ESR1_HUMAN
ID ESR1_HUMAN Reviewed; 595 AA.
AC P03372; Q13511; Q14276; Q5T5H7; Q6MZQ9; Q9NU51; Q9UDZ7; Q9UIS7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 282.
DE RecName: Full=Estrogen receptor;
DE Short=ER;
DE AltName: Full=ER-alpha;
DE AltName: Full=Estradiol receptor;
DE AltName: Full=Nuclear receptor subfamily 3 group A member 1;
GN Name=ESR1; Synonyms=ESR, NR3A1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-400.
RX PubMed=3754034; DOI=10.1038/320134a0;
RA Green S., Walter P., Kumar V., Krust A., Bornert J.-M., Argos P.,
RA Chambon P.;
RT "Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-
RT A.";
RL Nature 320:134-139(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-400.
RX PubMed=3753802; DOI=10.1126/science.3753802;
RA Greene G.L., Gilna P., Waterfield M., Baker A., Hort Y., Shine J.;
RT "Sequence and expression of human estrogen receptor complementary DNA.";
RL Science 231:1150-1154(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=8600466; DOI=10.1093/nar/24.5.962;
RA Pink J.J., Wu S.Q., Wolf D.M., Bilimoria M.M., Jordan V.C.;
RT "A novel 80 kDa human estrogen receptor containing a duplication of exons 6
RT and 7.";
RL Nucleic Acids Res. 24:962-969(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE PROMOTER USAGE, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Placenta;
RX PubMed=16165085; DOI=10.1016/j.bbrc.2005.08.226;
RA Wang Z., Zhang X., Shen P., Loggie B.W., Chang Y., Deuel T.F.;
RT "Identification, cloning, and expression of human estrogen receptor-
RT alpha36, a novel variant of human estrogen receptor-alpha66.";
RL Biochem. Biophys. Res. Commun. 336:1023-1027(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 110-117, PHOSPHORYLATION, AND MUTAGENESIS.
RX PubMed=7476978; DOI=10.1210/mend.9.8.7476978;
RA Joel P.B., Traish A.M., Lannigan D.A.;
RT "Estradiol and phorbol ester cause phosphorylation of serine 118 in the
RT human estrogen receptor.";
RL Mol. Endocrinol. 9:1041-1052(1995).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 152-595 (ISOFORM 1).
RX PubMed=10619354; DOI=10.1016/s0960-0760(99)00126-0;
RA Schubert E.L., Lee M.K., Newman B., King M.C.;
RT "Single nucleotide polymorphisms (SNPs) in the estrogen receptor gene and
RT breast cancer susceptibility.";
RL J. Steroid Biochem. Mol. Biol. 71:21-27(1999).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 216-434 (ISOFORM 2).
RC TISSUE=Mammary carcinoma;
RX PubMed=7916651;
RA Pfeffer U., Fecarotta E., Castagnetta L., Vidali G.;
RT "Estrogen receptor variant messenger RNA lacking exon 4 in estrogen-
RT responsive human breast cancer cell lines.";
RL Cancer Res. 53:741-743(1993).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 354-548.
RC TISSUE=Mammary carcinoma;
RA Naundorf H., Becker M., Fiebig C., Buettner B., Fichtner I.;
RT "Mechanisms of acquired tamoxifen resistance in a xenotransplanted human
RT breast carcinoma.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP PROTEIN SEQUENCE OF 532-542, AND PHOSPHORYLATION AT TYR-537.
RX PubMed=7539106; DOI=10.1210/mend.9.1.7539106;
RA Arnold S.F., Obourn J.D., Jaffe H., Notides A.C.;
RT "Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and
RT by src family tyrosine kinases in vitro.";
RL Mol. Endocrinol. 9:24-33(1995).
RN [15]
RP MUTAGENESIS OF CYS-447.
RX PubMed=1577818; DOI=10.1016/s0021-9258(19)50174-0;
RA Reese J.C., Katzenellenbogen B.S.;
RT "Characterization of a temperature-sensitive mutation in the hormone
RT binding domain of the human estrogen receptor. Studies in cell extracts and
RT intact cells and their implications for hormone-dependent transcriptional
RT activation.";
RL J. Biol. Chem. 267:9868-9873(1992).
RN [16]
RP INTERACTION WITH GTF2B.
RX PubMed=1517211; DOI=10.1016/s0021-9258(19)37087-5;
RA Ing N.H., Beekman J.M., Tsai S.Y., Tsai M.J., O'Malley B.W.;
RT "Members of the steroid hormone receptor superfamily interact with TFIIB
RT (S300-II).";
RL J. Biol. Chem. 267:17617-17623(1992).
RN [17]
RP PHOSPHORYLATION AT SER-167 BY CK2.
RX PubMed=7838153; DOI=10.1210/mend.8.9.7838153;
RA Arnold S.F., Obourn J.D., Jaffe H., Notides A.C.;
RT "Serine 167 is the major estradiol-induced phosphorylation site on the
RT human estrogen receptor.";
RL Mol. Endocrinol. 8:1208-1214(1994).
RN [18]
RP FUNCTION IN TRANSREPRESSION OF NF-KAPPA-B.
RX PubMed=7651415; DOI=10.1128/mcb.15.9.4971;
RA Stein B., Yang M.X.;
RT "Repression of the interleukin-6 promoter by estrogen receptor is mediated
RT by NF-kappa B and C/EBP beta.";
RL Mol. Cell. Biol. 15:4971-4979(1995).
RN [19]
RP MUTAGENESIS OF VAL-364.
RX PubMed=8961262; DOI=10.1210/mend.10.12.8961262;
RA McInerney E.M., Ince B.A., Shapiro D.J., Katzenellenbogen B.S.;
RT "A transcriptionally active estrogen receptor mutant is a novel type of
RT dominant negative inhibitor of estrogen action.";
RL Mol. Endocrinol. 10:1519-1526(1996).
RN [20]
RP RETRACTED PAPER.
RX PubMed=10409727; DOI=10.1128/mcb.19.8.5363;
RA Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H.,
RA Yanagisawa J., Metzger D., Hashimoto S., Kato S.;
RT "Purification and identification of p68 RNA helicase acting as a
RT transcriptional coactivator specific for the activation function 1 of human
RT estrogen receptor alpha.";
RL Mol. Cell. Biol. 19:5363-5372(1999).
RN [21]
RP RETRACTION NOTICE OF PUBMED:10409727.
RX PubMed=24509260; DOI=10.1128/mcb.01458-13;
RA Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H.,
RA Yanagisawa J., Metzger D., Hashimoto S., Kato S.;
RL Mol. Cell. Biol. 34:915-915(2014).
RN [22]
RP FUNCTION (ISOFORM 3), TISSUE SPECIFICITY, ALTERNATIVE PROMOTER USAGE
RP (ISOFORM 3), AND SUBUNIT.
RX PubMed=10970861; DOI=10.1093/emboj/19.17.4688;
RA Flouriot G., Brand H., Denger S., Metivier R., Kos M., Reid G.,
RA Sonntag-Buck V., Gannon F.;
RT "Identification of a new isoform of the human estrogen receptor-alpha (hER-
RT alpha) that is encoded by distinct transcripts and that is able to repress
RT hER-alpha activation function 1.";
RL EMBO J. 19:4688-4700(2000).
RN [23]
RP MUTAGENESIS OF LEU-39 AND TYR-43.
RX PubMed=11075817; DOI=10.1210/mend.14.11.0546;
RA Metivier R., Petit F.G., Valotaire Y., Pakdel F.;
RT "Function of N-terminal transactivation domain of the estrogen receptor
RT requires a potential alpha-helical structure and is negatively regulated by
RT the A domain.";
RL Mol. Endocrinol. 14:1849-1871(2000).
RN [24]
RP INTERACTION WITH NCOA1; NCOA2 AND NCOA3, SUBUNIT, AND MUTAGENESIS OF
RP LEU-539.
RX PubMed=12554772; DOI=10.1210/me.2002-0351;
RA Bai Y., Giguere V.;
RT "Isoform-selective interactions between estrogen receptors and steroid
RT receptor coactivators promoted by estradiol and ErbB-2 signaling in living
RT cells.";
RL Mol. Endocrinol. 17:589-599(2003).
RN [25]
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), AND PALMITOYLATION (ISOFORM 3).
RX PubMed=12682286; DOI=10.1073/pnas.0831079100;
RA Li L., Haynes M.P., Bender J.R.;
RT "Plasma membrane localization and function of the estrogen receptor alpha
RT variant (ER46) in human endothelial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4807-4812(2003).
RN [26]
RP GLYCOSYLATION.
RX PubMed=8999954; DOI=10.1074/jbc.272.4.2421;
RA Jiang M.S., Hart G.W.;
RT "A subpopulation of estrogen receptors are modified by O-linked N-
RT acetylglucosamine.";
RL J. Biol. Chem. 272:2421-2428(1997).
RN [27]
RP FUNCTION, AND INTERACTION WITH SP1.
RX PubMed=9328340; DOI=10.1210/mend.11.11.9916;
RA Porter W., Saville B., Hoivik D., Safe S.;
RT "Functional synergy between the transcription factor Sp1 and the estrogen
RT receptor.";
RL Mol. Endocrinol. 11:1569-1580(1997).
RN [28]
RP INTERACTION WITH AKAP13.
RX PubMed=9627117; DOI=10.1038/sj.onc.1201783;
RA Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O., Pagliai K.,
RA Gray K., Gutkind S., Segars J.;
RT "Characterization of Brx, a novel Dbl family member that modulates estrogen
RT receptor action.";
RL Oncogene 16:2513-2526(1998).
RN [29]
RP PHOSPHORYLATION AT SER-104 AND SER-106, AND MUTAGENESIS OF SER-104 AND
RP SER-106.
RX PubMed=10428798; DOI=10.1074/jbc.274.32.22296;
RA Rogatsky I., Trowbridge J.M., Garabedian M.J.;
RT "Potentiation of human estrogen receptor alpha transcriptional activation
RT through phosphorylation of serines 104 and 106 by the cyclin A-CDK2
RT complex.";
RL J. Biol. Chem. 274:22296-22302(1999).
RN [30]
RP INTERACTION WITH NCOA6.
RX PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
RA Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K.,
RA Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H.,
RA Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
RT "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator
RT essential for ligand-dependent transactivation by nuclear receptors in
RT vivo.";
RL J. Biol. Chem. 274:34283-34293(1999).
RN [31]
RP INTERACTION WITH PHB2.
RX PubMed=10359819; DOI=10.1073/pnas.96.12.6947;
RA Montano M.M., Ekena K., Delage-Mourroux R., Chang W., Martini P.,
RA Katzenellenbogen B.S.;
RT "An estrogen receptor-selective coregulator that potentiates the
RT effectiveness of antiestrogens and represses the activity of estrogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6947-6952(1999).
RN [32]
RP INTERACTION WITH NCOA2.
RX PubMed=11265755; DOI=10.1093/embo-reports/kvd028;
RA Benecke A., Chambon P., Gronemeyer H.;
RT "Synergy between estrogen receptor alpha activation functions AF1 and AF2
RT mediated by transcription intermediary factor TIF2.";
RL EMBO Rep. 1:151-157(2000).
RN [33]
RP FUNCTION, AND INTERACTION WITH SP1.
RX PubMed=10681512; DOI=10.1074/jbc.275.8.5379;
RA Saville B., Wormke M., Wang F., Nguyen T., Enmark E., Kuiper G.,
RA Gustafsson J.A., Safe S.;
RT "Ligand-, cell-, and estrogen receptor subtype (alpha/beta)-dependent
RT activation at GC-rich (Sp1) promoter elements.";
RL J. Biol. Chem. 275:5379-5387(2000).
RN [34]
RP FUNCTION, AND INTERACTION WITH SP3.
RX PubMed=10816575; DOI=10.1074/jbc.m002188200;
RA Stoner M., Wang F., Wormke M., Nguyen T., Samudio I., Vyhlidal C.,
RA Marme D., Finkenzeller G., Safe S.;
RT "Inhibition of vascular endothelial growth factor expression in HEC1A
RT endometrial cancer cells through interactions of estrogen receptor alpha
RT and Sp3 proteins.";
RL J. Biol. Chem. 275:22769-22779(2000).
RN [35]
RP INTERACTION WITH CITED1 AND EP300.
RX PubMed=11581164; DOI=10.1101/gad.906301;
RA Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y., Kato S.,
RA Isselbacher K.J., Brown M., Shioda T.;
RT "Selective coactivation of estrogen-dependent transcription by CITED1
RT CBP/p300-binding protein.";
RL Genes Dev. 15:2598-2612(2001).
RN [36]
RP FUNCTION, AND INTERACTION WITH JUN; JUNB AND JUND.
RX PubMed=11477071; DOI=10.1074/jbc.m101806200;
RA Teyssier C., Belguise K., Galtier F., Chalbos D.;
RT "Characterization of the physical interaction between estrogen receptor
RT alpha and JUN proteins.";
RL J. Biol. Chem. 276:36361-36369(2001).
RN [37]
RP INTERACTION WITH KDM5A.
RX PubMed=11358960; DOI=10.1074/jbc.m100313200;
RA Chan S.W., Hong W.;
RT "Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone
RT receptor-mediated transcription.";
RL J. Biol. Chem. 276:28402-28412(2001).
RN [38]
RP INTERACTION WITH PELP1.
RX PubMed=11481323; DOI=10.1074/jbc.m103783200;
RA Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A.,
RA Kumar R.;
RT "Molecular cloning and characterization of PELP1, a novel human coregulator
RT of estrogen receptor alpha.";
RL J. Biol. Chem. 276:38272-38279(2001).
RN [39]
RP INTERACTION WITH NCOA5.
RX PubMed=11113208; DOI=10.1128/mcb.21.1.343-353.2001;
RA Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F., Giguere V.;
RT "CIA, a novel estrogen receptor coactivator with a bifunctional nuclear
RT receptor interacting determinant.";
RL Mol. Cell. Biol. 21:343-353(2001).
RN [40]
RP FUNCTION, AND INTERACTION WITH NCOA1 AND DDX5.
RX PubMed=11682626; DOI=10.1210/mend.15.11.0727;
RA Metivier R., Penot G., Flouriot G., Pakdel F.;
RT "Synergism between ERalpha transactivation function 1 (AF-1) and AF-2
RT mediated by steroid receptor coactivator protein-1: requirement for the AF-
RT 1 alpha-helical core and for a direct interaction between the N- and C-
RT terminal domains.";
RL Mol. Endocrinol. 15:1953-1970(2001).
RN [41]
RP INTERACTION WITH PRMT2.
RX PubMed=12039952; DOI=10.1074/jbc.m201053200;
RA Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
RT "Identification of protein arginine methyltransferase 2 as a coactivator
RT for estrogen receptor alpha.";
RL J. Biol. Chem. 277:28624-28630(2002).
RN [42]
RP INTERACTION WITH NR2C1.
RX PubMed=12093804; DOI=10.1074/jbc.m203531200;
RA Hu Y.C., Shyr C.R., Che W., Mu X.M., Kim E., Chang C.;
RT "Suppression of estrogen receptor-mediated transcription and cell growth by
RT interaction with TR2 orphan receptor.";
RL J. Biol. Chem. 277:33571-33579(2002).
RN [43]
RP INTERACTION WITH NCOA7.
RX PubMed=11971969; DOI=10.1128/mcb.22.10.3358-3372.2002;
RA Shao W., Halachmi S., Brown M.;
RT "ERAP140, a conserved tissue-specific nuclear receptor coactivator.";
RL Mol. Cell. Biol. 22:3358-3372(2002).
RN [44]
RP INTERACTION WITH RBFOX2.
RX PubMed=11875103; DOI=10.1210/mend.16.3.0787;
RA Norris J.D., Fan D., Sherk A., McDonnell D.P.;
RT "A negative coregulator for the human ER.";
RL Mol. Endocrinol. 16:459-468(2002).
RN [45]
RP RETRACTED PAPER.
RX PubMed=12415108; DOI=10.1073/pnas.192569699;
RA Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
RT "Estrogen receptor-interacting protein that modulates its nongenomic
RT activity-crosstalk with Src/Erk phosphorylation cascade.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002).
RN [46]
RP RETRACTION NOTICE OF PUBMED:12415108.
RX PubMed=19666546; DOI=10.1073/pnas.0908685106;
RA Wong C.W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
RL Proc. Natl. Acad. Sci. U.S.A. 106:14180-14180(2009).
RN [47]
RP INTERACTION WITH SMARD1.
RX PubMed=12917342; DOI=10.1128/mcb.23.17.6210-6220.2003;
RA Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
RT "BAF60a mediates critical interactions between nuclear receptors and the
RT BRG1 chromatin-remodeling complex for transactivation.";
RL Mol. Cell. Biol. 23:6210-6220(2003).
