ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P03372


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ESR1_HUMAN
Primary accession number P03372
Secondary accession numbers Q13511 Q14276 Q9NU51 Q9UDZ7 Q9UIS7
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on June 1, 1994 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 140)
Name and origin of the protein
Protein name Estrogen receptor
Synonyms ER
Estradiol receptor
ER-alpha
Nuclear receptor subfamily 3 group A member 1
Gene name
Name: ESR1
Synonyms: ESR, NR3A1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
PubMed=3753802 [NCBI, ExPASy, EBI, Israel, Japan]
Greene G.L., Gilna P., Waterfield M., Baker A., Hort Y., Shine J.;
"Sequence and expression of human estrogen receptor complementary DNA.";
Science 231:1150-1154(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
DOI=10.1038/320134a0; PubMed=3754034 [NCBI, ExPASy, EBI, Israel, Japan]
Green S., Walter P., Kumar V., Krust A., Bornert J.-M., Argos P., Chambon P.;
"Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A.";
Nature 320:134-139(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT ASP-411 INS.
TISSUE=Mammary gland;
DOI=10.1093/nar/24.5.962; PubMed=8600466 [NCBI, ExPASy, EBI, Israel, Japan]
Pink J.J., Wu S.Q., Wolf D.M., Bilimoria M.M., Jordan V.C.;
"A novel 80 kDa human estrogen receptor containing a duplication of exons 6 and 7.";
Nucleic Acids Res. 24:962-969(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-77.
Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 152-595 (ISOFORM LONG).
DOI=10.1016/S0960-0760(99)00126-0; PubMed=10619354 [NCBI, ExPASy, EBI, Israel, Japan]
Schubert E.L., Lee M.K., Newman B., King M.C.;
"Single nucleotide polymorphisms (SNPs) in the estrogen receptor gene and breast cancer susceptibility.";
J. Steroid Biochem. Mol. Biol. 71:21-27(1999).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 216-434, AND ALTERNATIVE SPLICING.
TISSUE=Mammary carcinoma;
PubMed=7916651 [NCBI, ExPASy, EBI, Israel, Japan]
Pfeffer U., Fecarotta E., Castagnetta L., Vidali G.;
"Estrogen receptor variant messenger RNA lacking exon 4 in estrogen-responsive human breast cancer cell lines.";
Cancer Res. 53:741-743(1993).
[8]
PROTEIN SEQUENCE OF 110-117, PHOSPHORYLATION, AND MUTAGENESIS.
DOI=10.1210/me.9.8.1041; PubMed=7476978 [NCBI, ExPASy, EBI, Israel, Japan]
Joel P.B., Traish A.M., Lannigan D.A.;
"Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor.";
Mol. Endocrinol. 9:1041-1052(1995).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 354-548.
TISSUE=Mammary carcinoma;
Naundorf H., Becker M., Fiebig C., Buettner B., Fichtner I.;
"Mechanisms of acquired tamoxifen resistance in a xenotransplanted human breast carcinoma.";
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[10]
PROTEIN SEQUENCE OF 532-542, AND PHOSPHORYLATION.
DOI=10.1210/me.9.1.24; PubMed=7539106 [NCBI, ExPASy, EBI, Israel, Japan]
Arnold S.F., Obourn J.D., Jaffe H., Notides A.C.;
"Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro.";
Mol. Endocrinol. 9:24-33(1995).
[11]
MUTAGENESIS OF CYS-447.
PubMed=1577818 [NCBI, ExPASy, EBI, Israel, Japan]
Reese J.C., Katzenellenbogen B.S.;
"Characterization of a temperature-sensitive mutation in the hormone binding domain of the human estrogen receptor. Studies in cell extracts and intact cells and their implications for hormone-dependent transcriptional activation.";
J. Biol. Chem. 267:9868-9873(1992).
[12]
PHOSPHORYLATION.
DOI=10.1210/me.8.9.1208; PubMed=7838153 [NCBI, ExPASy, EBI, Israel, Japan]
Arnold S.F., Obourn J.D., Jaffe H., Notides A.C.;
"Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor.";
Mol. Endocrinol. 8:1208-1214(1994).
