTATOR SpecificSite hGH-V 2689 Asn 140 hGH-Vdelta4 has lost the N-glycosylation site at Asn 140 of hGH-V, but acquires a novel site at position 148 as well as a cystein-rich domain in the 65 carboxyl-terminal amino acids, potentially involved in multiple disulfide-bridge formation. 9820620 7 34 gly N-glycosylation 1356:1370 arg1 hGH-V hGH-V PUBTATOR hGH-V 2689 hGH-Vdelta4 has lost the N-glycosylation site at Asn 140 of hGH-V, but acquires a novel site at position 148 as well as a cystein-rich domain in the 65 carboxyl-terminal amino acids, potentially involved in multiple disulfide-bridge formation. 11310976 4 7 gly unglycosylated 1141:1154 arg1 glycophorin A glycophorin A PUBTATOR glycophorin A 2993 The results strongly suggest that glycophorin A in these patients is partly unglycosylated with respect to O-linked glycans. 11310976 3 33 gly galactose 924:932 arg1 glycophorin A glycophorin A galactose PUBTATOR glycophorin A 2993 The results showed a large deficit of N-acetylgalactosamine, galactose, and sialic acid residues in glycophorin A from patients with CDA type I and type II amounting to about 45% and 55%, respectively. 11310976 0 50 gly unglycosylated 100:113 arg1 Glycophorin A Glycophorin A PUBTATOR Glycophorin A 2993 Glycophorin A in two patients with congenital dyserythropoietic anemia type I and type II is partly unglycosylated. 11310976 3 61 gly N-acetylgalactosamine 901:921 arg1 glycophorin A glycophorin A N-acetylgalactosamine PUBTATOR glycophorin A 2993 The results showed a large deficit of N-acetylgalactosamine, galactose, and sialic acid residues in glycophorin A from patients with CDA type I and type II amounting to about 45% and 55%, respectively. 11310976 3 68 gly residues 951:958 arg1 glycophorin A glycophorin A residues PUBTATOR glycophorin A 2993 The results showed a large deficit of N-acetylgalactosamine, galactose, and sialic acid residues in glycophorin A from patients with CDA type I and type II amounting to about 45% and 55%, respectively. 7944407 1 4 gly glycoprotein 163:174 arg1 SPARC SPARC PUBTATOR SPARC 20692 SPARC (secreted protein, acidic and rich in cysteine) is a secreted, Ca+2-binding glycoprotein that modulates interactions between cells and their immediate extracellular matrix. 24501222 1 58 gly glycoprotein 173:184 arg1 HRG HRG PUBTATOR HRG P04196 Histidine-rich glycoprotein (HRG) is a plasma protein consisting of 6 distinct functional domains and is an important regulator of key cardiovascular processes, including angiogenesis and coagulation. 9311148 1 33 gly heterogeneity 146:158 arg1 human urinary erythropoietin human urinary erythropoietin PUBTATOR erythropoietin 2056 The site-specific glycan heterogeneity of human urinary erythropoietin was investigated by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). 9311148 1 63 gly erythropoietin 177:190 arg1 The site-specific glycan heterogeneity erythropoietin The site-specific glycan heterogeneity PUBTATOR erythropoietin 2056 The site-specific glycan heterogeneity of human urinary erythropoietin was investigated by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). 2226797 1 24 gly variant 217:223 arg1 The carbohydrate structures tissue plasminogen activator variant The carbohydrate structures PUBTATOR tissue plasminogen activator variant P00750 The carbohydrate structures of a genetically engineered human tissue plasminogen activator variant bearing a single N-glycosylation site at Asn 448 are reported. 2226797 0 48 gly variant 64:70 arg1 Carbohydrate structures tissue plasminogen activator variant Carbohydrate structures PUBTATOR tissue plasminogen activator variant P00750 Carbohydrate structures of a human tissue plasminogen activator variant expressed in recombinant Chinese hamster ovary cells. 8631363 9 10 part_of factor-alpha 1590:1601 arg1 Ser 4 tumor necrosis factor-alpha Ser 4 PUBTATOR SpecificSite tumor necrosis factor-alpha 7124 Ser 4 An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4. 8631363 9 62 gly 0-glycosylation 1551:1565 arg1 tumor necrosis factor-alpha tumor necrosis factor-alpha PUBTATOR tumor necrosis factor-alpha 7124 An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4. 8631363 8 73 gly 0-glycosylated 1262:1275 arg1 tumor necrosis factor-alpha tumor necrosis factor-alpha PUBTATOR tumor necrosis factor-alpha 7124 About 20% of tumor necrosis factor-alpha was found to be 0-glycosylated, based on the results of the sugar composition and structure analyses. 2965020 5 44 part_of HP1 1038:1040 arg1 residues 42-102 HP1 residues 42-102 PUBTATOR SpecificSite HP1 23468 residues 42-102 Comparison of the cDNA sequence of HP1 with that of human interleukin 6 disclosed a homology of 65% at the DNA level and of 42% at the protein level with a maximum of 57% for the segment spanning residues 42-102 of mature HP1. 8168913 1 81 gly glycoprotein 176:187 arg1 surface glycoprotein A surface glycoprotein A Cterm surface glycoprotein A Pneumocystis carinii surface glycoprotein A (gpA) exhibits host species-specific phenotypic and genotypic variation. 9032350 0 20 gly glycoprotein 78:89 arg1 glycoprotein H glycoprotein H Cterm 1 glycoprotein H Site-directed and linker insertion mutagenesis of herpes simplex virus type 1 glycoprotein H. 25651845 1 16 gly glycoprotein 161:172 arg1 Protein C Protein C OGER Protein C P02810 Protein C (PC) is a vitamin K-dependent plasma glycoprotein, which upon activation by thrombin in complex with thrombomodulin (TM), regulates the coagulation cascade through a feedback loop inhibition mechanism. 1932748 1 13 gly glycoprotein 221:232 arg1 the platelet membrane glycoprotein IIb the platelet membrane glycoprotein IIb PUBTATOR platelet membrane glycoprotein IIb 3674 We have isolated from an HEL cell cDNA library an alternatively spliced transcript for the platelet membrane glycoprotein IIb (GPIIb) that resulted from the deletion of the 34 amino acids of exon 28 of the GPIIb gene. 16118277 7 38 part_of HA 1198:1199 arg1 N223 HA N223 Cterm SpecificSite HA N223 This observation indicates that specific HA residues, such as N223, increase the sensitivity of the HI assay by altering receptor specificity and/or antibody-antigen binding. 9677334 11 70 part_of TPO 1513:1515 arg1 the Arg10 and Arg17 residues TPO the Arg10 and Arg17 residues PUBTATOR AminoAcid TPO 7066 Arg10 and Arg17 residues Moreover we found that the Arg10 and Arg17 residues of TPO seem to be specific determinants for TPO/c-Mpl recognition. 9677334 11 70 gly TPO 1513:1515 arg1 specific determinants TPO specific determinants PUBTATOR TPO 7066 Moreover we found that the Arg10 and Arg17 residues of TPO seem to be specific determinants for TPO/c-Mpl recognition. 20800224 4 2 gly N-glycosylated 546:559 arg1 mutant (C87S) recombinant NGAL mutant (C87S) recombinant NGAL PUBTATOR NGAL 3934 This study demonstrated that 7-9% of mutant (C87S) recombinant NGAL was N-glycosylated and no O-glycosylation was detected. 20800224 2 3 gly glycans 306:312 arg1 NGAL NGAL glycans PUBTATOR NGAL 3934 There is little information available about complex glycans on NGAL. 8212855 6 56 gly glycoprotein 942:953 arg1 glycoprotein G glycoprotein G OGER glycoprotein G P07996 These common structural features of the gX-like proteins were also found in glycoprotein G (gG) of human herpes simplex virus type 2 (HSV-2) and equine herpesvirus type 4 (EHV-4). 8212855 10 58 gly glycosylated 1637:1648 arg1 p32 p32 PUBTATOR p32 3622 Moreover tunicamycin treatment of cells infected with the virus indicated that p32 was glycosylated. 8212855 11 90 gly glycoprotein 1692:1703 arg1 p32 p32 PUBTATOR p32 3622 This allows us to conclude that p32 is a glycoprotein and like gX of PRV accumulates in the medium of infected cells. 18076768 0 32 part_of Asn 0:2 arg1 gp120 gp120 Asn PUBTATOR SpecificSite gp120 155971 Asn 362 Asn 362 in gp120 contributes to enhanced fusogenicity by CCR5-restricted HIV-1 envelope glycoprotein variants from patients with AIDS. 18076768 0 95 gly glycoprotein 88:99 arg1 HIV-1 envelope glycoprotein HIV-1 envelope glycoprotein PUBTATOR 1 envelope glycoprotein variants 155971 Asn 362 in gp120 contributes to enhanced fusogenicity by CCR5-restricted HIV-1 envelope glycoprotein variants from patients with AIDS. 1367474 3 4 gly glycosylation 480:492 arg1 tPA tPA PUBTATOR tPA P00750 Employing one of these strains to study the effect of glycosylation on secretion, we show that glycosylation in the catalytic domain of tPA plays an important role in folding and/or secretion of the molecule. 23527139 7 28 gly glycoprotein 991:1002 arg1 dengue envelope glycoprotein dengue envelope glycoprotein PUBTATOR envelope glycoprotein 100616444 Pre-processed the PDB coordinates of dengue envelope glycoprotein and other candidate proteins were prepared and energy minimized through AMBER99 force field distributed in MOE software. 23527139 0 87 gly glycoprotein 46:57 arg1 dengue envelope glycoprotein dengue envelope glycoprotein PUBTATOR envelope glycoprotein 100616444 Interaction and inhibition of dengue envelope glycoprotein with mammalian receptor DC-sign, an in-silico approach. 23289760 9 126 part_of gp120 2039:2043 arg1 the V1-V5 region gp120 the V1-V5 region OGER SiteSequence gp120 Q14624 V1-V5 region CONCLUSIONS: These findings suggest that the HIV-1 subtype B' viruses may mutate under the immune pressure, thus becoming resistant to the autologous nAbs, possibly by changing the number of PNGS in the V1-V5 region of the viral gp120. 9401066 0 75 gly glycosylated 56:67 arg1 a new glycosylated fibrinogen variant a new glycosylated fibrinogen variant PUBTATOR fibrinogen variant 2244 Fibrinogen Kaiserslautern (gamma 380 Lys to Asn): a new glycosylated fibrinogen variant with delayed polymerization. 10099302 2 55 gly interferon-gamma 333:348 arg1 the incomplete intracellular sialylation interferon-gamma the incomplete intracellular sialylation PUBTATOR interferon-gamma P01579 In this study, the incomplete intracellular sialylation of interferon-gamma (IFN-gamma), produced by Chinese hamster ovary cell culture, was minimized by supplementing the culture medium with N-acetylmannosamine (ManNAc), a direct intracellular precursor for sialic acid synthesis. 10099302 2 64 gly sialylation 318:328 arg1 IFN-gamma IFN-gamma PUBTATOR IFN-gamma P01579 In this study, the incomplete intracellular sialylation of interferon-gamma (IFN-gamma), produced by Chinese hamster ovary cell culture, was minimized by supplementing the culture medium with N-acetylmannosamine (ManNAc), a direct intracellular precursor for sialic acid synthesis. 10099302 2 64 gly sialylation 318:328 arg1 interferon-gamma interferon-gamma PUBTATOR interferon-gamma P01579 In this study, the incomplete intracellular sialylation of interferon-gamma (IFN-gamma), produced by Chinese hamster ovary cell culture, was minimized by supplementing the culture medium with N-acetylmannosamine (ManNAc), a direct intracellular precursor for sialic acid synthesis. 3123215 1 56 gly glycoprotein 115:126 arg1 Synaptophysin Synaptophysin PUBTATOR Synaptophysin 24804 Synaptophysin is a major glycoprotein of Mr approximately 38,000 (in deglycosylated form: Mr approximately 34,000) characteristic of a certain class of small (30-80 nm diameter) neurosecretory vesicles, including presynaptic vesicles, but also vesicles of various neuroendocrine cells of both neuronal and epithelial phenotype. 9712881 2 46 part_of AE1 223:225 arg1 Glu681 AE1 Glu681 PUBTATOR AminoAcid AE1 6521 Glu681 Glu681 of human AE1 may form part of the anion translocation apparatus and the permeability barrier. 9712881 0 70 part_of protein 55:61 arg1 Glu681 AE1 protein Glu681 PUBTATOR AminoAcid AE1 protein 6521 Glu681 Topology of the region surrounding Glu681 of human AE1 protein, the erythrocyte anion exchanger. 2825202 11 26 gly glycosylated 1745:1756 arg1 glycosylated pro-SAP-1 glycosylated pro-SAP-1 PUBTATOR AminoAcid SAP-1 22941 The molecular mass of glycosylated pro-SAP-1 is estimated at approximately 69 kDa, assuming glycosylation of all four sites. 2825202 12 115 gly glycosylated 1900:1911 arg1 glycosylated pro-SAP-1 glycosylated pro-SAP-1 PUBTATOR AminoAcid SAP-1 22941 The value is close to the reported 70-kDa value for glycosylated pro-SAP-1. 20172850 10 70 gly glycosylation 1253:1265 arg1 nephrin nephrin PUBTATOR nephrin 4868 In an additional patient with later manifestation, we discovered two further novel mutations, including the first one affecting a glycosylation site of nephrin. 17956937 8 37 gly attached 1824:1831 arg2 PSA AND oligosaccharides PSA oligosaccharides PUBTATOR PSA 354 The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum. 17956937 0 46 gly antigen 50:56 arg1 Oligosaccharide profiles prostate specific antigen Oligosaccharide profiles OGER prostate specific antigen P07288 Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach. 17956937 3 48 gly PSA 610:612 arg1 the glycan profiles PSA the glycan profiles PUBTATOR PSA 354 In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry. 17956937 6 70 gly predominant 1207:1217 arg2 the seminal plasma PSA AND high-mannose and hybrid types the seminal plasma PSA high-mannose and hybrid types PUBTATOR PSA 354 In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase. 17956937 3 73 gly PSA 558:560 arg1 free and complexed forms PSA free and complexed forms PUBTATOR PSA 354 In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry. 17956937 2 98 gly glycoprotein 428:439 arg1 alpha(1)-antichymotrypsin alpha(1)-antichymotrypsin PUBTATOR alpha(1)-antichymotrypsin 12 A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood. 17956937 8 104 gly N-glycosylation 1840:1854 arg1 PSA PSA PUBTATOR PSA 354 The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum. 17956937 1 105 gly antigen 225:231 arg1 The oligosaccharide structures prostate specific antigen The oligosaccharide structures OGER prostate specific antigen P07288 The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels. 9820842 7 16 gly glycoprotein 1331:1342 arg1 US5 US5 PUBTATOR US5 2703406 These findings establish that US5 does encode a glycoprotein and confirm the appropriateness of naming the US5 gene product gJ. 8364230 2 36 gly glycosylation 610:622 arg1 PK1de1FE1X PK1de1FE1X Cterm PK1de1FE1X 25692 Furthermore, the effect of the novel plasminogen activator (SUN9216), a plasminogen-plasminogen activator chimera, comprising the fibrin kringle 1 domain of a plasminogen, and the two kringles, and the serine protease domains of wild-type tissue plasminogen activator (t-PA), including a modification of the mannose glycosylation site on the kringle 1 of t-PA (PK1de1FE1X), was studied in this model. 