RN [48]
RP INTERACTION WITH DNTTIP2.
RX PubMed=15047147; DOI=10.1016/j.bbrc.2004.02.179;
RA Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M.,
RA Zhu Y.-J.;
RT "ERBP, a novel estrogen receptor binding protein enhancing the activity of
RT estrogen receptor.";
RL Biochem. Biophys. Res. Commun. 317:54-59(2004).
RN [49]
RP FUNCTION.
RX PubMed=15078875; DOI=10.1074/jbc.m402148200;
RA Merot Y., Metivier R., Penot G., Manu D., Saligaut C., Gannon F.,
RA Pakdel F., Kah O., Flouriot G.;
RT "The relative contribution exerted by AF-1 and AF-2 transactivation
RT functions in estrogen receptor alpha transcriptional activity depends upon
RT the differentiation stage of the cell.";
RL J. Biol. Chem. 279:26184-26191(2004).
RN [50]
RP INTERACTION WITH TXNRD1.
RX PubMed=15199063; DOI=10.1074/jbc.m402753200;
RA Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A.,
RA Spyrou G.;
RT "An alternative splicing variant of the selenoprotein thioredoxin reductase
RT is a modulator of estrogen signaling.";
RL J. Biol. Chem. 279:38721-38729(2004).
RN [51]
RP INTERACTION WITH PELP1 AND SRC, AND MUTAGENESIS OF TYR-537.
RX PubMed=14963108; DOI=10.1210/me.2003-0335;
RA Barletta F., Wong C.-W., McNally C., Komm B.S., Katzenellenbogen B.,
RA Cheskis B.J.;
RT "Characterization of the interactions of estrogen receptor and MNAR in the
RT activation of cSrc.";
RL Mol. Endocrinol. 18:1096-1108(2004).
RN [52]
RP FUNCTION, PHOSPHORYLATION AT SER-118, DEPHOSPHORYLATION AT SER-118 BY
RP PPP5C, AND MUTAGENESIS OF SER-118.
RX PubMed=14764652; DOI=10.1210/me.2003-0308;
RA Ikeda K., Ogawa S., Tsukui T., Horie-Inoue K., Ouchi Y., Kato S.,
RA Muramatsu M., Inoue S.;
RT "Protein phosphatase 5 is a negative regulator of estrogen receptor-
RT mediated transcription.";
RL Mol. Endocrinol. 18:1131-1143(2004).
RN [53]
RP FUNCTION IN NF-KAPPA-B TRANSREPRESSION.
RX PubMed=16043358; DOI=10.1016/j.cyto.2004.12.008;
RA Liu H., Liu K., Bodenner D.L.;
RT "Estrogen receptor inhibits interleukin-6 gene expression by disruption of
RT nuclear factor kappaB transactivation.";
RL Cytokine 31:251-257(2005).
RN [54]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DYNLL1.
RX PubMed=15891768; DOI=10.1038/sj.embor.7400417;
RA Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R.,
RA Kumar R.;
RT "Functional regulation of oestrogen receptor pathway by the dynein light
RT chain 1.";
RL EMBO Rep. 6:538-544(2005).
RN [55]
RP ERRATUM OF PUBMED:15891768.
RA Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R.,
RA Kumar R.;
RL EMBO Rep. 6:1101-1101(2005).
RN [56]
RP INTERACTION WITH HEXIM1.
RX PubMed=15940264; DOI=10.1038/sj.onc.1208728;
RA Wittmann B.M., Fujinaga K., Deng H., Ogba N., Montano M.M.;
RT "The breast cell growth inhibitor, estrogen down regulated gene 1,
RT modulates a novel functional interaction between estrogen receptor alpha
RT and transcriptional elongation factor cyclin T1.";
RL Oncogene 24:5576-5588(2005).
RN [57]
RP INTERACTION WITH KMT2D.
RX PubMed=16603732; DOI=10.1074/jbc.m513245200;
RA Mo R., Rao S.M., Zhu Y.-J.;
RT "Identification of the MLL2 complex as a coactivator for estrogen receptor
RT alpha.";
RL J. Biol. Chem. 281:15714-15720(2006).
RN [58]
RP FUNCTION.
RX PubMed=16684779; DOI=10.1074/jbc.m600021200;
RA Rayala S.K., den Hollander P., Manavathi B., Talukder A.H., Song C.,
RA Peng S., Barnekow A., Kremerskothen J., Kumar R.;
RT "Essential role of KIBRA in co-activator function of dynein light chain 1
RT in mammalian cells.";
RL J. Biol. Chem. 281:19092-19099(2006).
RN [59]
RP INTERACTION WITH MUC1.
RX PubMed=16427018; DOI=10.1016/j.molcel.2005.11.030;
RA Wei X., Xu H., Kufe D.;
RT "MUC1 oncoprotein stabilizes and activates estrogen receptor alpha.";
RL Mol. Cell 21:295-305(2006).
RN [60]
RP INTERACTION WITH UBE3A AND WBP2.
RX PubMed=16772533; DOI=10.1210/me.2005-0533;
RA Dhananjayan S.C., Ramamoorthy S., Khan O.Y., Ismail A., Sun J.,
RA Slingerland J., O'Malley B.W., Nawaz Z.;
RT "WW domain binding protein-2, an E6-associated protein interacting protein,
RT acts as a coactivator of estrogen and progesterone receptors.";
RL Mol. Endocrinol. 20:2343-2354(2006).
RN [61]
RP INTERACTION WITH ZNF366.
RX PubMed=17085477; DOI=10.1093/nar/gkl875;
RA Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M., Jat P.,
RA Kindle K.B., Heery D.M., Parker M.G., Buluwela L., Kamalati T., Ali S.;
RT "ZNF366 is an estrogen receptor corepressor that acts through CtBP and
RT histone deacetylases.";
RL Nucleic Acids Res. 34:6126-6136(2006).
RN [62]
RP FUNCTION.
RX PubMed=16617102; DOI=10.1073/pnas.0601989103;
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
RA Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RT "MTA1, a transcriptional activator of breast cancer amplified sequence 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6670-6675(2006).
RN [63]
RP ERRATUM OF PUBMED:16617102.
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
RA Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RL Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013).
RN [64]
RP INTERACTION WITH PBXIP1.
RX PubMed=17043237; DOI=10.1073/pnas.0607445103;
RA Manavathi B., Acconcia F., Rayala S.K., Kumar R.;
RT "An inherent role of microtubule network in the action of nuclear
RT receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15981-15986(2006).
RN [65]
RP INTERACTION WITH MAP1S.
RX PubMed=17658481; DOI=10.1016/j.bbrc.2007.06.179;
RA Eriksson M., Samuelsson H., Samuelsson E.-B., Liu L., McKeehan W.L.,
RA Benedikz E., Sundstroem E.;
RT "The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in
RT the brain.";
RL Biochem. Biophys. Res. Commun. 361:127-132(2007).
RN [66]
RP INTERACTION WITH CUEDC2.
RX PubMed=17347654; DOI=10.1038/sj.emboj.7601602;
RA Zhang P.-J., Zhao J., Li H.-Y., Man J.-H., He K., Zhou T., Pan X.,
RA Li A.-L., Gong W.-L., Jin B.-F., Xia Q., Yu M., Shen B.-F., Zhang X.-M.;
RT "CUE domain containing 2 regulates degradation of progesterone receptor by
RT ubiquitin-proteasome.";
RL EMBO J. 26:1831-1842(2007).
RN [67]
RP INTERACTION WITH MACROD1.
RX PubMed=17914104; DOI=10.1677/erc-06-0082;
RA Han W.-D., Zhao Y.-L., Meng Y.G., Zang L., Wu Z.-Q., Li Q., Si Y.-L.,
RA Huang K., Ba J.-M., Morinaga H., Nomura M., Mu Y.-M.;
RT "Estrogenically regulated LRP16 interacts with estrogen receptor alpha and
RT enhances the receptor's transcriptional activity.";
RL Endocr. Relat. Cancer 14:741-753(2007).
RN [68]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH KIF18A.
RX PubMed=17006958; DOI=10.1002/jcb.21000;
RA Luboshits G., Benayahu D.;
RT "MS-KIF18A, a kinesin, is associated with estrogen receptor.";
RL J. Cell. Biochem. 100:693-702(2007).
RN [69]
RP INTERACTION WITH PRMT2.
RX PubMed=17587566; DOI=10.1016/j.jsbmb.2007.05.006;
RA Meyer R., Wolf S.S., Obendorf M.;
RT "PRMT2, a member of the protein arginine methyltransferase family, is a
RT coactivator of the androgen receptor.";
RL J. Steroid Biochem. Mol. Biol. 107:1-14(2007).
RN [70]
RP INTERACTION WITH BCAS3.
RX PubMed=17505058; DOI=10.1210/me.2006-0514;
RA Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
RT "Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
RT coactivator, through proline-, glutamic acid-, and leucine-rich protein-1
RT (PELP1).";
RL Mol. Endocrinol. 21:1847-1860(2007).
RN [71]
RP INTERACTION WITH UIMC1.
RX PubMed=17311814; DOI=10.1093/nar/gkl1112;
RA Yan J., Kim Y.S., Yang X.-P., Albers M., Koegl M., Jetten A.M.;
RT "Ubiquitin-interaction motifs of RAP80 are critical in its regulation of
RT estrogen receptor alpha.";
RL Nucleic Acids Res. 35:1673-1686(2007).
RN [72]
RP INTERACTION WITH ATAD2.
RX PubMed=17998543; DOI=10.1073/pnas.0705814104;
RA Zou J.X., Revenko A.S., Li L.B., Gemo A.T., Chen H.-W.;
RT "ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is
RT required for coregulator occupancy and chromatin modification.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18067-18072(2007).
RN [73]
RP FUNCTION IN ASSOCIATION WITH AP-1.
RX PubMed=18247370; DOI=10.1002/jcp.21379;
RA Lambertini E., Tavanti E., Torreggiani E., Penolazzi L., Gambari R.,
RA Piva R.;
RT "ERalpha and AP-1 interact in vivo with a specific sequence of the F
RT promoter of the human ERalpha gene in osteoblasts.";
RL J. Cell. Physiol. 216:101-110(2008).
RN [74]
RP METHYLATION AT ARG-260 BY PRMT1, MUTAGENESIS OF ARG-260, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH PI3KR1/2; SRC AND PTK2/FAK1.
RX PubMed=18657504; DOI=10.1016/j.molcel.2008.05.025;
RA Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y., Sentis S.,
RA Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S., Corbo L.;
RT "Regulation of estrogen rapid signaling through arginine methylation by
RT PRMT1.";
RL Mol. Cell 31:212-221(2008).
RN [75]
RP FUNCTION IN NF-KAPPA-B TRANSREPRESSION, AND INTERACTION WITH RELA.
RX PubMed=17932106; DOI=10.1210/me.2007-0324;
RA Nettles K.W., Gil G., Nowak J., Metivier R., Sharma V.B., Greene G.L.;
RT "CBP Is a dosage-dependent regulator of nuclear factor-kappaB suppression
RT by the estrogen receptor.";
RL Mol. Endocrinol. 22:263-272(2008).
RN [76]
RP FUNCTION.
RX PubMed=17922032; DOI=10.1038/sj.onc.1210839;
RA Molli P.R., Singh R.R., Lee S.W., Kumar R.;
RT "MTA1-mediated transcriptional repression of BRCA1 tumor suppressor gene.";
RL Oncogene 27:1971-1980(2008).
RN [77]
RP INTERACTION WITH CCDC62.
RX PubMed=18563714; DOI=10.1002/pros.20774;
RA Chen M., Ni J., Zhang Y., Muyan M., Yeh S.;
RT "ERAP75 functions as a coactivator to enhance estrogen receptor alpha
RT transactivation in prostate stromal cells.";
RL Prostate 68:1273-1282(2008).
RN [78]
RP INTERACTION WITH SH2D4A AND PLCG.
RX PubMed=19712589; DOI=10.5483/bmbrep.2009.42.8.516;
RA Li T., Li W., Lu J., Liu H., Li Y., Zhao Y.;
RT "SH2D4A regulates cell proliferation via the ERalpha/PLC-gamma/PKC
RT pathway.";
RL BMB Rep. 42:516-522(2009).
RN [79]
RP INTERACTION WITH LDB1 AND RLIM.
RX PubMed=19117995; DOI=10.1158/0008-5472.can-08-1630;
RA Johnsen S.A., Guengoer C., Prenzel T., Riethdorf S., Riethdorf L.,
RA Taniguchi-Ishigaki N., Rau T., Tursun B., Furlow J.D., Sauter G.,
RA Scheffner M., Pantel K., Gannon F., Bach I.;
RT "Regulation of estrogen-dependent transcription by the LIM cofactors CLIM
RT and RLIM in breast cancer.";
RL Cancer Res. 69:128-136(2009).
RN [80]
RP INTERACTION WITH DNAAF4.
RX PubMed=19423554; DOI=10.1093/hmg/ddp215;
RA Massinen S., Tammimies K., Tapia-Paez I., Matsson H., Hokkanen M.E.,
RA Soederberg O., Landegren U., Castren E., Gustafsson J.A., Treuter E.,
RA Kere J.;
RT "Functional interaction of DYX1C1 with estrogen receptors suggests
RT involvement of hormonal pathways in dyslexia.";
RL Hum. Mol. Genet. 18:2802-2812(2009).
RN [81]
RP FUNCTION IN MUTUAL TRANSREPRESSION WITH NF-KAPPA-B, AND INTERACTION WITH
RP NFKB1 AND RELA.
RX PubMed=19350539; DOI=10.1002/jcb.22141;
RA Gionet N., Jansson D., Mader S., Pratt M.A.;
RT "NF-kappaB and estrogen receptor alpha interactions: Differential function
RT in estrogen receptor-negative and -positive hormone-independent breast
RT cancer cells.";
RL J. Cell. Biochem. 107:448-459(2009).
RN [82]
RP UBIQUITINATION, AND INTERACTION WITH OTUB1.
RX PubMed=19383985; DOI=10.1074/jbc.m109.007484;
RA Stanisic V., Malovannaya A., Qin J., Lonard D.M., O'Malley B.W.;
RT "OTU Domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1)
RT deubiquitinates estrogen receptor (ER) alpha and affects ERalpha
RT transcriptional activity.";
RL J. Biol. Chem. 284:16135-16145(2009).
RN [83]
RP PHOSPHORYLATION BY CSNK1D/CK1, AND INTERACTION WITH CSNK1D.
RX PubMed=19339517; DOI=10.1093/nar/gkp136;
RA Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J., Thomas R.S.,
RA Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.;
RT "CK1delta modulates the transcriptional activity of ERalpha via AIB1 in an
RT estrogen-dependent manner and regulates ERalpha-AIB1 interactions.";
RL Nucleic Acids Res. 37:3110-3123(2009).
RN [84]
RP INTERACTION WITH DDX17.
RX PubMed=19718048; DOI=10.1038/onc.2009.261;
RA Wortham N.C., Ahamed E., Nicol S.M., Thomas R.S., Periyasamy M., Jiang J.,
RA Ochocka A.M., Shousha S., Huson L., Bray S.E., Coombes R.C., Ali S.,
RA Fuller-Pace F.V.;
RT "The DEAD-box protein p72 regulates ERalpha-/oestrogen-dependent
RT transcription and cell growth, and is associated with improved survival in
RT ERalpha-positive breast cancer.";
RL Oncogene 28:4053-4064(2009).
RN [85]
RP INTERACTION WITH KIF18A.
RX PubMed=19636373; DOI=10.1371/journal.pone.0006407;
RA Zusev M., Benayahu D.;
RT "The regulation of MS-KIF18A expression and cross talk with estrogen
RT receptor.";
RL PLoS ONE 4:E6407-E6407(2009).
RN [86]
RP INTERACTION WITH TACC1.
RX PubMed=20078863; DOI=10.1186/1471-2199-11-3;
RA Guyot R., Vincent S., Bertin J., Samarut J., Ravel-Chapuis P.;
RT "The transforming acidic coiled coil (TACC1) protein modulates the
RT transcriptional activity of the nuclear receptors TR and RAR.";
RL BMC Mol. Biol. 11:3-3(2010).
RN [87]
RP FUNCTION, INTERACTION WITH CCAR2, AND SUBCELLULAR LOCATION.
RX PubMed=20074560; DOI=10.1016/j.bbrc.2010.01.025;
RA Koyama S., Wada-Hiraike O., Nakagawa S., Tanikawa M., Hiraike H.,
RA Miyamoto Y., Sone K., Oda K., Fukuhara H., Nakagawa K., Kato S., Yano T.,
RA Taketani Y.;
RT "Repression of estrogen receptor beta function by putative tumor suppressor
RT DBC1.";
RL Biochem. Biophys. Res. Commun. 392:357-362(2010).
