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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.
25-APR-2018, entry version 212.
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;
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;
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 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).
[15]
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).
[16]
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).
[17]
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 nad WBP2 (By similarity).
{ECO:0000250|UniProtKB:P03372, ECO:0000269|PubMed:10207113,
ECO:0000269|PubMed:10788465, ECO:0000269|PubMed:10840033,
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=2; 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: Dimethylated by PRMT1 at Arg-264. The methylation may favor
cytoplasmic localization (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}.
-!- 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.
UniGene; Mm.463262; -.
UniGene; Mm.489063; -.
UniGene; Mm.9213; -.
ProteinModelPortal; P19785; -.
SMR; P19785; -.
BioGrid; 199521; 25.
IntAct; P19785; 8.
MINT; P19785; -.
STRING; 10090.ENSMUSP00000070070; -.
BindingDB; P19785; -.
ChEMBL; CHEMBL3065; -.
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; ENSGT00760000118887; -.
HOGENOM; HOG000233468; -.
HOVERGEN; HBG108344; -.
InParanoid; P19785; -.
KO; K08550; -.
OMA; EAGPPAF; -.
OrthoDB; EOG091G03V4; -.
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-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.
ChiTaRS; Esr1; mouse.
PRO; PR:P19785; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000019768; -.
CleanEx; MM_ESR1; -.
ExpressionAtlas; P19785; baseline and differential.
Genevisible; P19785; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; 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:0001046; F:core promoter sequence-specific DNA binding; 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:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0004879; F:nuclear receptor activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0038052; F:RNA polymerase II transcription factor activity, estrogen-activated 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: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:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA 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:0016049; P:cell growth; NAS:UniProtKB.
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: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:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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: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: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: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; 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; 2.
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; Complete proteome; 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 Estrogen receptor.
/FTId=PRO_0000053621.
DOMAIN 315 551 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 189 254 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 189 209 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 225 249 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 188 Modulating (transactivation AF-1);
mediates interaction with MACROD1.
{ECO:0000250}.
REGION 35 178 Interaction with DDX5; self-association.
{ECO:0000250}.
REGION 35 47 Required for interaction with NCOA1.
{ECO:0000250}.
REGION 189 314 Mediates interaction with DNTTIP2.
{ECO:0000250}.
REGION 255 314 Hinge.
REGION 266 599 Interaction with AKAP13. {ECO:0000250}.
REGION 268 599 Self-association. {ECO:0000250}.
REGION 315 599 Transactivation AF-2. {ECO:0000250}.
COMPBIAS 64 72 Poly-Ala.
MOD_RES 108 108 Phosphoserine; by CDK2.
{ECO:0000250|UniProtKB:P03372}.
MOD_RES 110 110 Phosphoserine; by CDK2.
{ECO:0000250|UniProtKB:P03372}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000250|UniProtKB:P03372}.
MOD_RES 171 171 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P03372}.
MOD_RES 264 264 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000250|UniProtKB:P03372}.
MOD_RES 541 541 Phosphotyrosine; by Tyr-kinases.
{ECO:0000250|UniProtKB:P03372}.
LIPID 451 451 S-palmitoyl cysteine.
{ECO:0000269|PubMed:22031296}.
CARBOHYD 10 10 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:11226831}.
CARBOHYD 50 50 O-linked (GlcNAc) threonine.
{ECO:0000269|PubMed:11226831}.
CARBOHYD 575 575 O-linked (GlcNAc) threonine.
{ECO:0000269|PubMed:11226831,
ECO:0000269|PubMed:8999954}.
/FTId=CAR_000137.
VARIANT 591 591 E -> Q (in strain: SJL/J).
{ECO:0000269|Ref.4}.
MUTAGEN 362 362 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.
{ECO:0000269|PubMed:10207113}.
MUTAGEN 362 362 I->D: Abolishes transcriptional activity
and estrogen-induced interaction with
NCOA1. {ECO:0000269|PubMed:10207113}.
