Hmdb loader
Identification
HMDB Protein ID HMDBP12663
Secondary Accession Numbers None
Name Sulfotransferase 2A1
Synonyms
  1. ST2A1
  2. Bile salt sulfotransferase
  3. Hydroxysteroid sulfotransferase
  4. ST-20
  5. ST
Gene Name SULT2A1
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands (By similarity). Mediates the sulfation of a wide range of steroids and sterols, including pregnenolone, androsterone, DHEA, bile acids, cholesterol and as well many xenobiotics that contain alcohol and phenol functional groups (PubMed:7854148). Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Plays an important role in maintening steroid and lipid homeostasis. Plays a key role in bile acid metabolism (By similarity). In addition, catalyzes the metabolic activation of potent carcinogenic polycyclic arylmethanols (PubMed:7854148).
Pathways
  • Bile secretion
  • Chemical carcinogenesis - DNA adducts
  • Metabolism of xenobiotics by cytochrome P450
Reactions Not Available
GO Classification
Biological Process
response to nutrient levels
cellular response to vitamin D
sulfation
response to activity
thyroid hormone metabolic process
response to insecticide
3'-phosphoadenosine 5'-phosphosulfate metabolic process
steroid metabolic process
cholesterol metabolic process
ethanol catabolic process
aging
xenobiotic metabolic process
drug metabolic process
Cellular Component
cytosol
cytoplasm
Molecular Function
3'-phosphoadenosine 5'-phosphosulfate binding
sulfotransferase activity
steroid sulfotransferase activity
transferase activity
alcohol sulfotransferase activity
bile-salt sulfotransferase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 284
Molecular Weight 33134.355
Theoretical pI 8.403
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P15709
UniProtKB/Swiss-Prot Entry Name ST2A1_RAT
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Gibbs RA, Weinstock GM, Metzker ML, Muzny DM, Sodergren EJ, Scherer S, Scott G, Steffen D, Worley KC, Burch PE, Okwuonu G, Hines S, Lewis L, DeRamo C, Delgado O, Dugan-Rocha S, Miner G, Morgan M, Hawes A, Gill R, Celera, Holt RA, Adams MD, Amanatides PG, Baden-Tillson H, Barnstead M, Chin S, Evans CA, Ferriera S, Fosler C, Glodek A, Gu Z, Jennings D, Kraft CL, Nguyen T, Pfannkoch CM, Sitter C, Sutton GG, Venter JC, Woodage T, Smith D, Lee HM, Gustafson E, Cahill P, Kana A, Doucette-Stamm L, Weinstock K, Fechtel K, Weiss RB, Dunn DM, Green ED, Blakesley RW, Bouffard GG, De Jong PJ, Osoegawa K, Zhu B, Marra M, Schein J, Bosdet I, Fjell C, Jones S, Krzywinski M, Mathewson C, Siddiqui A, Wye N, McPherson J, Zhao S, Fraser CM, Shetty J, Shatsman S, Geer K, Chen Y, Abramzon S, Nierman WC, Havlak PH, Chen R, Durbin KJ, Egan A, Ren Y, Song XZ, Li B, Liu Y, Qin X, Cawley S, Worley KC, Cooney AJ, D'Souza LM, Martin K, Wu JQ, Gonzalez-Garay ML, Jackson AR, Kalafus KJ, McLeod MP, Milosavljevic A, Virk D, Volkov A, Wheeler DA, Zhang Z, Bailey JA, Eichler EE, Tuzun E, Birney E, Mongin E, Ureta-Vidal A, Woodwark C, Zdobnov E, Bork P, Suyama M, Torrents D, Alexandersson M, Trask BJ, Young JM, Huang H, Wang H, Xing H, Daniels S, Gietzen D, Schmidt J, Stevens K, Vitt U, Wingrove J, Camara F, Mar Alba M, Abril JF, Guigo R, Smit A, Dubchak I, Rubin EM, Couronne O, Poliakov A, Hubner N, Ganten D, Goesele C, Hummel O, Kreitler T, Lee YA, Monti J, Schulz H, Zimdahl H, Himmelbauer H, Lehrach H, Jacob HJ, Bromberg S, Gullings-Handley J, Jensen-Seaman MI, Kwitek AE, Lazar J, Pasko D, Tonellato PJ, Twigger S, Ponting CP, Duarte JM, Rice S, Goodstadt L, Beatson SA, Emes RD, Winter EE, Webber C, Brandt P, Nyakatura G, Adetobi M, Chiaromonte F, Elnitski L, Eswara P, Hardison RC, Hou M, Kolbe D, Makova K, Miller W, Nekrutenko A, Riemer C, Schwartz S, Taylor J, Yang S, Zhang Y, Lindpaintner K, Andrews TD, Caccamo M, Clamp M, Clarke L, Curwen V, Durbin R, Eyras E, Searle SM, Cooper GM, Batzoglou S, Brudno M, Sidow A, Stone EA, Venter JC, Payseur BA, Bourque G, Lopez-Otin C, Puente XS, Chakrabarti K, Chatterji S, Dewey C, Pachter L, Bray N, Yap VB, Caspi A, Tesler G, Pevzner PA, Haussler D, Roskin KM, Baertsch R, Clawson H, Furey TS, Hinrichs AS, Karolchik D, Kent WJ, Rosenbloom KR, Trumbower H, Weirauch M, Cooper DN, Stenson PD, Ma B, Brent M, Arumugam M, Shteynberg D, Copley RR, Taylor MS, Riethman H, Mudunuri U, Peterson J, Guyer M, Felsenfeld A, Old S, Mockrin S, Collins F: Genome sequence of the Brown Norway rat yields insights into mammalian evolution. Nature. 2004 Apr 1;428(6982):493-521. doi: 10.1038/nature02426. [PubMed:15057822 ]
  2. Ogura K, Kajita J, Narihata H, Watabe T, Ozawa S, Nagata K, Yamazoe Y, Kato R: Cloning and sequence analysis of a rat liver cDNA encoding hydroxysteroid sulfotransferase. Biochem Biophys Res Commun. 1989 Nov 30;165(1):168-74. doi: 10.1016/0006-291x(89)91050-4. [PubMed:2590219 ]
  3. Watabe T, Ogura K, Satsukawa M, Okuda H, Hiratsuka A: Molecular cloning and functions of rat liver hydroxysteroid sulfotransferases catalysing covalent binding of carcinogenic polycyclic arylmethanols to DNA. Chem Biol Interact. 1994 Jun;92(1-3):87-105. doi: 10.1016/0009-2797(94)90056-6. [PubMed:8033273 ]
  4. Glatt H, Seidel A, Harvey RG, Coughtrie MW: Activation of benzylic alcohols to mutagens by human hepatic sulphotransferases. Mutagenesis. 1994 Nov;9(6):553-7. doi: 10.1093/mutage/9.6.553. [PubMed:7854148 ]