GALNT2

GALNT2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2FFU, 2FFV, 4D0T, 4D0Z, 4D11, 5AJN, 5AJO, 5AJP, 5FV9
Identifiers
Aliases	GALNT2 , GalNAc-T2, polypeptide N-acetylgalactosaminyltransferase 2, CDG2T
External IDs	OMIM: 602274 MGI: 894694 HomoloGene: 3297 GeneCards: GALNT2
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1q42.13 Start 230,057,990 bp [1] End 230,282,122 bp [1]
Gene location (Mouse) Chr. Chromosome 8 (mouse) [2] Band 8|8 E2 Start 124,958,130 bp [2] End 125,072,463 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ascending aorta gastric mucosa right coronary artery stromal cell of endometrium body of pancreas palpebral conjunctiva right lobe of liver left coronary artery left adrenal gland saphenous vein Top expressed in mirror yolk sac pancreas stomach islet of Langerhans proximal tubule neural tube mesencephalon skeletal muscle tissue quadriceps femoris muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity manganese ion binding glycosyltransferase activity metal ion binding protein binding carbohydrate binding polypeptide N-acetylgalactosaminyltransferase activity Cellular component integral component of membrane integral component of Golgi membrane Golgi apparatus membrane Golgi membrane extracellular region Golgi cisterna membrane perinuclear region of cytoplasm Golgi stack extracellular exosome endoplasmic reticulum membrane Biological process protein O-linked glycosylation via serine protein glycosylation protein O-linked glycosylation via threonine O-glycan processing protein O-linked glycosylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2590 108148 Ensembl ENSG00000143641 ENSMUSG00000089704 UniProt Q10471 Q6PB93 RefSeq (mRNA) NM_001291866 NM_004481 NM_139272 RefSeq (protein) NP_001278795 NP_004472 NP_644678 Location (UCSC) Chr 1: 230.06 – 230.28 Mb Chr 8: 124.96 – 125.07 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Polypeptide N-acetylgalactosaminyltransferase 2 is an enzyme that in humans is encoded by the GALNT2 gene. ^{[5] [6] [7]}

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. ^[8] Individual GalNAc-transferases have distinct activities, and initiation of O-glycosylation in a cell is regulated by a repertoire of GalNAc-transferases. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000143641 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000089704 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Bennett EP, Weghuis DO, Merkx G, van Kessel AG, Eiberg H, Clausen H (Jul 1998). "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family". Glycobiology. 8 (6): 547–55. doi: 10.1093/glycob/8.6.547 . PMID   9592121.
6. White T, Bennett EP, Takio K, Sorensen T, Bonding N, Clausen H (Dec 1995). "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase". J Biol Chem. 270 (41): 24156–65. doi: 10.1074/jbc.270.41.24156 . PMID   7592619.
7. "Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)".
8. Netherton, Christopher L.; McCrossan, Mari-Clare; Denyer, Michael; Ponnambalam, Sreenivasan; Armstrong, John; Takamatsu, Haru-Hisa; Wileman, Thomas E. (November 2006). "African Swine Fever Virus Causes Microtubule-Dependent Dispersal of trans-Golgi Network" (PDF). Journal of Virology. 80 (22): 11385–11392. doi:10.1128/JVI.00439-06. PMC   1642160 . PMID   16956944.

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. doi:10.1242/jcs.111.1.45. 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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . 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. 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.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi: 10.1038/nature04727 . PMID   16710414.