ID ESR1_RAT Reviewed; 600 AA. AC P06211; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 04-NOV-2026, entry version 231. DE RecName: Full=Estrogen receptor; DE Short=ER; DE AltName: Full=ER-alpha; DE AltName: Full=Estradiol receptor; DE AltName: Full=Nuclear receptor subfamily 3 group A member 1; GN Name=Esr1; Synonyms=Esr, Estr, Nr3a1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; RA Muramatsu M.; RL Submitted (MAR-1987) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3031601; DOI=10.1093/nar/15.6.2499; RA Koike S., Sakai M.; RT "Molecular cloning and characterization of rat estrogen receptor cDNA."; RL Nucleic Acids Res. 15:2499-2513(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Uterus; RA Maggi A.M.A.; RL Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases. RN [4] RP INTERACTION WITH UBE1C. RX PubMed=11818503; DOI=10.1210/mend.16.2.0778; RA Fan M., Long X., Bailey J.A., Reed C.A., Osborne E., Gize E.A., Kirk E.A., RA Bigsby R.M., Nephew K.P.; RT "The activating enzyme of NEDD8 inhibits steroid receptor function."; RL Mol. Endocrinol. 16:315-330(2002). RN [5] RP INTERACTION WITH MAP1S. RX PubMed=17658481; DOI=10.1016/j.bbrc.2007.06.179; RA Eriksson M., Samuelsson H., Samuelsson E.-B., Liu L., McKeehan W.L., RA Benedikz E., Sundstroem E.; RT "The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in RT the brain."; RL Biochem. Biophys. Res. Commun. 361:127-132(2007). RN [6] RP INTERACTION WITH DNAAF4. RX PubMed=19423554; DOI=10.1093/hmg/ddp215; RA Massinen S., Tammimies K., Tapia-Paez I., Matsson H., Hokkanen M.E., RA Soederberg O., Landegren U., Castren E., Gustafsson J.A., Treuter E., RA Kere J.; RT "Functional interaction of DYX1C1 with estrogen receptors suggests RT involvement of hormonal pathways in dyslexia."; RL Hum. Mol. Genet. 18:2802-2812(2009). RN [7] RP FUNCTION, INTERACTION WITH BAG1; NEDD8 AND STUB1, TISSUE SPECIFICITY, AND RP UBIQUITINATION. RX PubMed=21808025; DOI=10.1073/pnas.1104391108; RA Zhang Q.G., Han D., Wang R.M., Dong Y., Yang F., Vadlamudi R.K., RA Brann D.W.; RT "C terminus of Hsc70-interacting protein (CHIP)-mediated degradation of RT hippocampal estrogen receptor-alpha and the critical period hypothesis of RT estrogen neuroprotection."; RL Proc. Natl. Acad. Sci. U.S.A. 108:E617-E624(2011). CC -!- FUNCTION: Nuclear hormone receptor. The steroid hormones and their CC receptors are involved in the regulation of eukaryotic gene expression CC and affect cellular proliferation and differentiation in target CC tissues. Ligand-dependent nuclear transactivation involves either CC direct homodimer binding to a palindromic estrogen response element CC (ERE) sequence or association with other DNA-binding transcription CC factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE- CC independent signaling. Ligand binding induces a conformational change CC allowing subsequent or combinatorial association with multiprotein CC coactivator complexes through LXXLL motifs of their respective CC components. Mutual transrepression occurs between the estrogen receptor CC (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa- CC B DNA-binding activity and inhibits NF-kappa-B-mediated transcription CC from the IL6 promoter and displace RELA/p65 and associated coregulators CC from the promoter. Recruited to the NF-kappa-B response element of the CC CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B CC components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act CC synergistically with NF-kappa-B to activate transcription involving CC respective recruitment adjacent response elements; the function CC involves CREBBP. Can activate the transcriptional activity of TFF1. CC Also mediates membrane-initiated estrogen signaling involving various CC kinase cascades. Essential for MTA1-mediated transcriptional regulation CC of BRCA1 and BCAS3 (By similarity). Maintains neuronal survival in CC response to ischemic reperfusion injury when in the presence of CC circulating estradiol (17-beta-estradiol/E2) (PubMed:21808025). CC {ECO:0000250, ECO:0000269|PubMed:21808025}. CC -!