8364230 2 36 gly glycosylation 610:622 arg1 t-PA t-PA PUBTATOR t-PA 25692 Furthermore, the effect of the novel plasminogen activator (SUN9216), a plasminogen-plasminogen activator chimera, comprising the fibrin kringle 1 domain of a plasminogen, and the two kringles, and the serine protease domains of wild-type tissue plasminogen activator (t-PA), including a modification of the mannose glycosylation site on the kringle 1 of t-PA (PK1de1FE1X), was studied in this model. 8364230 2 62 gly t-PA 649:652 arg1 the mannose glycosylation site t-PA the mannose glycosylation site PUBTATOR t-PA 25692 Furthermore, the effect of the novel plasminogen activator (SUN9216), a plasminogen-plasminogen activator chimera, comprising the fibrin kringle 1 domain of a plasminogen, and the two kringles, and the serine protease domains of wild-type tissue plasminogen activator (t-PA), including a modification of the mannose glycosylation site on the kringle 1 of t-PA (PK1de1FE1X), was studied in this model. 3200844 3 43 gly glycoprotein 402:413 arg1 np62 np62 PUBTATOR np62 65274 The major (62 kDa) nuclear pore glycoprotein (np62) was purified from rat liver nuclear envelopes by immunoaffinity chromatography and preparative gel electrophoresis. 12064867 4 10 gly deglycosylation 703:717 arg1 gp120 gp120 PUBTATOR gp120 3700 We found that soluble CD4 inhibited the deglycosylation of gp120 only when gp120 was caught by D7324 and not by NEA9205. 12064867 8 33 gly glycosylation 1314:1326 arg1 prototype HIV-1 LAI gp120 prototype HIV-1 LAI gp120 PUBTATOR gp120 155971 Finally, we determined the structural class of the glycan of one V1 glycosylation site of prototype HIV-1 LAI gp120, which remained unsolved from previous studies, and found that it belonged to the complex type of glycans. 12064867 1 43 gly glycosylation 149:161 arg1 HIV-1 envelope glycoprotein gp120 HIV-1 envelope glycoprotein gp120 PUBTATOR gp120 155971 Several functions have been assigned to the extensive glycosylation of HIV-1 envelope glycoprotein gp120, especially immune escape mechanisms, but the intramolecular interactions between gp120 and its carbohydrate complement are not well understood. 8643111 7 8 gly found 1433:1437 arg2 mLL2 AND the VK-appended oligosaccharides mLL2 the VK-appended oligosaccharides PUBTATOR mLL2 Q9UMN6 The humanized LL2 (hLL2), lacking light chain variable region glycosylation, exhibited immunoreactivities that were comparable to that of chimeric LL2 (cLL2), which was shown previously to have antigen-binding properties similar to its murine counterpart, suggesting that the VK-appended oligosaccharides found in mLL2 are not necessary for antigen binding. 8099782 5 23 gly deglycosylated 863:876 arg1 deglycosylated saposin B deglycosylated saposin B Cterm deglycosylated saposin B Neither native saposin B nor deglycosylated saposin B were hydrolyzed by trypsin, endoproteinase Glu-C (V-8), chymotrypsin, or a mixture of acid proteases isolated from human testis. 8099782 2 31 gly B 360:360 arg1 The carbohydrate chain saposin B The carbohydrate chain Cterm saposin B The carbohydrate chain of saposin B was removed and deglycosylated saposin B was characterized and compared with native saposin B. Deglycosylated saposin B stimulated the enzymatic hydrolysis of ganglioside GM1 by acid beta-galactosidase and sulfatide by arylsulfatase A to the same extent as native saposin B. 8099782 2 73 gly deglycosylated 378:391 arg1 deglycosylated saposin B deglycosylated saposin B Cterm deglycosylated saposin B The carbohydrate chain of saposin B was removed and deglycosylated saposin B was characterized and compared with native saposin B. Deglycosylated saposin B stimulated the enzymatic hydrolysis of ganglioside GM1 by acid beta-galactosidase and sulfatide by arylsulfatase A to the same extent as native saposin B. 8099782 7 93 gly deglycosylated 1138:1151 arg1 native and deglycosylated saposin B native and deglycosylated saposin B Cterm native and deglycosylated saposin B When native and deglycosylated saposin B were reduced under denaturing conditions and refolded under identical conditions examination of the refolded products indicated that each protein was refolded in a qualitatively different way. 8099782 3 95 gly deglycosylated 649:662 arg1 deglycosylated saposin B deglycosylated saposin B Cterm deglycosylated saposin B In addition deglycosylated saposin B bound sulfatide and GM1 ganglioside identical to native saposin B. 10597188 1 87 gly glycoprotein 83:94 arg1 Glycodelin Glycodelin PUBTATOR Glycodelin 5047 Glycodelin is a 28 kDa glycoprotein with structural homology to beta-lactoglobulins, particularly expressed in steroid-responsive tissues of the female reproductive tract. 8783018 0 48 gly glycosylated 39:50 arg1 glycosylated interferon-gamma variants glycosylated interferon-gamma variants PUBTATOR interferon-gamma variants 3458 Mass spectrometric characterization of glycosylated interferon-gamma variants separated by gel electrophoresis. 1448922 3 34 gly Asn-glycosylated 535:550 arg1 11.6K 11.6K Cterm 11.6K We show here that 11.6K is Asn-glycosylated with complex (endo H-resistant) oligosaccharides and that 11.6K is an integral membrane protein. 8388021 8 26 gly glycoprotein 1280:1291 arg1 the envelope glycoprotein the envelope glycoprotein PUBTATOR envelope glycoprotein 17276 The results demonstrate the importance of critical sites within the envelope glycoprotein as determinants of virus virulence. 8388021 5 48 gly glycoprotein 718:729 arg1 the envelope glycoprotein gene the envelope glycoprotein gene PUBTATOR envelope glycoprotein 17276 The nucleotide sequence of the envelope glycoprotein gene of each of the seven mutants was determined and the deduced amino acid sequence was compared with parent virus. 1482348 1 18 gly HGF 185:187 arg1 O-glycosylated oligosaccharide HGF O-glycosylated oligosaccharide PUBTATOR HGF 3082 The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated. 1601309 4 30 gly unglycosylated 946:959 arg1 unglycosylated bIL4 unglycosylated bIL4 Cterm bIL4 280824 The bIL4 cDNA is 570 bp in length and contains an open reading frame of 405 nucleotides (nt), coding for a 15.1-kDa precursor of 135 amino acids (aa), which should be reduced to 12.6 kDa for unglycosylated bIL4 after cleavage of a putative hydrophobic leader sequence of 24 aa. 7737160 0 59 gly glycosylated 34:45 arg1 glycosylated porcine platelet factor 4 glycosylated porcine platelet factor 4 OGER platelet factor 4 P02776 The complete primary structure of glycosylated porcine platelet factor 4. 18295294 4 8 part_of nsp4 554:557 arg1 nsp4 glycosylation site N176 nsp4 nsp4 glycosylation site N176 PUBTATOR SpecificSite nsp4 400668 site N176 We used reverse genetics to generate infectious clone viruses (icv) with an alanine substitution at nsp4 glycosylation site N176 or N237, or an asparagine to threonine substitution (nsp4-N258T), which is proposed to confer a temperature sensitive phenotype. 18295294 4 18 part_of site 573:576 arg1 nsp4-N258T nsp4 site PUBTATOR SpecificSite nsp4 400668 site N176 We used reverse genetics to generate infectious clone viruses (icv) with an alanine substitution at nsp4 glycosylation site N176 or N237, or an asparagine to threonine substitution (nsp4-N258T), which is proposed to confer a temperature sensitive phenotype. 18295294 4 50 part_of N237 586:589 arg1 nsp4-N258T nsp4 N237 PUBTATOR SpecificSite nsp4 400668 N237 We used reverse genetics to generate infectious clone viruses (icv) with an alanine substitution at nsp4 glycosylation site N176 or N237, or an asparagine to threonine substitution (nsp4-N258T), which is proposed to confer a temperature sensitive phenotype. 3087774 4 0 part_of alpha-chain 513:523 arg1 Asn-946 alpha-chain Asn-946 PUBTATOR SpecificSite alpha-chain 2217 site, Asn-946 A third potential Asn-Xaa-Thr/Ser glycosylation site, Asn-946 of the alpha-chain, is not modified. 3087774 4 0 part_of alpha-chain 513:523 arg1 A third potential Asn-Xaa-Thr/Ser glycosylation site alpha-chain A third potential Asn-Xaa-Thr/Ser glycosylation site PUBTATOR SpecificSite alpha-chain 2217 site, Asn-946 A third potential Asn-Xaa-Thr/Ser glycosylation site, Asn-946 of the alpha-chain, is not modified. 3087774 3 6 gly alpha-chain 391:401 arg1 carbohydrate attachment alpha-chain carbohydrate attachment PUBTATOR alpha-chain 2217 Two peptides only contained glucosamine, Unambiguous sequence analyses identified Asn-63 of the beta-chain and Asn-268 of the alpha-chain as the sites of carbohydrate attachment. 3087774 3 6 part_of alpha-chain 391:401 arg1 Asn-268 alpha-chain Asn-268 PUBTATOR SpecificSite alpha-chain 2217 Asn-268 Two peptides only contained glucosamine, Unambiguous sequence analyses identified Asn-63 of the beta-chain and Asn-268 of the alpha-chain as the sites of carbohydrate attachment. 3087774 3 6 part_of alpha-chain 391:401 arg1 Asn-63 alpha-chain Asn-63 PUBTATOR SpecificSite alpha-chain 2217 Asn-63 Two peptides only contained glucosamine, Unambiguous sequence analyses identified Asn-63 of the beta-chain and Asn-268 of the alpha-chain as the sites of carbohydrate attachment. 10207016 6 35 gly O-glycosylated 1378:1391 arg1 M protein M protein OGER M protein P54296 In addition, the pre-S2 domain of M protein, but not that of L protein, was found to be partially O-glycosylated by a Gal(beta1-3)GalNAcalpha-, Neu5Ac(alpha2-3)Gal(beta1-3)GalNAcalpha-, or GalNAcalpha-residue. 10207016 2 49 gly N-glycosylated 340:353 arg1 the M protein the M protein OGER M protein P54296 The pre-S2 domain, present only in M and L proteins, is further N-glycosylated at Asn-4 exclusively in the M protein. 18623533 2 20 gly attached 462:469 arg2 IFN-gamma AND the carbohydrate structures IFN-gamma the carbohydrate structures PUBTATOR IFN-gamma 3458 In addition to cell growth, metabolite, and productivity data, a detailed analysis of the carbohydrate structures attached to each glycosylation site of IFN-gamma was achieved using matrix-assisted laser desorption mass spectrometry (MALDI-MS) in combination with exoglycosidase array sequencing. 18623533 2 32 gly glycosylation 479:491 arg1 IFN-gamma IFN-gamma PUBTATOR IFN-gamma 3458 In addition to cell growth, metabolite, and productivity data, a detailed analysis of the carbohydrate structures attached to each glycosylation site of IFN-gamma was achieved using matrix-assisted laser desorption mass spectrometry (MALDI-MS) in combination with exoglycosidase array sequencing. 18623533 0 42 gly interferon-gamma 31:46 arg1 N-glycans interferon-gamma N-glycans PUBTATOR interferon-gamma 3458 N-glycans of recombinant human interferon-gamma change during batch culture of chinese hamster ovary cells. 8034709 11 76 gly unglycosylated 1365:1378 arg1 unglycosylated active SCCE unglycosylated active SCCE PUBTATOR SCCE 5650 The calculated molecular mass of unglycosylated active SCCE was 24.4 kDa. 6175959 10 24 part_of C3d 1196:1198 arg1 1-49 C3d 1-49 PUBTATOR SpecificSite C3d 100861467 residues 1-49 Comparison of residues 1-49 of C3d with a peptide from alpha(2)-macroglobulin [Swenson, R. P. & Howard, J. B. (1980) J. Biol. 6175959 12 70 gly glycosylation 1445:1457 arg1 alpha(2)-macroglobulin alpha(2)-macroglobulin PUBTATOR alpha(2)-macroglobulin 2 255, 8087-8091] shows a previously recognized identity of seven residues around the thiol ester site and a second region of identity around a known glycosylation site of alpha(2)-macroglobulin. 19065542 3 9 gly glycoproteins 502:514 arg1 ribonuclease B ribonuclease B Cterm ribonuclease B Model glycoproteins, including ribonuclease B, fetuin, horseradish peroxidase, and haptoglobin, were used here. 19065542 3 9 gly glycoproteins 502:514 arg1 haptoglobin haptoglobin OGER haptoglobin P00738 Model glycoproteins, including ribonuclease B, fetuin, horseradish peroxidase, and haptoglobin, were used here. 12237688 1 28 gly glycosylated 152:163 arg1 Human recombinant interferon-gamma Human recombinant interferon-gamma PUBTATOR interferon-gamma(IFN-gamma 3458 Human recombinant interferon-gamma(IFN-gamma) is not glycosylated at site 25 Asn or 97 Asn, but its bioactivity is the same as the native one. 12237688 1 28 gly glycosylated 152:163 arg1 IFN-gamma IFN-gamma PUBTATOR interferon-gamma(IFN-gamma 3458 Human recombinant interferon-gamma(IFN-gamma) is not glycosylated at site 25 Asn or 97 Asn, but its bioactivity is the same as the native one. 9140197 1 8 gly glycoprotein 208:219 arg1 glycoprotein 2 glycoprotein 2 PUBTATOR glycoprotein 2 2813 Two monoclonal antibody escape virus mutants (MARs), rescued from a human MAb to glycoprotein 2 (G2) and a bank vole monoclonal antibody (MAb) directed to glycoprotein 1 (G1) of Puumala virus, strain Sotkamo, were produced by using a combination of neutralization tests and antigen detection. 9140197 1 8 gly glycoprotein 208:219 arg1 G2 G2 PUBTATOR 2 (G2 2813 Two monoclonal antibody escape virus mutants (MARs), rescued from a human MAb to glycoprotein 2 (G2) and a bank vole monoclonal antibody (MAb) directed to glycoprotein 1 (G1) of Puumala virus, strain Sotkamo, were produced by using a combination of neutralization tests and antigen detection. 9140197 0 14 gly glycoproteins 58:70 arg1 G2 G2 Cterm G2 2813 Single amino acid substitutions in Puumala virus envelope glycoproteins G1 and G2 eliminate important neutralization epitopes. 