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

 ESR1_HUMAN              Reviewed;         595 AA.
P03372; Q13511; Q14276; Q5T5H7; Q6MZQ9; Q9NU51; Q9UDZ7; Q9UIS7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 2.
30-AUG-2017, entry version 243.
RecName: Full=Estrogen receptor;
Short=ER;
AltName: Full=ER-alpha;
AltName: Full=Estradiol receptor;
AltName: Full=Nuclear receptor subfamily 3 group A member 1;
Name=ESR1; Synonyms=ESR, NR3A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-400.
PubMed=3754034; DOI=10.1038/320134a0;
Green S., Walter P., Kumar V., Krust A., Bornert J.-M., Argos P.,
Chambon P.;
"Human oestrogen receptor cDNA: sequence, expression and homology to
v-erb-A.";
Nature 320:134-139(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-400.
PubMed=3753802; DOI=10.1126/science.3753802;
Greene G.L., Gilna P., Waterfield M., Baker A., Hort Y., Shine J.;
"Sequence and expression of human estrogen receptor complementary
DNA.";
Science 231:1150-1154(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mammary gland;
PubMed=8600466; DOI=10.1093/nar/24.5.962;
Pink J.J., Wu S.Q., Wolf D.M., Bilimoria M.M., Jordan V.C.;
"A novel 80 kDa human estrogen receptor containing a duplication of
exons 6 and 7.";
Nucleic Acids Res. 24:962-969(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE PROMOTER USAGE,
AND SUBCELLULAR LOCATION.
TISSUE=Placenta;
PubMed=16165085; DOI=10.1016/j.bbrc.2005.08.226;
Wang Z., Zhang X., Shen P., Loggie B.W., Chang Y., Deuel T.F.;
"Identification, cloning, and expression of human estrogen receptor-
alpha36, a novel variant of human estrogen receptor-alpha66.";
Biochem. Biophys. Res. Commun. 336:1023-1027(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 110-117, PHOSPHORYLATION, AND MUTAGENESIS.
PubMed=7476978; DOI=10.1210/mend.9.8.7476978;
Joel P.B., Traish A.M., Lannigan D.A.;
"Estradiol and phorbol ester cause phosphorylation of serine 118 in
the human estrogen receptor.";
Mol. Endocrinol. 9:1041-1052(1995).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 152-595 (ISOFORM 1).
PubMed=10619354; DOI=10.1016/S0960-0760(99)00126-0;
Schubert E.L., Lee M.K., Newman B., King M.C.;
"Single nucleotide polymorphisms (SNPs) in the estrogen receptor gene
and breast cancer susceptibility.";
J. Steroid Biochem. Mol. Biol. 71:21-27(1999).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 216-434 (ISOFORM 2).
TISSUE=Mammary carcinoma;
PubMed=7916651;
Pfeffer U., Fecarotta E., Castagnetta L., Vidali G.;
"Estrogen receptor variant messenger RNA lacking exon 4 in estrogen-
responsive human breast cancer cell lines.";
Cancer Res. 53:741-743(1993).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 354-548.
TISSUE=Mammary carcinoma;
Naundorf H., Becker M., Fiebig C., Buettner B., Fichtner I.;
"Mechanisms of acquired tamoxifen resistance in a xenotransplanted
human breast carcinoma.";
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[14]
PROTEIN SEQUENCE OF 532-542, AND PHOSPHORYLATION AT TYR-537.
PubMed=7539106; DOI=10.1210/mend.9.1.7539106;
Arnold S.F., Obourn J.D., Jaffe H., Notides A.C.;
"Phosphorylation of the human estrogen receptor on tyrosine 537 in
vivo and by src family tyrosine kinases in vitro.";
Mol. Endocrinol. 9:24-33(1995).
[15]
MUTAGENESIS OF CYS-447.
PubMed=1577818;
Reese J.C., Katzenellenbogen B.S.;
"Characterization of a temperature-sensitive mutation in the hormone
binding domain of the human estrogen receptor. Studies in cell
extracts and intact cells and their implications for hormone-dependent
transcriptional activation.";
J. Biol. Chem. 267:9868-9873(1992).
[16]
PHOSPHORYLATION AT SER-167 BY CK2.
PubMed=7838153; DOI=10.1210/mend.8.9.7838153;
Arnold S.F., Obourn J.D., Jaffe H., Notides A.C.;
"Serine 167 is the major estradiol-induced phosphorylation site on the
human estrogen receptor.";
Mol. Endocrinol. 8:1208-1214(1994).
[17]
FUNCTION IN TRANSREPRESSION OF NF-KAPPA-B.
PubMed=7651415; DOI=10.1128/MCB.15.9.4971;
Stein B., Yang M.X.;
"Repression of the interleukin-6 promoter by estrogen receptor is
mediated by NF-kappa B and C/EBP beta.";
Mol. Cell. Biol. 15:4971-4979(1995).
[18]
MUTAGENESIS OF VAL-364.
PubMed=8961262; DOI=10.1210/mend.10.12.8961262;
McInerney E.M., Ince B.A., Shapiro D.J., Katzenellenbogen B.S.;
"A transcriptionally active estrogen receptor mutant is a novel type
of dominant negative inhibitor of estrogen action.";
Mol. Endocrinol. 10:1519-1526(1996).
[19]
INTERACTION WITH DDX5, AND MUTAGENESIS OF SER-118.
PubMed=10409727; DOI=10.1128/MCB.19.8.5363;
Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H.,
Yanagisawa J., Metzger D., Hashimoto S., Kato S.;
"Purification and identification of p68 RNA helicase acting as a
transcriptional coactivator specific for the activation function 1 of
human estrogen receptor alpha.";
Mol. Cell. Biol. 19:5363-5372(1999).
[20]
FUNCTION (ISOFORM 3), TISSUE SPECIFICITY, ALTERNATIVE PROMOTER USAGE
(ISOFORM 3), AND SUBUNIT.
PubMed=10970861; DOI=10.1093/emboj/19.17.4688;
Flouriot G., Brand H., Denger S., Metivier R., Kos M., Reid G.,
Sonntag-Buck V., Gannon F.;
"Identification of a new isoform of the human estrogen receptor-alpha
(hER-alpha) that is encoded by distinct transcripts and that is able
to repress hER-alpha activation function 1.";
EMBO J. 19:4688-4700(2000).
[21]
MUTAGENESIS OF LEU-39 AND TYR-43.
PubMed=11075817; DOI=10.1210/mend.14.11.0546;
Metivier R., Petit F.G., Valotaire Y., Pakdel F.;
"Function of N-terminal transactivation domain of the estrogen
receptor requires a potential alpha-helical structure and is
negatively regulated by the A domain.";
Mol. Endocrinol. 14:1849-1871(2000).
[22]
INTERACTION WITH NCOA1; NCOA2 AND NCOA3, SUBUNIT, AND MUTAGENESIS OF
LEU-539.
PubMed=12554772; DOI=10.1210/me.2002-0351;
Bai Y., Giguere V.;
"Isoform-selective interactions between estrogen receptors and steroid
receptor coactivators promoted by estradiol and ErbB-2 signaling in
living cells.";
Mol. Endocrinol. 17:589-599(2003).
[23]
SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), AND PALMITOYLATION (ISOFORM
3).
PubMed=12682286; DOI=10.1073/pnas.0831079100;
Li L., Haynes M.P., Bender J.R.;
"Plasma membrane localization and function of the estrogen receptor
alpha variant (ER46) in human endothelial cells.";
Proc. Natl. Acad. Sci. U.S.A. 100:4807-4812(2003).
[24]
GLYCOSYLATION.
PubMed=8999954;
Jiang M.S., Hart G.W.;
"A subpopulation of estrogen receptors are modified by O-linked N-
acetylglucosamine.";
J. Biol. Chem. 272:2421-2428(1997).
[25]
FUNCTION, AND INTERACTION WITH SP1.
PubMed=9328340; DOI=10.1210/mend.11.11.9916;
Porter W., Saville B., Hoivik D., Safe S.;
"Functional synergy between the transcription factor Sp1 and the
estrogen receptor.";
Mol. Endocrinol. 11:1569-1580(1997).
[26]
INTERACTION WITH AKAP13.
PubMed=9627117; DOI=10.1038/sj.onc.1201783;
Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O.,
Pagliai K., Gray K., Gutkind S., Segars J.;
"Characterization of Brx, a novel Dbl family member that modulates
estrogen receptor action.";
Oncogene 16:2513-2526(1998).
[27]
PHOSPHORYLATION AT SER-104 AND SER-106, AND MUTAGENESIS.
PubMed=10428798; DOI=10.1074/jbc.274.32.22296;
Rogatsky I., Trowbridge J.M., Garabedian M.J.;
"Potentiation of human estrogen receptor alpha transcriptional
activation through phosphorylation of serines 104 and 106 by the
cyclin A-CDK2 complex.";
J. Biol. Chem. 274:22296-22302(1999).
[28]
INTERACTION WITH NCOA6.
PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y.,
Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D.,
Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
"A nuclear factor ASC-2, as a cancer-amplified transcriptional
coactivator essential for ligand-dependent transactivation by nuclear
receptors in vivo.";
J. Biol. Chem. 274:34283-34293(1999).
[29]
INTERACTION WITH PHB2.
PubMed=10359819; DOI=10.1073/pnas.96.12.6947;
Montano M.M., Ekena K., Delage-Mourroux R., Chang W., Martini P.,
Katzenellenbogen B.S.;
"An estrogen receptor-selective coregulator that potentiates the
effectiveness of antiestrogens and represses the activity of
estrogens.";
Proc. Natl. Acad. Sci. U.S.A. 96:6947-6952(1999).
[30]
INTERACTION WITH NCOA2.
PubMed=11265755; DOI=10.1093/embo-reports/kvd028;
Benecke A., Chambon P., Gronemeyer H.;
"Synergy between estrogen receptor alpha activation functions AF1 and
AF2 mediated by transcription intermediary factor TIF2.";
EMBO Rep. 1:151-157(2000).
[31]
FUNCTION, AND INTERACTION WITH SP1.
PubMed=10681512; DOI=10.1074/jbc.275.8.5379;
Saville B., Wormke M., Wang F., Nguyen T., Enmark E., Kuiper G.,
Gustafsson J.A., Safe S.;
"Ligand-, cell-, and estrogen receptor subtype (alpha/beta)-dependent
activation at GC-rich (Sp1) promoter elements.";
J. Biol. Chem. 275:5379-5387(2000).
[32]
FUNCTION, AND INTERACTION WITH SP3.
PubMed=10816575; DOI=10.1074/jbc.M002188200;
Stoner M., Wang F., Wormke M., Nguyen T., Samudio I., Vyhlidal C.,
Marme D., Finkenzeller G., Safe S.;
"Inhibition of vascular endothelial growth factor expression in HEC1A
endometrial cancer cells through interactions of estrogen receptor
alpha and Sp3 proteins.";
J. Biol. Chem. 275:22769-22779(2000).
[33]
INTERACTION WITH CITED1 AND EP300.
PubMed=11581164; DOI=10.1101/gad.906301;
Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y.,
Kato S., Isselbacher K.J., Brown M., Shioda T.;
"Selective coactivation of estrogen-dependent transcription by CITED1
CBP/p300-binding protein.";
Genes Dev. 15:2598-2612(2001).
[34]
FUNCTION, AND INTERACTION WITH JUN; JUNB AND JUND.
PubMed=11477071; DOI=10.1074/jbc.M101806200;
Teyssier C., Belguise K., Galtier F., Chalbos D.;
"Characterization of the physical interaction between estrogen
receptor alpha and JUN proteins.";
J. Biol. Chem. 276:36361-36369(2001).
[35]
INTERACTION WITH KDM5A.
PubMed=11358960; DOI=10.1074/jbc.M100313200;
Chan S.W., Hong W.;
"Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone
receptor-mediated transcription.";
J. Biol. Chem. 276:28402-28412(2001).
[36]
INTERACTION WITH NCOA5.
PubMed=11113208; DOI=10.1128/MCB.21.1.343-353.2001;
Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F.,
Giguere V.;
"CIA, a novel estrogen receptor coactivator with a bifunctional
nuclear receptor interacting determinant.";
Mol. Cell. Biol. 21:343-353(2001).
[37]
FUNCTION, AND INTERACTION WITH NCOA1 AND DDX5.
PubMed=11682626; DOI=10.1210/mend.15.11.0727;
Metivier R., Penot G., Flouriot G., Pakdel F.;
"Synergism between ERalpha transactivation function 1 (AF-1) and AF-2
mediated by steroid receptor coactivator protein-1: requirement for
the AF-1 alpha-helical core and for a direct interaction between the
N- and C-terminal domains.";
Mol. Endocrinol. 15:1953-1970(2001).
[38]
INTERACTION WITH PRMT2.
PubMed=12039952; DOI=10.1074/jbc.M201053200;
Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
"Identification of protein arginine methyltransferase 2 as a
coactivator for estrogen receptor alpha.";
J. Biol. Chem. 277:28624-28630(2002).
[39]
INTERACTION WITH NR2C1.
PubMed=12093804; DOI=10.1074/jbc.M203531200;
Hu Y.C., Shyr C.R., Che W., Mu X.M., Kim E., Chang C.;
"Suppression of estrogen receptor-mediated transcription and cell
growth by interaction with TR2 orphan receptor.";
J. Biol. Chem. 277:33571-33579(2002).
[40]
INTERACTION WITH NCOA7.