RN [88]
RP FUNCTION IN SYNERGISM WITH NF-KAPPA-B.
RX PubMed=20705611; DOI=10.1074/jbc.m110.155309;
RA Pradhan M., Bembinster L.A., Baumgarten S.C., Frasor J.;
RT "Proinflammatory cytokines enhance estrogen-dependent expression of the
RT multidrug transporter gene ABCG2 through estrogen receptor and NF{kappa}B
RT cooperativity at adjacent response elements.";
RL J. Biol. Chem. 285:31100-31106(2010).
RN [89]
RP INTERACTION WITH ZFHX3.
RX PubMed=20720010; DOI=10.1074/jbc.m110.128330;
RA Dong X.Y., Sun X., Guo P., Li Q., Sasahara M., Ishii Y., Dong J.T.;
RT "ATBF1 inhibits estrogen receptor (ER) function by selectively competing
RT with AIB1 for binding to the ER in ER-positive breast cancer cells.";
RL J. Biol. Chem. 285:32801-32809(2010).
RN [90]
RP INTERACTION WITH ESRRB.
RX PubMed=19755138; DOI=10.1016/j.mce.2009.09.007;
RA Bombail V., Collins F., Brown P., Saunders P.T.;
RT "Modulation of ER alpha transcriptional activity by the orphan nuclear
RT receptor ERR beta and evidence for differential effects of long- and short-
RT form splice variants.";
RL Mol. Cell. Endocrinol. 314:53-61(2010).
RN [91]
RP INTERACTION WITH SAV1 AND STK3/MST2.
RX PubMed=21104395; DOI=10.1007/s00109-010-0698-y;
RA Park Y., Park J., Lee Y., Lim W., Oh B.C., Shin C., Kim W., Lee Y.;
RT "Mammalian MST2 kinase and human Salvador activate and reduce estrogen
RT receptor alpha in the absence of ligand.";
RL J. Mol. Med. 89:181-191(2011).
RN [92]
RP FUNCTION (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM 3), TOPOLOGY (ISOFORM
RP 3), AND MUTAGENESIS OF ILE-386.
RX PubMed=21937726; DOI=10.1091/mbc.e11-05-0416;
RA Kim K.H., Toomre D., Bender J.R.;
RT "Splice isoform estrogen receptors as integral transmembrane proteins.";
RL Mol. Biol. Cell 22:4415-4423(2011).
RN [93]
RP FUNCTION IN ERE-INDEPENDENT SIGNALING.
RX PubMed=21330404; DOI=10.1210/me.2010-0425;
RA Heldring N., Isaacs G.D., Diehl A.G., Sun M., Cheung E., Ranish J.A.,
RA Kraus W.L.;
RT "Multiple sequence-specific DNA-binding proteins mediate estrogen receptor
RT signaling through a tethering pathway.";
RL Mol. Endocrinol. 25:564-574(2011).
RN [94]
RP INTERACTION WITH LMTK3, PHOSPHORYLATION, AND UBIQUITINATION.
RX PubMed=21602804; DOI=10.1038/nm.2351;
RA Giamas G., Filipovic A., Jacob J., Messier W., Zhang H., Yang D., Zhang W.,
RA Shifa B.A., Photiou A., Tralau-Stewart C., Castellano L., Green A.R.,
RA Coombes R.C., Ellis I.O., Ali S., Lenz H.J., Stebbing J.;
RT "Kinome screening for regulators of the estrogen receptor identifies LMTK3
RT as a new therapeutic target in breast cancer.";
RL Nat. Med. 17:715-719(2011).
RN [95]
RP SUBCELLULAR LOCATION, AND PALMITOYLATION.
RX PubMed=22031296; DOI=10.1091/mbc.e11-07-0638;
RA Pedram A., Razandi M., Deschenes R.J., Levin E.R.;
RT "DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors.";
RL Mol. Biol. Cell 23:188-199(2012).
RN [96]
RP FUNCTION IN SYNERGISM WITH NF-KAPPA-B.
RX PubMed=22083956; DOI=10.1128/mcb.05869-11;
RA Pradhan M., Baumgarten S.C., Bembinster L.A., Frasor J.;
RT "CBP mediates NF-kappaB-dependent histone acetylation and estrogen receptor
RT recruitment to an estrogen response element in the BIRC3 promoter.";
RL Mol. Cell. Biol. 32:569-575(2012).
RN [97]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CLOCK.
RX PubMed=23160374; DOI=10.1038/onc.2012.518;
RA Li S., Wang M., Ao X., Chang A.K., Yang C., Zhao F., Bi H., Liu Y.,
RA Xiao L., Wu H.;
RT "CLOCK is a substrate of SUMO and sumoylation of CLOCK upregulates the
RT transcriptional activity of estrogen receptor-alpha.";
RL Oncogene 32:4883-4891(2013).
RN [98]
RP INTERACTION WITH SFR1.
RX PubMed=23874500; DOI=10.1371/journal.pone.0068075;
RA Feng Y., Singleton D., Guo C., Gardner A., Pakala S., Kumar R., Jensen E.,
RA Zhang J., Khan S.;
RT "DNA homologous recombination factor SFR1 physically and functionally
RT interacts with estrogen receptor alpha.";
RL PLoS ONE 8:E68075-E68075(2013).
RN [99]
RP INTERACTION WITH TRIP4.
RX PubMed=25219498; DOI=10.1016/j.molcel.2014.08.007;
RA Yoo H.M., Kang S.H., Kim J.Y., Lee J.E., Seong M.W., Lee S.W., Ka S.H.,
RA Sou Y.S., Komatsu M., Tanaka K., Lee S.T., Noh D.Y., Baek S.H., Jeon Y.J.,
RA Chung C.H.;
RT "Modification of ASC1 by UFM1 is crucial for ERalpha transactivation and
RT breast cancer development.";
RL Mol. Cell 56:261-274(2014).
RN [100]
RP METHYLATION AT ARG-260, DEMETHYLATION AT ARG-260, AND SUBCELLULAR LOCATION.
RX PubMed=24498420; DOI=10.1371/journal.pone.0087982;
RA Poulard C., Rambaud J., Hussein N., Corbo L., Le Romancer M.;
RT "JMJD6 regulates ERalpha methylation on arginine.";
RL PLoS ONE 9:E87982-E87982(2014).
RN [101]
RP INTERACTION WITH DCAF13; LATS1 AND DCAF1, AND UBIQUITINATION.
RX PubMed=28068668; DOI=10.1038/nature20829;
RA Britschgi A., Duss S., Kim S., Couto J.P., Brinkhaus H., Koren S.,
RA De Silva D., Mertz K.D., Kaup D., Varga Z., Voshol H., Vissieres A.,
RA Leroy C., Roloff T., Stadler M.B., Scheel C.H., Miraglia L.J., Orth A.P.,
RA Bonamy G.M., Reddy V.A., Bentires-Alj M.;
RT "The Hippo kinases LATS1 and 2 control human breast cell fate via crosstalk
RT with ERalpha.";
RL Nature 541:541-545(2017).
RN [102]
RP STRUCTURE BY NMR OF 180-262.
RX PubMed=2247153; DOI=10.1038/348458a0;
RA Schwabe J.W.E., Neuhaus D., Rhodes D.;
RT "Solution structure of the DNA-binding domain of the oestrogen receptor.";
RL Nature 348:458-461(1990).
RN [103]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 180-262.
RX PubMed=8221895; DOI=10.1016/0092-8674(93)90390-c;
RA Schwabe J.W.E., Chapman L., Finch J.T., Rhodes D.;
RT "The crystal structure of the estrogen receptor DNA-binding domain bound to
RT DNA: how receptors discriminate between their response elements.";
RL Cell 75:567-578(1993).
RN [104]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 305-548.
RX PubMed=9338790; DOI=10.1038/39645;
RA Brzozowski A.M., Pike A.C.W., Dauter Z., Hubbard R.E., Bonn T.,
RA Engstroem O., Oehman L., Greene G.L., Gustafsson J.-A., Carlquist M.;
RT "Molecular basis of agonism and antagonism in the oestrogen receptor.";
RL Nature 389:753-758(1997).
RN [105]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 306-544.
RX PubMed=9600906; DOI=10.1073/pnas.95.11.5998;
RA Tanenbaum D.M., Wang Y., Williams S.P., Sigler P.B.;
RT "Crystallographic comparison of the estrogen and progesterone receptor's
RT ligand binding domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:5998-6003(1998).
RN [106]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 294-554.
RX PubMed=9875847; DOI=10.1016/s0092-8674(00)81717-1;
RA Shiau A.K., Barstad D., Loria P.M., Cheng L., Kushner P.J., Agard D.A.,
RA Greene G.L.;
RT "The structural basis of estrogen receptor/coactivator recognition and the
RT antagonism of this interaction by tamoxifen.";
RL Cell 95:927-937(1998).
RN [107]
RP 3D-STRUCTURE MODELING OF 311-547.
RX PubMed=9619507; DOI=10.1080/07391102.1998.10508206;
RA Maalouf G.J., Xu W., Smith T., Mohr S.C.;
RT "Homology model for the ligand-binding domain of the human estrogen
RT receptor.";
RL J. Biomol. Struct. Dyn. 15:841-850(1998).
RN [108]
RP VARIANT VAL-400.
RX PubMed=2792078; DOI=10.1002/j.1460-2075.1989.tb03604.x;
RA Tora L., Mullick A., Metzger D., Ponglikitmongkol M., Park I., Chambon P.;
RT "The cloned human oestrogen receptor contains a mutation which alters its
RT hormone binding properties.";
RL EMBO J. 8:1981-1986(1989).
RN [109]
RP VARIANT CYS-160.
RX PubMed=9195227;
RX DOI=10.1002/(sici)1098-1004(1997)9:6<531::aid-humu6>3.0.co;2-4;
RA Anderson T.I., Wooster R., Laake K., Collins N., Warren W., Skrede M.,
RA Eeles R., Tveit K.M., Johnston S.R.D., Dowsett M., Olsen A.O., Moeller P.,
RA Stratton M.R., Boerresen-Dale A.-L.;
RT "Screening for ESR mutations in breast and ovarian cancer patients.";
RL Hum. Mutat. 9:531-536(1997).
RN [110]
RP INVOLVEMENT IN BMD.
RX PubMed=10942433; DOI=10.1093/hmg/9.13.2043;
RA Becherini L., Gennari L., Masi L., Mansani R., Massart F., Morelli A.,
RA Falchetti A., Gonnelli S., Fiorelli G., Tanini A., Brandi M.L.;
RT "Evidence of a linkage disequilibrium between polymorphisms in the human
RT estrogen receptor alpha gene and their relationship to bone mass variation
RT in postmenopausal Italian women.";
RL Hum. Mol. Genet. 9:2043-2050(2000).
RN [111]
RP INTERACTION WITH GPER1.
RX PubMed=19749156; DOI=10.1210/me.2009-0120;
RA Vivacqua A., Lappano R., De Marco P., Sisci D., Aquila S., De Amicis F.,
RA Fuqua S.A., Ando S., Maggiolini M.;
RT "G protein-coupled receptor 30 expression is up-regulated by EGF and TGF
RT alpha in estrogen receptor alpha-positive cancer cells.";
RL Mol. Endocrinol. 23:1815-1826(2009).
RN [112]
RP VARIANTS TYR-6 AND ILE-264.
RX PubMed=17224074; DOI=10.1186/bcr1637;
RA Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S.,
RA Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M.,
RA Boerresen-Dale A.-L.;
RT "Somatic sequence alterations in twenty-one genes selected by expression
RT profile analysis of breast carcinomas.";
RL Breast Cancer Res. 9:R5-R5(2007).
RN [113]
RP VARIANT ESTRR HIS-375, AND CHARACTERIZATION OF VARIANT ESTRR HIS-375.
RX PubMed=23841731; DOI=10.1056/nejmoa1303611;
RA Quaynor S.D., Stradtman E.W. Jr., Kim H.G., Shen Y., Chorich L.P.,
RA Schreihofer D.A., Layman L.C.;
RT "Delayed puberty and estrogen resistance in a woman with estrogen receptor
RT alpha variant.";
RL N. Engl. J. Med. 369:164-171(2013).
RN [114]
RP VARIANT ESTRR HIS-394, AND CHARACTERIZATION OF VARIANT ESTRR HIS-394.
RX PubMed=27754803; DOI=10.1210/jc.2016-2749;
RA Bernard V., Kherra S., Francou B., Fagart J., Viengchareun S., Guechot J.,
RA Ladjouze A., Guiochon-Mantel A., Korach K.S., Binart N., Lombes M.,
RA Christin-Maitre S.;
RT "Familial multiplicity of estrogen insensitivity associated with a loss-of-
RT function ESR1 mutation.";
RL J. Clin. Endocrinol. Metab. 102:93-99(2017).
CC -!- FUNCTION: Nuclear hormone receptor. The steroid hormones and their
CC receptors are involved in the regulation of eukaryotic gene expression
CC and affect cellular proliferation and differentiation in target
CC tissues. Ligand-dependent nuclear transactivation involves either
CC direct homodimer binding to a palindromic estrogen response element
CC (ERE) sequence or association with other DNA-binding transcription
CC factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-
CC independent signaling. Ligand binding induces a conformational change
CC allowing subsequent or combinatorial association with multiprotein
CC coactivator complexes through LXXLL motifs of their respective
CC components. Mutual transrepression occurs between the estrogen receptor
CC (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-
CC B DNA-binding activity and inhibits NF-kappa-B-mediated transcription
CC from the IL6 promoter and displace RELA/p65 and associated coregulators
CC from the promoter. Recruited to the NF-kappa-B response element of the
CC CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B
CC components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act
CC synergistically with NF-kappa-B to activate transcription involving
CC respective recruitment adjacent response elements; the function
CC involves CREBBP. Can activate the transcriptional activity of TFF1.
CC Also mediates membrane-initiated estrogen signaling involving various
CC kinase cascades. Essential for MTA1-mediated transcriptional regulation
CC of BRCA1 and BCAS3 (PubMed:17922032). {ECO:0000269|PubMed:10681512,
CC ECO:0000269|PubMed:10816575, ECO:0000269|PubMed:11477071,
CC ECO:0000269|PubMed:11682626, ECO:0000269|PubMed:14764652,
CC ECO:0000269|PubMed:15078875, ECO:0000269|PubMed:15891768,
CC ECO:0000269|PubMed:16043358, ECO:0000269|PubMed:16617102,
CC ECO:0000269|PubMed:16684779, ECO:0000269|PubMed:17922032,
CC ECO:0000269|PubMed:17932106, ECO:0000269|PubMed:18247370,
CC ECO:0000269|PubMed:19350539, ECO:0000269|PubMed:20074560,
CC ECO:0000269|PubMed:20705611, ECO:0000269|PubMed:21330404,
CC ECO:0000269|PubMed:22083956, ECO:0000269|PubMed:7651415,
CC ECO:0000269|PubMed:9328340}.
CC -!- FUNCTION: [Isoform 3]: Involved in activation of NOS3 and endothelial
CC nitric oxide production (PubMed:21937726). Isoforms lacking one or
CC several functional domains are thought to modulate transcriptional
CC activity by competitive ligand or DNA binding and/or heterodimerization
CC with the full-length receptor (PubMed:10970861). Binds to ERE and
CC inhibits isoform 1 (PubMed:10970861). {ECO:0000269|PubMed:10970861,
CC ECO:0000269|PubMed:21937726}.
CC -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ESR2.
CC Interacts with FOXC2, MAP1S, SLC30A9, UBE1C and NCOA3 coactivator (By
CC similarity). Interacts with PELP1, the interaction is enhanced by 17-
CC beta-estradiol, the interaction increases ESR1 transcriptional activity
CC (PubMed:11481323, PubMed:14963108). Interacts with EP300; the
CC interaction is estrogen-dependent and enhanced by CITED1. Interacts
CC with CITED1; the interaction is estrogen-dependent. Interacts with
CC NCOA5 and NCOA6 coactivators. Interacts with NCOA7; the interaction is
CC a ligand-inducible. Interacts with PHB2, and UBE1C. Interacts with
CC AKAP13. Interacts with CUEDC2. Interacts with KDM5A. Interacts with
CC SMARD1. Interacts with HEXIM1. Interacts with PBXIP1. Interaction with
CC MUC1 is stimulated by 7 beta-estradiol (E2) and enhances ESR1-mediated
CC transcription. Interacts with DNTTIP2, FAM120B and UIMC1. Interacts
CC with isoform 4 of TXNRD1. Interacts with KMT2D/MLL2. Interacts with
CC ATAD2 and this interaction is enhanced by estradiol. Interacts with
CC KIF18A and LDB1. Interacts with RLIM (via C-terminus). Interacts with
CC MACROD1. Interacts with SH2D4A and PLCG. Interaction with SH2D4A blocks
CC binding to PLCG and inhibits estrogen-induced cell proliferation.
