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Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)

 ESR1_HUMAN              Reviewed;         595 AA.
P03372; Q13511; Q14276; Q5T5H7; Q6MZQ9; Q9NU51; Q9UDZ7; Q9UIS7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 2.
17-JUN-2020, entry version 272.
RecName: Full=Estrogen receptor;
Short=ER;
AltName: Full=ER-alpha;
AltName: Full=Estradiol receptor;
AltName: Full=Nuclear receptor subfamily 3 group A member 1;
Name=ESR1; Synonyms=ESR, NR3A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-400.
PubMed=3754034; DOI=10.1038/320134a0;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-400.
PubMed=3753802; DOI=10.1126/science.3753802;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mammary gland;
PubMed=8600466; DOI=10.1093/nar/24.5.962;
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].
NIEHS SNPs program;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE PROMOTER USAGE, AND
SUBCELLULAR LOCATION.
TISSUE=Placenta;
PubMed=16165085; DOI=10.1016/j.bbrc.2005.08.226;
Wang Z., Zhang X., Shen P., Loggie B.W., Chang Y., Deuel T.F.;
"Identification, cloning, and expression of human estrogen receptor-
alpha36, a novel variant of human estrogen receptor-alpha66.";
Biochem. Biophys. Res. Commun. 336:1023-1027(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 110-117, PHOSPHORYLATION, AND MUTAGENESIS.
PubMed=7476978; DOI=10.1210/mend.9.8.7476978;
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).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 152-595 (ISOFORM 1).
PubMed=10619354; DOI=10.1016/s0960-0760(99)00126-0;
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).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 216-434 (ISOFORM 2).
TISSUE=Mammary carcinoma;
PubMed=7916651;
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).
[13]
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.
[14]
PROTEIN SEQUENCE OF 532-542, AND PHOSPHORYLATION AT TYR-537.
PubMed=7539106; DOI=10.1210/mend.9.1.7539106;
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).
[15]
MUTAGENESIS OF CYS-447.
PubMed=1577818;
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).
[16]
INTERACTION WITH GTF2B.
PubMed=1517211;
Ing N.H., Beekman J.M., Tsai S.Y., Tsai M.J., O'Malley B.W.;
"Members of the steroid hormone receptor superfamily interact with TFIIB
(S300-II).";
J. Biol. Chem. 267:17617-17623(1992).
[17]
PHOSPHORYLATION AT SER-167 BY CK2.
PubMed=7838153; DOI=10.1210/mend.8.9.7838153;
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).
[18]
FUNCTION IN TRANSREPRESSION OF NF-KAPPA-B.
PubMed=7651415; DOI=10.1128/mcb.15.9.4971;
Stein B., Yang M.X.;
"Repression of the interleukin-6 promoter by estrogen receptor is mediated
by NF-kappa B and C/EBP beta.";
Mol. Cell. Biol. 15:4971-4979(1995).
[19]
MUTAGENESIS OF VAL-364.
PubMed=8961262; DOI=10.1210/mend.10.12.8961262;
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).
[20]
INTERACTION WITH DDX5, AND MUTAGENESIS OF SER-118.
PubMed=10409727; DOI=10.1128/mcb.19.8.5363;
Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H.,
Yanagisawa J., Metzger D., Hashimoto S., Kato S.;
"Purification and identification of p68 RNA helicase acting as a
transcriptional coactivator specific for the activation function 1 of human
estrogen receptor alpha.";
Mol. Cell. Biol. 19:5363-5372(1999).
[21]
FUNCTION (ISOFORM 3), TISSUE SPECIFICITY, ALTERNATIVE PROMOTER USAGE
(ISOFORM 3), AND SUBUNIT.
PubMed=10970861; DOI=10.1093/emboj/19.17.4688;
Flouriot G., Brand H., Denger S., Metivier R., Kos M., Reid G.,
Sonntag-Buck V., Gannon F.;
"Identification of a new isoform of the human estrogen receptor-alpha (hER-
alpha) that is encoded by distinct transcripts and that is able to repress
hER-alpha activation function 1.";
EMBO J. 19:4688-4700(2000).
[22]
MUTAGENESIS OF LEU-39 AND TYR-43.
PubMed=11075817; DOI=10.1210/mend.14.11.0546;
Metivier R., Petit F.G., Valotaire Y., Pakdel F.;
"Function of N-terminal transactivation domain of the estrogen receptor
requires a potential alpha-helical structure and is negatively regulated by
the A domain.";
Mol. Endocrinol. 14:1849-1871(2000).
[23]
INTERACTION WITH NCOA1; NCOA2 AND NCOA3, SUBUNIT, AND MUTAGENESIS OF
LEU-539.
PubMed=12554772; DOI=10.1210/me.2002-0351;
Bai Y., Giguere V.;
"Isoform-selective interactions between estrogen receptors and steroid
receptor coactivators promoted by estradiol and ErbB-2 signaling in living
cells.";
Mol. Endocrinol. 17:589-599(2003).
[24]
SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), AND PALMITOYLATION (ISOFORM 3).
PubMed=12682286; DOI=10.1073/pnas.0831079100;
Li L., Haynes M.P., Bender J.R.;
"Plasma membrane localization and function of the estrogen receptor alpha
variant (ER46) in human endothelial cells.";
Proc. Natl. Acad. Sci. U.S.A. 100:4807-4812(2003).
[25]
GLYCOSYLATION.
PubMed=8999954; DOI=10.1074/jbc.272.4.2421;
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).
[26]
FUNCTION, AND INTERACTION WITH SP1.
PubMed=9328340; DOI=10.1210/mend.11.11.9916;
Porter W., Saville B., Hoivik D., Safe S.;
"Functional synergy between the transcription factor Sp1 and the estrogen
receptor.";
Mol. Endocrinol. 11:1569-1580(1997).
[27]
INTERACTION WITH AKAP13.
PubMed=9627117; DOI=10.1038/sj.onc.1201783;
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).
[28]
PHOSPHORYLATION AT SER-104 AND SER-106, AND MUTAGENESIS.
PubMed=10428798; DOI=10.1074/jbc.274.32.22296;
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).
[29]
INTERACTION WITH NCOA6.
PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
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).
[30]
INTERACTION WITH PHB2.
PubMed=10359819; DOI=10.1073/pnas.96.12.6947;
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).
[31]
INTERACTION WITH NCOA2.
PubMed=11265755; DOI=10.1093/embo-reports/kvd028;
Benecke A., Chambon P., Gronemeyer H.;
"Synergy between estrogen receptor alpha activation functions AF1 and AF2
mediated by transcription intermediary factor TIF2.";
EMBO Rep. 1:151-157(2000).
[32]
FUNCTION, AND INTERACTION WITH SP1.
PubMed=10681512; DOI=10.1074/jbc.275.8.5379;
Saville B., Wormke M., Wang F., Nguyen T., Enmark E., Kuiper G.,
Gustafsson J.A., Safe S.;
"Ligand-, cell-, and estrogen receptor subtype (alpha/beta)-dependent
activation at GC-rich (Sp1) promoter elements.";
J. Biol. Chem. 275:5379-5387(2000).
[33]
FUNCTION, AND INTERACTION WITH SP3.
PubMed=10816575; DOI=10.1074/jbc.m002188200;
Stoner M., Wang F., Wormke M., Nguyen T., Samudio I., Vyhlidal C.,
Marme D., Finkenzeller G., Safe S.;
"Inhibition of vascular endothelial growth factor expression in HEC1A
endometrial cancer cells through interactions of estrogen receptor alpha
and Sp3 proteins.";
J. Biol. Chem. 275:22769-22779(2000).
[34]
INTERACTION WITH CITED1 AND EP300.
PubMed=11581164; DOI=10.1101/gad.906301;
Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y., Kato S.,
Isselbacher K.J., Brown M., Shioda T.;
"Selective coactivation of estrogen-dependent transcription by CITED1
CBP/p300-binding protein.";
Genes Dev. 15:2598-2612(2001).
[35]
FUNCTION, AND INTERACTION WITH JUN; JUNB AND JUND.
PubMed=11477071; DOI=10.1074/jbc.m101806200;
Teyssier C., Belguise K., Galtier F., Chalbos D.;
"Characterization of the physical interaction between estrogen receptor
alpha and JUN proteins.";
J. Biol. Chem. 276:36361-36369(2001).
[36]
INTERACTION WITH KDM5A.
PubMed=11358960; DOI=10.1074/jbc.m100313200;
Chan S.W., Hong W.;
"Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone
receptor-mediated transcription.";
J. Biol. Chem. 276:28402-28412(2001).
[37]
INTERACTION WITH NCOA5.
PubMed=11113208; DOI=10.1128/mcb.21.1.343-353.2001;
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).
[38]
FUNCTION, AND INTERACTION WITH NCOA1 AND DDX5.
PubMed=11682626; DOI=10.1210/mend.15.11.0727;
Metivier R., Penot G., Flouriot G., Pakdel F.;
"Synergism between ERalpha transactivation function 1 (AF-1) and AF-2
mediated by steroid receptor coactivator protein-1: requirement for the AF-
1 alpha-helical core and for a direct interaction between the N- and C-
terminal domains.";
Mol. Endocrinol. 15:1953-1970(2001).
[39]
INTERACTION WITH PRMT2.
PubMed=12039952; DOI=10.1074/jbc.m201053200;
Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
"Identification of protein arginine methyltransferase 2 as a coactivator
for estrogen receptor alpha.";
J. Biol. Chem. 277:28624-28630(2002).
[40]
INTERACTION WITH NR2C1.
PubMed=12093804; DOI=10.1074/jbc.m203531200;
Hu Y.C., Shyr C.R., Che W., Mu X.M., Kim E., Chang C.;
"Suppression of estrogen receptor-mediated transcription and cell growth by
interaction with TR2 orphan receptor.";
J. Biol. Chem. 277:33571-33579(2002).
[41]
INTERACTION WITH NCOA7.
PubMed=11971969; DOI=10.1128/mcb.22.10.3358-3372.2002;
Shao W., Halachmi S., Brown M.;
"ERAP140, a conserved tissue-specific nuclear receptor coactivator.";
Mol. Cell. Biol. 22:3358-3372(2002).
[42]
INTERACTION WITH RBFOX2.
PubMed=11875103; DOI=10.1210/mend.16.3.0787;
Norris J.D., Fan D., Sherk A., McDonnell D.P.;
"A negative coregulator for the human ER.";
Mol. Endocrinol. 16:459-468(2002).
[43]
INTERACTION WITH PELP1.
PubMed=12415108; DOI=10.1073/pnas.192569699;
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).
[44]
INTERACTION WITH SMARD1.
PubMed=12917342; DOI=10.1128/mcb.23.17.6210-6220.2003;
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).
[45]
INTERACTION WITH DNTTIP2.
PubMed=15047147; DOI=10.1016/j.bbrc.2004.02.179;
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).
[46]
FUNCTION.
PubMed=15078875; DOI=10.1074/jbc.m402148200;
Merot Y., Metivier R., Penot G., Manu D., Saligaut C., Gannon F.,
Pakdel F., Kah O., Flouriot G.;
"The relative contribution exerted by AF-1 and AF-2 transactivation
functions in estrogen receptor alpha transcriptional activity depends upon
the differentiation stage of the cell.";
J. Biol. Chem. 279:26184-26191(2004).
[47]
INTERACTION WITH TXNRD1.
PubMed=15199063; DOI=10.1074/jbc.m402753200;
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).
[48]
FUNCTION, PHOSPHORYLATION AT SER-118, DEPHOSPHORYLATION AT SER-118 BY
PPP5C, AND MUTAGENESIS OF SER-118.
PubMed=14764652; DOI=10.1210/me.2003-0308;
Ikeda K., Ogawa S., Tsukui T., Horie-Inoue K., Ouchi Y., Kato S.,
Muramatsu M., Inoue S.;
"Protein phosphatase 5 is a negative regulator of estrogen receptor-
mediated transcription.";
Mol. Endocrinol. 18:1131-1143(2004).
[49]
FUNCTION IN NF-KAPPA-B TRANSREPRESSION.
PubMed=16043358; DOI=10.1016/j.cyto.2004.12.008;
Liu H., Liu K., Bodenner D.L.;
"Estrogen receptor inhibits interleukin-6 gene expression by disruption of
nuclear factor kappaB transactivation.";
Cytokine 31:251-257(2005).
[50]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DYNLL1.
PubMed=15891768; DOI=10.1038/sj.embor.7400417;
Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R.,
Kumar R.;
"Functional regulation of oestrogen receptor pathway by the dynein light
chain 1.";
EMBO Rep. 6:538-544(2005).
[51]
ERRATUM OF PUBMED:15891768.
Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R.,
Kumar R.;
EMBO Rep. 6:1101-1101(2005).
[52]
INTERACTION WITH HEXIM1.
PubMed=15940264; DOI=10.1038/sj.onc.1208728;
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).
[53]
INTERACTION WITH KMT2D.
PubMed=16603732; DOI=10.1074/jbc.m513245200;
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).
[54]
FUNCTION.
PubMed=16684779; DOI=10.1074/jbc.m600021200;
Rayala S.K., den Hollander P., Manavathi B., Talukder A.H., Song C.,
Peng S., Barnekow A., Kremerskothen J., Kumar R.;
"Essential role of KIBRA in co-activator function of dynein light chain 1
in mammalian cells.";
J. Biol. Chem. 281:19092-19099(2006).
[55]
INTERACTION WITH MUC1.
PubMed=16427018; DOI=10.1016/j.molcel.2005.11.030;
Wei X., Xu H., Kufe D.;
"MUC1 oncoprotein stabilizes and activates estrogen receptor alpha.";
Mol. Cell 21:295-305(2006).
[56]
INTERACTION WITH UBE3A AND WBP2.
PubMed=16772533; DOI=10.1210/me.2005-0533;
Dhananjayan S.C., Ramamoorthy S., Khan O.Y., Ismail A., Sun J.,
Slingerland J., O'Malley B.W., Nawaz Z.;
"WW domain binding protein-2, an E6-associated protein interacting protein,
acts as a coactivator of estrogen and progesterone receptors.";
Mol. Endocrinol. 20:2343-2354(2006).
[57]
INTERACTION WITH ZNF366.
PubMed=17085477; DOI=10.1093/nar/gkl875;
Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M., Jat P.,
Kindle K.B., Heery D.M., Parker M.G., Buluwela L., Kamalati T., Ali S.;
"ZNF366 is an estrogen receptor corepressor that acts through CtBP and
histone deacetylases.";
Nucleic Acids Res. 34:6126-6136(2006).