PubMed=11971969; DOI=10.1128/MCB.22.10.3358-3372.2002;
Shao W., Halachmi S., Brown M.;
"ERAP140, a conserved tissue-specific nuclear receptor coactivator.";
Mol. Cell. Biol. 22:3358-3372(2002).
[41]
INTERACTION WITH RBFOX2.
PubMed=11875103; DOI=10.1210/mend.16.3.0787;
Norris J.D., Fan D., Sherk A., McDonnell D.P.;
"A negative coregulator for the human ER.";
Mol. Endocrinol. 16:459-468(2002).
[42]
INTERACTION WITH PELP1.
PubMed=12415108; DOI=10.1073/pnas.192569699;
Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
"Estrogen receptor-interacting protein that modulates its nongenomic
activity-crosstalk with Src/Erk phosphorylation cascade.";
Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002).
[43]
INTERACTION WITH SMARD1.
PubMed=12917342; DOI=10.1128/MCB.23.17.6210-6220.2003;
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
"BAF60a mediates critical interactions between nuclear receptors and
the BRG1 chromatin-remodeling complex for transactivation.";
Mol. Cell. Biol. 23:6210-6220(2003).
[44]
INTERACTION WITH DNTTIP2.
PubMed=15047147; DOI=10.1016/j.bbrc.2004.02.179;
Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W.,
Rao S.M., Zhu Y.-J.;
"ERBP, a novel estrogen receptor binding protein enhancing the
activity of estrogen receptor.";
Biochem. Biophys. Res. Commun. 317:54-59(2004).
[45]
FUNCTION.
PubMed=15078875; DOI=10.1074/jbc.M402148200;
Merot Y., Metivier R., Penot G., Manu D., Saligaut C., Gannon F.,
Pakdel F., Kah O., Flouriot G.;
"The relative contribution exerted by AF-1 and AF-2 transactivation
functions in estrogen receptor alpha transcriptional activity depends
upon the differentiation stage of the cell.";
J. Biol. Chem. 279:26184-26191(2004).
[46]
INTERACTION WITH TXNRD1.
PubMed=15199063; DOI=10.1074/jbc.M402753200;
Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A.,
Spyrou G.;
"An alternative splicing variant of the selenoprotein thioredoxin
reductase is a modulator of estrogen signaling.";
J. Biol. Chem. 279:38721-38729(2004).
[47]
FUNCTION, PHOSPHORYLATION AT SER-118, DEPHOSPHORYLATION AT SER-118 BY
PPP5C, AND MUTAGENESIS OF SER-118.
PubMed=14764652; DOI=10.1210/me.2003-0308;
Ikeda K., Ogawa S., Tsukui T., Horie-Inoue K., Ouchi Y., Kato S.,
Muramatsu M., Inoue S.;
"Protein phosphatase 5 is a negative regulator of estrogen receptor-
mediated transcription.";
Mol. Endocrinol. 18:1131-1143(2004).
[48]
FUNCTION IN NF-KAPPA-B TRANSREPRESSION.
PubMed=16043358; DOI=10.1016/j.cyto.2004.12.008;
Liu H., Liu K., Bodenner D.L.;
"Estrogen receptor inhibits interleukin-6 gene expression by
disruption of nuclear factor kappaB transactivation.";
Cytokine 31:251-257(2005).
[49]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DYNLL1.
PubMed=15891768; DOI=10.1038/sj.embor.7400417;
Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R.,
Kumar R.;
"Functional regulation of oestrogen receptor pathway by the dynein
light chain 1.";
EMBO Rep. 6:538-544(2005).
[50]
ERRATUM.
Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R.,
Kumar R.;
EMBO Rep. 6:1101-1101(2005).
[51]
INTERACTION WITH HEXIM1.
PubMed=15940264; DOI=10.1038/sj.onc.1208728;
Wittmann B.M., Fujinaga K., Deng H., Ogba N., Montano M.M.;
"The breast cell growth inhibitor, estrogen down regulated gene 1,
modulates a novel functional interaction between estrogen receptor
alpha and transcriptional elongation factor cyclin T1.";
Oncogene 24:5576-5588(2005).
[52]
INTERACTION WITH KMT2D.
PubMed=16603732; DOI=10.1074/jbc.M513245200;
Mo R., Rao S.M., Zhu Y.-J.;
"Identification of the MLL2 complex as a coactivator for estrogen
receptor alpha.";
J. Biol. Chem. 281:15714-15720(2006).
[53]
FUNCTION.
PubMed=16684779; DOI=10.1074/jbc.M600021200;
Rayala S.K., den Hollander P., Manavathi B., Talukder A.H., Song C.,
Peng S., Barnekow A., Kremerskothen J., Kumar R.;
"Essential role of KIBRA in co-activator function of dynein light
chain 1 in mammalian cells.";
J. Biol. Chem. 281:19092-19099(2006).
[54]
INTERACTION WITH MUC1.
PubMed=16427018; DOI=10.1016/j.molcel.2005.11.030;
Wei X., Xu H., Kufe D.;
"MUC1 oncoprotein stabilizes and activates estrogen receptor alpha.";
Mol. Cell 21:295-305(2006).
[55]
INTERACTION WITH ZNF366.
PubMed=17085477; DOI=10.1093/nar/gkl875;
Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M.,
Jat P., Kindle K.B., Heery D.M., Parker M.G., Buluwela L.,
Kamalati T., Ali S.;
"ZNF366 is an estrogen receptor corepressor that acts through CtBP and
histone deacetylases.";
Nucleic Acids Res. 34:6126-6136(2006).
[56]
FUNCTION.
PubMed=16617102; DOI=10.1073/pnas.0601989103;
Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P.,
Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
"MTA1, a transcriptional activator of breast cancer amplified sequence
3.";
Proc. Natl. Acad. Sci. U.S.A. 103:6670-6675(2006).
[57]
ERRATUM.
Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P.,
Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013).
[58]
INTERACTION WITH PBXIP1.
PubMed=17043237; DOI=10.1073/pnas.0607445103;
Manavathi B., Acconcia F., Rayala S.K., Kumar R.;
"An inherent role of microtubule network in the action of nuclear
receptor.";
Proc. Natl. Acad. Sci. U.S.A. 103:15981-15986(2006).
[59]
INTERACTION WITH MAP1S.
PubMed=17658481; DOI=10.1016/j.bbrc.2007.06.179;
Eriksson M., Samuelsson H., Samuelsson E.-B., Liu L., McKeehan W.L.,
Benedikz E., Sundstroem E.;
"The NMDAR subunit NR3A interacts with microtubule-associated protein
1S in the brain.";
Biochem. Biophys. Res. Commun. 361:127-132(2007).
[60]
INTERACTION WITH CUEDC2.
PubMed=17347654; DOI=10.1038/sj.emboj.7601602;
Zhang P.-J., Zhao J., Li H.-Y., Man J.-H., He K., Zhou T., Pan X.,
Li A.-L., Gong W.-L., Jin B.-F., Xia Q., Yu M., Shen B.-F.,
Zhang X.-M.;
"CUE domain containing 2 regulates degradation of progesterone
receptor by ubiquitin-proteasome.";
EMBO J. 26:1831-1842(2007).
[61]
INTERACTION WITH MACROD1.
PubMed=17914104; DOI=10.1677/ERC-06-0082;
Han W.-D., Zhao Y.-L., Meng Y.G., Zang L., Wu Z.-Q., Li Q., Si Y.-L.,
Huang K., Ba J.-M., Morinaga H., Nomura M., Mu Y.-M.;
"Estrogenically regulated LRP16 interacts with estrogen receptor alpha
and enhances the receptor's transcriptional activity.";
Endocr. Relat. Cancer 14:741-753(2007).
[62]
SUBCELLULAR LOCATION, AND INTERACTION WITH KIF18A.
PubMed=17006958; DOI=10.1002/jcb.21000;
Luboshits G., Benayahu D.;
"MS-KIF18A, a kinesin, is associated with estrogen receptor.";
J. Cell. Biochem. 100:693-702(2007).
[63]
INTERACTION WITH PRMT2.
PubMed=17587566; DOI=10.1016/j.jsbmb.2007.05.006;
Meyer R., Wolf S.S., Obendorf M.;
"PRMT2, a member of the protein arginine methyltransferase family, is
a coactivator of the androgen receptor.";
J. Steroid Biochem. Mol. Biol. 107:1-14(2007).
[64]
INTERACTION WITH BCAS3.
PubMed=17505058; DOI=10.1210/me.2006-0514;
Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
"Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
coactivator, through proline-, glutamic acid-, and leucine-rich
protein-1 (PELP1).";
Mol. Endocrinol. 21:1847-1860(2007).
[65]
INTERACTION WITH UIMC1.
PubMed=17311814; DOI=10.1093/nar/gkl1112;
Yan J., Kim Y.S., Yang X.-P., Albers M., Koegl M., Jetten A.M.;
"Ubiquitin-interaction motifs of RAP80 are critical in its regulation
of estrogen receptor alpha.";
Nucleic Acids Res. 35:1673-1686(2007).
[66]
INTERACTION WITH ATAD2.
PubMed=17998543; DOI=10.1073/pnas.0705814104;
Zou J.X., Revenko A.S., Li L.B., Gemo A.T., Chen H.-W.;
"ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is
required for coregulator occupancy and chromatin modification.";
Proc. Natl. Acad. Sci. U.S.A. 104:18067-18072(2007).
[67]
FUNCTION IN ASSOCIATION WITH AP-1.
PubMed=18247370; DOI=10.1002/jcp.21379;
Lambertini E., Tavanti E., Torreggiani E., Penolazzi L., Gambari R.,
Piva R.;
"ERalpha and AP-1 interact in vivo with a specific sequence of the F
promoter of the human ERalpha gene in osteoblasts.";
J. Cell. Physiol. 216:101-110(2008).
[68]
METHYLATION AT ARG-260 BY PRMT1, MUTAGENESIS OF ARG-260, SUBCELLULAR
LOCATION, AND INTERACTION WITH PI3KR1/2; SRC AND PTK2/FAK1.
PubMed=18657504; DOI=10.1016/j.molcel.2008.05.025;
Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y.,
Sentis S., Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S.,
Corbo L.;
"Regulation of estrogen rapid signaling through arginine methylation
by PRMT1.";
Mol. Cell 31:212-221(2008).
[69]
FUNCTION IN NF-KAPPA-B TRANSREPRESSION, AND INTERACTION WITH RELA.
PubMed=17932106; DOI=10.1210/me.2007-0324;
Nettles K.W., Gil G., Nowak J., Metivier R., Sharma V.B., Greene G.L.;
"CBP Is a dosage-dependent regulator of nuclear factor-kappaB
suppression by the estrogen receptor.";
Mol. Endocrinol. 22:263-272(2008).
[70]
FUNCTION.
PubMed=17922032; DOI=10.1038/sj.onc.1210839;
Molli P.R., Singh R.R., Lee S.W., Kumar R.;
"MTA1-mediated transcriptional repression of BRCA1 tumor suppressor
gene.";
Oncogene 27:1971-1980(2008).
[71]
INTERACTION WITH CCDC62.
PubMed=18563714; DOI=10.1002/pros.20774;
Chen M., Ni J., Zhang Y., Muyan M., Yeh S.;
"ERAP75 functions as a coactivator to enhance estrogen receptor alpha
transactivation in prostate stromal cells.";
Prostate 68:1273-1282(2008).
[72]
INTERACTION WITH SH2D4A AND PLCG.
PubMed=19712589; DOI=10.5483/BMBRep.2009.42.8.516;
Li T., Li W., Lu J., Liu H., Li Y., Zhao Y.;
"SH2D4A regulates cell proliferation via the ERalpha/PLC-gamma/PKC
pathway.";
BMB Rep. 42:516-522(2009).
[73]
INTERACTION WITH LDB1 AND RLIM.
PubMed=19117995; DOI=10.1158/0008-5472.CAN-08-1630;
Johnsen S.A., Guengoer C., Prenzel T., Riethdorf S., Riethdorf L.,
Taniguchi-Ishigaki N., Rau T., Tursun B., Furlow J.D., Sauter G.,
Scheffner M., Pantel K., Gannon F., Bach I.;
"Regulation of estrogen-dependent transcription by the LIM cofactors
CLIM and RLIM in breast cancer.";
Cancer Res. 69:128-136(2009).
[74]
INTERACTION WITH DNAAF4.
PubMed=19423554; DOI=10.1093/hmg/ddp215;
Massinen S., Tammimies K., Tapia-Paez I., Matsson H., Hokkanen M.E.,
Soederberg O., Landegren U., Castren E., Gustafsson J.A., Treuter E.,
Kere J.;
"Functional interaction of DYX1C1 with estrogen receptors suggests
involvement of hormonal pathways in dyslexia.";
Hum. Mol. Genet. 18:2802-2812(2009).
[75]
FUNCTION IN MUTUAL TRANSREPRESSION WITH NF-KAPPA-B, AND INTERACTION
WITH NFKB1 AND RELA.
PubMed=19350539; DOI=10.1002/jcb.22141;
Gionet N., Jansson D., Mader S., Pratt M.A.;
"NF-kappaB and estrogen receptor alpha interactions: Differential
function in estrogen receptor-negative and -positive hormone-
independent breast cancer cells.";
J. Cell. Biochem. 107:448-459(2009).
[76]
UBIQUITINATION, AND INTERACTION WITH OTUB1.
