Sulfotransferase 1A2

NameSulfotransferase 1A2
Synonyms
  • 2.8.2.1
  • Aryl sulfotransferase 2
  • P-PST 2
  • Phenol sulfotransferase 2
  • Phenol-sulfating phenol sulfotransferase 2
  • ST1A2
  • STP2
Gene NameSULT1A2
OrganismHuman
Amino acid sequence
>lcl|BSEQ0013446|Sulfotransferase 1A2
MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDM
IYQGGDLEKCHRAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLD
QKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWW
ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFKEMKKNPMTNY
TTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAKKMAGCSLSFRSEL
Number of residues295
Molecular Weight34309.49
Theoretical pINot Available
GO Classification
Functions
  • flavonol 3-sulfotransferase activity
  • aryl sulfotransferase activity
  • sulfotransferase activity
Processes
  • sulfation
  • phenol-containing compound metabolic process
  • amine biosynthetic process
  • catecholamine metabolic process
  • small molecule metabolic process
  • steroid metabolic process
  • xenobiotic metabolic process
  • 3'-phosphoadenosine 5'-phosphosulfate metabolic process
Components
  • cytosol
General FunctionSulfotransferase activity
Specific FunctionSulfotransferase 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.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDP50226
UniProtKB Entry NameST1A2_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0013447|Sulfotransferase 1A2 (SULT1A2)
ATGGAGCTGATCCAGGACATCTCTCGCCCGCCACTGGAGTACGTGAAGGGGGTCCCGCTC
ATCAAGTACTTTGCAGAGGCACTGGGGCCCCTGCAGAGCTTCCAGGCCCGGCCTGATGAC
CTGCTCATCAGCACCTACCCCAAGTCCGGCACCACCTGGGTGAGCCAGATTCTGGACATG
ATCTACCAGGGCGGTGACCTGGAAAAGTGTCACCGAGCTCCCATCTTCATGCGGGTGCCC
TTCCTTGAGTTCAAAGTCCCAGGGATTCCCTCAGGGATGGAGACTCTGAAAAACACACCA
GCCCCACGACTCCTGAAGACACACCTGCCCCTGGCTCTGCTCCCCCAGACTCTGTTGGAT
CAGAAGGTCAAGGTGGTCTATGTTGCCCGCAACGCAAAGGATGTGGCGGTTTCCTACTAC
CACTTCTACCACATGGCCAAAGTGTACCCTCACCCTGGGACCTGGGAAAGCTTCCTGGAG
AAGTTCATGGCTGGAGAAGTGTCCTATGGGTCCTGGTACCAGCACGTGCAAGAGTGGTGG
GAGCTGAGCCGCACCCACCCTGTTCTCTACCTCTTCTATGAAGACATGAAGGAGAACCCC
AAAAGGGAGATTCAAAAGATCCTGGAGTTTGTGGGGCGCTCCCTGCCAGAGGAGACTGTG
GACCTCATGGTTGAGCACACGTCGTTCAAGGAGATGAAGAAGAACCCTATGACCAACTAC
ACCACCGTCCGCCGGGAGTTCATGGACCACAGCATCTCCCCCTTCATGAGGAAAGGCATG
GCTGGGGACTGGAAGACCACCTTCACCGTGGCGCAGAATGAGCGCTTCGATGCGGACTAT
GCGGAGAAGATGGCAGGCTGCAGCCTCAGCTTCCGCTCTGAGCTGTGA
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:11454
Chromosome Location16
LocusNot Available
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. 8697101
  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. 7581483
  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. 8033246
  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. 8661000
  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. 8912648
  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. 9119390
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  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. 7889867
  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. 20417180
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