St6 beta-galactoside alpha-2,6-sialyltransferase 2

ST6 beta-galactoside alpha-2,6-sialyltransferase 2 is a protein that in humans is encoded by the ST6GAL2 gene.

ST6GAL2
Identifiers
Aliases	ST6GAL2, SIAT2, ST6GalII, ST6 beta-galactoside alpha-2,6-sialyltransferase 2
External IDs	OMIM: 608472; MGI: 2445190; HomoloGene: 13052; GeneCards: ST6GAL2; OMA:ST6GAL2 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2q12.3 Start 106,801,600 bp End 106,887,108 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right coronary artery ganglionic eminence Descending thoracic aorta ascending aorta left coronary artery germinal epithelium thyroid gland gonad right lobe of thyroid gland left lobe of thyroid gland n/a More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity catalytic activity sialyltransferase activity glycosyltransferase activity beta-galactoside alpha-2,6-sialyltransferase activity Cellular component integral component of membrane Golgi cisterna membrane Golgi apparatus membrane Golgi membrane Biological process multicellular organism development protein glycosylation oligosaccharide metabolic process sialylation protein N-linked glycosylation via asparagine growth carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 84620 240119 Ensembl ENSG00000144057 ENSMUSG00000024172 UniProt Q96JF0 Q76K27 RefSeq (mRNA) NM_001142351 NM_001142352 NM_032528 NM_001322362 NM_172829 RefSeq (protein) NP_001135823 NP_001135824 NP_001309291 NP_115917 NP_001334332 Location (UCSC) Chr 2: 106.8 – 106.89 Mb n/a PubMed search
Wikidata
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Function

This locus encodes a sialyltransferase. The encoded type II transmembrane protein catalyzes the transfer of sialic acid from CMP to an oligosaccharide substrate. Polymorphisms at this locus may be associated with variations in risperidone response in schizophrenic patients. Alternatively spliced transcript variants have been described. [provided by RefSeq, Jan 2012].

Further reading

• Krzewinski-Recchi MA, Julien S, Juliant S, Teintenier-Lelièvre M, Samyn-Petit B, Montiel MD, Mir AM, Cerutti M, Harduin-Lepers A, Delannoy P (March 2003). "Identification and functional expression of a second human beta-galactoside alpha2,6-sialyltransferase, ST6Gal II". Eur. J. Biochem. 270 (5): 950–61. doi:10.1046/j.1432-1033.2003.03458.x. PMID 12603328.
• Trynka G, Zhernakova A, Romanos J, Franke L, Hunt KA, Turner G, Bruinenberg M, Heap GA, Platteel M, Ryan AW, de Kovel C, Holmes GK, Howdle PD, Walters JR, Sanders DS, Mulder CJ, Mearin ML, Verbeek WH, Trimble V, Stevens FM, Kelleher D, Barisani D, Bardella MT, McManus R, van Heel DA, Wijmenga C (August 2009). "Coeliac disease-associated risk variants in TNFAIP3 and REL implicate altered NF-kappaB signalling". Gut. 58 (8): 1078–83. doi:10.1136/gut.2008.169052. PMID 19240061. S2CID 17111427.
• Lehoux S, Groux-Degroote S, Cazet A, Dhaenens CM, Maurage CA, Caillet-Boudin ML, Delannoy P, Krzewinski-Recchi MA (January 2010). "Transcriptional regulation of the human ST6GAL2 gene in cerebral cortex and neuronal cells". Glycoconj. J. 27 (1): 99–114. doi:10.1007/s10719-009-9260-y. PMID 19768537. S2CID 21921351.
• Ikeda M, Tomita Y, Mouri A, Koga M, Okochi T, Yoshimura R, Yamanouchi Y, Kinoshita Y, Hashimoto R, Williams HJ, Takeda M, Nakamura J, Nabeshima T, Owen MJ, O'Donovan MC, Honda H, Arinami T, Ozaki N, Iwata N (February 2010). "Identification of novel candidate genes for treatment response to risperidone and susceptibility for schizophrenia: integrated analysis among pharmacogenomics, mouse expression, and genetic case-control association approaches". Biol. Psychiatry. 67 (3): 263–9. doi:10.1016/j.biopsych.2009.08.030. PMID 19850283. S2CID 25280425.
• Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR (2010). "Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score". Mol. Med. 16 (7–8): 247–53. doi:10.2119/molmed.2009.00159. PMC 2896464. PMID 20379614.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.