SULT1A2

Protein-coding gene in the species Homo sapiens
SULT1A2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1Z29

Identifiers
AliasesSULT1A2, HAST4, P-PST, ST1A2, STP2, TSPST2, sulfotransferase family 1A member 2, P-PST 2
External IDsOMIM: 601292; MGI: 102896; HomoloGene: 128920; GeneCards: SULT1A2; OMA:SULT1A2 - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for SULT1A2
Genomic location for SULT1A2
Band16p11.2Start28,591,943 bp[1]
End28,597,050 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for SULT1A2
Genomic location for SULT1A2
Band7 F3|7 69.25 cMStart126,272,037 bp[2]
End126,275,604 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • duodenum

  • mucosa of transverse colon

  • right lobe of liver

  • rectum

  • testicle

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • upper lobe of left lung

  • right lung

  • spleen
Top expressed in
  • left lobe of liver

  • left colon

  • tunica adventitia of aorta

  • stroma of bone marrow

  • white adipose tissue

  • right lung lobe

  • intercostal muscle

  • subcutaneous adipose tissue

  • muscle of thigh

  • brown adipose tissue
More reference expression data
BioGPS
n/a
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
  • sulfation
  • lipid metabolism
  • amine biosynthetic process
  • xenobiotic metabolic process
  • ethanol catabolic process
  • 3'-phosphoadenosine 5'-phosphosulfate metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6799

20887

Ensembl

ENSG00000197165

ENSMUSG00000030711

UniProt

P50226

P52840

RefSeq (mRNA)

NM_001054
NM_177528
NM_001363863

NM_133670

RefSeq (protein)

NP_001045
NP_803564
NP_001350792

n/a

Location (UCSC)Chr 16: 28.59 – 28.6 MbChr 7: 126.27 – 126.28 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Sulfotransferase 1A2 is an enzyme that in humans is encoded by the SULT1A2 gene.[5][6][7]

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.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000197165 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030711 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ 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.
  7. ^ a b "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. doi:10.1096/fasebj.11.1.9034160. PMID 9034160. S2CID 12532583.
  • Windmill KF, Christiansen A, Teusner JT, et al. (1998). "Localisation of aryl sulfotransferase expression in human tissues using hybridisation histochemistry and immunohistochemistry" (PDF). Chem. Biol. Interact. 109 (1–3): 341–6. Bibcode:1998CBI...109..341W. 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. Bibcode:1994CBI....92..107Y. 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.
  • v
  • t
  • e
  • 1cjm: HUMAN SULT1A3 WITH SULFATE BOUND
    1cjm: HUMAN SULT1A3 WITH SULFATE BOUND
  • 1ls6: Human SULT1A1 complexed with PAP and p-Nitrophenol
    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)
    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)
    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
    2a3r: Crystal Structure of Human Sulfotransferase SULT1A3 in Complex with Dopamine and 3-Phosphoadenosine 5-Phosphate
  • 2d06: Human Sult1A1 Complexed With Pap and estradiol
    2d06: Human Sult1A1 Complexed With Pap and estradiol
Stub icon

This article on a gene on human chromosome 16 is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e