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

 ESR1_MOUSE              Reviewed;         599 AA.
P19785; Q9JJT5; Q9QY51; Q9QY52;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
26-FEB-2020, entry version 226.
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, Estr, Estra, Nr3a1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Uterus;
PubMed=2484714; DOI=10.1210/mend-1-10-735;
White R., Lees J.A., Needham M., Ham J., Parker M.;
"Structural organization and expression of the mouse estrogen receptor.";
Mol. Endocrinol. 1:735-744(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=10899303; DOI=10.1016/s0014-5793(00)01750-6;
Kos M., O'Brien S., Flouriot G., Gannon F.;
"Tissue-specific expression of multiple mRNA variants of the mouse estrogen
receptor alpha gene.";
FEBS Lett. 477:15-20(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 269-599, AND VARIANT GLN-591.
STRAIN=B10.S/J, and SJL/J; TISSUE=Spleen;
Ma R.Z., Teuscher C.;
"Screening for candidate genes of mouse autoimmune diseases.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH NRIP1.
PubMed=7641693; DOI=10.1002/j.1460-2075.1995.tb00044.x;
Cavailles V., Dauvois S., L'Horset F., Lopez G., Hoare S., Kushner P.J.,
Parker M.G.;
"Nuclear factor RIP140 modulates transcriptional activation by the estrogen
receptor.";
EMBO J. 14:3741-3751(1995).
[6]
INTERACTION WITH POU4F2.
PubMed=9448000; DOI=10.1128/mcb.18.2.1029;
Budhram-Mahadeo V., Parker M., Latchman D.S.;
"POU transcription factors Brn-3a and Brn-3b interact with the estrogen
receptor and differentially regulate transcriptional activity via an
estrogen response element.";
Mol. Cell. Biol. 18:1029-1041(1998).
[7]
FUNCTION, INTERACTION WITH NCOA1, AND MUTAGENESIS OF ILE-362; LYS-366;
LEU-376; VAL-380 AND LEU-543.
PubMed=10207113; DOI=10.1128/mcb.19.5.3895;
Mak H.Y., Hoare S., Henttu P.M., Parker M.G.;
"Molecular determinants of the estrogen receptor-coactivator interface.";
Mol. Cell. Biol. 19:3895-3903(1999).
[8]
FUNCTION, INTERACTION WITH NCOA1, AND MUTAGENESIS OF PHE-371; LEU-508;
ALA-509; LEU-512; LEU-515; GLY-525; ASP-542; 543-LEU-LEU-544; GLU-546;
547-MET-LEU-548 AND ASP-549.
PubMed=10840033; DOI=10.1074/jbc.m002497200;
Valentine J.E., Kalkhoven E., White R., Hoare S., Parker M.G.;
"Mutations in the estrogen receptor ligand binding domain discriminate
between hormone-dependent transactivation and transrepression.";
J. Biol. Chem. 275:25322-25329(2000).
[9]
INTERACTION WITH FAM120B.
PubMed=17595322; DOI=10.1210/me.2006-0520;
Li D., Kang Q., Wang D.-M.;
"Constitutive coactivator of peroxisome proliferator-activated receptor
(PPARgamma), a novel coactivator of PPARgamma that promotes adipogenesis.";
Mol. Endocrinol. 21:2320-2333(2007).
[10]
GLYCOSYLATION AT THR-575.
PubMed=8999954; DOI=10.1074/jbc.272.4.2421;
Jiang M.S., Hart G.W.;
"A subpopulation of estrogen receptors are modified by O-linked N-
acetylglucosamine.";
J. Biol. Chem. 272:2421-2428(1997).
[11]
GLYCOSYLATION AT SER-10; THR-50 AND THR-575.
PubMed=11226831; DOI=10.1016/s0960-0760(00)00167-9;
Cheng X., Hart G.W.;
"Glycosylation of the murine estrogen receptor-alpha.";
J. Steroid Biochem. Mol. Biol. 75:147-158(2000).
[12]
INTERACTION WITH NCOA3.
PubMed=9192892; DOI=10.1038/42652;
Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K.,
Rosenfeld M.G.;
"The transcriptional co-activator p/CIP binds CBP and mediates nuclear-
receptor function.";
Nature 387:677-684(1997).