CC Interacts with DYNLL1. Interacts with CCDC62 in the presence of
CC estradiol/E2; this interaction seems to enhance the transcription of
CC target genes. Interacts with NR2C1; the interaction prevents
CC homodimerization of ESR1 and suppresses its transcriptional activity
CC and cell growth. Interacts with DNAAF4. Interacts with PRMT2. Interacts
CC with RBFOX2. Interacts with STK3/MST2 only in the presence of SAV1 and
CC vice-versa. Binds to CSNK1D. Interacts with NCOA2; NCOA2 can interact
CC with ESR1 AF-1 and AF-2 domains simultaneously and mediate their
CC transcriptional synergy. Interacts with DDX5 (PubMed:11682626).
CC Interacts with NCOA1; the interaction seems to require a self-
CC association of N-terminal and C-terminal regions. Interacts with
CC ZNF366, DDX17, NFKB1, RELA, SP1 and SP3. Interacts with NRIP1 (By
CC similarity). Interacts with GPER1; the interaction occurs in an
CC estrogen-dependent manner. Interacts with CLOCK and the interaction is
CC stimulated by estrogen. Interacts with BCAS3. Interacts with TRIP4
CC (ufmylated); estrogen dependent. Interacts with LMTK3; the interaction
CC phosphorylates ESR1 (in vitro) and protects it against proteasomal
CC degradation. Interacts with CCAR2 (via N-terminus) in a ligand-
CC independent manner. Interacts with ZFHX3. Interacts with SFR1 in a
CC ligand-dependent and -independent manner (PubMed:23874500). Interacts
CC with DCAF13, LATS1 and DCAF1; regulates ESR1 ubiquitination and
CC ubiquitin-mediated proteasomal degradation (PubMed:28068668). Interacts
CC (via DNA-binding domain) with POU4F2 (C-terminus); this interaction
CC increases the estrogen receptor ESR1 transcriptional activity in a
CC DNA- and ligand 17-beta-estradiol-independent manner (By similarity).
CC Interacts with ESRRB isoform 1 (PubMed:19755138). Interacts with UBE3A
CC and WBP2 (PubMed:16772533). Interacts with GTF2B (PubMed:1517211).
CC Interacts with RBM39 (By similarity). In the absence of hormonal
CC ligand, interacts with TACC1 (PubMed:20078863). Interacts with PI3KR1
CC or PI3KR2 and PTK2/FAK1 (PubMed:18657504). Interacts with SRC
CC (PubMed:14963108, PubMed:18657504). {ECO:0000250,
CC ECO:0000250|UniProtKB:P19785, ECO:0000269|PubMed:10359819,
CC ECO:0000269|PubMed:10567404, ECO:0000269|PubMed:10681512,
CC ECO:0000269|PubMed:10816575, ECO:0000269|PubMed:10970861,
CC ECO:0000269|PubMed:11113208, ECO:0000269|PubMed:11265755,
CC ECO:0000269|PubMed:11358960, ECO:0000269|PubMed:11477071,
CC ECO:0000269|PubMed:11481323, ECO:0000269|PubMed:11581164,
CC ECO:0000269|PubMed:11682626, ECO:0000269|PubMed:11875103,
CC ECO:0000269|PubMed:11971969, ECO:0000269|PubMed:12039952,
CC ECO:0000269|PubMed:12093804, ECO:0000269|PubMed:12554772,
CC ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:14963108,
CC ECO:0000269|PubMed:15047147, ECO:0000269|PubMed:1517211,
CC ECO:0000269|PubMed:15199063, ECO:0000269|PubMed:15891768,
CC ECO:0000269|PubMed:15940264, ECO:0000269|PubMed:16427018,
CC ECO:0000269|PubMed:16603732, ECO:0000269|PubMed:16772533,
CC ECO:0000269|PubMed:17006958, ECO:0000269|PubMed:17043237,
CC ECO:0000269|PubMed:17085477, ECO:0000269|PubMed:17311814,
CC ECO:0000269|PubMed:17347654, ECO:0000269|PubMed:17505058,
CC ECO:0000269|PubMed:17587566, ECO:0000269|PubMed:17658481,
CC ECO:0000269|PubMed:17914104, ECO:0000269|PubMed:17932106,
CC ECO:0000269|PubMed:17998543, ECO:0000269|PubMed:18563714,
CC ECO:0000269|PubMed:18657504, ECO:0000269|PubMed:19117995,
CC ECO:0000269|PubMed:19339517, ECO:0000269|PubMed:19350539,
CC ECO:0000269|PubMed:19383985, ECO:0000269|PubMed:19423554,
CC ECO:0000269|PubMed:19636373, ECO:0000269|PubMed:19712589,
CC ECO:0000269|PubMed:19718048, ECO:0000269|PubMed:19749156,
CC ECO:0000269|PubMed:19755138, ECO:0000269|PubMed:20074560,
CC ECO:0000269|PubMed:20078863, ECO:0000269|PubMed:20720010,
CC ECO:0000269|PubMed:21104395, ECO:0000269|PubMed:21602804,
CC ECO:0000269|PubMed:23160374, ECO:0000269|PubMed:23874500,
CC ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:28068668,
CC ECO:0000269|PubMed:9328340, ECO:0000269|PubMed:9627117}.
CC -!- SUBUNIT: [Isoform 3]: Probably homodimerizes or heterodimerizes with
CC isoform 1 and ESR2. {ECO:0000269|PubMed:10970861}.
CC -!- INTERACTION:
CC P03372; Q12802: AKAP13; NbExp=3; IntAct=EBI-78473, EBI-1373806;
CC P03372; Q03989: ARID5A; NbExp=9; IntAct=EBI-78473, EBI-948603;
CC P03372; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-78473, EBI-10254793;
CC P03372; Q9Y294: ASF1A; NbExp=4; IntAct=EBI-78473, EBI-749553;
CC P03372; Q8IXJ9: ASXL1; NbExp=2; IntAct=EBI-78473, EBI-1646500;
CC P03372; Q6PL18: ATAD2; NbExp=5; IntAct=EBI-78473, EBI-6598454;
CC P03372; P18846: ATF1; NbExp=3; IntAct=EBI-78473, EBI-852794;
CC P03372; P62952: BLCAP; NbExp=2; IntAct=EBI-78473, EBI-3895726;
CC P03372; P38398: BRCA1; NbExp=14; IntAct=EBI-78473, EBI-349905;
CC P03372; P20290-2: BTF3; NbExp=5; IntAct=EBI-78473, EBI-1054703;
CC P03372; Q86Y37: CACUL1; NbExp=5; IntAct=EBI-78473, EBI-8168227;
CC P03372; P29279: CCN2; NbExp=7; IntAct=EBI-78473, EBI-2835375;
CC P03372; P17676: CEBPB; NbExp=2; IntAct=EBI-78473, EBI-969696;
CC P03372; Q99966: CITED1; NbExp=3; IntAct=EBI-78473, EBI-2624951;
CC P03372; Q9H467: CUEDC2; NbExp=2; IntAct=EBI-78473, EBI-1248228;
CC P03372; Q9NV06: DCAF13; NbExp=2; IntAct=EBI-78473, EBI-7402939;
CC P03372; O00429: DNM1L; NbExp=2; IntAct=EBI-78473, EBI-724571;
CC P03372; O60869: EDF1; NbExp=3; IntAct=EBI-78473, EBI-781301;
CC P03372; P00533: EGFR; NbExp=2; IntAct=EBI-78473, EBI-297353;
CC P03372; P03372: ESR1; NbExp=11; IntAct=EBI-78473, EBI-78473;
CC P03372; Q12778: FOXO1; NbExp=2; IntAct=EBI-78473, EBI-1108782;
CC P03372; O43524: FOXO3; NbExp=7; IntAct=EBI-78473, EBI-1644164;
CC P03372; Q9Y3R0: GRIP1; NbExp=2; IntAct=EBI-78473, EBI-5349621;
CC P03372; O00165: HAX1; NbExp=2; IntAct=EBI-78473, EBI-357001;
CC P03372; Q6NYC1: JMJD6; NbExp=8; IntAct=EBI-78473, EBI-8464037;
CC P03372; O15054: KDM6B; NbExp=2; IntAct=EBI-78473, EBI-2831260;
CC P03372; O14686: KMT2D; NbExp=3; IntAct=EBI-78473, EBI-996065;
CC P03372; O95835: LATS1; NbExp=2; IntAct=EBI-78473, EBI-444209;
CC P03372; Q6ZQX7-4: LIAT1; NbExp=3; IntAct=EBI-78473, EBI-25830459;
CC P03372; Q96Q04: LMTK3; NbExp=3; IntAct=EBI-78473, EBI-720814;
CC P03372; Q9BQ69: MACROD1; NbExp=6; IntAct=EBI-78473, EBI-5324932;
CC P03372; Q00987: MDM2; NbExp=2; IntAct=EBI-78473, EBI-389668;
CC P03372; Q15648: MED1; NbExp=3; IntAct=EBI-78473, EBI-394459;
CC P03372; P60660: MYL6; NbExp=3; IntAct=EBI-78473, EBI-300817;
CC P03372; Q15788: NCOA1; NbExp=8; IntAct=EBI-78473, EBI-455189;
CC P03372; Q15596: NCOA2; NbExp=5; IntAct=EBI-78473, EBI-81236;
CC P03372; Q9Y6Q9: NCOA3; NbExp=4; IntAct=EBI-78473, EBI-81196;
CC P03372; Q9UN36: NDRG2; NbExp=2; IntAct=EBI-78473, EBI-3895741;
CC P03372; PRO_0000030311 [P19838]: NFKB1; NbExp=3; IntAct=EBI-78473, EBI-697771;
CC P03372; Q96RI1-3: NR1H4; NbExp=2; IntAct=EBI-78473, EBI-10921781;
CC P03372; Q9BZ95: NSD3; NbExp=3; IntAct=EBI-78473, EBI-3390132;
CC P03372; Q9BTK6: PAGR1; NbExp=5; IntAct=EBI-78473, EBI-2372223;
CC P03372; Q96AQ6-1: PBXIP1; NbExp=3; IntAct=EBI-78473, EBI-15606280;
CC P03372; P06401: PGR; NbExp=20; IntAct=EBI-78473, EBI-78539;
CC P03372; P06401-1: PGR; NbExp=4; IntAct=EBI-78473, EBI-12590474;
CC P03372; Q99623: PHB2; NbExp=4; IntAct=EBI-78473, EBI-358348;
CC P03372; P36873: PPP1CC; NbExp=3; IntAct=EBI-78473, EBI-356283;
CC P03372; P53041: PPP5C; NbExp=4; IntAct=EBI-78473, EBI-716663;
CC P03372; P55345: PRMT2; NbExp=9; IntAct=EBI-78473, EBI-78458;
CC P03372; P60763: RAC3; NbExp=5; IntAct=EBI-78473, EBI-767084;
CC P03372; O43251: RBFOX2; NbExp=4; IntAct=EBI-78473, EBI-746056;
CC P03372; Q04206: RELA; NbExp=9; IntAct=EBI-78473, EBI-73886;
CC P03372; Q14151: SAFB2; NbExp=2; IntAct=EBI-78473, EBI-352869;
CC P03372; Q96HI0: SENP5; NbExp=2; IntAct=EBI-78473, EBI-3895753;
CC P03372; P08047: SP1; NbExp=2; IntAct=EBI-78473, EBI-298336;
CC P03372; Q02447: SP3; NbExp=4; IntAct=EBI-78473, EBI-348158;
CC P03372; P12931: SRC; NbExp=12; IntAct=EBI-78473, EBI-621482;
CC P03372; O15164: TRIM24; NbExp=3; IntAct=EBI-78473, EBI-2130378;
CC P03372; Q16881-4: TXNRD1; NbExp=4; IntAct=EBI-78473, EBI-9080335;
CC P03372; Q93009: USP7; NbExp=3; IntAct=EBI-78473, EBI-302474;
CC P03372; Q9UBK9: UXT; NbExp=2; IntAct=EBI-78473, EBI-357355;
CC P03372; O76024: WFS1; NbExp=3; IntAct=EBI-78473, EBI-720609;
CC P03372; Q8N895: ZNF366; NbExp=6; IntAct=EBI-78473, EBI-2813661;
CC P03372; P59598: Asxl1; Xeno; NbExp=2; IntAct=EBI-78473, EBI-5743705;
CC P03372; P05627: Jun; Xeno; NbExp=6; IntAct=EBI-78473, EBI-764369;
CC P03372; Q9JLI4: Ncoa6; Xeno; NbExp=2; IntAct=EBI-78473, EBI-286271;
CC P03372; Q60974: Ncor1; Xeno; NbExp=2; IntAct=EBI-78473, EBI-349004;
CC P03372; P62962: Pfn1; Xeno; NbExp=3; IntAct=EBI-78473, EBI-647096;
CC P03372; P00523: SRC; Xeno; NbExp=2; IntAct=EBI-78473, EBI-848039;
CC P03372-1; P03372-1: ESR1; NbExp=4; IntAct=EBI-15606245, EBI-15606245;
CC P03372-1; Q92731: ESR2; NbExp=5; IntAct=EBI-15606245, EBI-78505;
CC P03372-1; Q92993: KAT5; NbExp=3; IntAct=EBI-15606245, EBI-399080;
CC P03372-1; Q96AQ6-1: PBXIP1; NbExp=5; IntAct=EBI-15606245, EBI-15606280;
CC P03372-4; P00533: EGFR; NbExp=4; IntAct=EBI-4309277, EBI-297353;
CC P03372-4; P29353: SHC1; NbExp=2; IntAct=EBI-4309277, EBI-78835;
CC P03372-4; P12931: SRC; NbExp=2; IntAct=EBI-4309277, EBI-621482;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000255|PROSITE-
CC ProRule:PRU00407, ECO:0000269|PubMed:12682286,
CC ECO:0000269|PubMed:20074560}. Cytoplasm {ECO:0000269|PubMed:12682286,
CC ECO:0000269|PubMed:24498420}. Cell membrane
CC {ECO:0000269|PubMed:12682286}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12682286}; Cytoplasmic side
CC {ECO:0000269|PubMed:12682286}. Note=A minor fraction is associated with
CC the inner membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side. Cell membrane; Single-
CC pass type I membrane protein. Note=Associated with the inner membrane
CC via palmitoylation (Probable). At least a subset exists as a
CC transmembrane protein with a N-terminal extracellular domain.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Golgi apparatus. Cell membrane.
CC Note=Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus where
CC most probably palmitoylation occurs. Associated with the plasma
CC membrane when palmitoylated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Long, hER-alpha66, ER66;
CC IsoId=P03372-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P03372-2; Sequence=VSP_003680;
CC Name=3; Synonyms=hER-alpha46, ER46;
CC IsoId=P03372-3; Sequence=VSP_042460;
CC Name=4; Synonyms=hER-alpha36, ER36;
CC IsoId=P03372-4; Sequence=VSP_042460, VSP_042461;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:10970861). Not expressed
CC in the pituitary gland (PubMed:10970861).
CC {ECO:0000269|PubMed:10970861}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Widely expressed, however not
CC expressed in the pituitary gland. {ECO:0000269|PubMed:10970861}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain. The
CC modulating domain, also known as A/B or AF-1 domain has a ligand-
CC independent transactivation function. The C-terminus contains a ligand-
CC dependent transactivation domain, also known as E/F or AF-2 domain
CC which overlaps with the ligand binding domain. AF-1 and AF-2 activate
CC transcription independently and synergistically and act in a
CC promoter- and cell-specific manner. AF-1 seems to provide the major
CC transactivation function in differentiated cells.
CC -!- PTM: Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably
CC enhances transcriptional activity. Self-association induces
CC phosphorylation. Dephosphorylation at Ser-118 by PPP5C inhibits its
CC transactivation activity. Phosphorylated by LMTK3 in vitro.
CC {ECO:0000269|PubMed:10428798, ECO:0000269|PubMed:14764652,
CC ECO:0000269|PubMed:19339517, ECO:0000269|PubMed:21602804,
CC ECO:0000269|PubMed:7476978, ECO:0000269|PubMed:7539106,
CC ECO:0000269|PubMed:7838153}.
CC -!- PTM: Glycosylated; contains N-acetylglucosamine, probably O-linked.
CC {ECO:0000269|PubMed:8999954}.
CC -!- PTM: Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1
CC proteasomal degradation (PubMed:21602804, PubMed:28068668).
CC Deubiquitinated by OTUB1 (PubMed:19383985).