[58]
FUNCTION.
PubMed=16617102; DOI=10.1073/pnas.0601989103;
Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
"MTA1, a transcriptional activator of breast cancer amplified sequence 3.";
Proc. Natl. Acad. Sci. U.S.A. 103:6670-6675(2006).
[59]
ERRATUM OF PUBMED:16617102.
Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013).
[60]
INTERACTION WITH PBXIP1.
PubMed=17043237; DOI=10.1073/pnas.0607445103;
Manavathi B., Acconcia F., Rayala S.K., Kumar R.;
"An inherent role of microtubule network in the action of nuclear
receptor.";
Proc. Natl. Acad. Sci. U.S.A. 103:15981-15986(2006).
[61]
INTERACTION WITH MAP1S.
PubMed=17658481; DOI=10.1016/j.bbrc.2007.06.179;
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).
[62]
INTERACTION WITH CUEDC2.
PubMed=17347654; DOI=10.1038/sj.emboj.7601602;
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).
[63]
INTERACTION WITH MACROD1.
PubMed=17914104; DOI=10.1677/erc-06-0082;
Han W.-D., Zhao Y.-L., Meng Y.G., Zang L., Wu Z.-Q., Li Q., Si Y.-L.,
Huang K., Ba J.-M., Morinaga H., Nomura M., Mu Y.-M.;
"Estrogenically regulated LRP16 interacts with estrogen receptor alpha and
enhances the receptor's transcriptional activity.";
Endocr. Relat. Cancer 14:741-753(2007).
[64]
SUBCELLULAR LOCATION, AND INTERACTION WITH KIF18A.
PubMed=17006958; DOI=10.1002/jcb.21000;
Luboshits G., Benayahu D.;
"MS-KIF18A, a kinesin, is associated with estrogen receptor.";
J. Cell. Biochem. 100:693-702(2007).
[65]
INTERACTION WITH PRMT2.
PubMed=17587566; DOI=10.1016/j.jsbmb.2007.05.006;
Meyer R., Wolf S.S., Obendorf M.;
"PRMT2, a member of the protein arginine methyltransferase family, is a
coactivator of the androgen receptor.";
J. Steroid Biochem. Mol. Biol. 107:1-14(2007).
[66]
INTERACTION WITH BCAS3.
PubMed=17505058; DOI=10.1210/me.2006-0514;
Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
"Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
coactivator, through proline-, glutamic acid-, and leucine-rich protein-1
(PELP1).";
Mol. Endocrinol. 21:1847-1860(2007).
[67]
INTERACTION WITH UIMC1.
PubMed=17311814; DOI=10.1093/nar/gkl1112;
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).
[68]
INTERACTION WITH ATAD2.
PubMed=17998543; DOI=10.1073/pnas.0705814104;
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).
[69]
FUNCTION IN ASSOCIATION WITH AP-1.
PubMed=18247370; DOI=10.1002/jcp.21379;
Lambertini E., Tavanti E., Torreggiani E., Penolazzi L., Gambari R.,
Piva R.;
"ERalpha and AP-1 interact in vivo with a specific sequence of the F
promoter of the human ERalpha gene in osteoblasts.";
J. Cell. Physiol. 216:101-110(2008).
[70]
METHYLATION AT ARG-260 BY PRMT1, MUTAGENESIS OF ARG-260, SUBCELLULAR
LOCATION, AND INTERACTION WITH PI3KR1/2; SRC AND PTK2/FAK1.
PubMed=18657504; DOI=10.1016/j.molcel.2008.05.025;
Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y., Sentis S.,
Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S., Corbo L.;
"Regulation of estrogen rapid signaling through arginine methylation by
PRMT1.";
Mol. Cell 31:212-221(2008).
[71]
FUNCTION IN NF-KAPPA-B TRANSREPRESSION, AND INTERACTION WITH RELA.
PubMed=17932106; DOI=10.1210/me.2007-0324;
Nettles K.W., Gil G., Nowak J., Metivier R., Sharma V.B., Greene G.L.;
"CBP Is a dosage-dependent regulator of nuclear factor-kappaB suppression
by the estrogen receptor.";
Mol. Endocrinol. 22:263-272(2008).
[72]
FUNCTION.
PubMed=17922032; DOI=10.1038/sj.onc.1210839;
Molli P.R., Singh R.R., Lee S.W., Kumar R.;
"MTA1-mediated transcriptional repression of BRCA1 tumor suppressor gene.";
Oncogene 27:1971-1980(2008).
[73]
INTERACTION WITH CCDC62.
PubMed=18563714; DOI=10.1002/pros.20774;
Chen M., Ni J., Zhang Y., Muyan M., Yeh S.;
"ERAP75 functions as a coactivator to enhance estrogen receptor alpha
transactivation in prostate stromal cells.";
Prostate 68:1273-1282(2008).
[74]
INTERACTION WITH SH2D4A AND PLCG.
PubMed=19712589; DOI=10.5483/bmbrep.2009.42.8.516;
Li T., Li W., Lu J., Liu H., Li Y., Zhao Y.;
"SH2D4A regulates cell proliferation via the ERalpha/PLC-gamma/PKC
pathway.";
BMB Rep. 42:516-522(2009).
[75]
INTERACTION WITH LDB1 AND RLIM.
PubMed=19117995; DOI=10.1158/0008-5472.can-08-1630;
Johnsen S.A., Guengoer C., Prenzel T., Riethdorf S., Riethdorf L.,
Taniguchi-Ishigaki N., Rau T., Tursun B., Furlow J.D., Sauter G.,
Scheffner M., Pantel K., Gannon F., Bach I.;
"Regulation of estrogen-dependent transcription by the LIM cofactors CLIM
and RLIM in breast cancer.";
Cancer Res. 69:128-136(2009).
[76]
INTERACTION WITH DNAAF4.
PubMed=19423554; DOI=10.1093/hmg/ddp215;
Massinen S., Tammimies K., Tapia-Paez I., Matsson H., Hokkanen M.E.,
Soederberg O., Landegren U., Castren E., Gustafsson J.A., Treuter E.,
Kere J.;
"Functional interaction of DYX1C1 with estrogen receptors suggests
involvement of hormonal pathways in dyslexia.";
Hum. Mol. Genet. 18:2802-2812(2009).
[77]
FUNCTION IN MUTUAL TRANSREPRESSION WITH NF-KAPPA-B, AND INTERACTION WITH
NFKB1 AND RELA.
PubMed=19350539; DOI=10.1002/jcb.22141;
Gionet N., Jansson D., Mader S., Pratt M.A.;
"NF-kappaB and estrogen receptor alpha interactions: Differential function
in estrogen receptor-negative and -positive hormone-independent breast
cancer cells.";
J. Cell. Biochem. 107:448-459(2009).
[78]
UBIQUITINATION, AND INTERACTION WITH OTUB1.
PubMed=19383985; DOI=10.1074/jbc.m109.007484;
Stanisic V., Malovannaya A., Qin J., Lonard D.M., O'Malley B.W.;
"OTU Domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1)
deubiquitinates estrogen receptor (ER) alpha and affects ERalpha
transcriptional activity.";
J. Biol. Chem. 284:16135-16145(2009).
[79]
PHOSPHORYLATION BY CSNK1D/CK1, AND INTERACTION WITH CSNK1D.
PubMed=19339517; DOI=10.1093/nar/gkp136;
Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J., Thomas R.S.,
Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.;
"CK1delta modulates the transcriptional activity of ERalpha via AIB1 in an
estrogen-dependent manner and regulates ERalpha-AIB1 interactions.";
Nucleic Acids Res. 37:3110-3123(2009).
[80]
INTERACTION WITH DDX17.
PubMed=19718048; DOI=10.1038/onc.2009.261;
Wortham N.C., Ahamed E., Nicol S.M., Thomas R.S., Periyasamy M., Jiang J.,
Ochocka A.M., Shousha S., Huson L., Bray S.E., Coombes R.C., Ali S.,
Fuller-Pace F.V.;
"The DEAD-box protein p72 regulates ERalpha-/oestrogen-dependent
transcription and cell growth, and is associated with improved survival in
ERalpha-positive breast cancer.";
Oncogene 28:4053-4064(2009).
[81]
INTERACTION WITH KIF18A.
PubMed=19636373; DOI=10.1371/journal.pone.0006407;
Zusev M., Benayahu D.;
"The regulation of MS-KIF18A expression and cross talk with estrogen
receptor.";
PLoS ONE 4:E6407-E6407(2009).
[82]
INTERACTION WITH TACC1.
PubMed=20078863; DOI=10.1186/1471-2199-11-3;
Guyot R., Vincent S., Bertin J., Samarut J., Ravel-Chapuis P.;
"The transforming acidic coiled coil (TACC1) protein modulates the
transcriptional activity of the nuclear receptors TR and RAR.";
BMC Mol. Biol. 11:3-3(2010).
[83]
FUNCTION, INTERACTION WITH CCAR2, AND SUBCELLULAR LOCATION.
PubMed=20074560; DOI=10.1016/j.bbrc.2010.01.025;
Koyama S., Wada-Hiraike O., Nakagawa S., Tanikawa M., Hiraike H.,
Miyamoto Y., Sone K., Oda K., Fukuhara H., Nakagawa K., Kato S., Yano T.,
Taketani Y.;
"Repression of estrogen receptor beta function by putative tumor suppressor
DBC1.";
Biochem. Biophys. Res. Commun. 392:357-362(2010).
[84]
FUNCTION IN SYNERGISM WITH NF-KAPPA-B.
PubMed=20705611; DOI=10.1074/jbc.m110.155309;
Pradhan M., Bembinster L.A., Baumgarten S.C., Frasor J.;
"Proinflammatory cytokines enhance estrogen-dependent expression of the
multidrug transporter gene ABCG2 through estrogen receptor and NF{kappa}B
cooperativity at adjacent response elements.";
J. Biol. Chem. 285:31100-31106(2010).
[85]
INTERACTION WITH ZFHX3.
PubMed=20720010; DOI=10.1074/jbc.m110.128330;
Dong X.Y., Sun X., Guo P., Li Q., Sasahara M., Ishii Y., Dong J.T.;
"ATBF1 inhibits estrogen receptor (ER) function by selectively competing
with AIB1 for binding to the ER in ER-positive breast cancer cells.";
J. Biol. Chem. 285:32801-32809(2010).
[86]
INTERACTION WITH ESRRB.
PubMed=19755138; DOI=10.1016/j.mce.2009.09.007;
Bombail V., Collins F., Brown P., Saunders P.T.;
"Modulation of ER alpha transcriptional activity by the orphan nuclear
receptor ERR beta and evidence for differential effects of long- and short-
form splice variants.";
Mol. Cell. Endocrinol. 314:53-61(2010).
[87]
INTERACTION WITH SAV1 AND STK3/MST2.
PubMed=21104395; DOI=10.1007/s00109-010-0698-y;
Park Y., Park J., Lee Y., Lim W., Oh B.C., Shin C., Kim W., Lee Y.;
"Mammalian MST2 kinase and human Salvador activate and reduce estrogen
receptor alpha in the absence of ligand.";
J. Mol. Med. 89:181-191(2011).
[88]
FUNCTION (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM 3), TOPOLOGY (ISOFORM
3), AND MUTAGENESIS OF ILE-386.
PubMed=21937726; DOI=10.1091/mbc.e11-05-0416;
Kim K.H., Toomre D., Bender J.R.;
"Splice isoform estrogen receptors as integral transmembrane proteins.";
Mol. Biol. Cell 22:4415-4423(2011).
[89]
FUNCTION IN ERE-INDEPENDENT SIGNALING.
PubMed=21330404; DOI=10.1210/me.2010-0425;
Heldring N., Isaacs G.D., Diehl A.G., Sun M., Cheung E., Ranish J.A.,
Kraus W.L.;
"Multiple sequence-specific DNA-binding proteins mediate estrogen receptor
signaling through a tethering pathway.";
Mol. Endocrinol. 25:564-574(2011).
[90]
INTERACTION WITH LMTK3, PHOSPHORYLATION, AND UBIQUITINATION.
PubMed=21602804; DOI=10.1038/nm.2351;
Giamas G., Filipovic A., Jacob J., Messier W., Zhang H., Yang D., Zhang W.,
Shifa B.A., Photiou A., Tralau-Stewart C., Castellano L., Green A.R.,
Coombes R.C., Ellis I.O., Ali S., Lenz H.J., Stebbing J.;
"Kinome screening for regulators of the estrogen receptor identifies LMTK3
as a new therapeutic target in breast cancer.";
Nat. Med. 17:715-719(2011).
[91]
SUBCELLULAR LOCATION, AND PALMITOYLATION.
PubMed=22031296; DOI=10.1091/mbc.e11-07-0638;
Pedram A., Razandi M., Deschenes R.J., Levin E.R.;
"DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors.";
Mol. Biol. Cell 23:188-199(2012).
[92]
FUNCTION IN SYNERGISM WITH NF-KAPPA-B.
PubMed=22083956; DOI=10.1128/mcb.05869-11;
Pradhan M., Baumgarten S.C., Bembinster L.A., Frasor J.;
"CBP mediates NF-kappaB-dependent histone acetylation and estrogen receptor
recruitment to an estrogen response element in the BIRC3 promoter.";
Mol. Cell. Biol. 32:569-575(2012).
[93]
SUBCELLULAR LOCATION, AND INTERACTION WITH CLOCK.
PubMed=23160374; DOI=10.1038/onc.2012.518;
Li S., Wang M., Ao X., Chang A.K., Yang C., Zhao F., Bi H., Liu Y.,
Xiao L., Wu H.;
"CLOCK is a substrate of SUMO and sumoylation of CLOCK upregulates the
transcriptional activity of estrogen receptor-alpha.";
Oncogene 32:4883-4891(2013).
[94]
INTERACTION WITH SFR1.
PubMed=23874500; DOI=10.1371/journal.pone.0068075;
Feng Y., Singleton D., Guo C., Gardner A., Pakala S., Kumar R., Jensen E.,
Zhang J., Khan S.;
"DNA homologous recombination factor SFR1 physically and functionally
interacts with estrogen receptor alpha.";
PLoS ONE 8:E68075-E68075(2013).
[95]
INTERACTION WITH TRIP4.
