PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27453399-3 2016 Mucin-related glycopeptides incorporating these motifs were recognized by the monoclonal antibody (mAb) scFv-SM3, with activities depending on both the hydroxylation pattern (Glc/Gal/GlcNAc/GalNAc) of the sp(2)-iminosugar and the peptide aglycone structure (Ser/Thr). N-acetylgalactosaminuronic acid 190-196 LOC100508689 Homo sapiens 0-5 31548401-1 2019 Polypeptide N-acetylgalactosaminyl transferases (GalNAc-Ts) initiate mucin type O-glycosylation by catalyzing the transfer of N-acetylgalactosamine (GalNAc) to Ser or Thr on a protein substrate. N-acetylgalactosaminuronic acid 49-55 LOC100508689 Homo sapiens 69-74 22791304-2 2012 Mucin-type (N-acetylgalactosamine [GalNAc]-type) O-glycosylation is found in eumetazoan cells but absent in plants and yeast, making these cell types an obvious choice for de novo engineering of this O-glycosylation pathway. N-acetylgalactosaminuronic acid 35-41 LOC100508689 Homo sapiens 0-5 25324212-0 2014 Delineating binding modes of Gal/GalNAc and structural elements of the molecular recognition of tumor-associated mucin glycopeptides by the human macrophage galactose-type lectin. N-acetylgalactosaminuronic acid 33-39 LOC100508689 Homo sapiens 113-118 25727146-1 2015 Mucin-type O-glycans are a class of glycans initiated with N-acetylgalactosamine (GalNAc) alpha-linked primarily to Ser/Thr residues within glycoproteins and often extended or branched by sugars or saccharides. N-acetylgalactosaminuronic acid 82-88 LOC100508689 Homo sapiens 0-5 22791304-5 2012 Efficient GalNAc O-glycosylation of two stably coexpressed substrate O-glycoproteins was obtained, but a high degree of proline hydroxylation and hydroxyproline-linked arabinosides, on a mucin (MUC1)-derived substrate, was also observed. N-acetylgalactosaminuronic acid 10-16 LOC100508689 Homo sapiens 187-192 22183981-2 2012 Mucin-type O-glycosylation, consisting of glycans attached via O-linked N-acetylgalactosamine (GalNAc) to serine and threonine residues, is one of the most abundant forms of protein glycosylation in animals. N-acetylgalactosaminuronic acid 95-101 LOC100508689 Homo sapiens 0-5 20301232-2 2009 In mucins, O-glycans are covalently alpha-linked via an N-acetylgalactosamine (GalNAc) moiety to the -OH of serine or threonine by an O-glycosidic bond, and the structures are named mucin O-glycans or O-GalNAc glycans. N-acetylgalactosaminuronic acid 79-85 LOC100508689 Homo sapiens 3-8 20735851-2 2010 A large family of UDP-GalNAc polypeptide:N-acetyl-alpha-galactosaminyltransferases (GalNAc-Ts) catalyzes the first step of mucin type O-glycosylation by transferring GalNAc to serine and/or threonine residues of acceptor polypeptides. N-acetylgalactosaminuronic acid 22-28 LOC100508689 Homo sapiens 123-128 20735851-2 2010 A large family of UDP-GalNAc polypeptide:N-acetyl-alpha-galactosaminyltransferases (GalNAc-Ts) catalyzes the first step of mucin type O-glycosylation by transferring GalNAc to serine and/or threonine residues of acceptor polypeptides. N-acetylgalactosaminuronic acid 84-90 LOC100508689 Homo sapiens 123-128 21514575-1 2011 For the investigation of glycosidases, and for the construction of glycan arrays the p-nitrophenyl- and p-aminophenyl glycosides of mucin O-glycan core structures 1-7 and the 2,6-ST-antigen have been chemically synthesized using d-galactose as a precursor for GalNAc residues. N-acetylgalactosaminuronic acid 260-266 LOC100508689 Homo sapiens 132-137 14749330-10 2004 The results show that the mucin polypeptide undergoes dimerization and then becomes substituted with GalNAc residues prior to glycan elaboration to produce a mature mucin dimer, which then undergoes multimerization. N-acetylgalactosaminuronic