[13]
INTERACTION WITH NCOA6.
PubMed=10788465; DOI=10.1074/jbc.275.18.13510;
Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K.;
"Isolation and characterization of peroxisome proliferator-activated
receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR.";
J. Biol. Chem. 275:13510-13516(2000).
[14]
INTERACTION WITH RBM39.
PubMed=11704680; DOI=10.1074/jbc.m110417200;
Jung D.-J., Na S.-Y., Na D.S., Lee J.W.;
"Molecular cloning and characterization of CAPER, a novel coactivator of
activating protein-1 and estrogen receptors.";
J. Biol. Chem. 277:1229-1234(2002).
[15]
INTERACTION WITH PHB2.
PubMed=15140878; DOI=10.1074/jbc.m312300200;
Kurtev V., Margueron R., Kroboth K., Ogris E., Cavailles V., Seiser C.;
"Transcriptional regulation by the repressor of estrogen receptor activity
via recruitment of histone deacetylases.";
J. Biol. Chem. 279:24834-24843(2004).
[16]
INTERACTION WITH SLC30A9.
PubMed=15988012; DOI=10.1128/mcb.25.14.5965-5972.2005;
Chen Y.-H., Kim J.H., Stallcup M.R.;
"GAC63, a GRIP1-dependent nuclear receptor coactivator.";
Mol. Cell. Biol. 25:5965-5972(2005).
[17]
INTERACTION WITH FOXL2.
PubMed=20005806; DOI=10.1016/j.cell.2009.11.021;
Uhlenhaut N.H., Jakob S., Anlag K., Eisenberger T., Sekido R., Kress J.,
Treier A.C., Klugmann C., Klasen C., Holter N.I., Riethmacher D.,
Schutz G., Cooney A.J., Lovell-Badge R., Treier M.;
"Somatic sex reprogramming of adult ovaries to testes by FOXL2 ablation.";
Cell 139:1130-1142(2009).
[18]
PALMITOYLATION AT CYS-451, AND MUTAGENESIS OF CYS-451.
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).
-!- 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. Essential for MTA1-mediated transcriptional regulation
of BRCA1 and BCAS3. {ECO:0000269|PubMed:10207113,
ECO:0000269|PubMed:10840033}.
-!- SUBUNIT: Interacts with BCAS3. Binds DNA as a homodimer (By
similarity). Can form a heterodimer with ESR2 (By similarity).
Interacts with coactivator NCOA5. Interacts with NCOA7; the interaction
is ligand-inducible. Interacts with AKAP13, CUEDC2, HEXIM1, KDM5A,
MAP1S, PELP1, SMARD1, and UBE1C. Interacts with MUC1; the interaction
is stimulated by 7 beta-estradiol (E2) and enhances ERS1-mediated
transcription. Interacts with DNTTIP2, and UIMC1. Interacts with
KMT2D/MLL2. Interacts with ATAD2; the interaction is enhanced by
estradiol. Interacts with KIF18A and LDB1. Interacts with RLIM (via its
C-terminus). Interacts with MACROD1. Interacts with SH2D4A and PLCG.
Interacts with SH2D4A; the interaction blocks binding to PLCG and
inhibits estrogen-induced cell proliferation. Interacts with DYNLL1.
Interacts with CCDC62; the interaction requires estradiol and appears
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 PIK3R2, SRC and
PTK2/FAK1. Interacts with RBFOX2. Interacts with EP300; the interaction
is estrogen-dependent and enhanced by CITED1. Interacts with CITED1;
the interaction is estrogen-dependent (By similarity). Interacts with
FAM120B, FOXL2, PHB2 and SLC30A9. Interacts with coactivators NCOA3 and
NCOA6. 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 (By similarity).
