UniProtKB - P03372 (ESR1_HUMAN)
Estrogen receptor
ESR1
Functioni
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).
20 PublicationsInvolved 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).
2 PublicationsMiscellaneous
Caution
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 185 – 250 | Nuclear receptorPROSITE-ProRule annotationAdd BLAST | 66 | |
Zinc fingeri | 185 – 205 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 21 | |
Zinc fingeri | 221 – 245 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 25 |
GO - Molecular functioni
- ATPase binding Source: MGI
- beta-catenin binding Source: BHF-UCL
- chromatin binding Source: UniProtKB
- DNA-binding transcription activator activity, RNA polymerase II-specific Source: NTNU_SB
- DNA-binding transcription factor activity Source: BHF-UCL
- DNA-binding transcription factor activity, RNA polymerase II-specific Source: NTNU_SB
- enzyme binding Source: UniProtKB
- estrogen receptor activity Source: BHF-UCL
- estrogen receptor binding Source: CAFA
- estrogen response element binding Source: UniProtKB
- identical protein binding Source: IntAct
- nitric-oxide synthase regulator activity Source: UniProtKB
- nuclear receptor activity Source: BHF-UCL
- protein kinase binding Source: UniProtKB
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: UniProtKB
- sequence-specific double-stranded DNA binding Source: ARUK-UCL
- steroid binding Source: UniProtKB
- TBP-class protein binding Source: CAFA
- TFIIB-class transcription factor binding Source: CAFA
- transcription coactivator binding Source: UniProtKB
- transcription coregulator binding Source: UniProtKB
- transcription corepressor binding Source: ARUK-UCL
- zinc ion binding Source: InterPro
GO - Biological processi
- androgen metabolic process Source: Ensembl
- antral ovarian follicle growth Source: Ensembl
- cellular response to estradiol stimulus Source: ARUK-UCL
- cellular response to estrogen stimulus Source: Ensembl
- chromatin remodeling Source: UniProtKB
- epithelial cell development Source: Ensembl
- epithelial cell proliferation involved in mammary gland duct elongation Source: Ensembl
- intracellular estrogen receptor signaling pathway Source: CAFA
- intracellular steroid hormone receptor signaling pathway Source: UniProtKB
- male gonad development Source: Ensembl
- mammary gland alveolus development Source: Ensembl
- mammary gland branching involved in pregnancy Source: Ensembl
- negative regulation of DNA-binding transcription factor activity Source: UniProtKB
- negative regulation of gene expression Source: UniProtKB
- negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
- negative regulation of production of miRNAs involved in gene silencing by miRNA Source: BHF-UCL
- negative regulation of transcription by RNA polymerase II Source: BHF-UCL
- phospholipase C-activating G protein-coupled receptor signaling pathway Source: UniProtKB
- positive regulation of cytosolic calcium ion concentration Source: UniProtKB
- positive regulation of DNA-binding transcription factor activity Source: UniProtKB
- positive regulation of fibroblast proliferation Source: Ensembl
- positive regulation of nitric oxide biosynthetic process Source: UniProtKB
- positive regulation of nitric-oxide synthase activity Source: UniProtKB
- positive regulation of phospholipase C activity Source: UniProtKB
- positive regulation of RNA polymerase II transcription preinitiation complex assembly Source: CAFA
- positive regulation of transcription, DNA-templated Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: UniProtKB
- prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis Source: Ensembl
- prostate epithelial cord elongation Source: Ensembl
- protein localization to chromatin Source: BHF-UCL
- regulation of apoptotic process Source: Ensembl
- regulation of branching involved in prostate gland morphogenesis Source: Ensembl
- regulation of inflammatory response Source: Ensembl
- regulation of toll-like receptor signaling pathway Source: Ensembl
- regulation of transcription, DNA-templated Source: UniProtKB
- regulation of transcription by RNA polymerase II Source: GO_Central
- response to estradiol Source: BHF-UCL
- response to estrogen Source: UniProtKB
- signal transduction Source: ProtInc
- stem cell differentiation Source: Ensembl
- uterus development Source: Ensembl
- vagina development Source: Ensembl
Keywordsi
Molecular function | Activator, DNA-binding, Receptor |
Biological process | Transcription, Transcription regulation |
Ligand | Lipid-binding, Metal-binding, Steroid-binding, Zinc |
Enzyme and pathway databases
PathwayCommonsi | P03372 |
Reactomei | R-HSA-1251985, Nuclear signaling by ERBB4 R-HSA-1257604, PIP3 activates AKT signaling R-HSA-2219530, Constitutive Signaling by Aberrant PI3K in Cancer R-HSA-383280, Nuclear Receptor transcription pathway R-HSA-4090294, SUMOylation of intracellular receptors R-HSA-5689896, Ovarian tumor domain proteases R-HSA-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling R-HSA-8866910, TFAP2 (AP-2) family regulates transcription of growth factors and their receptors R-HSA-8931987, RUNX1 regulates estrogen receptor mediated transcription R-HSA-8939211, ESR-mediated signaling R-HSA-8939256, RUNX1 regulates transcription of genes involved in WNT signaling R-HSA-8939902, Regulation of RUNX2 expression and activity R-HSA-9009391, Extra-nuclear estrogen signaling R-HSA-9018519, Estrogen-dependent gene expression |
SignaLinki | P03372 |
SIGNORi | P03372 |
Protein family/group databases
MoonDBi | P03372, Predicted |
Chemistry databases
SwissLipidsi | SLP:000001568 |
Names & Taxonomyi
Protein namesi | Recommended name: Estrogen receptorShort name: ER Alternative name(s): ER-alpha Estradiol receptor Nuclear receptor subfamily 3 group A member 1 |
Gene namesi | Name:ESR1 Synonyms:ESR, NR3A1 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:3467, ESR1 |
MIMi | 133430, gene |
neXtProti | NX_P03372 |
VEuPathDBi | HostDB:ENSG00000091831 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 2 Publications
Plasma membrane
- Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
Nucleus
- Nucleus PROSITE-ProRule annotation2 Publications
Note: A minor fraction is associated with the inner membrane.
Cytoplasm and Cytosol
Plasma membrane
Nucleus
Note: Associated with the inner membrane via palmitoylation (Probable). At least a subset exists as a transmembrane protein with a N-terminal extracellular domain.Curated
Golgi apparatus
Plasma membrane
Nucleus
Note: Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus where most probably palmitoylation occurs. Associated with the plasma membrane when palmitoylated.