9140197 0 14 gly glycoproteins 58:70 arg1 G1 G1 Cterm G1 5544 Single amino acid substitutions in Puumala virus envelope glycoproteins G1 and G2 eliminate important neutralization epitopes. 9140197 1 19 gly glycoprotein 282:293 arg1 glycoprotein 1 glycoprotein 1 PUBTATOR glycoprotein 1 5544 Two monoclonal antibody escape virus mutants (MARs), rescued from a human MAb to glycoprotein 2 (G2) and a bank vole monoclonal antibody (MAb) directed to glycoprotein 1 (G1) of Puumala virus, strain Sotkamo, were produced by using a combination of neutralization tests and antigen detection. 9140197 1 19 gly glycoprotein 282:293 arg1 G1 G1 Cterm G1 5544 Two monoclonal antibody escape virus mutants (MARs), rescued from a human MAb to glycoprotein 2 (G2) and a bank vole monoclonal antibody (MAb) directed to glycoprotein 1 (G1) of Puumala virus, strain Sotkamo, were produced by using a combination of neutralization tests and antigen detection. 7535613 11 62 part_of PSA 1606:1608 arg1 Asn 61 PSA Asn 61 PUBTATOR SpecificSite PSA P07288 site, Asn 61 The PSA glycosylation site, Asn 61, is fully accessible to the solvent and is enclosed in a positive region of the isopotential map. 7535613 11 62 part_of PSA 1606:1608 arg1 The PSA glycosylation site PSA The PSA glycosylation site PUBTATOR SpecificSite PSA P07288 site, Asn 61 The PSA glycosylation site, Asn 61, is fully accessible to the solvent and is enclosed in a positive region of the isopotential map. 2041080 6 13 gly HA1 1200:1202 arg1 the carbohydrate HA1 the carbohydrate Cterm HA1 The observation that these mutants were not cleaved, even when the carbohydrate at asparagine 22 of HA1 was absent, underscores the fact that the basic peptide had to be generated by insertion to obtain cleavage. 18404400 3 26 part_of lysine 418:423 arg1 NTPDase3 NTPDase3 lysine PUBTATOR SpecificSite NTPDase3 956 lysine 79 The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7). 9820847 2 30 gly glycoprotein 432:443 arg1 VP7 VP7 Cterm VP7 The nucleotide sequence of the human (ID 45/2) rotavirus genome segment 8/9, which encodes the serotype-specific glycoprotein (VP7) has been determined. 7510285 1 29 gly glycoprotein 192:203 arg1 the L6 antigen the L6 antigen PUBTATOR L6 antigen 4071 The murine monoclonal antibody (mAb) L6 recognizes an integral membrane glycoprotein that is highly expressed on lung, breast, colon, and ovarian carcinomas and is referred to as the L6 antigen. 2571506 5 21 part_of Asn 826:828 arg1 CDR CDR)2 Asn PUBTATOR SpecificSite CDR)2 1039 Asn 58 The VH441 gene segment and all seven mAb contain a potential glycosylation site at Asn 58 in complementarity-determining region (CDR)2. 2571506 10 33 gly Glycosylation 1494:1506 arg1 CDR2 CDR2 PUBTATOR CDR2 1039 Glycosylation of CDR2 might contribute to the unique properties of this VH domain. 16845394 4 39 gly glycoprotein 734:745 arg1 its ligand P-selectin glycoprotein 1 its ligand P-selectin glycoprotein 1 PUBTATOR P-selectin glycoprotein 1 6404 This alteration increased the affinity of P-selectin for its ligand P-selectin glycoprotein 1 (PSGL-1) and thereby the strength of P-selectin-mediated rolling adhesion. 16845394 4 39 gly glycoprotein 734:745 arg1 PSGL-1 PSGL-1 PUBTATOR PSGL-1 6404 This alteration increased the affinity of P-selectin for its ligand P-selectin glycoprotein 1 (PSGL-1) and thereby the strength of P-selectin-mediated rolling adhesion. 11676606 8 46 part_of CD154 1220:1224 arg1 asparagine 240 CD154 asparagine 240 PUBTATOR SpecificSite CD154 959 asparagine 240 Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions. 11676606 6 69 gly structures 768:777 arg1 sCD154 CD154 structures PUBTATOR CD154 959 Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates. 6195967 0 38 gly heterogeneity 19:31 arg1 group-specific component group-specific component OGER group-specific component P02774 Post-translational heterogeneity of the human vitamin D-binding protein (group-specific component). 6195967 0 38 gly heterogeneity 19:31 arg1 the human vitamin D-binding protein the human vitamin D-binding protein PUBTATOR vitamin D-binding protein 2638 Post-translational heterogeneity of the human vitamin D-binding protein (group-specific component). 6195967 9 43 gly carbohydrate 1252:1263 arg1 Gc1 Gc1 carbohydrate PUBTATOR Gc1 79751 The cyanogen bromide fragment containing the galactosamine-containing carbohydrate in Gc1 was partially sequenced through 20 residues from the amino terminus. 11948877 3 28 gly albumin-p-aminophenyl 1094:1114 arg1 BSA-(GlcNAc)17 albumin BSA-(GlcNAc)17 OGER albumin P02768 It could be demonstrated for the first time, by use of UDP-6-biotinyl-Gal as a donor substrate, that the human recombinant galactosyltransferases beta3Gal-T5, beta4Gal-T1, and beta4Gal-T4 mediate biotinylation of the neoglycoconjugate bovine serum albumin-p-aminophenyl N-acetyl-beta-D-glucosaminide (BSA-(GlcNAc)17) and ovalbumin. 8132647 0 37 gly glycoprotein 28:39 arg1 GP-3 GP-3 OGER GP-3, a P05106 GP-3, a newly characterized glycoprotein on the inner surface of the zymogen granule membrane, undergoes regulated secretion. 8892291 1 24 gly glycoprotein 204:215 arg1 p23 p23 PUBTATOR p23 56351 Two mAb, C6B6 and 7D10, each significantly reduced infection of mice by Cryptosporidium parvum and reacted with a 23-kDa glycoprotein (p23) of geographically disperse C. parvum isolates. 2771955 0 116 gly glycoprotein 15:26 arg1 Human platelet glycoprotein IX Human platelet glycoprotein IX PUBTATOR platelet glycoprotein IX 2815 Human platelet glycoprotein IX: an adhesive prototype of leucine-rich glycoproteins with flank-center-flank structures. 1359371 0 14 gly glycoprotein 59:70 arg1 the avian Thy-1 glycoprotein the avian Thy-1 glycoprotein PUBTATOR Thy-1 glycoprotein 7070 Molecular cloning and primary structure of the avian Thy-1 glycoprotein. 9008840 4 20 gly Gp21 701:704 arg1 the glycan Gp21 the glycan Cterm Gp21 Different glycoforms were found for the glycan of Gp21 derived from two different batches of commercial HSTF. 9008840 8 76 gly glycoforms 1325:1334 arg1 Gp21 Gp21 Cterm Gp21 These observations indicate that the terminal GlcNAc residue in the minor glycoforms of Gp21 is exclusively located in the alpha (1-->3) branch of the Gp21 glycan. 8514796 1 2 gly unglycosylated 303:316 arg1 The erythropoietin receptor The erythropoietin receptor PUBTATOR erythropoietin receptor 13857 The erythropoietin receptor (EPO-R) is synthesized in transfected Ba/F3 cells as a major 64-kDa endoglycosidase H (Endo H)-sensitive species, with a single N-linked oligosaccharide, and a minor 62-kDa unglycosylated form. 3498943 0 79 gly glycoprotein 67:78 arg1 the murine cytotoxic T-cell membrane glycoprotein Ly-3 the murine cytotoxic T-cell membrane glycoprotein Ly-3 PUBTATOR T-cell membrane glycoprotein Ly-3 12526 Molecular characterization of the murine cytotoxic T-cell membrane glycoprotein Ly-3 (CD8). 8349598 1 61 gly present 271:277 arg2 thyrotropin AND Asn-linked oligosaccharides thyrotropin Asn-linked oligosaccharides OGER thyrotropin Asn-linked oligosaccharides terminating with the sequence SO4-4GalNAc beta 1,4GlcNAc beta 1,2Man alpha (S4GGnM) are present on the glycoprotein hormones lutropin and thyrotropin, pro-opiomelanocortin, and tissue factor pathway inhibitor. 8349598 1 61 gly present 271:277 arg1 tissue factor pathway inhibitor AND Asn-linked oligosaccharides tissue factor pathway inhibitor Asn-linked oligosaccharides OGER tissue factor pathway inhibitor P10646 Asn-linked oligosaccharides terminating with the sequence SO4-4GalNAc beta 1,4GlcNAc beta 1,2Man alpha (S4GGnM) are present on the glycoprotein hormones lutropin and thyrotropin, pro-opiomelanocortin, and tissue factor pathway inhibitor. 8349598 1 61 gly present 271:277 arg1 lutropin AND Asn-linked oligosaccharides lutropin Asn-linked oligosaccharides OGER lutropin Asn-linked oligosaccharides terminating with the sequence SO4-4GalNAc beta 1,4GlcNAc beta 1,2Man alpha (S4GGnM) are present on the glycoprotein hormones lutropin and thyrotropin, pro-opiomelanocortin, and tissue factor pathway inhibitor. 8349598 7 73 gly acceptors 1590:1598 arg1 Trf Trf acceptors PUBTATOR Trf 7018 In contrast Bowes, EL-4, and B16L6 cell extracts transferred GalNAc to oligosaccharides acceptors on Trf but not on hCG. 8349598 7 73 gly acceptors 1590:1598 arg1 hCG hCG acceptors OGER hCG In contrast Bowes, EL-4, and B16L6 cell extracts transferred GalNAc to oligosaccharides acceptors on Trf but not on hCG. 8349598 5 85 gly acceptors 1172:1180 arg1 transferrin transferrin acceptors PUBTATOR transferrin 7018 We have examined a number of tissues and cultured cell lines for the transfer of sulfate to the trisaccharide acceptor GGnM and transfer of GalNAc to oligosaccharide acceptors on protein which do, human chorionic gonadotropin (hCG), and do not, transferrin (Trf), contain the PXR/K motif. 8349598 1 90 gly present 271:277 arg2 thyrotropin AND Asn-linked oligosaccharides thyrotropin Asn-linked oligosaccharides OGER thyrotropin Asn-linked oligosaccharides terminating with the sequence SO4-4GalNAc beta 1,4GlcNAc beta 1,2Man alpha (S4GGnM) are present on the glycoprotein hormones lutropin and thyrotropin, pro-opiomelanocortin, and tissue factor pathway inhibitor. 8349598 1 90 gly present 271:277 arg1 tissue factor pathway inhibitor AND Asn-linked oligosaccharides tissue factor pathway inhibitor Asn-linked oligosaccharides OGER tissue factor pathway inhibitor P10646 Asn-linked oligosaccharides terminating with the sequence SO4-4GalNAc beta 1,4GlcNAc beta 1,2Man alpha (S4GGnM) are present on the glycoprotein hormones lutropin and thyrotropin, pro-opiomelanocortin, and tissue factor pathway inhibitor. 8349598 1 90 gly present 271:277 arg1 lutropin AND Asn-linked oligosaccharides lutropin Asn-linked oligosaccharides OGER lutropin Asn-linked oligosaccharides terminating with the sequence SO4-4GalNAc beta 1,4GlcNAc beta 1,2Man alpha (S4GGnM) are present on the glycoprotein hormones lutropin and thyrotropin, pro-opiomelanocortin, and tissue factor pathway inhibitor. 9689919 9 95 gly glycoprotein 1557:1568 arg1 a functional soluble secreted PEDF glycoprotein a functional soluble secreted PEDF glycoprotein PUBTATOR PEDF glycoprotein 281386 Thus, the bovine PEDF cDNA isolated here codes for a functional soluble secreted PEDF glycoprotein. 12175779 6 56 gly glycosylation 796:808 arg1 GLUT11 GLUT11 PUBTATOR GLUT11 66035 The putative glycosylation site of GLUT11 is present in loop 1. 3778488 4 3 gly glycosylation 613:625 arg1 aFGF aFGF PUBTATOR aFGF 2246 A potential glycosylation site Asn114-Gly115-Ser116 is present in aFGF but the mitogen does not bind to lectins suggesting that it may not be glycosylated. 2317204 2 62 gly B 275:275 arg1 degrading proteoglycan aggregates cathepsin B degrading proteoglycan aggregates PUBTATOR cathepsin B 1508 Cathepsin L was found to be much more extensive than cathepsin B in degrading proteoglycan aggregates. 11230417 1 31 gly B 298:298 arg1 the high-mannose-type glycans RNase B the high-mannose-type glycans OGER RNase B P07998 The production of mannosidase activity by all currently recognized species of human viridans group streptococci was determined using an assay in which bacterial growth was dependent on the degradation of the high-mannose-type glycans of RNase B and subsequent utilization of released mannose. 8325990 4 27 gly oligosaccharide 1018:1032 arg1 Asn289 Asn289 Asn289 AminoAcid Asn289 Removal of both N- and O-linked oligosaccharide from HPg resulted in a slight increase in the Kcat/Km for its activation, while a glycoform containing tetrasialyl-tetra-antennary complex oligosaccharide on Asn289 was a slightly poorer substrate for UK than plasma HPg, which contains bisialyl-biantennary complex carbohydrate on Asn289. 8325990 4 44 gly carbohydrate 1144:1155 arg1 Asn289 Asn289 Asn289 AminoAcid Asn289 Removal of both N- and O-linked oligosaccharide from HPg resulted in a slight increase in the Kcat/Km for its activation, while a glycoform containing tetrasialyl-tetra-antennary complex oligosaccharide on Asn289 was a slightly poorer substrate for UK than plasma HPg, which contains bisialyl-biantennary complex carbohydrate on Asn289. 8325990 5 57 gly glycans 1244:1250 arg1 Asn289 Asn289 Asn289 AminoAcid Asn289 The most dramatic differences were observed for HPgs with high mannose-type glycans on Asn289. 7685769 1 20 gly glycosylated 286:297 arg1 Recombinant human granulocyte colony stimulating factor Recombinant human granulocyte colony stimulating factor PUBTATOR granulocyte colony stimulating factor 1440 Recombinant human granulocyte colony stimulating factor (G-CSF) produced in Chinese hamster ovary cells is glycosylated. 7685769 1 20 gly glycosylated 286:297 arg1 G-CSF G-CSF PUBTATOR G-CSF 1440 Recombinant human granulocyte colony stimulating factor (G-CSF) produced in Chinese hamster ovary cells is glycosylated. 7685769 0 25 gly glycoforms 127:136 arg1 recombinant human granulocyte colony-stimulating factor recombinant human granulocyte colony-stimulating factor OGER granulocyte colony-stimulating factor P09919 Glycosidase digestion, electrophoresis and chromatographic analysis of recombinant human granulocyte colony-stimulating factor glycoforms produced in Chinese hamster ovary cells. 4038307 0 9 gly gamma-seminoprotein 80:98 arg1 the N-glycosidic carbohydrate units gamma-seminoprotein the N-glycosidic carbohydrate units PUBTATOR gamma-seminoprotein 354 Occurrence of the Y determinant on the N-glycosidic carbohydrate units of human gamma-seminoprotein. 4038307 1 12 gly derived 152:158 arg2 gamma-seminoprotein AND the oligosaccharides gamma-seminoprotein the oligosaccharides PUBTATOR gamma-seminoprotein 354 500-MHz H-NMR spectroscopy of the oligosaccharides derived from gamma-seminoprotein, a human seminal plasma glycoprotein, revealed considerable microheterogeneity both with respect to the degree of branching and with regard to the peripheral sugars. 