PubMed=25219498; DOI=10.1016/j.molcel.2014.08.007;
Yoo H.M., Kang S.H., Kim J.Y., Lee J.E., Seong M.W., Lee S.W., Ka S.H.,
Sou Y.S., Komatsu M., Tanaka K., Lee S.T., Noh D.Y., Baek S.H., Jeon Y.J.,
Chung C.H.;
"Modification of ASC1 by UFM1 is crucial for ERalpha transactivation and
breast cancer development.";
Mol. Cell 56:261-274(2014).
[96]
METHYLATION AT ARG-260, DEMETHYLATION AT ARG-260, AND SUBCELLULAR LOCATION.
PubMed=24498420; DOI=10.1371/journal.pone.0087982;
Poulard C., Rambaud J., Hussein N., Corbo L., Le Romancer M.;
"JMJD6 regulates ERalpha methylation on arginine.";
PLoS ONE 9:E87982-E87982(2014).
[97]
INTERACTION WITH DCAF13; LATS1 AND DCAF1, AND UBIQUITINATION.
PubMed=28068668; DOI=10.1038/nature20829;
Britschgi A., Duss S., Kim S., Couto J.P., Brinkhaus H., Koren S.,
De Silva D., Mertz K.D., Kaup D., Varga Z., Voshol H., Vissieres A.,
Leroy C., Roloff T., Stadler M.B., Scheel C.H., Miraglia L.J., Orth A.P.,
Bonamy G.M., Reddy V.A., Bentires-Alj M.;
"The Hippo kinases LATS1 and 2 control human breast cell fate via crosstalk
with ERalpha.";
Nature 541:541-545(2017).
[98]
STRUCTURE BY NMR OF 180-262.
PubMed=2247153; DOI=10.1038/348458a0;
Schwabe J.W.E., Neuhaus D., Rhodes D.;
"Solution structure of the DNA-binding domain of the oestrogen receptor.";
Nature 348:458-461(1990).
[99]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 180-262.
PubMed=8221895; DOI=10.1016/0092-8674(93)90390-c;
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).
[100]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 305-548.
PubMed=9338790; DOI=10.1038/39645;
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).
[101]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 306-544.
PubMed=9600906; DOI=10.1073/pnas.95.11.5998;
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).
[102]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 294-554.
PubMed=9875847; DOI=10.1016/s0092-8674(00)81717-1;
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).
[103]
3D-STRUCTURE MODELING OF 311-547.
PubMed=9619507; DOI=10.1080/07391102.1998.10508206;
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).
[104]
VARIANT VAL-400.
PubMed=2792078; DOI=10.1002/j.1460-2075.1989.tb03604.x;
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).
[105]
VARIANT CYS-160.
PubMed=9195227;
DOI=10.1002/(sici)1098-1004(1997)9:6<531::aid-humu6>3.0.co;2-4;
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).
[106]
INVOLVEMENT IN BMD.
PubMed=10942433; DOI=10.1093/hmg/9.13.2043;
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).
[107]
INTERACTION WITH GPER1.
PubMed=19749156; DOI=10.1210/me.2009-0120;
Vivacqua A., Lappano R., De Marco P., Sisci D., Aquila S., De Amicis F.,
Fuqua S.A., Ando S., Maggiolini M.;
"G protein-coupled receptor 30 expression is up-regulated by EGF and TGF
alpha in estrogen receptor alpha-positive cancer cells.";
Mol. Endocrinol. 23:1815-1826(2009).
[108]
VARIANTS TYR-6 AND ILE-264.
PubMed=17224074; DOI=10.1186/bcr1637;
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).
[109]
VARIANT ESTRR HIS-375, AND CHARACTERIZATION OF VARIANT ESTRR HIS-375.
PubMed=23841731; DOI=10.1056/nejmoa1303611;
Quaynor S.D., Stradtman E.W. Jr., Kim H.G., Shen Y., Chorich L.P.,
Schreihofer D.A., Layman L.C.;
"Delayed puberty and estrogen resistance in a woman with estrogen receptor
alpha variant.";
N. Engl. J. Med. 369:164-171(2013).
[110]
VARIANT ESTRR HIS-394, AND CHARACTERIZATION OF VARIANT ESTRR HIS-394.
PubMed=27754803; DOI=10.1210/jc.2016-2749;
Bernard V., Kherra S., Francou B., Fagart J., Viengchareun S., Guechot J.,
Ladjouze A., Guiochon-Mantel A., Korach K.S., Binart N., Lombes M.,
Christin-Maitre S.;
"Familial multiplicity of estrogen insensitivity associated with a loss-of-
function ESR1 mutation.";
J. Clin. Endocrinol. Metab. 102:93-99(2017).
-!- FUNCTION: Nuclear hormone receptor. The steroid hormones and their
receptors are involved in the regulation of eukaryotic gene expression
and affect cellular proliferation and differentiation in target
tissues. Ligand-dependent nuclear transactivation involves either
direct homodimer binding to a palindromic estrogen response element
(ERE) sequence or association with other DNA-binding transcription
factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-
independent signaling. Ligand binding induces a conformational change
allowing subsequent or combinatorial association with multiprotein
coactivator complexes through LXXLL motifs of their respective
components. Mutual transrepression occurs between the estrogen receptor
(ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-
B DNA-binding activity and inhibits NF-kappa-B-mediated transcription
from the IL6 promoter and displace RELA/p65 and associated coregulators
from the promoter. Recruited to the NF-kappa-B response element of the
CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B
components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act
synergistically with NF-kappa-B to activate transcription involving
respective recruitment adjacent response elements; the function
involves CREBBP. Can activate the transcriptional activity of TFF1.
Also mediates membrane-initiated estrogen signaling involving various
kinase cascades. Isoform 3 is involved in activation of NOS3 and
endothelial nitric oxide production. Isoforms lacking one or several
functional domains are thought to modulate transcriptional activity by
competitive ligand or DNA binding and/or heterodimerization with the
full-length receptor. Essential for MTA1-mediated transcriptional
regulation of BRCA1 and BCAS3. Isoform 3 can bind to ERE and inhibit
isoform 1. {ECO:0000269|PubMed:10681512, ECO:0000269|PubMed:10816575,
ECO:0000269|PubMed:11477071, ECO:0000269|PubMed:11682626,
ECO:0000269|PubMed:14764652, ECO:0000269|PubMed:15078875,
ECO:0000269|PubMed:15891768, ECO:0000269|PubMed:16043358,
ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:16684779,
ECO:0000269|PubMed:17922032, ECO:0000269|PubMed:17932106,
ECO:0000269|PubMed:18247370, ECO:0000269|PubMed:19350539,
ECO:0000269|PubMed:20074560, ECO:0000269|PubMed:20705611,
ECO:0000269|PubMed:21330404, ECO:0000269|PubMed:22083956,
ECO:0000269|PubMed:7651415, ECO:0000269|PubMed:9328340}.
-!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ESR2.
Isoform 3 can probably homodimerize or heterodimerize with isoform 1
and ESR2. Interacts with FOXC2, MAP1S, SLC30A9, UBE1C and NCOA3
coactivator (By similarity). Interacts with EP300; the interaction is
estrogen-dependent and enhanced by CITED1. Interacts with CITED1; the
interaction is estrogen-dependent. Interacts with NCOA5 and NCOA6
coactivators. Interacts with NCOA7; the interaction is a ligand-
inducible. Interacts with PHB2, PELP1 and UBE1C. Interacts with AKAP13.
Interacts with CUEDC2. Interacts with KDM5A. Interacts with SMARD1.
Interacts with HEXIM1. Interacts with PBXIP1. Interaction with MUC1 is
stimulated by 7 beta-estradiol (E2) and enhances ERS1-mediated
transcription. Interacts with DNTTIP2, FAM120B and UIMC1. Interacts
with isoform 4 of TXNRD1. Interacts with KMT2D/MLL2. Interacts with
ATAD2 and this interaction is enhanced by estradiol. Interacts with
KIF18A and LDB1. Interacts with RLIM (via C-terminus). Interacts with
MACROD1. Interacts with SH2D4A and PLCG. Interaction with SH2D4A blocks
binding to PLCG and inhibits estrogen-induced cell proliferation.
Interacts with DYNLL1. Interacts with CCDC62 in the presence of
estradiol/E2; this interaction seems to enhance the transcription of
target genes. Interacts with NR2C1; the interaction prevents
homodimerization of ESR1 and suppresses its transcriptional activity
and cell growth. Interacts with DNAAF4. Interacts with PRMT2. Interacts
with PI3KR1 or PI3KR2, SRC and PTK2/FAK1. Interacts with RBFOX2.
Interacts with STK3/MST2 only in the presence of SAV1 and vice-versa.
Binds to CSNK1D. Interacts with NCOA2; NCOA2 can interact with ESR1 AF-
1 and AF-2 domains simultaneously and mediate their transcriptional
synergy. Interacts with DDX5. Interacts with NCOA1; the interaction
seems to require a self-association of N-terminal and C-terminal
regions. Interacts with ZNF366, DDX17, NFKB1, RELA, SP1 and SP3.
Interacts with NRIP1 (By similarity). Interacts with GPER1; the
interaction occurs in an estrogen-dependent manner. Interacts with
CLOCK and the interaction is stimulated by estrogen. Interacts with
BCAS3. Interacts with TRIP4 (ufmylated); estrogen dependent. Interacts
with LMTK3; the interaction phosphorylates ESR1 (in vitro) and protects
it against proteasomal degradation. Interacts with CCAR2 (via N-
terminus) in a ligand-independent manner. Interacts with ZFHX3.
Interacts with SFR1 in a ligand-dependent and -independent manner
(PubMed:23874500). Interacts with DCAF13, LATS1 and DCAF1; regulates
ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation
(PubMed:28068668). Interacts (via DNA-binding domain) with POU4F2 (C-
terminus); this interaction increases the estrogen receptor ESR1
transcriptional activity in a DNA- and ligand 17-beta-estradiol-
independent manner (By similarity). Interacts with ESRRB isoform 1
(PubMed:19755138). Interacts with UBE3A and WBP2 (PubMed:16772533).
Interacts with GTF2B (PubMed:1517211). Interacts with RBM39 (By
similarity). In the absence of hormonal ligand, interacts with TACC1
(PubMed:20078863). {ECO:0000250, ECO:0000250|UniProtKB:P19785,
ECO:0000269|PubMed:10359819, ECO:0000269|PubMed:10409727,
ECO:0000269|PubMed:10567404, ECO:0000269|PubMed:10681512,
ECO:0000269|PubMed:10816575, ECO:0000269|PubMed:10970861,
ECO:0000269|PubMed:11113208, ECO:0000269|PubMed:11265755,
ECO:0000269|PubMed:11358960, ECO:0000269|PubMed:11477071,
ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:11682626,
ECO:0000269|PubMed:11875103, ECO:0000269|PubMed:11971969,
ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:12093804,
ECO:0000269|PubMed:12415108, ECO:0000269|PubMed:12554772,
ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:15047147,
ECO:0000269|PubMed:1517211, ECO:0000269|PubMed:15199063,
ECO:0000269|PubMed:15891768, ECO:0000269|PubMed:15940264,
ECO:0000269|PubMed:16427018, ECO:0000269|PubMed:16603732,
ECO:0000269|PubMed:16772533, ECO:0000269|PubMed:17006958,
ECO:0000269|PubMed:17043237, ECO:0000269|PubMed:17085477,
ECO:0000269|PubMed:17311814, ECO:0000269|PubMed:17347654,
ECO:0000269|PubMed:17505058, ECO:0000269|PubMed:17587566,
ECO:0000269|PubMed:17658481, ECO:0000269|PubMed:17914104,
ECO:0000269|PubMed:17932106, ECO:0000269|PubMed:17998543,
ECO:0000269|PubMed:18563714, ECO:0000269|PubMed:18657504,
ECO:0000269|PubMed:19117995, ECO:0000269|PubMed:19339517,
ECO:0000269|PubMed:19350539, ECO:0000269|PubMed:19383985,
ECO:0000269|PubMed:19423554, ECO:0000269|PubMed:19636373,
ECO:0000269|PubMed:19712589, ECO:0000269|PubMed:19718048,
ECO:0000269|PubMed:19749156, ECO:0000269|PubMed:19755138,
ECO:0000269|PubMed:20074560, ECO:0000269|PubMed:20078863,
ECO:0000269|PubMed:20720010, ECO:0000269|PubMed:21104395,
ECO:0000269|PubMed:21602804, ECO:0000269|PubMed:23160374,
ECO:0000269|PubMed:23874500, ECO:0000269|PubMed:25219498,
ECO:0000269|PubMed:28068668, ECO:0000269|PubMed:9328340,
ECO:0000269|PubMed:9627117}.
