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
- Functionsbile-salt sulfotransferase activity / sulfotransferase activityProcesses3'-phosphoadenosine 5'-phosphosulfate metabolic process / bile acid catabolic process / cellular lipid metabolic process / digestion / small molecule metabolic process / steroid metabolic process / sulfation / xenobiotic metabolic processComponentscytoplasm / 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
- Sulfotransfer_1 (PF00685)
- 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
Resource Link UniProtKB ID Q06520 UniProtKB Entry Name ST2A1_HUMAN GenBank Protein ID 306702 GenBank Gene ID L20000 GenAtlas ID SULT2A1 HGNC ID HGNC:11458 - General References
- Comer KA, Falany JL, Falany CN: Cloning and expression of human liver dehydroepiandrosterone sulphotransferase. Biochem J. 1993 Jan 1;289 ( Pt 1):233-40. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- Pedersen LC, Petrotchenko EV, Negishi M: Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase. FEBS Lett. 2000 Jun 9;475(1):61-4. [Article]
- 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. [Article]
- 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. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01812 Adenosine 3',5'-diphosphate experimental unknown Details DB02854 Aetiocholanolone experimental unknown Details DB04445 Mercuric iodide experimental unknown Details DB05812 Abiraterone approved unknown substrate Details DB09073 Palbociclib approved, investigational no substrate Details DB09288 Propacetamol experimental no substrate Details DB00675 Tamoxifen approved unknown substrate Details DB01708 Prasterone approved, investigational, nutraceutical unknown substrate Details DB00871 Terbutaline approved unknown substrate Details DB00960 Pindolol approved, investigational unknown substrate Details DB00968 Methyldopa approved no substrate Details DB12471 Ibrexafungerp approved, investigational unknown substrate Details DB00867 Ritodrine approved, investigational no substrate Details DB12243 Edaravone approved, investigational no substrate Details