4038307 1 14 gly glycoprotein 209:220 arg1 gamma-seminoprotein gamma-seminoprotein PUBTATOR gamma-seminoprotein 354 500-MHz H-NMR spectroscopy of the oligosaccharides derived from gamma-seminoprotein, a human seminal plasma glycoprotein, revealed considerable microheterogeneity both with respect to the degree of branching and with regard to the peripheral sugars. 6838832 0 17 gly plasminogen 96:106 arg1 the carbohydrate variants plasminogen the carbohydrate variants OGER plasminogen P00747 Amino acid sequence analysis of the asparagine-288 region of the carbohydrate variants of human plasminogen. 3311885 3 40 gly glycosylated 851:862 arg1 recombinant (R) GM-CSF recombinant (R) GM-CSF OGER CSF Despite the fact that both lymphokines contain at least one N-glycosylation site and have identical N-terminal residues (Ala-Pro-Thr), recombinant (R) GM-CSF was found to be heterogeneously glycosylated by yeast while RBoIL-2 was secreted without glycosylation. 11063734 5 13 gly glycosylation 683:695 arg1 proSP-B proSP-B PUBTATOR SP-B 6439 Of the two SP-B polymorphisms genotyped, the Ile131Thr variation affects a putative N-terminal N:-linked glycosylation site of proSP-B and the length variation of intron 4 has previously been suggested to associate with RDS. 11063734 11 59 gly SP-B 1581:1584 arg1 a determinant SP-B a determinant PUBTATOR SP-B 6439 We propose that the SP-B Ile131Thr polymorphism is a determinant for certain SP-A alleles as factors causing genetic susceptibility to RDS (6A(2), 1A(0)) or protection against it (6A(3), 1A(2)). 2209609 1 16 gly glycoprotein 251:262 arg1 sCD4 sCD4 PUBTATOR sCD4 79966 Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing. 2209609 1 16 gly glycoprotein 251:262 arg1 human CD4 glycoprotein human CD4 glycoprotein PUBTATOR CD4 glycoprotein P01730 Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing. 2209609 0 44 gly glycoprotein 117:128 arg1 a recombinant soluble CD4 glycoprotein a recombinant soluble CD4 glycoprotein PUBTATOR CD4 glycoprotein P01730 The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells. 11410585 4 34 gly present 798:804 arg1 bovine peripheral myelin P0 AND the HNK-1 epitope bovine peripheral myelin P0 the HNK-1 epitope Cterm P0 We recently described the structure of the N-glycan carrying the HNK-1 epitope, present on bovine peripheral myelin P0 (Voshol, H., van Zuylen, C. W. E. M., Orberger, G., Vliegenthart, J. F. G., and Schachner, M. (1996) J. Biol. 11410585 3 36 gly cell 625:628 arg1 3-O-SO(3)H-GlcUA(beta1-3)Gal(beta1-4)GlcNAc natural keller cell (HNK)-1 3-O-SO(3)H-GlcUA(beta1-3)Gal(beta1-4)GlcNAc PUBTATOR natural keller cell (HNK)-1 27087 Using monoclonal antibodies, the homophilic binding of the P0 glycoprotein was shown to be mediated via the human natural keller cell (HNK)-1 epitope (3-O-SO(3)H-GlcUA(beta1-3)Gal(beta1-4)GlcNAc) present on the N-glycans. 11410585 3 44 gly HNK 631:633 arg1 3-O-SO(3)H-GlcUA(beta1-3)Gal(beta1-4)GlcNAc natural keller cell (HNK)-1 3-O-SO(3)H-GlcUA(beta1-3)Gal(beta1-4)GlcNAc PUBTATOR natural keller cell (HNK)-1 27087 Using monoclonal antibodies, the homophilic binding of the P0 glycoprotein was shown to be mediated via the human natural keller cell (HNK)-1 epitope (3-O-SO(3)H-GlcUA(beta1-3)Gal(beta1-4)GlcNAc) present on the N-glycans. 11410585 3 63 gly natural 610:616 arg1 3-O-SO(3)H-GlcUA(beta1-3)Gal(beta1-4)GlcNAc natural keller cell (HNK)-1 3-O-SO(3)H-GlcUA(beta1-3)Gal(beta1-4)GlcNAc PUBTATOR natural keller cell (HNK)-1 27087 Using monoclonal antibodies, the homophilic binding of the P0 glycoprotein was shown to be mediated via the human natural keller cell (HNK)-1 epitope (3-O-SO(3)H-GlcUA(beta1-3)Gal(beta1-4)GlcNAc) present on the N-glycans. 11410585 3 83 gly keller 618:623 arg1 3-O-SO(3)H-GlcUA(beta1-3)Gal(beta1-4)GlcNAc natural keller cell (HNK)-1 3-O-SO(3)H-GlcUA(beta1-3)Gal(beta1-4)GlcNAc PUBTATOR natural keller cell (HNK)-1 27087 Using monoclonal antibodies, the homophilic binding of the P0 glycoprotein was shown to be mediated via the human natural keller cell (HNK)-1 epitope (3-O-SO(3)H-GlcUA(beta1-3)Gal(beta1-4)GlcNAc) present on the N-glycans. 1388166 0 23 gly oligosaccharides 22:37 arg1 tissue factor pathway inhibitor tissue factor pathway inhibitor oligosaccharides PUBTATOR tissue factor pathway inhibitor 7035 The asparagine-linked oligosaccharides on tissue factor pathway inhibitor terminate with SO4-4GalNAc beta 1, 4GlcNAc beta 1,2 Mana alpha. 1388166 2 48 gly TFPI 334:337 arg1 the oligosaccharides TFPI the oligosaccharides PUBTATOR TFPI 7035 We have determined that greater than 70% of the oligosaccharides on recombinant TFPI expressed in 293 cells terminate with the sequence SO4-4GalNAc beta 1, 4GlcNAc beta 1, 2Man alpha. 1388166 2 75 gly oligosaccharides 302:317 arg1 recombinant TFPI TFPI oligosaccharides PUBTATOR TFPI 7035 We have determined that greater than 70% of the oligosaccharides on recombinant TFPI expressed in 293 cells terminate with the sequence SO4-4GalNAc beta 1, 4GlcNAc beta 1, 2Man alpha. 1400492 7 85 gly glycosylation 814:826 arg1 cathepsins D cathepsins D OGER cathepsins D P25774 A single glycosylation site occurs in the mLAP sequence at a position corresponding to the first glycosylation site of cathepsins D. 8193553 0 39 gly O-glycans 36:44 arg1 recombinant glycophorin A glycophorin A O-glycans PUBTATOR glycophorin A 2993 Biochemical characterization of the O-glycans on recombinant glycophorin A expressed in Chinese hamster ovary cells. 8193553 4 72 gly A 730:730 arg1 The O-glycans glycophorin A The O-glycans PUBTATOR glycophorin A 2993 The O-glycans of human erythrocyte glycophorin A consist mainly of short oligosaccharides with one, two, or three sialic acid residues linked to a common disaccharide core, Gal beta 1-3GalNAc alpha 1-Ser/Thr, with the disialylated structure being the most abundant. 7688956 0 5 gly glycoprotein 76:87 arg1 Structure Structure PUBTATOR structure of the CAMPATH-1 antigen 1043 Structure of the CAMPATH-1 antigen, a glycosylphosphatidylinositol-anchored glycoprotein which is an exceptionally good target for complement lysis. 8652881 8 59 gly glycosylated 1472:1483 arg1 recombinant FVIII-delta II recombinant FVIII-delta II OGER FVIII P00451 The difference from the theoretical molecular molecular masses and the observation of broad molecular peaks suggest that recombinant FVIII-delta II has been effectively glycosylated by the host cell on both heavy and light chains. 2787353 7 37 gly rIL-2 1288:1292 arg1 the carbohydrate-binding site rIL-2 the carbohydrate-binding site PUBTATOR rIL-2 116562 Thus the carbohydrate-binding site of rIL-2 is distinct from the cell surface receptor-binding site, and might function preferentially in acidic microenvironments. 10648510 2 92 gly glycoprotein 336:347 arg1 RNase B RNase B OGER RNase B P07998 The ability of RNase B, a model glycoprotein with a single N-glycosylation site occupied by a family of high-mannose-type glycans (Man(5)- to Man(9)-GlcNAc(2)), to support growth of E. faecalis was investigated. 2457922 1 41 gly glycoprotein 320:331 arg1 biliary glycoprotein I biliary glycoprotein I PUBTATOR biliary glycoprotein I 634 We have isolated and sequenced four overlapping cDNA clones from a normal adult human colon library, which together gave the entire nucleotide sequence for biliary glycoprotein I (BGP I). 2457922 0 72 gly glycoprotein 43:54 arg1 biliary glycoprotein I biliary glycoprotein I PUBTATOR biliary glycoprotein I: 634 Molecular cloning of a cDNA coding biliary glycoprotein I: primary structure of a glycoprotein immunologically crossreactive with carcinoembryonic antigen. 7499420 3 50 gly N-glycosylation 417:431 arg1 PMP22 PMP22 PUBTATOR PMP22 5376 The positions of the four lipophilic domains and the N-glycosylation site of PMP22 are conserved in CL-20, suggesting that it also is an integral membrane glycoprotein. 9427707 8 45 part_of FVIII 1771:1775 arg1 FVIII residues 558 to 565 FVIII FVIII residues 558 to 565 PUBTATOR SpecificSite FVIII 2157 residues 558 To evaluate interaction of FVIII with factor IXa, we performed an inhibition assay using a synthetic peptide corresponding to FVIII residues 558 to 565, previously shown to be a factor IXa interaction site. 2846759 1 68 gly glycoprotein 157:168 arg1 the glycoprotein H (gH) gene the glycoprotein H (gH) gene PUBTATOR glycoprotein H 1682472 We present the nucleotide sequence of the glycoprotein H (gH) gene of herpesvirus saimiri (HVS), a representative of the T lymphotropic herpesviruses of New World monkeys, and compare the predicted amino acid sequence with sequences of homologous proteins from four human herpesviruses. 2846759 0 120 gly glycoprotein 16:27 arg1 glycoprotein H glycoprotein H PUBTATOR glycoprotein H 1682472 Conservation of glycoprotein H (gH) in herpesviruses: nucleotide sequence of the gH gene from herpesvirus saimiri. 21528263 1 0 gly P-glycoprotein 145:158 arg1 P-glycoprotein P-glycoprotein PUBTATOR P-glycoprotein 5243 Increased expression of P-glycoprotein, encoded by the MDR1 gene, is considered to be responsible for chemotherapy failure in a number of human cancers. 21528263 6 13 gly N-glycosylation 1048:1062 arg1 the P-glycoprotein the P-glycoprotein PUBTATOR P-glycoprotein 5243 An A to G nucleotide substitution giving rise to an amino acid substitution (Asn-->Asp) in codon 21 at the first potential N-glycosylation site of the P-glycoprotein was seen in primary tumors from four patients and in an axillar lymph node metastases from one of these patients. 21528263 6 20 gly P-glycoprotein 1076:1089 arg1 the P-glycoprotein the P-glycoprotein PUBTATOR P-glycoprotein 5243 An A to G nucleotide substitution giving rise to an amino acid substitution (Asn-->Asp) in codon 21 at the first potential N-glycosylation site of the P-glycoprotein was seen in primary tumors from four patients and in an axillar lymph node metastases from one of these patients. 1402395 6 37 gly glycoprotein 740:751 arg1 Prosaposin Prosaposin PUBTATOR Prosaposin 5660 Prosaposin is a 70 kDa glycoprotein containing four domains, one for each saposin, placed in tandem. 9520292 4 31 gly deglycosylated 679:692 arg1 the cathepsin D the cathepsin D PUBTATOR cathepsin D, 1509 No significant difference was detected in the immunoreactivity of patient serum with the glycosylated and deglycosylated forms of the cathepsin D, suggesting that patient humoral responses are directed primarily against the core protein. 9520292 4 55 gly glycosylated 662:673 arg1 the cathepsin D the cathepsin D PUBTATOR cathepsin D, 1509 No significant difference was detected in the immunoreactivity of patient serum with the glycosylated and deglycosylated forms of the cathepsin D, suggesting that patient humoral responses are directed primarily against the core protein. 9194614 11 61 gly hyperglycosylated 1680:1696 arg1 This rPhl p 1 This rPhl p 1 PUBTATOR rPhl p 1 1423 This rPhl p 1 is hyperglycosylated compared to the nPhl p 1, which only has a 5% carbohydrate content. 7524670 0 34 gly gonadotropin 69:80 arg1 N-linked oligosaccharides chorionic gonadotropin N-linked oligosaccharides OGER chorionic gonadotropin Structural analysis of N-linked oligosaccharides of equine chorionic gonadotropin and lutropin beta-subunits. 7524670 0 102 gly beta-subunits 95:107 arg1 N-linked oligosaccharides lutropin beta N-linked oligosaccharides OGER lutropin beta Structural analysis of N-linked oligosaccharides of equine chorionic gonadotropin and lutropin beta-subunits. 8189524 2 1 gly glycoprotein 422:433 arg1 HSV-1 glycoprotein H HSV-1 glycoprotein H Cterm HSV-1 glycoprotein H (gH In the alphaherpesvirus pseudorabies virus (PrV), seven glycoproteins that all constitute homologs of glycoproteins found in herpes simplex virus type 1 (HSV-1) have been characterized, including a homolog of HSV-1 glycoprotein H (gH). 8631761 7 34 gly fucosylated 1291:1301 arg1 the identically fucosylated and structurally related tissue plasminogen activator the identically fucosylated and structurally related tissue plasminogen activator OGER tissue plasminogen activator P00750 On the basis of these results, DSPAalpha1 is a suitable model for studying the influence of O-fucosylation on clearance rates, particularly in comparative studies with the identically fucosylated and structurally related tissue plasminogen activator. 8626811 1 46 gly glycoprotein 130:141 arg1 gp43 gp43 Cterm gp43 The 43,000-Da glycoprotein (gp43) of Paracoccidioides brasiliensis is an immunodominant antigen for antibody-dependent and immune cellular responses in patients with paracoccidioidomycosis. 8772226 1 13 gly glycoprotein 180:191 arg1 HRG HRG PUBTATOR HRG 3273 Two forms of histidine-rich glycoprotein (HRG) were detected on SDS-PAGE by silver staining and immunoblotting after isolation of the protein from pooled plasma using immuno-affinity chromatography followed by chromatography with heparin-Sepharose. 7479385 7 12 gly PSA 1222:1224 arg1 The experimentally determined carbohydrate content PSA The experimentally determined carbohydrate content PUBTATOR PSA 354 The experimentally determined carbohydrate content of PSA confirms that only one N-glycosylation site is occupied in the protein. 7479385 0 27 gly antigen 63:69 arg1 carbohydrate structure prostate specific antigen carbohydrate structure PUBTATOR prostate specific antigen 354 Molecular mass and carbohydrate structure of prostate specific antigen: studies for establishment of an international PSA standard. 8442916 3 88 gly glycoprotein 531:542 arg1 gp120 gp120 PUBTATOR gp120 3700 The molecular analysis of the env region encompassed all variable domains of the external glycoprotein, gp120. 3594570 1 27 gly glycoproteins 261:273 arg1 Mac-1 Mac-1 PUBTATOR Mac-1 3689 Leukocyte adhesion deficiency (LAD) is a heritable disease involving deficient expression of three related leukocyte adhesion glycoproteins: LFA-1, Mac-1, and p150,95. 