SULT1A2

SULT1A2

Available structures

Human UniProt search: PDBe RCSB

List of PDB id codes
1Z29

Identifiers

SULT1A2, HAST4, P-PST, ST1A2, STP2, TSPST2, sulfotransferase family 1A member 2

External IDs

HomoloGene: 128920 GeneCards: SULT1A2

Gene ontology
Molecular function	• transferase activity • sulfotransferase activity • flavonol 3-sulfotransferase activity • protein binding • aryl sulfotransferase activity
Cellular component	• cytoplasm • cytosol
Biological process	• steroid metabolic process • phenol-containing compound metabolic process • catecholamine metabolic process • 3'-phosphoadenosine 5'-phosphosulfate metabolic process • sulfation • lipid metabolic process • amine biosynthetic process • xenobiotic metabolic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse


6799


n/a


ENSG00000197165


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P50226


n/a

RefSeq (mRNA)


NM_001054 NM_177528


n/a

RefSeq (protein)


NP_001045.1 NP_803564.1


n/a

Location (UCSC)

Chr 16: 28.59 – 28.6 Mb

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PubMed search

^[1]

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View/Edit Human

Sulfotransferase 1A2 is an enzyme that in humans is encoded by the SULT1A2 gene.^[2]^[3]^[4]

Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes one of two phenol sulfotransferases with thermostable enzyme activity. Two alternatively spliced variants that encode the same protein have been described.^[4]

References

↑ "Human PubMed Reference:".
↑ Her C, Raftogianis R, Weinshilboum RM (Sep 1996). "Human phenol sulfotransferase STP2 gene: molecular cloning, structural characterization, and chromosomal localization". Genomics. 33 (3): 409–20. doi:10.1006/geno.1996.0216. PMID 8661000.
↑ Dooley TP, Huang Z (Dec 1996). "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. 228 (1): 134–40. doi:10.1006/bbrc.1996.1628. PMID 8912648.
1 2 "Entrez Gene: SULT1A2 sulfotransferase family, cytosolic, 1A, phenol-preferring, member 2".

Further reading

Weinshilboum RM, Otterness DM, Aksoy IA, et al. (1997). "Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes.". FASEB J. 11 (1): 3–14. PMID 9034160.
Windmill KF, Christiansen A, Teusner JT, et al. (1998). "Localisation of aryl sulfotransferase expression in human tissues using hybridisation histochemistry and immunohistochemistry.". Chem. Biol. Interact. 109 (1–3): 341–6. doi:10.1016/S0009-2797(97)00144-0. PMID 9566757.
Glatt H, Engelke CE, Pabel U, et al. (2000). "Sulfotransferases: genetics and role in toxicology". Toxicol. Lett. 112-113: 341–8. doi:10.1016/S0378-4274(99)00214-3. PMID 10720750.
Glatt H (2001). "Sulfotransferases in the bioactivation of xenobiotics". Chem. Biol. Interact. 129 (1–2): 141–70. doi:10.1016/S0009-2797(00)00202-7. PMID 11154739.
Glatt H, Boeing H, Engelke CE, et al. (2001). "Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects". Mutat. Res. 482 (1–2): 27–40. doi:10.1016/S0027-5107(01)00207-X. PMID 11535246.
Ozawa S, Nagata K, Shimada M, et al. (1995). "Primary structures and properties of two related forms of aryl sulfotransferases in human liver". Pharmacogenetics. 5 Spec No: S135–40. doi:10.1097/00008571-199512001-00015. PMID 7581483.
Yamazoe Y, Ozawa S, Nagata K, et al. (1995). "Characterization and expression of hepatic sulfotransferase involved in the metabolism of N-substituted aryl compounds". Environ. Health Perspect. 102 Suppl 6: 99–103. doi:10.1289/ehp.94102s699. PMC 1566861. PMID 7889867.
Yamazoe Y, Nagata K, Ozawa S, Kato R (1994). "Structural similarity and diversity of sulfotransferases". Chem. Biol. Interact. 92 (1–3): 107–17. doi:10.1016/0009-2797(94)90057-4. PMID 8033246.
Zhu X, Veronese ME, Iocco P, McManus ME (1996). "cDNA cloning and expression of a new form of human aryl sulfotransferase". Int. J. Biochem. Cell Biol. 28 (5): 565–71. doi:10.1016/1357-2725(95)00164-6. PMID 8697101.
Gaedigk A, Beatty BG, Grant DM (1997). "Cloning, structural organization, and chromosomal mapping of the human phenol sulfotransferase STP2 gene". Genomics. 40 (2): 242–6. doi:10.1006/geno.1996.4575. PMID 9119390.
Harris RM, Waring RH, Kirk CJ, Hughes PJ (2000). "Sulfation of "estrogenic" alkylphenols and 17beta-estradiol by human platelet phenol sulfotransferases". J. Biol. Chem. 275 (1): 159–66. doi:10.1074/jbc.275.1.159. PMID 10617600.
Engelke CE, Meinl W, Boeing H, Glatt H (2000). "Association between functional genetic polymorphisms of human sulfotransferases 1A1 and 1A2". Pharmacogenetics. 10 (2): 163–9. doi:10.1097/00008571-200003000-00008. PMID 10762004.
Carlini EJ, Raftogianis RB, Wood TC, et al. (2001). "Sulfation pharmacogenetics: SULT1A1 and SULT1A2 allele frequencies in Caucasian, Chinese and African-American subjects". Pharmacogenetics. 11 (1): 57–68. doi:10.1097/00008571-200102000-00007. PMID 11207031.

PDB gallery

1cjm: HUMAN SULT1A3 WITH SULFATE BOUND

1ls6: Human SULT1A1 complexed with PAP and p-Nitrophenol

1z28: Crystal Structures of SULT1A2 and SULT1A1*3: Implications in the bioactivation of N-hydroxy-2-acetylamino fluorine (OH-AAF)

1z29: Crystal Structures of SULT1A2 and SULT1A1*3: Implications in the bioactivation of N-hydroxy-2-acetylamino fluorine (OH-AAF)

2a3r: Crystal Structure of Human Sulfotransferase SULT1A3 in Complex with Dopamine and 3-Phosphoadenosine 5-Phosphate

2d06: Human Sult1A1 Complexed With Pap and estradiol

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