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UniProtKB/Swiss-Prot entry P03372

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ESR1_HUMAN
Primary accession number P03372
Secondary accession numbers Q13511 Q14276 Q9NU51 Q9UDZ7 Q9UIS7
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on June 1, 1994 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 148)
Name and origin of the protein
Protein name Estrogen receptor
Synonyms ER
Estradiol receptor
ER-alpha
Nuclear receptor subfamily 3 group A member 1
Gene name
Name: ESR1
Synonyms: ESR, NR3A1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
DOI=10.1126/science.3753802; PubMed=3753802 [NCBI, ExPASy, EBI, Israel, Japan]
Greene G.L., Gilna P., Waterfield M., Baker A., Hort Y., Shine J.;
"Sequence and expression of human estrogen receptor complementary DNA.";
Science 231:1150-1154(1986).
[2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
DOI=10.1038/320134a0; PubMed=3754034 [NCBI, ExPASy, EBI, Israel, Japan]
Green S., Walter P., Kumar V., Krust A., Bornert J.-M., Argos P., Chambon P.;
"Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A.";
Nature 320:134-139(1986).
[3]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT ASP-411 INS.
TISSUE=Mammary gland;
DOI=10.1093/nar/24.5.962; PubMed=8600466 [NCBI, ExPASy, EBI, Israel, Japan]
Pink J.J., Wu S.Q., Wolf D.M., Bilimoria M.M., Jordan V.C.;
"A novel 80 kDa human estrogen receptor containing a duplication of exons 6 and 7.";
Nucleic Acids Res. 24:962-969(1996).
[4]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-77.
NIEHS SNPs program;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 152-595 (ISOFORM LONG).
DOI=10.1016/S0960-0760(99)00126-0; PubMed=10619354 [NCBI, ExPASy, EBI, Israel, Japan]
Schubert E.L., Lee M.K., Newman B., King M.C.;
"Single nucleotide polymorphisms (SNPs) in the estrogen receptor gene and breast cancer susceptibility.";
J. Steroid Biochem. Mol. Biol. 71:21-27(1999).
[7]
 NUCLEOTIDE SEQUENCE [MRNA] OF 216-434, AND ALTERNATIVE SPLICING.
TISSUE=Mammary carcinoma;
PubMed=7916651 [NCBI, ExPASy, EBI, Israel, Japan]
Pfeffer U., Fecarotta E., Castagnetta L., Vidali G.;
"Estrogen receptor variant messenger RNA lacking exon 4 in estrogen-responsive human breast cancer cell lines.";
Cancer Res. 53:741-743(1993).
[8]
 PROTEIN SEQUENCE OF 110-117, PHOSPHORYLATION, AND MUTAGENESIS.
DOI=10.1210/me.9.8.1041; PubMed=7476978 [NCBI, ExPASy, EBI, Israel, Japan]
Joel P.B., Traish A.M., Lannigan D.A.;
"Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor.";
Mol. Endocrinol. 9:1041-1052(1995).
[9]
 NUCLEOTIDE SEQUENCE [MRNA] OF 354-548.
TISSUE=Mammary carcinoma;
Naundorf H., Becker M., Fiebig C., Buettner B., Fichtner I.;
"Mechanisms of acquired tamoxifen resistance in a xenotransplanted human breast carcinoma.";
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[10]
 PROTEIN SEQUENCE OF 532-542, AND PHOSPHORYLATION.
DOI=10.1210/me.9.1.24; PubMed=7539106 [NCBI, ExPASy, EBI, Israel, Japan]
Arnold S.F., Obourn J.D., Jaffe H., Notides A.C.;
"Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro.";
Mol. Endocrinol. 9:24-33(1995).
[11]
 MUTAGENESIS OF CYS-447.
PubMed=1577818 [NCBI, ExPASy, EBI, Israel, Japan]
Reese J.C., Katzenellenbogen B.S.;
"Characterization of a temperature-sensitive mutation in the hormone binding domain of the human estrogen receptor. Studies in cell extracts and intact cells and their implications for hormone-dependent transcriptional activation.";
J. Biol. Chem. 267:9868-9873(1992).
[12]
 PHOSPHORYLATION.
DOI=10.1210/me.8.9.1208; PubMed=7838153 [NCBI, ExPASy, EBI, Israel, Japan]
Arnold S.F., Obourn J.D., Jaffe H., Notides A.C.;
"Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor.";
Mol. Endocrinol. 8:1208-1214(1994).