PubMed=19383985; DOI=10.1074/jbc.M109.007484;
Stanisic V., Malovannaya A., Qin J., Lonard D.M., O'Malley B.W.;
"OTU Domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1)
deubiquitinates estrogen receptor (ER) alpha and affects ERalpha
transcriptional activity.";
J. Biol. Chem. 284:16135-16145(2009).
[77]
PHOSPHORYLATION BY CSNK1D/CK1, AND INTERACTION WITH CSNK1D.
PubMed=19339517; DOI=10.1093/nar/gkp136;
Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J.,
Thomas R.S., Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.;
"CK1delta modulates the transcriptional activity of ERalpha via AIB1
in an estrogen-dependent manner and regulates ERalpha-AIB1
interactions.";
Nucleic Acids Res. 37:3110-3123(2009).
[78]
INTERACTION WITH DDX17.
PubMed=19718048; DOI=10.1038/onc.2009.261;
Wortham N.C., Ahamed E., Nicol S.M., Thomas R.S., Periyasamy M.,
Jiang J., Ochocka A.M., Shousha S., Huson L., Bray S.E., Coombes R.C.,
Ali S., Fuller-Pace F.V.;
"The DEAD-box protein p72 regulates ERalpha-/oestrogen-dependent
transcription and cell growth, and is associated with improved
survival in ERalpha-positive breast cancer.";
Oncogene 28:4053-4064(2009).
[79]
INTERACTION WITH KIF18A.
PubMed=19636373; DOI=10.1371/journal.pone.0006407;
Zusev M., Benayahu D.;
"The regulation of MS-KIF18A expression and cross talk with estrogen
receptor.";
PLoS ONE 4:E6407-E6407(2009).
[80]
FUNCTION, INTERACTION WITH CCAR2, AND SUBCELLULAR LOCATION.
PubMed=20074560; DOI=10.1016/j.bbrc.2010.01.025;
Koyama S., Wada-Hiraike O., Nakagawa S., Tanikawa M., Hiraike H.,
Miyamoto Y., Sone K., Oda K., Fukuhara H., Nakagawa K., Kato S.,
Yano T., Taketani Y.;
"Repression of estrogen receptor beta function by putative tumor
suppressor DBC1.";
Biochem. Biophys. Res. Commun. 392:357-362(2010).
[81]
FUNCTION IN SYNERGISM WITH NF-KAPPA-B.
PubMed=20705611; DOI=10.1074/jbc.M110.155309;
Pradhan M., Bembinster L.A., Baumgarten S.C., Frasor J.;
"Proinflammatory cytokines enhance estrogen-dependent expression of
the multidrug transporter gene ABCG2 through estrogen receptor and
NF{kappa}B cooperativity at adjacent response elements.";
J. Biol. Chem. 285:31100-31106(2010).
[82]
INTERACTION WITH ZFHX3.
PubMed=20720010; DOI=10.1074/jbc.M110.128330;
Dong X.Y., Sun X., Guo P., Li Q., Sasahara M., Ishii Y., Dong J.T.;
"ATBF1 inhibits estrogen receptor (ER) function by selectively
competing with AIB1 for binding to the ER in ER-positive breast cancer
cells.";
J. Biol. Chem. 285:32801-32809(2010).
[83]
INTERACTION WITH ESRRB.
PubMed=19755138; DOI=10.1016/j.mce.2009.09.007;
Bombail V., Collins F., Brown P., Saunders P.T.;
"Modulation of ER alpha transcriptional activity by the orphan nuclear
receptor ERR beta and evidence for differential effects of long- and
short-form splice variants.";
Mol. Cell. Endocrinol. 314:53-61(2010).
[84]
INTERACTION WITH SAV1 AND STK3/MST2.
PubMed=21104395; DOI=10.1007/s00109-010-0698-y;
Park Y., Park J., Lee Y., Lim W., Oh B.C., Shin C., Kim W., Lee Y.;
"Mammalian MST2 kinase and human Salvador activate and reduce estrogen
receptor alpha in the absence of ligand.";
J. Mol. Med. 89:181-191(2011).
[85]
FUNCTION (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM 3), TOPOLOGY
(ISOFORM 3), AND MUTAGENESIS OF ILE-386.
PubMed=21937726; DOI=10.1091/mbc.E11-05-0416;
Kim K.H., Toomre D., Bender J.R.;
"Splice isoform estrogen receptors as integral transmembrane
proteins.";
Mol. Biol. Cell 22:4415-4423(2011).
[86]
FUNCTION IN ERE-INDEPENDENT SIGNALING.
PubMed=21330404; DOI=10.1210/me.2010-0425;
Heldring N., Isaacs G.D., Diehl A.G., Sun M., Cheung E., Ranish J.A.,
Kraus W.L.;
"Multiple sequence-specific DNA-binding proteins mediate estrogen
receptor signaling through a tethering pathway.";
Mol. Endocrinol. 25:564-574(2011).
[87]
INTERACTION WITH LMTK3, PHOSPHORYLATION, AND UBIQUITINATION.
PubMed=21602804; DOI=10.1038/nm.2351;
Giamas G., Filipovic A., Jacob J., Messier W., Zhang H., Yang D.,
Zhang W., Shifa B.A., Photiou A., Tralau-Stewart C., Castellano L.,
Green A.R., Coombes R.C., Ellis I.O., Ali S., Lenz H.J., Stebbing J.;
"Kinome screening for regulators of the estrogen receptor identifies
LMTK3 as a new therapeutic target in breast cancer.";
Nat. Med. 17:715-719(2011).
[88]
SUBCELLULAR LOCATION, AND PALMITOYLATION.
PubMed=22031296; DOI=10.1091/mbc.E11-07-0638;
Pedram A., Razandi M., Deschenes R.J., Levin E.R.;
"DHHC-7 and -21 are palmitoylacyltransferases for sex steroid
receptors.";
Mol. Biol. Cell 23:188-199(2012).
[89]
FUNCTION IN SYNERGISM WITH NF-KAPPA-B.
PubMed=22083956; DOI=10.1128/MCB.05869-11;
Pradhan M., Baumgarten S.C., Bembinster L.A., Frasor J.;
"CBP mediates NF-kappaB-dependent histone acetylation and estrogen
receptor recruitment to an estrogen response element in the BIRC3
promoter.";
Mol. Cell. Biol. 32:569-575(2012).
[90]
SUBCELLULAR LOCATION, AND INTERACTION WITH CLOCK.
PubMed=23160374; DOI=10.1038/onc.2012.518;
Li S., Wang M., Ao X., Chang A.K., Yang C., Zhao F., Bi H., Liu Y.,
Xiao L., Wu H.;
"CLOCK is a substrate of SUMO and sumoylation of CLOCK upregulates the
transcriptional activity of estrogen receptor-alpha.";
Oncogene 32:4883-4891(2013).
[91]
INTERACTION WITH SFR1.
PubMed=23874500; DOI=10.1371/journal.pone.0068075;
Feng Y., Singleton D., Guo C., Gardner A., Pakala S., Kumar R.,
Jensen E., Zhang J., Khan S.;
"DNA homologous recombination factor SFR1 physically and functionally
interacts with estrogen receptor alpha.";
PLoS ONE 8:E68075-E68075(2013).
[92]
INTERACTION WITH TRIP4.
PubMed=25219498; DOI=10.1016/j.molcel.2014.08.007;
Yoo H.M., Kang S.H., Kim J.Y., Lee J.E., Seong M.W., Lee S.W.,
Ka S.H., Sou Y.S., Komatsu M., Tanaka K., Lee S.T., Noh D.Y.,
Baek S.H., Jeon Y.J., Chung C.H.;
"Modification of ASC1 by UFM1 is crucial for ERalpha transactivation
and breast cancer development.";
Mol. Cell 56:261-274(2014).
[93]
INTERACTION WITH DCAF13; LATS1 AND DCAF1, AND UBIQUITINATION.
PubMed=28068668; DOI=10.1038/nature20829;
Britschgi A., Duss S., Kim S., Couto J.P., Brinkhaus H., Koren S.,
De Silva D., Mertz K.D., Kaup D., Varga Z., Voshol H., Vissieres A.,
Leroy C., Roloff T., Stadler M.B., Scheel C.H., Miraglia L.J.,
Orth A.P., Bonamy G.M., Reddy V.A., Bentires-Alj M.;
"The Hippo kinases LATS1 and 2 control human breast cell fate via
crosstalk with ERalpha.";
Nature 541:541-545(2017).
[94]
STRUCTURE BY NMR OF 180-262.
PubMed=2247153; DOI=10.1038/348458a0;
Schwabe J.W.E., Neuhaus D., Rhodes D.;
"Solution structure of the DNA-binding domain of the oestrogen
receptor.";
Nature 348:458-461(1990).
[95]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 180-262.
PubMed=8221895; DOI=10.1016/0092-8674(93)90390-C;
Schwabe J.W.E., Chapman L., Finch J.T., Rhodes D.;
"The crystal structure of the estrogen receptor DNA-binding domain
bound to DNA: how receptors discriminate between their response
elements.";
Cell 75:567-578(1993).
[96]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 305-548.
PubMed=9338790; DOI=10.1038/39645;
Brzozowski A.M., Pike A.C.W., Dauter Z., Hubbard R.E., Bonn T.,
Engstroem O., Oehman L., Greene G.L., Gustafsson J.-A., Carlquist M.;
"Molecular basis of agonism and antagonism in the oestrogen
receptor.";
Nature 389:753-758(1997).
[97]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 306-544.
PubMed=9600906; DOI=10.1073/pnas.95.11.5998;
Tanenbaum D.M., Wang Y., Williams S.P., Sigler P.B.;
"Crystallographic comparison of the estrogen and progesterone
receptor's ligand binding domains.";
Proc. Natl. Acad. Sci. U.S.A. 95:5998-6003(1998).
[98]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 294-554.
PubMed=9875847; DOI=10.1016/S0092-8674(00)81717-1;
Shiau A.K., Barstad D., Loria P.M., Cheng L., Kushner P.J.,
Agard D.A., Greene G.L.;
"The structural basis of estrogen receptor/coactivator recognition and
the antagonism of this interaction by tamoxifen.";
Cell 95:927-937(1998).
[99]
3D-STRUCTURE MODELING OF 311-547.
PubMed=9619507; DOI=10.1080/07391102.1998.10508206;
Maalouf G.J., Xu W., Smith T., Mohr S.C.;
"Homology model for the ligand-binding domain of the human estrogen
receptor.";
J. Biomol. Struct. Dyn. 15:841-850(1998).
[100]
VARIANT VAL-400.
PubMed=2792078;
Tora L., Mullick A., Metzger D., Ponglikitmongkol M., Park I.,
Chambon P.;
"The cloned human oestrogen receptor contains a mutation which alters
its hormone binding properties.";
EMBO J. 8:1981-1986(1989).
[101]
VARIANT CYS-160.
PubMed=9195227;
DOI=10.1002/(SICI)1098-1004(1997)9:6<531::AID-HUMU6>3.3.CO;2-J;
Anderson T.I., Wooster R., Laake K., Collins N., Warren W., Skrede M.,
Eeles R., Tveit K.M., Johnston S.R.D., Dowsett M., Olsen A.O.,
Moeller P., Stratton M.R., Boerresen-Dale A.-L.;
"Screening for ESR mutations in breast and ovarian cancer patients.";
Hum. Mutat. 9:531-536(1997).
[102]
INVOLVEMENT IN BMD.
PubMed=10942433; DOI=10.1093/hmg/9.13.2043;
Becherini L., Gennari L., Masi L., Mansani R., Massart F., Morelli A.,
Falchetti A., Gonnelli S., Fiorelli G., Tanini A., Brandi M.L.;
"Evidence of a linkage disequilibrium between polymorphisms in the
human estrogen receptor alpha gene and their relationship to bone mass
variation in postmenopausal Italian women.";
Hum. Mol. Genet. 9:2043-2050(2000).
[103]
INTERACTION WITH GPER1.
PubMed=19749156; DOI=10.1210/me.2009-0120;
Vivacqua A., Lappano R., De Marco P., Sisci D., Aquila S.,
De Amicis F., Fuqua S.A., Ando S., Maggiolini M.;
"G protein-coupled receptor 30 expression is up-regulated by EGF and
TGF alpha in estrogen receptor alpha-positive cancer cells.";
Mol. Endocrinol. 23:1815-1826(2009).
[104]
VARIANTS TYR-6 AND ILE-264.
PubMed=17224074; DOI=10.1186/bcr1637;
Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A.,
Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S.,
Kristensen V., Perou C.M., Boerresen-Dale A.-L.;
"Somatic sequence alterations in twenty-one genes selected by
expression profile analysis of breast carcinomas.";
Breast Cancer Res. 9:R5-R5(2007).
[105]
VARIANT ESTRR HIS-375, AND CHARACTERIZATION OF VARIANT ESTRR HIS-375.
PubMed=23841731; DOI=10.1056/NEJMoa1303611;
Quaynor S.D., Stradtman E.W. Jr., Kim H.G., Shen Y., Chorich L.P.,
Schreihofer D.A., Layman L.C.;
"Delayed puberty and estrogen resistance in a woman with estrogen
receptor alpha variant.";
N. Engl. J. Med. 369:164-171(2013).
[106]
VARIANT ESTRR HIS-394, AND CHARACTERIZATION OF VARIANT ESTRR HIS-394.