- SUBUNIT: Interacts with BCAS3. Binds DNA as a homodimer (By CC similarity). Can form a heterodimer with ESR2 (By similarity). CC Interacts with coactivator NCOA5. Interacts with PELP1, the interaction CC is enhanced by 17-beta-estradiol; the interaction increases ESR1 CC transcriptional activity (By similarity). Interacts with NCOA7; the CC interaction is ligand-inducible. Interacts with AKAP13, CUEDC2, HEXIM1, CC KDM5A, MAP1S, SMARD1, and UBE1C. Interacts with MUC1; the interaction CC is stimulated by 7 beta-estradiol (E2) and enhances ESR1-mediated CC transcription. Interacts with DNTTIP2, and UIMC1. Interacts with CC KMT2D/MLL2. Interacts with ATAD2; the interaction is enhanced by CC estradiol. Interacts with KIF18A and LDB1. Interacts with RLIM (via its CC C-terminus). Interacts with MACROD1. Interacts with SH2D4A and PLCG. CC Interacts with SH2D4A; the interaction blocks binding to PLCG and CC inhibits estrogen-induced cell proliferation. Interacts with DYNLL1. CC Interacts with CCDC62; the interaction requires estradiol and appears CC to enhance the transcription of target genes. Interacts with NR2C1; the CC interaction prevents homodimerization of ESR1 and suppresses its CC transcriptional activity and cell growth. Interacts with DNAAF4. CC Interacts with PRMT2. Interacts with RBFOX2. Interacts with EP300; the CC interaction is estrogen-dependent and enhanced by CITED1. Interacts CC with CITED1; the interaction is estrogen-dependent (By similarity). CC Interacts with FAM120B, FOXL2, PHB2 and SLC30A9. Interacts with CC coactivators NCOA3 and NCOA6. Interacts with STK3/MST2 only in the CC presence of SAV1 and vice-versa. Interacts with NCOA2; NCOA2 can CC interact with ESR1 AF-1 and AF-2 domains simultaneously and mediate CC their transcriptional synergy. Interacts with DDX5. Interacts with CC NCOA1; the interaction seems to require a self-association of N- CC terminal and C-terminal regions. Interacts with ZNF366, DDX17, NFKB1, CC RELA, SP1 and SP3. Interacts with NRIP1 (By similarity). Interacts with CC GPER1; the interaction occurs in an estrogen-dependent manner (By CC similarity). Interacts with TRIP4 (ufmylated); estrogen dependent (By CC similarity). Interacts with LMTK3; the interaction phosphorylates ESR1 CC (in vitro) and protects it against proteasomal degradation. Interacts CC with CCAR2 (via N-terminus) in a ligand-independent manner. Interacts CC with ZFHX3 (By similarity). Interacts with SFR1 in a ligand-dependent CC and -independent manner (By similarity). Interacts with DCAF13, LATS1 CC and DCAF1; regulates ESR1 ubiquitination and ubiquitin-mediated CC proteasomal degradation. Interacts (via DNA-binding domain) with POU4F2 CC (C-terminus); this interaction increases the estrogen receptor ESR1 CC transcriptional activity in a DNA- and ligand 17-beta-estradiol- CC independent manner (By similarity). Interacts with ESRRB isoform 1 (By CC similarity). Interacts with UBE3A and WBP2 (By similarity). Interacts CC with GTF2B (By similarity). Interacts with RBM39 (By similarity). In CC the absence of hormonal ligand, interacts with TACC1 (By similarity). CC Interacts with PI3KR1 or PI3KR2 and PTK2/FAK1 (By similarity). CC Interacts with SRC (By similarity). Interacts with BAG1; the CC interaction is promoted in the absence of estradiol (17-beta- CC estradiol/E2) (PubMed:21808025). Interacts with and ubiquitinated by CC STUB1; the interaction is promoted in the absence of estradiol (17- CC beta-estradiol/E2) (PubMed:21808025). Interacts with NEDD8 CC (PubMed:21808025). {ECO:0000250|UniProtKB:P03372, CC ECO:0000250|UniProtKB:P19785, ECO:0000269|PubMed:17658481, CC ECO:0000269|PubMed:19423554, ECO:0000269|PubMed:21808025}. CC -!