Interacts with BCAS3. Interacts with TRIP4 (ufmylated); estrogen
dependent (By similarity). 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 (By similarity). Interacts
with SFR1 in a ligand-dependent and -independent manner (By
similarity). Interacts with DCAF13, LATS1 and DCAF1; regulates ESR1
ubiquitination and ubiquitin-mediated proteasomal degradation (By
similarity). Interacts (via DNA-binding domain) with POU4F2 isoform 2
(C-terminus); this interaction increases the estrogen receptor ESR1
transcriptional activity in a DNA- and ligand 17-beta-estradiol-
independent manner (PubMed:9448000). Interacts with ESRRB isoform 1 (By
similarity). Interacts with UBE3A and WBP2 (By similarity). Interacts
with GTF2B (By similarity). Interacts with RBM39 (PubMed:11704680). In
the absence of hormonal ligand, interacts with TACC1 (By similarity).
{ECO:0000250|UniProtKB:P03372, ECO:0000269|PubMed:10207113,
ECO:0000269|PubMed:10788465, ECO:0000269|PubMed:10840033,
ECO:0000269|PubMed:11704680, ECO:0000269|PubMed:15988012,
ECO:0000269|PubMed:17595322, ECO:0000269|PubMed:20005806,
ECO:0000269|PubMed:7641693, ECO:0000269|PubMed:9192892,
ECO:0000269|PubMed:9448000}.
-!- INTERACTION:
Q15788:NCOA1 (xeno); NbExp=3; IntAct=EBI-346765, EBI-455189;
Q00175:Pgr; NbExp=5; IntAct=EBI-346765, EBI-346821;
O94763:URI1 (xeno); NbExp=2; IntAct=EBI-346765, EBI-357067;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane
{ECO:0000250}. Note=Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi
apparatus where most probably palmitoylation occurs. Associated with
the plasma membrane when palmitoylated. {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably
enhances transcriptional activity. Dephosphorylation at Ser-122 by
PPP5C inhibits its transactivation activity (By similarity).
Phosphorylated by LMTK3 (in vitro) (By similarity).
{ECO:0000250|UniProtKB:P03372}.
-!- PTM: Ubiquitinated. Deubiquitinated by OTUB1 (By similarity).
{ECO:0000250}.
-!- PTM: Palmitoylated at Cys-451 by ZDHHC7 and ZDHHC21. This modification
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}.
-!- PTM: Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1
proteasomal degradation. Deubiquitinated by OTUB1.
{ECO:0000250|UniProtKB:P03372}.
-!- PTM: Dimethylated by PRMT1 at Arg-264. The methylation may favor
cytoplasmic localization. Demethylated by JMJD6 at Arg-264.
{ECO:0000250|UniProtKB:P03372}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
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EMBL; M38651; AAA37580.1; -; mRNA.
EMBL; AK036627; BAC29510.1; -; mRNA.
EMBL; AK041525; BAC30973.1; -; mRNA.
EMBL; AJ276597; CAB85618.1; -; Genomic_DNA.
EMBL; AF128221; AAF22562.1; -; mRNA.
EMBL; AF128220; AAF22561.1; -; mRNA.
CCDS; CCDS56678.1; -.
PIR; A40061; QRMSE.
RefSeq; NP_001289460.1; NM_001302531.1.
RefSeq; NP_001289461.1; NM_001302532.1.
RefSeq; NP_031982.1; NM_007956.5.
RefSeq; XP_006512496.1; XM_006512433.3.
RefSeq; XP_006512497.1; XM_006512434.3.
RefSeq; XP_006512498.1; XM_006512435.2.
RefSeq; XP_011241368.1; XM_011243066.2.
RefSeq; XP_011241369.1; XM_011243067.2.
RefSeq; XP_011241370.1; XM_011243068.2.
SMR; P19785; -.
BioGrid; 199521; 28.
IntAct; P19785; 9.
MINT; P19785; -.
STRING; 10090.ENSMUSP00000070070; -.
BindingDB; P19785; -.
ChEMBL; CHEMBL3065; -.
DrugCentral; P19785; -.
GuidetoPHARMACOLOGY; 620; -.
GlyConnect; 145; -.
iPTMnet; P19785; -.
PhosphoSitePlus; P19785; -.
SwissPalm; P19785; -.
UniCarbKB; P19785; -.
PaxDb; P19785; -.
PRIDE; P19785; -.
DNASU; 13982; -.
Ensembl; ENSMUST00000067086; ENSMUSP00000070070; ENSMUSG00000019768.