acid 101-107 LOC100508689 Homo sapiens 26-31 15646032-1 2004 A UDP-GalNAc:polypeptide N-acetyl-galactosaminyl transferase which catalyses the transfer of GalNAc from UDP-GalNAc to serine and threonine residues in mucin polypeptide chains was purified to homogeneity from swine trachea epithelium (Mendicino J, Sangadala S: Mol Cell Biochem 185: 135-145, 1998). N-acetylgalactosaminuronic acid 6-12 LOC100508689 Homo sapiens 152-157 14749330-10 2004 The results show that the mucin polypeptide undergoes dimerization and then becomes substituted with GalNAc residues prior to glycan elaboration to produce a mature mucin dimer, which then undergoes multimerization. N-acetylgalactosaminuronic acid 101-107 LOC100508689 Homo sapiens 165-170 11415465-3 2001 With the use of capillary electrophoresis, MS and Edman degradation, our study suggests that, in the O-glycosylation of mucin-type proteins, approach and recognition signalling by gpGaNTase-T7 and gpGaNTase-T9 depend largely on the peptide"s primary structure (for example the presence of multiple clusters of hydroxy amino acids and the number of GalNAc residues attached to the peptide backbone). N-acetylgalactosaminuronic acid 348-354 LOC100508689 Homo sapiens 120-125 12386453-9 2001 The only structural element shared by all mucin O-glycan chains is a GalNAc residue linked to a serine or threonine residue of the apomucin. N-acetylgalactosaminuronic acid 69-75 LOC100508689 Homo sapiens 42-47 12364335-1 2002 Mucin type O-glycosylation begins with the transfer of GalNAc to serine and threonine residues on proteins by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminlytransferases. N-acetylgalactosaminuronic acid 55-61 LOC100508689 Homo sapiens 0-5 10217327-4 1999 Fluorescence binding studies indicate that alpha-N-acetylgalactosamine (GalNAc) glycosylation of a MUC1 mucin synthetic peptide TAPPAHGVT9SAPDTRPAPGS20T21APPA at threonine residues 9 and 21 and serine residue 20 enhanced the binding of antibody. N-acetylgalactosaminuronic acid 72-78 LOC100508689 Homo sapiens 104-109 2082812-6 1990 For a human salivary mucin (MG-2) it has been described that sialic acid in the sequence NeuAc (alpha 2,3)Gal(beta 1,3)GalNac- was specifically involved in the interaction with S. sanguis strains, in contrast to S. rattus BHT. N-acetylgalactosaminuronic acid 119-125 LOC100508689 Homo sapiens 21-26 8909998-5 1996 The decrease in mucin sialylation was achieved through the in situ beta-galactosylation of GalNAc alpha-O-benzyl into Gal beta 1-3GalNAc alpha-O-benzyl, which acts as a competitive substrate of Gal beta 1-3GalNAc alpha 2,3-sialyltransferase, as shown by the intracellular accumulation of NeuAc alpha 2-3Gal beta 1-3GalNAc alpha-O-benzyl in treated cells. N-acetylgalactosaminuronic acid 91-97 LOC100508689 Homo sapiens 16-21 7540808-5 1995 A comparison of mucin preparations purified by our method and by CsCl density gradient centrifugation indicated that the GalNAc/protein and GalNAc/DNA ratios were three times higher than those of the first method. N-acetylgalactosaminuronic acid 121-127 LOC100508689 Homo sapiens 16-21 7540808-5 1995 A comparison of mucin preparations purified by our method and by CsCl density gradient centrifugation indicated that the GalNAc/protein and GalNAc/DNA ratios were three times higher than those of the first method. N-acetylgalactosaminuronic acid 140-146 LOC100508689 Homo sapiens 16-21 1663364-7 1991 Indeed, the increased reactivity after sialidase treatment of ovine submaxillary mucin suggests the lectin reacts with peptide-linked N-acetylgalactosamine (GalNAc), since more than 98% of the glycan chains attached to this mucin are sialylated GalNAc. N-acetylgalactosaminuronic acid 157-163 LOC100508689 Homo sapiens 81-86 