Cytosol
- cytosol Source: Reactome
Golgi apparatus
- Golgi apparatus Source: UniProtKB-SubCell
Nucleus
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB
Plasma Membrane
- plasma membrane Source: UniProtKB
Other locations
- chromatin Source: BHF-UCL
- cytoplasm Source: UniProtKB
- integral component of membrane Source: UniProtKB-KW
- membrane Source: UniProtKB
- protein-containing complex Source: UniProtKB
- transcription preinitiation complex Source: CAFA
- transcription regulator complex Source: ComplexPortal
- transcriptionally active chromatin Source: UniProtKB
Keywords - Cellular componenti
Cell membrane, Cytoplasm, Golgi apparatus, Membrane, NucleusPathology & Biotechi
Involvement in diseasei
Estrogen resistance (ESTRR)2 Publications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_070072 | 375 | Q → H in ESTRR; results in highly reduced activity. 1 PublicationCorresponds to variant dbSNP:rs397509428EnsemblClinVar. | 1 | |
Natural variantiVAR_078516 | 394 | R → H in ESTRR; highly decreased estrogen receptor activity. 1 PublicationCorresponds to variant dbSNP:rs1131692059EnsemblClinVar. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 39 | L → P: Impairs AF-1 transactivation. 1 Publication | 1 | |
Mutagenesisi | 43 | Y → P: Impairs AF-1 transactivation. 1 Publication | 1 | |
Mutagenesisi | 104 | S → A: Loss of cyclin A-dependent induction of transcriptional activation. 1 Publication | 1 | |
Mutagenesisi | 106 | S → A: Loss of cyclin A-dependent induction of transcriptional activation. 1 Publication | 1 | |
Mutagenesisi | 118 | S → A: Decreases phosphorylation and transactivation activity. Abolishes AF-1 transactivation. Insensitive to PPP5C inhibition of transactivation activity. 2 Publications | 1 | |
Mutagenesisi | 118 | S → E: Enhances transactivation activity. Insensitive to PPP5C inhibition of transactivation activity. 1 Publication | 1 | |
Mutagenesisi | 260 | R → A or K: Loss of methylation. 1 Publication | 1 | |
Mutagenesisi | 364 | V → E: Has higher transcriptional activity in the absence of wild type ER. Inhibits transcriptional activity when coexpressed with the wild type receptor. 1 Publication | 1 | |
Mutagenesisi | 386 | I → C: Loss of transmembrane localization, no effect on peripheral membrane localization. Impairs activation of estrogen-induced activation of NOS3 and production of nitric oxide. No effect on binding to ERES. 1 Publication | 1 | |
Mutagenesisi | 447 | C → A: Loss of hormone binding capacity and temperature-sensitive loss in DNA-binding. 1 Publication | 1 | |
Mutagenesisi | 537 | Y → A: Reduces PELP1-mediated activation of transcriptional activity. 1 Publication | 1 | |
Mutagenesisi | 539 | L → A: Abolishes interaction with NCOA1, NCOA2 and NCOA3. 1 Publication | 1 |
Keywords - Diseasei
Disease variantOrganism-specific databases
DisGeNETi | 2099 |
MalaCardsi | ESR1 |
MIMi | 615363, phenotype |
OpenTargetsi | ENSG00000091831 |
Orphaneti | 785, Estrogen resistance syndrome |
PharmGKBi | PA156 |
Miscellaneous databases
Pharosi | P03372, Tclin |
Chemistry databases
ChEMBLi | CHEMBL206 |
DrugBanki | DB07567, (2R,3R,4S)-3-(4-HYDROXYPHENYL)-4-METHYL-2-[4-(2-PYRROLIDIN-1-YLETHOXY)PHENYL]CHROMAN-6-OL DB07638, (3AS,4R,9BR)-2,2-DIFLUORO-4-(4-HYDROXYPHENYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-8-OL DB08737, (3AS,4R,9BR)-4-(4-HYDROXYPHENYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-9-OL DB08020, (3AS,4R,9BR)-4-(4-HYDROXYPHENYL)-6-(METHOXYMETHYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-8-OL DB07678, (9ALPHA,13BETA,17BETA)-2-[(1Z)-BUT-1-EN-1-YL]ESTRA-1,3,5(10)-TRIENE-3,17-DIOL DB07707, (9BETA,11ALPHA,13ALPHA,14BETA,17ALPHA)-11-(METHOXYMETHYL)ESTRA-1(10),2,4-TRIENE-3,17-DIOL DB03802, 1-[4-(Octahydro-Pyrido[1,2-a]Pyrazin-2-Yl)-Phenyl]-2-Phenyl-1,2,3,4-Tetrahydro-Isoquinolin-6-Ol DB06871, 17-METHYL-17-ALPHA-DIHYDROEQUILENIN DB08773, 2-(4-hydroxyphenyl)benzo[b]thiophen-6-ol DB08398, 2-Amino-1-methyl-6-phenylimidazo(4,5-b)pyridine DB13869, 2-Methoxy-6-{(E)-[(4-methylphenyl)imino]methyl}phenol DB04471, 2-Phenyl-1-[4-(2-Piperidin-1-Yl-Ethoxy)-Phenyl]-1,2,3,4-Tetrahydro-Isoquinolin-6-Ol DB07708, 3-CHLORO-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL DB07712, 3-ETHYL-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL DB06898, 4-(2-amino-1-methyl-1H-imidazo[4,5-b]pyridin-6-yl)phenol DB08048, 4-(6-HYDROXY-1H-INDAZOL-3-YL)BENZENE-1,3-DIOL DB08595, 4-[(1S,2R,5S)-4,4,8-TRIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL DB07195, 4-[(1S,2S,5S)-5-(HYDROXYMETHYL)-6,8,9-TRIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL DB07086, 4-[(1S,2S,5S)-5-(HYDROXYMETHYL)-8-METHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL DB07087, 4-[(1S,2S,5S,9R)-5-(HYDROXYMETHYL)-8,9-DIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL DB08047, 4-[1-allyl-7-(trifluoromethyl)-1H-indazol-3-yl]benzene-1,3-diol DB06927, [5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-YL]ACETONITRILE DB04468, Afimoxifene DB01431, Allylestrenol DB05233, AP1081 DB06249, Arzoxifene DB06401, Bazedoxifene DB01878, Benzophenone DB06732, beta-Naphthoflavone DB05882, CHF 4227 DB00269, Chlorotrianisene DB00882, Clomifene DB02715, Compound 18 DB02615, Compound 19 DB03742, Compound 4-D DB00286, Conjugated estrogens DB05487, Custirsen DB01406, Danazol DB00304, Desogestrel DB00890, Dienestrol DB08320, DIETHYL (1R,2S,3R,4S)-5,6-BIS(4-HYDROXYPHENYL)-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2,3-DICARBOXYLATE DB00255, Diethylstilbestrol DB07932, dimethyl (1R,4S)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]hepta-2,5-diene-2,3-dicarboxylate DB00841, Dobutamine DB06374, Elacestrant DB11219, Enzacamene DB02187, Equilin DB07933, Erteberel DB00783, Estradiol DB13952, Estradiol acetate DB13953, Estradiol benzoate DB13954, Estradiol cypionate DB13955, Estradiol dienanthate DB13956, Estradiol valerate DB01196, Estramustine DB04573, Estriol DB14641, Estriol tripropionate DB00655, Estrone DB04574, Estrone sulfate DB00977, Ethinylestradiol DB00823, Ethynodiol diacetate DB09086, Eugenol DB15690, Fluoroestradiol F-18 DB01185, Fluoxymesterone DB00947, Fulvestrant DB01645, Genistein DB11619, Gestrinone DB00756, Hexachlorophene DB07931, Hexestrol DB11064, Homosalate DB06202, Lasofoxifene DB00367, Levonorgestrel DB00431, Lindane DB00603, Medroxyprogesterone acetate DB01065, Melatonin DB01357, Mestranol DB06710, Methyltestosterone DB00648, Mitotane DB07991, N-[(1R)-3-(4-HYDROXYPHENYL)-1-METHYLPROPYL]-2-(2-PHENYL-1H-INDOL-3-YL)ACETAMIDE DB01183, Naloxone DB03467, Naringenin DB09371, Norethynodrel DB00957, Norgestimate DB05662, NP-50301 DB09535, Octocrylene DB04938, Ospemifene DB01428, Oxybenzone DB04930, Permethrin DB04824, Phenolphthalein DB02746, Phthalic Acid DB09369, Polyestradiol phosphate DB01708, Prasterone DB00396, Progesterone DB12450, Propyl Gallate DB02757, Pyrazole DB04216, Quercetin DB04575, Quinestrol DB11541, Ractopamine DB00481, Raloxifene DB02709, Resveratrol DB02901, Stanolone DB13951, Stanolone acetate DB09317, Synthetic Conjugated Estrogens, A DB09318, Synthetic Conjugated Estrogens, B DB00675, Tamoxifen DB05966, TAS-108 DB00624, Testosterone DB13943, Testosterone cypionate DB13944, Testosterone enanthate DB13946, Testosterone undecanoate DB09070, Tibolone DB00539, Toremifene DB01108, Trilostane DB11478, Zeranol DB01593, Zinc DB14487, Zinc acetate DB14533, Zinc chloride DB14548, Zinc sulfate, unspecified form |