-!- INTERACTION:
P03372; Q12802: AKAP13; NbExp=3; IntAct=EBI-78473, EBI-1373806;
P03372; Q03989: ARID5A; NbExp=9; IntAct=EBI-78473, EBI-948603;
P03372; Q9Y294: ASF1A; NbExp=4; IntAct=EBI-78473, EBI-749553;
P03372; Q8IXJ9: ASXL1; NbExp=2; IntAct=EBI-78473, EBI-1646500;
P03372; Q6PL18: ATAD2; NbExp=5; IntAct=EBI-78473, EBI-6598454;
P03372; P18846: ATF1; NbExp=3; IntAct=EBI-78473, EBI-852794;
P03372; P62952: BLCAP; NbExp=2; IntAct=EBI-78473, EBI-3895726;
P03372; P38398: BRCA1; NbExp=14; IntAct=EBI-78473, EBI-349905;
P03372; P20290-2: BTF3; NbExp=5; IntAct=EBI-78473, EBI-1054703;
P03372; Q86Y37: CACUL1; NbExp=5; IntAct=EBI-78473, EBI-8168227;
P03372; P29279: CCN2; NbExp=7; IntAct=EBI-78473, EBI-2835375;
P03372; P17676: CEBPB; NbExp=2; IntAct=EBI-78473, EBI-969696;
P03372; Q99966: CITED1; NbExp=3; IntAct=EBI-78473, EBI-2624951;
P03372; Q9H467: CUEDC2; NbExp=2; IntAct=EBI-78473, EBI-1248228;
P03372; Q9NV06: DCAF13; NbExp=2; IntAct=EBI-78473, EBI-7402939;
P03372; O00429: DNM1L; NbExp=2; IntAct=EBI-78473, EBI-724571;
P03372; O60869: EDF1; NbExp=3; IntAct=EBI-78473, EBI-781301;
P03372; P00533: EGFR; NbExp=2; IntAct=EBI-78473, EBI-297353;
P03372; Q09472: EP300; NbExp=2; IntAct=EBI-78473, EBI-447295;
P03372; P03372: ESR1; NbExp=11; IntAct=EBI-78473, EBI-78473;
P03372; Q12778: FOXO1; NbExp=2; IntAct=EBI-78473, EBI-1108782;
P03372; O43524: FOXO3; NbExp=7; IntAct=EBI-78473, EBI-1644164;
P03372; Q9Y3R0: GRIP1; NbExp=2; IntAct=EBI-78473, EBI-5349621;
P03372; O00165: HAX1; NbExp=2; IntAct=EBI-78473, EBI-357001;
P03372; Q6NYC1: JMJD6; NbExp=8; IntAct=EBI-78473, EBI-8464037;
P03372; O15054: KDM6B; NbExp=2; IntAct=EBI-78473, EBI-2831260;
P03372; O14686: KMT2D; NbExp=3; IntAct=EBI-78473, EBI-996065;
P03372; O95835: LATS1; NbExp=2; IntAct=EBI-78473, EBI-444209;
P03372; Q96Q04: LMTK3; NbExp=3; IntAct=EBI-78473, EBI-720814;
P03372; Q9BQ69: MACROD1; NbExp=6; IntAct=EBI-78473, EBI-5324932;
P03372; Q00987: MDM2; NbExp=2; IntAct=EBI-78473, EBI-389668;
P03372; Q15648: MED1; NbExp=3; IntAct=EBI-78473, EBI-394459;
P03372; P60660: MYL6; NbExp=3; IntAct=EBI-78473, EBI-300817;
P03372; Q15788: NCOA1; NbExp=8; IntAct=EBI-78473, EBI-455189;
P03372; Q15596: NCOA2; NbExp=5; IntAct=EBI-78473, EBI-81236;
P03372; Q9Y6Q9: NCOA3; NbExp=4; IntAct=EBI-78473, EBI-81196;
P03372; Q9UN36: NDRG2; NbExp=2; IntAct=EBI-78473, EBI-3895741;
P03372; PRO_0000030311 [P19838]: NFKB1; NbExp=3; IntAct=EBI-78473, EBI-697771;
P03372; Q96RI1-3: NR1H4; NbExp=2; IntAct=EBI-78473, EBI-10921781;
P03372; Q9BZ95: NSD3; NbExp=3; IntAct=EBI-78473, EBI-3390132;
P03372; Q9BTK6: PAGR1; NbExp=5; IntAct=EBI-78473, EBI-2372223;
P03372; Q96AQ6-1: PBXIP1; NbExp=3; IntAct=EBI-78473, EBI-15606280;
P03372; P06401: PGR; NbExp=20; IntAct=EBI-78473, EBI-78539;
P03372; P06401-1: PGR; NbExp=4; IntAct=EBI-78473, EBI-12590474;
P03372; Q99623: PHB2; NbExp=4; IntAct=EBI-78473, EBI-358348;
P03372; P27986: PIK3R1; NbExp=7; IntAct=EBI-78473, EBI-79464;
P03372; P36873: PPP1CC; NbExp=3; IntAct=EBI-78473, EBI-356283;
P03372; P53041: PPP5C; NbExp=4; IntAct=EBI-78473, EBI-716663;
P03372; P55345: PRMT2; NbExp=9; IntAct=EBI-78473, EBI-78458;
P03372; P60763: RAC3; NbExp=5; IntAct=EBI-78473, EBI-767084;
P03372; O43251: RBFOX2; NbExp=4; IntAct=EBI-78473, EBI-746056;
P03372; Q04206: RELA; NbExp=9; IntAct=EBI-78473, EBI-73886;
P03372; Q14151: SAFB2; NbExp=2; IntAct=EBI-78473, EBI-352869;
P03372; Q96HI0: SENP5; NbExp=2; IntAct=EBI-78473, EBI-3895753;
P03372; P08047: SP1; NbExp=2; IntAct=EBI-78473, EBI-298336;
P03372; Q02447: SP3; NbExp=4; IntAct=EBI-78473, EBI-348158;
P03372; P12931: SRC; NbExp=12; IntAct=EBI-78473, EBI-621482;
P03372; O15164: TRIM24; NbExp=3; IntAct=EBI-78473, EBI-2130378;
P03372; Q16881-4: TXNRD1; NbExp=4; IntAct=EBI-78473, EBI-9080335;
P03372; Q9UBK9: UXT; NbExp=2; IntAct=EBI-78473, EBI-357355;
P03372; Q8N895: ZNF366; NbExp=6; IntAct=EBI-78473, EBI-2813661;
P03372; P59598: Asxl1; Xeno; NbExp=2; IntAct=EBI-78473, EBI-5743705;
P03372; P05627: Jun; Xeno; NbExp=6; IntAct=EBI-78473, EBI-764369;
P03372; Q9JLI4: Ncoa6; Xeno; NbExp=2; IntAct=EBI-78473, EBI-286271;
P03372; Q60974: Ncor1; Xeno; NbExp=2; IntAct=EBI-78473, EBI-349004;
P03372; P62962: Pfn1; Xeno; NbExp=3; IntAct=EBI-78473, EBI-647096;
P03372; P00523: SRC; Xeno; NbExp=2; IntAct=EBI-78473, EBI-848039;
P03372-1; P03372-1: ESR1; NbExp=4; IntAct=EBI-15606245, EBI-15606245;
P03372-1; Q92731: ESR2; NbExp=5; IntAct=EBI-15606245, EBI-78505;
P03372-1; Q92993: KAT5; NbExp=3; IntAct=EBI-15606245, EBI-399080;
P03372-1; Q96AQ6-1: PBXIP1; NbExp=5; IntAct=EBI-15606245, EBI-15606280;
P03372-4; P00533: EGFR; NbExp=4; IntAct=EBI-4309277, EBI-297353;
P03372-4; P29353: SHC1; NbExp=2; IntAct=EBI-4309277, EBI-78835;
P03372-4; P12931: SRC; NbExp=2; IntAct=EBI-4309277, EBI-621482;
-!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00407, ECO:0000269|PubMed:12682286,
ECO:0000269|PubMed:20074560}. Cytoplasm {ECO:0000269|PubMed:12682286,
ECO:0000269|PubMed:24498420}. Cell membrane
{ECO:0000269|PubMed:12682286}; Peripheral membrane protein
{ECO:0000269|PubMed:12682286}; Cytoplasmic side
{ECO:0000269|PubMed:12682286}. Note=A minor fraction is associated with
the inner membrane.
-!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm. Cell membrane;
Peripheral membrane protein; Cytoplasmic side. Cell membrane; Single-
pass type I membrane protein. Note=Associated with the inner membrane
via palmitoylation (Probable). At least a subset exists as a
transmembrane protein with a N-terminal extracellular domain.
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleus. Golgi apparatus. Cell membrane.
Note=Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus where
most probably palmitoylation occurs. Associated with the plasma
membrane when palmitoylated.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Long, hER-alpha66, ER66;
IsoId=P03372-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P03372-2; Sequence=VSP_003680;
Name=3; Synonyms=hER-alpha46, ER46;
IsoId=P03372-3; Sequence=VSP_042460;
Name=4; Synonyms=hER-alpha36, ER36;
IsoId=P03372-4; Sequence=VSP_042460, VSP_042461;
-!- TISSUE SPECIFICITY: Widely expressed. Isoform 3 is not expressed in the
pituitary gland. {ECO:0000269|PubMed:10970861}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
DNA-binding domain and a C-terminal ligand-binding domain. The
modulating domain, also known as A/B or AF-1 domain has a ligand-
independent transactivation function. The C-terminus contains a ligand-
dependent transactivation domain, also known as E/F or AF-2 domain
which overlaps with the ligand binding domain. AF-1 and AF-2 activate
transcription independently and synergistically and act in a
promoter- and cell-specific manner. AF-1 seems to provide the major
transactivation function in differentiated cells.
-!- PTM: Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably
enhances transcriptional activity. Self-association induces
phosphorylation. Dephosphorylation at Ser-118 by PPP5C inhibits its
transactivation activity. Phosphorylated by LMTK3 in vitro.
{ECO:0000269|PubMed:10428798, ECO:0000269|PubMed:14764652,
ECO:0000269|PubMed:19339517, ECO:0000269|PubMed:21602804,
ECO:0000269|PubMed:7476978, ECO:0000269|PubMed:7539106,
ECO:0000269|PubMed:7838153}.
-!- PTM: Glycosylated; contains N-acetylglucosamine, probably O-linked.
{ECO:0000269|PubMed:8999954}.
-!- PTM: Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1
proteasomal degradation (PubMed:21602804, PubMed:28068668).
Deubiquitinated by OTUB1 (PubMed:19383985).
{ECO:0000269|PubMed:19383985, ECO:0000269|PubMed:21602804,
ECO:0000269|PubMed:28068668}.
-!- PTM: Dimethylated by PRMT1 at Arg-260. The methylation may favor
cytoplasmic localization (PubMed:18657504, PubMed:24498420).
Demethylated by JMJD6 at Arg-260 (PubMed:24498420).
{ECO:0000269|PubMed:18657504, ECO:0000269|PubMed:24498420}.
-!- PTM: Palmitoylated (isoform 3). Not biotinylated (isoform 3).
{ECO:0000269|PubMed:22031296}.
-!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required
for plasma membrane targeting and for rapid intracellular signaling via
ERK and AKT kinases and cAMP generation, but not for signaling mediated
by the nuclear hormone receptor. {ECO:0000269|PubMed:22031296}.
-!- POLYMORPHISM: Genetic variations in ESR1 are correlated with bone
mineral density (BMD). Low BMD is a risk factor for osteoporotic
fracture. Osteoporosis is characterized by reduced bone mineral
density, disruption of bone microarchitecture, and the alteration of
the amount and variety of non-collagenous proteins in bone.
Osteoporotic bones are more at risk of fracture.
{ECO:0000269|PubMed:10942433}.
-!- DISEASE: Estrogen resistance (ESTRR) [MIM:615363]: A disorder
characterized by partial or complete resistance to estrogens, in the
presence of elevated estrogen serum levels. Clinical features include
absence of the pubertal growth spurt, delayed bone maturation, unfused
epiphyses, reduced bone mineral density, osteoporosis, continued growth
into adulthood and very tall adult stature. Glucose intolerance,
hyperinsulinemia and lipid abnormalities may also be present.
{ECO:0000269|PubMed:23841731, ECO:0000269|PubMed:27754803}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
-!- MISCELLANEOUS: Selective estrogen receptor modulators (SERMs), such as
tamoxifen, raloxifene, toremifene, lasofoxifene, clomifene, femarelle
and ormeloxifene, have tissue selective agonistic and antagonistic
effects on the estrogen receptor (ER). They interfere with the ER
association with coactivators or corepressors, mainly involving the AF-
2 domain.
-!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
{ECO:0000305}.
-!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
3. {ECO:0000305}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB00115.1; Type=Miscellaneous discrepancy; Note=contains an in-frame duplication of exons 6 and 7.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/esr1/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Estrogen receptor entry;
URL="https://en.wikipedia.org/wiki/Estrogen_receptor";
---------------------------------------------------------------------------
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---------------------------------------------------------------------------
EMBL; X03635; CAA27284.1; -; mRNA.
EMBL; M12674; AAA52399.1; -; mRNA.
EMBL; U47678; AAB00115.1; ALT_SEQ; mRNA.
EMBL; AY425004; AAQ91815.1; -; Genomic_DNA.
EMBL; BX640939; CAE45969.1; -; mRNA.
EMBL; AL049821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL078582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL356311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL590993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW47740.1; -; Genomic_DNA.
EMBL; BC128573; AAI28574.1; -; mRNA.
EMBL; BC128574; AAI28575.1; -; mRNA.
EMBL; AH008151; AAD52984.1; -; Genomic_DNA.
EMBL; X73067; CAA51528.1; -; mRNA.
EMBL; Z75126; CAA99436.1; -; mRNA.
CCDS; CCDS5234.1; -. [P03372-1]
PIR; S64737; S64737.
RefSeq; NP_000116.2; NM_000125.3. [P03372-1]
RefSeq; NP_001116212.1; NM_001122740.1. [P03372-1]
RefSeq; NP_001116213.1; NM_001122741.1. [P03372-1]
RefSeq; NP_001116214.1; NM_001122742.1. [P03372-1]
RefSeq; NP_001278159.1; NM_001291230.1.
RefSeq; NP_001278170.1; NM_001291241.1.
RefSeq; NP_001315029.1; NM_001328100.1.
RefSeq; XP_006715438.1; XM_006715375.3. [P03372-3]
RefSeq; XP_011533845.1; XM_011535543.2. [P03372-1]
RefSeq; XP_011533846.1; XM_011535544.2. [P03372-1]
RefSeq; XP_011533847.1; XM_011535545.2. [P03372-1]
RefSeq; XP_016865865.1; XM_017010376.1. [P03372-1]
RefSeq; XP_016865866.1; XM_017010377.1. [P03372-1]
RefSeq; XP_016865867.1; XM_017010378.1. [P03372-1]
RefSeq; XP_016865868.1; XM_017010379.1. [P03372-1]
RefSeq; XP_016865869.1; XM_017010380.1. [P03372-1]
RefSeq; XP_016865870.1; XM_017010381.1. [P03372-1]
PDB; 1A52; X-ray; 2.80 A; A/B=297-554.
PDB; 1AKF; Model; -; A=309-547.
PDB; 1ERE; X-ray; 3.10 A; A/B/C/D/E/F=301-553.
PDB; 1ERR; X-ray; 2.60 A; A/B=301-553.
PDB; 1G50; X-ray; 2.90 A; A/B/C=304-550.
PDB; 1GWQ; X-ray; 2.45 A; A/B=301-548.
PDB; 1GWR; X-ray; 2.40 A; A/B=305-549.
PDB; 1HCP; NMR; -; A=180-254.
PDB; 1HCQ; X-ray; 2.40 A; A/B/E/F=180-262.
PDB; 1L2I; X-ray; 1.95 A; A/B=297-554.
PDB; 1PCG; X-ray; 2.70 A; A/B=304-547.
PDB; 1QKT; X-ray; 2.20 A; A=304-551.
PDB; 1QKU; X-ray; 3.20 A; A/B/C=301-550.
PDB; 1R5K; X-ray; 2.70 A; A/B/C=297-554.
PDB; 1SJ0; X-ray; 1.90 A; A=307-554.