[13]
 GLYCOSYLATION.
DOI=10.1074/jbc.272.48.30122; PubMed=8999954 [NCBI, ExPASy, EBI, Israel, Japan]
Jiang M.S., Hart G.W.;
"A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine.";
J. Biol. Chem. 272:2421-2428(1997).
[14]
 INTERACTION WITH AKAP13.
DOI=10.1038/sj.onc.1201783; PubMed=9627117 [NCBI, ExPASy, EBI, Israel, Japan]
Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O., Pagliai K., Gray K., Gutkind S., Segars J.;
"Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action.";
Oncogene 16:2513-2526(1998).
[15]
 PHOSPHORYLATION AT SER-104 AND SER-106, AND MUTAGENESIS.
DOI=10.1074/jbc.274.32.22296; PubMed=10428798 [NCBI, ExPASy, EBI, Israel, Japan]
Rogatsky I., Trowbridge J.M., Garabedian M.J.;
"Potentiation of human estrogen receptor alpha transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin A-CDK2 complex.";
J. Biol. Chem. 274:22296-22302(1999).
[16]
 INTERACTION WITH NCOA6.
DOI=10.1074/jbc.274.48.34283; PubMed=10567404 [NCBI, ExPASy, EBI, Israel, Japan]
Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
"A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo.";
J. Biol. Chem. 274:34283-34293(1999).
[17]
 INTERACTION WITH PHB2.
DOI=10.1073/pnas.96.12.6947; PubMed=10359819 [NCBI, ExPASy, EBI, Israel, Japan]
Montano M.M., Ekena K., Delage-Mourroux R., Chang W., Martini P., Katzenellenbogen B.S.;
"An estrogen receptor-selective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens.";
Proc. Natl. Acad. Sci. U.S.A. 96:6947-6952(1999).
[18]
 INTERACTION WITH PBXIP1.
DOI=10.1074/jbc.M001323200; PubMed=10825160 [NCBI, ExPASy, EBI, Israel, Japan]
Abramovich C., Shen W.-F., Pineault N., Imren S., Montpetit B., Largman C., Humphries R.K.;
"Functional cloning and characterization of a novel nonhomeodomain protein that inhibits the binding of PBX1-HOX complexes to DNA.";
J. Biol. Chem. 275:26172-26177(2000).
[19]
 INTERACTION WITH KDM5A.
DOI=10.1074/jbc.M100313200; PubMed=11358960 [NCBI, ExPASy, EBI, Israel, Japan]
Chan S.W., Hong W.;
"Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone receptor-mediated transcription.";
J. Biol. Chem. 276:28402-28412(2001).
[20]
 INTERACTION WITH NCOA5.
DOI=10.1128/MCB.21.1.343-353.2001; PubMed=11113208 [NCBI, ExPASy, EBI, Israel, Japan]
Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F., Giguere V.;
"CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant.";
Mol. Cell. Biol. 21:343-353(2001).
[21]
 INTERACTION WITH NCOA7.
DOI=10.1128/MCB.22.10.3358-3372.2002; PubMed=11971969 [NCBI, ExPASy, EBI, Israel, Japan]
Shao W., Halachmi S., Brown M.;
"ERAP140, a conserved tissue-specific nuclear receptor coactivator.";
Mol. Cell. Biol. 22:3358-3372(2002).
[22]
 INTERACTION WITH PELP1.
DOI=10.1073/pnas.192569699; PubMed=12415108 [NCBI, ExPASy, EBI, Israel, Japan]
Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
"Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade.";
Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002).
[23]
 INTERACTION WITH SMARD1.
DOI=10.1128/MCB.23.17.6210-6220.2003; PubMed=12917342 [NCBI, ExPASy, EBI, Israel, Japan]
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
"BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation.";
Mol. Cell. Biol. 23:6210-6220(2003).
[24]
 INTERACTION WITH DNTTIP2.
DOI=10.1016/j.bbrc.2004.02.179; PubMed=15047147 [NCBI, ExPASy, EBI, Israel, Japan]
Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M., Zhu Y.-J.;
"ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor.";
Biochem. Biophys. Res. Commun. 317:54-59(2004).
[25]
 INTERACTION WITH TXNRD1.
