GAL3ST2

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)
End	241,804,287 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	93,804,216 bp
RNA expression pattern
	Top expressed in
	rectum; ; stromal cell of endometrium; ; right uterine tube; ; superior frontal gyrus; ; right lobe of liver; ; appendix; ; gallbladder; ; nucleus accumbens; ; prefrontal cortex; ; dorsolateral prefrontal cortex;
	Top expressed in
	jejunum; ; ileum; ; colon; ; duodenum; ; morula; ; blastocyst; ; spleen; ; thymus; ; ovary; ; islet of Langerhans;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity ; sulfotransferase activity ; galactosylceramide sulfotransferase activity ; 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
	64090
	381334
	ENSG00000154252 ; ENSG00000276126
	ENSMUSG00000094651
	Q9H3Q3
	Q6XQH0
	NM_022134
	NM_199366
	NP_071417
	NP_001192178
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 17, 2023

Galactose-3-O-sulfotransferase 2 is an enzyme that in humans is encoded by the GAL3ST2 gene.^[5]^[6]

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.^[6]

Related Research Articles

The enzyme UDP-glucose 4-epimerase, also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.

Carbohydrate sulfotransferase 6 is an enzyme that in humans is encoded by the CHST6 gene.

Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the GCNT1 gene.

Carbohydrate sulfotransferase 2 is an enzyme that in humans is encoded by the CHST2 gene.

Carbohydrate sulfotransferase 4 is an enzyme that in humans is encoded by the CHST4 gene.

CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase is an enzyme that in humans is encoded by the ST3GAL4 gene.

Galactosylceramide sulfotransferase is an enzyme that in humans is encoded by the GAL3ST1 gene.

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 is an enzyme that in humans is encoded by the B3GNT2 gene.

Carbohydrate sulfotransferase 1 is an enzyme that in humans is encoded by the CHST1 gene.

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 is an enzyme that in humans is encoded by the B3GAT3 gene.

ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, also known as sialyltransferase 3C (SIAT3-C) or sialyltransferase 7D (SIAT7-D) is a sialyltransferase enzyme that in humans is encoded by the ST6GALNAC4 gene.

Beta-1,4-galactosyltransferase 5 is an enzyme that in humans is encoded by the B4GALT5 gene.

Beta-1,3-galactosyltransferase 5 is an enzyme that in humans is encoded by the B3GALT5 gene.

Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 is an enzyme that in humans is encoded by the HS3ST3A1 gene.

Galactose-3-O-sulfotransferase 4 is an enzyme that in humans is encoded by the GAL3ST4 gene.

Heparan sulfate glucosamine 3-O-sulfotransferase 3B1 is an enzyme that in humans is encoded by the HS3ST3B1 gene. Heparan sulfate biosynthetic enzymes are key components in generating myriad distinct heparan sulfate fine structures that carry out multiple biologic activities. The enzyme encoded by this gene is a member of the heparan sulfate biosynthetic enzyme family. It is a type II integral membrane protein and possesses heparan sulfate glucosaminyl 3-O-sulfotransferase activity ( HS3ST3A1). The Sulfotransferase domain of this enzyme is highly similar to the same domain of heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1 and these two enzymes sulfate an identical disaccharide. This gene is widely expressed, with the most abundant expression in liver and placenta.

Galactose-3-O-sulfotransferase 3 is an enzyme that in humans is encoded by the GAL3ST3 gene.

Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3 is an enzyme that in humans is encoded by the NDST3 gene. It catalyses the reaction:

3'-phosphoadenylyl sulfate + α-D-glucosaminyl-[heparan sulfate]_(n) = adenosine 3',5'-bisphosphate + 2 H⁺ + N-sulfo-α-D-glucosaminyl-[heparan sulfate]_(n)

<span class="mw-page-title-main">Carbohydrate sulfotransferase</span>

Carbohydrate sulfotransferases are sulfotransferase enzymes that transfer sulfate to carbohydrate groups in glycoproteins and glycolipids. Carbohydrates are used by cells for a wide range of functions from structural purposes to extracellular communication. Carbohydrates are suitable for such a wide variety of functions due to the diversity in structure generated from monosaccharide composition, glycosidic linkage positions, chain branching, and covalent modification. Possible covalent modifications include acetylation, methylation, phosphorylation, and sulfation. Sulfation, performed by carbohydrate sulfotransferases, generates carbohydrate sulfate esters. These sulfate esters are only located extracellularly, whether through excretion into the extracellular matrix (ECM) or by presentation on the cell surface. As extracellular compounds, sulfated carbohydrates are mediators of intercellular communication, cellular adhesion, and ECM maintenance.

Galactose-3-O-sulfotransferases is a family of several mammalian galactose-3-O-sulfotransferase proteins. Gal-3-O-sulfotransferase is thought to play a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans.

References

1 2 3 ENSG00000276126 GRCh38: Ensembl release 89: ENSG00000154252, ENSG00000276126 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000094651 - 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.
↑ 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.
1 2 "Entrez Gene: GAL3ST2 galactose-3-O-sulfotransferase 2".

Venter JC, Adams MD, Myers EW, et al. (2001). "The sequence of the human genome". Science. 291 (5507): 1304–51. Bibcode:2001Sci...291.1304V. 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. Bibcode:2002PNAS...9916899M. 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.

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[refGRCh38Ensembl-1] 1 2 3 ENSG00000276126 GRCh38: Ensembl release 89: ENSG00000154252, ENSG00000276126 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000094651 - 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.

[pmid11029462-5] 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.

[entrez-6] 1 2 "Entrez Gene: GAL3ST2 galactose-3-O-sulfotransferase 2".

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GAL3ST2

Related Research Articles

References

Further reading