3594570 1 27 gly glycoproteins 261:273 arg1 p150,95 p150,95 PUBTATOR p150 10036 Leukocyte adhesion deficiency (LAD) is a heritable disease involving deficient expression of three related leukocyte adhesion glycoproteins: LFA-1, Mac-1, and p150,95. 3594570 1 27 gly glycoproteins 261:273 arg1 LFA-1 LFA-1 PUBTATOR LFA-1 3683 Leukocyte adhesion deficiency (LAD) is a heritable disease involving deficient expression of three related leukocyte adhesion glycoproteins: LFA-1, Mac-1, and p150,95. 31958346 2 38 gly N-glycosylation 381:395 arg1 the major subunits the major subunits OGER subunits 14799 In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain. 31958346 2 38 gly N-glycosylation 381:395 arg1 mouse GluA1 mouse GluA1 PUBTATOR GluA1 14799 In this study, we performed a comprehensive N-glycosylation analysis of mouse GluA1, one of the major subunits of α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate type glutamate receptor, which possesses six potential N-glycosylation sites in the N-terminal domain. 31958346 11 42 part_of GluA1 1782:1786 arg1 the N401-glycosite GluA1 the N401-glycosite PUBTATOR SpecificSite GluA1 2890 N401 Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain. 31958346 11 71 gly N401-glycosite 1764:1777 arg1 GluA1 GluA1 PUBTATOR GluA1 2890 Taken together, we propose that the N401-glycosite of GluA1 receives a unique control of modification, and we also propose a novel N-glycosylation occupancy regulatory mechanism by Bip that might be associated with α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors function in the brain. 31004621 9 25 part_of RSV 1680:1682 arg1 position N116 RSV F N116Q position N116 Cterm SpecificSite RSV F N116Q position N116 Infection with recombinant virus lacking the N-glycosylation site at position N116 (RSV F N116Q) resulted in significant higher neutralizing antibody titers compared to RSV F WT infection, which is surprising since this N-glycan is present in the p27 peptide which is assumed to be absent from the mature F protein in virions. 31004621 3 100 part_of F1 726:727 arg1 N500 F1 N500 Cterm SpecificSite F1 N500 The RSV F sequence possesses five N-glycosylation sites located in the F2 subunit (N27 and N70), the p27 peptide (N116 and N126) and the F1 subunit (N500). 31004621 9 108 part_of F 1684:1684 arg1 position N116 RSV F N116Q position N116 Cterm SpecificSite RSV F N116Q position N116 Infection with recombinant virus lacking the N-glycosylation site at position N116 (RSV F N116Q) resulted in significant higher neutralizing antibody titers compared to RSV F WT infection, which is surprising since this N-glycan is present in the p27 peptide which is assumed to be absent from the mature F protein in virions. 11588155 5 12 gly apoB100 982:988 arg1 The N-glycan composition apoB100 The N-glycan composition PUBTATOR apoB100 338 The N-glycan composition of apoB100 derived from five LDL subpopulations (LDL1, d = 1.018-1.023; LDL2, d = 1.023-1.030; LDL3, d = 1.030-1.040; LDL4, d = 1.040-1.051; LDL5, d = 1.051-1.065 g/ml) did not vary in normolipidemic or hypercholesterolemic subjects. 11588155 1 79 gly B100 279:282 arg1 The carbohydrate composition apolipoprotein (apo) B100 The carbohydrate composition PUBTATOR apolipoprotein (apo) B100 338 The carbohydrate composition of apolipoprotein (apo) B100, particularly its degree of sialylation, may contribute to the atherogenic properties of low-density lipoprotein (LDL). 31572782 4 37 gly receptor 498:505 arg1 the glycan pattern IgE high-affinity receptor (FcεRIα) the glycan pattern PUBTATOR IgE high-affinity receptor (FcεRIα) 2205 The employed methodology allowed dissecting the glycan pattern of the IgE high-affinity receptor (FcεRIα) expressed in human HEK 293 cells, identifying the presence and relative abundance of specific glycan epitopes. 31325506 7 38 gly glycopeptides 1520:1532 arg1 BSM BSM Cterm BSM 281333 The N-glycosylation sites were identified from the analysis of glycopeptides from BSM. 31325506 0 47 gly mucin 33:37 arg1 N-glycans mucin N-glycans PUBTATOR mucin 281333 N-glycans of bovine submaxillary mucin contain core-fucosylated and sulfated glycans but not sialylated glycans. 31325506 1 60 gly heavily-glycosylated 150:169 arg1 Bovine submaxillary mucin Bovine submaxillary mucin PUBTATOR mucin 281333 Bovine submaxillary mucin (BSM) is a heavily-glycosylated macromolecular (approximately 4 MDa) protein and is used in various biomaterial applications in light of its high viscosity and biocompatibility, in addition to use as a biochemical substrate or inhibitor as a result of its abundant O-glycans. 31356638 4 12 gly glycosylated 622:633 arg1 N207Q N207Q Cterm N207Q Q9Y6Y0 Here we report that mutation of a single glycosylated residue of NS1 (N207Q) abolishes the ability of NS1 to trigger EGL disruption and induce endothelial hyperpermeability. 31356638 4 12 gly glycosylated 622:633 arg1 NS1 NS1 OGER NS1 Q9Y6Y0 Here we report that mutation of a single glycosylated residue of NS1 (N207Q) abolishes the ability of NS1 to trigger EGL disruption and induce endothelial hyperpermeability. 31356638 3 44 gly NS1 489:491 arg1 the molecular determinants NS1 the molecular determinants OGER NS1 Q9Y6Y0 However, the molecular determinants of NS1 required to trigger EGL disruption and the cellular pathway(s) involved remain unknown. 31113887 9 1 gly glycoprotein 1606:1617 arg1 Env Env PUBTATOR Env 105221759 Differentially glycosylated CD4 receptors were biochemically purified and used in neutralization assays and microscale thermophoresis to show that the glycans on chimpanzee CD4 reduce binding affinity with the lentiviral surface glycoprotein, Env. 31113887 9 24 gly glycosylated 1392:1403 arg1 Differentially glycosylated CD4 receptors Differentially glycosylated CD4 receptors PUBTATOR CD4 receptors 450124 Differentially glycosylated CD4 receptors were biochemically purified and used in neutralization assays and microscale thermophoresis to show that the glycans on chimpanzee CD4 reduce binding affinity with the lentiviral surface glycoprotein, Env. 31113887 9 31 gly glycans 1528:1534 arg1 chimpanzee CD4 CD4 glycans PUBTATOR CD4 450124 Differentially glycosylated CD4 receptors were biochemically purified and used in neutralization assays and microscale thermophoresis to show that the glycans on chimpanzee CD4 reduce binding affinity with the lentiviral surface glycoprotein, Env. 31113887 7 78 gly glycosylated 1040:1051 arg1 chimpanzee CD4 chimpanzee CD4 PUBTATOR CD4 450124 Doubly glycosylated forms of chimpanzee CD4 reduce HIV-1 and SIVcpz infection by as much as two orders of magnitude. 31302509 7 25 gly glycosylated 1033:1044 arg1 XPR1 receptors XPR1 receptors PUBTATOR XPR1 receptors 9213 While this substitution introduces an N-linked glycosylation site, XPR1 receptors are not glycosylated indicating that this replacement alters the virus-receptor interface independently of glycosylation. 32054416 7 27 gly glycosylation 1088:1100 arg1 CTLA-4 CTLA-4 PUBTATOR CTLA-4 12477 This finding may also contribute to the understanding of the glycosylation of CTLA-4 and its related biologic function. 30427586 3 53 gly glycoproteins 509:521 arg1 IgG IgG Cterm IgG Using a set of four representative and biopharmaceutically relevant glycoproteins (IgG, fibrinogen, lactotransferrin, and ribonuclease B), the benefits and limitations of the developed workflow are highlighted and a state-of-the-art blueprint for conducting high-quality in-depth N- and O-glycoproteomic analyses is provided. 30427586 3 53 gly glycoproteins 509:521 arg1 lactotransferrin lactotransferrin OGER lactotransferrin P02788 Using a set of four representative and biopharmaceutically relevant glycoproteins (IgG, fibrinogen, lactotransferrin, and ribonuclease B), the benefits and limitations of the developed workflow are highlighted and a state-of-the-art blueprint for conducting high-quality in-depth N- and O-glycoproteomic analyses is provided. 32168410 3 21 gly linked 375:380 arg2 FXIII-B AND the glycan structures FXIII-B the glycan structures PUBTATOR FXIII-B 2165 OBJECTIVE: To reveal the glycan structures linked to FXIII-B, to design a method for deglycosylating the native protein, to find out if deglycosylation influences the dimeric structure of FXIII-B and its clearance from the circulation. 32168410 7 33 gly deglycosylated 895:908 arg1 deglycosylated FXIII-B deglycosylated FXIII-B PUBTATOR FXIII-B 2165 The structure of deglycosylated FXIII-B was investigated by gel filtration. 32168410 11 82 gly FXIII-B 1271:1277 arg1 The total N-glycan profile FXIII-B The total N-glycan profile PUBTATOR FXIII-B 2165 The total N-glycan profile of FXIII-B featured nine individual structures; three were fucosylated and each structure contained at least one sialic acid. 32168410 13 88 gly attached 1596:1603 arg1 FXIII-B AND the glycan moieties FXIII-B the glycan moieties PUBTATOR FXIII-B 2165 CONCLUSION: Characterization of the glycan moieties attached to FXIII-B is reported for the first time. 32168410 8 97 gly deglycosylated 971:984 arg1 deglycosylated and native FXIII-B deglycosylated and native FXIII-B PUBTATOR FXIII-B 2165 The clearance of deglycosylated and native FXIII-B from plasma was compared in FXIII-B knock out mice. 31296534 7 6 gly hyperglycosylated 1058:1074 arg1 GRP94 GRP94 PUBTATOR GRP94 7184 GRP94 was also hyperglycosylated in wild-type cells treated with ER stress inducers including thapsigargin, dithiothreitol, and NGI-1. 31296534 6 63 gly hyperglycosylated 916:932 arg1 the lumenal ER chaperone GRP94 the lumenal ER chaperone GRP94 PUBTATOR GRP94 7184 Remarkably, the lumenal ER chaperone GRP94 was hyperglycosylated in STT3A-deficient cells, bearing glycans on five silent sites in addition to the normal glycosylation site. 30904681 2 5 gly Glycosylation 295:307 arg1 B2GP1 B2GP1 PUBTATOR B2GP1 350 Glycosylation of B2GP1 can impact auto antibody recognition leading to the development of antiphospholipid syndrome (APS), which can result in miscarriages or thrombosis. 30904681 0 11 gly glycosylation 66:78 arg1 B2GP1 B2GP1 PUBTATOR B2GP1 350 Simultaneous characterization of SNPs and N-glycans from multiple glycosylation sites of intact β-2-glycoprotein-1 (B2GP1) by ESI-qTOF-MS. 30904681 0 11 gly glycosylation 66:78 arg1 intact β-2-glycoprotein-1 intact β-2-glycoprotein-1 PUBTATOR -2-glycoprotein-1 350 Simultaneous characterization of SNPs and N-glycans from multiple glycosylation sites of intact β-2-glycoprotein-1 (B2GP1) by ESI-qTOF-MS. 30904681 9 12 gly B2GP1 1411:1415 arg1 glycan compositions B2GP1 glycan compositions PUBTATOR B2GP1 350 Our method allows a fast determination of genetic variants and glycan compositions of human B2GP1 to be potentially used as diagnostic marker. 30904681 1 52 gly glycosylated 150:161 arg1 B2GP1 B2GP1 PUBTATOR B2GP1 350 The highly glycosylated ß-2-glycoprotein-1 (B2GP1), also called apolipoprotein H, is a 50 kDa human plasma protein with four or five N-glycosylation sites. 30904681 1 52 gly glycosylated 150:161 arg1 also called apolipoprotein H also called apolipoprotein H PUBTATOR apolipoprotein H 350 The highly glycosylated ß-2-glycoprotein-1 (B2GP1), also called apolipoprotein H, is a 50 kDa human plasma protein with four or five N-glycosylation sites. 10441114 0 43 gly glycosylated 6:17 arg1 human plasma endostatin human plasma endostatin PUBTATOR endostatin 80781 Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV. 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. 21573946 3 3 gly EC-SOD 483:488 arg1 a precise N-glycan profile EC-SOD a precise N-glycan profile PUBTATOR EC-SOD 20657 Thus, a precise N-glycan profile of the recombinant EC-SOD is not available. 21573946 1 14 gly N-glycosylated 229:242 arg1 EC-SOD EC-SOD PUBTATOR EC-SOD 20657 Extracellular superoxide dismutase (EC-SOD), the major SOD isoenzyme in biological fluids, is known to be N-glycosylated and heterogeneous as was detected in most glycoproteins. 21573946 1 14 gly N-glycosylated 229:242 arg1 Extracellular superoxide dismutase Extracellular superoxide dismutase PUBTATOR Extracellular superoxide dismutase 20657 Extracellular superoxide dismutase (EC-SOD), the major SOD isoenzyme in biological fluids, is known to be N-glycosylated and heterogeneous as was detected in most glycoproteins. 21573946 1 14 gly N-glycosylated 229:242 arg1 the major SOD isoenzyme the major SOD isoenzyme PUBTATOR SOD isoenzyme 6649 Extracellular superoxide dismutase (EC-SOD), the major SOD isoenzyme in biological fluids, is known to be N-glycosylated and heterogeneous as was detected in most glycoproteins. 32258897 0 48 gly Heterogeneity 14:26 arg1 rhIFN-β rhIFN-β Cterm rhIFN-β 3456 Glycosylation Heterogeneity of Hyperglycosylated Recombinant Human Interferon-β (rhIFN-β). 32258897 0 48 gly Heterogeneity 14:26 arg1 Hyperglycosylated Recombinant Human Interferon-β Hyperglycosylated Recombinant Human Interferon-β PUBTATOR Human Interferon-β 3456 Glycosylation Heterogeneity of Hyperglycosylated Recombinant Human Interferon-β (rhIFN-β). 32258897 0 57 gly Hyperglycosylated 31:47 arg1 rhIFN-β rhIFN-β Cterm rhIFN-β 3456 Glycosylation Heterogeneity of Hyperglycosylated Recombinant Human Interferon-β (rhIFN-β). 32258897 0 57 gly Hyperglycosylated 31:47 arg1 Hyperglycosylated Recombinant Human Interferon-β Hyperglycosylated Recombinant Human Interferon-β PUBTATOR Human Interferon-β 3456 Glycosylation Heterogeneity of Hyperglycosylated Recombinant Human Interferon-β (rhIFN-β). 30935958 9 33 gly N-glycosylated 1111:1124 arg1 In vivo PrP In vivo PrP PUBTATOR PrP Q9NP58 In vivo PrP is N-glycosylated at positions Asn181 and Asn197. 15750791 3 4 gly glycosylated 422:433 arg1 Edg-1/S1P1 Edg-1/S1P1 PUBTATOR S1P1 1901 Our recent novel studies established that Edg-1/S1P1 is glycosylated in its N-terminal extracellular portion and further identified the specific glycosylation site as asparagine 30. 15750791 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. 