DOI=10.1074/jbc.M402753200; PubMed=15199063 [NCBI, ExPASy, EBI, Israel, Japan]
Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A., Spyrou G.;
"An alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signaling.";
J. Biol. Chem. 279:38721-38729(2004).
[26]
 INTERACTION WITH HEXIM1.
DOI=10.1038/sj.onc.1208728; PubMed=15940264 [NCBI, ExPASy, EBI, Israel, Japan]
Wittmann B.M., Fujinaga K., Deng H., Ogba N., Montano M.M.;
"The breast cell growth inhibitor, estrogen down regulated gene 1, modulates a novel functional interaction between estrogen receptor alpha and transcriptional elongation factor cyclin T1.";
Oncogene 24:5576-5588(2005).
[27]
 INTERACTION WITH MLL2.
DOI=10.1074/jbc.M513245200; PubMed=16603732 [NCBI, ExPASy, EBI, Israel, Japan]
Mo R., Rao S.M., Zhu Y.-J.;
"Identification of the MLL2 complex as a coactivator for estrogen receptor alpha.";
J. Biol. Chem. 281:15714-15720(2006).
[28]
 INTERACTION WITH MUC1.
DOI=10.1016/j.molcel.2005.11.030; PubMed=16427018 [NCBI, ExPASy, EBI, Israel, Japan]
Wei X., Xu H., Kufe D.;
"MUC1 oncoprotein stabilizes and activates estrogen receptor alpha.";
Mol. Cell 21:295-305(2006).
[29]
 INTERACTION WITH MAP1S.
DOI=10.1016/j.bbrc.2007.06.179; PubMed=17658481 [NCBI, ExPASy, EBI, Israel, Japan]
Eriksson M., Samuelsson H., Samuelsson E.-B., Liu L., McKeehan W.L., Benedikz E., Sundstroem E.;
"The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in the brain.";
Biochem. Biophys. Res. Commun. 361:127-132(2007).
[30]
 INTERACTION WITH CUEDC2.
DOI=10.1038/sj.emboj.7601602; PubMed=17347654 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang P.-J., Zhao J., Li H.-Y., Man J.-H., He K., Zhou T., Pan X., Li A.-L., Gong W.-L., Jin B.-F., Xia Q., Yu M., Shen B.-F., Zhang X.-M.;
"CUE domain containing 2 regulates degradation of progesterone receptor by ubiquitin-proteasome.";
EMBO J. 26:1831-1842(2007).
[31]
 INTERACTION WITH UIMC1.
DOI=10.1093/nar/gkl1112; PubMed=17311814 [NCBI, ExPASy, EBI, Israel, Japan]
Yan J., Kim Y.S., Yang X.-P., Albers M., Koegl M., Jetten A.M.;
"Ubiquitin-interaction motifs of RAP80 are critical in its regulation of estrogen receptor alpha.";
Nucleic Acids Res. 35:1673-1686(2007).
[32]
 INTERACTION WITH ATAD2.
DOI=10.1073/pnas.0705814104; PubMed=17998543 [NCBI, ExPASy, EBI, Israel, Japan]
Zou J.X., Revenko A.S., Li L.B., Gemo A.T., Chen H.-W.;
"ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is required for coregulator occupancy and chromatin modification.";
Proc. Natl. Acad. Sci. U.S.A. 104:18067-18072(2007).
[33]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7 AND SER-10, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[34]
 STRUCTURE BY NMR OF 180-262.
DOI=10.1038/348458a0; PubMed=2247153 [NCBI, ExPASy, EBI, Israel, Japan]
Schwabe J.W.E., Neuhaus D., Rhodes D.;
"Solution structure of the DNA-binding domain of the oestrogen receptor.";
Nature 348:458-461(1990).
[35]
 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 180-262.
DOI=10.1016/0092-8674(93)90390-C; PubMed=8221895 [NCBI, ExPASy, EBI, Israel, Japan]
Schwabe J.W.E., Chapman L., Finch J.T., Rhodes D.;
"The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements.";
Cell 75:567-578(1993).
[36]
 X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 305-548.
DOI=10.1038/39645; PubMed=9338790 [NCBI, ExPASy, EBI, Israel, Japan]
Brzozowski A.M., Pike A.C.W., Dauter Z., Hubbard R.E., Bonn T., Engstroem O., Oehman L., Greene G.L., Gustafsson J.-A., Carlquist M.;
"Molecular basis of agonism and antagonism in the oestrogen receptor.";
Nature 389:753-758(1997).
