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Showing Protein Sulfotransferase 1A1 (HMDBP00341)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 5 metabolites
Identification
HMDB Protein ID HMDBP00341
Secondary Accession Numbers
  • 5577
Name Sulfotransferase 1A1
Synonyms
  1. Aryl sulfotransferase 1
  2. HAST1/HAST2
  3. P-PST 1
  4. Phenol sulfotransferase 1
  5. Phenol-sulfating phenol sulfotransferase 1
  6. ST1A1
  7. ST1A3
  8. Thermostable phenol sulfotransferase
  9. Ts-PST
Gene Name SULT1A1
Protein Type Enzyme
Biological Properties
General Function Involved in sulfotransferase activity
Specific Function Sulfotransferase 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.
Pathways
  • Acetaminophen Metabolism Pathway
  • Chemical carcinogenesis - DNA adducts
  • Lamivudine Metabolism Pathway
  • Sulfite oxidase deficiency
  • Sulfur metabolism
  • Sulfur metabolism
  • Tamoxifen Action Pathway
  • Tamoxifen Metabolism Pathway
Reactions
Phosphoadenosine phosphosulfate + a phenol → Adenosine 3',5'-diphosphate + an aryl sulfate details
Phosphoadenosine phosphosulfate + Phenol → Adenosine 3',5'-diphosphate + Phenol sulphate details
GO Classification
Biological Process
estrogen metabolic process
flavonoid metabolic process
sulfation
xenobiotic metabolic process
3'-phosphoadenosine 5'-phosphosulfate metabolic process
amine metabolic process
catecholamine metabolic process
Cellular Component
cytosol
Function
catalytic activity
transferase activity
transferase activity, transferring sulfur-containing groups
sulfotransferase activity
Molecular Function
aryl sulfotransferase activity
flavonol 3-sulfotransferase activity
steroid sulfotransferase activity
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 16
Locus 16p12.1
SNPs SULT1A1
Gene Sequence 
>888 bp
ATGGAGCTGATCCAGGACACCTCCCGCCCGCCACTGGAGTACGTGAAGGGGGTCCCGCTC
ATCAAGTACTTTGCAGAGGCACTGGGGCCCCTGCAGAGCTTCCAGGCCCGGCCTGATGAC
CTGCTCATCAGCACCTACCCCAAGTCCGGCACCACCTGGGTGAGCCAGATTCTGGACATG
ATCTACCAGGGTGGTGACCTGGAGAAGTGTCACCGAGCTCCCATCTTCATGCGGGTGCCC
TTCCTTGAGTTCAAAGCCCCAGGGATTCCCTCAGGGATGGAGACTCTGAAAGACACACCG
GCCCCACGACTCCTGAAGACACACCTGCCCCTGGCTCTGCTCCCCCAGACTCTGTTGGAT
CAGAAGGTCAAGGTGGTCTATGTTGCCCGCAACGCAAAGGATGTGGCAGTTTCCTACTAC
CACTTCTACCACATGGCCAAGGTGCACCCTGAGCCTGGGACCTGGGACAGCTTCCTGGAG
AAGTTCATGGTCGGAGAAGTGTCCTACGGATCCTGGTACCAGCACGTGCAGGAGTGGTGG
GAGCTGAGCCGCACCCACCCTGTTCTCTACCTCTTCTATGAAGACATGAAGGAGAACCCC
AAAAGGGAGATTCAAAAGATCCTGGAGTTTGTGGGGCACTCCCTGCCAGAGGAGACCGTG
GACTTCATGGTTCAGCACACGTCGTTCAAGGAGATGAAGAAGAACCCTATGACCAACTAC
ACCACCGTCCCCCAGGAGTTCATGGACCACAGCATCTCCCCCTTCATGAGGAAAGGCATG
GCTGGGGACTGGAAGACCACCTTCACCGTGGCGCAGAATGAGCGCTTCGATGCGGACTAT
GCGGAGAAGATGGCAGGCTGCAGCCTCAGCTTCCGCTCTGAGCTGTGA
Protein Properties
Number of Residues 295
Molecular Weight 34165.13
Theoretical pI 6.624
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Sulfotransferase 1A1
MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDM
IYQGGDLEKCHRAPIFMRVPFLEFKAPGIPSGMETLKDTPAPRLLKTHLPLALLPQTLLD
QKVKVVYVARNAKDVAVSYYHFYHMAKVHPEPGTWDSFLEKFMVGEVSYGSWYQHVQEWW
ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDFMVQHTSFKEMKKNPMTNY
TTVPQEFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL
GenBank ID Protein 21104442
UniProtKB/Swiss-Prot ID P50225
UniProtKB/Swiss-Prot Entry Name ST1A1_HUMAN
PDB IDs
GenBank Gene ID AB062428
GeneCard ID SULT1A1
GenAtlas ID SULT1A1
HGNC ID HGNC:11453
References
General References
  1. 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. [PubMed:15489334 ]
  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. [PubMed:8484775 ]
  3. 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. [PubMed:8363592 ]
  4. 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. [PubMed:7864863 ]
  5. 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. [PubMed:8423770 ]
  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. [PubMed: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. [PubMed:7581483 ]
  8. Yamazoe Y, Nagata K, Ozawa S, Kato R: Structural similarity and diversity of sulfotransferases. Chem Biol Interact. 1994 Jun;92(1-3):107-17. [PubMed:8033246 ]
  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. [PubMed:8924211 ]
  10. 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. [PubMed:8912648 ]
  11. 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. [PubMed:9855620 ]
  12. 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. [PubMed:8288252 ]
  13. 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. [PubMed:8093002 ]
  14. 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. [PubMed:8033270 ]
  15. Raftogianis RB, Wood TC, Otterness DM, Van Loon JA, Weinshilboum RM: Phenol sulfotransferase pharmacogenetics in humans: association of common SULT1A1 alleles with TS PST phenotype. Biochem Biophys Res Commun. 1997 Oct 9;239(1):298-304. [PubMed:9345314 ]
  16. 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. [PubMed:10762004 ]
  17. Gamage NU, Duggleby RG, Barnett AC, Tresillian M, Latham CF, Liyou NE, McManus ME, Martin JL: Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition. J Biol Chem. 2003 Feb 28;278(9):7655-62. Epub 2002 Dec 5. [PubMed:12471039 ]