DrugCentrali | P03372 |
GuidetoPHARMACOLOGYi | 620 |
Genetic variation databases
BioMutai | ESR1 |
DMDMi | 544257 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000053618 | 1 – 595 | Estrogen receptorAdd BLAST | 595 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 10 | O-linked (GlcNAc) serineBy similarity | 1 | |
Modified residuei | 104 | Phosphoserine; by CDK21 Publication | 1 | |
Modified residuei | 106 | Phosphoserine; by CDK21 Publication | 1 | |
Modified residuei | 118 | Phosphoserine1 Publication | 1 | |
Modified residuei | 167 | Phosphoserine; by CK21 Publication | 1 | |
Modified residuei | 260 | Asymmetric dimethylarginine; by PRMT12 Publications | 1 | |
Lipidationi | 447 | S-palmitoyl cysteineBy similarity | 1 | |
Modified residuei | 537 | Phosphotyrosine; by Tyr-kinases1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
Glycoprotein, Lipoprotein, Methylation, Palmitate, Phosphoprotein, Ubl conjugationProteomic databases
CPTACi | CPTAC-1241 CPTAC-145 |
EPDi | P03372 |
jPOSTi | P03372 |
MassIVEi | P03372 |
PaxDbi | P03372 |
PeptideAtlasi | P03372 |
PRIDEi | P03372 |
ProteomicsDBi | 51607 [P03372-1] 51608 [P03372-2] 51609 [P03372-3] 51610 [P03372-4] |
PTM databases
GlyConnecti | 144, 1 O-Linked glycan |
GlyGeni | P03372, 2 sites, 1 O-linked glycan (1 site) |
iPTMneti | P03372 |
PhosphoSitePlusi | P03372 |
SwissPalmi | P03372 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000091831, Expressed in endometrium and 168 other tissues |
ExpressionAtlasi | P03372, baseline and differential |
Genevisiblei | P03372, HS |
Organism-specific databases
HPAi | ENSG00000091831, Tissue enhanced (cervix, endometrium, fallopian tube) |
Interactioni
Subunit structurei
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. 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 (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).
By similarity61 PublicationsBinary interactionsi
P03372
ESR1 - isoform 1 [P03372-1]
With | #Exp. | IntAct |
---|---|---|
itself | 4 | EBI-15606245,EBI-15606245 |
ESR2 [Q92731] | 5 | EBI-15606245,EBI-78505 |
KAT5 [Q92993] | 3 | EBI-15606245,EBI-399080 |
PBXIP1 - isoform 1 [Q96AQ6-1] | 5 | EBI-15606245,EBI-15606280 |
Isoform 4 [P03372-4]
With | #Exp. | IntAct |
---|---|---|
EGFR [P00533] | 4 | EBI-4309277,EBI-297353 |
SHC1 [P29353] | 2 | EBI-4309277,EBI-78835 |
SRC [P12931] | 2 | EBI-4309277,EBI-621482 |
GO - Molecular functioni
- ATPase binding Source: MGI
- beta-catenin binding Source: BHF-UCL
- enzyme binding Source: UniProtKB
- estrogen receptor binding Source: CAFA
- identical protein binding Source: IntAct
- protein kinase binding Source: UniProtKB
- TBP-class protein binding Source: CAFA
- TFIIB-class transcription factor binding Source: CAFA
- transcription coactivator binding Source: UniProtKB
- transcription coregulator binding Source: UniProtKB
- transcription corepressor binding Source: ARUK-UCL
Protein-protein interaction databases
BioGRIDi | 108403, 2158 interactors |
ComplexPortali | CPX-5156, ERalpha-NCOA2 activated estrogen receptor complex |
CORUMi | P03372 |
DIPi | DIP-5965N |
ELMi | P03372 |
IntActi | P03372, 1904 interactors |
MINTi | P03372 |
STRINGi | 9606.ENSP00000405330 |
Chemistry databases
BindingDBi | P03372 |
Miscellaneous databases
RNActi | P03372, protein |
Structurei
Secondary structure
3D structure databases
SASBDBi | P03372 |
SMRi | P03372 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P03372 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 311 – 547 | NR LBDPROSITE-ProRule annotationAdd BLAST | 237 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 184 | Modulating (transactivation AF-1); mediates interaction with MACROD11 PublicationAdd BLAST | 184 | |
Regioni | 35 – 174 | Interaction with DDX5; self-association1 PublicationAdd BLAST | 140 | |
Regioni | 35 – 47 | Required for interaction with NCOA11 PublicationAdd BLAST | 13 | |
Regioni | 147 – 174 | DisorderedSequence analysisAdd BLAST | 28 | |
Regioni | 185 – 310 | Mediates interaction with DNTTIP21 PublicationAdd BLAST | 126 | |
Regioni | 251 – 310 | HingeAdd BLAST | 60 | |
Regioni | 259 – 282 | DisorderedSequence analysisAdd BLAST | 24 | |
Regioni | 262 – 595 | Interaction with AKAP131 PublicationAdd BLAST | 334 | |
Regioni | 264 – 595 | Self-associationAdd BLAST | 332 | |
Regioni | 311 – 595 | Transactivation AF-2Add BLAST | 285 | |
Regioni | 553 – 573 | DisorderedSequence analysisAdd BLAST | 21 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 558 – 573 | Polar residuesSequence analysisAdd BLAST | 16 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 185 – 205 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 21 | |
Zinc fingeri | 221 – 245 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 25 |
Keywords - Domaini
Transmembrane, Zinc-fingerPhylogenomic databases
eggNOGi | KOG3575, Eukaryota |
GeneTreei | ENSGT00940000158133 |
InParanoidi | P03372 |
OMAi | NRPYTEV |
OrthoDBi | 487299at2759 |
PhylomeDBi | P03372 |
TreeFami | TF323751 |
Family and domain databases
DisProti | DP00074 |
Gene3Di | 1.10.565.10, 1 hit 3.30.50.10, 1 hit |
IDEALi | IID00013 |
InterProi | View protein in InterPro IPR024178, Est_rcpt/est-rel_rcp IPR001292, Estr_rcpt IPR035500, NHR-like_dom_sf IPR000536, Nucl_hrmn_rcpt_lig-bd IPR001723, Nuclear_hrmn_rcpt IPR024736, Oestrogen-typ_rcpt_final_C_dom IPR001628, Znf_hrmn_rcpt IPR013088, Znf_NHR/GATA |
Pfami | View protein in Pfam PF12743, ESR1_C, 1 hit PF00104, Hormone_recep, 1 hit PF02159, Oest_recep, 1 hit PF00105, zf-C4, 1 hit |
PIRSFi | PIRSF500101, ER-a, 1 hit PIRSF002527, ER-like_NR, 1 hit |
PRINTSi | PR00543, OESTROGENR PR00398, STRDHORMONER PR00047, STROIDFINGER |
SMARTi | View protein in SMART SM00430, HOLI, 1 hit SM00399, ZnF_C4, 1 hit |
SUPFAMi | SSF48508, SSF48508, 1 hit |
PROSITEi | View protein in PROSITE PS51843, NR_LBD, 1 hit PS00031, NUCLEAR_REC_DBD_1, 1 hit PS51030, NUCLEAR_REC_DBD_2, 1 hit |
s (4+)i Sequence
Sequence statusi: Complete.