[37]
 X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 306-544.
DOI=10.1073/pnas.95.11.5998; PubMed=9600906 [NCBI, ExPASy, EBI, Israel, Japan]
Tanenbaum D.M., Wang Y., Williams S.P., Sigler P.B.;
"Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains.";
Proc. Natl. Acad. Sci. U.S.A. 95:5998-6003(1998).
[38]
 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 294-554.
DOI=10.1016/S0092-8674(00)81717-1; PubMed=9875847 [NCBI, ExPASy, EBI, Israel, Japan]
Shiau A.K., Barstad D., Loria P.M., Cheng L., Kushner P.J., Agard D.A., Greene G.L.;
"The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen.";
Cell 95:927-937(1998).
[39]
 3D-STRUCTURE MODELING OF 311-547.
PubMed=9619507 [NCBI, ExPASy, EBI, Israel, Japan]
Maalouf G.J., Xu W., Smith T., Mohr S.C.;
"Homology model for the ligand-binding domain of the human estrogen receptor.";
J. Biomol. Struct. Dyn. 15:841-850(1998).
[40]
 VARIANT VAL-400.
PubMed=2792078 [NCBI, ExPASy, EBI, Israel, Japan]
Tora L., Mullick A., Metzger D., Ponglikitmongkol M., Park I., Chambon P.;
"The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties.";
EMBO J. 8:1981-1986(1989).
[41]
 VARIANT GLU-364.
DOI=10.1210/me.10.12.1519; PubMed=8961262 [NCBI, ExPASy, EBI, Israel, Japan]
McInerney E.M., Ince B.A., Shapiro D.J., Katzenellenbogen B.S.;
"A transcriptionally active estrogen receptor mutant is a novel type of dominant negative inhibitor of estrogen action.";
Mol. Endocrinol. 10:1519-1526(1996).
[42]
 VARIANT CYS-160.
DOI=10.1002/(SICI)1098-1004(1997)9:6<531::AID-HUMU6>3.3.CO;2-J; PubMed=9195227 [NCBI, ExPASy, EBI, Israel, Japan]
Anderson T.I., Wooster R., Laake K., Collins N., Warren W., Skrede M., Eeles R., Tveit K.M., Johnston S.R.D., Dowsett M., Olsen A.O., Moeller P., Stratton M.R., Boerresen-Dale A.-L.;
"Screening for ESR mutations in breast and ovarian cancer patients.";
Hum. Mutat. 9:531-536(1997).
[43]
 INVOLVEMENT IN BMD.
DOI=10.1093/hmg/9.13.2043; PubMed=10942433 [NCBI, ExPASy, EBI, Israel, Japan]
Becherini L., Gennari L., Masi L., Mansani R., Massart F., Morelli A., Falchetti A., Gonnelli S., Fiorelli G., Tanini A., Brandi M.L.;
"Evidence of a linkage disequilibrium between polymorphisms in the human estrogen receptor alpha gene and their relationship to bone mass variation in postmenopausal Italian women.";
Hum. Mol. Genet. 9:2043-2050(2000).
[44]
 VARIANTS TYR-6 AND ILE-264.
DOI=10.1186/bcr1637; PubMed=17224074 [NCBI, ExPASy, EBI, Israel, Japan]
Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M., Boerresen-Dale A.-L.;
"Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas.";
Breast Cancer Res. 9:R5-R5(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X03635; CAA27284.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12674; AAA52399.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U47678; AAB00115.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY425004; AAQ91815.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X73067; CAA51528.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL078582; CAI42285.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356311; CAI42285.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590993; CAI42285.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123500; AAD52984.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123494; AAD52984.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123495; AAD52984.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123496; AAD52984.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123497; AAD52984.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123498; AAD52984.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123499; AAD52984.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z75126; CAA99436.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00218352; -.
IPI00294982; -.
PIR S64737; S64737.
RefSeq NP_000116.2; -.
NP_001116212.1; -.
NP_001116213.1; -.
NP_001116214.1; -.