31244828 1 64 gly glycoprotein 172:183 arg1 MOG MOG PUBTATOR MOG 4340 Autoantibodies to myelin oligodendrocytes glycoprotein (MOG) are found in a fraction of patients with inflammatory demyelination and are detected with MOG-transfected cells. 31244828 12 66 gly glycoforms 1843:1852 arg1 MOG MOG PUBTATOR MOG 4340 The most abundant glycoforms of MOG expressed in HEK cells are diantennary, contain a core fucose, an antennary fucose, and are decorated with α2,6 linked Neu5Ac, while details of the glycoforms of MOG in myelin remain to be identified. 31244828 12 75 gly glycoforms 1677:1686 arg1 MOG MOG PUBTATOR MOG 4340 The most abundant glycoforms of MOG expressed in HEK cells are diantennary, contain a core fucose, an antennary fucose, and are decorated with α2,6 linked Neu5Ac, while details of the glycoforms of MOG in myelin remain to be identified. 32109505 6 11 gly glycosylation 765:777 arg1 TRPM8 TRPM8 PUBTATOR TRPM8 79054 The glycosylation state of TRPM8 in cells untreated and treated with a deglycosylating agent was addressed with Terahertz (THz) spectroscopy. 32109505 4 62 gly N-glycosylation 463:477 arg1 TRPM8 channel TRPM8 channel PUBTATOR TRPM8 channel 79054 This work focuses on the N-glycosylation of TRPM8 channel that was previously studied by our group in relation to proliferation and migration of tumoral cells. 32109505 3 75 gly N-glycosylated 390:403 arg1 TRPM8 TRPM8 PUBTATOR TRPM8 79054 TRPM8 is N-glycosylated, with a single site per subunit. 32109505 0 81 gly N-glycosylation 0:14 arg1 TRPM8 protein TRPM8 protein PUBTATOR TRPM8 protein 79054 N-glycosylation state of TRPM8 protein revealed by terahertz spectroscopy and molecular modelling. 31507595 8 85 gly glycoforms 1353:1362 arg1 CD52-Fc CD52-Fc PUBTATOR CD52 P31358 When glycoforms of CD52-Fc were fractionated by anion exchange MonoQ-GL chromatography, bioactive fractions displayed mainly tetra-antennary, α-2,3 sialylated N-glycan structures and a lower relative abundance of bisecting GlcNAc structures compared to non-bioactive fractions. 31393126 9 94 gly attached 1435:1442 arg2 MRJP2 AND 18, 17, and 2 N-glycans MRJP2 18, 17, and 2 N-glycans PUBTATOR MRJP2 406091 There were 18, 17, and 2 N-glycans attached to MRJP1, MRJP2, and MRJP3, respectively. 31393126 9 94 gly attached 1435:1442 arg2 MRJP3 AND 18, 17, and 2 N-glycans MRJP3 18, 17, and 2 N-glycans PUBTATOR MRJP3 406121 There were 18, 17, and 2 N-glycans attached to MRJP1, MRJP2, and MRJP3, respectively. 31393126 9 94 gly attached 1435:1442 arg1 MRJP1 AND 18, 17, and 2 N-glycans MRJP1 18, 17, and 2 N-glycans PUBTATOR MRJP1 406090 There were 18, 17, and 2 N-glycans attached to MRJP1, MRJP2, and MRJP3, respectively. 32110292 7 35 gly N-glycosylation 1393:1407 arg1 IgG IgG Cterm IgG Combined with high-energy collisional dissociation for the fragmentation of glycans, fine mapping of the N-glycosylation profile of IgG is achieved. 32110292 3 87 gly N-Glycosylation 433:447 arg1 IgG IgG Cterm IgG N-Glycosylation of IgG is crucial for its effector function and makes IgG highly heterogeneous both in structure and function, although all four subclasses of IgG contain only a single N-glycosylation site in the Fc region with a highly similar amino acid sequence. 31412214 7 21 gly glycosylation 1337:1349 arg1 non-GPI-anchored cytosolic CD59 non-GPI-anchored cytosolic CD59 PUBTATOR CD59 966 Our results suggest that CD59 is retrotranslocated from the endoplasmic reticulum to the cytosol, a process mediated by recognition of trimmed N-linked oligosaccharides, supported by the partial glycosylation of non-GPI-anchored cytosolic CD59 as well as the failure of N-linked glycosylation site mutant CD59 to reach the cytosol or rescue GSIS. 31065929 0 38 gly Glycosylation 0:12 arg1 dentin matrix protein 1 dentin matrix protein 1 PUBTATOR dentin matrix protein 1 13406 Glycosylation of dentin matrix protein 1 is critical for fracture healing via promoting chondrogenesis. 32331833 0 37 gly Glycosylation 0:12 arg1 DMP1 DMP1 PUBTATOR DMP1 13406 Glycosylation of DMP1 promotes bone reconstruction in long bone defects. 31186110 0 43 gly glycosylated 6:17 arg1 Novel glycosylated human interferon alpha 2b Novel glycosylated human interferon alpha 2b PUBTATOR interferon alpha 2b 3440 Novel glycosylated human interferon alpha 2b expressed in glycoengineered Pichia pastoris and its biological activity: N-linked glycoengineering approach. 32280962 0 33 gly glycoprotein 46:57 arg1 Glycan characterization pregnancy-specific glycoprotein 1 Glycan characterization OGER pregnancy-specific glycoprotein 1 P11464 Glycan characterization of pregnancy-specific glycoprotein 1 and its identification as a novel Galectin-1 ligand. 32280962 1 35 gly glycoprotein 140:151 arg1 Pregnancy-specific beta 1 glycoprotein Pregnancy-specific beta 1 glycoprotein PUBTATOR Pregnancy-specific beta 1 glycoprotein 653492 Pregnancy-specific beta 1 glycoprotein (PSG1) is secreted from trophoblast cells of the human placenta in increasing concentrations as pregnancy progresses, becoming one of the most abundant proteins in maternal serum in the third trimester. 32280962 1 35 gly glycoprotein 140:151 arg1 PSG1 PSG1 PUBTATOR PSG1 5669 Pregnancy-specific beta 1 glycoprotein (PSG1) is secreted from trophoblast cells of the human placenta in increasing concentrations as pregnancy progresses, becoming one of the most abundant proteins in maternal serum in the third trimester. 32280962 0 42 gly glycoprotein 46:57 arg1 pregnancy-specific glycoprotein 1 pregnancy-specific glycoprotein 1 OGER pregnancy-specific glycoprotein 1 P11464 Glycan characterization of pregnancy-specific glycoprotein 1 and its identification as a novel Galectin-1 ligand. 32280962 3 50 gly PSG1 528:531 arg1 the glycan composition PSG1 the glycan composition PUBTATOR PSG1 5669 We carried out glycomic and glycoproteomic studies to characterize the glycan composition of PSG1 purified from serum of pregnant women and identified the presence of complex N-glycans containing poly LacNAc epitopes with α2,3 sialyation at four sites. 32273875 2 42 gly carbohydrates 251:263 arg1 factor VIII factor VIII carbohydrates PUBTATOR factor VIII 14069 Oligomannose carbohydrates at N239 and/or N2118 on factor VIII allow its binding to the macrophage mannose receptor expressed on human dendritic cells, thereby leading to factor VIII endocytosis and presentation to CD4+ T lymphocytes. 31888963 3 44 part_of CD16a 542:546 arg1 N162 CD16a N162 PUBTATOR SpecificSite CD16a 2214 N162 Furthermore, post-translational modification impacts antibody binding affinity, most notably the composition of the asparagine(N)-linked glycan at N162 of CD16a. 31888963 9 77 part_of CD16a 1313:1317 arg1 N38 CD16a N38 PUBTATOR SpecificSite CD16a 2214 N38 and N74 N38 and N74 of CD16a both contain highly processed complex-type N-glycans with N-acetyllactosamine repeats and complex-type biantennary N-glycans dominate at N169. 31611356 1 45 gly sites 277:281 arg1 HIV-1 gp120 HIV-1 gp120 sites PUBTATOR HIV-1 gp120 155971 Griffithsin (Grft) is an antiviral lectin that has been shown to potently inhibit HIV-1 by binding high-mannose N-linked glycosylation sites on HIV-1 gp120. 31611356 2 74 part_of gp120 357:361 arg1 N295 gp120 N295 PUBTATOR SpecificSite gp120 3700 N295 A key factor for Grft potency is glycosylation at N295 of gp120, which is directly adjacent to N332, a target glycan for an entire class of broadly neutralizing antibodies (bNAbs). 31516400 1 30 gly glycoprotein 147:158 arg1 Background Background Cterm Background: N-linked Background: N-linked glycoprotein is a highly interesting class of proteins for clinical and biological research. 32005658 6 15 gly modified 1356:1363 arg3 HEK-sKlotho AND an unusual N-glycan structure HEK-sKlotho an unusual N-glycan structure OGER HEK P29319 MS and glycopeptide-mapping analyses revealed that HEK-sKlotho is uniquely modified with an unusual N-glycan structure consisting of N,N'-di-N-acetyllactose diamine at multiple N-linked sites, one of which at Asn-126 was adjacent to a putative GalNAc transfer motif. 32005658 5 71 gly sialylated 1154:1163 arg1 heavily sialylated CHO-sKlotho heavily sialylated CHO-sKlotho Cterm CHO-sKlotho Q9UEF7 Chinese hamster ovary (CHO)- and human embryonic kidney (HEK)-derived WT sKlotho proteins had varied activities in FGF23 co-receptor and β-glucuronidase assays in vitro and distinct properties in vivo Sialidase treatment of heavily sialylated CHO-sKlotho increased its co-receptor activity 3-fold, yet it remained less active than hyposialylated HEK-sKlotho. 32005658 5 89 gly hyposialylated 1253:1266 arg1 hyposialylated HEK-sKlotho hyposialylated HEK-sKlotho OGER HEK P29319 Chinese hamster ovary (CHO)- and human embryonic kidney (HEK)-derived WT sKlotho proteins had varied activities in FGF23 co-receptor and β-glucuronidase assays in vitro and distinct properties in vivo Sialidase treatment of heavily sialylated CHO-sKlotho increased its co-receptor activity 3-fold, yet it remained less active than hyposialylated HEK-sKlotho. 31625659 0 9 gly Dectin-1 62:69 arg1 The Core Fucose Dectin-1 The Core Fucose PUBTATOR Dectin-1 Q9BXN2 The Core Fucose on an IgG Antibody is an Endogenous Ligand of Dectin-1. 30898876 5 6 gly presence 1178:1185 arg1 protein 1 low-density lipoprotein receptor-related protein 1 presence PUBTATOR low-density lipoprotein receptor-related protein 1 4035 Our results further revealed that LDN presence on low-density lipoprotein receptor-related protein 1 and nicastrin depends on B3GALNT2, indicating the occurrence of type-I LDN in vivo in mammalian cells. 30898876 5 6 gly presence 1178:1185 arg1 nicastrin nicastrin presence OGER nicastrin Q92542 Our results further revealed that LDN presence on low-density lipoprotein receptor-related protein 1 and nicastrin depends on B3GALNT2, indicating the occurrence of type-I LDN in vivo in mammalian cells. 31097672 1 48 gly α-2-HS-glycoprotein 153:171 arg1 gene name: AHSG gene name: AHSG OGER AHSG P02765 Fetuin, also known as α-2-HS-glycoprotein (gene name: AHSG), is one of the more abundant glycoproteins secreted into the bloodstream. 32197300 6 2 gly glycoproteins 982:994 arg1 viral Env glycoproteins viral Env glycoproteins PUBTATOR Env glycoproteins 155971 Third, the N126K mutation did not interfere with the expression and processing of viral Env glycoproteins, but it disrupted the Asn126-based glycosylation site in gp41. 32197300 1 38 gly HIV-1 187:191 arg1 the C-terminal heptad repeat (CHR) region HIV-1 gp41 the C-terminal heptad repeat (CHR) region Cterm HIV-1 gp41 Peptides derived from the C-terminal heptad repeat (CHR) region of HIV-1 gp41 is potent viral membrane fusion inhibitors, such as the first clinically approved peptide drug T20 and a group of newly-designed peptides. 30257863 5 54 gly glycosylation 777:789 arg1 Kir7.1 Kir7.1 PUBTATOR Kir7.1 3769 Using Western blotting analysis, we observed that multiple GPCRs tested caused a striking reduction in the complex glycosylation of Kir7.1. 30257863 0 59 gly glycosylation 52:64 arg1 the inwardly rectifying potassium channel Kir7.1 the inwardly rectifying potassium channel Kir7.1 PUBTATOR Kir7.1 3769 G protein-coupled receptors differentially regulate glycosylation and activity of the inwardly rectifying potassium channel Kir7.1. 30659065 11 16 part_of IgM 1842:1844 arg1 N209 IgM N209 OGER SpecificSite IgM P01871 sites N46, N209, and N272 IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms. 30659065 11 16 part_of IgM 1842:1844 arg1 N272 IgM N272 OGER SpecificSite IgM P01871 sites N46, N209, and N272 IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms. 30659065 11 16 part_of IgM 1842:1844 arg1 N46 IgM N46 OGER SpecificSite IgM P01871 sites N46, N209, and N272 IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms. 30659065 11 16 part_of IgM 1842:1844 arg1 IgM sites IgM IgM sites OGER SpecificSite IgM P01871 sites N46, N209, and N272 IgM sites N46, N209, and N272 displayed mostly complex glycans, whereas sites N279 and N439 displayed higher relative abundances of high-mannose glycoforms. 31572358 7 133 gly N-glycosylated 1265:1278 arg1 ACPA-IgG ACPA-IgG PUBTATOR Remarkably, ACPA 5657 Remarkably, ACPA-IgG are heavily N-glycosylated in the variable domain due to somatic mutations that generate abundant N-glycosylation consensus sequences. 31461788 0 80 gly Glycosylation 0:12 arg1 DMP1 DMP1 PUBTATOR DMP1 13406 Glycosylation of DMP1 maintains cranial sutures in mice. 31202607 7 0 part_of N565 1484:1487 arg1 GluN3A GluN3A N565 PUBTATOR SpecificSite GluN3A 116443 N565 We also found that AAL has the most profound effect on GluN1/GluN3 receptors, and this effect is mediated partly by a single N-glycosylation site on the GluN3 subunit (specifically, N565 on GluN3A and N465 on GluN3B). 31202607 7 0 part_of N565 1484:1487 arg1 GluN3B GluN3B N565 PUBTATOR SpecificSite GluN3B 116444 N565 We also found that AAL has the most profound effect on GluN1/GluN3 receptors, and this effect is mediated partly by a single N-glycosylation site on the GluN3 subunit (specifically, N565 on GluN3A and N465 on GluN3B). 32321762 8 19 gly PrPC 1645:1648 arg1 the GPI-glycan structure PrPC the GPI-glycan structure PUBTATOR PrPC 5621 In summary, we report the GPI-glycan structure of human PrPC, including the ω-site amino acid for GPI attachment and the sialic acid linkage type. 32321762 6 62 part_of PrPC 1188:1191 arg1 Ser-231 PrPC Ser-231 PUBTATOR SpecificSite PrPC 5621 Ser-231 Gly-229 in human PrPC does not correspond to Ser-231, the previously reported ω site of Syrian hamster PrPC We found that approximately 41% and 28% of GPI anchors in human PrPCs from human and mouse knock-in brains, respectively, have N-acetylneuraminic acid in the side-chain. 32321762 6 70 part_of Gly-229 1085:1091 arg1 human PrPC PrPC Gly-229 PUBTATOR SpecificSite PrPC 5621 Gly-229 Gly-229 in human PrPC does not correspond to Ser-231, the previously reported ω site of Syrian hamster PrPC We found that approximately 41% and 28% of GPI anchors in human PrPCs from human and mouse knock-in brains, respectively, have N-acetylneuraminic acid in the side-chain. 