Ensembl; ENSMUST00000105589; ENSMUSP00000101214; ENSMUSG00000019768.
Ensembl; ENSMUST00000105590; ENSMUSP00000101215; ENSMUSG00000019768.
GeneID; 13982; -.
KEGG; mmu:13982; -.
UCSC; uc007egu.3; mouse.
CTD; 2099; -.
MGI; MGI:1352467; Esr1.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00940000158133; -.
HOGENOM; CLU_007368_11_1_1; -.
InParanoid; P19785; -.
KO; K08550; -.
OMA; TMEPLHD; -.
OrthoDB; 487299at2759; -.
PhylomeDB; P19785; -.
TreeFam; TF323751; -.
Reactome; R-MMU-1251985; Nuclear signaling by ERBB4.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
Reactome; R-MMU-8931987; RUNX1 regulates estrogen receptor mediated transcription.
Reactome; R-MMU-8939211; ESR-mediated signaling.
Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
ChiTaRS; Esr1; mouse.
PRO; PR:P19785; -.
Proteomes; UP000000589; Chromosome 10.
RNAct; P19785; protein.
Bgee; ENSMUSG00000019768; Expressed in uterus and 218 other tissues.
ExpressionAtlas; P19785; baseline and differential.
Genevisible; P19785; MM.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043204; C:perikaryon; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0030315; C:T-tubule; ISO:MGI.
GO; GO:0043195; C:terminal bouton; ISO:MGI.
GO; GO:0097550; C:transcriptional preinitiation complex; ISO:MGI.
GO; GO:0035327; C:transcriptionally active chromatin; ISO:MGI.
GO; GO:0051117; F:ATPase binding; ISO:MGI.
GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0030284; F:estrogen receptor activity; ISO:MGI.
GO; GO:0030331; F:estrogen receptor binding; ISO:MGI.
GO; GO:0034056; F:estrogen response element binding; ISO:MGI.
GO; GO:0042562; F:hormone binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0004879; F:nuclear receptor activity; IDA:MGI.
GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; ISO:MGI.
GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
GO; GO:0003707; F:steroid hormone receptor activity; ISO:MGI.
GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
GO; GO:0001093; F:TFIIB-class transcription factor binding; ISO:MGI.
GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0031798; F:type 1 metabotropic glutamate receptor binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0008209; P:androgen metabolic process; IMP:MGI.
GO; GO:0001547; P:antral ovarian follicle growth; IMP:MGI.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
GO; GO:0071391; P:cellular response to estrogen stimulus; IMP:MGI.
GO; GO:0002064; P:epithelial cell development; IMP:MGI.
GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IMP:MGI.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISO:MGI.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:UniProtKB.
GO; GO:0008584; P:male gonad development; IMP:MGI.
GO; GO:0060749; P:mammary gland alveolus development; IMP:MGI.
GO; GO:0060745; P:mammary gland branching involved in pregnancy; IMP:MGI.
GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0046325; P:negative regulation of glucose import; ISO:MGI.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0045839; P:negative regulation of mitotic nuclear division; NAS:UniProtKB.
GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0090209; P:negative regulation of triglyceride metabolic process; ISO:MGI.
GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISS: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; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; IMP:MGI.
GO; GO:0060523; P:prostate epithelial cord elongation; IMP:MGI.
GO; GO:0071168; P:protein localization to chromatin; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IMP:MGI.
GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0032355; P:response to estradiol; ISO:MGI.
GO; GO:0043627; P:response to estrogen; ISO:MGI.
GO; GO:0060011; P:Sertoli cell proliferation; ISO:MGI.
GO; GO:0048863; P:stem cell differentiation; IDA:CAFA.
GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
GO; GO:0060065; P:uterus development; IGI:MGI.
GO; GO:0060068; P:vagina development; IGI:MGI.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR-like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR024178; Oest_rcpt/oest-rel_rcp.
InterPro; IPR001292; Oestr_rcpt.
InterPro; IPR024736; Oestrogen-typ_rcpt_final_C_dom.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF12743; ESR1_C; 1.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF02159; Oest_recep; 1.
Pfam; PF00105; zf-C4; 1.