UniGene Hs.208124
3D structure databases
PDB
1A52; X-ray; 2.80 A; A/B=297-554.[ExPASy / RCSB / EBI]
1AKF; Model; -; A=309-547.[ExPASy / RCSB / EBI]
1ERE; X-ray; 3.10 A; A/B/C/D/E/F=301-553.[ExPASy / RCSB / EBI]
1ERR; X-ray; 2.60 A; A/B=301-553.[ExPASy / RCSB / EBI]
1G50; X-ray; 2.90 A; A/B/C=304-550.[ExPASy / RCSB / EBI]
1GWQ; X-ray; 2.45 A; A/B=301-548.[ExPASy / RCSB / EBI]
1GWR; X-ray; 2.40 A; A/B=305-549.[ExPASy / RCSB / EBI]
1HCP; NMR; -; A=180-254.[ExPASy / RCSB / EBI]
1HCQ; X-ray; 2.40 A; A/B/E/F=180-262.[ExPASy / RCSB / EBI]
1L2I; X-ray; 1.95 A; A/B=297-554.[ExPASy / RCSB / EBI]
1PCG; X-ray; 2.70 A; A/B=304-547.[ExPASy / RCSB / EBI]
1QKT; X-ray; 2.20 A; A=304-551.[ExPASy / RCSB / EBI]
1QKU; X-ray; 3.20 A; A/B/C=301-550.[ExPASy / RCSB / EBI]
1R5K; X-ray; 2.70 A; A/B/C=297-554.[ExPASy / RCSB / EBI]
1SJ0; X-ray; 1.90 A; A=307-554.[ExPASy / RCSB / EBI]
1UOM; X-ray; 2.28 A; A=301-553.[ExPASy / RCSB / EBI]
1X7E; X-ray; 2.80 A; A/B=305-549.[ExPASy / RCSB / EBI]
1X7R; X-ray; 2.00 A; A=305-549.[ExPASy / RCSB / EBI]
1XP1; X-ray; 1.80 A; A=307-554.[ExPASy / RCSB / EBI]
1XP6; X-ray; 1.70 A; A=307-554.[ExPASy / RCSB / EBI]
1XP9; X-ray; 1.80 A; A=307-554.[ExPASy / RCSB / EBI]
1XPC; X-ray; 1.60 A; A=307-554.[ExPASy / RCSB / EBI]
1XQC; X-ray; 2.05 A; A/B/C/D=301-553.[ExPASy / RCSB / EBI]
1YIM; X-ray; 1.90 A; A=307-554.[ExPASy / RCSB / EBI]
1YIN; X-ray; 2.20 A; A=307-554.[ExPASy / RCSB / EBI]
1ZKY; X-ray; 2.25 A; A/B=298-554.[ExPASy / RCSB / EBI]
2AYR; X-ray; 1.90 A; A=304-551.[ExPASy / RCSB / EBI]
2B1V; X-ray; 1.80 A; A/B=298-554.[ExPASy / RCSB / EBI]
2B1Z; X-ray; 1.78 A; A/B=298-554.[ExPASy / RCSB / EBI]
2B23; X-ray; 2.10 A; A/B=298-554.[ExPASy / RCSB / EBI]
2BJ4; X-ray; 2.00 A; A=305-533, B=305-533.[ExPASy / RCSB / EBI]
2FAI; X-ray; 2.10 A; A/B=298-554.[ExPASy / RCSB / EBI]
2G44; X-ray; 2.65 A; A/B=298-554.[ExPASy / RCSB / EBI]
2G5O; X-ray; 2.30 A; A/B=298-554.[ExPASy / RCSB / EBI]
2I0J; X-ray; 2.90 A; A/B/C/D=304-547.[ExPASy / RCSB / EBI]
2IOG; X-ray; 1.60 A; A=309-554.[ExPASy / RCSB / EBI]
2IOK; X-ray; 2.40 A; A/B=301-554.[ExPASy / RCSB / EBI]
2JF9; X-ray; 2.10 A; A/B/C=304-533.[ExPASy / RCSB / EBI]
2JFA; X-ray; 2.55 A; A=304-533, B=304-533.[ExPASy / RCSB / EBI]
2OCF; X-ray; 2.95 A; A=298-595.[ExPASy / RCSB / EBI]
2OUZ; X-ray; 2.00 A; A=301-553.[ExPASy / RCSB / EBI]
2P15; X-ray; 1.94 A; A/B=298-554.[ExPASy / RCSB / EBI]
2POG; X-ray; 1.84 A; A/B=304-551.[ExPASy / RCSB / EBI]
2Q6J; X-ray; 2.70 A; A/B=298-554.[ExPASy / RCSB / EBI]
2Q70; X-ray; 1.95 A; A/B=304-551.[ExPASy / RCSB / EBI]
2QA6; X-ray; 2.60 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QA8; X-ray; 1.85 A; A=298-554, B=298-554.[ExPASy / RCSB / EBI]
2QAB; X-ray; 1.89 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QE4; X-ray; 2.40 A; A/B=304-551.[ExPASy / RCSB / EBI]
