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]
End	230,282,122 bp[1]
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)[2]
End	125,072,463 bp[2]
RNA expression pattern
	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
	; ;
	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
	2590
	108148
	ENSG00000143641
	ENSMUSG00000089704
	Q10471
	Q6PB93
	NM_001291866; NM_004481
	NM_139272
	NP_001278795; NP_004472
	NP_644678
	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

GRCh38: Ensembl release 89: ENSG00000143641 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000089704 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
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.
"Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)".
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.

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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000143641 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid9592121-5] 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.

[pmid7592619-6] 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.

[entrez-7] "Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)".

[trans-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.

GALNT2

References

Further reading