1663364-7 1991 Indeed, the increased reactivity after sialidase treatment of ovine submaxillary mucin suggests the lectin reacts with peptide-linked N-acetylgalactosamine (GalNAc), since more than 98% of the glycan chains attached to this mucin are sialylated GalNAc. N-acetylgalactosaminuronic acid 157-163 LOC100508689 Homo sapiens 224-229 1663364-7 1991 Indeed, the increased reactivity after sialidase treatment of ovine submaxillary mucin suggests the lectin reacts with peptide-linked N-acetylgalactosamine (GalNAc), since more than 98% of the glycan chains attached to this mucin are sialylated GalNAc. N-acetylgalactosaminuronic acid 245-251 LOC100508689 Homo sapiens 81-86 1663364-8 1991 The binding of SSA-M to sialidase-treated porcine mucin was inhibited strongly by GalNAc and disaccharides containing galactose (lactose, melibiose, and N-acetyllactosamine) but not by free galactose (Gal), suggesting that the glycan for optimum binding is Gal beta(1-3)GalNAc. N-acetylgalactosaminuronic acid 82-88 LOC100508689 Homo sapiens 50-55 2201583-1 1990 Rat and human colonic mucin glycoproteins bind to the Gal/GalNAc adherence lectin on the surface of Entamoeba histolytica in vitro, thus inhibiting the organism from adhering to and lysing the target cells. N-acetylgalactosaminuronic acid 58-64 LOC100508689 Homo sapiens 22-27 34495529-0 2021 Mucin-Type O-GalNAc Glycosylation in Health and Disease. N-acetylgalactosaminuronic acid 13-19 LOC100508689 Homo sapiens 0-5 34931806-6 2022 Here, we attempt to do the same for the core GalNAc residue of mucin O-linked glycosylation. N-acetylgalactosaminuronic acid 45-51 LOC100508689 Homo sapiens 63-68 34576978-1 2021 Mucin-type O-glycosylation involves the attachment of glycans to an initial O-linked N-acetylgalactosamine (GalNAc) on serine and threonine residues on proteins. N-acetylgalactosaminuronic acid 108-114 LOC100508689 Homo sapiens 0-5 34495529-1 2021 Mucin-type GalNAc O-glycosylation is one of the most abundant and unique post-translational modifications. N-acetylgalactosaminuronic acid 11-17 LOC100508689 Homo sapiens 0-5 33068214-2 2021 Mucin-type O-glycosylation is initiated by the transfer of N-acetyl-galactosamine (GalNAc) to the hydroxyl group of serine, threonine and tyrosine residues through catalysis by a family of glycosyltransferases, the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (E.C. N-acetylgalactosaminuronic acid 83-89 LOC100508689 Homo sapiens 0-5 2775721-14 1989 These observations together with the results of earlier studies indicate that steric interactions of the O-linked GalNAc residue with the peptide core are primarily responsible for the expanded mucin structure and that these perturbations extend to the nonglycosylated amino acid residues. N-acetylgalactosaminuronic acid 114-120 LOC100508689 Homo sapiens 194-199 3335536-3 1988 The mucin-type sugar chains of all hCGs include sialylated and nonsialylated Gal beta 1----3GalNAc and Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAc. N-acetylgalactosaminuronic acid 92-98 LOC100508689 Homo sapiens 4-9 7216166-7 1981 When the asialo-mucin had been [14C]sialylated by an ovine submaxillary gland cell-free preparation analysis of the product oligosaccharide chain revealed the introduction of [14C]sialic acid to position C-6 on the GalNAc residues. N-acetylgalactosaminuronic acid 215-221 LOC100508689 Homo sapiens 16-21 35587262-4 2022 To evaluate its efficiency as a donor, it was coupled to a 6-OH GalNAc acceptor, producing an extended Leb-containing Tn mucin core structure in 84% yield, and to L-serine in 72% yield. N-acetylgalactosaminuronic acid 64-70 LOC100508689 Homo sapiens 121-126 2450649-3 1988 Binding of the antibody to ovine submaxillary mucin glycoprotein