This entry describes 4 produced by isoformsialternative promoter usage and alternative splicing. AlignAdd to basketThis entry has 4 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKIPLERPLG EVYLDSSKPA
60 70 80 90 100
VYNYPEGAAY EFNAAAAANA QVYGQTGLPY GPGSEAAAFG SNGLGGFPPL
110 120 130 140 150
NSVSPSPLML LHPPPQLSPF LQPHGQQVPY YLENEPSGYT VREAGPPAFY
160 170 180 190 200
RPNSDNRRQG GRERLASTND KGSMAMESAK ETRYCAVCND YASGYHYGVW
210 220 230 240 250
SCEGCKAFFK RSIQGHNDYM CPATNQCTID KNRRKSCQAC RLRKCYEVGM
260 270 280 290 300
MKGGIRKDRR GGRMLKHKRQ RDDGEGRGEV GSAGDMRAAN LWPSPLMIKR
310 320 330 340 350
SKKNSLALSL TADQMVSALL DAEPPILYSE YDPTRPFSEA SMMGLLTNLA
360 370 380 390 400
DRELVHMINW AKRVPGFVDL TLHDQVHLLE CAWLEILMIG LVWRSMEHPG
410 420 430 440 450
KLLFAPNLLL DRNQGKCVEG MVEIFDMLLA TSSRFRMMNL QGEEFVCLKS
460 470 480 490 500
IILLNSGVYT FLSSTLKSLE EKDHIHRVLD KITDTLIHLM AKAGLTLQQQ
510 520 530 540 550
HQRLAQLLLI LSHIRHMSNK GMEHLYSMKC KNVVPLYDLL LEMLDAHRLH
560 570 580 590
APTSRGGASV EETDQSHLAT AGSTSSHSLQ KYYITGEAEG FPATV
The sequence of this isoform differs from the canonical sequence as follows:
1-173: Missing.
458-595: VYTFLSSTLK...GEAEGFPATV → FTISHVEAKKRILNLHPKIFGNKWFPRV
Computationally mapped potential isoform sequencesi
There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketQ9H2M1 | Q9H2M1_HUMAN | ER-alpha | ESR1 | 334 | Annotation score: | ||
H0Y4W6 | H0Y4W6_HUMAN | Estrogen receptor | ESR1 | 310 | Annotation score: | ||
Q9UE35 | Q9UE35_HUMAN | Estrogen receptor | ESR1 estrogen receptor | 115 | Annotation score: | ||
Q5T5H8 | Q5T5H8_HUMAN | Estrogen receptor | ESR1 | 84 | Annotation score: | ||
Q9H2M2 | Q9H2M2_HUMAN | Estrogen receptor | ESR1 | 152 | Annotation score: | ||
B0QYW7 | B0QYW7_HUMAN | Estrogen receptor | ESR1 | 107 | Annotation score: | ||
A0A1W2PP92 | A0A1W2PP92_HUMAN | Estrogen receptor | ESR1 | 44 | Annotation score: |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 452 | I → L in CAE45969 (PubMed:17974005).Curated | 1 |
Polymorphismi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_033028 | 6 | H → Y in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs139960913EnsemblClinVar. | 1 | |
Natural variantiVAR_018905 | 77 | G → S. Corresponds to variant dbSNP:rs9340773EnsemblClinVar. | 1 | |
Natural variantiVAR_004671 | 160 | G → C1 PublicationCorresponds to variant dbSNP:rs149308960EnsemblClinVar. | 1 | |
Natural variantiVAR_033029 | 264 | M → I in a breast cancer sample; somatic mutation. 1 Publication | 1 | |
Natural variantiVAR_070072 | 375 | Q → H in ESTRR; results in highly reduced activity. 1 PublicationCorresponds to variant dbSNP:rs397509428EnsemblClinVar. | 1 | |
Natural variantiVAR_078516 | 394 | R → H in ESTRR; highly decreased estrogen receptor activity. 1 PublicationCorresponds to variant dbSNP:rs1131692059EnsemblClinVar. | 1 | |
Natural variantiVAR_004673 | 400 | G → V Destabilizes the receptor and decreases its affinity for estradiol at 25 degrees Celsius, but not at 4 degrees Celsius. 3 Publications | 1 | |
Natural variantiVAR_010143 | 411 | D → RNQGKCVEGMVEIFDMLLAT SSRFRMMNLQGEEFVCLKSI ILLNSGVYTFLSSTLKSLEE KDHIHRVLDKITDTLIHLMA KAGLTLQQQHQRLAQLLLIL SHIRHM in a 80 kDa form found in a breast cancer line; contains an in-frame duplication of exons 6 and 7. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_042460 | 1 – 173 | Missing in isoform 3 and isoform 4. 2 PublicationsAdd BLAST | 173 | |
Alternative sequenceiVSP_003680 | 255 – 366 | Missing in isoform 2. 1 PublicationAdd BLAST | 112 | |
Alternative sequenceiVSP_042461 | 458 – 595 | VYTFL…FPATV → FTISHVEAKKRILNLHPKIF GNKWFPRV in isoform 4. 2 PublicationsAdd BLAST | 138 |
Sequence databases
Genome annotation databases
Ensembli | ENST00000206249; ENSP00000206249; ENSG00000091831 ENST00000338799; ENSP00000342630; ENSG00000091831 ENST00000440973; ENSP00000405330; ENSG00000091831 ENST00000443427; ENSP00000387500; ENSG00000091831 |
GeneIDi | 2099 |
KEGGi | hsa:2099 |
MANE-Selecti | ENST00000206249.8; ENSP00000206249.3; NM_000125.4; NP_000116.2 |
UCSCi | uc003qom.5, human [P03372-1] |
Keywords - Coding sequence diversityi
Alternative promoter usage, Alternative splicingSimilar proteinsi
Cross-referencesi
Web resourcesi
NIEHS-SNPs |
Wikipedia Estrogen receptor entry |
Sequence databases
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1A52 | X-ray | 2.80 | A/B | 297-554 | [»] | |
1ERE | X-ray | 3.10 | A/B/C/D/E/F | 301-553 | [»] | |
1ERR | X-ray | 2.60 | A/B | 301-553 | [»] | |
1G50 | X-ray | 2.90 | A/B/C | 304-550 | [»] | |
1GWQ | X-ray | 2.45 | A/B | 301-548 | [»] | |
1GWR | X-ray | 2.40 | A/B | 305-549 | [»] | |
1HCP | NMR | - | A | 180-254 | [»] | |
1HCQ | X-ray | 2.40 | A/B/E/F | 180-262 | [»] | |
1L2I | X-ray | 1.95 | A/B | 297-554 | [»] | |
1PCG | X-ray | 2.70 | A/B | 304-547 | [»] | |
1QKT | X-ray | 2.20 | A | 304-551 | [»] | |
1QKU | X-ray | 3.20 | A/B/C | 301-550 | [»] | |