PDB; 1UOM; X-ray; 2.28 A; A=301-553.
PDB; 1X7E; X-ray; 2.80 A; A/B=305-549.
PDB; 1X7R; X-ray; 2.00 A; A=305-549.
PDB; 1XP1; X-ray; 1.80 A; A=307-554.
PDB; 1XP6; X-ray; 1.70 A; A=307-554.
PDB; 1XP9; X-ray; 1.80 A; A=307-554.
PDB; 1XPC; X-ray; 1.60 A; A=307-554.
PDB; 1XQC; X-ray; 2.05 A; A/B/C/D=301-553.
PDB; 1YIM; X-ray; 1.90 A; A=307-554.
PDB; 1YIN; X-ray; 2.20 A; A=307-554.
PDB; 1ZKY; X-ray; 2.25 A; A/B=298-554.
PDB; 2AYR; X-ray; 1.90 A; A=304-551.
PDB; 2B1V; X-ray; 1.80 A; A/B=298-554.
PDB; 2B1Z; X-ray; 1.78 A; A/B=298-554.
PDB; 2B23; X-ray; 2.10 A; A/B=298-554.
PDB; 2BJ4; X-ray; 2.00 A; A/B=305-533.
PDB; 2FAI; X-ray; 2.10 A; A/B=298-554.
PDB; 2G44; X-ray; 2.65 A; A/B=298-554.
PDB; 2G5O; X-ray; 2.30 A; A/B=298-554.
PDB; 2I0J; X-ray; 2.90 A; A/B/C/D=304-547.
PDB; 2IOG; X-ray; 1.60 A; A=309-554.
PDB; 2IOK; X-ray; 2.40 A; A/B=301-554.
PDB; 2JF9; X-ray; 2.10 A; A/B/C=304-533.
PDB; 2JFA; X-ray; 2.55 A; A/B=304-533.
PDB; 2LLO; NMR; -; B=287-305.
PDB; 2LLQ; NMR; -; B=287-305.
PDB; 2OCF; X-ray; 2.95 A; A=298-595.
PDB; 2OUZ; X-ray; 2.00 A; A=301-553.
PDB; 2P15; X-ray; 1.94 A; A/B=298-554.
PDB; 2POG; X-ray; 1.84 A; A/B=304-551.
PDB; 2Q6J; X-ray; 2.70 A; A/B=298-554.
PDB; 2Q70; X-ray; 1.95 A; A/B=304-551.
PDB; 2QA6; X-ray; 2.60 A; A/B=298-554.
PDB; 2QA8; X-ray; 1.85 A; A/B=298-554.
PDB; 2QAB; X-ray; 1.89 A; A/B=298-554.
PDB; 2QE4; X-ray; 2.40 A; A/B=304-551.
PDB; 2QGT; X-ray; 2.15 A; A/B=298-554.
PDB; 2QGW; X-ray; 2.39 A; A/B=298-554.
PDB; 2QH6; X-ray; 2.70 A; A/B=298-554.
PDB; 2QR9; X-ray; 2.00 A; A/B=298-554.
PDB; 2QSE; X-ray; 1.85 A; A/B=298-554.
PDB; 2QXM; X-ray; 2.30 A; A/B=298-554.
PDB; 2QXS; X-ray; 1.70 A; A/B=298-554.
PDB; 2QZO; X-ray; 1.72 A; A/B=298-554.
PDB; 2R6W; X-ray; 2.00 A; A/B=304-551.
PDB; 2R6Y; X-ray; 2.00 A; A/B=304-551.
PDB; 2YAT; X-ray; 2.60 A; A=301-551.
PDB; 2YJA; X-ray; 1.82 A; B=299-551.
PDB; 3CBM; X-ray; 1.69 A; B=298-307.
PDB; 3CBO; X-ray; 1.65 A; B=298-307.
PDB; 3CBP; X-ray; 1.42 A; B=298-307.
PDB; 3DT3; X-ray; 2.40 A; A/B=299-551.
PDB; 3ERD; X-ray; 2.03 A; A/B=297-554.
PDB; 3ERT; X-ray; 1.90 A; A=297-554.
PDB; 3HLV; X-ray; 3.00 A; A/B=298-550.
PDB; 3HM1; X-ray; 2.33 A; A/B=298-550.
PDB; 3L03; X-ray; 1.90 A; A/B=298-550.
PDB; 3OS8; X-ray; 2.03 A; A/B/C/D=299-553.
PDB; 3OS9; X-ray; 2.30 A; A/B/C/D=299-553.
PDB; 3OSA; X-ray; 2.30 A; A/B/C/D=299-553.
PDB; 3Q95; X-ray; 2.05 A; A/B=298-554.
PDB; 3UU7; X-ray; 2.20 A; A/B=302-552.
PDB; 3UUA; X-ray; 2.05 A; A/B=302-552.
PDB; 3UUC; X-ray; 2.10 A; A/B/C/D=302-552.
PDB; 3UUD; X-ray; 1.60 A; A/B=302-552.
PDB; 4AA6; X-ray; 2.60 A; A/B/E/F=182-252.
PDB; 4DMA; X-ray; 2.30 A; A/B=303-549.
PDB; 4IU7; X-ray; 2.29 A; A/B=303-549.
PDB; 4IUI; X-ray; 2.30 A; A/B=303-549.
PDB; 4IV2; X-ray; 2.14 A; A/B=303-549.
PDB; 4IV4; X-ray; 2.30 A; A/B=303-549.
PDB; 4IVW; X-ray; 2.06 A; A/B=303-549.
PDB; 4IVY; X-ray; 1.95 A; A/B=303-549.
PDB; 4IW6; X-ray; 1.98 A; A/B=303-549.
PDB; 4IW8; X-ray; 2.04 A; A/B=303-549.
PDB; 4IWC; X-ray; 2.24 A; A/B=303-549.
PDB; 4IWF; X-ray; 1.93 A; A/B=303-549.
PDB; 4JC3; X-ray; 2.05 A; B=585-595.
PDB; 4JDD; X-ray; 2.10 A; B=585-595.
PDB; 4MG5; X-ray; 2.05 A; A/B=302-552.
PDB; 4MG6; X-ray; 2.10 A; A/B=302-552.
PDB; 4MG7; X-ray; 2.15 A; A/B=302-552.
PDB; 4MG8; X-ray; 1.85 A; A/B=302-552.
PDB; 4MG9; X-ray; 2.00 A; A/B=302-552.
PDB; 4MGA; X-ray; 1.80 A; A/B=302-552.
PDB; 4MGB; X-ray; 1.85 A; A/B=302-552.
PDB; 4MGC; X-ray; 2.15 A; A/B=302-552.
PDB; 4MGD; X-ray; 1.90 A; A/B=302-552.
PDB; 4O6F; X-ray; 2.82 A; B=261-271.
PDB; 4PP6; X-ray; 2.20 A; A/B=305-548.
PDB; 4PPP; X-ray; 2.69 A; A/B=305-548.
PDB; 4PPS; X-ray; 1.93 A; A/B=305-548.
PDB; 4PXM; X-ray; 1.90 A; A/B=299-554.
PDB; 4Q13; X-ray; 2.24 A; A/B=299-554.
PDB; 4Q50; X-ray; 3.07 A; A/B/C/D/E/F/G/H=299-554.
PDB; 4TUZ; X-ray; 1.90 A; A/B=302-552.
PDB; 4TV1; X-ray; 1.85 A; A/B=302-552.
PDB; 4XI3; X-ray; 2.49 A; A/B/C/D=306-548.
PDB; 4ZN7; X-ray; 1.93 A; A/B=301-559.
PDB; 4ZN9; X-ray; 2.21 A; A/B=301-559.
PDB; 4ZNH; X-ray; 1.93 A; A/B=301-559.
PDB; 4ZNS; X-ray; 1.86 A; A/B=301-559.
PDB; 4ZNT; X-ray; 1.90 A; A/B=301-559.
PDB; 4ZNU; X-ray; 2.40 A; A/B=301-559.
PDB; 4ZNV; X-ray; 1.77 A; A/B=301-559.
PDB; 4ZNW; X-ray; 2.31 A; A/B=301-559.
PDB; 5AAU; X-ray; 1.90 A; A/B=307-554.
PDB; 5AAV; X-ray; 1.95 A; A=307-554, B=306-554.
PDB; 5ACC; X-ray; 1.88 A; A=307-554.
PDB; 5AK2; X-ray; 2.19 A; A/B=307-554.
PDB; 5DI7; X-ray; 2.24 A; A/B=298-554.
PDB; 5DID; X-ray; 2.24 A; A/B=298-554.
PDB; 5DIE; X-ray; 2.24 A; A/B=298-554.
PDB; 5DIG; X-ray; 2.24 A; A/B=298-554.
PDB; 5DK9; X-ray; 2.28 A; A/B=298-554.
PDB; 5DKB; X-ray; 2.40 A; A/B=298-554.
PDB; 5DKE; X-ray; 2.60 A; A/B=298-554.
PDB; 5DKG; X-ray; 2.15 A; A/B=298-554.
PDB; 5DKS; X-ray; 2.60 A; A/B=298-554.
PDB; 5DL4; X-ray; 2.10 A; A/B=298-554.
PDB; 5DLR; X-ray; 2.26 A; A/B=298-554.
PDB; 5DMC; X-ray; 2.40 A; A/B=298-554.
PDB; 5DMF; X-ray; 2.40 A; A/B=298-554.
PDB; 5DP0; X-ray; 2.38 A; A/B=298-554.
PDB; 5DRJ; X-ray; 2.07 A; A/B=298-554.
PDB; 5DRM; X-ray; 2.24 A; A/B=298-554.
PDB; 5DTV; X-ray; 2.29 A; A/B=298-554.
PDB; 5DU5; X-ray; 2.19 A; A/B=298-554.
PDB; 5DUE; X-ray; 2.09 A; A/B=298-554.
PDB; 5DUG; X-ray; 2.25 A; A/B=298-554.
PDB; 5DUH; X-ray; 2.24 A; A/B=298-554.
PDB; 5DVS; X-ray; 2.28 A; A/B=298-554.
PDB; 5DVV; X-ray; 2.50 A; A/B=298-554.
PDB; 5DWE; X-ray; 1.92 A; A/B=298-554.
PDB; 5DWG; X-ray; 2.30 A; A/B=298-554.
PDB; 5DWI; X-ray; 2.43 A; A/B=298-554.
PDB; 5DWJ; X-ray; 2.00 A; A/B=298-554.
PDB; 5DX3; X-ray; 2.09 A; A/B=297-554.
PDB; 5DXB; X-ray; 2.08 A; A/B=297-554.
PDB; 5DXE; X-ray; 1.50 A; A/B=297-554.
PDB; 5DXG; X-ray; 1.86 A; A/B=297-554.
PDB; 5DXK; X-ray; 2.23 A; A/B=298-554.
PDB; 5DXM; X-ray; 2.37 A; A/B=298-554.
PDB; 5DXP; X-ray; 2.20 A; A/B=298-554.
PDB; 5DXQ; X-ray; 2.40 A; A/B=298-554.
PDB; 5DXR; X-ray; 2.28 A; A/B=298-554.
PDB; 5DY8; X-ray; 2.03 A; A/B=298-554.
PDB; 5DYB; X-ray; 2.27 A; A/B=298-554.
PDB; 5DYD; X-ray; 2.48 A; A/B=298-554.
PDB; 5DZ0; X-ray; 2.24 A; A/B=298-554.
PDB; 5DZ1; X-ray; 2.20 A; A/B=298-554.
PDB; 5DZ3; X-ray; 2.15 A; A/B=298-554.
PDB; 5DZH; X-ray; 2.11 A; A/B=298-554.
PDB; 5DZI; X-ray; 1.90 A; A/B=298-554.
PDB; 5E0W; X-ray; 2.00 A; A/B=298-554.
PDB; 5E0X; X-ray; 2.01 A; A/B=298-554.
PDB; 5E14; X-ray; 2.22 A; A/B=298-554.
PDB; 5E15; X-ray; 2.10 A; A/B=298-554.
PDB; 5E19; X-ray; 2.24 A; A/B=298-554.
PDB; 5E1C; X-ray; 1.98 A; A/B=298-554.
PDB; 5EGV; X-ray; 2.86 A; A/B=298-554.
PDB; 5EHJ; X-ray; 2.50 A; A/B=298-554.
PDB; 5EI1; X-ray; 2.40 A; A/B=298-554.
PDB; 5EIT; X-ray; 2.68 A; A/B=298-554.
PDB; 5FQP; X-ray; 1.88 A; A=307-554.
PDB; 5FQR; X-ray; 1.88 A; A=307-554.
PDB; 5FQS; X-ray; 1.94 A; A=307-554.
PDB; 5FQT; X-ray; 1.99 A; A=307-554.
PDB; 5FQV; X-ray; 1.74 A; A=307-554.
PDB; 5GS4; X-ray; 2.40 A; A=305-547.
PDB; 5GTR; X-ray; 2.80 A; A=305-547.
PDB; 5HYR; X-ray; 2.27 A; A/B=302-559.
PDB; 5JMM; X-ray; 2.10 A; A/B=302-552.
PDB; 5KCC; X-ray; 2.39 A; A/B=298-554, A/B=304-549.
PDB; 5KCD; X-ray; 1.82 A; A/B=298-554, A/B=305-549.
PDB; 5KCE; X-ray; 1.85 A; A/B=298-554, A/B=303-549.
PDB; 5KCF; X-ray; 2.07 A; A/B=298-554, A/B=303-549.
PDB; 5KCT; X-ray; 1.60 A; A/B=298-554, A/B=303-548.
PDB; 5KCU; X-ray; 2.03 A; A/B=298-554, A/B=303-548.
PDB; 5KCW; X-ray; 1.91 A; A/B=303-549, A/B=298-554.
PDB; 5KD9; X-ray; 1.78 A; A/B=298-554, A/B=303-549.
PDB; 5KR9; X-ray; 2.25 A; A/B=298-554.
PDB; 5KRA; X-ray; 2.40 A; A/B/E/F=298-554.
PDB; 5KRC; X-ray; 2.40 A; A/B=298-554.
PDB; 5KRF; X-ray; 2.19 A; A/B=298-554.
PDB; 5KRH; X-ray; 2.24 A; A/B=298-554.
PDB; 5KRI; X-ray; 2.25 A; A/B=298-554.
PDB; 5KRJ; X-ray; 2.70 A; A/B=298-554.