PubMed=27754803; DOI=10.1210/jc.2016-2749;
Bernard V., Kherra S., Francou B., Fagart J., Viengchareun S.,
Guechot J., Ladjouze A., Guiochon-Mantel A., Korach K.S., Binart N.,
Lombes M., Christin-Maitre S.;
"Familial multiplicity of estrogen insensitivity associated with a
loss-of-function ESR1 mutation.";
J. Clin. Endocrinol. Metab. 102:93-99(2017).
-!- FUNCTION: Nuclear hormone receptor. The steroid hormones and their
receptors are involved in the regulation of eukaryotic gene
expression and affect cellular proliferation and differentiation
in target tissues. Ligand-dependent nuclear transactivation
involves either direct homodimer binding to a palindromic estrogen
response element (ERE) sequence or association with other DNA-
binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2,
Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding
induces a conformational change allowing subsequent or
combinatorial association with multiprotein coactivator complexes
through LXXLL motifs of their respective components. Mutual
transrepression occurs between the estrogen receptor (ER) and NF-
kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-
binding activity and inhibits NF-kappa-B-mediated transcription
from the IL6 promoter and displace RELA/p65 and associated
coregulators from the promoter. Recruited to the NF-kappa-B
response element of the CCL2 and IL8 promoters and can displace
CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50
on ERE sequences. Can also act synergistically with NF-kappa-B to
activate transcription involving respective recruitment adjacent
response elements; the function involves CREBBP. Can activate the
transcriptional activity of TFF1. Also mediates membrane-initiated
estrogen signaling involving various kinase cascades. Isoform 3 is
involved in activation of NOS3 and endothelial nitric oxide
production. Isoforms lacking one or several functional domains are
thought to modulate transcriptional activity by competitive ligand
or DNA binding and/or heterodimerization with the full length
receptor. Essential for MTA1-mediated transcriptional regulation
of BRCA1 and BCAS3. Isoform 3 can bind to ERE and inhibit isoform
1. {ECO:0000269|PubMed:10681512, ECO:0000269|PubMed:10816575,
ECO:0000269|PubMed:11477071, ECO:0000269|PubMed:11682626,
ECO:0000269|PubMed:14764652, ECO:0000269|PubMed:15078875,
ECO:0000269|PubMed:15891768, ECO:0000269|PubMed:16043358,
ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:16684779,
ECO:0000269|PubMed:17922032, ECO:0000269|PubMed:17932106,
ECO:0000269|PubMed:18247370, ECO:0000269|PubMed:19350539,
ECO:0000269|PubMed:20074560, ECO:0000269|PubMed:20705611,
ECO:0000269|PubMed:21330404, ECO:0000269|PubMed:22083956,
ECO:0000269|PubMed:7651415, ECO:0000269|PubMed:9328340}.
-!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with
ESR2. Isoform 3 can probably homodimerize or heterodimerize with
isoform 1 and ESR2. Interacts with FOXC2, MAP1S, SLC30A9, UBE1C
and NCOA3 coactivator (By similarity). Interacts with EP300; the
interaction is estrogen-dependent and enhanced by CITED1.
Interacts with CITED1; the interaction is estrogen-dependent.
Interacts with NCOA5 and NCOA6 coactivators. Interacts with NCOA7;
the interaction is a ligand-inducible. Interacts with PHB2, PELP1
and UBE1C. Interacts with AKAP13. Interacts with CUEDC2. Interacts
with KDM5A. Interacts with SMARD1. Interacts with HEXIM1.
Interacts with PBXIP1. Interaction with MUC1 is stimulated by 7
beta-estradiol (E2) and enhances ERS1-mediated transcription.
Interacts with DNTTIP2, FAM120B and UIMC1. Interacts with isoform
4 of TXNRD1. Interacts with KMT2D/MLL2. Interacts with ATAD2 and
this interaction is enhanced by estradiol. Interacts with KIF18A
and LDB1. Interacts with RLIM (via C-terminus). Interacts with
MACROD1. Interacts with SH2D4A and PLCG. Interaction with SH2D4A
blocks binding to PLCG and inhibits estrogen-induced cell
proliferation. Interacts with DYNLL1. Interacts with CCDC62 in the
presence of estradiol/E2; this interaction seems to enhance the
transcription of target genes. Interacts with NR2C1; the
interaction prevents homodimerization of ESR1 and suppresses its
transcriptional activity and cell growth. Interacts with DNAAF4.
Interacts with PRMT2. Interacts with PI3KR1 or PI3KR2, SRC and
PTK2/FAK1. Interacts with RBFOX2. Interacts with STK3/MST2 only in
the presence of SAV1 and vice-versa. Binds to CSNK1D. Interacts
with NCOA2; NCOA2 can interact with ESR1 AF-1 and AF-2 domains
simultaneously and mediate their transcriptional synergy.
Interacts with DDX5. Interacts with NCOA1; the interaction seems
to require a self-association of N-terminal and C-terminal
regions. Interacts with ZNF366, DDX17, NFKB1, RELA, SP1 and SP3.
Interacts with NRIP1 (By similarity). Interacts with GPER1; the
interaction occurs in an estrogen-dependent manner. Interacts with
CLOCK and the interaction is stimulated by estrogen. Interacts
with BCAS3. Interacts with TRIP4 (ufmylated); estrogen dependent.
Interacts with LMTK3; the interaction phosphorylates ESR1 (in
vitro) and protects it against proteasomal degradation. Interacts
with CCAR2 (via N-terminus) in a ligand-independent manner.
Interacts with ZFHX3. Interacts with SFR1 in a ligand-dependent
and -independent manner (PubMed:23874500). Interacts with DCAF13,
LATS1 and DCAF1; regulates ESR1 ubiquitination and ubiquitin-
mediated proteasomal degradation (PubMed:28068668). Interacts (via
DNA-binding domain) with POU4F2 (C-terminus); this interaction
increases the estrogen receptor ESR1 transcriptional activity in a
DNA- and ligand 17-beta-estradiol-independent manner (By
similarity). Interacts with ESRRB isoform 1 (PubMed:19755138).
{ECO:0000250, ECO:0000250|UniProtKB:P19785,
ECO:0000269|PubMed:10359819, ECO:0000269|PubMed:10409727,
ECO:0000269|PubMed:10567404, ECO:0000269|PubMed:10681512,
ECO:0000269|PubMed:10816575, ECO:0000269|PubMed:10970861,
ECO:0000269|PubMed:11113208, ECO:0000269|PubMed:11265755,
ECO:0000269|PubMed:11358960, ECO:0000269|PubMed:11477071,
ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:11682626,
ECO:0000269|PubMed:11875103, ECO:0000269|PubMed:11971969,
ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:12093804,
ECO:0000269|PubMed:12415108, ECO:0000269|PubMed:12554772,
ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:15047147,
ECO:0000269|PubMed:15199063, ECO:0000269|PubMed:15891768,
ECO:0000269|PubMed:15940264, ECO:0000269|PubMed:16427018,
ECO:0000269|PubMed:16603732, ECO:0000269|PubMed:17006958,
ECO:0000269|PubMed:17043237, ECO:0000269|PubMed:17085477,
ECO:0000269|PubMed:17311814, ECO:0000269|PubMed:17347654,
ECO:0000269|PubMed:17505058, ECO:0000269|PubMed:17587566,
ECO:0000269|PubMed:17658481, ECO:0000269|PubMed:17914104,
ECO:0000269|PubMed:17932106, ECO:0000269|PubMed:17998543,
ECO:0000269|PubMed:18563714, ECO:0000269|PubMed:18657504,
ECO:0000269|PubMed:19117995, ECO:0000269|PubMed:19339517,
ECO:0000269|PubMed:19350539, ECO:0000269|PubMed:19383985,
ECO:0000269|PubMed:19423554, ECO:0000269|PubMed:19636373,
ECO:0000269|PubMed:19712589, ECO:0000269|PubMed:19718048,
ECO:0000269|PubMed:19749156, ECO:0000269|PubMed:19755138,
ECO:0000269|PubMed:20074560, ECO:0000269|PubMed:20720010,
ECO:0000269|PubMed:21104395, ECO:0000269|PubMed:21602804,
ECO:0000269|PubMed:23160374, ECO:0000269|PubMed:23874500,
ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:28068668,
ECO:0000269|PubMed:9328340, ECO:0000269|PubMed:9627117}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-78473, EBI-78473;
Q12802:AKAP13; NbExp=3; IntAct=EBI-78473, EBI-1373806;
Q03989:ARID5A; NbExp=9; IntAct=EBI-78473, EBI-948603;
Q9Y294:ASF1A; NbExp=2; IntAct=EBI-78473, EBI-749553;
Q8IXJ9:ASXL1; NbExp=2; IntAct=EBI-78473, EBI-1646500;
P59598:Asxl1 (xeno); NbExp=2; IntAct=EBI-78473, EBI-5743705;
P62952:BLCAP; NbExp=2; IntAct=EBI-78473, EBI-3895726;
P38398:BRCA1; NbExp=12; IntAct=EBI-78473, EBI-349905;
P20290-2:BTF3; NbExp=5; IntAct=EBI-78473, EBI-1054703;
Q86Y37:CACUL1; NbExp=5; IntAct=EBI-78473, EBI-8168227;
Q99966:CITED1; NbExp=3; IntAct=EBI-78473, EBI-2624951;
Q9H467:CUEDC2; NbExp=2; IntAct=EBI-78473, EBI-1248228;
Q92841:DDX17; NbExp=8; IntAct=EBI-78473, EBI-746012;
P17844:DDX5; NbExp=9; IntAct=EBI-78473, EBI-351962;
O00429:DNM1L; NbExp=2; IntAct=EBI-78473, EBI-724571;
P00533:EGFR; NbExp=4; IntAct=EBI-4309277, EBI-297353;
Q09472:EP300; NbExp=2; IntAct=EBI-78473, EBI-447295;
Q12778:FOXO1; NbExp=2; IntAct=EBI-78473, EBI-1108782;
Q9Y3R0:GRIP1; NbExp=2; IntAct=EBI-78473, EBI-5349621;
O00165:HAX1; NbExp=2; IntAct=EBI-78473, EBI-357001;
P05627:Jun (xeno); NbExp=6; IntAct=EBI-78473, EBI-764369;
O15054:KDM6B; NbExp=2; IntAct=EBI-78473, EBI-2831260;
O14686:KMT2D; NbExp=3; IntAct=EBI-78473, EBI-996065;
Q9BQ69:MACROD1; NbExp=4; IntAct=EBI-78473, EBI-5324932;
Q00987:MDM2; NbExp=2; IntAct=EBI-78473, EBI-389668;
Q13330:MTA1; NbExp=4; IntAct=EBI-78473, EBI-714236;
O94776:MTA2; NbExp=3; IntAct=EBI-78473, EBI-1783035;
Q9BTC8:MTA3; NbExp=3; IntAct=EBI-78473, EBI-2461787;
P60660:MYL6; NbExp=3; IntAct=EBI-78473, EBI-300817;
Q15788:NCOA1; NbExp=10; IntAct=EBI-78473, EBI-455189;
Q15596:NCOA2; NbExp=8; IntAct=EBI-78473, EBI-81236;
Q9Y6Q9:NCOA3; NbExp=4; IntAct=EBI-78473, EBI-81196;
Q9JLI4:Ncoa6 (xeno); NbExp=2; IntAct=EBI-78473, EBI-286271;
Q9UN36:NDRG2; NbExp=2; IntAct=EBI-78473, EBI-3895741;
P19838:NFKB1; NbExp=3; IntAct=EBI-78473, EBI-697771;
Q96RI1-3:NR1H4; NbExp=2; IntAct=EBI-78473, EBI-10921781;
Q9BTK6:PAGR1; NbExp=5; IntAct=EBI-78473, EBI-2372223;
Q96AQ6:PBXIP1; NbExp=9; IntAct=EBI-78473, EBI-740845;
P62962:Pfn1 (xeno); NbExp=3; IntAct=EBI-78473, EBI-647096;
P06401:PGR; NbExp=20; IntAct=EBI-78473, EBI-78539;
P06401-1:PGR; NbExp=4; IntAct=EBI-78473, EBI-12590474;
Q99623:PHB2; NbExp=4; IntAct=EBI-78473, EBI-358348;
P27986:PIK3R1; NbExp=6; IntAct=EBI-78473, EBI-79464;
P53041:PPP5C; NbExp=4; IntAct=EBI-78473, EBI-716663;
P55345:PRMT2; NbExp=9; IntAct=EBI-78473, EBI-78458;
P60763:RAC3; NbExp=5; IntAct=EBI-78473, EBI-767084;
O43251:RBFOX2; NbExp=4; IntAct=EBI-78473, EBI-746056;
Q04206:RELA; NbExp=7; IntAct=EBI-78473, EBI-73886;
Q14151:SAFB2; NbExp=2; IntAct=EBI-78473, EBI-352869;
Q96HI0:SENP5; NbExp=2; IntAct=EBI-78473, EBI-3895753;
P29353:SHC1; NbExp=2; IntAct=EBI-4309277, EBI-78835;
P51532:SMARCA4; NbExp=3; IntAct=EBI-78473, EBI-302489;
P08047:SP1; NbExp=2; IntAct=EBI-78473, EBI-298336;
Q02447:SP3; NbExp=2; IntAct=EBI-78473, EBI-348158;
P12931:SRC; NbExp=9; IntAct=EBI-78473, EBI-621482;
Q16881-4:TXNRD1; NbExp=4; IntAct=EBI-78473, EBI-9080335;
Q8N895:ZNF366; NbExp=6; IntAct=EBI-78473, EBI-2813661;
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00407, ECO:0000269|PubMed:12682286,
ECO:0000269|PubMed:20074560}. Cytoplasm
{ECO:0000269|PubMed:12682286}. Cell membrane
{ECO:0000269|PubMed:12682286}; Peripheral membrane protein
{ECO:0000269|PubMed:12682286}; Cytoplasmic side
{ECO:0000269|PubMed:12682286}. Note=A minor fraction is associated
with the inner membrane.