2QGT; X-ray; 2.15 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QGW; X-ray; 2.39 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QH6; X-ray; 2.70 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QR9; X-ray; 2.00 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QSE; X-ray; 1.85 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QXM; X-ray; 2.30 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QXS; X-ray; 1.70 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QZO; X-ray; 1.72 A; A=298-554, B=298-554.[ExPASy / RCSB / EBI]
2R6W; X-ray; 2.00 A; A/B=304-551.[ExPASy / RCSB / EBI]
2R6Y; X-ray; 2.00 A; A/B=304-551.[ExPASy / RCSB / EBI]
3CBM; X-ray; 1.69 A; B=298-307.[ExPASy / RCSB / EBI]
3CBO; X-ray; 1.65 A; B=298-307.[ExPASy / RCSB / EBI]
3CBP; X-ray; 1.42 A; B=298-307.[ExPASy / RCSB / EBI]
3DT3; X-ray; 2.40 A; A/B=299-551.[ExPASy / RCSB / EBI]
3ERD; X-ray; 2.03 A; A/B=297-554.[ExPASy / RCSB / EBI]
3ERT; X-ray; 1.90 A; A=297-554.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A52; -.
1AKF; -.
1ERE; -.
1ERR; -.
1G50; -.
1GWQ; -.
1GWR; -.
1HCP; -.
1HCQ; -.
1L2I; -.
1PCG; -.
1QKT; -.
1QKU; -.
1R5K; -.
1SJ0; -.
1UOM; -.
1X7E; -.
1X7R; -.
1XP1; -.
1XP6; -.
1XP9; -.
1XPC; -.
1XQC; -.
1YIM; -.
1YIN; -.
1ZKY; -.
2AYR; -.
2B1V; -.
2B1Z; -.
2B23; -.
2BJ4; -.
2FAI; -.
2G44; -.
2G5O; -.
2I0J; -.
2IOG; -.
2IOK; -.
2JF9; -.
2JFA; -.
2OCF; -.
2OUZ; -.
2P15; -.
2POG; -.
2Q6J; -.
2Q70; -.
2QA6; -.
2QA8; -.
2QAB; -.
2QE4; -.
2QGT; -.
2QGW; -.
2QH6; -.
2QR9; -.
2QSE; -.
2QXM; -.
2QXS; -.
2QZO; -.
2R6W; -.
2R6Y; -.
3CBM; -.
3CBO; -.
3CBP; -.
3DT3; -.
3ERD; -.
3ERT; -.
DisProt DP00074; -.
ModBase P03372.
Protein-protein interaction databases
DIP DIP:5965N; -.
IntAct P03372; 20.
PTM databases
GlycoSuiteDB P03372; -.
PhosphoSite P03372; -.
Enzyme and pathway databases
Pathway_Interaction_DB hnf3apathway; FOXA1 transcription factor network.
foxm1pathway; FOXM1 transcription factor network.
er_nongenomic_pathway; Plasma membrane estrogen receptor signaling.
smad2_3nuclearpathway; Regulation of nuclear SMAD2/3 signaling.
telomerasepathway; Regulation of Telomerase.
hdac_classii_pathway; Signaling events mediated by HDAC Class II.
p38alphabetadownstreampathway; Signaling mediated by p38-alpha and p38-beta.
Organism-specific databases
GeneCards GC06P152023; -.
HGNC HGNC:3467; ESR1.
GenAtlas ESR1.
HPA CAB000037; -.
HPA000449; -.
HPA000450; -.
MIM 133430; gene. [NCBI / EBI]
Orphanet 785; Estrogen resistance syndrome.
PharmGKB PA156; -.
Gene expression databases
ArrayExpress P03372; -.
Bgee P03372; -.
CleanEx HS_ESR1; -.
GermOnline ENSG00000091831; Homo sapiens.
Ontologies
GO
GO:0016585; Cellular component: chromatin remodeling complex (non-traceable author statement from UniProtKB).
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005730; Cellular component: nucleolus (inferred from direct assay from HPA).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from HPA).
GO:0030284; Molecular function: estrogen receptor activity (non-traceable author statement from UniProtKB).
