SULT1E1

SULT1E1
Identifiers
Aliases	SULT1E1, EST, EST-1, ST1E1, STE, sulfotransferase family 1E member 1
External IDs	OMIM: 600043; MGI: 98431; GeneCards: SULT1E1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1G3M, 1HY3, 4JVL, 4JVM, 4JVN
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 2.8.2.4 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 4 (human) Band 4q13.3 Start 69,841,212 bp End 69,860,145 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5 E1|5 43.56 cM Start 87,723,828 bp End 87,739,453 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in human penis right adrenal gland buccal mucosa cell left adrenal cortex right adrenal cortex skin of leg jejunal mucosa skin of abdomen duodenum olfactory zone of nasal mucosa Top expressed in olfactory epithelium efferent ductule seminal vesicula decidua subcutaneous adipose tissue spermatocyte submandibular gland white adipose tissue parotid gland tunica adventitia of aorta 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 Databases NCBI: entry; OMA: entry Species Human Mouse 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 Mb Chr 5: 87.72 – 87.74 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Estrogen sulfotransferase is an enzyme that in humans is encoded by the SULT1E1 gene.

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.

See also

• Steroidogenic enzyme
• Steroid sulfotransferase
• Estrone sulfotransferase
• Steroid sulfatase

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.