MUTAGEN 366 366 K->A: Greatly reduces transcriptional
activity and estrogen-induced interaction
with NCOA1.
{ECO:0000269|PubMed:10207113}.
MUTAGEN 366 366 K->D: Abolishes transcriptional activity
and estrogen-induced interaction with
NCOA1. {ECO:0000269|PubMed:10207113}.
MUTAGEN 366 366 K->L: Reduces transcriptional activity
and estrogen-induced interaction with
NCOA1. {ECO:0000269|PubMed:10207113}.
MUTAGEN 371 371 F->A: Abolishes estrogen-dependent NF-
kappa B transcriptional repression,
impairs transcriptional activity,
abolishes estrogen-induced interaction
with NCOA1.
{ECO:0000269|PubMed:10840033}.
MUTAGEN 376 376 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.
{ECO:0000269|PubMed:10207113}.
MUTAGEN 376 376 L->D: Reduces transcriptional activity
and estrogen-induced interaction with
NCOA1. {ECO:0000269|PubMed:10207113}.
MUTAGEN 380 380 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.
{ECO:0000269|PubMed:10207113}.
MUTAGEN 380 380 V->D: Abolishes transcriptional activity
and estrogen-induced interaction with
NCOA1. {ECO:0000269|PubMed:10207113}.
MUTAGEN 451 451 C->A: Loss of ZDHHC7 and ZDHHC21 binding.
Loss of palmitoylation.
{ECO:0000269|PubMed:22031296}.
MUTAGEN 508 508 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.
{ECO:0000269|PubMed:10840033}.
MUTAGEN 508 508 L->E: Abolishes DNA-binding, abolishes
transcriptional activity and estrogen-
dependent NF-kappa B transcriptional
repression; when associated with E-512
and E-515. {ECO:0000269|PubMed:10840033}.
MUTAGEN 509 509 A->E: Reduces DNA-binding,, attenuates
transcriptional activity, does not effect
estrogen-dependent NF-kappa B
transcriptional repression.
{ECO:0000269|PubMed:10840033}.
MUTAGEN 512 512 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.
{ECO:0000269|PubMed:10840033}.
MUTAGEN 512 512 L->E: Abolishes DNA-binding, abolishes
transcriptional activity and estrogen-
dependent NF-kappa B transcriptional
repression; when associated with E-508
and E-515. {ECO:0000269|PubMed:10840033}.
MUTAGEN 515 515 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.
{ECO:0000269|PubMed:10840033}.
MUTAGEN 515 515 L->E: Abolishes DNA-binding, abolishes
transcriptional activity and estrogen-
dependent NF-kappa B transcriptional
repression; when associated with E-508
and E-512. {ECO:0000269|PubMed:10840033}.
MUTAGEN 525 525 G->R: Abolishes estrogen binding; impairs
repression of NF-kappa activity.
{ECO:0000269|PubMed:10840033}.
MUTAGEN 542 542 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.
{ECO:0000269|PubMed:10840033}.
MUTAGEN 543 544 LL->AA: Abolishes estrogen-dependent NF-
kappa B transcriptional repression,
abolishes estrogen-induced interaction
with NCOA1.
{ECO:0000269|PubMed:10840033}.
MUTAGEN 543 543 L->A: Abolishes estrogen-induced
interaction with NCOA1.
{ECO:0000269|PubMed:10207113}.
MUTAGEN 546 546 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.
{ECO:0000269|PubMed:10840033}.
MUTAGEN 547 548 ML->AA: No effect on estrogen-dependent
NF-kappa B transcriptional repression,
greatly impairs transcriptional activity,
abolishes estrogen-induced interaction
with NCOA1.
{ECO:0000269|PubMed:10840033}.
MUTAGEN 549 549 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.
{ECO:0000269|PubMed:10840033}.
CONFLICT 269 269 L -> M (in Ref. 4; AAF22561).
{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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