PIRSF; PIRSF500101; ER-a; 1.
PIRSF; PIRSF002527; ER-like_NR; 1.
PRINTS; PR00543; OESTROGENR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
Activator; Cell membrane; Cytoplasm; DNA-binding; Glycoprotein;
Golgi apparatus; Lipid-binding; Lipoprotein; Membrane; Metal-binding;
Methylation; Nucleus; Palmitate; Phosphoprotein; Receptor;
Reference proteome; Steroid-binding; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1..599
/note="Estrogen receptor"
/id="PRO_0000053621"
DOMAIN 315..551
/note="NR LBD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
DNA_BIND 189..254
/note="Nuclear receptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 189..209
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 225..249
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
REGION 1..188
/note="Modulating (transactivation AF-1); mediates
interaction with MACROD1"
/evidence="ECO:0000250"
REGION 35..178
/note="Interaction with DDX5; self-association"
/evidence="ECO:0000250"
REGION 35..47
/note="Required for interaction with NCOA1"
/evidence="ECO:0000250"
REGION 189..314
/note="Mediates interaction with DNTTIP2"
/evidence="ECO:0000250"
REGION 255..314
/note="Hinge"
REGION 266..599
/note="Interaction with AKAP13"
/evidence="ECO:0000250"
REGION 268..599
/note="Self-association"
/evidence="ECO:0000250"
REGION 315..599
/note="Transactivation AF-2"
/evidence="ECO:0000250"
COMPBIAS 64..72
/note="Poly-Ala"
MOD_RES 108
/note="Phosphoserine; by CDK2"
/evidence="ECO:0000250|UniProtKB:P03372"
MOD_RES 110
/note="Phosphoserine; by CDK2"
/evidence="ECO:0000250|UniProtKB:P03372"
MOD_RES 122
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P03372"
MOD_RES 171
/note="Phosphoserine; by CK2"
/evidence="ECO:0000250|UniProtKB:P03372"
MOD_RES 264
/note="Asymmetric dimethylarginine; by PRMT1"
/evidence="ECO:0000250|UniProtKB:P03372"
MOD_RES 541
/note="Phosphotyrosine; by Tyr-kinases"
/evidence="ECO:0000250|UniProtKB:P03372"
LIPID 451
/note="S-palmitoyl cysteine"
/evidence="ECO:0000269|PubMed:22031296"
CARBOHYD 10
/note="O-linked (GlcNAc) serine"
/evidence="ECO:0000269|PubMed:11226831"
CARBOHYD 50
/note="O-linked (GlcNAc) threonine"
/evidence="ECO:0000269|PubMed:11226831"
CARBOHYD 575
/note="O-linked (GlcNAc) threonine"
/evidence="ECO:0000269|PubMed:11226831,
ECO:0000269|PubMed:8999954"
/id="CAR_000137"
VARIANT 591
/note="E -> Q (in strain: SJL/J)"
/evidence="ECO:0000269|Ref.4"
MUTAGEN 362
/note="I->A: No effect on transcriptional activity and
estrogen-induced interaction with NCOA1. Abolishes
estrogen-induced interaction with NCOA1; when associated
with A-376 and A-380."
/evidence="ECO:0000269|PubMed:10207113"
MUTAGEN 362
/note="I->D: Abolishes transcriptional activity and
estrogen-induced interaction with NCOA1."
/evidence="ECO:0000269|PubMed:10207113"
MUTAGEN 366
/note="K->A: Greatly reduces transcriptional activity and
estrogen-induced interaction with NCOA1."
/evidence="ECO:0000269|PubMed:10207113"
MUTAGEN 366
/note="K->D: Abolishes transcriptional activity and
estrogen-induced interaction with NCOA1."
/evidence="ECO:0000269|PubMed:10207113"
MUTAGEN 366
/note="K->L: Reduces transcriptional activity and estrogen-
induced interaction with NCOA1."
/evidence="ECO:0000269|PubMed:10207113"
MUTAGEN 371
/note="F->A: Abolishes estrogen-dependent NF-kappa B
transcriptional repression, impairs transcriptional
activity, abolishes estrogen-induced interaction with
NCOA1."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 376
/note="L->A: Reduces transcriptional activity, no effect on
estrogen-induced interaction with NCOA1. Abolishes
estrogen-induced interaction with NCOA1; when associated
with A-362 and A-380."