1R5K | X-ray | 2.70 | A/B/C | 297-554 | [»] | |
1SJ0 | X-ray | 1.90 | A | 307-554 | [»] | |
1UOM | X-ray | 2.28 | A | 301-553 | [»] | |
1X7E | X-ray | 2.80 | A/B | 305-549 | [»] | |
1X7R | X-ray | 2.00 | A | 305-549 | [»] | |
1XP1 | X-ray | 1.80 | A | 307-554 | [»] | |
1XP6 | X-ray | 1.70 | A | 307-554 | [»] | |
1XP9 | X-ray | 1.80 | A | 307-554 | [»] | |
1XPC | X-ray | 1.60 | A | 307-554 | [»] | |
1XQC | X-ray | 2.05 | A/B/C/D | 301-553 | [»] | |
1YIM | X-ray | 1.90 | A | 307-554 | [»] | |
1YIN | X-ray | 2.20 | A | 307-554 | [»] | |
1ZKY | X-ray | 2.25 | A/B | 298-554 | [»] | |
2AYR | X-ray | 1.90 | A | 304-551 | [»] | |
2B1V | X-ray | 1.80 | A/B | 298-554 | [»] | |
2B1Z | X-ray | 1.78 | A/B | 298-554 | [»] | |
2B23 | X-ray | 2.10 | A/B | 298-554 | [»] | |
2BJ4 | X-ray | 2.00 | A/B | 305-533 | [»] | |
2FAI | X-ray | 2.10 | A/B | 298-554 | [»] | |
2G44 | X-ray | 2.65 | A/B | 298-554 | [»] | |
2G5O | X-ray | 2.30 | A/B | 298-554 | [»] | |
2I0J | X-ray | 2.90 | A/B/C/D | 304-547 | [»] | |
2IOG | X-ray | 1.60 | A | 309-554 | [»] | |
2IOK | X-ray | 2.40 | A/B | 301-554 | [»] | |
2JF9 | X-ray | 2.10 | A/B/C | 304-533 | [»] | |
2JFA | X-ray | 2.55 | A/B | 304-533 | [»] | |
2LLO | NMR | - | B | 287-305 | [»] | |
2LLQ | NMR | - | B | 287-305 | [»] | |
2OCF | X-ray | 2.95 | A | 298-595 | [»] | |
2OUZ | X-ray | 2.00 | A | 301-553 | [»] | |
2P15 | X-ray | 1.94 | A/B | 298-554 | [»] | |
2POG | X-ray | 1.84 | A/B | 304-551 | [»] | |
2Q6J | X-ray | 2.70 | A/B | 298-554 | [»] | |
2Q70 | X-ray | 1.95 | A/B | 304-551 | [»] | |
2QA6 | X-ray | 2.60 | A/B | 298-554 | [»] | |
2QA8 | X-ray | 1.85 | A/B | 298-554 | [»] | |
2QAB | X-ray | 1.89 | A/B | 298-554 | [»] | |
2QE4 | X-ray | 2.40 | A/B | 304-551 | [»] | |
2QGT | X-ray | 2.15 | A/B | 298-554 | [»] | |
2QGW | X-ray | 2.39 | A/B | 298-554 | [»] | |
2QH6 | X-ray | 2.70 | A/B | 298-554 | [»] | |
2QR9 | X-ray | 2.00 | A/B | 298-554 | [»] | |
2QSE | X-ray | 1.85 | A/B | 298-554 | [»] | |
2QXM | X-ray | 2.30 | A/B | 298-554 | [»] | |
2QXS | X-ray | 1.70 | A/B | 298-554 | [»] | |
2QZO | X-ray | 1.72 | A/B | 298-554 | [»] | |
2R6W | X-ray | 2.00 | A/B | 304-551 | [»] | |
2R6Y | X-ray | 2.00 | A/B | 304-551 | [»] | |
2YAT | X-ray | 2.60 | A | 301-551 | [»] | |
2YJA | X-ray | 1.82 | B | 299-551 | [»] | |
3CBM | X-ray | 1.69 | B | 298-307 | [»] | |
3CBO | X-ray | 1.65 | B | 298-307 | [»] | |
3CBP | X-ray | 1.42 | B | 298-307 | [»] | |
3DT3 | X-ray | 2.40 | A/B | 299-551 | [»] | |
3ERD | X-ray | 2.03 | A/B | 297-554 | [»] | |
3ERT | X-ray | 1.90 | A | 297-554 | [»] | |
3HLV | X-ray | 3.00 | A/B | 298-550 | [»] | |
3HM1 | X-ray | 2.33 | A/B | 298-550 | [»] | |
3L03 | X-ray | 1.90 | A/B | 298-550 | [»] | |
3OS8 | X-ray | 2.03 | A/B/C/D | 299-553 | [»] | |
3OS9 | X-ray | 2.30 | A/B/C/D | 299-553 | [»] | |
3OSA | X-ray | 2.30 | A/B/C/D | 299-553 | [»] | |
3Q95 | X-ray | 2.05 | A/B | 298-554 | [»] | |
3UU7 | X-ray | 2.20 | A/B | 302-552 | [»] | |
3UUA | X-ray | 2.05 | A/B | 302-552 | [»] | |
3UUC | X-ray | 2.10 | A/B/C/D | 302-552 | [»] | |
3UUD | X-ray | 1.60 | A/B | 302-552 | [»] | |
4AA6 | X-ray | 2.60 | A/B/E/F | 182-252 | [»] | |
4DMA | X-ray | 2.30 | A/B | 303-549 | [»] | |
4IU7 | X-ray | 2.29 | A/B | 303-549 | [»] | |
4IUI | X-ray | 2.30 | A/B | 303-549 | [»] | |
4IV2 | X-ray | 2.14 | A/B | 303-549 | [»] | |
4IV4 | X-ray | 2.30 | A/B | 303-549 | [»] | |
4IVW | X-ray | 2.06 | A/B | 303-549 | [»] | |
4IVY | X-ray | 1.95 | A/B | 303-549 | [»] | |
4IW6 | X-ray | 1.98 | A/B | 303-549 | [»] | |
4IW8 | X-ray | 2.04 | A/B | 303-549 | [»] | |
4IWC | X-ray | 2.24 | A/B | 303-549 | [»] | |
4IWF | X-ray | 1.93 | A/B | 303-549 | [»] | |
4JC3 | X-ray | 2.05 | B | 585-595 | [»] | |
4JDD | X-ray | 2.10 | B | 585-595 | [»] | |
4MG5 | X-ray | 2.05 | A/B | 302-552 | [»] | |
4MG6 | X-ray | 2.10 | A/B | 302-552 | [»] | |
4MG7 | X-ray | 2.15 | A/B | 302-552 | [»] | |
4MG8 | X-ray | 1.85 | A/B | 302-552 | [»] | |
4MG9 | X-ray | 2.00 | A/B | 302-552 | [»] | |
4MGA | X-ray | 1.80 | A/B | 302-552 | [»] | |
4MGB | X-ray | 1.85 | A/B | 302-552 | [»] | |
4MGC | X-ray | 2.15 | A/B | 302-552 | [»] | |
4MGD | X-ray | 1.90 | A/B | 302-552 | [»] | |
4O6F | X-ray | 2.82 | B | 261-271 | [»] | |
4PP6 | X-ray | 2.20 | A/B | 305-548 | [»] | |
4PPP | X-ray | 2.69 | A/B | 305-548 | [»] | |
4PPS | X-ray | 1.93 | A/B | 305-548 | [»] | |
4PXM | X-ray | 1.90 | A/B | 299-554 | [»] | |
4Q13 | X-ray | 2.24 | A/B | 299-554 | [»] | |
4Q50 | X-ray | 3.07 | A/B/C/D/E/F/G/H | 299-554 | [»] | |
4TUZ | X-ray | 1.90 | A/B | 302-552 | [»] | |
4TV1 | X-ray | 1.85 | A/B | 302-552 | [»] | |
4XI3 | X-ray | 2.49 | A/B/C/D | 306-548 | [»] | |
4ZN7 | X-ray | 1.93 | A/B | 301-559 | [»] | |
4ZN9 | X-ray | 2.21 | A/B | 301-559 | [»] | |
4ZNH | X-ray | 1.93 | A/B | 301-559 | [»] | |
4ZNS | X-ray | 1.86 | A/B | 301-559 | [»] | |
4ZNT | X-ray | 1.90 | A/B | 301-559 | [»] | |