-!- SUBCELLULAR LOCATION: Isoform 3: Nucleus. Cytoplasm. Cell
membrane; Peripheral membrane protein; Cytoplasmic side. Cell
membrane; Single-pass type I membrane protein. Note=Associated
with the inner membrane via palmitoylation (Probable). At least a
subset exists as a transmembrane protein with a N-terminal
extracellular domain. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleus. Golgi apparatus. Cell membrane.
Note=Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus
where most probably palmitoylation occurs. Associated with the
plasma membrane when palmitoylated.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Long, hER-alpha66, ER66;
IsoId=P03372-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P03372-2; Sequence=VSP_003680;
Note=No experimental confirmation available.;
Name=3; Synonyms=hER-alpha46, ER46;
IsoId=P03372-3; Sequence=VSP_042460;
Note=Produced by alternative promoter usage.;
Name=4; Synonyms=hER-alpha36, ER36;
IsoId=P03372-4; Sequence=VSP_042460, VSP_042461;
Note=Produced by alternative splicing of isoform 3.;
-!- TISSUE SPECIFICITY: Widely expressed. Isoform 3 is not expressed
in the pituitary gland. {ECO:0000269|PubMed:10970861}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain. The
modulating domain, also known as A/B or AF-1 domain has a ligand-
independent transactivation function. The C-terminus contains a
ligand-dependent transactivation domain, also known as E/F or AF-2
domain which overlaps with the ligand binding domain. AF-1 and AF-
2 activate transcription independently and synergistically and act
in a promoter- and cell-specific manner. AF-1 seems to provide the
major transactivation function in differentiated cells.
-!- PTM: Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation
probably enhances transcriptional activity. Self-association
induces phosphorylation. Dephosphorylation at Ser-118 by PPP5C
inhibits its transactivation activity. Phosphorylated by LMTK3 in
vitro. {ECO:0000269|PubMed:10428798, ECO:0000269|PubMed:14764652,
ECO:0000269|PubMed:19339517, ECO:0000269|PubMed:21602804,
ECO:0000269|PubMed:7476978, ECO:0000269|PubMed:7539106,
ECO:0000269|PubMed:7838153}.
-!- PTM: Glycosylated; contains N-acetylglucosamine, probably O-
linked. {ECO:0000269|PubMed:8999954}.
-!- PTM: Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1
proteasomal degradation (PubMed:21602804, PubMed:28068668).
Deubiquitinated by OTUB1 (PubMed:19383985).
{ECO:0000269|PubMed:19383985, ECO:0000269|PubMed:21602804,
ECO:0000269|PubMed:28068668}.
-!- PTM: Dimethylated by PRMT1 at Arg-260. The methylation may favor
cytoplasmic localization. {ECO:0000269|PubMed:18657504}.
-!- PTM: Palmitoylated (isoform 3). Not biotinylated (isoform 3).
{ECO:0000269|PubMed:22031296}.
-!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is
required for plasma membrane targeting and for rapid intracellular
signaling via ERK and AKT kinases and cAMP generation, but not for
signaling mediated by the nuclear hormone receptor.
{ECO:0000269|PubMed:22031296}.
-!- POLYMORPHISM: Genetic variations in ESR1 are correlated with bone
mineral density (BMD). Low BMD is a risk factor for osteoporotic
fracture. Osteoporosis is characterized by reduced bone mineral
density, disruption of bone microarchitecture, and the alteration
of the amount and variety of non-collagenous proteins in bone.
Osteoporotic bones are more at risk of fracture.
{ECO:0000269|PubMed:10942433}.
-!- DISEASE: Estrogen resistance (ESTRR) [MIM:615363]: A disorder
characterized by partial or complete resistance to estrogens, in
the presence of elevated estrogen serum levels. Clinical features
include absence of the pubertal growth spurt, delayed bone
maturation, unfused epiphyses, reduced bone mineral density,
osteoporosis, continued growth into adulthood and very tall adult
stature. Glucose intolerance, hyperinsulinemia and lipid
abnormalities may also be present. {ECO:0000269|PubMed:23841731,
ECO:0000269|PubMed:27754803}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Selective estrogen receptor modulators (SERMs),
such as tamoxifen, raloxifene, toremifene, lasofoxifene,
clomifene, femarelle and ormeloxifene, have tissue selective
agonistic and antagonistic effects on the estrogen receptor (ER).
They interfere with the ER association with coactivators or
corepressors, mainly involving the AF-2 domain.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB00115.1; Type=Miscellaneous discrepancy; Note=contains an in-frame duplication of exons 6 and 7.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/esr1/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Estrogen receptor entry;
URL="https://en.wikipedia.org/wiki/Estrogen_receptor";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X03635; CAA27284.1; -; mRNA.
EMBL; M12674; AAA52399.1; -; mRNA.
EMBL; U47678; AAB00115.1; ALT_SEQ; mRNA.
EMBL; AY425004; AAQ91815.1; -; Genomic_DNA.
EMBL; BX640939; CAE45969.1; -; mRNA.
EMBL; AL049821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL078582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL356311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL590993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW47740.1; -; Genomic_DNA.
EMBL; BC128573; AAI28574.1; -; mRNA.
EMBL; BC128574; AAI28575.1; -; mRNA.
EMBL; AH008151; AAD52984.1; -; Genomic_DNA.
EMBL; X73067; CAA51528.1; -; mRNA.
EMBL; Z75126; CAA99436.1; -; mRNA.
CCDS; CCDS5234.1; -. [P03372-1]
PIR; S64737; S64737.
RefSeq; NP_000116.2; NM_000125.3. [P03372-1]
RefSeq; NP_001116212.1; NM_001122740.1. [P03372-1]
RefSeq; NP_001116213.1; NM_001122741.1. [P03372-1]
RefSeq; NP_001116214.1; NM_001122742.1. [P03372-1]
RefSeq; NP_001278159.1; NM_001291230.1.
RefSeq; NP_001278170.1; NM_001291241.1.
RefSeq; NP_001315029.1; NM_001328100.1.
RefSeq; XP_006715438.1; XM_006715375.3. [P03372-3]
RefSeq; XP_011533845.1; XM_011535543.2. [P03372-1]
RefSeq; XP_011533846.1; XM_011535544.2. [P03372-1]
RefSeq; XP_011533847.1; XM_011535545.2. [P03372-1]
RefSeq; XP_016865865.1; XM_017010376.1. [P03372-1]
RefSeq; XP_016865866.1; XM_017010377.1. [P03372-1]
RefSeq; XP_016865867.1; XM_017010378.1. [P03372-1]
RefSeq; XP_016865868.1; XM_017010379.1. [P03372-1]
RefSeq; XP_016865869.1; XM_017010380.1. [P03372-1]
RefSeq; XP_016865870.1; XM_017010381.1. [P03372-1]
UniGene; Hs.208124; -.
UniGene; Hs.744830; -.
PDB; 1A52; X-ray; 2.80 A; A/B=297-554.
PDB; 1AKF; Model; -; A=309-547.
PDB; 1ERE; X-ray; 3.10 A; A/B/C/D/E/F=301-553.
PDB; 1ERR; X-ray; 2.60 A; A/B=301-553.
PDB; 1G50; X-ray; 2.90 A; A/B/C=304-550.
PDB; 1GWQ; X-ray; 2.45 A; A/B=301-548.
PDB; 1GWR; X-ray; 2.40 A; A/B=305-549.
PDB; 1HCP; NMR; -; A=180-254.
PDB; 1HCQ; X-ray; 2.40 A; A/B/E/F=180-262.
PDB; 1L2I; X-ray; 1.95 A; A/B=297-554.
PDB; 1PCG; X-ray; 2.70 A; A/B=304-547.
PDB; 1QKT; X-ray; 2.20 A; A=304-551.
PDB; 1QKU; X-ray; 3.20 A; A/B/C=301-550.
PDB; 1R5K; X-ray; 2.70 A; A/B/C=297-554.
PDB; 1SJ0; X-ray; 1.90 A; A=307-554.
PDB; 1UOM; X-ray; 2.28 A; A=301-553.
PDB; 1X7E; X-ray; 2.80 A; A/B=305-549.
PDB; 1X7R; X-ray; 2.00 A; A=305-549.
PDB; 1XP1; X-ray; 1.80 A; A=307-554.
PDB; 1XP6; X-ray; 1.70 A; A=307-554.
PDB; 1XP9; X-ray; 1.80 A; A=307-554.
PDB; 1XPC; X-ray; 1.60 A; A=307-554.
PDB; 1XQC; X-ray; 2.05 A; A/B/C/D=301-553.
PDB; 1YIM; X-ray; 1.90 A; A=307-554.
PDB; 1YIN; X-ray; 2.20 A; A=307-554.
PDB; 1ZKY; X-ray; 2.25 A; A/B=298-554.
PDB; 2AYR; X-ray; 1.90 A; A=304-551.
PDB; 2B1V; X-ray; 1.80 A; A/B=298-554.
PDB; 2B1Z; X-ray; 1.78 A; A/B=298-554.
PDB; 2B23; X-ray; 2.10 A; A/B=298-554.
PDB; 2BJ4; X-ray; 2.00 A; A/B=305-533.
PDB; 2FAI; X-ray; 2.10 A; A/B=298-554.
PDB; 2G44; X-ray; 2.65 A; A/B=298-554.
PDB; 2G5O; X-ray; 2.30 A; A/B=298-554.
PDB; 2I0J; X-ray; 2.90 A; A/B/C/D=304-547.
PDB; 2IOG; X-ray; 1.60 A; A=309-554.
PDB; 2IOK; X-ray; 2.40 A; A/B=301-554.
PDB; 2JF9; X-ray; 2.10 A; A/B/C=304-533.
PDB; 2JFA; X-ray; 2.55 A; A/B=304-533.
PDB; 2LLO; NMR; -; B=287-305.
PDB; 2LLQ; NMR; -; B=287-305.
PDB; 2OCF; X-ray; 2.95 A; A=298-595.
PDB; 2OUZ; X-ray; 2.00 A; A=301-553.
PDB; 2P15; X-ray; 1.94 A; A/B=298-554.
PDB; 2POG; X-ray; 1.84 A; A/B=304-551.
PDB; 2Q6J; X-ray; 2.70 A; A/B=298-554.
PDB; 2Q70; X-ray; 1.95 A; A/B=304-551.
PDB; 2QA6; X-ray; 2.60 A; A/B=298-554.
PDB; 2QA8; X-ray; 1.85 A; A/B=298-554.
PDB; 2QAB; X-ray; 1.89 A; A/B=298-554.
PDB; 2QE4; X-ray; 2.40 A; A/B=304-551.
PDB; 2QGT; X-ray; 2.15 A; A/B=298-554.
PDB; 2QGW; X-ray; 2.39 A; A/B=298-554.
PDB; 2QH6; X-ray; 2.70 A; A/B=298-554.
PDB; 2QR9; X-ray; 2.00 A; A/B=298-554.
PDB; 2QSE; X-ray; 1.85 A; A/B=298-554.
PDB; 2QXM; X-ray; 2.30 A; A/B=298-554.
PDB; 2QXS; X-ray; 1.70 A; A/B=298-554.
PDB; 2QZO; X-ray; 1.72 A; A/B=298-554.
PDB; 2R6W; X-ray; 2.00 A; A/B=304-551.
PDB; 2R6Y; X-ray; 2.00 A; A/B=304-551.
PDB; 2YAT; X-ray; 2.60 A; A=301-551.
PDB; 2YJA; X-ray; 1.82 A; B=299-551.
PDB; 3CBM; X-ray; 1.69 A; B=298-307.
PDB; 3CBO; X-ray; 1.65 A; B=298-307.
PDB; 3CBP; X-ray; 1.42 A; B=298-307.
PDB; 3DT3; X-ray; 2.40 A; A/B=299-551.
PDB; 3ERD; X-ray; 2.03 A; A/B=297-554.
PDB; 3ERT; X-ray; 1.90 A; A=297-554.
PDB; 3HLV; X-ray; 3.00 A; A/B=298-550.
PDB; 3HM1; X-ray; 2.33 A; A/B=298-550.
PDB; 3L03; X-ray; 1.90 A; A/B=298-550.
PDB; 3OS8; X-ray; 2.03 A; A/B/C/D=299-553.
PDB; 3OS9; X-ray; 2.30 A; A/B/C/D=299-553.
PDB; 3OSA; X-ray; 2.30 A; A/B/C/D=299-553.
PDB; 3Q95; X-ray; 2.05 A; A/B=298-554.
PDB; 3Q97; X-ray; 2.10 A; A/B=298-554.