- INTERACTION: CC P06211; P50503: St13; NbExp=4; IntAct=EBI-7983651, EBI-917694; CC P06211; P62989: Ubb; NbExp=5; IntAct=EBI-7983651, EBI-7038538; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. CC Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane CC {ECO:0000250}. Note=Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi CC apparatus where most probably palmitoylation occurs. Associated with CC the plasma membrane when palmitoylated. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in the CA1 region of the hippocampus, CC expression decreases with age (at protein level) (PubMed:21808025). CC Expressed in the uterus (at protein level) (PubMed:21808025). CC {ECO:0000269|PubMed:21808025}. CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a CC DNA-binding domain and a C-terminal ligand-binding domain. The CC modulating domain, also known as A/B or AF-1 domain has a ligand- CC independent transactivation function. The C-terminus contains a ligand- CC dependent transactivation domain, also known as E/F or AF-2 domain CC which overlaps with the ligand binding domain. AF-1 and AF-2 activate CC transcription independently and synergistically and act in a CC promoter- and cell-specific manner (By similarity). {ECO:0000250}. CC -!- PTM: Phosphorylated by cyclin A/CDK2 and. Dephosphorylation at Ser-123 CC by PPP5C inhibits its transactivation activity (By similarity). CC Phosphorylated by LMTK3 (in vitro) (By similarity). CC {ECO:0000250|UniProtKB:P03372}. CC -!- PTM: Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1 CC proteasomal degradation (By similarity). Deubiquitinated by OTUB1 (By CC similarity). Ubiquitinated by STUB1/CHIP; in the CA1 hippocampal region CC following loss of endogenous circulating estradiol (17-beta- CC estradiol/E2) (PubMed:21808025). Ubiquitinated by UBR5, leading to its CC degradation: UBR5 specifically recognizes and binds ligand-bound ESR1 CC when it is not associated with coactivators (NCOAs) (By similarity). In CC presence of NCOAs, the UBR5-degron is not accessible, preventing its CC ubiquitination and degradation (By similarity). CC {ECO:0000250|UniProtKB:P03372, ECO:0000269|PubMed:21808025}. CC -!- PTM: Palmitoylated at Cys-452 by ZDHHC7 and ZDHHC21. This modification CC is required for plasma membrane targeting and for rapid intracellular CC signaling via ERK and AKT kinases and cAMP generation, but not for CC signaling mediated by the nuclear hormone receptor (By similarity). CC {ECO:0000250}. CC -!- PTM: Dimethylated by PRMT1 at Arg-265. The methylation may favor CC cytoplasmic localization. Demethylated by JMJD6 at Arg-265. CC {ECO:0000250|UniProtKB:P03372}. CC -!- MISCELLANEOUS: In the absence of ligand, steroid hormone receptors are CC thought to be weakly associated with nuclear components; hormone CC binding greatly increases receptor affinity. The hormone-receptor CC complex appears to recognize discrete DNA sequences upstream of CC transcriptional start sites. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y00102; CAA68287.1; -; mRNA. DR EMBL; X61098; CAA43411.1; -; mRNA. DR PIR; S07379; QRRTE. DR RefSeq; NP_036821.2; NM_012689.2. DR AlphaFoldDB; P06211; -. DR SMR; P06211; -. DR BioGRID; 247000; 11. DR CORUM; P06211; -. DR DIP; DIP-41279N; -. DR FunCoup; P06211; 466. DR IntAct; P06211; 6. DR STRING; 10116.ENSRNOP00000026350; -. DR BindingDB; P06211; -. DR ChEMBL; CHEMBL2724; -. DR DrugCentral; P06211; -. DR GuidetoPHARMACOLOGY; 620; -. DR GlyCosmos; P06211; 2 sites, No reported glycans. DR GlyGen; P06211; 2 sites. DR iPTMnet; P06211; -. DR PhosphoSitePlus; P06211; -. DR SwissPalm; P06211; -. DR PaxDb; 10116-ENSRNOP00000026350; -. DR GeneID; 24890; -. DR KEGG; rno:24890; -. DR UCSC; RGD:2581; rat. DR AGR; RGD:2581; -. DR CTD; 2099; -. DR RGD; 2581; Esr1. DR eggNOG; KOG3575; Eukaryota. DR InParanoid; P06211; -. DR OrthoDB; 5799427at2759; -. DR PhylomeDB; P06211; -. DR Reactome; R-RNO-1251985; Nuclear signaling by ERBB4. DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling. DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway. DR Reactome; R-RNO-4090294; SUMOylation of intracellular receptors. DR Reactome; R-RNO-5689896; Ovarian tumor domain proteases. DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-RNO-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors. DR Reactome; R-RNO-8931987; RUNX1 regulates estrogen receptor mediated transcription. DR Reactome; R-RNO-8939211; ESR-mediated signaling. DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling. DR Reactome; R-RNO-9018519; Estrogen-dependent gene expression. DR Reactome; R-RNO-9841251; Mitochondrial unfolded protein response (UPRmt). DR PRO; PR:P06211; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0000785; C:chromatin; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0000791; C:euchromatin; ISO:RGD. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043204; C:perikaryon; IDA:RGD. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:0030315; C:T-tubule; IDA:RGD. DR GO; GO:0043195; C:terminal bouton; IDA:RGD. DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD. DR GO; GO:0071889; F:14-3-3 protein binding; ISO:RGD. DR GO; GO:0051117; F:ATPase binding; ISO:RGD. DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD. DR GO; GO:0005516; F:calmodulin binding; ISO:RGD. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IMP:RGD. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD. DR GO; GO:0019899; F:enzyme binding; IPI:RGD. DR GO; GO:0099130; F:estrogen binding; IDA:RGD. DR GO; GO:0034056; F:estrogen response element binding; ISO:RGD. DR GO; GO:0042562; F:hormone binding; IDA:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0030284; F:nuclear estrogen receptor activity; ISO:RGD. DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:RGD. DR GO; GO:0004879; F:nuclear receptor activity; ISO:RGD. DR GO; GO:0003707; F:nuclear steroid receptor activity; IDA:RGD. DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IPI:RGD. DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:RGD. DR GO; GO:0019901; F:protein kinase binding; ISO:RGD. DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD. DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD. DR GO; GO:0005496; F:steroid binding; IDA:UniProtKB. DR GO; GO:0017025; F:TBP-class protein binding; ISO:RGD. DR GO; GO:0001093; F:TFIIB-class transcription factor binding; ISO:RGD. DR GO; GO:0001223; F:transcription coactivator binding; IPI:RGD. DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD. DR GO; GO:0001222; F:transcription corepressor binding; ISO:RGD. DR GO; GO:0031798; F:type 1 metabotropic glutamate receptor binding; IPI:RGD. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0008209; P:androgen metabolic process; ISO:RGD. DR GO; GO:0001547; P:antral ovarian follicle growth; ISO:RGD. DR GO; GO:1990375; P:baculum development; IEP:RGD. DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB. DR GO; GO:0071391; P:cellular response to estrogen stimulus; IEP:RGD. DR GO; GO:1904568; P:cellular response to wortmannin; IEP:RGD. DR GO; GO:0046697; P:decidualization; IEP:RGD. DR GO; GO:0002064; P:epithelial cell development; ISO:RGD. DR GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; ISO:RGD. DR GO; GO:0030520; P:estrogen receptor signaling pathway; ISO:RGD. DR GO; GO:0008584; P:male gonad development; IEP:RGD. DR GO; GO:0060749; P:mammary gland alveolus development; ISO:RGD. DR GO; GO:0060745; P:mammary gland branching involved in pregnancy; ISO:RGD. DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB. DR GO; GO:0046325; P:negative regulation of D-glucose import across plasma membrane; IDA:RGD. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD. DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:RGD. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD. DR GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; IMP:UniProtKB. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0090209; P:negative regulation of triglyceride metabolic process; IDA:RGD. DR GO; GO:0030518; P:nuclear receptor-mediated steroid hormone signaling pathway; IDA:UniProtKB. DR GO; GO:0002076; P:osteoblast development; IEP:RGD. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:RGD. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:RGD. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:RGD. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB. DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; ISO:RGD. DR GO; GO:0060523; P:prostate epithelial cord elongation; ISO:RGD. DR GO; GO:0071168; P:protein localization to chromatin; ISO:RGD. DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD. DR GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; ISO:RGD. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD. DR GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; ISO:RGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0032355; P:response to estradiol; IEP:RGD. DR GO; GO:0043627; P:response to estrogen; ISO:RGD. DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; ISO:RGD. DR GO; GO:0060009; P:Sertoli cell development; IEP:RGD. DR GO; GO:0060011; P:Sertoli cell proliferation; IMP:RGD. DR GO; GO:0048863; P:stem cell differentiation; ISO:RGD. DR GO; GO:0043401; P:steroid hormone receptor signaling pathway; ISO:RGD. DR GO; GO:0060065; P:uterus development; ISO:RGD. DR GO; GO:0060068; P:vagina development; ISO:RGD. DR CDD; cd07171; NR_DBD_ER; 1. DR CDD; cd06949; NR_LBD_ER; 1. DR FunFam; 1.10.565.10:FF:000010; Estrogen receptor; 1. DR FunFam; 3.30.50.10:FF:000014; Estrogen receptor beta; 1. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1. DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1. DR InterPro; IPR024178; Est_rcpt/est-rel_rcp. DR InterPro; IPR001292; Estr_rcpt. DR InterPro; IPR046944; Estr_rcpt_N. DR InterPro; IPR035500; NHR-like_dom_sf. DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd. DR InterPro; IPR050200; Nuclear_hormone_rcpt_NR3. DR InterPro; IPR001723; Nuclear_hrmn_rcpt. DR InterPro; IPR024736; Oestrogen-typ_rcpt_final_C_dom. DR InterPro; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. DR PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1. DR Pfam; PF12743; ESR1_C; 1. DR Pfam; PF00104; Hormone_recep; 1. DR Pfam; PF02159; Oest_recep; 1. DR Pfam; PF00105; zf-C4; 1. DR PIRSF; PIRSF500101; ER-a; 1. DR PIRSF; PIRSF002527; ER-like_NR; 1. DR PRINTS; PR00543; OESTROGENR. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1. DR PROSITE; PS51843; NR_LBD; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. PE 1: Evidence at protein level; KW Activator; Cell membrane; Cytoplasm; DNA-binding; Glycoprotein; KW Golgi apparatus; Lipid-binding; Lipoprotein; Membrane; Metal-binding; KW Methylation; Nucleus; Palmitate; Phosphoprotein; Receptor; KW Reference proteome; Steroid-binding; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..600 FT /note="Estrogen receptor" FT /id="PRO_0000053623" FT DOMAIN 316..552 FT /note="NR LBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189" FT DNA_BIND 190..255 FT /note="Nuclear receptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 190..210 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 226..250 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT REGION 1..189 FT /note="Modulating (transactivation AF-1); mediates FT interaction with MACROD1" FT /evidence="ECO:0000250" FT REGION 35..179 FT /note="Interaction with DDX5; self-association" FT /evidence="ECO:0000250" FT REGION 35..47 FT /note="Required for interaction with NCOA1" FT /evidence="ECO:0000250" FT REGION 148..177 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 190..315 FT /note="Mediates interaction with DNTTIP2" FT /evidence="ECO:0000250" FT REGION 256..315 FT /note="Hinge" FT REGION 267..600 FT /note="Interaction with AKAP13" FT /evidence="ECO:0000250" FT REGION 269..600 FT /note="Self-association" FT /evidence="ECO:0000250" FT REGION 316..600 FT /note="Transactivation AF-2" FT /evidence="ECO:0000250" FT REGION 558..581 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 159..170 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 569..581 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 358 FT /ligand="17beta-estradiol" FT /ligand_id="ChEBI:CHEBI:16469" FT /evidence="ECO:0000250|UniProtKB:P03372" FT BINDING 399 FT /ligand="17beta-estradiol" FT /ligand_id="ChEBI:CHEBI:16469" FT /evidence="ECO:0000250|UniProtKB:P03372" FT BINDING 529 FT /ligand="17beta-estradiol" FT /ligand_id="ChEBI:CHEBI:16469" FT /evidence="ECO:0000250|UniProtKB:P03372" FT MOD_RES 109 FT /note="Phosphoserine; by CDK2" FT /evidence="ECO:0000250|UniProtKB:P03372" FT MOD_RES 111 FT /note="Phosphoserine; by CDK2" FT /evidence="ECO:0000250|UniProtKB:P03372" FT MOD_RES 123 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P03372" FT MOD_RES 172 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000250|UniProtKB:P03372" FT MOD_RES 265 FT /note="Asymmetric dimethylarginine; by PRMT1" FT /evidence="ECO:0000250|UniProtKB:P03372" FT MOD_RES 542 FT /note="Phosphotyrosine; by Tyr-kinases" FT /evidence="ECO:0000250|UniProtKB:P03372" FT LIPID 452 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CARBOHYD 10 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT CARBOHYD 576 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000250" FT CONFLICT 488 FT /note="N -> T (in Ref. 3; CAA43411)" FT /evidence="ECO:0000305" SQ SEQUENCE 600 AA; 67030 MW; C9C7D8CACE0F57D8 CRC64; MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKMPMERALG EVYVDNSKPA VFNYPEGAAY EFNAAAAAAA AGASAPVYGQ SSITYGPGSE AAAFGANSLG AFPQLNSVSP SPLMLLHPPP HVSPFLHPHG HQVPYYLENE PSAYAVRDTG PPAFYRSNSD NRRQNGRERL SSSSEKGNMI MESAKETRYC AVCNDYASGY HYGVWSCEGC KAFFKRSIQG HNDYMCPATN QCTIDKNRRK SCQACRLRKC YEVGMMKGGI RKDRRGGRML KHKRQRDDLE GRNEMGTSGD MRAANLWPSP LVIKHTKKNS PALSLTADQM VSALLDAEPP LIYSEYDPSR PFSEASMMGL LTNLADRELV HMINWAKRVP GFGDLNLHDQ VHLLECAWLE ILMIGLVWRS MEHPGKLLFA PNLLLDRNQG KCVEGMVEIF DMLLATSSRF RMMNLQGEEF VCLKSIILLN SGVYTFLSST LKSLEEKDHI HRVLDKINDT LIHLMAKAGL TLQQQHRRLA QLLLILSHIR HMSNKGMEHL YNMKCKNVVP LYDLLLEMLD AHRLHAPASR MGVPPEEPSQ SQLTTTSSTS AHSLQTYYIP PEAEGFPNTI //