4ZNU | X-ray | 2.40 | A/B | 301-559 | [»] | |
4ZNV | X-ray | 1.77 | A/B | 301-559 | [»] | |
4ZNW | X-ray | 2.31 | A/B | 301-559 | [»] | |
5AAU | X-ray | 1.90 | A/B | 307-554 | [»] | |
5AAV | X-ray | 1.95 | A | 307-554 | [»] | |
B | 306-554 | [»] | ||||
5ACC | X-ray | 1.88 | A | 307-554 | [»] | |
5AK2 | X-ray | 2.19 | A/B | 307-554 | [»] | |
5DI7 | X-ray | 2.24 | A/B | 298-554 | [»] | |
5DID | X-ray | 2.24 | A/B | 298-554 | [»] | |
5DIE | X-ray | 2.24 | A/B | 298-554 | [»] | |
5DIG | X-ray | 2.24 | A/B | 298-554 | [»] | |
5DK9 | X-ray | 2.28 | A/B | 298-554 | [»] | |
5DKB | X-ray | 2.40 | A/B | 298-554 | [»] | |
5DKE | X-ray | 2.60 | A/B | 298-554 | [»] | |
5DKG | X-ray | 2.15 | A/B | 298-554 | [»] | |
5DKS | X-ray | 2.60 | A/B | 298-554 | [»] | |
5DL4 | X-ray | 2.10 | A/B | 298-554 | [»] | |
5DLR | X-ray | 2.26 | A/B | 298-554 | [»] | |
5DMC | X-ray | 2.40 | A/B | 298-554 | [»] | |
5DMF | X-ray | 2.40 | A/B | 298-554 | [»] | |
5DP0 | X-ray | 2.38 | A/B | 298-554 | [»] | |
5DRJ | X-ray | 2.07 | A/B | 298-554 | [»] | |
5DRM | X-ray | 2.24 | A/B | 298-554 | [»] | |
5DTV | X-ray | 2.29 | A/B | 298-554 | [»] | |
5DU5 | X-ray | 2.19 | A/B | 298-554 | [»] | |
5DUE | X-ray | 2.09 | A/B | 298-554 | [»] | |
5DUG | X-ray | 2.25 | A/B | 298-554 | [»] | |
5DUH | X-ray | 2.24 | A/B | 298-554 | [»] | |
5DVS | X-ray | 2.28 | A/B | 298-554 | [»] | |
5DVV | X-ray | 2.50 | A/B | 298-554 | [»] | |
5DWE | X-ray | 1.92 | A/B | 298-554 | [»] | |
5DWG | X-ray | 2.30 | A/B | 298-554 | [»] | |
5DWI | X-ray | 2.43 | A/B | 298-554 | [»] | |
5DWJ | X-ray | 2.00 | A/B | 298-554 | [»] | |
5DX3 | X-ray | 2.09 | A/B | 297-554 | [»] | |
5DXB | X-ray | 2.08 | A/B | 297-554 | [»] | |
5DXE | X-ray | 1.50 | A/B | 297-554 | [»] | |
5DXG | X-ray | 1.86 | A/B | 297-554 | [»] | |
5DXK | X-ray | 2.23 | A/B | 298-554 | [»] | |
5DXM | X-ray | 2.37 | A/B | 298-554 | [»] | |
5DXP | X-ray | 2.20 | A/B | 298-554 | [»] | |
5DXQ | X-ray | 2.40 | A/B | 298-554 | [»] | |
5DXR | X-ray | 2.28 | A/B | 298-554 | [»] | |
5DY8 | X-ray | 2.03 | A/B | 298-554 | [»] | |
5DYB | X-ray | 2.27 | A/B | 298-554 | [»] | |
5DYD | X-ray | 2.48 | A/B | 298-554 | [»] | |
5DZ0 | X-ray | 2.24 | A/B | 298-554 | [»] | |
5DZ1 | X-ray | 2.20 | A/B | 298-554 | [»] | |
5DZ3 | X-ray | 2.15 | A/B | 298-554 | [»] | |
5DZH | X-ray | 2.11 | A/B | 298-554 | [»] | |
5DZI | X-ray | 1.90 | A/B | 298-554 | [»] | |
5E0W | X-ray | 2.00 | A/B | 298-554 | [»] | |
5E0X | X-ray | 2.01 | A/B | 298-554 | [»] | |
5E14 | X-ray | 2.22 | A/B | 298-554 | [»] | |
5E15 | X-ray | 2.10 | A/B | 298-554 | [»] | |
5E19 | X-ray | 2.24 | A/B | 298-554 | [»] | |
5E1C | X-ray | 1.98 | A/B | 298-554 | [»] | |
5EGV | X-ray | 2.86 | A/B | 298-554 | [»] | |
5EHJ | X-ray | 2.50 | A/B | 298-554 | [»] | |
5EI1 | X-ray | 2.40 | A/B | 298-554 | [»] | |
5EIT | X-ray | 2.68 | A/B | 298-554 | [»] | |
5FQP | X-ray | 1.88 | A | 307-554 | [»] | |
5FQR | X-ray | 1.88 | A | 307-554 | [»] | |
5FQS | X-ray | 1.94 | A | 307-554 | [»] | |
5FQT | X-ray | 1.99 | A | 307-554 | [»] | |
5FQV | X-ray | 1.74 | A | 307-554 | [»] | |
5GS4 | X-ray | 2.40 | A | 305-547 | [»] | |
5GTR | X-ray | 2.80 | A | 305-547 | [»] | |
5HYR | X-ray | 2.27 | A/B | 302-559 | [»] | |
5JMM | X-ray | 2.10 | A/B | 302-552 | [»] | |
5KCC | X-ray | 2.39 | A/B | 298-554 | [»] | |
A/B | 304-549 | [»] | ||||
5KCD | X-ray | 1.82 | A/B | 298-554 | [»] | |
A/B | 305-549 | [»] | ||||
5KCE | X-ray | 1.85 | A/B | 298-554 | [»] | |
A/B | 303-549 | [»] | ||||
5KCF | X-ray | 2.07 | A/B | 298-554 | [»] | |
A/B | 303-549 | [»] | ||||
5KCT | X-ray | 1.60 | A/B | 298-554 | [»] | |
A/B | 303-548 | [»] | ||||
5KCU | X-ray | 2.03 | A/B | 298-554 | [»] | |
A/B | 303-548 | [»] | ||||
5KCW | X-ray | 1.91 | A/B | 303-549 | [»] | |
A/B | 298-554 | [»] | ||||
5KD9 | X-ray | 1.78 | A/B | 298-554 | [»] | |
A/B | 303-549 | [»] | ||||
5KR9 | X-ray | 2.25 | A/B | 298-554 | [»] | |
5KRA | X-ray | 2.40 | A/B/E/F | 298-554 | [»] | |
5KRC | X-ray | 2.40 | A/B | 298-554 | [»] | |
5KRF | X-ray | 2.19 | A/B | 298-554 | [»] | |
5KRH | X-ray | 2.24 | A/B | 298-554 | [»] | |
5KRI | X-ray | 2.25 | A/B | 298-554 | [»] | |
5KRJ | X-ray | 2.70 | A/B | 298-554 | [»] | |
5KRK | X-ray | 2.39 | A/B | 298-554 | [»] | |
5KRL | X-ray | 2.40 | A/B | 298-554 | [»] | |
5KRM | X-ray | 2.24 | A/B | 298-554 | [»] | |
5KRO | X-ray | 2.10 | A/B | 298-554 | [»] | |
5N10 | X-ray | 1.60 | C/D/F | 584-595 | [»] | |
5T0X | NMR | - | B/C | 287-305 | [»] | |
5T1Z | X-ray | 2.10 | A/B | 298-554 | [»] | |
5T92 | X-ray | 2.22 | A/B | 301-553 | [»] | |
5T97 | X-ray | 3.00 | A/B | 301-553 | [»] | |
5TLD | X-ray | 2.38 | A/B | 298-554 | [»] | |
5TLF | X-ray | 2.20 | A/B | 298-554 | [»] | |
5TLG | X-ray | 2.23 | A/B | 298-554 | [»] | |
5TLL | X-ray | 2.42 | A/B | 298-554 | [»] | |
5TLM | X-ray | 2.50 | A/B | 298-554 | [»] | |
5TLO | X-ray | 2.28 | A/B | 298-554 | [»] | |
