GAL3ST2

Galactose-3-O-sulfotransferase 2 is an enzyme that in humans is encoded by the GAL3ST2 gene.[4][5]

GAL3ST2
Identifiers
Aliases	GAL3ST2, GAL3ST-2, GP3ST, galactose-3-O-sulfotransferase 2
External IDs	OMIM: 608237 MGI: 2685834 HomoloGene: 41471 GeneCards: GAL3ST2
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q37.3 Start 241,776,822 bp[1] End 241,804,287 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • sulfotransferase activity • galactosylceramide sulfotransferase activity • GO:0001948 protein binding Cellular component • integral component of membrane • Golgi cisterna membrane • Golgi apparatus • membrane Biological process • glycolipid biosynthetic process • biological process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	64090	381334
Ensembl	ENSG00000154252 ENSG00000276126	n/a
UniProt	Q9H3Q3	Q6XQH0
RefSeq (mRNA)	NM_022134	NM_199366
RefSeq (protein)	NP_071417	NP_001192178
Location (UCSC)	Chr 2: 241.78 – 241.8 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes a member of the galactose-3-O-sulfotransferase protein family. The product of this gene catalyzes sulfonation by transferring a sulfate group to the hydroxyl at C-3 of nonreducing beta-galactosyl residues, and it can act on both type 1 and type 2 (Galbeta 1-3/1-4GlcNAc-R) oligosaccharides with similar efficiencies, and on core 1 glycans. This enzyme has been implicated in tumor metastasis processes. This gene is different from the GAL3ST3 gene located on chromosome 11, which has also been referred to as GAL3ST2 and encodes a related enzyme with distinct tissue distribution and substrate specificities, compared to galactose-3-O-sulfotransferase 2.[5]

References

1. ENSG00000276126 GRCh38: Ensembl release 89: ENSG00000154252, ENSG00000276126 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Honke K, Tsuda M, Koyota S, Wada Y, Iida-Tanaka N, Ishizuka I, Nakayama J, Taniguchi N (Feb 2001). "Molecular cloning and characterization of a human beta-Gal-3'-sulfotransferase that acts on both type 1 and type 2 (Gal beta 1-3/1-4GlcNAc-R) oligosaccharides". J Biol Chem. 276 (1): 267–74. doi:10.1074/jbc.M005666200. PMID 11029462.
5. "Entrez Gene: GAL3ST2 galactose-3-O-sulfotransferase 2".

Further reading

• Venter JC, Adams MD, Myers EW, et al. (2001). "The sequence of the human genome". Science. 291 (5507): 1304–51. doi:10.1126/science.1058040. PMID 11181995.
• Suzuki A, Hiraoka N, Suzuki M, et al. (2001). "Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans". J. Biol. Chem. 276 (26): 24388–95. doi:10.1074/jbc.M103135200. PMID 11323440.
• Seko A, Hara-Kuge S, Yamashita K (2001). "Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1-->3galNAc residue in O-glycans". J. Biol. Chem. 276 (28): 25697–704. doi:10.1074/jbc.M101558200. PMID 11333265.
• Ikeda N, Eguchi H, Nishihara S, et al. (2001). "A remodeling system of the 3'-sulfo-Lewis a and 3'-sulfo-Lewis x epitopes". J. Biol. Chem. 276 (42): 38588–94. doi:10.1074/jbc.M107390200. PMID 11504739.
• Koma M, Miyagawa S, Honke K, et al. (2002). "The possibility of reducing xenoantigen levels with a novel gal 3'-sulfotransferase (GP3ST)". J. Biochem. 131 (4): 517–22. doi:10.1093/oxfordjournals.jbchem.a003129. PMID 11926988.
• Seko A, Nagata K, Yonezawa S, Yamashita K (2003). "Down-regulation of Gal 3-O-sulfotransferase-2 (Gal3ST-2) expression in human colonic non-mucinous adenocarcinoma". Jpn. J. Cancer Res. 93 (5): 507–15. doi:10.1111/j.1349-7006.2002.tb01285.x. PMC 5927024. PMID 12036446.
• 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. PMC 139241. PMID 12477932.
• Chandrasekaran EV, Lakhaman SS, Chawda R, et al. (2004). "Identification of physiologically relevant substrates for cloned Gal: 3-O-sulfotransferases (Gal3STs): distinct high affinity of Gal3ST-2 and LS180 sulfotransferase for the globo H backbone, Gal3ST-3 for N-glycan multiterminal Galbeta1, 4GlcNAcbeta units and 6-sulfoGalbeta1, 4GlcNAcbeta, and Gal3ST-4 for the mucin core-2 trisaccharide". J. Biol. Chem. 279 (11): 10032–41. doi:10.1074/jbc.M311989200. PMID 14701868.
• 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.
• Shi BZ, Hu P, Geng F, et al. (2005). "Gal3ST-2 involved in tumor metastasis process by regulation of adhesion ability to selectins and expression of integrins". Biochem. Biophys. Res. Commun. 332 (4): 934–40. doi:10.1016/j.bbrc.2005.05.040. PMID 15921657.
• Seko A, Sumiya J, Yamashita K (2006). "Porcine, mouse and human galactose 3-O-sulphotransferase-2 enzymes have different substrate specificities; the porcine enzyme requires basic compounds for its catalytic activity". Biochem. J. 391 (Pt 1): 77–85. doi:10.1042/BJ20050362. PMC 1237141. PMID 15926885.