PDB; 5KRK; X-ray; 2.39 A; A/B=298-554.
PDB; 5KRL; X-ray; 2.40 A; A/B=298-554.
PDB; 5KRM; X-ray; 2.24 A; A/B=298-554.
PDB; 5KRO; X-ray; 2.10 A; A/B=298-554.
PDB; 5N10; X-ray; 1.60 A; C/D/F=584-595.
PDB; 5T0X; NMR; -; B/C=287-305.
PDB; 5T1Z; X-ray; 2.10 A; A/B=298-554.
PDB; 5T92; X-ray; 2.22 A; A/B=301-553.
PDB; 5T97; X-ray; 3.00 A; A/B=301-553.
PDB; 5TLD; X-ray; 2.38 A; A/B=298-554.
PDB; 5TLF; X-ray; 2.20 A; A/B=298-554.
PDB; 5TLG; X-ray; 2.23 A; A/B=298-554.
PDB; 5TLL; X-ray; 2.42 A; A/B=298-554.
PDB; 5TLM; X-ray; 2.50 A; A/B=298-554.
PDB; 5TLO; X-ray; 2.28 A; A/B=298-554.
PDB; 5TLP; X-ray; 2.08 A; A/B=298-554.
PDB; 5TLT; X-ray; 1.90 A; A/B=298-554.
PDB; 5TLU; X-ray; 2.22 A; A/B=298-554.
PDB; 5TLV; X-ray; 2.32 A; A/B=298-554.
PDB; 5TLX; X-ray; 2.10 A; A/B=298-554.
PDB; 5TLY; X-ray; 2.14 A; A/B=298-554.
PDB; 5TM1; X-ray; 2.23 A; A/B=298-554.
PDB; 5TM2; X-ray; 2.60 A; A/B=298-554.
PDB; 5TM3; X-ray; 2.19 A; A/B=298-554.
PDB; 5TM4; X-ray; 2.25 A; A/B=298-554.
PDB; 5TM5; X-ray; 2.24 A; A/B=298-554.
PDB; 5TM6; X-ray; 2.54 A; A/B=298-554.
PDB; 5TM7; X-ray; 2.40 A; A/B=298-554.
PDB; 5TM8; X-ray; 1.99 A; A/B=298-554.
PDB; 5TM9; X-ray; 2.50 A; A/B=298-554.
PDB; 5TML; X-ray; 2.25 A; A/B=298-554.
PDB; 5TMM; X-ray; 2.20 A; A/B=298-554.
PDB; 5TMO; X-ray; 2.17 A; A/B=298-554.
PDB; 5TMQ; X-ray; 2.24 A; A/B=298-554.
PDB; 5TMR; X-ray; 2.30 A; A/B=298-554.
PDB; 5TMS; X-ray; 2.24 A; A/B=298-554.
PDB; 5TMT; X-ray; 2.05 A; A/B=298-554.
PDB; 5TMU; X-ray; 2.43 A; A/B=298-554.
PDB; 5TMV; X-ray; 2.38 A; A/B=298-554.
PDB; 5TMW; X-ray; 2.29 A; A/B=298-554.
PDB; 5TMZ; X-ray; 2.21 A; A/B=298-554.
PDB; 5TN1; X-ray; 2.06 A; A/B=298-554.
PDB; 5TN3; X-ray; 2.54 A; A/B=298-554.
PDB; 5TN4; X-ray; 1.86 A; A/B=298-554.
PDB; 5TN5; X-ray; 1.89 A; A/B=298-554.
PDB; 5TN6; X-ray; 2.09 A; A/B=298-554.
PDB; 5TN7; X-ray; 2.24 A; A/B=298-554.
PDB; 5TN8; X-ray; 2.65 A; A/B=298-554.
PDB; 5TN9; X-ray; 2.25 A; A/B/C/D=298-554.
PDB; 5TNB; X-ray; 2.08 A; A/B/C/D=298-554.
PDB; 5U2B; X-ray; 2.22 A; A/B/C/D/E/F=298-554.
PDB; 5U2D; X-ray; 1.86 A; A/B=298-554.
PDB; 5UFW; X-ray; 1.58 A; A/B=306-554.
PDB; 5UFX; X-ray; 1.55 A; A/B=306-554.
PDB; 5W9C; X-ray; 1.80 A; A/B/C/D=306-554.
PDB; 5W9D; X-ray; 1.65 A; A/B=306-554.
PDB; 5WGD; X-ray; 1.80 A; A/B=297-554.
PDB; 5WGQ; X-ray; 2.30 A; A/B=297-554.
PDB; 6B0F; X-ray; 2.86 A; A/B=301-553.
PDB; 6C42; X-ray; 2.00 A; A/B=307-554.
PDB; 6CBZ; X-ray; 1.65 A; A/B=305-554.
PDB; 6CHW; X-ray; 1.89 A; A=306-551.
PDB; 6CHZ; X-ray; 1.68 A; A=307-554.
PDB; 6CZN; X-ray; 2.50 A; A/B=298-554.
PDB; 6D0F; X-ray; 2.50 A; A/B=305-554.
PDB; 6DF6; X-ray; 2.50 A; A/B/C/D=298-553.
PDB; 6DFN; X-ray; 2.10 A; A/B/C/D=298-553.
PDB; 6HHP; X-ray; 1.80 A; B=588-595.
PDB; 6HKB; X-ray; 1.70 A; B=588-595.
PDB; 6HKF; X-ray; 1.80 A; B=588-595.
PDB; 6HMU; X-ray; 1.20 A; B=588-595.
PDB; 6IAR; X-ray; 1.84 A; A=307-547.
PDB; 6OWC; X-ray; 1.85 A; A/B=298-554.
PDB; 6PET; X-ray; 2.20 A; A/B/C/D=298-553.
PDB; 6PFM; X-ray; 2.84 A; A/D=298-553.
PDB; 6PIT; X-ray; 2.25 A; A/B=297-554.
PDB; 6PSJ; X-ray; 1.80 A; A/B=307-554.
PDB; 6SBO; X-ray; 1.48 A; A/B=297-554.
PDB; 6SQ0; X-ray; 1.77 A; A/B=307-554.
PDB; 6SUO; X-ray; 1.74 A; A/B=307-554.
PDB; 6V87; X-ray; 2.40 A; A/B=307-554.
PDB; 6V8T; X-ray; 2.10 A; A/B=307-554.
PDB; 6VGH; X-ray; 2.10 A; A/B=307-554.
PDB; 6VIG; X-ray; 1.45 A; A/B/C/D=306-554.
PDB; 6VJ1; X-ray; 1.68 A; A/B/D/E=306-554.
PDB; 6VJD; X-ray; 1.80 A; A/B/C/D=307-554.
PDB; 6VMU; X-ray; 1.70 A; A/B/C/D=307-554.
PDB; 6VNN; X-ray; 1.64 A; A/B/C/D=307-554.
PDB; 6VPK; X-ray; 1.70 A; A/B/C/D=306-554.
PDBsum; 1A52; -.
PDBsum; 1AKF; -.
PDBsum; 1ERE; -.
PDBsum; 1ERR; -.
PDBsum; 1G50; -.
PDBsum; 1GWQ; -.
PDBsum; 1GWR; -.
PDBsum; 1HCP; -.
PDBsum; 1HCQ; -.
PDBsum; 1L2I; -.
PDBsum; 1PCG; -.
PDBsum; 1QKT; -.
PDBsum; 1QKU; -.
PDBsum; 1R5K; -.
PDBsum; 1SJ0; -.
PDBsum; 1UOM; -.
PDBsum; 1X7E; -.
PDBsum; 1X7R; -.
PDBsum; 1XP1; -.
PDBsum; 1XP6; -.
PDBsum; 1XP9; -.
PDBsum; 1XPC; -.
PDBsum; 1XQC; -.
PDBsum; 1YIM; -.
PDBsum; 1YIN; -.
PDBsum; 1ZKY; -.
PDBsum; 2AYR; -.
PDBsum; 2B1V; -.
PDBsum; 2B1Z; -.
PDBsum; 2B23; -.
PDBsum; 2BJ4; -.
PDBsum; 2FAI; -.
PDBsum; 2G44; -.
PDBsum; 2G5O; -.
PDBsum; 2I0J; -.
PDBsum; 2IOG; -.
PDBsum; 2IOK; -.
PDBsum; 2JF9; -.
PDBsum; 2JFA; -.
PDBsum; 2LLO; -.
PDBsum; 2LLQ; -.
PDBsum; 2OCF; -.
PDBsum; 2OUZ; -.
PDBsum; 2P15; -.
PDBsum; 2POG; -.
PDBsum; 2Q6J; -.
PDBsum; 2Q70; -.
PDBsum; 2QA6; -.
PDBsum; 2QA8; -.
PDBsum; 2QAB; -.
PDBsum; 2QE4; -.
PDBsum; 2QGT; -.
PDBsum; 2QGW; -.
PDBsum; 2QH6; -.
PDBsum; 2QR9; -.
PDBsum; 2QSE; -.
PDBsum; 2QXM; -.
PDBsum; 2QXS; -.
PDBsum; 2QZO; -.
PDBsum; 2R6W; -.
PDBsum; 2R6Y; -.
PDBsum; 2YAT; -.
PDBsum; 2YJA; -.
PDBsum; 3CBM; -.
PDBsum; 3CBO; -.
PDBsum; 3CBP; -.
PDBsum; 3DT3; -.
PDBsum; 3ERD; -.
PDBsum; 3ERT; -.
PDBsum; 3HLV; -.
PDBsum; 3HM1; -.
PDBsum; 3L03; -.
PDBsum; 3OS8; -.
PDBsum; 3OS9; -.
PDBsum; 3OSA; -.
PDBsum; 3Q95; -.
PDBsum; 3UU7; -.
PDBsum; 3UUA; -.
PDBsum; 3UUC; -.
PDBsum; 3UUD; -.
PDBsum; 4AA6; -.
PDBsum; 4DMA; -.
PDBsum; 4IU7; -.
PDBsum; 4IUI; -.
PDBsum; 4IV2; -.
PDBsum; 4IV4; -.
PDBsum; 4IVW; -.
PDBsum; 4IVY; -.
PDBsum; 4IW6; -.
PDBsum; 4IW8; -.
PDBsum; 4IWC; -.
PDBsum; 4IWF; -.
PDBsum; 4JC3; -.
PDBsum; 4JDD; -.
PDBsum; 4MG5; -.
PDBsum; 4MG6; -.
PDBsum; 4MG7; -.
PDBsum; 4MG8; -.
PDBsum; 4MG9; -.
PDBsum; 4MGA; -.
PDBsum; 4MGB; -.
PDBsum; 4MGC; -.
PDBsum; 4MGD; -.
PDBsum; 4O6F; -.
PDBsum; 4PP6; -.
PDBsum; 4PPP; -.
PDBsum; 4PPS; -.
PDBsum; 4PXM; -.
PDBsum; 4Q13; -.
PDBsum; 4Q50; -.
PDBsum; 4TUZ; -.
PDBsum; 4TV1; -.
PDBsum; 4XI3; -.
PDBsum; 4ZN7; -.
PDBsum; 4ZN9; -.
PDBsum; 4ZNH; -.
PDBsum; 4ZNS; -.
PDBsum; 4ZNT; -.
PDBsum; 4ZNU; -.
PDBsum; 4ZNV; -.
PDBsum; 4ZNW; -.
PDBsum; 5AAU; -.
PDBsum; 5AAV; -.
PDBsum; 5ACC; -.
PDBsum; 5AK2; -.
PDBsum; 5DI7; -.
PDBsum; 5DID; -.
PDBsum; 5DIE; -.
PDBsum; 5DIG; -.
PDBsum; 5DK9; -.
PDBsum; 5DKB; -.
PDBsum; 5DKE; -.
PDBsum; 5DKG; -.
PDBsum; 5DKS; -.
PDBsum; 5DL4; -.
PDBsum; 5DLR; -.
PDBsum; 5DMC; -.
PDBsum; 5DMF; -.
PDBsum; 5DP0; -.
PDBsum; 5DRJ; -.
PDBsum; 5DRM; -.
PDBsum; 5DTV; -.
PDBsum; 5DU5; -.
PDBsum; 5DUE; -.
PDBsum; 5DUG; -.
PDBsum; 5DUH; -.
PDBsum; 5DVS; -.
PDBsum; 5DVV; -.
PDBsum; 5DWE; -.
PDBsum; 5DWG; -.
PDBsum; 5DWI; -.
PDBsum; 5DWJ; -.
PDBsum; 5DX3; -.
PDBsum; 5DXB; -.
PDBsum; 5DXE; -.
PDBsum; 5DXG; -.
PDBsum; 5DXK; -.
PDBsum; 5DXM; -.
PDBsum; 5DXP; -.
PDBsum; 5DXQ; -.
PDBsum; 5DXR; -.
PDBsum; 5DY8; -.
PDBsum; 5DYB; -.
PDBsum; 5DYD; -.
PDBsum; 5DZ0; -.
PDBsum; 5DZ1; -.
PDBsum; 5DZ3; -.
PDBsum; 5DZH; -.
PDBsum; 5DZI; -.
PDBsum; 5E0W; -.
PDBsum; 5E0X; -.
PDBsum; 5E14; -.
PDBsum; 5E15; -.
PDBsum; 5E19; -.
PDBsum; 5E1C; -.
PDBsum; 5EGV; -.
PDBsum; 5EHJ; -.
PDBsum; 5EI1; -.
PDBsum; 5EIT; -.
PDBsum; 5FQP; -.
PDBsum; 5FQR; -.
PDBsum; 5FQS; -.
PDBsum; 5FQT; -.
PDBsum; 5FQV; -.
PDBsum; 5GS4; -.
PDBsum; 5GTR; -.
PDBsum; 5HYR; -.
PDBsum; 5JMM; -.
PDBsum; 5KCC; -.
PDBsum; 5KCD; -.
PDBsum; 5KCE; -.
PDBsum; 5KCF; -.
PDBsum; 5KCT; -.
PDBsum; 5KCU; -.
PDBsum; 5KCW; -.
PDBsum; 5KD9; -.
PDBsum; 5KR9; -.
PDBsum; 5KRA; -.
PDBsum; 5KRC; -.
PDBsum; 5KRF; -.
PDBsum; 5KRH; -.
PDBsum; 5KRI; -.
PDBsum; 5KRJ; -.
PDBsum; 5KRK; -.
PDBsum; 5KRL; -.
PDBsum; 5KRM; -.