/evidence="ECO:0000269|PubMed:10207113"
MUTAGEN 376
/note="L->D: Reduces transcriptional activity and estrogen-
induced interaction with NCOA1."
/evidence="ECO:0000269|PubMed:10207113"
MUTAGEN 380
/note="V->A: No effect on transcriptional activity and
estrogen-induced interaction with NCOA1. Abolishes
estrogen-induced interaction with NCOA1; when associated
with A-362 and A-376."
/evidence="ECO:0000269|PubMed:10207113"
MUTAGEN 380
/note="V->D: Abolishes transcriptional activity and
estrogen-induced interaction with NCOA1."
/evidence="ECO:0000269|PubMed:10207113"
MUTAGEN 451
/note="C->A: Loss of ZDHHC7 and ZDHHC21 binding. Loss of
palmitoylation."
/evidence="ECO:0000269|PubMed:22031296"
MUTAGEN 508
/note="L->A: Reduces DNA-binding, attenuates
transcriptional activity, does not effect estrogen-
dependent NF-kappa B transcriptional repression; when
associated with E-512 and E-515."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 508
/note="L->E: Abolishes DNA-binding, abolishes
transcriptional activity and estrogen-dependent NF-kappa B
transcriptional repression; when associated with E-512 and
E-515."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 509
/note="A->E: Reduces DNA-binding,, attenuates
transcriptional activity, does not effect estrogen-
dependent NF-kappa B transcriptional repression."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 512
/note="L->A: Reduces DNA-binding, attenuates
transcriptional activity, does not effect estrogen-
dependent NF-kappa B transcriptional repression; when
associated with E-508 and E-515."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 512
/note="L->E: Abolishes DNA-binding, abolishes
transcriptional activity and estrogen-dependent NF-kappa B
transcriptional repression; when associated with E-508 and
E-515."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 515
/note="L->A: Reduces DNA-binding, attenuates
transcriptional activity, does not effect estrogen-
dependent NF-kappa B transcriptional repression; when
associated with E-508 and E-512."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 515
/note="L->E: Abolishes DNA-binding, abolishes
transcriptional activity and estrogen-dependent NF-kappa B
transcriptional repression; when associated with E-508 and
E-512."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 525
/note="G->R: Abolishes estrogen binding; impairs repression
of NF-kappa activity."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 542
/note="D->N: Abolishes estrogen-dependent NF-kappa B
transcriptional repression, impairs transcriptional
activity, impairs estrogen-induced interaction with NCOA1;
when associated with Q-546 and N-548."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 543..544
/note="LL->AA: Abolishes estrogen-dependent NF-kappa B
transcriptional repression, abolishes estrogen-induced
interaction with NCOA1."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 543
/note="L->A: Abolishes estrogen-induced interaction with
NCOA1."
/evidence="ECO:0000269|PubMed:10207113"
MUTAGEN 546
/note="E->Q: Abolishes estrogen-dependent NF-kappa B
transcriptional repression, impairs transcriptional
activity, impairs estrogen-induced interaction with NCOA1;
when associated with N-542 and N-548."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 547..548
/note="ML->AA: No effect on estrogen-dependent NF-kappa B
transcriptional repression, greatly impairs transcriptional
activity, abolishes estrogen-induced interaction with
NCOA1."
/evidence="ECO:0000269|PubMed:10840033"
MUTAGEN 549
/note="D->N: Abolishes estrogen-dependent NF-kappa B
transcriptional repression, impairs transcriptional
activity, impairs estrogen-induced interaction with NCOA1;
when associated with N-542 and Q-546."
