Sulfotransferase 1A2

Details

Name
Sulfotransferase 1A2
Synonyms
  • 2.8.2.1
  • Aryl sulfotransferase 2
  • P-PST 2
  • Phenol sulfotransferase 2
  • Phenol-sulfating phenol sulfotransferase 2
  • ST1A2
  • STP2
Gene Name
SULT1A2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0052028|Sulfotransferase 1A2
MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDM
IYQGGDLEKCHRAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLD
QKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWW
ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFKEMKKNPMTNY
TTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAKKMAGCSLSFRSEL
Number of residues
295
Molecular Weight
34309.49
Theoretical pI
Not Available
GO Classification
Functions
aryl sulfotransferase activity / flavonol 3-sulfotransferase activity / sulfotransferase activity
Processes
3'-phosphoadenosine 5'-phosphosulfate metabolic process / amine biosynthetic process / catecholamine metabolic process / ethanol catabolic process / phenol-containing compound metabolic process / steroid metabolic process / sulfation / xenobiotic metabolic process
Components
cytosol
General Function
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Is also responsible for the sulfonation and activation of minoxidil. Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.
Specific Function
Aryl sulfotransferase activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0052029|Sulfotransferase 1A2 (SULT1A2)
ATGGAGCTGATCCAGGACATCTCTCGCCCGCCACTGGAGTACGTGAAGGGGGTCCCGCTC
ATCAAGTACTTTGCAGAGGCACTGGGGCCCCTGCAGAGCTTCCAGGCCCGGCCTGATGAC
CTGCTCATCAGCACCTACCCCAAGTCCGGCACCACCTGGGTGAGCCAGATTCTGGACATG
ATCTACCAGGGCGGTGACCTGGAAAAGTGTCACCGAGCTCCCATCTTCATGCGGGTGCCC
TTCCTTGAGTTCAAAGTCCCAGGGATTCCCTCAGGGATGGAGACTCTGAAAAACACACCA
GCCCCACGACTCCTGAAGACACACCTGCCCCTGGCTCTGCTCCCCCAGACTCTGTTGGAT
CAGAAGGTCAAGGTGGTCTATGTTGCCCGCAACGCAAAGGATGTGGCGGTTTCCTACTAC
CACTTCTACCACATGGCCAAAGTGTACCCTCACCCTGGGACCTGGGAAAGCTTCCTGGAG
AAGTTCATGGCTGGAGAAGTGTCCTATGGGTCCTGGTACCAGCACGTGCAAGAGTGGTGG
GAGCTGAGCCGCACCCACCCTGTTCTCTACCTCTTCTATGAAGACATGAAGGAGAACCCC
AAAAGGGAGATTCAAAAGATCCTGGAGTTTGTGGGGCGCTCCCTGCCAGAGGAGACTGTG
GACCTCATGGTTGAGCACACGTCGTTCAAGGAGATGAAGAAGAACCCTATGACCAACTAC
ACCACCGTCCGCCGGGAGTTCATGGACCACAGCATCTCCCCCTTCATGAGGAAAGGCATG
GCTGGGGACTGGAAGACCACCTTCACCGTGGCGCAGAATGAGCGCTTCGATGCGGACTAT
GCGAAGAAGATGGCAGGCTGCAGCCTCAGCTTCCGCTCTGAGCTGTGA
Chromosome Location
16
Locus
16p11.2
External Identifiers
ResourceLink
UniProtKB IDP50226
UniProtKB Entry NameST1A2_HUMAN
HGNC IDHGNC:11454
General References
  1. Zhu X, Veronese ME, Iocco P, McManus ME: cDNA cloning and expression of a new form of human aryl sulfotransferase. Int J Biochem Cell Biol. 1996 May;28(5):565-71. [Article]
  2. Ozawa S, Nagata K, Shimada M, Ueda M, Tsuzuki T, Yamazoe Y, Kato R: Primary structures and properties of two related forms of aryl sulfotransferases in human liver. Pharmacogenetics. 1995;5 Spec No:S135-40. [Article]
  3. Yamazoe Y, Nagata K, Ozawa S, Kato R: Structural similarity and diversity of sulfotransferases. Chem Biol Interact. 1994 Jun;92(1-3):107-17. [Article]
  4. Her C, Raftogianis R, Weinshilboum RM: Human phenol sulfotransferase STP2 gene: molecular cloning, structural characterization, and chromosomal localization. Genomics. 1996 May 1;33(3):409-20. [Article]
  5. Dooley TP, Huang Z: Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16. Biochem Biophys Res Commun. 1996 Nov 1;228(1):134-40. [Article]
  6. Gaedigk A, Beatty BG, Grant DM: Cloning, structural organization, and chromosomal mapping of the human phenol sulfotransferase STP2 gene. Genomics. 1997 Mar 1;40(2):242-6. [Article]
  7. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [Article]
  8. 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]
  9. Yamazoe Y, Ozawa S, Nagata K, Gong DW, Kato R: Characterization and expression of hepatic sulfotransferase involved in the metabolism of N-substituted aryl compounds. Environ Health Perspect. 1994 Oct;102 Suppl 6:99-103. [Article]
  10. Lu J, Li H, Zhang J, Li M, Liu MY, An X, Liu MC, Chang W: Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate inhibition and the role of Tyr149 in SULT1A2. Biochem Biophys Res Commun. 2010 May 28;396(2):429-34. doi: 10.1016/j.bbrc.2010.04.109. Epub 2010 Apr 22. [Article]
  11. Engelke CE, Meinl W, Boeing H, Glatt H: Association between functional genetic polymorphisms of human sulfotransferases 1A1 and 1A2. Pharmacogenetics. 2000 Mar;10(2):163-9. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB09100Thyroid, porcineapprovedunknownsubstrateDetails
DB00714Apomorphineapproved, investigationalunknownsubstrateDetails
DB00871TerbutalineapprovedunknownsubstrateDetails
DB00960Pindololapproved, investigationalunknownsubstrateDetails
DB00968MethyldopaapprovednosubstrateDetails
DB12471Ibrexafungerpapproved, investigationalunknownsubstrateDetails