PDB; 3UU7; X-ray; 2.20 A; A/B=302-552.
PDB; 3UUA; X-ray; 2.05 A; A/B=302-552.
PDB; 3UUC; X-ray; 2.10 A; A/B/C/D=302-552.
PDB; 3UUD; X-ray; 1.60 A; A/B=302-552.
PDB; 4AA6; X-ray; 2.60 A; A/B/E/F=182-252.
PDB; 4DMA; X-ray; 2.30 A; A/B=303-549.
PDB; 4IU7; X-ray; 2.29 A; A/B=303-549.
PDB; 4IUI; X-ray; 2.30 A; A/B=303-549.
PDB; 4IV2; X-ray; 2.14 A; A/B=303-549.
PDB; 4IV4; X-ray; 2.30 A; A/B=303-549.
PDB; 4IVW; X-ray; 2.06 A; A/B=303-549.
PDB; 4IVY; X-ray; 1.95 A; A/B=303-549.
PDB; 4IW6; X-ray; 1.98 A; A/B=303-549.
PDB; 4IW8; X-ray; 2.04 A; A/B=303-549.
PDB; 4IWC; X-ray; 2.24 A; A/B=303-549.
PDB; 4IWF; X-ray; 1.93 A; A/B=303-549.
PDB; 4JC3; X-ray; 2.05 A; B=585-595.
PDB; 4JDD; X-ray; 2.10 A; B=585-595.
PDB; 4MG5; X-ray; 2.05 A; A/B=302-552.
PDB; 4MG6; X-ray; 2.10 A; A/B=302-552.
PDB; 4MG7; X-ray; 2.15 A; A/B=302-552.
PDB; 4MG8; X-ray; 1.85 A; A/B=302-552.
PDB; 4MG9; X-ray; 2.00 A; A/B=302-552.
PDB; 4MGA; X-ray; 1.80 A; A/B=302-552.
PDB; 4MGB; X-ray; 1.85 A; A/B=302-552.
PDB; 4MGC; X-ray; 2.15 A; A/B=302-552.
PDB; 4MGD; X-ray; 1.90 A; A/B=302-552.
PDB; 4O6F; X-ray; 2.82 A; B=261-271.
PDB; 4PP6; X-ray; 2.20 A; A/B=305-548.
PDB; 4PPP; X-ray; 2.69 A; A/B=305-548.
PDB; 4PPS; X-ray; 1.93 A; A/B=305-548.
PDB; 4PXM; X-ray; 1.90 A; A/B=299-554.
PDB; 4Q13; X-ray; 2.24 A; A/B=299-554.
PDB; 4Q50; X-ray; 3.07 A; A/B/C/D/E/F/G/H=299-554.
PDB; 4TUZ; X-ray; 1.90 A; A/B=302-552.
PDB; 4TV1; X-ray; 1.85 A; A/B=302-552.
PDB; 4XI3; X-ray; 2.49 A; A/B/C/D=306-548.
PDB; 4ZN7; X-ray; 1.93 A; A/B=301-559.
PDB; 4ZN9; X-ray; 2.21 A; A/B=301-559.
PDB; 4ZNH; X-ray; 1.93 A; A/B=301-559.
PDB; 4ZNS; X-ray; 1.86 A; A/B=301-559.
PDB; 4ZNT; X-ray; 1.90 A; A/B=301-559.
PDB; 4ZNU; X-ray; 2.40 A; A/B=301-559.
PDB; 4ZNV; X-ray; 1.77 A; A/B=301-559.
PDB; 4ZNW; X-ray; 2.31 A; A/B=301-559.
PDB; 5AAU; X-ray; 1.90 A; A/B=307-554.
PDB; 5AAV; X-ray; 1.95 A; A=307-554, B=306-554.
PDB; 5ACC; X-ray; 1.88 A; A=307-554.
PDB; 5AK2; X-ray; 2.19 A; A/B=307-554.
PDB; 5DI7; X-ray; 2.24 A; A/B=298-554.
PDB; 5DID; X-ray; 2.24 A; A/B=298-554.
PDB; 5DIE; X-ray; 2.24 A; A/B=298-554.
PDB; 5DIG; X-ray; 2.24 A; A/B=298-554.
PDB; 5DK9; X-ray; 2.28 A; A/B=298-554.
PDB; 5DKB; X-ray; 2.40 A; A/B=298-554.
PDB; 5DKE; X-ray; 2.60 A; A/B=298-554.
PDB; 5DKG; X-ray; 2.15 A; A/B=298-554.
PDB; 5DKS; X-ray; 2.60 A; A/B=298-554.
PDB; 5DL4; X-ray; 2.10 A; A/B=298-554.
PDB; 5DLR; X-ray; 2.26 A; A/B=298-554.
PDB; 5DMC; X-ray; 2.40 A; A/B=298-554.
PDB; 5DMF; X-ray; 2.40 A; A/B=298-554.
PDB; 5DP0; X-ray; 2.38 A; A/B=298-554.
PDB; 5DRJ; X-ray; 2.07 A; A/B=298-554.
PDB; 5DRM; X-ray; 2.24 A; A/B=298-554.
PDB; 5DTV; X-ray; 2.29 A; A/B=298-554.
PDB; 5DU5; X-ray; 2.19 A; A/B=298-554.
PDB; 5DUE; X-ray; 2.09 A; A/B=298-554.
PDB; 5DUG; X-ray; 2.25 A; A/B=298-554.
PDB; 5DUH; X-ray; 2.24 A; A/B=298-554.
PDB; 5DVS; X-ray; 2.28 A; A/B=298-554.
PDB; 5DVV; X-ray; 2.50 A; A/B=298-554.
PDB; 5DWE; X-ray; 1.92 A; A/B=298-554.
PDB; 5DWG; X-ray; 2.30 A; A/B=298-554.
PDB; 5DWI; X-ray; 2.43 A; A/B=298-554.
PDB; 5DWJ; X-ray; 2.00 A; A/B=298-554.
PDB; 5DX3; X-ray; 2.09 A; A/B=297-554.
PDB; 5DXB; X-ray; 2.08 A; A/B=297-554.
PDB; 5DXE; X-ray; 1.50 A; A/B=297-554.
PDB; 5DXG; X-ray; 1.86 A; A/B=297-554.
PDB; 5DXK; X-ray; 2.23 A; A/B=298-554.
PDB; 5DXM; X-ray; 2.37 A; A/B=298-554.
PDB; 5DXP; X-ray; 2.20 A; A/B=298-554.
PDB; 5DXQ; X-ray; 2.40 A; A/B=298-554.
PDB; 5DXR; X-ray; 2.28 A; A/B=298-554.
PDB; 5DY8; X-ray; 2.03 A; A/B=298-554.
PDB; 5DYB; X-ray; 2.27 A; A/B=298-554.
PDB; 5DYD; X-ray; 2.48 A; A/B=298-554.
PDB; 5DZ0; X-ray; 2.24 A; A/B=298-554.
PDB; 5DZ1; X-ray; 2.20 A; A/B=298-554.
PDB; 5DZ3; X-ray; 2.15 A; A/B=298-554.
PDB; 5DZH; X-ray; 2.11 A; A/B=298-554.
PDB; 5DZI; X-ray; 1.90 A; A/B=298-554.
PDB; 5E0W; X-ray; 2.00 A; A/B=298-554.
PDB; 5E0X; X-ray; 2.01 A; A/B=298-554.
PDB; 5E14; X-ray; 2.22 A; A/B=298-554.
PDB; 5E15; X-ray; 2.10 A; A/B=298-554.
PDB; 5E19; X-ray; 2.24 A; A/B=298-554.
PDB; 5E1C; X-ray; 1.98 A; A/B=298-554.
PDB; 5EGV; X-ray; 2.86 A; A/B=298-554.
PDB; 5EHJ; X-ray; 2.50 A; A/B=298-554.
PDB; 5EI1; X-ray; 2.40 A; A/B=298-554.
PDB; 5EIT; X-ray; 2.68 A; A/B=298-554.
PDB; 5FQP; X-ray; 1.88 A; A=307-554.
PDB; 5FQR; X-ray; 1.88 A; A=307-554.
PDB; 5FQS; X-ray; 1.94 A; A=307-554.
PDB; 5FQT; X-ray; 1.99 A; A=307-554.
PDB; 5FQV; X-ray; 1.74 A; A=307-554.
PDB; 5HYR; X-ray; 2.27 A; A/B=302-559.
PDB; 5JMM; X-ray; 2.10 A; A/B=302-552.
PDB; 5KCC; X-ray; 2.39 A; A/B=298-554, A/B=304-549.
PDB; 5KCD; X-ray; 1.82 A; A/B=298-554, A/B=305-549.
PDB; 5KCE; X-ray; 1.85 A; A/B=298-554, A/B=303-549.
PDB; 5KCF; X-ray; 2.07 A; A/B=298-554, A/B=303-549.
PDB; 5KCT; X-ray; 1.60 A; A/B=298-554, A/B=303-548.
PDB; 5KCU; X-ray; 2.03 A; A/B=298-554, A/B=303-548.
PDB; 5KCW; X-ray; 1.91 A; A/B=303-549, A/B=298-554.
PDB; 5KD9; X-ray; 1.78 A; A/B=298-554, A/B=303-549.
PDB; 5KR9; X-ray; 2.25 A; A/B=298-554.
PDB; 5KRA; X-ray; 2.40 A; A/B/E/F=298-554.
PDB; 5KRC; X-ray; 2.40 A; A/B=298-554.
PDB; 5KRF; X-ray; 2.19 A; A/B=298-554.
PDB; 5KRH; X-ray; 2.24 A; A/B=298-554.
PDB; 5KRI; X-ray; 2.25 A; A/B=298-554.
PDB; 5KRJ; X-ray; 2.70 A; A/B=298-554.
PDB; 5KRK; X-ray; 2.39 A; A/B=298-554.
PDB; 5KRL; X-ray; 2.40 A; A/B=298-554.
PDB; 5KRM; X-ray; 2.24 A; A/B=298-554.
PDB; 5KRO; X-ray; 2.10 A; A/B=298-554.
PDB; 5N10; X-ray; 1.60 A; C/D/F=584-595.
PDB; 5T0X; NMR; -; B/C=287-305.
PDB; 5T92; X-ray; 2.22 A; A/B=301-553.
PDB; 5T97; X-ray; 3.00 A; A/B=301-553.
PDB; 5TLD; X-ray; 2.38 A; A/B=298-554.
PDB; 5TLF; X-ray; 2.20 A; A/B=298-554.
PDB; 5TLG; X-ray; 2.23 A; A/B=298-554.
PDB; 5TLL; X-ray; 2.42 A; A/B=298-554.
PDB; 5TLM; X-ray; 2.50 A; A/B=298-554.
PDB; 5TLO; X-ray; 2.28 A; A/B=298-554.
PDB; 5TLP; X-ray; 2.08 A; A/B=298-554.
PDB; 5TLT; X-ray; 1.90 A; A/B=298-554.
PDB; 5TLU; X-ray; 2.22 A; A/B=298-554.
PDB; 5TLV; X-ray; 2.32 A; A/B=298-554.
PDB; 5TLX; X-ray; 2.10 A; A/B=298-554.
PDB; 5TLY; X-ray; 2.14 A; A/B=298-554.
PDB; 5TM1; X-ray; 2.23 A; A/B=298-554.
PDB; 5TM2; X-ray; 2.60 A; A/B=298-554.
PDB; 5TM3; X-ray; 2.19 A; A/B=298-554.
PDB; 5TM4; X-ray; 2.25 A; A/B=298-554.
PDB; 5TM5; X-ray; 2.24 A; A/B=298-554.
PDB; 5TM6; X-ray; 2.54 A; A/B=298-554.
PDB; 5TM7; X-ray; 2.40 A; A/B=298-554.
PDB; 5TM8; X-ray; 1.99 A; A/B=298-554.
PDB; 5TM9; X-ray; 2.50 A; A/B=298-554.
PDB; 5TML; X-ray; 2.25 A; A/B=298-554.
PDB; 5TMM; X-ray; 2.20 A; A/B=298-554.
PDB; 5TMO; X-ray; 2.17 A; A/B=298-554.
PDB; 5TMQ; X-ray; 2.24 A; A/B=298-554.
PDB; 5TMR; X-ray; 2.30 A; A/B=298-554.
PDB; 5TMS; X-ray; 2.24 A; A/B=298-554.
PDB; 5TMT; X-ray; 2.05 A; A/B=298-554.
PDB; 5TMU; X-ray; 2.43 A; A/B=298-554.
PDB; 5TMV; X-ray; 2.38 A; A/B=298-554.
PDB; 5TMW; X-ray; 2.29 A; A/B=298-554.
PDB; 5TMZ; X-ray; 2.21 A; A/B=298-554.
PDB; 5TN1; X-ray; 2.06 A; A/B=298-554.
PDB; 5TN3; X-ray; 2.54 A; A/B=298-554.
PDB; 5TN4; X-ray; 1.86 A; A/B=298-554.
PDB; 5TN5; X-ray; 1.89 A; A/B=298-554.
PDB; 5TN6; X-ray; 2.09 A; A/B=298-554.
PDB; 5TN7; X-ray; 2.24 A; A/B=298-554.
PDB; 5TN8; X-ray; 2.65 A; A/B=298-554.
PDB; 5TN9; X-ray; 2.25 A; A/B/C/D=298-554.
