GALNT2

From Wikipedia, the free encyclopedia

UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)

PDB rendering based on 2ffu.

Available structures: 2ffu, 2ffv

Identifiers

Symbol(s)

GALNT2; GalNAc-T2

External IDs

OMIM: 602274 MGI: 894694 HomoloGene: 3297

Gene ontology
Molecular Function:	• polypeptide N-acetylgalactosaminyltransferase activity • calcium ion binding • sugar binding • transferase activity, transferring glycosyl groups • manganese ion binding
Cellular Component:	• membrane • integral to membrane
Biological Process:	• protein amino acid O-linked glycosylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004481 (mRNA)
NP_004472 (protein)

NM_139272 (mRNA)
NP_644678 (protein)

Location

Chr 1: 228.27 - 228.48 Mb

Chr 8: 127.12 - 127.23 Mb

Pubmed search

[1]

[2]

UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2), also known as GALNT2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2).

[edit] Further reading

White T, Bennett EP, Takio K, et al. (1995). "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase.". J. Biol. Chem. 270 (41): 24156-65. PMID 7592619.
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. 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. 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. 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 ( Pt 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. PMID 9442070.
Bennett EP, Weghuis DO, Merkx G, et al. (1998). "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.". Glycobiology 8 (6): 547-55. PMID 9592121.
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. PMID 12477932.
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. 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. PMID 15489334.
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.