5TLP | X-ray | 2.08 | A/B | 298-554 | [»] | |
5TLT | X-ray | 1.90 | A/B | 298-554 | [»] | |
5TLU | X-ray | 2.22 | A/B | 298-554 | [»] | |
5TLV | X-ray | 2.32 | A/B | 298-554 | [»] | |
5TLX | X-ray | 2.10 | A/B | 298-554 | [»] | |
5TLY | X-ray | 2.14 | A/B | 298-554 | [»] | |
5TM1 | X-ray | 2.23 | A/B | 298-554 | [»] | |
5TM2 | X-ray | 2.60 | A/B | 298-554 | [»] | |
5TM3 | X-ray | 2.19 | A/B | 298-554 | [»] | |
5TM4 | X-ray | 2.25 | A/B | 298-554 | [»] | |
5TM5 | X-ray | 2.24 | A/B | 298-554 | [»] | |
5TM6 | X-ray | 2.54 | A/B | 298-554 | [»] | |
5TM7 | X-ray | 2.40 | A/B | 298-554 | [»] | |
5TM8 | X-ray | 1.99 | A/B | 298-554 | [»] | |
5TM9 | X-ray | 2.50 | A/B | 298-554 | [»] | |
5TML | X-ray | 2.25 | A/B | 298-554 | [»] | |
5TMM | X-ray | 2.20 | A/B | 298-554 | [»] | |
5TMO | X-ray | 2.17 | A/B | 298-554 | [»] | |
5TMQ | X-ray | 2.24 | A/B | 298-554 | [»] | |
5TMR | X-ray | 2.30 | A/B | 298-554 | [»] | |
5TMS | X-ray | 2.24 | A/B | 298-554 | [»] | |
5TMT | X-ray | 2.05 | A/B | 298-554 | [»] | |
5TMU | X-ray | 2.43 | A/B | 298-554 | [»] | |
5TMV | X-ray | 2.38 | A/B | 298-554 | [»] | |
5TMW | X-ray | 2.29 | A/B | 298-554 | [»] | |
5TMZ | X-ray | 2.21 | A/B | 298-554 | [»] | |
5TN1 | X-ray | 2.06 | A/B | 298-554 | [»] | |
5TN3 | X-ray | 2.54 | A/B | 298-554 | [»] | |
5TN4 | X-ray | 1.86 | A/B | 298-554 | [»] | |
5TN5 | X-ray | 1.89 | A/B | 298-554 | [»] | |
5TN6 | X-ray | 2.09 | A/B | 298-554 | [»] | |
5TN7 | X-ray | 2.24 | A/B | 298-554 | [»] | |
5TN8 | X-ray | 2.65 | A/B | 298-554 | [»] | |
5TN9 | X-ray | 2.25 | A/B/C/D | 298-554 | [»] | |
5TNB | X-ray | 2.08 | A/B/C/D | 298-554 | [»] | |
5U2B | X-ray | 2.22 | A/B/C/D/E/F | 298-554 | [»] | |
5U2D | X-ray | 1.86 | A/B | 298-554 | [»] | |
5UFW | X-ray | 1.58 | A/B | 306-554 | [»] | |
5UFX | X-ray | 1.55 | A/B | 306-554 | [»] | |
5W9C | X-ray | 1.80 | A/B/C/D | 306-554 | [»] | |
5W9D | X-ray | 1.65 | A/B | 306-554 | [»] | |
5WGD | X-ray | 1.80 | A/B | 297-554 | [»] | |
5WGQ | X-ray | 2.30 | A/B | 297-554 | [»] | |
6B0F | X-ray | 2.86 | A/B | 301-553 | [»] | |
6C42 | X-ray | 2.00 | A/B | 307-554 | [»] | |
6CBZ | X-ray | 1.65 | A/B | 305-554 | [»] | |
6CHW | X-ray | 1.89 | A | 306-551 | [»] | |
6CHZ | X-ray | 1.68 | A | 307-554 | [»] | |
6CZN | X-ray | 2.50 | A/B | 298-554 | [»] | |
6D0F | X-ray | 2.50 | A/B | 305-554 | [»] | |
6DF6 | X-ray | 2.50 | A/B/C/D | 298-553 | [»] | |
6DFN | X-ray | 2.10 | A/B/C/D | 298-553 | [»] | |
6HHP | X-ray | 1.80 | B | 588-595 | [»] | |
6HKB | X-ray | 1.70 | B | 588-595 | [»] | |
6HKF | X-ray | 1.80 | B | 588-595 | [»] | |
6HMU | X-ray | 1.20 | B | 588-595 | [»] | |
6IAR | X-ray | 1.84 | A | 307-547 | [»] | |
6OWC | X-ray | 1.85 | A/B | 298-554 | [»] | |
6PET | X-ray | 2.20 | A/B/C/D | 298-553 | [»] | |
6PFM | X-ray | 2.84 | A/D | 298-553 | [»] | |
6PIT | X-ray | 2.25 | A/B | 297-554 | [»] | |
6PSJ | X-ray | 1.80 | A/B | 307-554 | [»] | |
6SBO | X-ray | 1.48 | A/B | 297-554 | [»] | |
6SQ0 | X-ray | 1.77 | A/B | 307-554 | [»] | |
6SUO | X-ray | 1.74 | A/B | 307-554 | [»] | |
6TJM | X-ray | 1.85 | B | 588-595 | [»] | |
6TL3 | X-ray | 2.46 | B | 588-595 | [»] | |
6V87 | X-ray | 2.40 | A/B | 307-554 | [»] | |
6V8T | X-ray | 2.10 | A/B | 307-554 | [»] | |
6VGH | X-ray | 2.10 | A/B | 307-554 | [»] | |
6VIG | X-ray | 1.45 | A/B/C/D | 306-554 | [»] | |
6VJ1 | X-ray | 1.68 | A/B/D/E | 306-554 | [»] | |
6VJD | X-ray | 1.80 | A/B/C/D | 307-554 | [»] | |
6VMU | X-ray | 1.70 | A/B/C/D | 307-554 | [»] | |
6VPF | X-ray | 1.60 | A/B/C/D | 306-554 | [»] | |
6VPK | X-ray | 1.70 | A/B/C/D | 306-554 | [»] | |
6VVP | X-ray | 2.60 | A/B/C/D | 306-554 | [»] | |
6WOK | X-ray | 2.31 | A/B/C/D | 298-553 | [»] | |
6ZOQ | X-ray | 1.80 | A/B | 307-554 | [»] | |
6ZOR | X-ray | 1.97 | A/B | 307-554 | [»] | |
6ZOS | X-ray | 2.00 | A/B | 307-554 | [»] | |
7B9M | X-ray | 1.70 | B | 588-595 | [»] | |
7B9R | X-ray | 1.15 | B | 588-595 | [»] | |
7B9T | X-ray | 1.15 | B | 588-595 | [»] | |
7BA3 | X-ray | 1.40 | B | 588-595 | [»] | |
7BA5 | X-ray | 1.45 | B | 588-595 | [»] | |
7BA6 | X-ray | 1.40 | B | 588-595 | [»] | |
7BA7 | X-ray | 1.45 | B | 588-595 | [»] | |
7BA8 | X-ray | 1.20 | B | 588-595 | [»] | |
7BA9 | X-ray | 1.48 | B | 588-595 | [»] | |
7BAA | X-ray | 1.10 | B | 588-595 | [»] | |
7BAB | X-ray | 1.30 | B | 588-595 | [»] | |
7JHD | X-ray | 2.40 | A/B | 305-554 | [»] | |
7KBS | X-ray | 1.83 | A/B | 307-554 | [»] | |
7KCA | X-ray | 1.78 | A/B | 306-554 | [»] | |
7KCD | X-ray | 1.80 | A/B/C/D | 307-554 | [»] | |
7MSA | X-ray | 2.24 | A/B/C/D | 298-553 | [»] | |
7NDO | X-ray | 1.60 | A/B | 304-548 | [»] | |
7NEL | X-ray | 1.45 | A/B | 304-548 | [»] | |
7NFB | X-ray | 1.33 | A/B | 304-548 | [»] | |
7NFW | X-ray | 1.19 | B | 588-595 | [»] | |
7RRX | X-ray | 1.78 | A/B/C/D | 298-554 | [»] | |
7RRY | X-ray | 1.87 | A/B/C/D | 298-554 | [»] | |
7RRZ | X-ray | 1.83 | A/B/C/D | 298-554 | [»] | |