PDB; 5TNB; X-ray; 2.08 A; A/B/C/D=298-554.
PDB; 5U2B; X-ray; 2.22 A; A/B/C/D/E/F=298-554.
PDB; 5U2D; X-ray; 1.86 A; A/B=298-554.
PDBsum; 1A52; -.
PDBsum; 1AKF; -.
PDBsum; 1ERE; -.
PDBsum; 1ERR; -.
PDBsum; 1G50; -.
PDBsum; 1GWQ; -.
PDBsum; 1GWR; -.
PDBsum; 1HCP; -.
PDBsum; 1HCQ; -.
PDBsum; 1L2I; -.
PDBsum; 1PCG; -.
PDBsum; 1QKT; -.
PDBsum; 1QKU; -.
PDBsum; 1R5K; -.
PDBsum; 1SJ0; -.
PDBsum; 1UOM; -.
PDBsum; 1X7E; -.
PDBsum; 1X7R; -.
PDBsum; 1XP1; -.
PDBsum; 1XP6; -.
PDBsum; 1XP9; -.
PDBsum; 1XPC; -.
PDBsum; 1XQC; -.
PDBsum; 1YIM; -.
PDBsum; 1YIN; -.
PDBsum; 1ZKY; -.
PDBsum; 2AYR; -.
PDBsum; 2B1V; -.
PDBsum; 2B1Z; -.
PDBsum; 2B23; -.
PDBsum; 2BJ4; -.
PDBsum; 2FAI; -.
PDBsum; 2G44; -.
PDBsum; 2G5O; -.
PDBsum; 2I0J; -.
PDBsum; 2IOG; -.
PDBsum; 2IOK; -.
PDBsum; 2JF9; -.
PDBsum; 2JFA; -.
PDBsum; 2LLO; -.
PDBsum; 2LLQ; -.
PDBsum; 2OCF; -.
PDBsum; 2OUZ; -.
PDBsum; 2P15; -.
PDBsum; 2POG; -.
PDBsum; 2Q6J; -.
PDBsum; 2Q70; -.
PDBsum; 2QA6; -.
PDBsum; 2QA8; -.
PDBsum; 2QAB; -.
PDBsum; 2QE4; -.
PDBsum; 2QGT; -.
PDBsum; 2QGW; -.
PDBsum; 2QH6; -.
PDBsum; 2QR9; -.
PDBsum; 2QSE; -.
PDBsum; 2QXM; -.
PDBsum; 2QXS; -.
PDBsum; 2QZO; -.
PDBsum; 2R6W; -.
PDBsum; 2R6Y; -.
PDBsum; 2YAT; -.
PDBsum; 2YJA; -.
PDBsum; 3CBM; -.
PDBsum; 3CBO; -.
PDBsum; 3CBP; -.
PDBsum; 3DT3; -.
PDBsum; 3ERD; -.
PDBsum; 3ERT; -.
PDBsum; 3HLV; -.
PDBsum; 3HM1; -.
PDBsum; 3L03; -.
PDBsum; 3OS8; -.
PDBsum; 3OS9; -.
PDBsum; 3OSA; -.
PDBsum; 3Q95; -.
PDBsum; 3Q97; -.
PDBsum; 3UU7; -.
PDBsum; 3UUA; -.
PDBsum; 3UUC; -.
PDBsum; 3UUD; -.
PDBsum; 4AA6; -.
PDBsum; 4DMA; -.
PDBsum; 4IU7; -.
PDBsum; 4IUI; -.
PDBsum; 4IV2; -.
PDBsum; 4IV4; -.
PDBsum; 4IVW; -.
PDBsum; 4IVY; -.
PDBsum; 4IW6; -.
PDBsum; 4IW8; -.
PDBsum; 4IWC; -.
PDBsum; 4IWF; -.
PDBsum; 4JC3; -.
PDBsum; 4JDD; -.
PDBsum; 4MG5; -.
PDBsum; 4MG6; -.
PDBsum; 4MG7; -.
PDBsum; 4MG8; -.
PDBsum; 4MG9; -.
PDBsum; 4MGA; -.
PDBsum; 4MGB; -.
PDBsum; 4MGC; -.
PDBsum; 4MGD; -.
PDBsum; 4O6F; -.
PDBsum; 4PP6; -.
PDBsum; 4PPP; -.
PDBsum; 4PPS; -.
PDBsum; 4PXM; -.
PDBsum; 4Q13; -.
PDBsum; 4Q50; -.
PDBsum; 4TUZ; -.
PDBsum; 4TV1; -.
PDBsum; 4XI3; -.
PDBsum; 4ZN7; -.
PDBsum; 4ZN9; -.
PDBsum; 4ZNH; -.
PDBsum; 4ZNS; -.
PDBsum; 4ZNT; -.
PDBsum; 4ZNU; -.
PDBsum; 4ZNV; -.
PDBsum; 4ZNW; -.
PDBsum; 5AAU; -.
PDBsum; 5AAV; -.
PDBsum; 5ACC; -.
PDBsum; 5AK2; -.
PDBsum; 5DI7; -.
PDBsum; 5DID; -.
PDBsum; 5DIE; -.
PDBsum; 5DIG; -.
PDBsum; 5DK9; -.
PDBsum; 5DKB; -.
PDBsum; 5DKE; -.
PDBsum; 5DKG; -.
PDBsum; 5DKS; -.
PDBsum; 5DL4; -.
PDBsum; 5DLR; -.
PDBsum; 5DMC; -.
PDBsum; 5DMF; -.
PDBsum; 5DP0; -.
PDBsum; 5DRJ; -.
PDBsum; 5DRM; -.
PDBsum; 5DTV; -.
PDBsum; 5DU5; -.
PDBsum; 5DUE; -.
PDBsum; 5DUG; -.
PDBsum; 5DUH; -.
PDBsum; 5DVS; -.
PDBsum; 5DVV; -.
PDBsum; 5DWE; -.
PDBsum; 5DWG; -.
PDBsum; 5DWI; -.
PDBsum; 5DWJ; -.
PDBsum; 5DX3; -.
PDBsum; 5DXB; -.
PDBsum; 5DXE; -.
PDBsum; 5DXG; -.
PDBsum; 5DXK; -.
PDBsum; 5DXM; -.
PDBsum; 5DXP; -.
PDBsum; 5DXQ; -.
PDBsum; 5DXR; -.
PDBsum; 5DY8; -.
PDBsum; 5DYB; -.
PDBsum; 5DYD; -.
PDBsum; 5DZ0; -.
PDBsum; 5DZ1; -.
PDBsum; 5DZ3; -.
PDBsum; 5DZH; -.
PDBsum; 5DZI; -.
PDBsum; 5E0W; -.
PDBsum; 5E0X; -.
PDBsum; 5E14; -.
PDBsum; 5E15; -.
PDBsum; 5E19; -.
PDBsum; 5E1C; -.
PDBsum; 5EGV; -.
PDBsum; 5EHJ; -.
PDBsum; 5EI1; -.
PDBsum; 5EIT; -.
PDBsum; 5FQP; -.
PDBsum; 5FQR; -.
PDBsum; 5FQS; -.
PDBsum; 5FQT; -.
PDBsum; 5FQV; -.
PDBsum; 5HYR; -.
PDBsum; 5JMM; -.
PDBsum; 5KCC; -.
PDBsum; 5KCD; -.
PDBsum; 5KCE; -.
PDBsum; 5KCF; -.
PDBsum; 5KCT; -.
PDBsum; 5KCU; -.
PDBsum; 5KCW; -.
PDBsum; 5KD9; -.
PDBsum; 5KR9; -.
PDBsum; 5KRA; -.
PDBsum; 5KRC; -.
PDBsum; 5KRF; -.
PDBsum; 5KRH; -.
PDBsum; 5KRI; -.
PDBsum; 5KRJ; -.
PDBsum; 5KRK; -.
PDBsum; 5KRL; -.
PDBsum; 5KRM; -.
PDBsum; 5KRO; -.
PDBsum; 5N10; -.
PDBsum; 5T0X; -.
PDBsum; 5T92; -.
PDBsum; 5T97; -.
PDBsum; 5TLD; -.
PDBsum; 5TLF; -.
PDBsum; 5TLG; -.
PDBsum; 5TLL; -.
PDBsum; 5TLM; -.
PDBsum; 5TLO; -.
PDBsum; 5TLP; -.
PDBsum; 5TLT; -.
PDBsum; 5TLU; -.
PDBsum; 5TLV; -.
PDBsum; 5TLX; -.
PDBsum; 5TLY; -.
PDBsum; 5TM1; -.
PDBsum; 5TM2; -.
PDBsum; 5TM3; -.
PDBsum; 5TM4; -.
PDBsum; 5TM5; -.
PDBsum; 5TM6; -.
PDBsum; 5TM7; -.
PDBsum; 5TM8; -.
PDBsum; 5TM9; -.
PDBsum; 5TML; -.
PDBsum; 5TMM; -.
PDBsum; 5TMO; -.
PDBsum; 5TMQ; -.
PDBsum; 5TMR; -.
PDBsum; 5TMS; -.
PDBsum; 5TMT; -.
PDBsum; 5TMU; -.
PDBsum; 5TMV; -.
PDBsum; 5TMW; -.
PDBsum; 5TMZ; -.
PDBsum; 5TN1; -.
PDBsum; 5TN3; -.
PDBsum; 5TN4; -.
PDBsum; 5TN5; -.
PDBsum; 5TN6; -.
PDBsum; 5TN7; -.
PDBsum; 5TN8; -.
PDBsum; 5TN9; -.
PDBsum; 5TNB; -.
PDBsum; 5U2B; -.
PDBsum; 5U2D; -.
DisProt; DP00074; -.
ProteinModelPortal; P03372; -.
SMR; P03372; -.
BioGrid; 108403; 706.
DIP; DIP-5965N; -.
ELM; P03372; -.
IntAct; P03372; 472.
MINT; MINT-129047; -.
STRING; 9606.ENSP00000206249; -.
BindingDB; P03372; -.
ChEMBL; CHEMBL206; -.
DrugBank; DB06871; 17-METHYL-17-ALPHA-DIHYDROEQUILENIN.
DrugBank; DB07708; 3-CHLORO-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL.
DrugBank; DB07712; 3-ETHYL-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL.
DrugBank; DB06927; [5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-YL]ACETONITRILE.
DrugBank; DB04468; Afimoxifene.
DrugBank; DB01431; Allylestrenol.
DrugBank; DB05233; AP1081.
DrugBank; DB05338; atamestane-plus-toremifene.
DrugBank; DB06401; Bazedoxifene.
DrugBank; DB05487; CC-8490.
DrugBank; DB05882; CHF 4227.
DrugBank; DB00269; Chlorotrianisene.
DrugBank; DB00882; Clomifene.
DrugBank; DB02715; Compound 18.
DrugBank; DB02615; Compound 19.
DrugBank; DB03742; Compound 4-D.
DrugBank; DB00286; Conjugated Equine Estrogens.
DrugBank; DB01406; Danazol.
DrugBank; DB00304; Desogestrel.
DrugBank; DB00890; Dienestrol.
DrugBank; DB00255; Diethylstilbestrol.
DrugBank; DB00783; Estradiol.
DrugBank; DB01196; Estramustine.
DrugBank; DB04573; Estriol.
DrugBank; DB00655; Estrone.
DrugBank; DB04574; Estrone sulfate.
DrugBank; DB00977; Ethinyl Estradiol.
DrugBank; DB00823; Ethynodiol diacetate.
DrugBank; DB00294; Etonogestrel.
DrugBank; DB01185; Fluoxymesterone.
DrugBank; DB00947; Fulvestrant.
DrugBank; DB01645; Genistein.
DrugBank; DB06202; Lasofoxifene.
DrugBank; DB00367; Levonorgestrel.
DrugBank; DB00603; Medroxyprogesterone acetate.
DrugBank; DB01065; Melatonin.
DrugBank; DB01357; Mestranol.
DrugBank; DB07991; N-[(1R)-3-(4-HYDROXYPHENYL)-1-METHYLPROPYL]-2-(2-PHENYL-1H-INDOL-3-YL)ACETAMIDE.
DrugBank; DB01183; Naloxone.
DrugBank; DB00957; Norgestimate.
DrugBank; DB05662; NP-50301.
DrugBank; DB04938; Ospemifene.
DrugBank; DB01708; Prasterone.
DrugBank; DB00396; Progesterone.
DrugBank; DB04575; Quinestrol.
DrugBank; DB00481; Raloxifene.
DrugBank; DB08773; RALOXIFENE CORE.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB09070; Tibolone.
DrugBank; DB00539; Toremifene.
DrugBank; DB01108; Trilostane.
GuidetoPHARMACOLOGY; 620; -.
SwissLipids; SLP:000001568; -.
iPTMnet; P03372; -.
PhosphoSitePlus; P03372; -.
SwissPalm; P03372; -.
UniCarbKB; P03372; -.
BioMuta; ESR1; -.
DMDM; 544257; -.
EPD; P03372; -.
PaxDb; P03372; -.
PeptideAtlas; P03372; -.
PRIDE; P03372; -.
DNASU; 2099; -.