[13]
GLYCOSYLATION.
DOI=10.1074/jbc.272.48.30122; PubMed=8999954 [NCBI, ExPASy, EBI, Israel, Japan]
Jiang M.S., Hart G.W.;
"A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine.";
J. Biol. Chem. 272:2421-2428(1997).
[14]
INTERACTION WITH AKAP13.
DOI=10.1038/sj.onc.1201783; PubMed=9627117 [NCBI, ExPASy, EBI, Israel, Japan]
Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O., Pagliai K., Gray K., Gutkind S., Segars J.;
"Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action.";
Oncogene 16:2513-2526(1998).
[15]
PHOSPHORYLATION AT SER-104 AND SER-106, AND MUTAGENESIS.
DOI=10.1074/jbc.274.32.22296; PubMed=10428798 [NCBI, ExPASy, EBI, Israel, Japan]
Rogatsky I., Trowbridge J.M., Garabedian M.J.;
"Potentiation of human estrogen receptor alpha transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin A-CDK2 complex.";
J. Biol. Chem. 274:22296-22302(1999).
[16]
INTERACTION WITH NCOA6.
DOI=10.1074/jbc.274.48.34283; PubMed=10567404 [NCBI, ExPASy, EBI, Israel, Japan]
Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
"A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo.";
J. Biol. Chem. 274:34283-34293(1999).
[17]
INTERACTION WITH PHB2.
DOI=10.1073/pnas.96.12.6947; PubMed=10359819 [NCBI, ExPASy, EBI, Israel, Japan]
Montano M.M., Ekena K., Delage-Mourroux R., Chang W., Martini P., Katzenellenbogen B.S.;
"An estrogen receptor-selective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens.";
Proc. Natl. Acad. Sci. U.S.A. 96:6947-6952(1999).
[18]
INTERACTION WITH PBXIP1.
DOI=10.1074/jbc.M001323200; PubMed=10825160 [NCBI, ExPASy, EBI, Israel, Japan]
Abramovich C., Shen W.-F., Pineault N., Imren S., Montpetit B., Largman C., Humphries R.K.;
"Functional cloning and characterization of a novel nonhomeodomain protein that inhibits the binding of PBX1-HOX complexes to DNA.";
J. Biol. Chem. 275:26172-26177(2000).
[19]
INTERACTION WITH JARID1A.
DOI=10.1074/jbc.M100313200; PubMed=11358960 [NCBI, ExPASy, EBI, Israel, Japan]
Chan S.W., Hong W.;
"Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone receptor-mediated transcription.";
J. Biol. Chem. 276:28402-28412(2001).
[20]
INTERACTION WITH NCOA5.
DOI=10.1128/MCB.21.1.343-353.2001; PubMed=11113208 [NCBI, ExPASy, EBI, Israel, Japan]
Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F., Giguere V.;
"CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant.";
Mol. Cell. Biol. 21:343-353(2001).
[21]
INTERACTION WITH NCOA7.
DOI=10.1128/MCB.22.10.3358-3372.2002; PubMed=11971969 [NCBI, ExPASy, EBI, Israel, Japan]
Shao W., Halachmi S., Brown M.;
"ERAP140, a conserved tissue-specific nuclear receptor coactivator.";
Mol. Cell. Biol. 22:3358-3372(2002).
[22]
INTERACTION WITH PELP1.
DOI=10.1073/pnas.192569699; PubMed=12415108 [NCBI, ExPASy, EBI, Israel, Japan]
Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
"Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade.";
Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002).
[23]
INTERACTION WITH SMARD1.
DOI=10.1128/MCB.23.17.6210-6220.2003; PubMed=12917342 [NCBI, ExPASy, EBI, Israel, Japan]
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
"BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation.";
Mol. Cell. Biol. 23:6210-6220(2003).
[24]
INTERACTION WITH DNTTIP2.
DOI=10.1016/j.bbrc.2004.02.179; PubMed=15047147 [NCBI, ExPASy, EBI, Israel, Japan]
Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M., Zhu Y.-J.;
"ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor.";
Biochem. Biophys. Res. Commun. 317:54-59(2004).
[25]
INTERACTION WITH TXNRD1.
