GALNT1

UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1), also known as GALNT1, is a human gene.cite web | title = Entrez Gene: GALNT1 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2589| accessdate = ]

PBB_Summary
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summary_text = This gene encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. Transcript variants derived from this gene that utilize alternative polyA signals have been described in the literature.cite web | title = Entrez Gene: GALNT1 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2589| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Paulson JC, Colley KJ |title=Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation. |journal=J. Biol. Chem. |volume=264 |issue= 30 |pages= 17615–8 |year= 1989 |pmid= 2681181 |doi=
*cite journal | author=White T, Bennett EP, Takio K, "et al." |title=Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. |journal=J. Biol. Chem. |volume=270 |issue= 41 |pages= 24156–65 |year= 1995 |pmid= 7592619 |doi=
*cite journal | author=Bennett EP, Hassan H, Clausen H |title=cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3. |journal=J. Biol. Chem. |volume=271 |issue= 29 |pages= 17006–12 |year= 1996 |pmid= 8663203 |doi=
*cite journal | author=Meurer JA, Naylor JM, Baker CA, "et al." |title=cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase. |journal=J. Biochem. |volume=118 |issue= 3 |pages= 568–74 |year= 1996 |pmid= 8690719 |doi=
*cite journal | author=Meurer JA, Drong RF, Homa FL, "et al." |title=Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene. |journal=Glycobiology |volume=6 |issue= 2 |pages= 231–41 |year= 1996 |pmid= 8727794 |doi=
*cite journal | author=Takai S, Hinoda Y, Adachi T, "et al." |title=A human UDP-GalNAc: polypeptide, N-acetylgalactosaminyltransferase type 1 gene is located at the chromosomal region 18q12.1. |journal=Hum. Genet. |volume=99 |issue= 3 |pages= 293–4 |year= 1997 |pmid= 9050910 |doi=
*cite journal | author=Wandall HH, Hassan H, Mirgorodskaya E, "et al." |title=Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 23503–14 |year= 1997 |pmid= 9295285 |doi=
*cite journal | author=Müller S, Goletz S, Packer N, "et al." |title=Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo. |journal=J. Biol. Chem. |volume=272 |issue= 40 |pages= 24780–93 |year= 1997 |pmid= 9312074 |doi=
*cite journal | author=Röttger S, White J, Wandall HH, "et al." |title=Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. |journal=J. Cell. Sci. |volume=111 ( Pt 1) |issue= |pages= 45–60 |year= 1998 |pmid= 9394011 |doi=
*cite journal | author=Bennett EP, Weghuis DO, Merkx G, "et al." |title=Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family. |journal=Glycobiology |volume=8 |issue= 6 |pages= 547–55 |year= 1998 |pmid= 9592121 |doi=
*cite journal | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097–108 |year= 1999 |pmid= 9847074 |doi=
*cite journal | author=Tenno M, Toba S, Kézdy FJ, "et al." |title=Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1). |journal=Eur. J. Biochem. |volume=269 |issue= 17 |pages= 4308–16 |year= 2002 |pmid= 12199709 |doi=
*cite journal | author=Tenno M, Saeki A, Kézdy FJ, "et al." |title=The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47088–96 |year= 2003 |pmid= 12364335 |doi= 10.1074/jbc.M207369200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Kinarsky L, Suryanarayanan G, Prakash O, "et al." |title=Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core. |journal=Glycobiology |volume=13 |issue= 12 |pages= 929–39 |year= 2004 |pmid= 12925576 |doi= 10.1093/glycob/cwg109
*cite journal | author=Brokx RD, Revers L, Zhang Q, "et al." |title=Nuclear magnetic resonance-based dissection of a glycosyltransferase specificity for the mucin MUC1 tandem repeat. |journal=Biochemistry |volume=42 |issue= 47 |pages= 13817–25 |year= 2004 |pmid= 14636048 |doi= 10.1021/bi0353070
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504

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