GALNT2

UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)
PDB rendering based on 2ffu.
Available structures PDB 2FFU, 2FFV
Identifiers
Symbols	GALNT2; GalNAc-T2
External IDs	OMIM: 602274 MGI: 894694 HomoloGene: 3297 GeneCards: GALNT2 Gene
EC number	2.4.1.41
Gene Ontology Molecular function • polypeptide N-acetylgalactosaminyltransferase activity • sugar binding • transferase activity, transferring glycosyl groups • manganese ion binding Cellular component • extracellular region • Golgi apparatus • Golgi apparatus • Golgi stack • membrane • integral to membrane • integral to Golgi membrane • Golgi cisterna membrane • perinuclear region of cytoplasm Biological process • immunoglobulin biosynthetic process • protein O-linked glycosylation via serine • protein O-linked glycosylation via threonine Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2590	108148
Ensembl	ENSG00000143641	ENSMUSG00000089704
UniProt	Q10471	Q3UA32
RefSeq (mRNA)	NM_004481	NM_139272.2
RefSeq (protein)	NP_004472	NP_644678.2
Location (UCSC)	Chr 1: 230.19 – 230.42 Mb	Chr 8: 122.43 – 126.87 Mb
PubMed search	[1]	[2]

Polypeptide N-acetylgalactosaminyltransferase 2 is an enzyme that in humans is encoded by the GALNT2 gene.

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. The localization site of this particular enzyme is preponderantly the trans-Golgi. Individual GalNAc-transferases have distinct activities and initiation of O-glycosylation in a cell is regulated by a repertoire of GalNAc-transferases.

Further reading

• Bennett EP, Hassan H, Clausen H (1996). "cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.". J. Biol. Chem. 271 (29): 17006–12. doi:10.1074/jbc.271.29.17006. PMID 8663203. 
• Wandall HH, Hassan H, Mirgorodskaya E, et al. (1997). "Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3.". J. Biol. Chem. 272 (38): 23503–14. doi:10.1074/jbc.272.38.23503. PMID 9295285. 
• Müller S, Goletz S, Packer N, et al. (1997). "Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo.". J. Biol. Chem. 272 (40): 24780–93. doi:10.1074/jbc.272.40.24780. PMID 9312074. 
• Röttger S, White J, Wandall HH, et al. (1998). "Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus.". J. Cell. Sci. 111 (1): 45–60. PMID 9394011. 
• Mattu TS, Pleass RJ, Willis AC, et al. (1998). "The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions.". J. Biol. Chem. 273 (4): 2260–72. doi:10.1074/jbc.273.4.2260. PMID 9442070. 
• Iwasaki H, Zhang Y, Tachibana K, et al. (2003). "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.". J. Biol. Chem. 278 (8): 5613–21. doi:10.1074/jbc.M211097200. PMID 12438318. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Marcos NT, Cruz A, Silva F, et al. (2003). "Polypeptide GalNAc-transferases, ST6GalNAc-transferase I, and ST3Gal-transferase I expression in gastric carcinoma cell lines". J. Histochem. Cytochem. 51 (6): 761–71. doi:10.1177/002215540305100607. PMID 12754287. 
• Kinarsky L, Suryanarayanan G, Prakash O, et al. (2004). "Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core". Glycobiology 13 (12): 929–39. doi:10.1093/glycob/cwg109. PMID 12925576. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.