Bile salt sulfotransferase

Details

Name
Bile salt sulfotransferase
Synonyms
  • 2.8.2.14
  • Dehydroepiandrosterone sulfotransferase
  • DHEA-ST
  • HST
  • Hydroxysteroid Sulfotransferase
  • ST2
  • ST2A1
  • ST2A3
  • STD
  • Sulfotransferase 2A1
Gene Name
SULT2A1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0010624|Bile salt sulfotransferase
MSDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYPKSGTNWLAEILCLMHSK
GDAKWIQSVPIWERSPWVESEIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLM
RNPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFL
LLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVV
DKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRELFPWE
Number of residues
285
Molecular Weight
33779.57
Theoretical pI
5.76
GO Classification
Functions
bile-salt sulfotransferase activity / sulfotransferase activity
Processes
3'-phosphoadenosine 5'-phosphosulfate metabolic process / bile acid catabolic process / cellular lipid metabolic process / digestion / small molecule metabolic process / steroid metabolic process / sulfation / xenobiotic metabolic process
Components
cytoplasm / cytosol
General Function
Sulfotransferase activity
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0010625|Bile salt sulfotransferase (SULT2A1)
ATGTCGGACGATTTCTTATGGTTTGAAGGCATAGCTTTCCCTACTATGGGTTTCAGATCC
GAAACCTTAAGAAAAGTACGTGATGAGTTCGTGATAAGGGATGAAGATGTAATAATATTG
ACTTACCCCAAATCAGGAACAAACTGGTTGGCTGAGATTCTCTGCCTGATGCACTCCAAG
GGGGATGCCAAGTGGATCCAATCTGTGCCCATCTGGGAGCGATCACCCTGGGTAGAGAGT
GAGATTGGGTATACAGCACTCAGTGAAACGGAGAGTCCACGTTTATTCTCCTCCCACCTC
CCCATCCAGTTATTCCCCAAGTCTTTCTTCAGTTCCAAGGCCAAGGTGATTTATCTCATG
AGAAATCCCAGAGATGTTTTGGTGTCTGGTTATTTTTTCTGGAAAAACATGAAGTTTATT
AAGAAACCAAAGTCATGGGAAGAATATTTTGAATGGTTTTGTCAAGGAACTGTGCTATAT
GGGTCATGGTTTGACCACATTCATGGCTGGATGCCCATGAGAGAGGAGAAAAACTTCCTG
TTACTGAGTTATGAGGAGCTGAAACAGGACACAGGAAGAACCATAGAGAAGATCTGTCAA
TTCCTGGGAAAGACGTTAGAACCCGAAGAACTGAACTTAATTCTCAAGAACAGCTCCTTT
CAGAGCATGAAAGAAAACAAGATGTCCAATTATTCCCTCCTGAGTGTTGATTATGTAGTG
GACAAAGCACAACTTCTGAGAAAAGGTGTATCTGGGGACTGGAAAAATCACTTCACAGTG
GCCCAAGCTGAAGACTTTGATAAATTGTTCCAAGAGAAGATGGCAGATCTTCCTCGAGAG
CTGTTCCCATGGGAATAA
Chromosome Location
19
Locus
19q13.3
External Identifiers
ResourceLink
UniProtKB IDQ06520
UniProtKB Entry NameST2A1_HUMAN
GenBank Protein ID306702
GenBank Gene IDL20000
GenAtlas IDSULT2A1
HGNC IDHGNC:11458
General References
  1. Comer KA, Falany JL, Falany CN: Cloning and expression of human liver dehydroepiandrosterone sulphotransferase. Biochem J. 1993 Jan 1;289 ( Pt 1):233-40. [PubMed:7678732]
  2. Otterness DM, Wieben ED, Wood TC, Watson WG, Madden BJ, McCormick DJ, Weinshilboum RM: Human liver dehydroepiandrosterone sulfotransferase: molecular cloning and expression of cDNA. Mol Pharmacol. 1992 May;41(5):865-72. [PubMed:1588921]
  3. Forbes KJ, Hagen M, Glatt H, Hume R, Coughtrie MW: Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme. Mol Cell Endocrinol. 1995 Jul;112(1):53-60. [PubMed:7589785]
  4. Luu-The V, Dufort I, Paquet N, Reimnitz G, Labrie F: Structural characterization and expression of the human dehydroepiandrosterone sulfotransferase gene. DNA Cell Biol. 1995 Jun;14(6):511-8. [PubMed:7598806]
  5. Otterness DM, Her C, Aksoy S, Kimura S, Wieben ED, Weinshilboum RM: Human dehydroepiandrosterone sulfotransferase gene: molecular cloning and structural characterization. DNA Cell Biol. 1995 Apr;14(4):331-41. [PubMed:7710689]
  6. Kong AN, Yang L, Ma M, Tao D, Bjornsson TD: Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver. Biochem Biophys Res Commun. 1992 Aug 31;187(1):448-54. [PubMed:1520333]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334]
  8. Radominska A, Comer KA, Zimniak P, Falany J, Iscan M, Falany CN: Human liver steroid sulphotransferase sulphates bile acids. Biochem J. 1990 Dec 15;272(3):597-604. [PubMed:2268288]
  9. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [PubMed:21269460]
  10. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]
  11. Pedersen LC, Petrotchenko EV, Negishi M: Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase. FEBS Lett. 2000 Jun 9;475(1):61-4. [PubMed:10854859]
  12. Rehse PH, Zhou M, Lin SX: Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate. Biochem J. 2002 May 15;364(Pt 1):165-71. [PubMed:11988089]
  13. Chang HJ, Shi R, Rehse P, Lin SX: Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex. J Biol Chem. 2004 Jan 23;279(4):2689-96. Epub 2003 Oct 21. [PubMed:14573603]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01708Prasteroneapproved, investigational, nutraceuticalunknownDetails
DB01812Adenosine-3'-5'-DiphosphateexperimentalunknownDetails
DB02854AetiocholanoloneexperimentalunknownDetails
DB04445Mercuric iodideexperimentalunknownDetails
DB05812AbirateroneapprovedunknownsubstrateDetails
DB09073Palbociclibapproved, investigationalnosubstrateDetails
DB09288PropacetamolexperimentalnosubstrateDetails
DB00675TamoxifenapprovedunknownsubstrateDetails