CC {ECO:0000269|PubMed:19383985, ECO:0000269|PubMed:21602804,
CC ECO:0000269|PubMed:28068668}.
CC -!- PTM: Dimethylated by PRMT1 at Arg-260. The methylation may favor
CC cytoplasmic localization (PubMed:18657504, PubMed:24498420).
CC Demethylated by JMJD6 at Arg-260 (PubMed:24498420).
CC {ECO:0000269|PubMed:18657504, ECO:0000269|PubMed:24498420}.
CC -!- PTM: Palmitoylated (isoform 3). Not biotinylated (isoform 3).
CC {ECO:0000269|PubMed:22031296}.
CC -!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required
CC for plasma membrane targeting and for rapid intracellular signaling via
CC ERK and AKT kinases and cAMP generation, but not for signaling mediated
CC by the nuclear hormone receptor. {ECO:0000269|PubMed:22031296}.
CC -!- POLYMORPHISM: Genetic variations in ESR1 are correlated with bone
CC mineral density (BMD). Low BMD is a risk factor for osteoporotic
CC fracture. Osteoporosis is characterized by reduced bone mineral
CC density, disruption of bone microarchitecture, and the alteration of
CC the amount and variety of non-collagenous proteins in bone.
CC Osteoporotic bones are more at risk of fracture.
CC {ECO:0000269|PubMed:10942433}.
CC -!- DISEASE: Estrogen resistance (ESTRR) [MIM:615363]: A disorder
CC characterized by partial or complete resistance to estrogens, in the
CC presence of elevated estrogen serum levels. Clinical features include
CC absence of the pubertal growth spurt, delayed bone maturation, unfused
CC epiphyses, reduced bone mineral density, osteoporosis, continued growth
CC into adulthood and very tall adult stature. Glucose intolerance,
CC hyperinsulinemia and lipid abnormalities may also be present.
CC {ECO:0000269|PubMed:23841731, ECO:0000269|PubMed:27754803}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Selective estrogen receptor modulators (SERMs), such as
CC tamoxifen, raloxifene, toremifene, lasofoxifene, clomifene, femarelle
CC and ormeloxifene, have tissue selective agonistic and antagonistic
CC effects on the estrogen receptor (ER). They interfere with the ER
CC association with coactivators or corepressors, mainly involving the AF-
CC 2 domain.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
CC 3. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was reported to be activated by DDX5. However, this study has
CC been retracted due to concerns of image manipulation.
CC {ECO:0000305|PubMed:10409727, ECO:0000305|PubMed:24509260}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB00115.1; Type=Miscellaneous discrepancy; Note=contains an in-frame duplication of exons 6 and 7.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/esr1/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Estrogen receptor entry;
CC URL="https://en.wikipedia.org/wiki/Estrogen_receptor";
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CC ---------------------------------------------------------------------------
DR EMBL; X03635; CAA27284.1; -; mRNA.
DR EMBL; M12674; AAA52399.1; -; mRNA.
DR EMBL; U47678; AAB00115.1; ALT_SEQ; mRNA.
DR EMBL; AY425004; AAQ91815.1; -; Genomic_DNA.
DR EMBL; BX640939; CAE45969.1; -; mRNA.
DR EMBL; AL049821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL078582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47740.1; -; Genomic_DNA.
DR EMBL; BC128573; AAI28574.1; -; mRNA.
DR EMBL; BC128574; AAI28575.1; -; mRNA.
DR EMBL; AH008151; AAD52984.1; -; Genomic_DNA.
DR EMBL; X73067; CAA51528.1; -; mRNA.
DR EMBL; Z75126; CAA99436.1; -; mRNA.
DR CCDS; CCDS5234.1; -. [P03372-1]
DR PIR; S64737; S64737.
DR RefSeq; NP_000116.2; NM_000125.3. [P03372-1]
DR RefSeq; NP_001116212.1; NM_001122740.1. [P03372-1]
DR RefSeq; NP_001116213.1; NM_001122741.1. [P03372-1]
DR RefSeq; NP_001116214.1; NM_001122742.1. [P03372-1]
DR RefSeq; NP_001278159.1; NM_001291230.1.
DR RefSeq; NP_001278170.1; NM_001291241.1.
DR RefSeq; NP_001315029.1; NM_001328100.1.
DR RefSeq; XP_006715438.1; XM_006715375.3. [P03372-3]
DR RefSeq; XP_011533845.1; XM_011535543.2. [P03372-1]
DR RefSeq; XP_011533846.1; XM_011535544.2. [P03372-1]
DR RefSeq; XP_011533847.1; XM_011535545.2. [P03372-1]
DR RefSeq; XP_016865865.1; XM_017010376.1. [P03372-1]
DR RefSeq; XP_016865866.1; XM_017010377.1. [P03372-1]
DR RefSeq; XP_016865867.1; XM_017010378.1. [P03372-1]
DR RefSeq; XP_016865868.1; XM_017010379.1. [P03372-1]
DR RefSeq; XP_016865869.1; XM_017010380.1. [P03372-1]
DR RefSeq; XP_016865870.1; XM_017010381.1. [P03372-1]
DR PDB; 1A52; X-ray; 2.80 A; A/B=297-554.
DR PDB; 1ERE; X-ray; 3.10 A; A/B/C/D/E/F=301-553.
DR PDB; 1ERR; X-ray; 2.60 A; A/B=301-553.
DR PDB; 1G50; X-ray; 2.90 A; A/B/C=304-550.
DR PDB; 1GWQ; X-ray; 2.45 A; A/B=301-548.
DR PDB; 1GWR; X-ray; 2.40 A; A/B=305-549.
DR PDB; 1HCP; NMR; -; A=180-254.
DR PDB; 1HCQ; X-ray; 2.40 A; A/B/E/F=180-262.
DR PDB; 1L2I; X-ray; 1.95 A; A/B=297-554.
DR PDB; 1PCG; X-ray; 2.70 A; A/B=304-547.
DR PDB; 1QKT; X-ray; 2.20 A; A=304-551.
DR PDB; 1QKU; X-ray; 3.20 A; A/B/C=301-550.
DR PDB; 1R5K; X-ray; 2.70 A; A/B/C=297-554.
DR PDB; 1SJ0; X-ray; 1.90 A; A=307-554.
DR PDB; 1UOM; X-ray; 2.28 A; A=301-553.
DR PDB; 1X7E; X-ray; 2.80 A; A/B=305-549.
DR PDB; 1X7R; X-ray; 2.00 A; A=305-549.
DR PDB; 1XP1; X-ray; 1.80 A; A=307-554.
DR PDB; 1XP6; X-ray; 1.70 A; A=307-554.
DR PDB; 1XP9; X-ray; 1.80 A; A=307-554.
DR PDB; 1XPC; X-ray; 1.60 A; A=307-554.
DR PDB; 1XQC; X-ray; 2.05 A; A/B/C/D=301-553.
DR PDB; 1YIM; X-ray; 1.90 A; A=307-554.
DR PDB; 1YIN; X-ray; 2.20 A; A=307-554.
DR PDB; 1ZKY; X-ray; 2.25 A; A/B=298-554.
DR PDB; 2AYR; X-ray; 1.90 A; A=304-551.
DR PDB; 2B1V; X-ray; 1.80 A; A/B=298-554.
DR PDB; 2B1Z; X-ray; 1.78 A; A/B=298-554.
DR PDB; 2B23; X-ray; 2.10 A; A/B=298-554.
DR PDB; 2BJ4; X-ray; 2.00 A; A/B=305-533.
DR PDB; 2FAI; X-ray; 2.10 A; A/B=298-554.
DR PDB; 2G44; X-ray; 2.65 A; A/B=298-554.
DR PDB; 2G5O; X-ray; 2.30 A; A/B=298-554.
DR PDB; 2I0J; X-ray; 2.90 A; A/B/C/D=304-547.
DR PDB; 2IOG; X-ray; 1.60 A; A=309-554.
DR PDB; 2IOK; X-ray; 2.40 A; A/B=301-554.
DR PDB; 2JF9; X-ray; 2.10 A; A/B/C=304-533.
DR PDB; 2JFA; X-ray; 2.55 A; A/B=304-533.
DR PDB; 2LLO; NMR; -; B=287-305.
DR PDB; 2LLQ; NMR; -; B=287-305.
DR PDB; 2OCF; X-ray; 2.95 A; A=298-595.
DR PDB; 2OUZ; X-ray; 2.00 A; A=301-553.
DR PDB; 2P15; X-ray; 1.94 A; A/B=298-554.
DR PDB; 2POG; X-ray; 1.84 A; A/B=304-551.
DR PDB; 2Q6J; X-ray; 2.70 A; A/B=298-554.
DR PDB; 2Q70; X-ray; 1.95 A; A/B=304-551.
DR PDB; 2QA6; X-ray; 2.60 A; A/B=298-554.
DR PDB; 2QA8; X-ray; 1.85 A; A/B=298-554.
DR PDB; 2QAB; X-ray; 1.89 A; A/B=298-554.
DR PDB; 2QE4; X-ray; 2.40 A; A/B=304-551.
DR PDB; 2QGT; X-ray; 2.15 A; A/B=298-554.
DR PDB; 2QGW; X-ray; 2.39 A; A/B=298-554.
DR PDB; 2QH6; X-ray; 2.70 A; A/B=298-554.
DR PDB; 2QR9; X-ray; 2.00 A; A/B=298-554.
DR PDB; 2QSE; X-ray; 1.85 A; A/B=298-554.
DR PDB; 2QXM; X-ray; 2.30 A; A/B=298-554.
DR PDB; 2QXS; X-ray; 1.70 A; A/B=298-554.
DR PDB; 2QZO; X-ray; 1.72 A; A/B=298-554.
DR PDB; 2R6W; X-ray; 2.00 A; A/B=304-551.
DR PDB; 2R6Y; X-ray; 2.00 A; A/B=304-551.
DR PDB; 2YAT; X-ray; 2.60 A; A=301-551.
DR PDB; 2YJA; X-ray; 1.82 A; B=299-551.
DR PDB; 3CBM; X-ray; 1.69 A; B=298-307.
DR PDB; 3CBO; X-ray; 1.65 A; B=298-307.
DR PDB; 3CBP; X-ray; 1.42 A; B=298-307.
DR PDB; 3DT3; X-ray; 2.40 A; A/B=299-551.
DR PDB; 3ERD; X-ray; 2.03 A; A/B=297-554.
DR PDB; 3ERT; X-ray; 1.90 A; A=297-554.
DR PDB; 3HLV; X-ray; 3.00 A; A/B=298-550.
DR PDB; 3HM1; X-ray; 2.33 A; A/B=298-550.
DR PDB; 3L03; X-ray; 1.90 A; A/B=298-550.
DR PDB; 3OS8; X-ray; 2.03 A; A/B/C/D=299-553.
DR PDB; 3OS9; X-ray; 2.30 A; A/B/C/D=299-553.
DR PDB; 3OSA; X-ray; 2.30 A; A/B/C/D=299-553.
DR PDB; 3Q95; X-ray; 2.05 A; A/B=298-554.
DR PDB; 3UU7; X-ray; 2.20 A; A/B=302-552.
DR PDB; 3UUA; X-ray; 2.05 A; A/B=302-552.
DR PDB; 3UUC; X-ray; 2.10 A; A/B/C/D=302-552.
DR PDB; 3UUD; X-ray; 1.60 A; A/B=302-552.
DR PDB; 4AA6; X-ray; 2.60 A; A/B/E/F=182-252.
DR PDB; 4DMA; X-ray; 2.30 A; A/B=303-549.
DR PDB; 4IU7; X-ray; 2.29 A; A/B=303-549.
DR PDB; 4IUI; X-ray; 2.30 A; A/B=303-549.
DR PDB; 4IV2; X-ray; 2.14 A; A/B=303-549.
DR PDB; 4IV4; X-ray; 2.30 A; A/B=303-549.
DR PDB; 4IVW; X-ray; 2.06 A; A/B=303-549.
DR PDB; 4IVY; X-ray; 1.95 A; A/B=303-549.
DR PDB; 4IW6; X-ray; 1.98 A; A/B=303-549.
DR PDB; 4IW8; X-ray; 2.04 A; A/B=303-549.
DR PDB; 4IWC; X-ray; 2.24 A; A/B=303-549.
DR PDB; 4IWF; X-ray; 1.93 A; A/B=303-549.
DR PDB; 4JC3; X-ray; 2.05 A; B=585-595.
DR PDB; 4JDD; X-ray; 2.10 A; B=585-595.
DR PDB; 4MG5; X-ray; 2.05 A; A/B=302-552.
DR PDB; 4MG6; X-ray; 2.10 A; A/B=302-552.
DR PDB; 4MG7; X-ray; 2.15 A; A/B=302-552.
DR PDB; 4MG8; X-ray; 1.85 A; A/B=302-552.
DR PDB; 4MG9; X-ray; 2.00 A; A/B=302-552.
DR PDB; 4MGA; X-ray; 1.80 A; A/B=302-552.
DR PDB; 4MGB; X-ray; 1.85 A; A/B=302-552.
DR PDB; 4MGC; X-ray; 2.15 A; A/B=302-552.
DR PDB; 4MGD; X-ray; 1.90 A; A/B=302-552.
DR PDB; 4O6F; X-ray; 2.82 A; B=261-271.
DR PDB; 4PP6; X-ray; 2.20 A; A/B=305-548.
DR PDB; 4PPP; X-ray; 2.69 A; A/B=305-548.
DR PDB; 4PPS; X-ray; 1.93 A; A/B=305-548.
DR PDB; 4PXM; X-ray; 1.90 A; A/B=299-554.
DR PDB; 4Q13; X-ray; 2.24 A; A/B=299-554.
DR PDB; 4Q50; X-ray; 3.07 A; A/B/C/D/E/F/G/H=299-554.
DR PDB; 4TUZ; X-ray; 1.90 A; A/B=302-552.
DR PDB; 4TV1; X-ray; 1.85 A; A/B=302-552.
DR PDB; 4XI3; X-ray; 2.49 A; A/B/C/D=306-548.
DR PDB; 4ZN7; X-ray; 1.93 A; A/B=301-559.
DR PDB; 4ZN9; X-ray; 2.21 A; A/B=301-559.
DR PDB; 4ZNH; X-ray; 1.93 A; A/B=301-559.
DR PDB; 4ZNS; X-ray; 1.86 A; A/B=301-559.
DR PDB; 4ZNT; X-ray; 1.90 A; A/B=301-559.
DR PDB; 4ZNU; X-ray; 2.40 A; A/B=301-559.
DR PDB; 4ZNV; X-ray; 1.77 A; A/B=301-559.
DR PDB; 4ZNW; X-ray; 2.31 A; A/B=301-559.
DR PDB; 5AAU; X-ray; 1.90 A; A/B=307-554.
DR PDB; 5AAV; X-ray; 1.95 A; A=307-554, B=306-554.
DR PDB; 5ACC; X-ray; 1.88 A; A=307-554.
DR PDB; 5AK2; X-ray; 2.19 A; A/B=307-554.
DR PDB; 5DI7; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5DID; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5DIE; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5DIG; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5DK9; X-ray; 2.28 A; A/B=298-554.
DR PDB; 5DKB; X-ray; 2.40 A; A/B=298-554.
DR PDB; 5DKE; X-ray; 2.60 A; A/B=298-554.
DR PDB; 5DKG; X-ray; 2.15 A; A/B=298-554.
DR PDB; 5DKS; X-ray; 2.60 A; A/B=298-554.
DR PDB; 5DL4; X-ray; 2.10 A; A/B=298-554.
DR PDB; 5DLR; X-ray; 2.26 A; A/B=298-554.
DR PDB; 5DMC; X-ray; 2.40 A; A/B=298-554.
DR PDB; 5DMF; X-ray; 2.40 A; A/B=298-554.
DR PDB; 5DP0; X-ray; 2.38 A; A/B=298-554.
DR PDB; 5DRJ; X-ray; 2.07 A; A/B=298-554.
DR PDB; 5DRM; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5DTV; X-ray; 2.29 A; A/B=298-554.
DR PDB; 5DU5; X-ray; 2.19 A; A/B=298-554.
DR PDB; 5DUE; X-ray; 2.09 A; A/B=298-554.
DR PDB; 5DUG; X-ray; 2.25 A; A/B=298-554.
DR PDB; 5DUH; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5DVS; X-ray; 2.28 A; A/B=298-554.
DR PDB; 5DVV; X-ray; 2.50 A; A/B=298-554.
DR PDB; 5DWE; X-ray; 1.92 A; A/B=298-554.
DR PDB; 5DWG; X-ray; 2.30 A; A/B=298-554.
DR PDB; 5DWI; X-ray; 2.43 A; A/B=298-554.
DR PDB; 5DWJ; X-ray; 2.00 A; A/B=298-554.
