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1 to 25 of 25  Show
  1. 1
    "cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase."
    Meurer J.A., Naylor J.M., Baker C.A., Thomsen D.R., Homa F.L., Elhammer A.P.
    J. Biochem. 118:568-574(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
    Category: Sequences.
    Tissue: Salivary gland.
    Source: UniProtKB/Swiss-Prot (reviewed).
  2. 2
    "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase."
    White T., Bennett E.P., Takio K., Soerensen T., Bonding N., Clausen H.
    J. Biol. Chem. 270:24156-24165(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Category: Expression, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  3. 3
    "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Category: Sequences.
    Tissue: PNS.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 50494 other entries.

  4. 4
    "Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene."
    Meurer J.A., Drong R.F., Homa F.L., Slightom J.L., Elhammer A.P.
    Glycobiology 6:231-241(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 512-559 (ISOFORM 1).
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  5. 5
    "Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3."
    Wandall H.H., Hassan H., Mirgorodskaya E., Kristensen A.K., Roepstorff P., Bennett E.P., Nielsen P.A., Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H.
    J. Biol. Chem. 272:23503-23514(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 other entries.

  6. 6
    "Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus."
    Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A., Bennett E.P., Whitehouse C., Berger E.G., Clausen H., Nilsson T.
    J. Cell Sci. 111:45-60(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Category: Subcellular Location.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 other entries.

  7. 7
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 17600 other entries.

  8. 8
    "Nuclear magnetic resonance-based dissection of a glycosyltransferase specificity for the mucin MUC1 tandem repeat."
    Brokx R.D., Revers L., Zhang Q., Yang S., Mal T.K., Ikura M., Gariepy J.
    Biochemistry 42:13817-13825(2003) [PubMed] [Europe PMC] [Abstract]
    Annotation: First simultaneous kinetic description of O-glycosylation events by recombinant UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase I at all putative O-glycosylation sites within human mucin MUC1 containing 5 tandem repeats.Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 4 other entries.

  9. 9
    "Interleukin-4 induces specific pp-GalNAc-T expression and alterations in mucin O-glycosylation in colonic epithelial cells."
    Kanoh A., Takeuchi H., Kato K., Waki M., Usami K., Irimura T.
    Biochim. Biophys. Acta 1780:577-584(2008) [PubMed] [Europe PMC] [Abstract]
    Annotation: The results indicated that IL-4-treated LS174T cells are able to produce mucins with a higher degree of O-glycosylation than untreated counterparts.Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 13 other entries.

  10. 10
    "Association of single nucleotide polymorphisms in glycosylation genes with risk of epithelial ovarian cancer."
    Sellers T.A., Huang Y., Cunningham J., Goode E.L., Sutphen R., Vierkant R.A., Kelemen L.E., Fredericksen Z.S., Liebow M., Pankratz V.S., Hartmann L.C., Myer J., Iversen E.S. Jr., Schildkraut J.M., Phelan C.
    Cancer Epidemiol. Biomarkers Prev. 17:397-404(2008) [PubMed] [Europe PMC] [Abstract]
    Annotation: Observational study of gene-disease association. (HuGE Navigator)Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 4 other entries.

  11. 11
    "Screening for replication of genome-wide SNP associations in sporadic ALS."
    Cronin S., Tomik B., Bradley D.G., Slowik A., Hardiman O.
    Eur. J. Hum. Genet. 17:213-218(2009) [PubMed] [Europe PMC] [Abstract]
    Annotation: Observational study and genome-wide association study of gene-disease association. (HuGE Navigator)Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 64 other entries.

  12. 12
    "Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2."
    Perrine C.L., Ganguli A., Wu P., Bertozzi C.R., Fritz T.A., Raman J., Tabak L.A., Gerken T.A.
    J. Biol. Chem. 284:20387-20397(2009) [PubMed] [Europe PMC] [Abstract]
    Annotation: GalNAc T10 has a large and pronounced glycopeptide preference for Ser/Thr-O-GalNAc only at the +1 position from the acceptor site whereas T1 and T2 have significantly reduced and variable preferences for Ser/Thr-O-GalNAc.Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 10 other entries.

  13. 13
    "Genomic profiling of microRNAs in bladder cancer: miR-129 is associated with poor outcome and promotes cell death in vitro."
    Dyrskjot L., Ostenfeld M.S., Bramsen J.B., Silahtaroglu A.N., Lamy P., Ramanathan R., Fristrup N., Jensen J.L., Andersen C.L., Zieger K., Kauppinen S., Ulhoi B.P., Kjems J., Borre M., Orntoft T.F.
    Cancer Res. 69:4851-4860(2009) [PubMed] [Europe PMC] [Abstract]
    Annotation: A direct link between miR-129 and the two putative targets GALNT1 and SOX4 in bladder cancer.Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 5 other entries.

  14. 14
    "Site directed processing: role of amino acid sequences and glycosylation of acceptor glycopeptides in the assembly of extended mucin type O-glycan core 2."
    Brockhausen I., Dowler T., Paulsen H.
    Biochim. Biophys. Acta 1790:1244-1257(2009) [PubMed] [Europe PMC] [Abstract]
    Annotation: Data show that the sequences and O-glycosylation patterns direct the addition of the first and second sugar residues by ppGalNAc-T and C1GalT which act in a site directed fashion.Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 11 other entries.