GO:0034056; Molecular function: estrogen response element binding (inferred from direct assay from UniProtKB).
GO:0030235; Molecular function: nitric-oxide synthase regulator activity (non-traceable author statement from UniProtKB).
GO:0047485; Molecular function: protein N-terminus binding (inferred from physical interaction from UniProtKB).
GO:0005496; Molecular function: steroid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003700; Molecular function: transcription factor activity (non-traceable author statement from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030520; Biological process: estrogen receptor signaling pathway (non-traceable author statement from UniProtKB).
GO:0048386; Biological process: positive regulation of retinoic acid receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (non-traceable author statement from UniProtKB).
GO:0006351; Biological process: transcription, DNA-dependent (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR008946; Nucl_hormone_rcpt_ligand-bd.
IPR000536; Nucl_hrmn_rcpt_lig-bd_core.
IPR001292; Oestr_rcpt_AF1.
IPR001723; Str_hrmn_rcpt.
IPR001628; Znf_hrmn_rcpt.
IPR013088; Znf_NHR/GATA.
Graphical view of domain structure.
Gene3D G3DSA:1.10.565.10; Nucl_hrmn_rcpt_lig_bd; 1.
G3DSA:3.30.50.10; Znf_NHR/GATA; 1.
Pfam PF00104; Hormone_recep; 1.
PF02159; Oest_recep; 1.
PF00105; zf-C4; 1.
Pfam graphical view of domain structure.
PRINTS PR00543; OESTROGENR.
PR00398; STRDHORMONER.
PR00047; STROIDFINGER.
ProDom PD000035; Znf_C4steroid; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00430; HOLI; 1.
SM00399; ZnF_C4; 1.
SMART graphical view of domain structure.
PROSITE PS00031; NUCLEAR_REC_DBD_1; 1.
PS51030; NUCLEAR_REC_DBD_2; 1.
PROSITE graphical view of domain structure (profiles).
Other
SWISS-3DIMAGE P03372.
Proteomic databases
PRIDE P03372; -.
Genome annotation databases
Ensembl ENSG00000091831; Homo sapiens. [Contig view]
GeneID 2099; -.
KEGG hsa:2099; -.
Phylogenomic databases
HOGENOM P03372; -.
HOVERGEN P03372; -.
OMA P03372; ENEPSGY.
Other
DrugBank DB00269; Chlorotrianisene.
DB00882; Clomifene.
DB00286; Conjugated Estrogens.
DB01406; Danazol.
DB00304; Desogestrel.
DB00890; Dienestrol.
DB00255; Diethylstilbestrol.
DB00858; Dromostanolone.
DB01395; Drospirenone.
DB00783; Estradiol.
DB01196; Estramustine.
DB04573; Estriol.
DB00655; Estrone.
DB00977; Ethinyl Estradiol.
DB00823; Ethynodiol Diacetate.
DB00294; Etonogestrel.
DB01185; Fluoxymesterone.
DB00947; Fulvestrant.
DB01006; Letrozole.
DB00367; Levonorgestrel.
DB00603; Medroxyprogesterone.
DB00351; Megestrol.
DB01065; Melatonin.
DB01357; Mestranol.
DB01183; Naloxone.
DB00957; Norgestimate.
DB00506; Norgestrel.
DB00396; Progesterone.
DB04575; Quinestrol.
DB00481; Raloxifene.
DB00675; Tamoxifen.
DB00539; Toremifene.
NextBio 8491; -.
SOURCE ESR1; Homo sapiens.
ProtoNet P03372.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Direct protein sequencing; DNA-binding; Glycoprotein; Lipid-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Receptor; Steroid-binding; Transcription; Transcription regulation; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   595  595     Estrogen receptor. PRO_0000053618
DNA_BIND   185   250  66     Nuclear receptor. 
ZN_FING   185   205  21     NR C4-type. 
ZN_FING   221   245  25     NR C4-type. 
REGION   1   184  184     Modulating. 
REGION   185   310  126     Mediates interaction with DNTTIP2. 
REGION   251   310  60     Hinge. 
REGION   262   595  334     Interaction with AKAP13. 
REGION   311   551  241     Steroid-binding. 
MOD_RES   7     7        Phosphothreonine. 
MOD_RES   10    10        Phosphoserine. 
MOD_RES   104   104        Phosphoserine; by CDK2. 
