{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P03372","secondaryAccessions":["Q13511","Q14276","Q5T5H7","Q6MZQ9","Q9NU51","Q9UDZ7","Q9UIS7"],"uniProtkbId":"ESR1_HUMAN","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1994-06-01","entryVersion":300,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Estrogen receptor"},"shortNames":[{"value":"ER"}]},"alternativeNames":[{"fullName":{"value":"ER-alpha"}},{"fullName":{"value":"Estradiol receptor"}},{"fullName":{"value":"Nuclear receptor subfamily 3 group A member 1"}}]},"genes":[{"geneName":{"value":"ESR1"},"synonyms":[{"value":"ESR"},{"value":"NR3A1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P06211"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10681512"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10816575"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11477071"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11682626"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14764652"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15078875"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15891768"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16043358"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16617102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16684779"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17922032"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17932106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18247370"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19350539"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20074560"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20705611"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21330404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22083956"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37478846"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7651415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9328340"}],"value":"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 (PubMed:17922032). Maintains neuronal survival in response to ischemic reperfusion injury when in the presence of circulating estradiol (17-beta-estradiol/E2) (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10970861"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21937726"}],"value":"Involved in activation of NOS3 and endothelial nitric oxide production (PubMed:21937726). Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full-length receptor (PubMed:10970861). Binds to ERE and inhibits isoform 1 (PubMed:10970861)"}],"commentType":"FUNCTION","molecule":"Isoform 3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P06211"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10359819"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10567404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10681512"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10816575"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10970861"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11113208"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11265755"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11358960"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11477071"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11481323"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11581164"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11682626"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11875103"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11971969"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12039952"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12093804"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12554772"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12917342"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14963108"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15047147"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1517211"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15199063"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15891768"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15940264"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16427018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16603732"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16772533"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17006958"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17043237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17085477"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17311814"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17347654"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17505058"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17587566"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17658481"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17914104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17932106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17998543"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18563714"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18657504"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19117995"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19350539"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19383985"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19423554"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19636373"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19712589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19718048"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19749156"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19755138"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20074560"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20078863"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20720010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21104395"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21602804"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23160374"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23874500"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25219498"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28068668"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9328340"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9627117"}],"value":"Binds DNA as a homodimer. Can form a heterodimer with ESR2. Interacts with FOXC2, MAP1S, SLC30A9, UBE1C and NCOA3 coactivator (By similarity). Interacts with PELP1, the interaction is enhanced by 17-beta-estradiol, the interaction increases ESR1 transcriptional activity (PubMed:11481323, PubMed:14963108). Interacts with EP300; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with CITED1; the interaction is estrogen-dependent. Interacts with NCOA5 and NCOA6 coactivators. Interacts with NCOA7; the interaction is a ligand-inducible. Interacts with PHB2, and UBE1C. Interacts with AKAP13. Interacts with CUEDC2. Interacts with KDM5A. Interacts with SMARD1. Interacts with HEXIM1. Interacts with PBXIP1. Interaction with MUC1 is stimulated by 7 beta-estradiol (E2) and enhances ESR1-mediated transcription. Interacts with DNTTIP2, FAM120B and UIMC1. Interacts with isoform 4 of TXNRD1. Interacts with KMT2D/MLL2. Interacts with ATAD2 and this interaction is enhanced by estradiol. Interacts with KIF18A and LDB1. Interacts with RLIM (via C-terminus). Interacts with MACROD1. Interacts with SH2D4A and PLCG. Interaction with SH2D4A blocks binding to PLCG and inhibits estrogen-induced cell proliferation. Interacts with DYNLL1. Interacts with CCDC62 in the presence of estradiol/E2; this interaction seems to enhance the transcription of target genes. Interacts with NR2C1; the interaction prevents homodimerization of ESR1 and suppresses its transcriptional activity and cell growth. Interacts with DNAAF4. Interacts with PRMT2. Interacts with RBFOX2. Interacts with STK3/MST2 only in the presence of SAV1 and vice-versa. Interacts with NCOA2; NCOA2 can interact with ESR1 AF-1 and AF-2 domains simultaneously and mediate their transcriptional synergy. Interacts with DDX5 (PubMed:11682626). Interacts with NCOA1; the interaction seems to require a self-association of N-terminal and C-terminal regions. Interacts with ZNF366, DDX17, NFKB1, RELA, SP1 and SP3. Interacts with NRIP1 (By similarity). Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts with CLOCK and the interaction is stimulated by estrogen. Interacts with BCAS3. Interacts with TRIP4 (ufmylated); estrogen dependent. Interacts with LMTK3; the interaction phosphorylates ESR1 (in vitro) and protects it against proteasomal degradation. Interacts with CCAR2 (via N-terminus) in a ligand-independent manner. Interacts with ZFHX3. Interacts with SFR1 in a ligand-dependent and -independent manner (PubMed:23874500). Interacts with DCAF13, LATS1 and DCAF1; regulates ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation (PubMed:28068668). Interacts (via DNA-binding domain) with POU4F2 (C-terminus); this interaction increases the estrogen receptor ESR1 transcriptional activity in a DNA- and ligand 17-beta-estradiol-independent manner (By similarity). Interacts with ESRRB isoform 1 (PubMed:19755138). Interacts with UBE3A and WBP2 (PubMed:16772533). Interacts with GTF2B (PubMed:1517211). Interacts with RBM39 (By similarity). In the absence of hormonal ligand, interacts with TACC1 (PubMed:20078863). Interacts with PI3KR1 or PI3KR2 and PTK2/FAK1 (PubMed:18657504). Interacts with SRC (PubMed:14963108, PubMed:18657504). Interacts with BAG1; the interaction is promoted in the absence of estradiol (17-beta-estradiol/E2) (By similarity). Interacts with and ubiquitinated by STUB1; the interaction is promoted in the absence of estradiol (17-beta-estradiol/E2) (By similarity). Interacts with NEDD8 (By similarity)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10970861"}],"value":"Probably homodimerizes or heterodimerizes with isoform 1 and ESR2"}],"commentType":"SUBUNIT","molecule":"Isoform 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AF-1 seems to provide the major transactivation function in differentiated cells"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10428798"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14764652"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21602804"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7476978"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7539106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7838153"}],"value":"Phosphorylated by cyclin A/CDK2. Self-association induces phosphorylation. Dephosphorylation at Ser-118 by PPP5C inhibits its transactivation activity. 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