PDBsum; 5KRO; -.
PDBsum; 5N10; -.
PDBsum; 5T0X; -.
PDBsum; 5T1Z; -.
PDBsum; 5T92; -.
PDBsum; 5T97; -.
PDBsum; 5TLD; -.
PDBsum; 5TLF; -.
PDBsum; 5TLG; -.
PDBsum; 5TLL; -.
PDBsum; 5TLM; -.
PDBsum; 5TLO; -.
PDBsum; 5TLP; -.
PDBsum; 5TLT; -.
PDBsum; 5TLU; -.
PDBsum; 5TLV; -.
PDBsum; 5TLX; -.
PDBsum; 5TLY; -.
PDBsum; 5TM1; -.
PDBsum; 5TM2; -.
PDBsum; 5TM3; -.
PDBsum; 5TM4; -.
PDBsum; 5TM5; -.
PDBsum; 5TM6; -.
PDBsum; 5TM7; -.
PDBsum; 5TM8; -.
PDBsum; 5TM9; -.
PDBsum; 5TML; -.
PDBsum; 5TMM; -.
PDBsum; 5TMO; -.
PDBsum; 5TMQ; -.
PDBsum; 5TMR; -.
PDBsum; 5TMS; -.
PDBsum; 5TMT; -.
PDBsum; 5TMU; -.
PDBsum; 5TMV; -.
PDBsum; 5TMW; -.
PDBsum; 5TMZ; -.
PDBsum; 5TN1; -.
PDBsum; 5TN3; -.
PDBsum; 5TN4; -.
PDBsum; 5TN5; -.
PDBsum; 5TN6; -.
PDBsum; 5TN7; -.
PDBsum; 5TN8; -.
PDBsum; 5TN9; -.
PDBsum; 5TNB; -.
PDBsum; 5U2B; -.
PDBsum; 5U2D; -.
PDBsum; 5UFW; -.
PDBsum; 5UFX; -.
PDBsum; 5W9C; -.
PDBsum; 5W9D; -.
PDBsum; 5WGD; -.
PDBsum; 5WGQ; -.
PDBsum; 6B0F; -.
PDBsum; 6C42; -.
PDBsum; 6CBZ; -.
PDBsum; 6CHW; -.
PDBsum; 6CHZ; -.
PDBsum; 6CZN; -.
PDBsum; 6D0F; -.
PDBsum; 6DF6; -.
PDBsum; 6DFN; -.
PDBsum; 6HHP; -.
PDBsum; 6HKB; -.
PDBsum; 6HKF; -.
PDBsum; 6HMU; -.
PDBsum; 6IAR; -.
PDBsum; 6OWC; -.
PDBsum; 6PET; -.
PDBsum; 6PFM; -.
PDBsum; 6PIT; -.
PDBsum; 6PSJ; -.
PDBsum; 6SBO; -.
PDBsum; 6SQ0; -.
PDBsum; 6SUO; -.
PDBsum; 6V87; -.
PDBsum; 6V8T; -.
PDBsum; 6VGH; -.
PDBsum; 6VIG; -.
PDBsum; 6VJ1; -.
PDBsum; 6VJD; -.
PDBsum; 6VMU; -.
PDBsum; 6VNN; -.
PDBsum; 6VPK; -.
SMR; P03372; -.
BioGRID; 108403; 749.
CORUM; P03372; -.
DIP; DIP-5965N; -.
ELM; P03372; -.
IntAct; P03372; 1901.
MINT; P03372; -.
STRING; 9606.ENSP00000405330; -.
BindingDB; P03372; -.
ChEMBL; CHEMBL206; -.
DrugBank; DB07567; (2R,3R,4S)-3-(4-HYDROXYPHENYL)-4-METHYL-2-[4-(2-PYRROLIDIN-1-YLETHOXY)PHENYL]CHROMAN-6-OL.
DrugBank; DB07638; (3AS,4R,9BR)-2,2-DIFLUORO-4-(4-HYDROXYPHENYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-8-OL.
DrugBank; DB08737; (3AS,4R,9BR)-4-(4-HYDROXYPHENYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-9-OL.
DrugBank; DB08020; (3AS,4R,9BR)-4-(4-HYDROXYPHENYL)-6-(METHOXYMETHYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-8-OL.
DrugBank; DB07678; (9ALPHA,13BETA,17BETA)-2-[(1Z)-BUT-1-EN-1-YL]ESTRA-1,3,5(10)-TRIENE-3,17-DIOL.
DrugBank; DB07707; (9BETA,11ALPHA,13ALPHA,14BETA,17ALPHA)-11-(METHOXYMETHYL)ESTRA-1(10),2,4-TRIENE-3,17-DIOL.
DrugBank; DB03802; 1-[4-(Octahydro-Pyrido[1,2-a]Pyrazin-2-Yl)-Phenyl]-2-Phenyl-1,2,3,4-Tetrahydro-Isoquinolin-6-Ol.
DrugBank; DB06871; 17-METHYL-17-ALPHA-DIHYDROEQUILENIN.
DrugBank; DB08773; 2-(4-hydroxyphenyl)benzo[b]thiophen-6-ol.
DrugBank; DB08398; 2-Amino-1-methyl-6-phenylimidazo(4,5-b)pyridine.
DrugBank; DB13869; 2-Methoxy-6-{(E)-[(4-methylphenyl)imino]methyl}phenol.
DrugBank; DB04471; 2-Phenyl-1-[4-(2-Piperidin-1-Yl-Ethoxy)-Phenyl]-1,2,3,4-Tetrahydro-Isoquinolin-6-Ol.
DrugBank; DB07708; 3-CHLORO-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL.
DrugBank; DB07712; 3-ETHYL-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL.
DrugBank; DB06898; 4-(2-amino-1-methyl-1H-imidazo[4,5-b]pyridin-6-yl)phenol.
DrugBank; DB08048; 4-(6-HYDROXY-1H-INDAZOL-3-YL)BENZENE-1,3-DIOL.
DrugBank; DB08595; 4-[(1S,2R,5S)-4,4,8-TRIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL.
DrugBank; DB07195; 4-[(1S,2S,5S)-5-(HYDROXYMETHYL)-6,8,9-TRIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL.
DrugBank; DB07086; 4-[(1S,2S,5S)-5-(HYDROXYMETHYL)-8-METHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL.
DrugBank; DB07087; 4-[(1S,2S,5S,9R)-5-(HYDROXYMETHYL)-8,9-DIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL.
DrugBank; DB08047; 4-[1-allyl-7-(trifluoromethyl)-1H-indazol-3-yl]benzene-1,3-diol.
DrugBank; DB06927; [5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-YL]ACETONITRILE.
DrugBank; DB04468; Afimoxifene.
DrugBank; DB01431; Allylestrenol.
DrugBank; DB05233; AP1081.
DrugBank; DB06249; Arzoxifene.
DrugBank; DB06401; Bazedoxifene.
DrugBank; DB01878; Benzophenone.
DrugBank; DB06732; beta-Naphthoflavone.
DrugBank; DB05882; CHF 4227.
DrugBank; DB00269; Chlorotrianisene.
DrugBank; DB00882; Clomifene.
DrugBank; DB02715; Compound 18.
DrugBank; DB02615; Compound 19.
DrugBank; DB03742; Compound 4-D.
DrugBank; DB00286; Conjugated estrogens.
DrugBank; DB05487; Custirsen.
DrugBank; DB01406; Danazol.
DrugBank; DB00304; Desogestrel.
DrugBank; DB00890; Dienestrol.
DrugBank; DB08320; DIETHYL (1R,2S,3R,4S)-5,6-BIS(4-HYDROXYPHENYL)-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2,3-DICARBOXYLATE.
DrugBank; DB00255; Diethylstilbestrol.
DrugBank; DB07932; dimethyl (1R,4S)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]hepta-2,5-diene-2,3-dicarboxylate.
DrugBank; DB00841; Dobutamine.
DrugBank; DB06374; Elacestrant.
DrugBank; DB11219; Enzacamene.
DrugBank; DB02187; Equilin.
DrugBank; DB07933; Erteberel.
DrugBank; DB00783; Estradiol.
DrugBank; DB13952; Estradiol acetate.
DrugBank; DB13953; Estradiol benzoate.
DrugBank; DB13954; Estradiol cypionate.
DrugBank; DB13955; Estradiol dienanthate.
DrugBank; DB13956; Estradiol valerate.
DrugBank; DB01196; Estramustine.
DrugBank; DB04573; Estriol.
DrugBank; DB14641; Estriol tripropionate.
DrugBank; DB00655; Estrone.
DrugBank; DB04574; Estrone sulfate.
DrugBank; DB00977; Ethinylestradiol.
DrugBank; DB00823; Ethynodiol diacetate.
DrugBank; DB00294; Etonogestrel.
DrugBank; DB09086; Eugenol.
DrugBank; DB01185; Fluoxymesterone.
DrugBank; DB00947; Fulvestrant.
DrugBank; DB01645; Genistein.
DrugBank; DB11619; Gestrinone.
DrugBank; DB00756; Hexachlorophene.
DrugBank; DB07931; Hexestrol.
DrugBank; DB11064; Homosalate.
DrugBank; DB06202; Lasofoxifene.
DrugBank; DB00367; Levonorgestrel.
DrugBank; DB00431; Lindane.
DrugBank; DB00603; Medroxyprogesterone acetate.
DrugBank; DB01065; Melatonin.
DrugBank; DB01357; Mestranol.
DrugBank; DB06710; Methyltestosterone.
DrugBank; DB00648; Mitotane.
DrugBank; DB07991; N-[(1R)-3-(4-HYDROXYPHENYL)-1-METHYLPROPYL]-2-(2-PHENYL-1H-INDOL-3-YL)ACETAMIDE.
DrugBank; DB01183; Naloxone.
DrugBank; DB03467; Naringenin.
DrugBank; DB09371; Norethynodrel.
DrugBank; DB00957; Norgestimate.
DrugBank; DB05662; NP-50301.
DrugBank; DB09535; Octocrylene.
DrugBank; DB04938; Ospemifene.
DrugBank; DB01428; Oxybenzone.
DrugBank; DB04930; Permethrin.
DrugBank; DB04824; Phenolphthalein.
DrugBank; DB02746; Phthalic Acid.
DrugBank; DB09369; Polyestradiol phosphate.
DrugBank; DB01708; Prasterone.
DrugBank; DB00396; Progesterone.
DrugBank; DB12450; Propyl Gallate.
DrugBank; DB02757; Pyrazole.
DrugBank; DB04216; Quercetin.
DrugBank; DB04575; Quinestrol.
DrugBank; DB11541; Ractopamine.
DrugBank; DB00481; Raloxifene.
DrugBank; DB02709; Resveratrol.
DrugBank; DB02901; Stanolone.
DrugBank; DB13951; Stanolone acetate.
DrugBank; DB09317; Synthetic Conjugated Estrogens, A.
DrugBank; DB09318; Synthetic Conjugated Estrogens, B.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB05966; TAS-108.
DrugBank; DB00624; Testosterone.
DrugBank; DB13943; Testosterone cypionate.
DrugBank; DB13944; Testosterone enanthate.
DrugBank; DB13946; Testosterone undecanoate.
DrugBank; DB09070; Tibolone.
DrugBank; DB00539; Toremifene.
DrugBank; DB01108; Trilostane.
DrugBank; DB11478; Zeranol.
DrugBank; DB01593; Zinc.
DrugBank; DB14487; Zinc acetate.
DrugBank; DB14533; Zinc chloride.
DrugCentral; P03372; -.
GuidetoPHARMACOLOGY; 620; -.
SwissLipids; SLP:000001568; -.
MoonDB; P03372; Predicted.
GlyConnect; 144; -.
iPTMnet; P03372; -.
PhosphoSitePlus; P03372; -.
SwissPalm; P03372; -.
UniCarbKB; P03372; -.
BioMuta; ESR1; -.
DMDM; 544257; -.
CPTAC; CPTAC-1241; -.
CPTAC; CPTAC-145; -.
EPD; P03372; -.
jPOST; P03372; -.
MassIVE; P03372; -.
PaxDb; P03372; -.
PeptideAtlas; P03372; -.
PRIDE; P03372; -.
ProteomicsDB; 51607; -. [P03372-1]
ProteomicsDB; 51608; -. [P03372-2]
ProteomicsDB; 51609; -. [P03372-3]
ProteomicsDB; 51610; -. [P03372-4]
ABCD; P03372; 5 sequenced antibodies.
Antibodypedia; 739; 3930 antibodies.
DNASU; 2099; -.
Ensembl; ENST00000206249; ENSP00000206249; ENSG00000091831. [P03372-1]
Ensembl; ENST00000338799; ENSP00000342630; ENSG00000091831. [P03372-1]
Ensembl; ENST00000440973; ENSP00000405330; ENSG00000091831. [P03372-1]
Ensembl; ENST00000443427; ENSP00000387500; ENSG00000091831. [P03372-1]
GeneID; 2099; -.
KEGG; hsa:2099; -.
UCSC; uc003qom.5; human. [P03372-1]
CTD; 2099; -.
DisGeNET; 2099; -.
EuPathDB; HostDB:ENSG00000091831.21; -.
GeneCards; ESR1; -.
HGNC; HGNC:3467; ESR1.
HPA; ENSG00000091831; Tissue enhanced (cervix, uterine, endometrium).
MalaCards; ESR1; -.
MIM; 133430; gene.
MIM; 615363; phenotype.
neXtProt; NX_P03372; -.
OpenTargets; ENSG00000091831; -.
Orphanet; 785; Estrogen resistance syndrome.
PharmGKB; PA156; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00940000158133; -.
InParanoid; P03372; -.
KO; K08550; -.
OMA; LHAPANF; -.
OrthoDB; 487299at2759; -.
PhylomeDB; P03372; -.
TreeFam; TF323751; -.
Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
Reactome; R-HSA-8931987; RUNX1 regulates estrogen receptor mediated transcription.
Reactome; R-HSA-8939211; ESR-mediated signaling.
Reactome; R-HSA-8939256; RUNX1 regulates transcription of genes involved in WNT signaling.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
SignaLink; P03372; -.
SIGNOR; P03372; -.
BioGRID-ORCS; 2099; 14 hits in 808 CRISPR screens.
ChiTaRS; ESR1; human.
EvolutionaryTrace; P03372; -.
GeneWiki; Estrogen_receptor_alpha; -.
GenomeRNAi; 2099; -.
Pharos; P03372; Tclin.