32321762 4 97 gly PrPC isolated 744:756 arg1 GPI-glycan structures PrPC GPI-glycan structures PUBTATOR PrPC 5621 Here, we report GPI-glycan structures of human PrPC isolated from human brain and from brains of a knock-in mouse model in which the mouse prion protein (Prnp) gene was replaced with the human PRNP gene. 31501225 7 68 gly glycopeptides 1163:1175 arg1 IgA2 IgA2 OGER IgA2 P01877 In contrast, the two glycopeptides of IgA2 fell back down in HBV-related HCC patients. 31501225 6 80 gly glycopeptides 974:986 arg1 IgA2 IgA2 OGER IgA2 P01877 TPLTAN 205ITK (H5N5S1F1) and (H5N4S2F1) corresponding to the glycopeptides of IgA2 were significantly elevated in serum from patients with HBV infection and even higher in HBV-related LC patients, as compared with healthy donor. 31511323 11 14 gly glycosylation 1654:1666 arg1 NaV1.5 NaV1.5 PUBTATOR NaV1.5 Q8NEY1 In conclusion, our results indicate that N-linked glycosylation of β2 is required for surface localization of NaV1.5, a property that is often defective in inherited cardiac arrhythmias. 31511323 0 80 gly N-Glycosylation 0:14 arg1 the voltage-gated sodium channel β2 subunit the voltage-gated sodium channel β2 subunit OGER subunit Q99250 N-Glycosylation of the voltage-gated sodium channel β2 subunit is required for efficient trafficking of NaV1.5/β2 to the plasma membrane. 17222411 2 48 part_of possesses 235:243 arg1 Podoplanin AND a platelet aggregation-stimulating (PLAG) domain Podoplanin a platelet aggregation-stimulating (PLAG) domain OGER AminoAcid Podoplanin Q86YL7 domain, and Thr52 Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity. 8193553 8 29 gly had 1392:1394 arg1 Recombinant glycophorin A AND the same O-glycan composition Recombinant glycophorin A the same O-glycan composition PUBTATOR Recombinant glycophorin A 2993 Recombinant glycophorin A had the same O-glycan composition, whether purified from clones expressing high or moderate levels of the recombinant glycoprotein. 25213400 9 5 gly containing 825:834 arg1 MS2 AND one glucuronic acid MS2 one glucuronic acid PUBTATOR MS2 100271694 The most charged glycan is MS2 containing three sulfate groups and one glucuronic acid; whereas the least charged one is the BA2 residue. 8631363 3 11 gly contained 418:426 arg1 the tumor necrosis factor-alpha AND galactose the tumor necrosis factor-alpha galactose PUBTATOR tumor necrosis factor-alpha 7124 Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components. 8631363 3 11 gly contained 418:426 arg1 the tumor necrosis factor-alpha AND N-acetylneuraminic acid the tumor necrosis factor-alpha N-acetylneuraminic acid PUBTATOR tumor necrosis factor-alpha 7124 Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components. 8631363 3 11 gly contained 418:426 arg1 the tumor necrosis factor-alpha AND N-acetylgalactosamine the tumor necrosis factor-alpha N-acetylgalactosamine PUBTATOR tumor necrosis factor-alpha 7124 Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components. 8631363 3 11 gly contained 418:426 arg1 the tumor necrosis factor-alpha AND sugar components the tumor necrosis factor-alpha sugar components PUBTATOR tumor necrosis factor-alpha 7124 Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components. 9343410 4 12 gly contain 790:796 arg1 Sp1 AND a dominant O-GlcNAc residue Sp1 a dominant O-GlcNAc residue OGER Sp1 Q8N907 When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site. 25213400 11 26 gly contains 1144:1151 arg1 GP4 AND one sialic acid GP4 one sialic acid PUBTATOR GP4 948 The most mannose rich are the glycans MS2 and GP4, each of them has four mannoses; OPPE1 contains five N-acetylglucosamines and one sulfated glucuronic acid; GP4 contains one sialic acid. 18381078 2 19 gly contain 340:346 arg1 ADAM10 AND high-mannose and complex-type glycans ADAM10 high-mannose and complex-type glycans PUBTATOR ADAM10 102 In this work, ADAM10 was found to contain high-mannose and complex-type glycans. 8638940 4 6 gly contains 743:750 arg1 Each subunit AND one N-linked oligosaccharide Each subunit one N-linked oligosaccharide OGER Each subunit P20933 Each subunit of glycosylasparaginase contains one N-linked oligosaccharide (N38, alpha-subunit; N308, beta-subunit). 7780197 1 21 gly contains 140:147 arg1 TfR AND three N-linked oligosaccharides TfR three N-linked oligosaccharides PUBTATOR TfR 7037 The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule. 7780197 1 21 gly contains 140:147 arg1 The human transferrin receptor AND three N-linked oligosaccharides The human transferrin receptor three N-linked oligosaccharides PUBTATOR transferrin receptor 7037 The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule. 26348848 4 81 gly had 707:709 arg1 wild type Kv3.1a and Kv1.1 α-subunits AND oligomannose N-glycans wild type Kv3.1a and Kv1.1 α-subunits oligomannose N-glycans PUBTATOR Kv1.1 α-subunits 3736 Western blots revealed that wild type Kv3.1a and Kv1.1 α-subunits had complex and oligomannose N-glycans, respectively, and that abolishment of the N-glycosylation site(s) generated Kv proteins without N-glycans. 9194614 11 7 gly has 1735:1737 arg1 the nPhl p 1 AND a 5% carbohydrate content the nPhl p 1 a 5% carbohydrate content PUBTATOR nPhl p 1 1423 This rPhl p 1 is hyperglycosylated compared to the nPhl p 1, which only has a 5% carbohydrate content. 31888963 9 84 gly contain 1324:1330 arg1 CD16a AND highly processed complex-type N-glycans CD16a highly processed complex-type N-glycans PUBTATOR CD16a 2214 N38 and N74 of CD16a both contain highly processed complex-type N-glycans with N-acetyllactosamine repeats and complex-type biantennary N-glycans dominate at N169. 2168975 4 50 gly having 512:517 arg1 QN-1 AND an additional N-linked oligosaccharide QN-1 an additional N-linked oligosaccharide OGER QN-1 Q5TB80 We found that one mutant protein (QN-1) having an additional N-linked oligosaccharide at amino acid 117 in the extracellular domain was incorporated into VSV virions but that the virions containing this glycoprotein were not infectious. 21264968 4 127 part_of containing 1629:1638 arg1 densely glycosylated MUC4 AND Ser5 densely glycosylated MUC4 Ser5 PUBTATOR AminoAcid MUC4 4585 residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15 In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15. 21264968 4 127 part_of containing 1629:1638 arg1 densely glycosylated MUC4 AND Thr6 densely glycosylated MUC4 Thr6 PUBTATOR AminoAcid MUC4 4585 residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15 In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15. 21264968 4 127 part_of containing 1629:1638 arg1 densely glycosylated MUC4 AND Ser2 densely glycosylated MUC4 Ser2 PUBTATOR AminoAcid MUC4 4585 residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15 In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15. 21264968 4 127 part_of containing 1629:1638 arg1 densely glycosylated MUC4 AND Thr10 densely glycosylated MUC4 Thr10 PUBTATOR AminoAcid MUC4 4585 residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15 In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15. 21264968 4 127 part_of containing 1629:1638 arg1 densely glycosylated MUC4 AND Thr15 densely glycosylated MUC4 Thr15 PUBTATOR AminoAcid MUC4 4585 residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15 In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15. 21264968 4 127 gly containing 1629:1638 arg1 densely glycosylated MUC4 AND six α-GalNAc residues densely glycosylated MUC4 Thr15 six α-GalNAc residues PUBTATOR AminoAcid MUC4 4585 residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15 In the present study, O-glycosylation was initiated specifically at Thr10 in naked MUC4 peptide and additional introduction of α-GalNAc proceeded preferentially but randomly at three other Thr residues to afford densely glycosylated MUC4 containing six α-GalNAc residues at Thr1, Ser2, Ser5, Thr6, Thr10, and Thr15. 8357534 4 44 gly contain 715:721 arg1 C-3 AND exclusively truncated, oligomannose-type chains C-3 the same positions exclusively truncated, oligomannose-type chains PUBTATOR E-3 and C-3 P01024 positions In contrast, the isoforms E-3 and C-3, the major forms of elastase and cathepsin G respectively, contain exclusively truncated, oligomannose-type chains at the same positions in the sequence of each protein. 8357534 4 44 gly contain 715:721 arg1 E-3 AND exclusively truncated, oligomannose-type chains E-3 the same positions exclusively truncated, oligomannose-type chains PUBTATOR E-3 and C-3 P01024 positions In contrast, the isoforms E-3 and C-3, the major forms of elastase and cathepsin G respectively, contain exclusively truncated, oligomannose-type chains at the same positions in the sequence of each protein. 7620335 1 59 gly has 159:161 arg1 Human blood coagulation factor X AND two N-linked oligosaccharides Human blood coagulation factor X two N-linked oligosaccharides OGER factor X P00742 Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa. 7620335 1 59 gly has 159:161 arg1 Human blood coagulation factor X AND two O-linked oligosaccharides Human blood coagulation factor X two O-linked oligosaccharides OGER factor X P00742 Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa. 31826991 14 56 gly have 2317:2320 arg1 H3 HAs AND one or more key high-mannose glycosites H3 HAs one or more key high-mannose glycosites OGER H3 HAs Q92839 While it is known that both H1 and H3 HAs have one or more key high-mannose glycosites in the head region, little is known about similar glycosylation of LPAIV strains H2N1, H5N1, H6N1, or H11N9, which may pose future health risks. 14693913 5 2 gly contain 868:874 arg1 hBSSL AND 16 Pro-rich 11-amino-acid repeats hBSSL The C-terminal 192 residues 16 Pro-rich 11-amino-acid repeats PUBTATOR hBSSL 1056 residues The C-terminal 192 residues of hBSSL contain 16 Pro-rich 11-amino-acid repeats, which include 32 Ser/Thr residues as potential O-glycosylation sites. 15590981 1 38 gly have 185:188 arg1 Pituitary equine luteinizing hormone AND different linked carbohydrates Pituitary equine luteinizing hormone different linked carbohydrates OGER luteinizing hormone Pituitary equine luteinizing hormone (eLH) and fetal chorionic gonadotrophin (eCG) have identical polypeptidic chains, but different linked carbohydrates. 15590981 1 38 gly have 185:188 arg1 fetal chorionic gonadotrophin AND different linked carbohydrates fetal chorionic gonadotrophin different linked carbohydrates OGER chorionic gonadotrophin Pituitary equine luteinizing hormone (eLH) and fetal chorionic gonadotrophin (eCG) have identical polypeptidic chains, but different linked carbohydrates. 8357534 2 39 part_of has 374:376 arg1 cathepsin G AND Asn-64 cathepsin G Asn-64 PUBTATOR SpecificSite cathepsin G 1511 Asn-64 Elastase has two N-glycosylation sites occupied (Asn-45 and Asn-144), whereas cathepsin G has only one (Asn-64). 10861210 2 70 gly contained 502:510 arg1 Human AE1 AND a high-mannose oligosaccharide Human AE1 a high-mannose oligosaccharide PUBTATOR Human AE1 6521 Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained a high-mannose oligosaccharide. 16622833 2 16 gly contain 275:281 arg1 A1PI AND diantennary N-glycans but also triantennary and even traces A1PI diantennary N-glycans but also triantennary and even traces PUBTATOR A1PI 5265 The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI. 6980014 6 52 gly contain 902:908 arg1 II AND one carbohydrate chain II fragments II and III each one carbohydrate chain Cterm Site II fragments On the other hand, fragments II and III each contain one carbohydrate chain exclusively by the biantennary type of complex N-glycoside. 18279659 3 52 gly has 416:418 arg1 ABCB6 AND a primary determinant ABCB6 a primary determinant PUBTATOR ABCB6 10058 We show here that ABCB6 has an N-terminal hydrophobic region of 220 residues that functions as a primary determinant of co-translational targeting to the endoplasmic reticulum (ER), but it does not have any known features of a mitochondrial targeting sequence. 7780197 0 65 gly contains 62:69 arg1 human transferrin receptor AND a high-mannose oligosaccharide human transferrin receptor The critical glycosylation site a high-mannose oligosaccharide PUBTATOR transferrin receptor 7037 site The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide. 22246941 2 3 part_of contains 317:324 arg1 Hedgehog APRIL AND Cys(196) Hedgehog APRIL Cys(196) PUBTATOR SpecificSite Hedgehog APRIL O75888 Cys(196) and Cys(211) Hedgehog APRIL contains two cysteine residues (Cys(196) and Cys(211)), a furin protease cleavage site and a conserved putative N-glycosylation site (Asn(124)). 22246941 2 3 part_of contains 317:324 arg1 Hedgehog APRIL AND Cys(211) Hedgehog APRIL Cys(211) PUBTATOR SpecificSite Hedgehog APRIL O75888 Cys(196) and Cys(211) Hedgehog APRIL contains two cysteine residues (Cys(196) and Cys(211)), a furin protease cleavage site and a conserved putative N-glycosylation site (Asn(124)). 20543007 6 74 part_of contains 965:972 arg1 heavy-chain CDR3 AND three residues heavy-chain CDR3 three residues PUBTATOR SpecificSite CDR3 8163 residues ((99) Structural studies combined with mutagenesis data identified an aggregation 'hot spot' in heavy-chain CDR3 (H-CDR3) that contains three residues ((99)FHW(100a)). 20543007 6 74 part_of contains 965:972 arg1 H-CDR3 AND three residues H-CDR3 three residues PUBTATOR SpecificSite CDR3 8163 residues ((99) Structural studies combined with mutagenesis data identified an aggregation 'hot spot' in heavy-chain CDR3 (H-CDR3) that contains three residues ((99)FHW(100a)). 