SULT2B1

SULT2B1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1Q1Q, 1Q1Z, 1Q20, 1Q22
Identifiers
Aliases	SULT2B1, HSST2, sulfotransferase family 2B member 1, ARCI14
External IDs	OMIM: 604125; MGI: 1926342; HomoloGene: 49487; GeneCards: SULT2B1; OMA:SULT2B1 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19q13.33 Start 48,552,172 bp End 48,599,425 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 B3 Start 45,379,407 bp End 45,434,093 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of abdomen skin of leg gingival epithelium skin of arm mucosa of pharynx oral cavity vulva skin of thigh epithelium of esophagus cervix epithelium Top expressed in lip esophagus jejunum duodenum skin of abdomen skin of external ear intestinal villus ileum skin of back epidermis More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity sulfotransferase activity protein binding alcohol sulfotransferase activity steroid sulfotransferase activity nucleic acid binding cholesterol binding steroid hormone binding Cellular component extracellular exosome endoplasmic reticulum intracellular membrane-bounded organelle nucleus cytoplasm cytosol Biological process steroid metabolic process sulfate assimilation lipid metabolism 3'-phosphoadenosine 5'-phosphosulfate metabolic process cholesterol metabolic process negative regulation of cell population proliferation positive regulation of epidermal cell differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6820 54200 Ensembl ENSG00000088002 ENSMUSG00000003271 UniProt O00204 O35400 RefSeq (mRNA) NM_004605 NM_177973 NM_017465 NM_001360784 RefSeq (protein) NP_004596 NP_814444 NP_086393 NP_001347713 Location (UCSC) Chr 19: 48.55 – 48.6 Mb Chr 7: 45.38 – 45.43 Mb PubMed search
Wikidata
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Sulfotransferase family cytosolic 2B member 1 is an enzyme that in humans is encoded by the SULT2B1 gene.

Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic chemical compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene sulfates dehydroepiandrosterone but not 4-nitrophenol, a typical substrate for the phenol and estrogen sulfotransferase subfamilies. Two alternatively spliced variants that encode different isoforms have been described.

See also

• Steroid sulfotransferase
• Steroidogenic enzyme

Further reading

• Weinshilboum RM, Otterness DM, Aksoy IA, et al. (1997). "Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes". FASEB J. 11 (1): 3–14. doi:10.1096/fasebj.11.1.9034160. PMID 9034160. S2CID 12532583.
• Glatt H, Engelke CE, Pabel U, et al. (2000). "Sulfotransferases: genetics and role in toxicology". Toxicol. Lett. 112–113: 341–8. doi:10.1016/S0378-4274(99)00214-3. PMID 10720750.
• Glatt H (2001). "Sulfotransferases in the bioactivation of xenobiotics". Chem. Biol. Interact. 129 (1–2): 141–70. Bibcode:2000CBI...129..141G. doi:10.1016/S0009-2797(00)00202-7. PMID 11154739.
• Glatt H, Boeing H, Engelke CE, et al. (2001). "Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects". Mutat. Res. 482 (1–2): 27–40. doi:10.1016/S0027-5107(01)00207-X. PMID 11535246.
• Meloche CA, Falany CN (2001). "Expression and characterization of the human 3 beta-hydroxysteroid sulfotransferases (SULT2B1a and SULT2B1b)". J. Steroid Biochem. Mol. Biol. 77 (4–5): 261–9. doi:10.1016/S0960-0760(01)00064-4. PMID 11457664. S2CID 20589491.
• Geese WJ, Raftogianis RB (2001). "Biochemical characterization and tissue distribution of human SULT2B1". Biochem. Biophys. Res. Commun. 288 (1): 280–9. doi:10.1006/bbrc.2001.5746. PMID 11863786.
• Fuda H, Lee YC, Shimizu C, et al. (2002). "Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase". J. Biol. Chem. 277 (39): 36161–6. doi:10.1074/jbc.M207165200. PMID 12145317.
• Pai TG, Sugahara T, Suiko M, et al. (2003). "Differential xenoestrogen-sulfating activities of the human cytosolic sulfotransferases: molecular cloning, expression, and purification of human SULT2B1a and SULT2B1b sulfotransferases". Biochim. Biophys. Acta. 1573 (2): 165–70. doi:10.1016/s0304-4165(02)00416-6. PMID 12399026.
• 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.
• Lee KA, Fuda H, Lee YC, et al. (2004). "Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms". J. Biol. Chem. 278 (45): 44593–9. doi:10.1074/jbc.M308312200. PMID 12923182.
• Yanai H, Javitt NB, Higashi Y, et al. (2004). "Expression of cholesterol sulfotransferase (SULT2B1b) in human platelets". Circulation. 109 (1): 92–6. doi:10.1161/01.CIR.0000108925.95658.8D. PMID 14676143. S2CID 14696645.
• 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.
• He D, Meloche CA, Dumas NA, et al. (2004). "Different subcellular localization of sulphotransferase 2B1b in human placenta and prostate". Biochem. J. 379 (Pt 3): 533–40. doi:10.1042/BJ20031524. PMC 1224114. PMID 14741047.
• Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19". Nature. 428 (6982): 529–35. Bibcode:2004Natur.428..529G. doi:10.1038/nature02399. PMID 15057824.
• Higashi Y, Fuda H, Yanai H, et al. (2004). "Expression of cholesterol sulfotransferase (SULT2B1b) in human skin and primary cultures of human epidermal keratinocytes". J. Invest. Dermatol. 122 (5): 1207–13. doi:10.1111/j.0022-202X.2004.22416.x. PMID 15140224.