Ensembl; ENST00000206249; ENSP00000206249; ENSG00000091831. [P03372-1]
Ensembl; ENST00000338799; ENSP00000342630; ENSG00000091831. [P03372-1]
Ensembl; ENST00000440973; ENSP00000405330; ENSG00000091831. [P03372-1]
Ensembl; ENST00000443427; ENSP00000387500; ENSG00000091831. [P03372-1]
GeneID; 2099; -.
KEGG; hsa:2099; -.
UCSC; uc003qom.5; human. [P03372-1]
CTD; 2099; -.
DisGeNET; 2099; -.
GeneCards; ESR1; -.
HGNC; HGNC:3467; ESR1.
HPA; CAB000037; -.
HPA; CAB055099; -.
HPA; CAB072858; -.
HPA; HPA000449; -.
HPA; HPA000450; -.
MalaCards; ESR1; -.
MIM; 133430; gene.
MIM; 615363; phenotype.
neXtProt; NX_P03372; -.
OpenTargets; ENSG00000091831; -.
Orphanet; 785; Estrogen resistance syndrome.
PharmGKB; PA156; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00760000118887; -.
HOVERGEN; HBG108344; -.
InParanoid; P03372; -.
KO; K08550; -.
OMA; EAGPPAF; -.
OrthoDB; EOG091G03V4; -.
PhylomeDB; P03372; -.
TreeFam; TF323751; -.
Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
SignaLink; P03372; -.
SIGNOR; P03372; -.
ChiTaRS; ESR1; human.
EvolutionaryTrace; P03372; -.
GeneWiki; Estrogen_receptor_alpha; -.
GenomeRNAi; 2099; -.
PRO; PR:P03372; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000091831; -.
CleanEx; HS_ESR1; -.
ExpressionAtlas; P03372; baseline and differential.
Genevisible; P03372; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0097550; C:transcriptional preinitiation complex; IDA:CAFA.
GO; GO:0035327; C:transcriptionally active chromatin; IDA:UniProtKB.
GO; GO:0051117; F:ATPase binding; IDA:MGI.
GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030284; F:estrogen receptor activity; IDA:CAFA.
GO; GO:0030331; F:estrogen receptor binding; IPI:CAFA.
GO; GO:0034056; F:estrogen response element binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; NAS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0038052; F:RNA polymerase II transcription factor activity, estrogen-activated sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
GO; GO:0003707; F:steroid hormone receptor activity; TAS:ProtInc.
GO; GO:0017025; F:TBP-class protein binding; IPI:CAFA.
GO; GO:0001093; F:TFIIB-class transcription factor binding; IPI:CAFA.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0008209; P:androgen metabolic process; IEA:Ensembl.
GO; GO:0001547; P:antral ovarian follicle growth; IEA:Ensembl.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:BHF-UCL.
GO; GO:0071391; P:cellular response to estrogen stimulus; IEA:Ensembl.
GO; GO:0006338; P:chromatin remodeling; NAS:UniProtKB.
GO; GO:0002064; P:epithelial cell development; IEA:Ensembl.
GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IEA:Ensembl.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:CAFA.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:UniProtKB.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
GO; GO:0060745; P:mammary gland branching involved in pregnancy; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:UniProtKB.
GO; GO:0010863; P:positive regulation of phospholipase C activity; ISS:UniProtKB.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IDA:CAFA.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; IEA:Ensembl.
GO; GO:0060523; P:prostate epithelial cord elongation; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0071168; P:protein localization to chromatin; IMP:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IEA:Ensembl.
GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL.
GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; TAS:ProtInc.
GO; GO:0060065; P:uterus development; IEA:Ensembl.
GO; GO:0060068; P:vagina development; IEA:Ensembl.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR024178; Oest_rcpt/oest-rel_rcp.
InterPro; IPR001292; Oestr_rcpt.
InterPro; IPR024736; Oestrogen-typ_rcpt_final_C_dom.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF12743; ESR1_C; 1.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF02159; Oest_recep; 1.
Pfam; PF00105; zf-C4; 1.
PIRSF; PIRSF500101; ER-a; 1.
PIRSF; PIRSF002527; ER-like_NR; 1.
PRINTS; PR00543; OESTROGENR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative promoter usage;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; DNA-binding;
Glycoprotein; Golgi apparatus; Lipid-binding; Lipoprotein; Membrane;
Metal-binding; Methylation; Nucleus; Palmitate; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Steroid-binding;
Transcription; Transcription regulation; Transmembrane;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 595 Estrogen receptor.
/FTId=PRO_0000053618.
DNA_BIND 185 250 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 185 205 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 221 245 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 184 Modulating (transactivation AF-1);
mediates interaction with MACROD1.
{ECO:0000269|PubMed:17914104}.
REGION 35 174 Interaction with DDX5; self-association.
REGION 35 47 Required for interaction with NCOA1.
REGION 185 310 Mediates interaction with DNTTIP2.
{ECO:0000269|PubMed:15047147}.
REGION 251 310 Hinge.
REGION 262 595 Interaction with AKAP13.
{ECO:0000269|PubMed:9627117}.
REGION 264 595 Self-association.
REGION 311 595 Transactivation AF-2.
REGION 311 551 Steroid-binding.
MOD_RES 104 104 Phosphoserine; by CDK2.
{ECO:0000269|PubMed:10428798}.
MOD_RES 106 106 Phosphoserine; by CDK2.
{ECO:0000269|PubMed:10428798}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000269|PubMed:14764652}.
MOD_RES 167 167 Phosphoserine; by CK2.
{ECO:0000269|PubMed:7838153}.
MOD_RES 260 260 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000269|PubMed:18657504}.
MOD_RES 537 537 Phosphotyrosine; by Tyr-kinases.
{ECO:0000269|PubMed:7539106}.
LIPID 447 447 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 10 10 O-linked (GlcNAc) serine. {ECO:0000250}.
VAR_SEQ 1 173 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:16165085,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_042460.
VAR_SEQ 255 366 Missing (in isoform 2).
{ECO:0000303|PubMed:3753802}.
/FTId=VSP_003680.
VAR_SEQ 458 595 VYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQ
QQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDL
LLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQ
KYYITGEAEGFPATV -> FTISHVEAKKRILNLHPKIFGN
KWFPRV (in isoform 4).
{ECO:0000303|PubMed:16165085,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_042461.
VARIANT 6 6 H -> Y (in a breast cancer sample;
somatic mutation; dbSNP:rs139960913).
{ECO:0000269|PubMed:17224074}.
/FTId=VAR_033028.
VARIANT 77 77 G -> S (in dbSNP:rs9340773).
/FTId=VAR_018905.
VARIANT 160 160 G -> C (in dbSNP:rs149308960).
{ECO:0000269|PubMed:9195227}.
/FTId=VAR_004671.
VARIANT 264 264 M -> I (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:17224074}.
/FTId=VAR_033029.
VARIANT 375 375 Q -> H (in ESTRR; results in highly
reduced activity; dbSNP:rs397509428).
{ECO:0000269|PubMed:23841731}.
/FTId=VAR_070072.
VARIANT 394 394 R -> H (in ESTRR; highly decreased
estrogen receptor activity).
{ECO:0000269|PubMed:27754803}.
/FTId=VAR_078516.
VARIANT 400 400 G -> V (destabilizes the receptor and
decreases its affinity for estradiol at
25 degrees Celsius, but not at 4 degrees
Celsius). {ECO:0000269|PubMed:2792078,
ECO:0000269|PubMed:3753802,
ECO:0000269|PubMed:3754034}.
/FTId=VAR_004673.
VARIANT 411 411 D -> RNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVC
LKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIH
LMAKAGLTLQQQHQRLAQLLLILSHIRHM (in a 80
kDa form found in a breast cancer line;
contains an in-frame duplication of exons
6 and 7).
/FTId=VAR_010143.
MUTAGEN 39 39 L->P: Impairs AF-1 transactivation.
{ECO:0000269|PubMed:11075817}.
MUTAGEN 43 43 Y->P: Impairs AF-1 transactivation.
{ECO:0000269|PubMed:11075817}.
MUTAGEN 104 104 S->A: Loss of cyclin A-dependent
induction of transcriptional activation.
MUTAGEN 106 106 S->A: Loss of cyclin A-dependent
induction of transcriptional activation.
MUTAGEN 118 118 S->A: Decreases phosphorylation and
transactivation activity. Abolishes AF-1
transactivation. Insensitive to PPP5C
inhibition of transactivation activity.
{ECO:0000269|PubMed:10409727,
ECO:0000269|PubMed:14764652}.
MUTAGEN 118 118 S->E: Enhances transactivation activity.
Enhances interaction with DDX5.
Insensitive to PPP5C inhibition of
transactivation activity.
{ECO:0000269|PubMed:10409727,
ECO:0000269|PubMed:14764652}.
MUTAGEN 260 260 R->A,K: Loss of methylation.
{ECO:0000269|PubMed:18657504}.
MUTAGEN 364 364 V->E: Has higher transcriptional activity
in the absence of wild type ER. Inhibits
transcriptional activity when coexpressed
with the wild type receptor.
{ECO:0000269|PubMed:8961262}.
MUTAGEN 386 386 I->C: Loss of transmembrane localization,
no effect on peripheral membrane
localization. Impairs activation of
estrogen-induced activation of NOS3 and
production of nitric oxide. No effect on
binding to ERES.
{ECO:0000269|PubMed:21937726}.
MUTAGEN 447 447 C->A: Loss of hormone binding capacity
and temperature-sensitive loss in DNA-
binding. {ECO:0000269|PubMed:1577818}.
MUTAGEN 539 539 L->A: Abolishes interaction with NCOA1,
NCOA2 and NCOA3.
{ECO:0000269|PubMed:12554772}.
CONFLICT 452 452 I -> L (in Ref. 5; CAE45969).
{ECO:0000305}.
TURN 186 188 {ECO:0000244|PDB:1HCQ}.
STRAND 189 191 {ECO:0000244|PDB:1HCP}.
STRAND 194 196 {ECO:0000244|PDB:1HCQ}.
STRAND 199 201 {ECO:0000244|PDB:1HCQ}.
HELIX 203 213 {ECO:0000244|PDB:1HCQ}.
STRAND 222 225 {ECO:0000244|PDB:1HCQ}.
TURN 231 236 {ECO:0000244|PDB:1HCQ}.
HELIX 238 248 {ECO:0000244|PDB:1HCQ}.
HELIX 288 291 {ECO:0000244|PDB:2LLO}.
HELIX 302 304 {ECO:0000244|PDB:3Q95}.
HELIX 307 309 {ECO:0000244|PDB:3UUD}.
HELIX 312 322 {ECO:0000244|PDB:5DXE}.
STRAND 330 332 {ECO:0000244|PDB:2YJA}.
STRAND 334 336 {ECO:0000244|PDB:2QZO}.
HELIX 339 361 {ECO:0000244|PDB:5DXE}.
HELIX 367 369 {ECO:0000244|PDB:5DXE}.
HELIX 372 394 {ECO:0000244|PDB:5DXE}.
TURN 395 397 {ECO:0000244|PDB:5DXE}.
STRAND 402 405 {ECO:0000244|PDB:5DXE}.
STRAND 408 410 {ECO:0000244|PDB:5DXE}.
HELIX 412 415 {ECO:0000244|PDB:5DXE}.
STRAND 418 420 {ECO:0000244|PDB:5KCW}.
HELIX 421 438 {ECO:0000244|PDB:5DXE}.
HELIX 442 455 {ECO:0000244|PDB:5DXE}.
HELIX 458 460 {ECO:0000244|PDB:5DXE}.
TURN 464 466 {ECO:0000244|PDB:2B1V}.
HELIX 467 469 {ECO:0000244|PDB:3UUD}.
HELIX 473 492 {ECO:0000244|PDB:5DXE}.
HELIX 497 530 {ECO:0000244|PDB:5DXE}.
STRAND 531 533 {ECO:0000244|PDB:2OUZ}.
HELIX 538 545 {ECO:0000244|PDB:5DXE}.
HELIX 547 549 {ECO:0000244|PDB:5AAU}.
SEQUENCE 595 AA; 66216 MW; 5455C57AB0CCCAA7 CRC64;
MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKIPLERPLG EVYLDSSKPA VYNYPEGAAY
EFNAAAAANA QVYGQTGLPY GPGSEAAAFG SNGLGGFPPL NSVSPSPLML LHPPPQLSPF
LQPHGQQVPY YLENEPSGYT VREAGPPAFY RPNSDNRRQG GRERLASTND KGSMAMESAK
ETRYCAVCND YASGYHYGVW SCEGCKAFFK RSIQGHNDYM CPATNQCTID KNRRKSCQAC
RLRKCYEVGM MKGGIRKDRR GGRMLKHKRQ RDDGEGRGEV GSAGDMRAAN LWPSPLMIKR
SKKNSLALSL TADQMVSALL DAEPPILYSE YDPTRPFSEA SMMGLLTNLA DRELVHMINW
AKRVPGFVDL TLHDQVHLLE CAWLEILMIG LVWRSMEHPG KLLFAPNLLL DRNQGKCVEG
MVEIFDMLLA TSSRFRMMNL QGEEFVCLKS IILLNSGVYT FLSSTLKSLE EKDHIHRVLD
KITDTLIHLM AKAGLTLQQQ HQRLAQLLLI LSHIRHMSNK GMEHLYSMKC KNVVPLYDLL
LEMLDAHRLH APTSRGGASV EETDQSHLAT AGSTSSHSLQ KYYITGEAEG FPATV


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