DR PDB; 5DX3; X-ray; 2.09 A; A/B=297-554.
DR PDB; 5DXB; X-ray; 2.08 A; A/B=297-554.
DR PDB; 5DXE; X-ray; 1.50 A; A/B=297-554.
DR PDB; 5DXG; X-ray; 1.86 A; A/B=297-554.
DR PDB; 5DXK; X-ray; 2.23 A; A/B=298-554.
DR PDB; 5DXM; X-ray; 2.37 A; A/B=298-554.
DR PDB; 5DXP; X-ray; 2.20 A; A/B=298-554.
DR PDB; 5DXQ; X-ray; 2.40 A; A/B=298-554.
DR PDB; 5DXR; X-ray; 2.28 A; A/B=298-554.
DR PDB; 5DY8; X-ray; 2.03 A; A/B=298-554.
DR PDB; 5DYB; X-ray; 2.27 A; A/B=298-554.
DR PDB; 5DYD; X-ray; 2.48 A; A/B=298-554.
DR PDB; 5DZ0; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5DZ1; X-ray; 2.20 A; A/B=298-554.
DR PDB; 5DZ3; X-ray; 2.15 A; A/B=298-554.
DR PDB; 5DZH; X-ray; 2.11 A; A/B=298-554.
DR PDB; 5DZI; X-ray; 1.90 A; A/B=298-554.
DR PDB; 5E0W; X-ray; 2.00 A; A/B=298-554.
DR PDB; 5E0X; X-ray; 2.01 A; A/B=298-554.
DR PDB; 5E14; X-ray; 2.22 A; A/B=298-554.
DR PDB; 5E15; X-ray; 2.10 A; A/B=298-554.
DR PDB; 5E19; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5E1C; X-ray; 1.98 A; A/B=298-554.
DR PDB; 5EGV; X-ray; 2.86 A; A/B=298-554.
DR PDB; 5EHJ; X-ray; 2.50 A; A/B=298-554.
DR PDB; 5EI1; X-ray; 2.40 A; A/B=298-554.
DR PDB; 5EIT; X-ray; 2.68 A; A/B=298-554.
DR PDB; 5FQP; X-ray; 1.88 A; A=307-554.
DR PDB; 5FQR; X-ray; 1.88 A; A=307-554.
DR PDB; 5FQS; X-ray; 1.94 A; A=307-554.
DR PDB; 5FQT; X-ray; 1.99 A; A=307-554.
DR PDB; 5FQV; X-ray; 1.74 A; A=307-554.
DR PDB; 5GS4; X-ray; 2.40 A; A=305-547.
DR PDB; 5GTR; X-ray; 2.80 A; A=305-547.
DR PDB; 5HYR; X-ray; 2.27 A; A/B=302-559.
DR PDB; 5JMM; X-ray; 2.10 A; A/B=302-552.
DR PDB; 5KCC; X-ray; 2.39 A; A/B=298-554, A/B=304-549.
DR PDB; 5KCD; X-ray; 1.82 A; A/B=298-554, A/B=305-549.
DR PDB; 5KCE; X-ray; 1.85 A; A/B=298-554, A/B=303-549.
DR PDB; 5KCF; X-ray; 2.07 A; A/B=298-554, A/B=303-549.
DR PDB; 5KCT; X-ray; 1.60 A; A/B=298-554, A/B=303-548.
DR PDB; 5KCU; X-ray; 2.03 A; A/B=298-554, A/B=303-548.
DR PDB; 5KCW; X-ray; 1.91 A; A/B=303-549, A/B=298-554.
DR PDB; 5KD9; X-ray; 1.78 A; A/B=298-554, A/B=303-549.
DR PDB; 5KR9; X-ray; 2.25 A; A/B=298-554.
DR PDB; 5KRA; X-ray; 2.40 A; A/B/E/F=298-554.
DR PDB; 5KRC; X-ray; 2.40 A; A/B=298-554.
DR PDB; 5KRF; X-ray; 2.19 A; A/B=298-554.
DR PDB; 5KRH; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5KRI; X-ray; 2.25 A; A/B=298-554.
DR PDB; 5KRJ; X-ray; 2.70 A; A/B=298-554.
DR PDB; 5KRK; X-ray; 2.39 A; A/B=298-554.
DR PDB; 5KRL; X-ray; 2.40 A; A/B=298-554.
DR PDB; 5KRM; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5KRO; X-ray; 2.10 A; A/B=298-554.
DR PDB; 5N10; X-ray; 1.60 A; C/D/F=584-595.
DR PDB; 5T0X; NMR; -; B/C=287-305.
DR PDB; 5T1Z; X-ray; 2.10 A; A/B=298-554.
DR PDB; 5T92; X-ray; 2.22 A; A/B=301-553.
DR PDB; 5T97; X-ray; 3.00 A; A/B=301-553.
DR PDB; 5TLD; X-ray; 2.38 A; A/B=298-554.
DR PDB; 5TLF; X-ray; 2.20 A; A/B=298-554.
DR PDB; 5TLG; X-ray; 2.23 A; A/B=298-554.
DR PDB; 5TLL; X-ray; 2.42 A; A/B=298-554.
DR PDB; 5TLM; X-ray; 2.50 A; A/B=298-554.
DR PDB; 5TLO; X-ray; 2.28 A; A/B=298-554.
DR PDB; 5TLP; X-ray; 2.08 A; A/B=298-554.
DR PDB; 5TLT; X-ray; 1.90 A; A/B=298-554.
DR PDB; 5TLU; X-ray; 2.22 A; A/B=298-554.
DR PDB; 5TLV; X-ray; 2.32 A; A/B=298-554.
DR PDB; 5TLX; X-ray; 2.10 A; A/B=298-554.
DR PDB; 5TLY; X-ray; 2.14 A; A/B=298-554.
DR PDB; 5TM1; X-ray; 2.23 A; A/B=298-554.
DR PDB; 5TM2; X-ray; 2.60 A; A/B=298-554.
DR PDB; 5TM3; X-ray; 2.19 A; A/B=298-554.
DR PDB; 5TM4; X-ray; 2.25 A; A/B=298-554.
DR PDB; 5TM5; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5TM6; X-ray; 2.54 A; A/B=298-554.
DR PDB; 5TM7; X-ray; 2.40 A; A/B=298-554.
DR PDB; 5TM8; X-ray; 1.99 A; A/B=298-554.
DR PDB; 5TM9; X-ray; 2.50 A; A/B=298-554.
DR PDB; 5TML; X-ray; 2.25 A; A/B=298-554.
DR PDB; 5TMM; X-ray; 2.20 A; A/B=298-554.
DR PDB; 5TMO; X-ray; 2.17 A; A/B=298-554.
DR PDB; 5TMQ; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5TMR; X-ray; 2.30 A; A/B=298-554.
DR PDB; 5TMS; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5TMT; X-ray; 2.05 A; A/B=298-554.
DR PDB; 5TMU; X-ray; 2.43 A; A/B=298-554.
DR PDB; 5TMV; X-ray; 2.38 A; A/B=298-554.
DR PDB; 5TMW; X-ray; 2.29 A; A/B=298-554.
DR PDB; 5TMZ; X-ray; 2.21 A; A/B=298-554.
DR PDB; 5TN1; X-ray; 2.06 A; A/B=298-554.
DR PDB; 5TN3; X-ray; 2.54 A; A/B=298-554.
DR PDB; 5TN4; X-ray; 1.86 A; A/B=298-554.
DR PDB; 5TN5; X-ray; 1.89 A; A/B=298-554.
DR PDB; 5TN6; X-ray; 2.09 A; A/B=298-554.
DR PDB; 5TN7; X-ray; 2.24 A; A/B=298-554.
DR PDB; 5TN8; X-ray; 2.65 A; A/B=298-554.
DR PDB; 5TN9; X-ray; 2.25 A; A/B/C/D=298-554.
DR PDB; 5TNB; X-ray; 2.08 A; A/B/C/D=298-554.
DR PDB; 5U2B; X-ray; 2.22 A; A/B/C/D/E/F=298-554.
DR PDB; 5U2D; X-ray; 1.86 A; A/B=298-554.
DR PDB; 5UFW; X-ray; 1.58 A; A/B=306-554.
DR PDB; 5UFX; X-ray; 1.55 A; A/B=306-554.
DR PDB; 5W9C; X-ray; 1.80 A; A/B/C/D=306-554.
DR PDB; 5W9D; X-ray; 1.65 A; A/B=306-554.
DR PDB; 5WGD; X-ray; 1.80 A; A/B=297-554.
DR PDB; 5WGQ; X-ray; 2.30 A; A/B=297-554.
DR PDB; 6B0F; X-ray; 2.86 A; A/B=301-553.
DR PDB; 6C42; X-ray; 2.00 A; A/B=307-554.
DR PDB; 6CBZ; X-ray; 1.65 A; A/B=305-554.
DR PDB; 6CHW; X-ray; 1.89 A; A=306-551.
DR PDB; 6CHZ; X-ray; 1.68 A; A=307-554.
DR PDB; 6CZN; X-ray; 2.50 A; A/B=298-554.
DR PDB; 6D0F; X-ray; 2.50 A; A/B=305-554.
DR PDB; 6DF6; X-ray; 2.50 A; A/B/C/D=298-553.
DR PDB; 6DFN; X-ray; 2.10 A; A/B/C/D=298-553.
DR PDB; 6HHP; X-ray; 1.80 A; B=588-595.
DR PDB; 6HKB; X-ray; 1.70 A; B=588-595.
DR PDB; 6HKF; X-ray; 1.80 A; B=588-595.
DR PDB; 6HMU; X-ray; 1.20 A; B=588-595.
DR PDB; 6IAR; X-ray; 1.84 A; A=307-547.
DR PDB; 6OWC; X-ray; 1.85 A; A/B=298-554.
DR PDB; 6PET; X-ray; 2.20 A; A/B/C/D=298-553.
DR PDB; 6PFM; X-ray; 2.84 A; A/D=298-553.
DR PDB; 6PIT; X-ray; 2.25 A; A/B=297-554.
DR PDB; 6PSJ; X-ray; 1.80 A; A/B=307-554.
DR PDB; 6SBO; X-ray; 1.48 A; A/B=297-554.
DR PDB; 6SQ0; X-ray; 1.77 A; A/B=307-554.
DR PDB; 6SUO; X-ray; 1.74 A; A/B=307-554.
DR PDB; 6TJM; X-ray; 1.85 A; B=588-595.
DR PDB; 6TL3; X-ray; 2.46 A; B=588-595.
DR PDB; 6V87; X-ray; 2.40 A; A/B=307-554.
DR PDB; 6V8T; X-ray; 2.10 A; A/B=307-554.
DR PDB; 6VGH; X-ray; 2.10 A; A/B=307-554.
DR PDB; 6VIG; X-ray; 1.45 A; A/B/C/D=306-554.
DR PDB; 6VJD; X-ray; 1.80 A; A/B/C/D=307-554.
DR PDB; 6VMU; X-ray; 1.70 A; A/B/C/D=307-554.
DR PDB; 6VPF; X-ray; 1.60 A; A/B/C/D=306-554.
DR PDB; 6VPK; X-ray; 1.70 A; A/B/C/D=306-554.
DR PDB; 6VVP; X-ray; 2.60 A; A/B/C/D=306-554.
DR PDB; 6WOK; X-ray; 2.31 A; A/B/C/D=298-553.
DR PDB; 6ZOQ; X-ray; 1.80 A; A/B=307-554.
DR PDB; 6ZOR; X-ray; 1.97 A; A/B=307-554.
DR PDB; 6ZOS; X-ray; 2.00 A; A/B=307-554.
DR PDB; 7B9M; X-ray; 1.70 A; B=588-595.
DR PDB; 7B9R; X-ray; 1.15 A; B=588-595.
DR PDB; 7B9T; X-ray; 1.15 A; B=588-595.
DR PDB; 7BA3; X-ray; 1.40 A; B=588-595.
DR PDB; 7BA5; X-ray; 1.45 A; B=588-595.
DR PDB; 7BA6; X-ray; 1.40 A; B=588-595.
DR PDB; 7BA7; X-ray; 1.45 A; B=588-595.
DR PDB; 7BA8; X-ray; 1.20 A; B=588-595.
DR PDB; 7BA9; X-ray; 1.48 A; B=588-595.
DR PDB; 7BAA; X-ray; 1.10 A; B=588-595.
DR PDB; 7BAB; X-ray; 1.30 A; B=588-595.
DR PDB; 7JHD; X-ray; 2.40 A; A/B=305-554.
DR PDB; 7KBS; X-ray; 1.83 A; A/B=307-554.
DR PDB; 7KCA; X-ray; 1.78 A; A/B=306-554.
DR PDB; 7KCD; X-ray; 1.80 A; A/B/C/D=307-554.
DR PDB; 7MSA; X-ray; 2.24 A; A/B/C/D=298-553.
DR PDB; 7NDO; X-ray; 1.60 A; A/B=304-548.
DR PDB; 7NEL; X-ray; 1.45 A; A/B=304-548.
DR PDB; 7NFB; X-ray; 1.33 A; A/B=304-548.
DR PDB; 7NFW; X-ray; 1.19 A; B=588-595.
DR PDB; 7NIZ; X-ray; 1.48 A; B=588-595.
DR PDB; 7RRX; X-ray; 1.78 A; A/B/C/D=298-554.
DR PDB; 7RRY; X-ray; 1.87 A; A/B/C/D=298-554.
DR PDB; 7RRZ; X-ray; 1.83 A; A/B/C/D=298-554.
DR PDB; 7RS0; X-ray; 1.67 A; A/B/C/D=298-554.
DR PDB; 7RS1; X-ray; 1.59 A; A/B/C/D=298-554.
DR PDB; 7RS2; X-ray; 1.72 A; A/B/C/D=298-554.
DR PDB; 7RS3; X-ray; 1.84 A; A/B/C/D=298-554.
DR PDB; 7RS4; X-ray; 1.78 A; A/B/C/D=298-554.
DR PDB; 7RS7; X-ray; 1.58 A; A/B/C/D=298-554.
DR PDB; 7RS8; X-ray; 1.64 A; A/B/C/D=298-554.
DR PDB; 7RS9; X-ray; 1.70 A; A/B/C/D=298-554.
DR PDB; 7TE7; X-ray; 1.85 A; A=306-554.
DR PDB; 7UJ7; X-ray; 1.68 A; A/B/C/D=306-554.
DR PDBsum; 1A52; -.
DR PDBsum; 1ERE; -.
DR PDBsum; 1ERR; -.
DR PDBsum; 1G50; -.
DR PDBsum; 1GWQ; -.
DR PDBsum; 1GWR; -.
DR PDBsum; 1HCP; -.
DR PDBsum; 1HCQ; -.
DR PDBsum; 1L2I; -.
DR PDBsum; 1PCG; -.
DR PDBsum; 1QKT; -.
DR PDBsum; 1QKU; -.
DR PDBsum; 1R5K; -.
DR PDBsum; 1SJ0; -.
DR PDBsum; 1UOM; -.
DR PDBsum; 1X7E; -.
DR PDBsum; 1X7R; -.
DR PDBsum; 1XP1; -.
DR PDBsum; 1XP6; -.
DR PDBsum; 1XP9; -.
DR PDBsum; 1XPC; -.
DR PDBsum; 1XQC; -.
DR PDBsum; 1YIM; -.
DR PDBsum; 1YIN; -.
DR PDBsum; 1ZKY; -.
DR PDBsum; 2AYR; -.
DR PDBsum; 2B1V; -.
DR PDBsum; 2B1Z; -.
DR PDBsum; 2B23; -.
DR PDBsum; 2BJ4; -.
DR PDBsum; 2FAI; -.
DR PDBsum; 2G44; -.
DR PDBsum; 2G5O; -.
DR PDBsum; 2I0J; -.
DR PDBsum; 2IOG; -.
DR PDBsum; 2IOK; -.
DR PDBsum; 2JF9; -.
DR PDBsum; 2JFA; -.
DR PDBsum; 2LLO; -.
DR PDBsum; 2LLQ; -.
DR PDBsum; 2OCF; -.
DR PDBsum; 2OUZ; -.
DR PDBsum; 2P15; -.
DR PDBsum; 2POG; -.
DR PDBsum; 2Q6J; -.
DR PDBsum; 2Q70; -.
DR PDBsum; 2QA6; -.
DR PDBsum; 2QA8; -.
DR PDBsum; 2QAB; -.
DR PDBsum; 2QE4; -.
DR PDBsum; 2QGT; -.
DR PDBsum; 2QGW; -.
DR PDBsum; 2QH6; -.
DR PDBsum; 2QR9; -.
DR PDBsum; 2QSE; -.
DR PDBsum; 2QXM; -.
DR PDBsum; 2QXS; -.
