Sulfotransferase 1A1

NameSulfotransferase 1A1
Synonyms
  • 2.8.2.1
  • Aryl sulfotransferase 1
  • HAST1/HAST2
  • P-PST 1
  • Phenol sulfotransferase 1
  • Phenol-sulfating phenol sulfotransferase 1
  • ST1A1
  • ST1A3
  • STP
  • STP1
  • Thermostable phenol sulfotransferase
  • Ts-PST
Gene NameSULT1A1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0037102|Sulfotransferase 1A1
MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDM
IYQGGDLEKCHRAPIFMRVPFLEFKAPGIPSGMETLKDTPAPRLLKTHLPLALLPQTLLD
QKVKVVYVARNAKDVAVSYYHFYHMAKVHPEPGTWDSFLEKFMVGEVSYGSWYQHVQEWW
ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDFVVQHTSFKEMKKNPMTNY
TTVPQEFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL
Number of residues295
Molecular Weight34165.13
Theoretical pI6.61
GO Classification
Functions
  • flavonol 3-sulfotransferase activity
  • steroid sulfotransferase activity
  • aryl sulfotransferase activity
  • sulfotransferase activity
Processes
  • sulfation
  • amine metabolic process
  • flavonoid metabolic process
  • catecholamine metabolic process
  • small molecule metabolic process
  • xenobiotic metabolic process
  • estrogen 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. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is 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 ID179042
UniProtKB IDP50225
UniProtKB Entry NameST1A1_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0016255|Sulfotransferase 1A1 (SULT1A1)
ATGGAGCTGATCCAGGACACCTCCCGCCCGCCACTGGAGTACGTGAAGGGGGTCCCGCTC
ATCAAGTACTTTGCAGAGGCACTGGGGCCCCTGCAGAGCTTCCAGGCCCGGCCTGATGAC
CTGCTCATCAGCACCTACCCCAAGTCCGGCACTACCTGGGTAAGCCAGATTCTGGACATG
ATCTACCAGGGTGGTGACCTGGAGAAGTGTCACCGAGCTCCCATCTTCATGCGGGTGCCC
TTCCTTGAGTTCAAAGCCCCAGGGATTCCCTCAGGGATGGAGACTCTGAAAGACACACCG
GCCCCACGACTCCTGAAGACACACCTGCCCCTGGCTCTGCTCCCCCAGACTCTGTTGGAT
CAGAAGGTCAAGGTGGTCTATGTTGCCCGCAACGCAAAGGATGTGGCAGTTTCCTACTAC
CACTTCTACCACATGGCCAAGGTGCACCCTGAGCCTGGGACCTGGGACAGCTTCCTGGAG
AAGTTCATGGTCGGAGAAGTGTCCTACGGATCCTGGTACCAGCACGTGCAGGAGTGGTGG
GAGCTGAGCCGCACCCACCCTGTTCTCTACCTCTTCTATGAAGACATGAAGGAGAACCCG
AAAAGGGAGATTCAAAAGATCCTGGAGTTTGTGGGGCGCTCCCTGCCAGAGGAGACCGTG
GACTTCGTGGTTCAGCACACGTCGTTCAAGGAGATGAAGAAGAACCCTATGACCAACTAC
ACCACCGTCCCCCAGGAGTTCATGGACCACAGCATCTCCCCCTTCATGAGGAAAGGCATG
GCTGGGGACTGGAAGACCACCTTCACCGTGGCGCAGAATGAGCGCTTCGATGCGGACTAT
GCGGAGAAGATGGCAGGCTGCAGCCTCAGCTTCCGCTCTGAGCTGTGA
GenBank Gene IDL10819
GeneCard IDNot Available
GenAtlas IDSULT1A1
HGNC IDHGNC:11453
Chromosome Location16
Locus16p12.1
References
  1. Zhu X, Veronese ME, Bernard CC, Sansom LN, McManus ME: Identification of two human brain aryl sulfotransferase cDNAs. Biochem Biophys Res Commun. 1993 Aug 31;195(1):120-7. 8363592
  2. Zhu X, Veronese ME, Sansom LN, McManus ME: Molecular characterisation of a human aryl sulfotransferase cDNA. Biochem Biophys Res Commun. 1993 Apr 30;192(2):671-6. 8484775
  3. Wilborn TW, Comer KA, Dooley TP, Reardon IM, Heinrikson RL, Falany CN: Sequence analysis and expression of the cDNA for the phenol-sulfating form of human liver phenol sulfotransferase. Mol Pharmacol. 1993 Jan;43(1):70-7. 8423770
  4. 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
  5. Hwang SR, Kohn AB, Hook VY: Molecular cloning of an isoform of phenol sulfotransferase from human brain hippocampus. Biochem Biophys Res Commun. 1995 Feb 15;207(2):701-7. 7864863
  6. Jones AL, Hagen M, Coughtrie MW, Roberts RC, Glatt H: Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form. Biochem Biophys Res Commun. 1995 Mar 17;208(2):855-62. 7695643
  7. 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
  8. 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
  9. Bernier F, Soucy P, Luu-The V: Human phenol sulfotransferase gene contains two alternative promoters: Structure and expression of the gene. DNA Cell Biol. 1996 May;15(5):367-75. 8924211
  10. Dajani R, Hood AM, Coughtrie MW: A single amino acid, glu146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3. Mol Pharmacol. 1998 Dec;54(6):942-8. 9855620
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  13. Dooley TP, Obermoeller RD, Leiter EH, Chapman HD, Falany CN, Deng Z, Siciliano MJ: Mapping of the phenol sulfotransferase gene (STP) to human chromosome 16p12.1-p11.2 and to mouse chromosome 7. Genomics. 1993 Nov;18(2):440-3. 8288252
  14. Veronese ME, Burgess W, Zhu X, McManus ME: Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies. Biochem J. 1994 Sep 1;302 ( Pt 2):497-502. 8093002
  15. Falany CN, Zhuang W, Falany JL: Characterization of expressed human phenol-sulfating phenol sulfotransferase: effect of mutating cys70 on activity and thermostability. Chem Biol Interact. 1994 Jun;92(1-3):57-66. 8033270
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  19. Gamage NU, Tsvetanov S, Duggleby RG, McManus ME, Martin JL: The structure of human SULT1A1 crystallized with estradiol. An insight into active site plasticity and substrate inhibition with multi-ring substrates. J Biol Chem. 2005 Dec 16;280(50):41482-6. Epub 2005 Oct 12. 16221673
  20. 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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