was strongly inhibited by the O-linked disaccharide NeuAc alpha 2----6GalNAc alpha 1----O-serine, less strongly by NeuAc alpha 2----6GalNAc beta 1----O-propyl, and weakly by the monosaccharide GalNac. N-acetylgalactosaminuronic acid 258-264 LOC100508689 Homo sapiens 46-51 3160388-3 1985 Rat colon also catalyzes the in vitro transfer of GlcNAc from UDP-GlcNAc to GlcNAc beta 1-3GalNAc-mucin to form GlcNAc beta 1-3(GlcNAc beta 1-6) GalNAc-mucin. N-acetylgalactosaminuronic acid 91-97 LOC100508689 Homo sapiens 98-103 3160388-6 1985 The beta 3-GlcNAc-transferase from pig colon is activated by Triton X-100, has an absolute requirement for Mn2+, and transfers GlcNAc to GalNAc-alpha-phenyl, GalNAc-alpha-benzyl, and GalNAc-ovine submaxillary mucin with apparent Km values of 5, 2, and 3 mM and Vmax values of 59, 62, and 37 nmol h-1 (mg of protein)-1, respectively. N-acetylgalactosaminuronic acid 137-143 LOC100508689 Homo sapiens 209-214 3160388-6 1985 The beta 3-GlcNAc-transferase from pig colon is activated by Triton X-100, has an absolute requirement for Mn2+, and transfers GlcNAc to GalNAc-alpha-phenyl, GalNAc-alpha-benzyl, and GalNAc-ovine submaxillary mucin with apparent Km values of 5, 2, and 3 mM and Vmax values of 59, 62, and 37 nmol h-1 (mg of protein)-1, respectively. N-acetylgalactosaminuronic acid 158-164 LOC100508689 Homo sapiens 209-214 3160388-6 1985 The beta 3-GlcNAc-transferase from pig colon is activated by Triton X-100, has an absolute requirement for Mn2+, and transfers GlcNAc to GalNAc-alpha-phenyl, GalNAc-alpha-benzyl, and GalNAc-ovine submaxillary mucin with apparent Km values of 5, 2, and 3 mM and Vmax values of 59, 62, and 37 nmol h-1 (mg of protein)-1, respectively. N-acetylgalactosaminuronic acid 158-164 LOC100508689 Homo sapiens 209-214 6795195-7 1981 Reductive alkali treatment of mucin resulted in release of oligosaccharides with concomitant conversion of 77% of GalNAc to its reduced derivative N-acetylgalactosaminitol (GalNAcol) thus demonstrating O-glycosidic linkage of GalNAc to protein. N-acetylgalactosaminuronic acid 114-120 LOC100508689 Homo sapiens 30-35 6795195-7 1981 Reductive alkali treatment of mucin resulted in release of oligosaccharides with concomitant conversion of 77% of GalNAc to its reduced derivative N-acetylgalactosaminitol (GalNAcol) thus demonstrating O-glycosidic linkage of GalNAc to protein. N-acetylgalactosaminuronic acid 173-179 LOC100508689 Homo sapiens 30-35 32501708-7 2020 Here we apply it to representative mucin glycopeptides with O-linked glycans: three GalNAc localization variants, a pair with alpha/beta GalNAc anomers, and another with GalNAc/GlcNAc isomers. N-acetylgalactosaminuronic acid 84-90 LOC100508689 Homo sapiens 35-40 32501708-7 2020 Here we apply it to representative mucin glycopeptides with O-linked glycans: three GalNAc localization variants, a pair with alpha/beta GalNAc anomers, and another with GalNAc/GlcNAc isomers. N-acetylgalactosaminuronic acid 137-143 LOC100508689 Homo sapiens 35-40 32501708-7 2020 Here we apply it to representative mucin glycopeptides with O-linked glycans: three GalNAc localization variants, a pair with alpha/beta GalNAc anomers, and another with GalNAc/GlcNAc isomers. N-acetylgalactosaminuronic acid 137-143 LOC100508689 Homo sapiens 35-40 32304323-0 2020 Ser and Thr Acceptor Preferences of the GalNAc-Ts Vary Among Isoenzymes to Modulate Mucin Type O-Glycosylation. N-acetylgalactosaminuronic acid 40-46 LOC100508689 Homo sapiens 84-89 32304323-1 2020 A family of polypeptide GalNAc-transferases (GalNAc-Ts) initiates mucin-type O-glycosylation, transferring GalNAc onto hydroxyl groups of Ser and Thr residues of target substrates. N-acetylgalactosaminuronic acid 24-30 LOC100508689 Homo sapiens 66-71