SULT1E1

Protein-coding gene in the species Homo sapiens
SULT1E1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1G3M, 1HY3, 4JVL, 4JVM, 4JVN

Identifiers
AliasesSULT1E1, EST, EST-1, ST1E1, STE, sulfotransferase family 1E member 1
External IDsOMIM: 600043 MGI: 98431 HomoloGene: 101388 GeneCards: SULT1E1
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for SULT1E1
Genomic location for SULT1E1
Band4q13.3Start69,841,212 bp[1]
End69,860,145 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for SULT1E1
Genomic location for SULT1E1
Band5 E1|5 43.56 cMStart87,723,828 bp[2]
End87,739,453 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • human penis

  • right adrenal gland

  • jejunal mucosa

  • skin of abdomen

  • duodenum

  • right lobe of liver

  • vagina

  • right lung

  • minor salivary glands

  • metanephros
Top expressed in
  • olfactory epithelium

  • seminal vesicula

  • subcutaneous adipose tissue

  • spermatocyte

  • submandibular gland

  • white adipose tissue

  • parotid gland

  • seminiferous tubule

  • cumulus cell

  • vas deferens
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • estrone sulfotransferase activity
  • transferase activity
  • sulfotransferase activity
  • steroid binding
  • steroid sulfotransferase activity
  • flavonol 3-sulfotransferase activity
  • protein binding
  • lipid binding
  • aryl sulfotransferase activity
Cellular component
  • cytoplasm
  • cytosol
  • nuclear membrane
Biological process
  • steroid metabolic process
  • positive regulation of fat cell differentiation
  • estrogen metabolic process
  • sulfation
  • ethanol catabolic process
  • estrogen catabolic process
  • 3'-phosphoadenosine 5'-phosphosulfate metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6783

20860

Ensembl

ENSG00000109193

ENSMUSG00000029272

UniProt

P49888

P49891
Q9D566

RefSeq (mRNA)

NM_005420

NM_023135

RefSeq (protein)

NP_005411

NP_075624

Location (UCSC)Chr 4: 69.84 – 69.86 MbChr 5: 87.72 – 87.74 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Estrogen sulfotransferase is an enzyme that in humans is encoded by the SULT1E1 gene.[5][6]

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 a protein that transfers a sulfo moiety to and from estrone, which may control levels of estrogen receptors.[6]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000109193 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029272 – 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. ^ Bernier F, Leblanc G, Labrie F, Luu-The V (Dec 1994). "Structure of human estrogen and aryl sulfotransferase gene. Two mRNA species issued from a single gene". J Biol Chem. 269 (45): 28200–5. doi:10.1016/S0021-9258(18)46914-1. PMID 7961757.
  6. ^ a b "Entrez Gene: SULT1E1 sulfotransferase family 1E, estrogen-preferring, member 1".

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.
  • 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. Bibcode:2000CBI...129..141G. 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.
  • Falany CN, Krasnykh V, Falany JL (1995). "Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase". J. Steroid Biochem. Mol. Biol. 52 (6): 529–39. doi:10.1016/0960-0760(95)00015-R. PMID 7779757. S2CID 1341801.
  • Aksoy IA, Wood TC, Weinshilboum R (1994). "Human liver estrogen sulfotransferase: identification by cDNA cloning and expression". Biochem. Biophys. Res. Commun. 200 (3): 1621–9. doi:10.1006/bbrc.1994.1637. PMID 8185618.
  • Her C, Aksoy IA, Kimura S, et al. (1996). "Human estrogen sulfotransferase gene (STE): cloning, structure, and chromosomal localization". Genomics. 29 (1): 16–23. doi:10.1006/geno.1995.1210. PMID 8530066.
  • Falany JL, Falany CN (1996). "Expression of cytosolic sulfotransferases in normal mammary epithelial cells and breast cancer cell lines". Cancer Res. 56 (7): 1551–5. PMID 8603401.
  • Her C, Szumlanski C, Aksoy IA, Weinshilboum RM (1997). "Human jejunal estrogen sulfotransferase and dehydroepiandrosterone sulfotransferase: immunochemical characterization of individual variation". Drug Metab. Dispos. 24 (12): 1328–35. PMID 8971138.
  • Song WC, Qian Y, Sun X, Negishi M (1997). "Cellular localization and regulation of expression of testicular estrogen sulfotransferase". Endocrinology. 138 (11): 5006–12. doi:10.1210/endo.138.11.5512. PMID 9348232.
  • Rubin GL, Harrold AJ, Mills JA, et al. (1999). "Regulation of sulphotransferase expression in the endometrium during the menstrual cycle, by oral contraceptives and during early pregnancy". Mol. Hum. Reprod. 5 (11): 995–1002. doi:10.1093/molehr/5.11.995. PMID 10541560.
  • Meinl W, Glatt H (2001). "Structure and localization of the human SULT1B1 gene: neighborhood to SULT1E1 and a SULT1D pseudogene". Biochem. Biophys. Res. Commun. 288 (4): 855–62. doi:10.1006/bbrc.2001.5829. PMID 11688987.
  • Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M (2002). "Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction". J. Biol. Chem. 277 (20): 17928–32. doi:10.1074/jbc.M111651200. PMID 11884392.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Shevtsov S, Petrotchenko EV, Pedersen LC, Negishi M (2003). "Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase". Environ. Health Perspect. 111 (7): 884–8. doi:10.1289/ehp.6056. PMC 1241520. PMID 12782487.
  • v
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  • 1g3m: CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE IN COMPLEX WITH IN-ACTIVE COFACTOR PAP AND 3,5,3',5'-TETRACHLORO-BIPHENYL-4,4'-DIOL
    1g3m: CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE IN COMPLEX WITH IN-ACTIVE COFACTOR PAP AND 3,5,3',5'-TETRACHLORO-BIPHENYL-4,4'-DIOL
  • 1hy3: CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE V269E MUTANT IN THE PRESENCE OF PAPS
    1hy3: CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE V269E MUTANT IN THE PRESENCE OF PAPS
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