DR PDBsum; 2QZO; -.
DR PDBsum; 2R6W; -.
DR PDBsum; 2R6Y; -.
DR PDBsum; 2YAT; -.
DR PDBsum; 2YJA; -.
DR PDBsum; 3CBM; -.
DR PDBsum; 3CBO; -.
DR PDBsum; 3CBP; -.
DR PDBsum; 3DT3; -.
DR PDBsum; 3ERD; -.
DR PDBsum; 3ERT; -.
DR PDBsum; 3HLV; -.
DR PDBsum; 3HM1; -.
DR PDBsum; 3L03; -.
DR PDBsum; 3OS8; -.
DR PDBsum; 3OS9; -.
DR PDBsum; 3OSA; -.
DR PDBsum; 3Q95; -.
DR PDBsum; 3UU7; -.
DR PDBsum; 3UUA; -.
DR PDBsum; 3UUC; -.
DR PDBsum; 3UUD; -.
DR PDBsum; 4AA6; -.
DR PDBsum; 4DMA; -.
DR PDBsum; 4IU7; -.
DR PDBsum; 4IUI; -.
DR PDBsum; 4IV2; -.
DR PDBsum; 4IV4; -.
DR PDBsum; 4IVW; -.
DR PDBsum; 4IVY; -.
DR PDBsum; 4IW6; -.
DR PDBsum; 4IW8; -.
DR PDBsum; 4IWC; -.
DR PDBsum; 4IWF; -.
DR PDBsum; 4JC3; -.
DR PDBsum; 4JDD; -.
DR PDBsum; 4MG5; -.
DR PDBsum; 4MG6; -.
DR PDBsum; 4MG7; -.
DR PDBsum; 4MG8; -.
DR PDBsum; 4MG9; -.
DR PDBsum; 4MGA; -.
DR PDBsum; 4MGB; -.
DR PDBsum; 4MGC; -.
DR PDBsum; 4MGD; -.
DR PDBsum; 4O6F; -.
DR PDBsum; 4PP6; -.
DR PDBsum; 4PPP; -.
DR PDBsum; 4PPS; -.
DR PDBsum; 4PXM; -.
DR PDBsum; 4Q13; -.
DR PDBsum; 4Q50; -.
DR PDBsum; 4TUZ; -.
DR PDBsum; 4TV1; -.
DR PDBsum; 4XI3; -.
DR PDBsum; 4ZN7; -.
DR PDBsum; 4ZN9; -.
DR PDBsum; 4ZNH; -.
DR PDBsum; 4ZNS; -.
DR PDBsum; 4ZNT; -.
DR PDBsum; 4ZNU; -.
DR PDBsum; 4ZNV; -.
DR PDBsum; 4ZNW; -.
DR PDBsum; 5AAU; -.
DR PDBsum; 5AAV; -.
DR PDBsum; 5ACC; -.
DR PDBsum; 5AK2; -.
DR PDBsum; 5DI7; -.
DR PDBsum; 5DID; -.
DR PDBsum; 5DIE; -.
DR PDBsum; 5DIG; -.
DR PDBsum; 5DK9; -.
DR PDBsum; 5DKB; -.
DR PDBsum; 5DKE; -.
DR PDBsum; 5DKG; -.
DR PDBsum; 5DKS; -.
DR PDBsum; 5DL4; -.
DR PDBsum; 5DLR; -.
DR PDBsum; 5DMC; -.
DR PDBsum; 5DMF; -.
DR PDBsum; 5DP0; -.
DR PDBsum; 5DRJ; -.
DR PDBsum; 5DRM; -.
DR PDBsum; 5DTV; -.
DR PDBsum; 5DU5; -.
DR PDBsum; 5DUE; -.
DR PDBsum; 5DUG; -.
DR PDBsum; 5DUH; -.
DR PDBsum; 5DVS; -.
DR PDBsum; 5DVV; -.
DR PDBsum; 5DWE; -.
DR PDBsum; 5DWG; -.
DR PDBsum; 5DWI; -.
DR PDBsum; 5DWJ; -.
DR PDBsum; 5DX3; -.
DR PDBsum; 5DXB; -.
DR PDBsum; 5DXE; -.
DR PDBsum; 5DXG; -.
DR PDBsum; 5DXK; -.
DR PDBsum; 5DXM; -.
DR PDBsum; 5DXP; -.
DR PDBsum; 5DXQ; -.
DR PDBsum; 5DXR; -.
DR PDBsum; 5DY8; -.
DR PDBsum; 5DYB; -.
DR PDBsum; 5DYD; -.
DR PDBsum; 5DZ0; -.
DR PDBsum; 5DZ1; -.
DR PDBsum; 5DZ3; -.
DR PDBsum; 5DZH; -.
DR PDBsum; 5DZI; -.
DR PDBsum; 5E0W; -.
DR PDBsum; 5E0X; -.
DR PDBsum; 5E14; -.
DR PDBsum; 5E15; -.
DR PDBsum; 5E19; -.
DR PDBsum; 5E1C; -.
DR PDBsum; 5EGV; -.
DR PDBsum; 5EHJ; -.
DR PDBsum; 5EI1; -.
DR PDBsum; 5EIT; -.
DR PDBsum; 5FQP; -.
DR PDBsum; 5FQR; -.
DR PDBsum; 5FQS; -.
DR PDBsum; 5FQT; -.
DR PDBsum; 5FQV; -.
DR PDBsum; 5GS4; -.
DR PDBsum; 5GTR; -.
DR PDBsum; 5HYR; -.
DR PDBsum; 5JMM; -.
DR PDBsum; 5KCC; -.
DR PDBsum; 5KCD; -.
DR PDBsum; 5KCE; -.
DR PDBsum; 5KCF; -.
DR PDBsum; 5KCT; -.
DR PDBsum; 5KCU; -.
DR PDBsum; 5KCW; -.
DR PDBsum; 5KD9; -.
DR PDBsum; 5KR9; -.
DR PDBsum; 5KRA; -.
DR PDBsum; 5KRC; -.
DR PDBsum; 5KRF; -.
DR PDBsum; 5KRH; -.
DR PDBsum; 5KRI; -.
DR PDBsum; 5KRJ; -.
DR PDBsum; 5KRK; -.
DR PDBsum; 5KRL; -.
DR PDBsum; 5KRM; -.
DR PDBsum; 5KRO; -.
DR PDBsum; 5N10; -.
DR PDBsum; 5T0X; -.
DR PDBsum; 5T1Z; -.
DR PDBsum; 5T92; -.
DR PDBsum; 5T97; -.
DR PDBsum; 5TLD; -.
DR PDBsum; 5TLF; -.
DR PDBsum; 5TLG; -.
DR PDBsum; 5TLL; -.
DR PDBsum; 5TLM; -.
DR PDBsum; 5TLO; -.
DR PDBsum; 5TLP; -.
DR PDBsum; 5TLT; -.
DR PDBsum; 5TLU; -.
DR PDBsum; 5TLV; -.
DR PDBsum; 5TLX; -.
DR PDBsum; 5TLY; -.
DR PDBsum; 5TM1; -.
DR PDBsum; 5TM2; -.
DR PDBsum; 5TM3; -.
DR PDBsum; 5TM4; -.
DR PDBsum; 5TM5; -.
DR PDBsum; 5TM6; -.
DR PDBsum; 5TM7; -.
DR PDBsum; 5TM8; -.
DR PDBsum; 5TM9; -.
DR PDBsum; 5TML; -.
DR PDBsum; 5TMM; -.
DR PDBsum; 5TMO; -.
DR PDBsum; 5TMQ; -.
DR PDBsum; 5TMR; -.
DR PDBsum; 5TMS; -.
DR PDBsum; 5TMT; -.
DR PDBsum; 5TMU; -.
DR PDBsum; 5TMV; -.
DR PDBsum; 5TMW; -.
DR PDBsum; 5TMZ; -.
DR PDBsum; 5TN1; -.
DR PDBsum; 5TN3; -.
DR PDBsum; 5TN4; -.
DR PDBsum; 5TN5; -.
DR PDBsum; 5TN6; -.
DR PDBsum; 5TN7; -.
DR PDBsum; 5TN8; -.
DR PDBsum; 5TN9; -.
DR PDBsum; 5TNB; -.
DR PDBsum; 5U2B; -.
DR PDBsum; 5U2D; -.
DR PDBsum; 5UFW; -.
DR PDBsum; 5UFX; -.
DR PDBsum; 5W9C; -.
DR PDBsum; 5W9D; -.
DR PDBsum; 5WGD; -.
DR PDBsum; 5WGQ; -.
DR PDBsum; 6B0F; -.
DR PDBsum; 6C42; -.
DR PDBsum; 6CBZ; -.
DR PDBsum; 6CHW; -.
DR PDBsum; 6CHZ; -.
DR PDBsum; 6CZN; -.
DR PDBsum; 6D0F; -.
DR PDBsum; 6DF6; -.
DR PDBsum; 6DFN; -.
DR PDBsum; 6HHP; -.
DR PDBsum; 6HKB; -.
DR PDBsum; 6HKF; -.
DR PDBsum; 6HMU; -.
DR PDBsum; 6IAR; -.
DR PDBsum; 6OWC; -.
DR PDBsum; 6PET; -.
DR PDBsum; 6PFM; -.
DR PDBsum; 6PIT; -.
DR PDBsum; 6PSJ; -.
DR PDBsum; 6SBO; -.
DR PDBsum; 6SQ0; -.
DR PDBsum; 6SUO; -.
DR PDBsum; 6TJM; -.
DR PDBsum; 6TL3; -.
DR PDBsum; 6V87; -.
DR PDBsum; 6V8T; -.
DR PDBsum; 6VGH; -.
DR PDBsum; 6VIG; -.
DR PDBsum; 6VJD; -.
DR PDBsum; 6VMU; -.
DR PDBsum; 6VPF; -.
DR PDBsum; 6VPK; -.
DR PDBsum; 6VVP; -.
DR PDBsum; 6WOK; -.
DR PDBsum; 6ZOQ; -.
DR PDBsum; 6ZOR; -.
DR PDBsum; 6ZOS; -.
DR PDBsum; 7B9M; -.
DR PDBsum; 7B9R; -.
DR PDBsum; 7B9T; -.
DR PDBsum; 7BA3; -.
DR PDBsum; 7BA5; -.
DR PDBsum; 7BA6; -.
DR PDBsum; 7BA7; -.
DR PDBsum; 7BA8; -.
DR PDBsum; 7BA9; -.
DR PDBsum; 7BAA; -.
DR PDBsum; 7BAB; -.
DR PDBsum; 7JHD; -.
DR PDBsum; 7KBS; -.
DR PDBsum; 7KCA; -.
DR PDBsum; 7KCD; -.
DR PDBsum; 7MSA; -.
DR PDBsum; 7NDO; -.
DR PDBsum; 7NEL; -.
DR PDBsum; 7NFB; -.
DR PDBsum; 7NFW; -.
DR PDBsum; 7NIZ; -.
DR PDBsum; 7RRX; -.
DR PDBsum; 7RRY; -.
DR PDBsum; 7RRZ; -.
DR PDBsum; 7RS0; -.
DR PDBsum; 7RS1; -.
DR PDBsum; 7RS2; -.
DR PDBsum; 7RS3; -.
DR PDBsum; 7RS4; -.
DR PDBsum; 7RS7; -.
DR PDBsum; 7RS8; -.
DR PDBsum; 7RS9; -.
DR PDBsum; 7TE7; -.
DR PDBsum; 7UJ7; -.
DR AlphaFoldDB; P03372; -.
DR SASBDB; P03372; -.
DR SMR; P03372; -.
DR BioGRID; 108403; 2262.
DR ComplexPortal; CPX-5156; ERalpha-NCOA2 activated estrogen receptor complex.
DR CORUM; P03372; -.
DR DIP; DIP-5965N; -.
DR ELM; P03372; -.
DR IntAct; P03372; 1907.
DR MINT; P03372; -.
DR STRING; 9606.ENSP00000405330; -.
DR BindingDB; P03372; -.
DR ChEMBL; CHEMBL206; -.
DR DrugBank; DB07567; (2R,3R,4S)-3-(4-HYDROXYPHENYL)-4-METHYL-2-[4-(2-PYRROLIDIN-1-YLETHOXY)PHENYL]CHROMAN-6-OL.
DR DrugBank; DB07638; (3AS,4R,9BR)-2,2-DIFLUORO-4-(4-HYDROXYPHENYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-8-OL.
DR DrugBank; DB08737; (3AS,4R,9BR)-4-(4-HYDROXYPHENYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-9-OL.
DR DrugBank; DB08020; (3AS,4R,9BR)-4-(4-HYDROXYPHENYL)-6-(METHOXYMETHYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-8-OL.
DR DrugBank; DB07678; (9ALPHA,13BETA,17BETA)-2-[(1Z)-BUT-1-EN-1-YL]ESTRA-1,3,5(10)-TRIENE-3,17-DIOL.
DR DrugBank; DB07707; (9BETA,11ALPHA,13ALPHA,14BETA,17ALPHA)-11-(METHOXYMETHYL)ESTRA-1(10),2,4-TRIENE-3,17-DIOL.
DR DrugBank; DB03802; 1-[4-(Octahydro-Pyrido[1,2-a]Pyrazin-2-Yl)-Phenyl]-2-Phenyl-1,2,3,4-Tetrahydro-Isoquinolin-6-Ol.
DR DrugBank; DB06871; 17-METHYL-17-ALPHA-DIHYDROEQUILENIN.
DR DrugBank; DB08773; 2-(4-hydroxyphenyl)benzo[b]thiophen-6-ol.
DR DrugBank; DB08398; 2-Amino-1-methyl-6-phenylimidazo(4,5-b)pyridine.
DR DrugBank; DB13869; 2-Methoxy-6-{(E)-[(4-methylphenyl)imino]methyl}phenol.
DR DrugBank; DB04471; 2-Phenyl-1-[4-(2-Piperidin-1-Yl-Ethoxy)-Phenyl]-1,2,3,4-Tetrahydro-Isoquinolin-6-Ol.
DR DrugBank; DB07708; 3-CHLORO-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL.
DR DrugBank; DB07712; 3-ETHYL-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL.
DR DrugBank; DB06898; 4-(2-amino-1-methyl-1H-imidazo[4,5-b]pyridin-6-yl)phenol.
DR DrugBank; DB08048; 4-(6-HYDROXY-1H-INDAZOL-3-YL)BENZENE-1,3-DIOL.
DR DrugBank; DB08595; 4-[(1S,2R,5S)-4,4,8-TRIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL.
DR DrugBank; DB07195; 4-[(1S,2S,5S)-5-(HYDROXYMETHYL)-6,8,9-TRIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL.
DR DrugBank; DB07086; 4-[(1S,2S,5S)-5-(HYDROXYMETHYL)-8-METHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL.
DR DrugBank; DB07087; 4-[(1S,2S,5S,9R)-5-(HYDROXYMETHYL)-8,9-DIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL.
DR DrugBank; DB08047; 4-[1-allyl-7-(trifluoromethyl)-1H-indazol-3-yl]benzene-1,3-diol.
DR DrugBank; DB06927; [5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-YL]ACETONITRILE.
DR DrugBank; DB04468; Afimoxifene.
DR DrugBank; DB01431; Allylestrenol.
DR DrugBank; DB05233; AP1081.
DR DrugBank; DB06249; Arzoxifene.
DR DrugBank; DB06401; Bazedoxifene.
DR DrugBank; DB01878; Benzophenone.
DR DrugBank; DB06732; beta-Naphthoflavone.
DR DrugBank; DB05882; CHF 4227.
DR DrugBank; DB00269; Chlorotrianisene.
DR DrugBank; DB00882; Clomifene.
DR DrugBank; DB02715; Compound 18.
DR DrugBank; DB02615; Compound 19.
DR DrugBank; DB03742; Compound 4-D.
DR DrugBank; DB00286; Conjugated estrogens.
DR DrugBank; DB05487; Custirsen.
DR DrugBank; DB01406; Danazol.
DR DrugBank; DB00304; Desogestrel.
DR DrugBank; DB00890; Dienestrol.
DR DrugBank; DB08320; DIETHYL (1R,2S,3R,4S)-5,6-BIS(4-HYDROXYPHENYL)-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2,3-DICARBOXYLATE.
DR DrugBank; DB00255; Diethylstilbestrol.
DR DrugBank; DB07932; dimethyl (1R,4S)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]hepta-2,5-diene-2,3-dicarboxylate.
DR DrugBank; DB00841; Dobutamine.
DR DrugBank; DB06374; Elacestrant.
DR DrugBank; DB11219; Enzacamene.
DR DrugBank; DB02187; Equilin.
DR DrugBank; DB07933; Erteberel.
