PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32329196-6 2020 We demonstrate that loss of individual GalNAc-T isoforms causes distinct epithelial phenotypes through their effect on specific biological pathways; GalNAc-T1 targets are associated with components of the endomembrane system, GalNAc-T2 targets with cell-ECM adhesion, and GalNAc-T3 targets with epithelial differentiation. N-acetylgalactosaminuronic acid 39-45 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 226-235 29208955-4 2017 The GalNAc-T4 structure bound to a monoglycopeptide shows that the GalNAc-binding site of its lectin domain is rotated relative to the homologous GalNAc-T2 structure, explaining their different long-range preferences. N-acetylgalactosaminuronic acid 4-10 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 146-155 29039611-5 2017 In silico analysis based on publically available data was indicative for altered expression of five GalNAc-Ts (GALNT2, T4, T6, T9 and T14) in ovarian high-grade serous carcinoma (HGSC) samples compared to non-tumoral (control) ovarian tissue. N-acetylgalactosaminuronic acid 100-106 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 111-117 25548287-6 2015 The expression patterns of GalNAc transferases in the infected cells suggested that initial additions of GalNAc were carried out by initiating GalNAc transferases, in particular GalNAc-T2, whereas subsequent GalNAc additions were carried out by followup transferases, in particular GalNAc-T10. N-acetylgalactosaminuronic acid 27-33 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 178-187 27071848-4 2016 Two of these compounds, the GalNAc and galactose derivatives, were further tested on a model GT, such as GalNAc-T2 (an important GT widely distributed in human tissues), to probe that both compounds bound in the medium-high micromolar range. N-acetylgalactosaminuronic acid 28-34 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 105-114 25744272-2 2015 The early step in O-glycan formation is the attachment of N-acetylgalactosamine (GalNAc) to the serine/threonine of the hinge region; the process is catalysed by UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2). N-acetylgalactosaminuronic acid 81-87 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 162-244 25744272-2 2015 The early step in O-glycan formation is the attachment of N-acetylgalactosamine (GalNAc) to the serine/threonine of the hinge region; the process is catalysed by UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2). N-acetylgalactosaminuronic acid 81-87 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 246-252 25548287-6 2015 The expression patterns of GalNAc transferases in the infected cells suggested that initial additions of GalNAc were carried out by initiating GalNAc transferases, in particular GalNAc-T2, whereas subsequent GalNAc additions were carried out by followup transferases, in particular GalNAc-T10. N-acetylgalactosaminuronic acid 105-111 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 178-187 23117232-9 2012 Notably, we found that GALNT2 increased the expression of Tn antigen (GalNAc-Ser/Thr) on beta1-integrin as revealed by Vicia Villosa agglutinin (VVA) binding. N-acetylgalactosaminuronic acid 70-76 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 23-29 20735851-4 2010 RESULTS: The present study demonstrates that an isoform of the human GalNAc-Ts family, GalNAc-T2, retains its localization and functionality upon expression in N. benthamiana L. plants. N-acetylgalactosaminuronic acid 69-75 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 87-96 20735851-7 2010 Ectopic expression of GalNAc-T2 is sufficient to "arm" tobacco cells with the ability to perform GalNAc-glycosylation, as evidenced by the attachment of GalNAc to Thr-119 of the endogenous enzyme endochitinase. N-acetylgalactosaminuronic acid 97-103 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 22-31 17215257-4 2007 Here, we report the direct carbohydrate binding of two GalNAc-transferase lectin domains, GalNAc-T4 and GalNAc-T2, representing isoforms reported to have distinct glycopeptide activity (GalNAc-T4) and isoforms without apparent distinct GalNAc-glycopeptide specificity (GalNAc-T2). N-acetylgalactosaminuronic acid 55-61 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 104-113 17215257-4 2007 Here, we report the direct carbohydrate binding of two GalNAc-transferase lectin domains, GalNAc-T4 and GalNAc-T2, representing isoforms reported to have distinct glycopeptide activity (GalNAc-T4) and isoforms without apparent distinct GalNAc-glycopeptide specificity (GalNAc-T2). N-acetylgalactosaminuronic acid 55-61 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 269-278 35373202-7 2022 Our studies also show local conformational changes in the peptide backbone during incorporation of GalNAc residues, which might explain GalNAc-T2/T3/T4 fine specificities toward the MUC1 substrate. N-acetylgalactosaminuronic acid 99-105 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 136-145 12507512-2 2003 This type II membrane protein contains all motifs that are conserved in the pp-GalNAc-T family proteins and forms a subfamily with pp-GalNAc-T2 on the phylogenetic tree. N-acetylgalactosaminuronic acid 79-85 polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens 134-143