MOD_RES   106   106        Phosphoserine; by CDK2. 
MOD_RES   118   118        Phosphoserine. 
MOD_RES   167   167        Phosphoserine; by CK2. 
MOD_RES   537   537        Phosphotyrosine; by Tyr-kinases. 
CARBOHYD   10    10        O-linked (GlcNAc) (By similarity). 
VAR_SEQ   255   366        Missing (in isoform Short). VSP_003680
VARIANT   6     6  1     H -> Y (in a breast cancer sample; somatic mutation). VAR_033028 
VARIANT   77    77  1     G -> S (in dbSNP:rs9340773 [NCBI]). VAR_018905 
VARIANT   160   160  1     G -> C. VAR_004671 
VARIANT   264   264  1     M -> I (in a breast cancer sample; somatic mutation). VAR_033029 
VARIANT   364   364  1     V -> E (in estrogen resistance; dominant-negative inhibitor of the wild-type ESR). VAR_004672 [3D]
VARIANT   400   400  1     G -> V (destabilizes the receptor and decreases its affinity for estradiol at 25 degrees Celsius, but not at 4 degrees Celsius). VAR_004673 [3D]
VARIANT   411   411  1     D -> RNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSI ILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMA KAGLTLQQQHQRLAQLLLILSHIRHM (in a 80 kDa form found in a breast cancer line; contains an in-frame duplication of exons 6 and 7). VAR_010143
MUTAGEN   104   104        S->A: Loss of cyclin A-dependent induction of transcriptional activation. 
MUTAGEN   106   106        S->A: Loss of cyclin A-dependent induction of transcriptional activation. 
MUTAGEN   118   118        S->A: Decrease in phosphorylation. 
MUTAGEN   447   447        C->A: Loss of hormone binding capacity and temperature-sensitive loss in DNA-binding. 
TURN   186   188  3      
STRAND   194   196  3      
STRAND   199   201  3      
HELIX   203   213  11      
STRAND   222   225  4      
TURN   231   236  6      
HELIX   238   248  11      
HELIX   306   308  3      
HELIX   312   322  11      
HELIX   339   363  25      
HELIX   367   369  3      
HELIX   372   395  24      
STRAND   401   405  5      
STRAND   408   411  4      
HELIX   412   417  6      
HELIX   421   438  18      
HELIX   442   455  14      
HELIX   466   492  27      
HELIX   497   530  34      
HELIX   538   545  8      
Sequence information
Length: 595 AA [This is the length of the unprocessed precursor] Molecular weight: 66216 Da [This is the MW of the unprocessed precursor] CRC64: 5455C57AB0CCCAA7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKIPLERPLG EVYLDSSKPA VYNYPEGAAY 

        70         80         90        100        110        120 
EFNAAAAANA QVYGQTGLPY GPGSEAAAFG SNGLGGFPPL NSVSPSPLML LHPPPQLSPF 

       130        140        150        160        170        180 
LQPHGQQVPY YLENEPSGYT VREAGPPAFY RPNSDNRRQG GRERLASTND KGSMAMESAK 

       190        200        210        220        230        240 
ETRYCAVCND YASGYHYGVW SCEGCKAFFK RSIQGHNDYM CPATNQCTID KNRRKSCQAC 

       250        260        270        280        290        300 
RLRKCYEVGM MKGGIRKDRR GGRMLKHKRQ RDDGEGRGEV GSAGDMRAAN LWPSPLMIKR 

       310        320        330        340        350        360 
SKKNSLALSL TADQMVSALL DAEPPILYSE YDPTRPFSEA SMMGLLTNLA DRELVHMINW 

       370        380        390        400        410        420 
AKRVPGFVDL TLHDQVHLLE CAWLEILMIG LVWRSMEHPG KLLFAPNLLL DRNQGKCVEG 

       430        440        450        460        470        480 
MVEIFDMLLA TSSRFRMMNL QGEEFVCLKS IILLNSGVYT FLSSTLKSLE EKDHIHRVLD 

       490        500        510        520        530        540 
KITDTLIHLM AKAGLTLQQQ HQRLAQLLLI LSHIRHMSNK GMEHLYSMKC KNVVPLYDLL 

       550        560        570        580        590 
LEMLDAHRLH APTSRGGASV EETDQSHLAT AGSTSSHSLQ KYYITGEAEG FPATV
P03372 in FASTA format

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