DOI=10.1074/jbc.M402753200; PubMed=15199063 [NCBI, ExPASy, EBI, Israel, Japan]
Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A., Spyrou G.;
"An alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signaling.";
J. Biol. Chem. 279:38721-38729(2004).
[26]
INTERACTION WITH HEXIM1.
DOI=10.1038/sj.onc.1208728; PubMed=15940264 [NCBI, ExPASy, EBI, Israel, Japan]
Wittmann B.M., Fujinaga K., Deng H., Ogba N., Montano M.M.;
"The breast cell growth inhibitor, estrogen down regulated gene 1, modulates a novel functional interaction between estrogen receptor alpha and transcriptional elongation factor cyclin T1.";
Oncogene 24:5576-5588(2005).
[27]
INTERACTION WITH MLL2.
DOI=10.1074/jbc.M513245200; PubMed=16603732 [NCBI, ExPASy, EBI, Israel, Japan]
Mo R., Rao S.M., Zhu Y.-J.;
"Identification of the MLL2 complex as a coactivator for estrogen receptor alpha.";
J. Biol. Chem. 281:15714-15720(2006).
[28]
INTERACTION WITH MUC1.
DOI=10.1016/j.molcel.2005.11.030; PubMed=16427018 [NCBI, ExPASy, EBI, Israel, Japan]
Wei X., Xu H., Kufe D.;
"MUC1 oncoprotein stabilizes and activates estrogen receptor alpha.";
Mol. Cell 21:295-305(2006).
[29]
INTERACTION WITH MAP1S.
DOI=10.1016/j.bbrc.2007.06.179; PubMed=17658481 [NCBI, ExPASy, EBI, Israel, Japan]
Eriksson M., Samuelsson H., Samuelsson E.-B., Liu L., McKeehan W.L., Benedikz E., Sundstroem E.;
"The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in the brain.";
Biochem. Biophys. Res. Commun. 361:127-132(2007).
[30]
INTERACTION WITH CUEDC2.
DOI=10.1038/sj.emboj.7601602; PubMed=17347654 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang P.-J., Zhao J., Li H.-Y., Man J.-H., He K., Zhou T., Pan X., Li A.-L., Gong W.-L., Jin B.-F., Xia Q., Yu M., Shen B.-F., Zhang X.-M.;
"CUE domain containing 2 regulates degradation of progesterone receptor by ubiquitin-proteasome.";
EMBO J. 26:1831-1842(2007).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7 AND SER-10, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[32]
STRUCTURE BY NMR OF 180-262.
DOI=10.1038/348458a0; PubMed=2247153 [NCBI, ExPASy, EBI, Israel, Japan]
Schwabe J.W.E., Neuhaus D., Rhodes D.;
"Solution structure of the DNA-binding domain of the oestrogen receptor.";
Nature 348:458-461(1990).
[33]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 180-262.
DOI=10.1016/0092-8674(93)90390-C; PubMed=8221895 [NCBI, ExPASy, EBI, Israel, Japan]
Schwabe J.W.E., Chapman L., Finch J.T., Rhodes D.;
"The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements.";
Cell 75:567-578(1993).
[34]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 305-548.
DOI=10.1038/39645; PubMed=9338790 [NCBI, ExPASy, EBI, Israel, Japan]
Brzozowski A.M., Pike A.C.W., Dauter Z., Hubbard R.E., Bonn T., Engstroem O., Oehman L., Greene G.L., Gustafsson J.-A., Carlquist M.;
"Molecular basis of agonism and antagonism in the oestrogen receptor.";
Nature 389:753-758(1997).
[35]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 306-544.
DOI=10.1073/pnas.95.11.5998; PubMed=9600906 [NCBI, ExPASy, EBI, Israel, Japan]
Tanenbaum D.M., Wang Y., Williams S.P., Sigler P.B.;
"Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains.";
Proc. Natl. Acad. Sci. U.S.A. 95:5998-6003(1998).
[36]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 294-554.
DOI=10.1016/S0092-8674(00)81717-1; PubMed=9875847 [NCBI, ExPASy, EBI, Israel, Japan]
Shiau A.K., Barstad D., Loria P.M., Cheng L., Kushner P.J., Agard D.A., Greene G.L.;
"The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen.";
Cell 95:927-937(1998).
