- GALNT2
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2), also known as GALNT2, is a human
gene .cite web | title = Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2590| accessdate = ]PBB_Summary
section_title =
summary_text = This gene encodes polypeptide N-acetylgalactosaminyltransferase 2, a member of the GalNAc-transferases family. This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. Individual GalNAc-transferases have distinct activities and initiation of O-glycosylation in a cell is regulated by a repertoire of GalNAc-transferases.cite web | title = Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2590| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*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=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=Mattu TS, Pleass RJ, Willis AC, "et al." |title=The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions. |journal=J. Biol. Chem. |volume=273 |issue= 4 |pages= 2260–72 |year= 1998 |pmid= 9442070 |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=Iwasaki H, Zhang Y, Tachibana K, "et al." |title=Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2. |journal=J. Biol. Chem. |volume=278 |issue= 8 |pages= 5613–21 |year= 2003 |pmid= 12438318 |doi= 10.1074/jbc.M211097200
*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=Marcos NT, Cruz A, Silva F, "et al." |title=Polypeptide GalNAc-transferases, ST6GalNAc-transferase I, and ST3Gal-transferase I expression in gastric carcinoma cell lines. |journal=J. Histochem. Cytochem. |volume=51 |issue= 6 |pages= 761–71 |year= 2003 |pmid= 12754287 |doi=
*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=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*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
*cite journal | author=Gregory SG, Barlow KF, McLay KE, "et al." |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727PBB_Controls
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