PRO; PR:P03372; -.
Proteomes; UP000005640; Chromosome 6.
RNAct; P03372; protein.
Bgee; ENSG00000091831; Expressed in endometrium and 151 other tissues.
ExpressionAtlas; P03372; baseline and differential.
Genevisible; P03372; HS.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
GO; GO:0097550; C:transcriptional preinitiation complex; IDA:CAFA.
GO; GO:0035327; C:transcriptionally active chromatin; IDA:UniProtKB.
GO; GO:0051117; F:ATPase binding; IDA:MGI.
GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:BHF-UCL.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030284; F:estrogen receptor activity; IDA:BHF-UCL.
GO; GO:0030331; F:estrogen receptor binding; IPI:CAFA.
GO; GO:0034056; F:estrogen response element binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; NAS:UniProtKB.
GO; GO:0004879; F:nuclear receptor activity; IDA:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
GO; GO:0017025; F:TBP-class protein binding; IPI:CAFA.
GO; GO:0001093; F:TFIIB-class transcription factor binding; IPI:CAFA.
GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0008209; P:androgen metabolic process; IEA:Ensembl.
GO; GO:0001547; P:antral ovarian follicle growth; IEA:Ensembl.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:BHF-UCL.
GO; GO:0071391; P:cellular response to estrogen stimulus; IEA:Ensembl.
GO; GO:0006338; P:chromatin remodeling; NAS:UniProtKB.
GO; GO:0002064; P:epithelial cell development; IEA:Ensembl.
GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IEA:Ensembl.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:CAFA.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:UniProtKB.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
GO; GO:0060745; P:mammary gland branching involved in pregnancy; IEA:Ensembl.
GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:UniProtKB.
GO; GO:0010863; P:positive regulation of phospholipase C activity; ISS:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IDA:CAFA.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; IEA:Ensembl.
GO; GO:0060523; P:prostate epithelial cord elongation; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0071168; P:protein localization to chromatin; IMP:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IEA:Ensembl.
GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; TAS:Reactome.
GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0030111; P:regulation of Wnt signaling pathway; TAS:Reactome.
GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL.
GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; TAS:ProtInc.
GO; GO:0060065; P:uterus development; IEA:Ensembl.
GO; GO:0060068; P:vagina development; IEA:Ensembl.
DisProt; DP00074; -.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
IDEAL; IID00013; -.
InterPro; IPR035500; NHR-like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR024178; Oest_rcpt/oest-rel_rcp.
InterPro; IPR001292; Oestr_rcpt.
InterPro; IPR024736; Oestrogen-typ_rcpt_final_C_dom.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF12743; ESR1_C; 1.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF02159; Oest_recep; 1.
Pfam; PF00105; zf-C4; 1.
PIRSF; PIRSF500101; ER-a; 1.
PIRSF; PIRSF002527; ER-like_NR; 1.
PRINTS; PR00543; OESTROGENR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative promoter usage; Alternative splicing;
Cell membrane; Cytoplasm; Direct protein sequencing; Disease mutation;
DNA-binding; Glycoprotein; Golgi apparatus; Lipid-binding; Lipoprotein;
Membrane; Metal-binding; Methylation; Nucleus; Palmitate; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Steroid-binding; Transcription;
Transcription regulation; Transmembrane; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1..595
/note="Estrogen receptor"
/id="PRO_0000053618"
DOMAIN 311..547
/note="NR LBD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
DNA_BIND 185..250
/note="Nuclear receptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 185..205
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 221..245
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
REGION 1..184
/note="Modulating (transactivation AF-1); mediates
interaction with MACROD1"
/evidence="ECO:0000269|PubMed:17914104"
REGION 35..174
/note="Interaction with DDX5; self-association"
REGION 35..47
/note="Required for interaction with NCOA1"
REGION 185..310
/note="Mediates interaction with DNTTIP2"
/evidence="ECO:0000269|PubMed:15047147"
REGION 251..310
/note="Hinge"
REGION 262..595
/note="Interaction with AKAP13"
/evidence="ECO:0000269|PubMed:9627117"
REGION 264..595
/note="Self-association"
REGION 311..595
/note="Transactivation AF-2"
MOD_RES 104
/note="Phosphoserine; by CDK2"
/evidence="ECO:0000269|PubMed:10428798"
MOD_RES 106
/note="Phosphoserine; by CDK2"
/evidence="ECO:0000269|PubMed:10428798"
MOD_RES 118
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:14764652"
MOD_RES 167
/note="Phosphoserine; by CK2"
/evidence="ECO:0000269|PubMed:7838153"
MOD_RES 260
/note="Asymmetric dimethylarginine; by PRMT1"
/evidence="ECO:0000269|PubMed:18657504,
ECO:0000269|PubMed:24498420"
MOD_RES 537
/note="Phosphotyrosine; by Tyr-kinases"
/evidence="ECO:0000269|PubMed:7539106"
LIPID 447
/note="S-palmitoyl cysteine"
/evidence="ECO:0000250"
CARBOHYD 10
/note="O-linked (GlcNAc) serine"
/evidence="ECO:0000250"
VAR_SEQ 1..173
/note="Missing (in isoform 3 and isoform 4)"
/evidence="ECO:0000303|PubMed:16165085,
ECO:0000303|PubMed:17974005"
/id="VSP_042460"
VAR_SEQ 255..366
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:3753802"
/id="VSP_003680"
VAR_SEQ 458..595
/note="VYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLL
ILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHL
ATAGSTSSHSLQKYYITGEAEGFPATV -> FTISHVEAKKRILNLHPKIFGNKWFPRV
(in isoform 4)"
/evidence="ECO:0000303|PubMed:16165085,
ECO:0000303|PubMed:17974005"
/id="VSP_042461"
VARIANT 6
/note="H -> Y (in a breast cancer sample; somatic mutation;
dbSNP:rs139960913)"
/evidence="ECO:0000269|PubMed:17224074"
/id="VAR_033028"
VARIANT 77
/note="G -> S (in dbSNP:rs9340773)"
/id="VAR_018905"
VARIANT 160
/note="G -> C (in dbSNP:rs149308960)"
/evidence="ECO:0000269|PubMed:9195227"
/id="VAR_004671"
VARIANT 264
/note="M -> I (in a breast cancer sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:17224074"
/id="VAR_033029"
VARIANT 375
/note="Q -> H (in ESTRR; results in highly reduced
activity; dbSNP:rs397509428)"
/evidence="ECO:0000269|PubMed:23841731"
/id="VAR_070072"
VARIANT 394
/note="R -> H (in ESTRR; highly decreased estrogen receptor
activity; dbSNP:rs1131692059)"
/evidence="ECO:0000269|PubMed:27754803"
/id="VAR_078516"
VARIANT 400
/note="G -> V (destabilizes the receptor and decreases its
affinity for estradiol at 25 degrees Celsius, but not at 4
degrees Celsius)"
/evidence="ECO:0000269|PubMed:2792078,
ECO:0000269|PubMed:3753802, ECO:0000269|PubMed:3754034"
/id="VAR_004673"
VARIANT 411
/note="D -> RNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGV
YTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHM
(in a 80 kDa form found in a breast cancer line; contains
an in-frame duplication of exons 6 and 7)"
/id="VAR_010143"
MUTAGEN 39
/note="L->P: Impairs AF-1 transactivation."
/evidence="ECO:0000269|PubMed:11075817"
MUTAGEN 43
/note="Y->P: Impairs AF-1 transactivation."
/evidence="ECO:0000269|PubMed:11075817"
MUTAGEN 104
/note="S->A: Loss of cyclin A-dependent induction of
transcriptional activation."
MUTAGEN 106
/note="S->A: Loss of cyclin A-dependent induction of
transcriptional activation."
MUTAGEN 118
/note="S->A: Decreases phosphorylation and transactivation
activity. Abolishes AF-1 transactivation. Insensitive to
PPP5C inhibition of transactivation activity."
/evidence="ECO:0000269|PubMed:10409727,
ECO:0000269|PubMed:14764652"
MUTAGEN 118
/note="S->E: Enhances transactivation activity. Enhances
interaction with DDX5. Insensitive to PPP5C inhibition of
transactivation activity."
/evidence="ECO:0000269|PubMed:10409727,
ECO:0000269|PubMed:14764652"
MUTAGEN 260
/note="R->A,K: Loss of methylation."
/evidence="ECO:0000269|PubMed:18657504"
MUTAGEN 364
/note="V->E: Has higher transcriptional activity in the
absence of wild type ER. Inhibits transcriptional activity
when coexpressed with the wild type receptor."
/evidence="ECO:0000269|PubMed:8961262"
MUTAGEN 386
/note="I->C: Loss of transmembrane localization, no effect
on peripheral membrane localization. Impairs activation of
estrogen-induced activation of NOS3 and production of
nitric oxide. No effect on binding to ERES."
/evidence="ECO:0000269|PubMed:21937726"
MUTAGEN 447
/note="C->A: Loss of hormone binding capacity and
temperature-sensitive loss in DNA-binding."
/evidence="ECO:0000269|PubMed:1577818"
MUTAGEN 539
/note="L->A: Abolishes interaction with NCOA1, NCOA2 and
NCOA3."
/evidence="ECO:0000269|PubMed:12554772"
CONFLICT 452
/note="I -> L (in Ref. 5; CAE45969)"
/evidence="ECO:0000305"
TURN 186..188
/evidence="ECO:0000244|PDB:1HCQ"
STRAND 189..191
/evidence="ECO:0000244|PDB:1HCP"
STRAND 194..196
/evidence="ECO:0000244|PDB:1HCQ"
STRAND 199..201
/evidence="ECO:0000244|PDB:1HCQ"
HELIX 203..213
/evidence="ECO:0000244|PDB:1HCQ"
STRAND 222..225
/evidence="ECO:0000244|PDB:1HCQ"
TURN 231..236
/evidence="ECO:0000244|PDB:1HCQ"
HELIX 238..248
/evidence="ECO:0000244|PDB:1HCQ"
HELIX 288..291
/evidence="ECO:0000244|PDB:2LLO"
HELIX 302..304
/evidence="ECO:0000244|PDB:3Q95"
HELIX 307..309
/evidence="ECO:0000244|PDB:6SBO"
HELIX 312..322
/evidence="ECO:0000244|PDB:6SBO"
STRAND 330..332
/evidence="ECO:0000244|PDB:2YJA"
STRAND 334..336
/evidence="ECO:0000244|PDB:2QZO"
HELIX 339..363
/evidence="ECO:0000244|PDB:6SBO"
HELIX 367..369
/evidence="ECO:0000244|PDB:6SBO"
HELIX 372..395
/evidence="ECO:0000244|PDB:6SBO"
STRAND 396..398
/evidence="ECO:0000244|PDB:2QE4"
STRAND 401..405
/evidence="ECO:0000244|PDB:6SBO"
STRAND 408..411
/evidence="ECO:0000244|PDB:6SBO"
HELIX 412..417
/evidence="ECO:0000244|PDB:6SBO"
STRAND 418..420
/evidence="ECO:0000244|PDB:5KCW"
HELIX 421..438
/evidence="ECO:0000244|PDB:6SBO"
HELIX 442..455
/evidence="ECO:0000244|PDB:6SBO"
HELIX 458..460
/evidence="ECO:0000244|PDB:6SBO"
HELIX 466..492
/evidence="ECO:0000244|PDB:6SBO"
HELIX 497..527
/evidence="ECO:0000244|PDB:6SBO"
STRAND 528..530
/evidence="ECO:0000244|PDB:1XPC"
STRAND 531..533
/evidence="ECO:0000244|PDB:2OUZ"
HELIX 537..544
/evidence="ECO:0000244|PDB:6SBO"
HELIX 547..549
/evidence="ECO:0000244|PDB:6SUO"
HELIX 588..590
/evidence="ECO:0000244|PDB:5N10"
SEQUENCE 595 AA; 66216 MW; 5455C57AB0CCCAA7 CRC64;
MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKIPLERPLG EVYLDSSKPA VYNYPEGAAY
EFNAAAAANA QVYGQTGLPY GPGSEAAAFG SNGLGGFPPL NSVSPSPLML LHPPPQLSPF
LQPHGQQVPY YLENEPSGYT VREAGPPAFY RPNSDNRRQG GRERLASTND KGSMAMESAK
ETRYCAVCND YASGYHYGVW SCEGCKAFFK RSIQGHNDYM CPATNQCTID KNRRKSCQAC
RLRKCYEVGM MKGGIRKDRR GGRMLKHKRQ RDDGEGRGEV GSAGDMRAAN LWPSPLMIKR
SKKNSLALSL TADQMVSALL DAEPPILYSE YDPTRPFSEA SMMGLLTNLA DRELVHMINW
AKRVPGFVDL TLHDQVHLLE CAWLEILMIG LVWRSMEHPG KLLFAPNLLL DRNQGKCVEG
MVEIFDMLLA TSSRFRMMNL QGEEFVCLKS IILLNSGVYT FLSSTLKSLE EKDHIHRVLD
KITDTLIHLM AKAGLTLQQQ HQRLAQLLLI LSHIRHMSNK GMEHLYSMKC KNVVPLYDLL
LEMLDAHRLH APTSRGGASV EETDQSHLAT AGSTSSHSLQ KYYITGEAEG FPATV


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[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
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[Esr1 Esr Estr Nr3a1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
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[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (Fragment)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (Fragment)
[ESR2 ESTRB NR3A2] Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)
[Esr2 Erbeta Nr3a2] Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)
[Esr2 Estrb Nr3a2] Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)
[ESRRA ERR1 ESRL1 NR3B1] Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[Esrra Err1 Estrra Nr3b1] Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[Esrra Nr3b1] Steroid hormone receptor ERR1 (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[Esrrb Err-2 Err2 Nr3b2] Steroid hormone receptor ERR2 (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2)
[ESRRB ERRB2 ESRL2 NR3B2] Steroid hormone receptor ERR2 (ERR beta-2) (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2)
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[Esrrb Err2 Esrl2 Nr3b2] Steroid hormone receptor ERR2 (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2)
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[AR DHTR NR3C4] Androgen receptor (Dihydrotestosterone receptor) (Nuclear receptor subfamily 3 group C member 4)
[NR1D2] Nuclear receptor subfamily 1 group D member 2 (Orphan nuclear hormone receptor BD73) (Rev-erb alpha-related receptor) (RVR) (Rev-erb-beta) (V-erbA-related protein 1-related) (EAR-1R)
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Bibliography :
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