[37]
3D-STRUCTURE MODELING OF 311-547.
PubMed=9619507 [NCBI, ExPASy, EBI, Israel, Japan]
Maalouf G.J., Xu W., Smith T., Mohr S.C.;
"Homology model for the ligand-binding domain of the human estrogen receptor.";
J. Biomol. Struct. Dyn. 15:841-850(1998).
[38]
VARIANT VAL-400.
PubMed=2792078 [NCBI, ExPASy, EBI, Israel, Japan]
Tora L., Mullick A., Metzger D., Ponglikitmongkol M., Park I., Chambon P.;
"The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties.";
EMBO J. 8:1981-1986(1989).
[39]
VARIANT GLU-364.
DOI=10.1210/me.10.12.1519; PubMed=8961262 [NCBI, ExPASy, EBI, Israel, Japan]
McInerney E.M., Ince B.A., Shapiro D.J., Katzenellenbogen B.S.;
"A transcriptionally active estrogen receptor mutant is a novel type of dominant negative inhibitor of estrogen action.";
Mol. Endocrinol. 10:1519-1526(1996).
[40]
VARIANT CYS-160.
DOI=10.1002/(SICI)1098-1004(1997)9:6<531::AID-HUMU6>3.3.CO;2-J; PubMed=9195227 [NCBI, ExPASy, EBI, Israel, Japan]
Anderson T.I., Wooster R., Laake K., Collins N., Warren W., Skrede M., Eeles R., Tveit K.M., Johnston S.R.D., Dowsett M., Olsen A.O., Moeller P., Stratton M.R., Boerresen-Dale A.-L.;
"Screening for ESR mutations in breast and ovarian cancer patients.";
Hum. Mutat. 9:531-536(1997).
[41]
INVOLVEMENT IN BMD.
DOI=10.1093/hmg/9.13.2043; PubMed=10942433 [NCBI, ExPASy, EBI, Israel, Japan]
Becherini L., Gennari L., Masi L., Mansani R., Massart F., Morelli A., Falchetti A., Gonnelli S., Fiorelli G., Tanini A., Brandi M.L.;
"Evidence of a linkage disequilibrium between polymorphisms in the human estrogen receptor alpha gene and their relationship to bone mass variation in postmenopausal Italian women.";
Hum. Mol. Genet. 9:2043-2050(2000).
[42]
VARIANTS TYR-6 AND ILE-264.
DOI=10.1186/bcr1637; PubMed=17224074 [NCBI, ExPASy, EBI, Israel, Japan]
Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M., Boerresen-Dale A.L.;
"Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas.";
Breast Cancer Res. 9:R5-R5(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X03635; CAA27284.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12674; AAA52399.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U47678; AAB00115.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY425004; AAQ91815.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X73067; CAA51528.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL078582; CAI42285.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356311; CAI42285.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590993; CAI42285.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123500; AAD52984.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123494; AAD52984.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123495; AAD52984.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123496; AAD52984.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123497; AAD52984.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123498; AAD52984.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF123499; AAD52984.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z75126; CAA99436.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64737; S64737.
RefSeq NP_000116.2; -.
NP_001116212.1; -.
NP_001116213.1; -.
NP_001116214.1; -.