15616124 6 39 gly had 772:774 arg1 most labeled intracellular FVII AND one N-glycan most labeled intracellular FVII one N-glycan Cterm FVII 2155 Immediately after pulse, most labeled intracellular FVII had one N-glycan, but during a 1-h chase, the vast majority was processed into FVII with two N-glycans, demonstrating posttranslational N-glycosylation of FVII. 24780636 1 1 gly possesses 127:135 arg1 Transferrin AND N-glycans Transferrin N-glycans PUBTATOR Transferrin 7018 Transferrin is an iron-transport protein which possesses N-glycans at Asn432 and Asn630 in humans. 1388166 1 88 gly contains 207:214 arg1 TFPI AND sulfated Asn-linked oligosaccharides TFPI sulfated Asn-linked oligosaccharides PUBTATOR TFPI 7035 Tissue factor pathway inhibitor (TFPI) produced by endothelial cells contains sulfated Asn-linked oligosaccharides. 1388166 1 88 gly contains 207:214 arg1 Tissue factor pathway inhibitor AND sulfated Asn-linked oligosaccharides Tissue factor pathway inhibitor sulfated Asn-linked oligosaccharides PUBTATOR Tissue factor pathway inhibitor 7035 Tissue factor pathway inhibitor (TFPI) produced by endothelial cells contains sulfated Asn-linked oligosaccharides. 15616124 3 7 part_of has 416:418 arg1 Human FVII AND N322 Human FVII N322 Cterm SpecificSite Human FVII 2155 N145 and N322 Human FVII has two N-glycosylation sites (N145 and N322). 15616124 3 7 part_of has 416:418 arg1 Human FVII AND N145 Human FVII N145 Cterm SpecificSite Human FVII 2155 N145 and N322 Human FVII has two N-glycosylation sites (N145 and N322). 7916636 4 39 part_of contain 471:477 arg1 urinary kallikrein AND a Lys-162 urinary kallikrein a Lys-162 PUBTATOR SpecificSite kallikrein 9622 Lys-162 The human kallikrein gene and urinary kallikrein both contain a Lys-162 instead of the reported Glu-162. 8706658 2 23 part_of has 429:431 arg1 Human leukotriene C4 synthase AND residues 37-58 Human leukotriene C4 synthase residues 37-58 PUBTATOR SpecificSite Human leukotriene C4 synthase 4056 residues 37-58 Human leukotriene C4 synthase shares substantial amino acid identity in its consensus N-terminal two-thirds with 5-lipoxygenase-activating protein and has a region (residues 37-58) that exhibits 46% amino acid identity with a domain of this protein (residues 41 -62) to which an inhibitor binds. 8157687 0 90 gly contains 424:431 arg1 the complement glycoprotein iC3b AND oligosaccharides the complement glycoprotein iC3b oligosaccharides Cterm iC3b Differential recognition by conglutinin and mannan-binding protein of N-glycans presented on neoglycolipids and glycoproteins with special reference to complement glycoprotein C3 and ribonuclease B. Conglutinin and mannan-binding protein are serum proteins that have similar carbohydrate binding specificities toward high mannose-type oligosaccharides, and yet only conglutinin binds the complement glycoprotein iC3b, which contains oligosaccharides of this type. 10712595 9 2 gly have 1629:1632 arg1 Salmon antithrombin AND three complex oligosaccharide side chains Salmon antithrombin three complex oligosaccharide side chains PUBTATOR antithrombin 462 Salmon antithrombin appears to have three complex oligosaccharide side chains containing sialic acid terminally linked alpha(2-3) to galactose, while trace amounts of Galbeta(1-4)GlcNAc suggest microheterogeneity due to partial loss of sialic acid. 24338886 6 90 gly has 1224:1226 arg1 rhEPO AND a highly uniform bi-antennary N-linked glycan composition rhEPO a highly uniform bi-antennary N-linked glycan composition OGER rhEPO P29676 In summary, the mass spectrometric analyses revealed that rhEPO derived from glycoengineered Pichia has a highly uniform bi-antennary N-linked glycan composition and preserves the orthogonal O-linked glycosylation site present on endogenous human EPO and CHO-derived rhEPO. 12175779 11 16 gly has 1468:1470 arg1 GLUT11-L AND glucose transport activity GLUT11-L glucose transport activity PUBTATOR GLUT11 66035 Furthermore, a liposome reconstitution functional assay showed that GLUT11-L has glucose transport activity. 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. 7479385 4 94 gly contains 771:778 arg1 PSA AND a carbohydrate residue PSA a carbohydrate residue PUBTATOR PSA 354 The predominant PSA molecular species detected by ISMS was at relative molecular mass (M(r)) of 28,430, indicating that PSA contains a carbohydrate residue of M(r) 2,351, for a total percentage of carbohydrate of 8.3%. 16567801 7 92 gly contained 1535:1543 arg1 Human UPIa AND high mannose glycans Human UPIa high mannose glycans PUBTATOR UPIa 11045 Human UPIa contained exclusively high mannose glycans, and human UPIb contained only complex glycans. 22688517 6 30 gly carry 1238:1242 arg1 recombinant human LOX-1 AND heterogeneous complex type N-glycans recombinant human LOX-1 one potential glycosylation 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. 2350186 2 85 gly has 382:384 arg1 Normal murine IgM AND five N-linked oligosaccharides Normal murine IgM five N-linked oligosaccharides OGER IgM P01872 Normal murine IgM has five N-linked oligosaccharides in the constant region of each heavy or mu-chain. 10383441 4 35 part_of contains 571:578 arg1 murine DNase I AND Lys74 murine DNase I Lys74 PUBTATOR AminoAcid DNase I 13419 Lys27 and Lys74 We now demonstrate that murine DNase I, which contains Lys27 and Lys74, is phosphorylated only 20.9% when expressed in the same COS-1 cell system. 10383441 4 35 part_of contains 571:578 arg1 murine DNase I AND Lys27 murine DNase I Lys27 PUBTATOR AminoAcid DNase I 13419 Lys27 and Lys74 We now demonstrate that murine DNase I, which contains Lys27 and Lys74, is phosphorylated only 20.9% when expressed in the same COS-1 cell system. 1567356 1 10 gly contains 95:102 arg1 OMD AND tetra-antennary glycan chains OMD tetra-antennary glycan chains OGER Orosomucoid (OMD Q99983 Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains. 1567356 1 10 gly contains 95:102 arg1 OMD AND tri- OMD tri- OGER Orosomucoid (OMD Q99983 Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains. 1567356 1 10 gly contains 95:102 arg1 OMD AND complex bi- OMD complex bi- OGER Orosomucoid (OMD Q99983 Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains. 1567356 1 10 gly contains 95:102 arg1 Orosomucoid AND tetra-antennary glycan chains Orosomucoid tetra-antennary glycan chains OGER Orosomucoid (OMD Q99983 Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains. 1567356 1 10 gly contains 95:102 arg1 Orosomucoid AND tri- Orosomucoid tri- OGER Orosomucoid (OMD Q99983 Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains. 1567356 1 10 gly contains 95:102 arg1 Orosomucoid AND complex bi- Orosomucoid complex bi- OGER Orosomucoid (OMD Q99983 Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains. 19822741 2 29 gly containing 406:415 arg1 HA AND glycans HA glycans Cterm HA Viral transmission begins with a critical interaction between hemagglutinin (HA) glycoprotein, which is on the viral coat of influenza, and sialic acid (SA) containing glycans, which are on the host cell surface. 10712595 0 8 gly has 20:22 arg1 Salmon antithrombin AND only three carbohydrate side chains Salmon antithrombin only three carbohydrate side chains PUBTATOR antithrombin 462 Salmon antithrombin has only three carbohydrate side chains, and shows functional similarities to human beta-antithrombin. 7613477 5 46 gly contain 1180:1186 arg1 LCAT AND triantennary LCAT Asn84 triantennary PUBTATOR LCAT 3931 Asn20, Asn84, Asn272, and Asn384 All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures. 7613477 5 46 gly contain 1180:1186 arg1 LCAT AND sialylated triantennary and/or biantennary complex structures LCAT Asn84 sialylated triantennary and/or biantennary complex structures PUBTATOR LCAT 3931 Asn20, Asn84, Asn272, and Asn384 All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures. 1840295 9 34 gly containing 1438:1447 arg1 control type II tPA AND sugar control type II tPA sugar PUBTATOR tPA P00750 In the dMM-treated sample, type I tPA (with sugars at sites 117, 184 and 448) was found to have 2- to 3-fold increased catalytic activity and an affinity for lysine which was greater than that of type I from untreated preparations, but less than that of control type II tPA (containing sugar only at sites 117 and 448). 11595658 1 42 part_of contains 154:161 arg1 The corticotropin-releasing factor (CRF) receptor type 1 AND N38 The corticotropin-releasing factor (CRF) receptor type 1 N38 PUBTATOR SpecificSite corticotropin-releasing factor (CRF) receptor type 1 1394 N38, N45, N78, N90, and N98 The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98. 11595658 1 42 part_of contains 154:161 arg1 The corticotropin-releasing factor (CRF) receptor type 1 AND N98 The corticotropin-releasing factor (CRF) receptor type 1 N98 PUBTATOR SpecificSite corticotropin-releasing factor (CRF) receptor type 1 1394 N38, N45, N78, N90, and N98 The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98. 11595658 1 42 part_of contains 154:161 arg1 The corticotropin-releasing factor (CRF) receptor type 1 AND N90 The corticotropin-releasing factor (CRF) receptor type 1 N90 PUBTATOR SpecificSite corticotropin-releasing factor (CRF) receptor type 1 1394 N38, N45, N78, N90, and N98 The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98. 11595658 1 42 part_of contains 154:161 arg1 The corticotropin-releasing factor (CRF) receptor type 1 AND N45 The corticotropin-releasing factor (CRF) receptor type 1 N45 PUBTATOR SpecificSite corticotropin-releasing factor (CRF) receptor type 1 1394 N38, N45, N78, N90, and N98 The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98. 11595658 1 42 part_of contains 154:161 arg1 The corticotropin-releasing factor (CRF) receptor type 1 AND N78 The corticotropin-releasing factor (CRF) receptor type 1 N78 PUBTATOR SpecificSite corticotropin-releasing factor (CRF) receptor type 1 1394 N38, N45, N78, N90, and N98 The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98. 11595658 1 42 part_of contains 154:161 arg1 CRFR1 AND N38 CRFR1 N38 PUBTATOR SpecificSite CRFR1 1394 N38, N45, N78, N90, and N98 The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98. 11595658 1 42 part_of contains 154:161 arg1 CRFR1 AND N98 CRFR1 N98 PUBTATOR SpecificSite CRFR1 1394 N38, N45, N78, N90, and N98 The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98. 11595658 1 42 part_of contains 154:161 arg1 CRFR1 AND N90 CRFR1 N90 PUBTATOR SpecificSite CRFR1 1394 N38, N45, N78, N90, and N98 The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98. 11595658 1 42 part_of contains 154:161 arg1 CRFR1 AND N45 CRFR1 N45 PUBTATOR SpecificSite CRFR1 1394 N38, N45, N78, N90, and N98 The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98. 11595658 1 42 part_of contains 154:161 arg1 CRFR1 AND N78 CRFR1 N78 PUBTATOR SpecificSite CRFR1 1394 N38, N45, N78, N90, and N98 The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98. 10731668 2 32 gly contains 370:377 arg1 the CHO sEGFR AND one oligosaccharide chain the CHO sEGFR one oligosaccharide chain PUBTATOR CHO sEGFR P00533 We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ). 14985108 6 45 gly contains 696:703 arg1 gONC AND a high-mannose core structure gONC a high-mannose core structure Cterm gONC We found that gONC contains a high-mannose core structure. 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. 16227292 1 17 part_of contain 215:221 arg1 Gc AND N60 Gc N60 Cterm SpecificSite Gc N60 The membrane glycoproteins (Gn and Gc) of Bunyamwera virus (BUN, family Bunyaviridae) contain three potential sites for the attachment of N-linked glycans: one site (N60) on Gn and two (N624 and N1169) on Gc. 8068684 7 84 gly contains 1270:1277 arg1 NHE-1 AND O-linked oligosaccharide NHE-1 O-linked oligosaccharide PUBTATOR NHE-1 6548 In addition, treatment of NHE-1 with neuraminidase and O-glycosidase demonstrated that NHE-1 also contains O-linked oligosaccharide. 16567801 7 26 gly contained 1594:1602 arg1 human UPIb AND only complex glycans human UPIb only complex glycans PUBTATOR UPIb 7348 Human UPIa contained exclusively high mannose glycans, and human UPIb contained only complex glycans. 24884609 9 6 gly contained 1294:1302 arg1 recombinant ITIH4 AND high-mannose N-linked glycans recombinant ITIH4 high-mannose N-linked glycans PUBTATOR ITIH4 3700 Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4. 24884609 9 6 part_of contained 1294:1302 arg1 recombinant ITIH4 AND Site N274 recombinant ITIH4 Site N274 high-mannose N-linked glycans PUBTATOR SpecificSite ITIH4 3700 N274 Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4. 8157687 0 63 gly have 262:265 arg1 mannan-binding protein AND similar carbohydrate binding specificities mannan-binding protein similar carbohydrate binding specificities OGER mannan-binding protein P11226 Differential recognition by conglutinin and mannan-binding protein of N-glycans presented on neoglycolipids and glycoproteins with special reference to complement glycoprotein C3 and ribonuclease B. Conglutinin and mannan-binding protein are serum proteins that have similar carbohydrate binding specificities toward high mannose-type oligosaccharides, and yet only conglutinin binds the complement glycoprotein iC3b, which contains oligosaccharides of this type. 8157687 6 92 gly contains 1537:1544 arg1 RNase B AND high mannose-type oligosaccharides RNase B Asn-34 high mannose-type oligosaccharides OGER RNase B P07998 Asn-34 From these and additional observations with RNase B, which contains high mannose-type oligosaccharides at Asn-34, it is clear that the protein moieties of these glycoproteins markedly influence the presentation of the oligosaccharides such that biological specificity is mediated by the commonly occurring high mannose-type oligosaccharides in the context of specific carrier proteins. 9792708 1 41 gly contains 144:151 arg1 The mouse hepatitis virus (MHV) membrane (M) protein AND only O-linked oligosaccharides The mouse hepatitis virus (MHV) membrane (M) protein only O-linked oligosaccharides OGER M) protein P54296 The mouse hepatitis virus (MHV) membrane (M) protein contains only O-linked oligosaccharides.