Sulfotransferase family cytosolic 2B member 1
Details
- Name
- Sulfotransferase family cytosolic 2B member 1
- Synonyms
- 2.8.2.2
- Alcohol sulfotransferase
- HSST2
- Hydroxysteroid sulfotransferase 2
- ST2B1
- Gene Name
- SULT2B1
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0002516|Sulfotransferase family cytosolic 2B member 1 MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRD DDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPR LMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFL KGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSV VAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQ MRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETP HPRPS
- Number of residues
- 365
- Molecular Weight
- 41307.32
- Theoretical pI
- 5.05
- GO Classification
- Functionsalcohol sulfotransferase activity / steroid sulfotransferase activityProcesses3'-phosphoadenosine 5'-phosphosulfate metabolic process / small molecule metabolic process / steroid metabolic process / sulfate assimilation / xenobiotic metabolic processComponentscytoplasm / cytosol / endoplasmic reticulum / extracellular exosome / intracellular membrane-bounded organelle / nucleus
- General Function
- Steroid sulfotransferase activity
- Specific Function
- Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates hydroxysteroids like DHEA. Isoform 1 preferentially sulfonates cholesterol, and isoform 2 avidly sulfonates pregnenolone but not cholesterol.
- Pfam Domain Function
- Sulfotransfer_1 (PF00685)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0010883|Sulfotransferase family cytosolic 2B member 1 (SULT2B1) ATGGCGTCTCCCCCACCTTTCCACAGCCAGAAGTTGCCAGGTGAATACTTCCGGTACAAG GGCGTCCCCTTCCCCGTCGGCCTGTACTCGCTCGAGAGCATCAGCTTGGCGGAGAACACC CAAGATGTGCGGGACGACGACATCTTTATCATCACCTACCCCAAGTCAGGCACGACCTGG ATGATCGAGATCATCTGCTTAATCCTGAAGGAAGGGGATCCATCCTGGATCCGCTCCGTG CCCATCTGGGAGCGGGCACCCTGGTGTGAGACCATTGTGGGTGCCTTCAGCCTCCCGGAC CAGTACAGCCCCCGCCTCATGAGCTCCCATCTTCCCATCCAGATCTTCACCAAGGCCTTC TTCAGCTCCAAGGCCAAGGTGATCTACATGGGCCGCAACCCCCGGGACGTTGTGGTCTCC CTCTATCATTACTCCAAGATCGCCGGGCAGTTAAAGGACCCGGGCACACCCGACCAGTTC CTGAGGGACTTCCTCAAAGGCGAAGTGCAGTTTGGCTCCTGGTTCGACCACATTAAGGGC TGGCTTCGGATGAAGGGCAAAGACAACTTCCTATTTATCACCTACGAGGAGCTGCAGCAG GACTTACAGGGCTCCGTGGAGCGCATCTGTGGGTTCCTGGGCCGTCCGCTGGGCAAGGAG GCACTGGGCTCCGTCGTGGCACACTCAACCTTCAGCGCCATGAAGGCCAACACCATGTCC AACTACACGCTGCTGCCTCCCAGCCTGCTGGACCACCGTCGCGGGGCCTTCCTCCGGAAA GGGGTCTGCGGCGACTGGAAGAACCACTTCACGGTGGCCCAGAGCGAAGCCTTCGATCGT GCCTACCGCAAGCAGATGCGGGGGATGCCGACCTTCCCCTGGGATGAAGACCCGGAGGAG GACGGCAGCCCAGATCCTGAGCCCAGCCCTGAGCCTGAGCCCAAGCCCAGCCTTGAGCCC AACACCAGCCTGGAGCGTGAGCCCAGACCCAACTCCAGCCCCAGCCCCAGCCCCGGCCAG GCCTCTGAGACCCCGCACCCACGACCCTCATAA
- Chromosome Location
- 19
- Locus
- 19q13.3
- External Identifiers
Resource Link UniProtKB ID O00204 UniProtKB Entry Name ST2B1_HUMAN GenBank Protein ID 1923291 GenBank Gene ID U92314 GenAtlas ID SULT2B1 HGNC ID HGNC:11459 - General References
- Her C, Wood TC, Eichler EE, Mohrenweiser HW, Ramagli LS, Siciliano MJ, Weinshilboum RM: Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a single chromosome 19 gene. Genomics. 1998 Nov 1;53(3):284-95. [Article]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [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]
- Fuda H, Lee YC, Shimizu C, Javitt NB, Strott CA: 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. 2002 Sep 27;277(39):36161-6. Epub 2002 Jul 26. [Article]
- He D, Falany CN: Characterization of proline-serine-rich carboxyl terminus in human sulfotransferase 2B1b: immunogenicity, subcellular localization, kinetic properties, and phosphorylation. Drug Metab Dispos. 2006 Oct;34(10):1749-55. Epub 2006 Jul 19. [Article]
- Salman ED, He D, Runge-Morris M, Kocarek TA, Falany CN: Site-directed mutagenesis of human cytosolic sulfotransferase (SULT) 2B1b to phospho-mimetic Ser348Asp results in an isoform with increased catalytic activity. J Steroid Biochem Mol Biol. 2011 Nov;127(3-5):315-23. doi: 10.1016/j.jsbmb.2011.07.010. Epub 2011 Aug 6. [Article]
- Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC: 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. 2003 Nov 7;278(45):44593-9. Epub 2003 Aug 14. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01812 Adenosine 3',5'-diphosphate experimental unknown Details DB02789 Pregnenolone approved, experimental unknown Details DB03309 N-cyclohexyltaurine experimental unknown Details DB01708 Prasterone approved, investigational, nutraceutical unknown substrate Details