UniGene Hs.208124
3D structure databases
PDB
1A52; X-ray; 2.80 A; A/B=297-554.[ExPASy / RCSB / EBI]
1AKF; Model; -; A=309-547.[ExPASy / RCSB / EBI]
1ERE; X-ray; 3.10 A; A/B/C/D/E/F=301-553.[ExPASy / RCSB / EBI]
1ERR; X-ray; 2.60 A; A/B=301-553.[ExPASy / RCSB / EBI]
1G50; X-ray; 2.90 A; A/B/C=304-550.[ExPASy / RCSB / EBI]
1GWQ; X-ray; 2.45 A; A/B=301-548.[ExPASy / RCSB / EBI]
1GWR; X-ray; 2.40 A; A/B=305-549.[ExPASy / RCSB / EBI]
1HCP; NMR; -; A=180-254.[ExPASy / RCSB / EBI]
1HCQ; X-ray; 2.40 A; A/B/E/F=180-262.[ExPASy / RCSB / EBI]
1L2I; X-ray; 1.95 A; A/B=297-554.[ExPASy / RCSB / EBI]
1PCG; X-ray; 2.70 A; A/B=304-547.[ExPASy / RCSB / EBI]
1QKT; X-ray; 2.20 A; A=304-551.[ExPASy / RCSB / EBI]
1QKU; X-ray; 3.20 A; A/B/C=301-550.[ExPASy / RCSB / EBI]
1R5K; X-ray; 2.70 A; A/B/C=297-554.[ExPASy / RCSB / EBI]
1SJ0; X-ray; 1.90 A; A=307-554.[ExPASy / RCSB / EBI]
1UOM; X-ray; 2.28 A; A=301-553.[ExPASy / RCSB / EBI]
1X7E; X-ray; 2.80 A; A/B=305-549.[ExPASy / RCSB / EBI]
1X7R; X-ray; 2.00 A; A=305-549.[ExPASy / RCSB / EBI]
1XP1; X-ray; 1.80 A; A=307-554.[ExPASy / RCSB / EBI]
1XP6; X-ray; 1.70 A; A=307-554.[ExPASy / RCSB / EBI]
1XP9; X-ray; 1.80 A; A=307-554.[ExPASy / RCSB / EBI]
1XPC; X-ray; 1.60 A; A=307-554.[ExPASy / RCSB / EBI]
1XQC; X-ray; 2.05 A; A/B/C/D=301-553.[ExPASy / RCSB / EBI]
1YIM; X-ray; 1.90 A; A=307-554.[ExPASy / RCSB / EBI]
1YIN; X-ray; 2.20 A; A=307-554.[ExPASy / RCSB / EBI]
1ZKY; X-ray; 2.25 A; A/B=298-554.[ExPASy / RCSB / EBI]
2AYR; X-ray; 1.90 A; A=304-551.[ExPASy / RCSB / EBI]
2B1V; X-ray; 1.80 A; A/B=298-554.[ExPASy / RCSB / EBI]
2B1Z; X-ray; 1.78 A; A/B=298-554.[ExPASy / RCSB / EBI]
2B23; X-ray; 2.10 A; A/B=298-554.[ExPASy / RCSB / EBI]
2BJ4; X-ray; 2.00 A; A/B=304-533.[ExPASy / RCSB / EBI]
2FAI; X-ray; 2.10 A; A/B=298-554.[ExPASy / RCSB / EBI]
2G44; X-ray; 2.65 A; A/B=298-554.[ExPASy / RCSB / EBI]
2G5O; X-ray; 2.30 A; A/B=298-554.[ExPASy / RCSB / EBI]
2I0J; X-ray; 2.90 A; A/B/C/D=304-547.[ExPASy / RCSB / EBI]
2IOG; X-ray; 1.60 A; A=309-554.[ExPASy / RCSB / EBI]
2IOK; X-ray; 2.40 A; A/B=301-554.[ExPASy / RCSB / EBI]
2JF9; X-ray; 2.10 A; A/B/C=303-533.[ExPASy / RCSB / EBI]
2JFA; X-ray; 2.55 A; A/B=303-533.[ExPASy / RCSB / EBI]
2OCF; X-ray; 2.95 A; A=298-595.[ExPASy / RCSB / EBI]
2OUZ; X-ray; 2.00 A; A=301-553.[ExPASy / RCSB / EBI]
2P15; X-ray; 1.94 A; A/B=298-554.[ExPASy / RCSB / EBI]
2POG; X-ray; 1.84 A; A/B=304-551.[ExPASy / RCSB / EBI]
2Q6J; X-ray; 2.70 A; A/B=298-554.[ExPASy / RCSB / EBI]
2Q70; X-ray; 1.95 A; A/B=304-551.[ExPASy / RCSB / EBI]
2QA6; X-ray; 2.60 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QA8; X-ray; 1.85 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QAB; X-ray; 1.89 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QE4; X-ray; 2.40 A; A/B=304-551.[ExPASy / RCSB / EBI]
2QGT; X-ray; 2.15 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QGW; X-ray; 2.39 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QH6; X-ray; 2.70 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QR9; X-ray; 2.00 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QSE; X-ray; 1.85 A; A/B=298-554.[ExPASy / RCSB / EBI]
2QXM; X-ray; 2.30 A; A/B=298-554.[ExPASy / RCSB / EBI]
2R6W; X-ray; 2.00 A; A/B=304-551.[ExPASy / RCSB / EBI]
2R6Y; X-ray; 2.00 A; A/B=304-551.[ExPASy / RCSB / EBI]
3CBM; X-ray; 1.69 A; B=298-307.[ExPASy / RCSB / EBI]
3ERD; X-ray; 2.03 A; A/B=297-554.[ExPASy / RCSB / EBI]
3ERT; X-ray; 1.90 A; A=297-554.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A52; -.
