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GALNT2
Identifiers
Aliases	GALNT2, GalNAc-T2, polypeptide N-acetylgalactosaminyltransferase 2, CDG2T
External IDs	OMIM: 602274; MGI: 894694; GeneCards: GALNT2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2FFU, 2FFV, 4D0T, 4D0Z, 4D11, 5AJN, 5AJO, 5AJP, 5FV9
Enzyme activity
Gene location (Human)
Chr.	Chromosome 1 (human)
End	230,282,122 bp
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)
End	125,072,463 bp
RNA expression pattern
	Top expressed in
	Descending thoracic aorta; ; ascending aorta; ; cartilage tissue; ; gastric mucosa; ; right coronary artery; ; stromal cell of endometrium; ; body of pancreas; ; palpebral conjunctiva; ; right lobe of liver; ; left coronary artery;
	Top expressed in
	lens; ; yolk sac; ; pancreas; ; stomach; ; islet of Langerhans; ; proximal tubule; ; neural tube; ; mesencephalon; ; skeletal muscle tissue; ; right kidney;
	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
Databases	NCBI: entry; OMA: entry
	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

1 2 3 GRCh38: Ensembl release 89: ENSG00000143641 – Ensembl, May 2017
1 2 3 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 (July 1998). "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family". Glycobiology. 8 (6): 547–555. doi:10.1093/glycob/8.6.547. PMID 9592121.
↑ White T, Bennett EP, Takio K, Sorensen T, Bonding N, Clausen H (December 1995). "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase". The Journal of Biological Chemistry. 270 (41): 24156–24165. doi:10.1074/jbc.270.41.24156. PMID 7592619.
1 2 "Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)".
↑ Netherton CL, McCrossan MC, Denyer M, Ponnambalam S, Armstrong J, Takamatsu HH, et al. (November 2006). "African Swine Fever Virus Causes Microtubule-Dependent Dispersal of trans-Golgi Network". 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". The Journal of Biological Chemistry. 271 (29): 17006–17012. doi:10.1074/jbc.271.29.17006. PMID 8663203.
Wandall HH, Hassan H, Mirgorodskaya E, Kristensen AK, Roepstorff P, Bennett EP, et al. (September 1997). "Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3". The Journal of Biological Chemistry. 272 (38): 23503–23514. doi:10.1074/jbc.272.38.23503. PMID 9295285.
Müller S, Goletz S, Packer N, Gooley A, Lawson AM, Hanisch FG (October 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". The Journal of Biological Chemistry. 272 (40): 24780–24793. doi:10.1074/jbc.272.40.24780. PMID 9312074.
Röttger S, White J, Wandall HH, Olivo JC, Stark A, Bennett EP, et al. (January 1998). "Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus". Journal of Cell Science. 111 ( Pt 1) (1): 45–60. doi:10.1242/jcs.111.1.45. PMID 9394011.
Mattu TS, Pleass RJ, Willis AC, Kilian M, Wormald MR, Lellouch AC, et al. (January 1998). "The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions". The Journal of Biological Chemistry. 273 (4): 2260–2272. doi:10.1074/jbc.273.4.2260. PMID 9442070.
Iwasaki H, Zhang Y, Tachibana K, Gotoh M, Kikuchi N, Kwon YD, et al. (February 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". The Journal of Biological Chemistry. 278 (8): 5613–5621. doi:10.1074/jbc.M211097200. PMID 12438318.
Marcos NT, Cruz A, Silva F, Almeida R, David L, Mandel U, et al. (June 2003). "Polypeptide GalNAc-transferases, ST6GalNAc-transferase I, and ST3Gal-transferase I expression in gastric carcinoma cell lines". The Journal of Histochemistry and Cytochemistry. 51 (6): 761–771. doi:10.1177/002215540305100607. PMID 12754287. S2CID 16133163.
Kinarsky L, Suryanarayanan G, Prakash O, Paulsen H, Clausen H, Hanisch FG, et al. (December 2003). "Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core". Glycobiology. 13 (12): 929–939. doi:10.1093/glycob/cwg109. PMID 12925576.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000143641 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[Bennett_1998-5] Bennett EP, Weghuis DO, Merkx G, van Kessel AG, Eiberg H, Clausen H (July 1998). "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family". Glycobiology. 8 (6): 547–555. doi:10.1093/glycob/8.6.547. PMID 9592121.

[White_1995-6] White T, Bennett EP, Takio K, Sorensen T, Bonding N, Clausen H (December 1995). "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase". The Journal of Biological Chemistry. 270 (41): 24156–24165. doi:10.1074/jbc.270.41.24156. PMID 7592619.

[entrez-7] 1 2 "Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)".

[trans-8] Netherton CL, McCrossan MC, Denyer M, Ponnambalam S, Armstrong J, Takamatsu HH, et al. (November 2006). "African Swine Fever Virus Causes Microtubule-Dependent Dispersal of trans-Golgi Network". Journal of Virology. 80 (22): 11385–11392. doi:10.1128/JVI.00439-06. PMC 1642160. PMID 16956944.

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// Workers AI · dad joke modeWhat did GALNT2 say to its friend? "Let's bond.

References

Further reading