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Identification
HMDB Protein ID HMDBP00350
Secondary Accession Numbers
  • 5586
  • HMDBP09339
Name Sulfotransferase 1A2
Synonyms
  1. Aryl sulfotransferase 2
  2. P-PST 2
  3. Phenol sulfotransferase 2
  4. Phenol-sulfating phenol sulfotransferase 2
  5. ST1A2
Gene Name SULT1A2
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. 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.
Pathways
  • Chemical carcinogenesis
  • sulfur metabolism
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
phenol-containing compound metabolic process
sulfation
amine biosynthetic process
steroid metabolic process
xenobiotic metabolic process
3'-phosphoadenosine 5'-phosphosulfate 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
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 16
Locus 16p12.1
SNPs SULT1A2
Gene Sequence
>888 bp
ATGGAGCTGATCCAGGACATCTCTCGCCCGCCACTGGAGTACGTGAAGGGGGTCCCGCTC
ATCAAGTACTTTGCAGAGGCACTGGGGCCCCTGCAGAGCTTCCAGGCCCGGCCTGATGAC
CTGCTCATCAGCACCTACCCCAAGTCCGGCACCACCTGGGTGAGCCAGATTCTGGACATG
ATCTACCAGGGCGGTGACCTGGAAAAGTGTCACCGAGCTCCCATCTTCATGCGGGTGCCC
TTCCTTGAGTTCAAAGTCCCAGGGATTCCCTCAGGGATGGAGACTCTGAAAAACACACCA
GCCCCACGACTCCTGAAGACACACCTGCCCCTGGCTCTGCTCCCCCAGACTCTGTTGGAT
CAGAAGGTCAAGGTGGTCTATGTTGCCCGCAACGCAAAGGATGTGGCGGTTTCCTACTAC
CACTTCTACCACATGGCCAAAGTGTACCCTCACCCTGGGACCTGGGAAAGCTTCCTGGAG
AAGTTCATGGCTGGAGAAGTGTCCTATGGGTCCTGGTACCAGCACGTGCAAGAGTGGTGG
GAGCTGAGCCGCACCCACCCTGTTCTCTACCTCTTCTATGAAGACATGAAGGAGAACCCC
AAAAGGGAGATTCAAAAGATCCTGGAGTTTGTGGGGCGCTCCCTGCCAGAGGAGACTGTG
GACCTCATGGTTGAGCACACGTCGTTCAAGGAGATGAAGAAGAACCCTATGACCAACTAC
ACCACCGTCCGCCGGGAGTTCATGGACCACAGCATCTCCCCCTTCATGAGGAAAGGCATG
GCTGGGGACTGGAAGACCACCTTCACCGTGGCGCAGAATGAGCGCTTCGATGCGGACTAT
GCGGAGAAGATGGCAGGCTGCAGCCTCAGCTTCCGCTCTGAGCTGTGA
Protein Properties
Number of Residues 295
Molecular Weight 34310.43
Theoretical pI 7.276
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Sulfotransferase 1A2
MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDM
IYQGGDLEKCHRAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLD
QKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWW
ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFKEMKKNPMTNY
TTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAKKMAGCSLSFRSEL
GenBank ID Protein 4507303
UniProtKB/Swiss-Prot ID P50226
UniProtKB/Swiss-Prot Entry Name ST1A2_HUMAN
PDB IDs
GenBank Gene ID NM_001054.3
GeneCard ID SULT1A2
GenAtlas ID SULT1A2
HGNC ID HGNC:11454
References
General References
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  4. 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 ]
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  6. 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 ]
  7. 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 ]
  8. 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. [PubMed:8697101 ]
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