1AKF; -.
1ERE; -.
1ERR; -.
1G50; -.
1GWQ; -.
1GWR; -.
1HCP; -.
1HCQ; -.
1L2I; -.
1PCG; -.
1QKT; -.
1QKU; -.
1R5K; -.
1SJ0; -.
1UOM; -.
1X7E; -.
1X7R; -.
1XP1; -.
1XP6; -.
1XP9; -.
1XPC; -.
1XQC; -.
1YIM; -.
1YIN; -.
1ZKY; -.
2AYR; -.
2B1V; -.
2B1Z; -.
2B23; -.
2BJ4; -.
2FAI; -.
2G44; -.
2G5O; -.
2I0J; -.
2IOG; -.
2IOK; -.
2JF9; -.
2JFA; -.
2OCF; -.
2OUZ; -.
2P15; -.
2POG; -.
2Q6J; -.
2Q70; -.
2QA6; -.
2QA8; -.
2QAB; -.
2QE4; -.
2QGT; -.
2QGW; -.
2QH6; -.
2QR9; -.
2QSE; -.
2QXM; -.
2R6W; -.
2R6Y; -.
3CBM; -.
3ERD; -.
3ERT; -.
DisProt DP00074; -.
ModBase P03372.
Protein-protein interaction databases
DIP DIP:5965N; -.
IntAct P03372; -.
PTM databases
GlycoSuiteDB P03372; -.
PhosphoSite P03372; -.
Polymorphism databases
NIEHS-SNPs ESR1.
Organism-specific databases
HGNC HGNC:3467; ESR1.
GenAtlas ESR1.
HPA CAB000037; -.
HPA000449; -.
HPA000450; -.
MIM 133430; gene. [NCBI / EBI]
Orphanet 785; Estrogen resistance syndrome.
PharmGKB PA156; -.
GeneCards P03372.
Gene expression databases
ArrayExpress P03372; -.
CleanEx HS_ESR1; -.
GermOnline ENSG00000091831; Homo sapiens.
Ontologies
GO
GO:0016585; Cellular component: chromatin remodeling complex (non-traceable author statement from UniProtKB).
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005730; Cellular component: nucleolus (inferred from direct assay from HPA).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from HPA).
GO:0030284; Molecular function: estrogen receptor activity (non-traceable author statement from UniProtKB).
GO:0030235; Molecular function: nitric-oxide synthase regulator activity (non-traceable author statement from UniProtKB).
GO:0047485; Molecular function: protein N-terminus binding (inferred from physical interaction from UniProtKB).
GO:0030520; Biological process: estrogen receptor signaling pathway (non-traceable author statement from UniProtKB).
GO:0048386; Biological process: positive regulation of retinoic acid receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR008946; Nucl_hormone_rcpt_ligand-bd.
IPR000536; Nucl_hrmn_rcpt_lig-bd_core.
IPR001292; Oestr_rcpt_AF1.
IPR001723; Str_hrmn_rcpt.
IPR001628; Znf_hrmn_rcpt.
IPR013088; Znf_NHR/GATA.
Graphical view of domain structure.
Gene3D G3DSA:1.10.565.10; Nucl_hrmn_rcpt_lig_bd; 1.<