/evidence="ECO:0000269|PubMed:10840033"
CONFLICT 269
/note="L -> M (in Ref. 4; AAF22561)"
/evidence="ECO:0000305"
SEQUENCE 599 AA; 66955 MW; 05F5E2FC21CC0A8B CRC64;
MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKMPMERALG EVYVDNSKPT VFNYPEGAAY
EFNAAAAAAA AASAPVYGQS GIAYGPGSEA AAFSANSLGA FPQLNSVSPS PLMLLHPPPQ
LSPFLHPHGQ QVPYYLENEP SAYAVRDTGP PAFYRSNSDN RRQNGRERLS SSNEKGNMIM
ESAKETRYCA VCNDYASGYH YGVWSCEGCK AFFKRSIQGH NDYMCPATNQ CTIDKNRRKS
CQACRLRKCY EVGMMKGGIR KDRRGGRMLK HKRQRDDLEG RNEMGASGDM RAANLWPSPL
VIKHTKKNSP ALSLTADQMV SALLDAEPPM IYSEYDPSRP FSEASMMGLL TNLADRELVH
MINWAKRVPG FGDLNLHDQV HLLECAWLEI LMIGLVWRSM EHPGKLLFAP NLLLDRNQGK
CVEGMVEIFD MLLATSSRFR MMNLQGEEFV CLKSIILLNS GVYTFLSSTL KSLEEKDHIH
RVLDKITDTL IHLMAKAGLT LQQQHRRLAQ LLLILSHIRH MSNKGMEHLY NMKCKNVVPL
YDLLLEMLDA HRLHAPASRM GVPPEEPSQT QLATTSSTSA HSLQTYYIPP EAEGFPNTI


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Related Genes :
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[Esr1 Esr Estr Estra Nr3a1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[Esr1 Esr Estr Nr3a1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (Fragment)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR2 ESTRB NR3A2] Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)
[Esr2 Erbeta Nr3a2] Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)
[Esr2 Estrb Nr3a2] Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (Fragment)
[ESRRA ERR1 ESRL1 NR3B1] Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[Esrra Err1 Estrra Nr3b1] Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[Esrra Nr3b1] Steroid hormone receptor ERR1 (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[Esrrb Err-2 Err2 Nr3b2] Steroid hormone receptor ERR2 (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2)
[ESRRB ERRB2 ESRL2 NR3B2] Steroid hormone receptor ERR2 (ERR beta-2) (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2)
[Esrrg Err3 Kiaa0832 Nr3b3] Estrogen-related receptor gamma (Estrogen receptor-related protein 3) (Nuclear receptor subfamily 3 group B member 3)
[Esrrb Err2 Esrl2 Nr3b2] Steroid hormone receptor ERR2 (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2)
[NR5A2 B1F CPF FTF] Nuclear receptor subfamily 5 group A member 2 (Alpha-1-fetoprotein transcription factor) (B1-binding factor) (hB1F) (CYP7A promoter-binding factor) (Hepatocytic transcription factor) (Liver receptor homolog 1) (LRH-1)
[AR DHTR NR3C4] Androgen receptor (Dihydrotestosterone receptor) (Nuclear receptor subfamily 3 group C member 4)
[NR1D2] Nuclear receptor subfamily 1 group D member 2 (Orphan nuclear hormone receptor BD73) (Rev-erb alpha-related receptor) (RVR) (Rev-erb-beta) (V-erbA-related protein 1-related) (EAR-1R)
[THRA EAR7 ERBA1 NR1A1 THRA1 THRA2] Thyroid hormone receptor alpha (Nuclear receptor subfamily 1 group A member 1) (V-erbA-related protein 7) (EAR-7) (c-erbA-1) (c-erbA-alpha)
[RARA NR1B1] Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[Rara Nr1b1] Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1)
[ftz-f1 NR5A3 CG4059] Nuclear hormone receptor FTZ-F1 (FTZ-F1 alpha) (Nuclear receptor subfamily 5 group A member 3)

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[28087261] DNA aptamer probes for detection of estrogen receptor α positive carcinomas.
[26573009] Macromolecular Modelling and Docking Simulations for the Discovery of Selective GPER Ligands.
[25943116] Estrogen-Induced Cholestasis Leads to Repressed CYP2D6 Expression in CYP2D6-Humanized Mice.
[25769926] Estradiol inhibits Th17 cell differentiation through inhibition of RORγT transcription by recruiting the ERα/REA complex to estrogen response elements of the RORγT promoter.
[25675114] Estrogen and Estrogen Receptor-α-Mediated Transrepression of Bile Salt Export Pump.
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