  15. 15
    Annotation: the present analysis fails to replicate an earlier reported association of a GALNT1 variant with risk of ovarian cancerImported.
    Source: GeneRIF:2589.

    This publication is mapped to 4 other entries.

  16. 16
    "Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes."
    Gill D.J., Chia J., Senewiratne J., Bard F.
    J. Cell Biol. 189:843-858(2010) [PubMed] [Europe PMC] [Abstract]
    Annotation: Growth factor stimulation regulates O-glycosylation initiation in a Src-dependent fashion by GalNac-T redistribution from golgi to the endoplasmic reticulum.Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 6 other entries.

  17. 17
    "Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferases."
    Gerken T.A., Jamison O., Perrine C.L., Collette J.C., Moinova H., Ravi L., Markowitz S.D., Shen W., Patel H., Tabak L.A.
    J. Biol. Chem. 286:14493-14507(2011) [PubMed] [Europe PMC] [Abstract]
    Annotation: each ppGalNAc T isoform may be uniquely sensitive to peptide sequence and overall charge which together dictates the substrate sites that will be glycosylatedImported.
    Source: GeneRIF:2589.

    This publication is mapped to 6 other entries.

  18. 18
    "Elucidation of the sugar recognition ability of the lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3 by using unnatural glycopeptide substrates."
    Yoshimura Y., Nudelman A.S., Levery S.B., Wandall H.H., Bennett E.P., Hindsgaul O., Clausen H., Nishimura S.
    Glycobiology 22:429-438(2012) [PubMed] [Europe PMC] [Abstract]
    Annotation: Utilizing unnatural glycopeptide substrates for GalNAc-T3 we demonstrated that the GalNAc-specific sugar recognition of the lectin domain regulates further glycosylation.Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 4 other entries.

  19. 19
    "Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family."
    Bennett E.P., Mandel U., Clausen H., Gerken T.A., Fritz T.A., Tabak L.A.
    Glycobiology 22:736-756(2012) [PubMed] [Europe PMC] [Abstract]
    Annotation: The GALNT1 is the glycosyltransferase enzyme family covering a single known glycosidic linkage.Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 6 other entries.

  20. 20
    "ppGalNAc T1 as a potential novel marker for human bladder cancer."
    Ding M.X., Wang H.F., Wang J.S., Zhan H., Zuo Y.G., Yang D.L., Liu J.Y., Wang W., Ke C.X., Yan R.P.
    Asian Pac. J. Cancer Prev. 13:5653-5657(2012) [PubMed] [Europe PMC] [Abstract]
    Annotation: High ppGalNAc T1 expresdsion is associated with bladder cancer.Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 4 other entries.

  21. 21
    "Knockdown of GALNT1 suppresses malignant phenotype of hepatocellular carcinoma by suppressing EGFR signaling."
    Huang M.J., Hu R.H., Chou C.H., Hsu C.L., Liu Y.W., Huang J., Hung J.S., Lai I.R., Juan H.F., Yu S.L., Wu Y.M., Huang M.C.
    Oncotarget 6:5650-5665(2015) [PubMed] [Europe PMC] [Abstract]
    Annotation: Study demonstrates that down-regulation of GALNT1 is sufficient to suppress malignant phenotype of HCC cells by decreasing EGFR signaling.Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 45 other entries.

  22. 22
    "A human interactome in three quantitative dimensions organized by stoichiometries and abundances."
    Hein M.Y., Hubner N.C., Poser I., Cox J., Nagaraj N., Toyoda Y., Gak I.A., Weisswange I., Mansfeld J., Buchholz F., Hyman A.A., Mann M.
    Cell 163:712-723(2015) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:Q10472.

    This publication is mapped to 5384 other entries.

  23. 23
    "GALNT1-Mediated Glycosylation and Activation of Sonic Hedgehog Signaling Maintains the Self-Renewal and Tumor-Initiating Capacity of Bladder Cancer Stem Cells."
    Li C., Du Y., Yang Z., He L., Wang Y., Hao L., Ding M., Yan R., Wang J., Fan Z.
    Cancer Res. 76:1273-1283(2016) [PubMed] [Europe PMC] [Abstract]
    Annotation: appears to be responsive to the inhibition of GALNT1 and SHH signalingImported.
    Source: GeneRIF:2589.

    This publication is mapped to 11 other entries.

  24. 24
    "Down regulation of GALNT3 contributes to endothelial cell injury via activation of p38 MAPK signaling pathway."
    Guo L., Wang L., Li H., Yang X., Yang B., Li M., Huang J., Gu D.
    Atherosclerosis 245:94-100(2016) [PubMed] [Europe PMC] [Abstract]
    Annotation: Expression of GALNT3 was reduced in CAD patients and down regulation of GALNT3 contributed to endothelial injury by promoting apoptosis and up-regulating the expression of MMP-2 and MMP-14 genes via p38 MAPK activation.Imported.
    Source: GeneRIF:2589.

    This publication is mapped to 10 other entries.

  25. 25
    "gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer."
    Dominguez M., Dejgaard K., Fullekrug J., Dahan S., Fazel A., Paccaud J.P., Thomas D.Y., Bergeron J.J., Nilsson T.
    J. Cell Biol. 140:751-765(1998) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:Q10472.

    This publication is cited by 5 and mapped to 13 other entries.

1 to 25 of 25  Show