DR DrugBank; DB12235; Estetrol.
DR DrugBank; DB00783; Estradiol.
DR DrugBank; DB13952; Estradiol acetate.
DR DrugBank; DB13953; Estradiol benzoate.
DR DrugBank; DB13954; Estradiol cypionate.
DR DrugBank; DB13955; Estradiol dienanthate.
DR DrugBank; DB13956; Estradiol valerate.
DR DrugBank; DB01196; Estramustine.
DR DrugBank; DB04573; Estriol.
DR DrugBank; DB14641; Estriol tripropionate.
DR DrugBank; DB00655; Estrone.
DR DrugBank; DB04574; Estrone sulfate.
DR DrugBank; DB00977; Ethinylestradiol.
DR DrugBank; DB00823; Ethynodiol diacetate.
DR DrugBank; DB09086; Eugenol.
DR DrugBank; DB15690; Fluoroestradiol F-18.
DR DrugBank; DB01185; Fluoxymesterone.
DR DrugBank; DB00947; Fulvestrant.
DR DrugBank; DB01645; Genistein.
DR DrugBank; DB11619; Gestrinone.
DR DrugBank; DB00756; Hexachlorophene.
DR DrugBank; DB07931; Hexestrol.
DR DrugBank; DB11064; Homosalate.
DR DrugBank; DB06202; Lasofoxifene.
DR DrugBank; DB00367; Levonorgestrel.
DR DrugBank; DB00431; Lindane.
DR DrugBank; DB00603; Medroxyprogesterone acetate.
DR DrugBank; DB01065; Melatonin.
DR DrugBank; DB01357; Mestranol.
DR DrugBank; DB06710; Methyltestosterone.
DR DrugBank; DB00648; Mitotane.
DR DrugBank; DB07991; N-[(1R)-3-(4-HYDROXYPHENYL)-1-METHYLPROPYL]-2-(2-PHENYL-1H-INDOL-3-YL)ACETAMIDE.
DR DrugBank; DB01183; Naloxone.
DR DrugBank; DB03467; Naringenin.
DR DrugBank; DB09371; Norethynodrel.
DR DrugBank; DB00957; Norgestimate.
DR DrugBank; DB05662; NP-50301.
DR DrugBank; DB09535; Octocrylene.
DR DrugBank; DB04938; Ospemifene.
DR DrugBank; DB01428; Oxybenzone.
DR DrugBank; DB04930; Permethrin.
DR DrugBank; DB04824; Phenolphthalein.
DR DrugBank; DB02746; Phthalic Acid.
DR DrugBank; DB09369; Polyestradiol phosphate.
DR DrugBank; DB01708; Prasterone.
DR DrugBank; DB00396; Progesterone.
DR DrugBank; DB12450; Propyl Gallate.
DR DrugBank; DB02757; Pyrazole.
DR DrugBank; DB04216; Quercetin.
DR DrugBank; DB04575; Quinestrol.
DR DrugBank; DB11541; Ractopamine.
DR DrugBank; DB00481; Raloxifene.
DR DrugBank; DB02709; Resveratrol.
DR DrugBank; DB02901; Stanolone.
DR DrugBank; DB13951; Stanolone acetate.
DR DrugBank; DB09317; Synthetic Conjugated Estrogens, A.
DR DrugBank; DB09318; Synthetic Conjugated Estrogens, B.
DR DrugBank; DB00675; Tamoxifen.
DR DrugBank; DB05966; TAS-108.
DR DrugBank; DB00624; Testosterone.
DR DrugBank; DB13943; Testosterone cypionate.
DR DrugBank; DB13944; Testosterone enanthate.
DR DrugBank; DB13946; Testosterone undecanoate.
DR DrugBank; DB09070; Tibolone.
DR DrugBank; DB00539; Toremifene.
DR DrugBank; DB01108; Trilostane.
DR DrugBank; DB11478; Zeranol.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR DrugCentral; P03372; -.
DR GuidetoPHARMACOLOGY; 620; -.
DR SwissLipids; SLP:000001568; -.
DR MoonDB; P03372; Predicted.
DR GlyConnect; 144; 1 O-Linked glycan.
DR GlyGen; P03372; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P03372; -.
DR PhosphoSitePlus; P03372; -.
DR SwissPalm; P03372; -.
DR BioMuta; ESR1; -.
DR DMDM; 544257; -.
DR CPTAC; CPTAC-1241; -.
DR CPTAC; CPTAC-145; -.
DR EPD; P03372; -.
DR jPOST; P03372; -.
DR MassIVE; P03372; -.
DR PaxDb; P03372; -.
DR PeptideAtlas; P03372; -.
DR PRIDE; P03372; -.
DR ProteomicsDB; 51607; -. [P03372-1]
DR ProteomicsDB; 51608; -. [P03372-2]
DR ProteomicsDB; 51609; -. [P03372-3]
DR ProteomicsDB; 51610; -. [P03372-4]
DR ABCD; P03372; 5 sequenced antibodies.
DR Antibodypedia; 739; 4181 antibodies from 55 providers.
DR DNASU; 2099; -.
DR Ensembl; ENST00000206249.8; ENSP00000206249.3; ENSG00000091831.25. [P03372-1]
DR Ensembl; ENST00000338799.9; ENSP00000342630.5; ENSG00000091831.25. [P03372-1]
DR Ensembl; ENST00000440973.5; ENSP00000405330.1; ENSG00000091831.25. [P03372-1]
DR Ensembl; ENST00000443427.5; ENSP00000387500.1; ENSG00000091831.25. [P03372-1]
DR GeneID; 2099; -.
DR KEGG; hsa:2099; -.
DR MANE-Select; ENST00000206249.8; ENSP00000206249.3; NM_000125.4; NP_000116.2.
DR UCSC; uc003qom.5; human. [P03372-1]
DR CTD; 2099; -.
DR DisGeNET; 2099; -.
DR GeneCards; ESR1; -.
DR HGNC; HGNC:3467; ESR1.
DR HPA; ENSG00000091831; Tissue enhanced (cervix, endometrium, fallopian tube).
DR MalaCards; ESR1; -.
DR MIM; 133430; gene.
DR MIM; 615363; phenotype.
DR neXtProt; NX_P03372; -.
DR OpenTargets; ENSG00000091831; -.
DR Orphanet; 785; Estrogen resistance syndrome.
DR PharmGKB; PA156; -.
DR VEuPathDB; HostDB:ENSG00000091831; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000158133; -.
DR InParanoid; P03372; -.
DR OMA; QCDARDE; -.
DR OrthoDB; 487299at2759; -.
DR PhylomeDB; P03372; -.
DR TreeFam; TF323751; -.
DR PathwayCommons; P03372; -.
DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR Reactome; R-HSA-8931987; RUNX1 regulates estrogen receptor mediated transcription.
DR Reactome; R-HSA-8939211; ESR-mediated signaling.
DR Reactome; R-HSA-8939256; RUNX1 regulates transcription of genes involved in WNT signaling.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; P03372; -.
DR SIGNOR; P03372; -.
DR BioGRID-ORCS; 2099; 29 hits in 1095 CRISPR screens.
DR ChiTaRS; ESR1; human.
DR EvolutionaryTrace; P03372; -.
DR GeneWiki; Estrogen_receptor_alpha; -.
DR GenomeRNAi; 2099; -.
DR Pharos; P03372; Tclin.
DR PRO; PR:P03372; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P03372; protein.
DR Bgee; ENSG00000091831; Expressed in oviduct epithelium and 158 other tissues.
DR ExpressionAtlas; P03372; baseline and differential.
DR Genevisible; P03372; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0097550; C:transcription preinitiation complex; IDA:CAFA.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0051117; F:ATPase binding; IDA:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0034056; F:estrogen response element binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; NAS:UniProtKB.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IDA:BHF-UCL.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:CAFA.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IPI:CAFA.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; IPI:CAFA.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:ARUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008209; P:androgen metabolic process; IEA:Ensembl.
DR GO; GO:0001547; P:antral ovarian follicle growth; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:ARUK-UCL.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; NAS:UniProtKB.
DR GO; GO:0002064; P:epithelial cell development; IEA:Ensembl.
DR GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:CAFA.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
DR GO; GO:0060745; P:mammary gland branching involved in pregnancy; IEA:Ensembl.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:1903799; P:negative regulation of miRNA maturation; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:UniProtKB.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IDA:CAFA.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; IEA:Ensembl.
DR GO; GO:0060523; P:prostate epithelial cord elongation; IEA:Ensembl.
DR GO; GO:0071168; P:protein localization to chromatin; IMP:BHF-UCL.
DR GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IEA:Ensembl.
DR GO; GO:1904035; P:regulation of epithelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL.
DR GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0060065; P:uterus development; IEA:Ensembl.
DR GO; GO:0060068; P:vagina development; IEA:Ensembl.
DR DisProt; DP00074; -.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID00013; -.
DR InterPro; IPR024178; Est_rcpt/est-rel_rcp.
DR InterPro; IPR001292; Estr_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR024736; Oestrogen-typ_rcpt_final_C_dom.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF12743; ESR1_C; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF02159; Oest_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PIRSF; PIRSF500101; ER-a; 1.
DR PIRSF; PIRSF002527; ER-like_NR; 1.
DR PRINTS; PR00543; OESTROGENR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative promoter usage; Alternative splicing;
KW Cell membrane; Cytoplasm; Direct protein sequencing; Disease variant;
KW DNA-binding; Glycoprotein; Golgi apparatus; Lipid-binding; Lipoprotein;
KW Membrane; Metal-binding; Methylation; Nucleus; Palmitate; Phosphoprotein;
KW Receptor; Reference proteome; Steroid-binding; Transcription;
KW Transcription regulation; Transmembrane; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..595
FT /note="Estrogen receptor"
FT /id="PRO_0000053618"
FT DOMAIN 311..547
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 185..250
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 185..205
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 221..245
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..184
FT /note="Modulating (transactivation AF-1); mediates
FT interaction with MACROD1"
FT /evidence="ECO:0000269|PubMed:17914104"
FT REGION 35..174
FT /note="Interaction with DDX5; self-association"
FT /evidence="ECO:0000269|PubMed:11682626"
FT REGION 35..47
FT /note="Required for interaction with NCOA1"
FT /evidence="ECO:0000269|PubMed:11682626"
FT REGION 147..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..310
FT /note="Mediates interaction with DNTTIP2"
FT /evidence="ECO:0000269|PubMed:15047147"
FT REGION 251..310
FT /note="Hinge"
FT REGION 259..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..595
FT /note="Interaction with AKAP13"
FT /evidence="ECO:0000269|PubMed:9627117"
FT REGION 264..595
FT /note="Self-association"
FT REGION 311..595
FT /note="Transactivation AF-2"
FT REGION 553..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000269|PubMed:10428798"
FT MOD_RES 106
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000269|PubMed:10428798"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14764652"
FT MOD_RES 167
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:7838153"
FT MOD_RES 260
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:18657504,
FT ECO:0000269|PubMed:24498420"
FT MOD_RES 537
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000269|PubMed:7539106"
FT LIPID 447
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 10
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..173
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16165085,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_042460"
FT VAR_SEQ 255..366
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3753802"
FT /id="VSP_003680"
FT VAR_SEQ 458..595
FT /note="VYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLL
FT ILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHL
FT ATAGSTSSHSLQKYYITGEAEGFPATV -> FTISHVEAKKRILNLHPKIFGNKWFPRV
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16165085,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_042461"
FT VARIANT 6
FT /note="H -> Y (in a breast cancer sample; somatic mutation;
FT dbSNP:rs139960913)"
FT /evidence="ECO:0000269|PubMed:17224074"
FT /id="VAR_033028"
FT VARIANT 77
FT /note="G -> S (in dbSNP:rs9340773)"
FT /id="VAR_018905"
FT VARIANT 160
FT /note="G -> C (in dbSNP:rs149308960)"
FT /evidence="ECO:0000269|PubMed:9195227"
FT /id="VAR_004671"
FT VARIANT 264
FT /note="M -> I (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17224074"
FT /id="VAR_033029"
FT VARIANT 375
FT /note="Q -> H (in ESTRR; results in highly reduced
FT activity; dbSNP:rs397509428)"
FT /evidence="ECO:0000269|PubMed:23841731"
FT /id="VAR_070072"
FT VARIANT 394
FT /note="R -> H (in ESTRR; highly decreased estrogen receptor
FT activity; dbSNP:rs1131692059)"
FT /evidence="ECO:0000269|PubMed:27754803"
FT /id="VAR_078516"
FT VARIANT 400
FT /note="G -> V (destabilizes the receptor and decreases its
FT affinity for estradiol at 25 degrees Celsius, but not at 4
FT degrees Celsius)"
FT /evidence="ECO:0000269|PubMed:2792078,
FT ECO:0000269|PubMed:3753802, ECO:0000269|PubMed:3754034"
FT /id="VAR_004673"
FT VARIANT 411
FT /note="D -> RNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGV
FT YTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHM
FT (in a 80 kDa form found in a breast cancer line; contains
FT an in-frame duplication of exons 6 and 7)"
FT /id="VAR_010143"
FT MUTAGEN 39
FT /note="L->P: Impairs AF-1 transactivation."
FT /evidence="ECO:0000269|PubMed:11075817"
FT MUTAGEN 43
FT /note="Y->P: Impairs AF-1 transactivation."
FT /evidence="ECO:0000269|PubMed:11075817"
FT MUTAGEN 104
FT /note="S->A: Loss of cyclin A-dependent induction of
FT transcriptional activation."
FT /evidence="ECO:0000269|PubMed:10428798"
FT MUTAGEN 106
FT /note="S->A: Loss of cyclin A-dependent induction of
FT transcriptional activation."
FT /evidence="ECO:0000269|PubMed:10428798"
FT MUTAGEN 118
FT /note="S->A: Decreases phosphorylation and transactivation
FT activity. Abolishes AF-1 transactivation. Insensitive to
FT PPP5C inhibition of transactivation activity."
FT /evidence="ECO:0000269|PubMed:10409727,
FT ECO:0000269|PubMed:14764652"
FT MUTAGEN 118
FT /note="S->E: Enhances transactivation activity. Insensitive
FT to PPP5C inhibition of transactivation activity."
FT /evidence="ECO:0000269|PubMed:14764652"
FT MUTAGEN 260
FT /note="R->A,K: Loss of methylation."
FT /evidence="ECO:0000269|PubMed:18657504"
FT MUTAGEN 364
FT /note="V->E: Has higher transcriptional activity in the
FT absence of wild type ER. Inhibits transcriptional activity
FT when coexpressed with the wild type receptor."
FT /evidence="ECO:0000269|PubMed:8961262"
FT MUTAGEN 386
FT /note="I->C: Loss of transmembrane localization, no effect
FT on peripheral membrane localization. Impairs activation of
FT estrogen-induced activation of NOS3 and production of
FT nitric oxide. No effect on binding to ERES."
FT /evidence="ECO:0000269|PubMed:21937726"
FT MUTAGEN 447
FT /note="C->A: Loss of hormone binding capacity and
FT temperature-sensitive loss in DNA-binding."
FT /evidence="ECO:0000269|PubMed:1577818"
FT MUTAGEN 537
FT /note="Y->A: Reduces PELP1-mediated activation of
FT transcriptional activity."
FT /evidence="ECO:0000269|PubMed:14963108"
FT MUTAGEN 539
FT /note="L->A: Abolishes interaction with NCOA1, NCOA2 and
FT NCOA3."
FT /evidence="ECO:0000269|PubMed:12554772"
FT CONFLICT 452
FT /note="I -> L (in Ref. 5; CAE45969)"
FT /evidence="ECO:0000305"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1HCQ"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1HCP"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1HCQ"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1HCQ"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:1HCQ"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1HCQ"
FT TURN 231..236
FT /evidence="ECO:0007829|PDB:1HCQ"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:1HCQ"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:2LLO"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3Q95"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:7NFB"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:7NFB"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:7RRX"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:2QZO"
FT HELIX 339..363
FT /evidence="ECO:0007829|PDB:7NFB"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:7NFB"
FT HELIX 372..395
FT /evidence="ECO:0007829|PDB:7NFB"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2QE4"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:7NFB"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:7NFB"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:7NFB"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:6VMU"
FT HELIX 421..438
FT /evidence="ECO:0007829|PDB:7NFB"
FT HELIX 442..455
FT /evidence="ECO:0007829|PDB:7NFB"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:6VIG"
FT HELIX 466..492
FT /evidence="ECO:0007829|PDB:7NFB"
FT HELIX 497..530
FT /evidence="ECO:0007829|PDB:7NFB"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:7RS0"
FT HELIX 538..545
FT /evidence="ECO:0007829|PDB:7NFB"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:6SUO"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:5N10"
SQ 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