7RS0 | X-ray | 1.67 | A/B/C/D | 298-554 | [»] | |
7RS1 | X-ray | 1.59 | A/B/C/D | 298-554 | [»] | |
7RS2 | X-ray | 1.72 | A/B/C/D | 298-554 | [»] | |
7RS3 | X-ray | 1.84 | A/B/C/D | 298-554 | [»] | |
7RS4 | X-ray | 1.78 | A/B/C/D | 298-554 | [»] | |
7RS7 | X-ray | 1.58 | A/B/C/D | 298-554 | [»] | |
7RS8 | X-ray | 1.64 | A/B/C/D | 298-554 | [»] | |
7RS9 | X-ray | 1.70 | A/B/C/D | 298-554 | [»] | |
SASBDBi | P03372 | |||||
SMRi | P03372 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 108403, 2158 interactors |
ComplexPortali | CPX-5156, ERalpha-NCOA2 activated estrogen receptor complex |
CORUMi | P03372 |
DIPi | DIP-5965N |
ELMi | P03372 |
IntActi | P03372, 1904 interactors |
MINTi | P03372 |
STRINGi | 9606.ENSP00000405330 |
Chemistry databases
BindingDBi | P03372 |
ChEMBLi | CHEMBL206 |
DrugBanki | DB07567, (2R,3R,4S)-3-(4-HYDROXYPHENYL)-4-METHYL-2-[4-(2-PYRROLIDIN-1-YLETHOXY)PHENYL]CHROMAN-6-OL DB07638, (3AS,4R,9BR)-2,2-DIFLUORO-4-(4-HYDROXYPHENYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-8-OL DB08737, (3AS,4R,9BR)-4-(4-HYDROXYPHENYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-9-OL DB08020, (3AS,4R,9BR)-4-(4-HYDROXYPHENYL)-6-(METHOXYMETHYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-8-OL DB07678, (9ALPHA,13BETA,17BETA)-2-[(1Z)-BUT-1-EN-1-YL]ESTRA-1,3,5(10)-TRIENE-3,17-DIOL DB07707, (9BETA,11ALPHA,13ALPHA,14BETA,17ALPHA)-11-(METHOXYMETHYL)ESTRA-1(10),2,4-TRIENE-3,17-DIOL DB03802, 1-[4-(Octahydro-Pyrido[1,2-a]Pyrazin-2-Yl)-Phenyl]-2-Phenyl-1,2,3,4-Tetrahydro-Isoquinolin-6-Ol DB06871, 17-METHYL-17-ALPHA-DIHYDROEQUILENIN DB08773, 2-(4-hydroxyphenyl)benzo[b]thiophen-6-ol DB08398, 2-Amino-1-methyl-6-phenylimidazo(4,5-b)pyridine DB13869, 2-Methoxy-6-{(E)-[(4-methylphenyl)imino]methyl}phenol DB04471, 2-Phenyl-1-[4-(2-Piperidin-1-Yl-Ethoxy)-Phenyl]-1,2,3,4-Tetrahydro-Isoquinolin-6-Ol DB07708, 3-CHLORO-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL DB07712, 3-ETHYL-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL DB06898, 4-(2-amino-1-methyl-1H-imidazo[4,5-b]pyridin-6-yl)phenol DB08048, 4-(6-HYDROXY-1H-INDAZOL-3-YL)BENZENE-1,3-DIOL DB08595, 4-[(1S,2R,5S)-4,4,8-TRIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL DB07195, 4-[(1S,2S,5S)-5-(HYDROXYMETHYL)-6,8,9-TRIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL DB07086, 4-[(1S,2S,5S)-5-(HYDROXYMETHYL)-8-METHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL DB07087, 4-[(1S,2S,5S,9R)-5-(HYDROXYMETHYL)-8,9-DIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL DB08047, 4-[1-allyl-7-(trifluoromethyl)-1H-indazol-3-yl]benzene-1,3-diol DB06927, [5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-YL]ACETONITRILE DB04468, Afimoxifene DB01431, Allylestrenol DB05233, AP1081 DB06249, Arzoxifene DB06401, Bazedoxifene DB01878, Benzophenone DB06732, beta-Naphthoflavone DB05882, CHF 4227 DB00269, Chlorotrianisene DB00882, Clomifene DB02715, Compound 18 DB02615, Compound 19 DB03742, Compound 4-D DB00286, Conjugated estrogens DB05487, Custirsen DB01406, Danazol DB00304, Desogestrel DB00890, Dienestrol DB08320, DIETHYL (1R,2S,3R,4S)-5,6-BIS(4-HYDROXYPHENYL)-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2,3-DICARBOXYLATE DB00255, Diethylstilbestrol DB07932, dimethyl (1R,4S)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]hepta-2,5-diene-2,3-dicarboxylate DB00841, Dobutamine DB06374, Elacestrant DB11219, Enzacamene DB02187, Equilin DB07933, Erteberel DB00783, Estradiol DB13952, Estradiol acetate DB13953, Estradiol benzoate DB13954, Estradiol cypionate DB13955, Estradiol dienanthate DB13956, Estradiol valerate DB01196, Estramustine DB04573, Estriol DB14641, Estriol tripropionate DB00655, Estrone DB04574, Estrone sulfate DB00977, Ethinylestradiol DB00823, Ethynodiol diacetate DB09086, Eugenol DB15690, Fluoroestradiol F-18 DB01185, Fluoxymesterone DB00947, Fulvestrant DB01645, Genistein DB11619, Gestrinone DB00756, Hexachlorophene DB07931, Hexestrol DB11064, Homosalate DB06202, Lasofoxifene DB00367, Levonorgestrel DB00431, Lindane DB00603, Medroxyprogesterone acetate DB01065, Melatonin DB01357, Mestranol DB06710, Methyltestosterone DB00648, Mitotane DB07991, N-[(1R)-3-(4-HYDROXYPHENYL)-1-METHYLPROPYL]-2-(2-PHENYL-1H-INDOL-3-YL)ACETAMIDE DB01183, Naloxone DB03467, Naringenin DB09371, Norethynodrel DB00957, Norgestimate DB05662, NP-50301 DB09535, Octocrylene DB04938, Ospemifene DB01428, Oxybenzone DB04930, Permethrin DB04824, Phenolphthalein DB02746, Phthalic Acid DB09369, Polyestradiol phosphate DB01708, Prasterone DB00396, Progesterone DB12450, Propyl Gallate DB02757, Pyrazole DB04216, Quercetin DB04575, Quinestrol DB11541, Ractopamine DB00481, Raloxifene DB02709, Resveratrol DB02901, Stanolone DB13951, Stanolone acetate DB09317, Synthetic Conjugated Estrogens, A DB09318, Synthetic Conjugated Estrogens, B DB00675, Tamoxifen DB05966, TAS-108 DB00624, Testosterone DB13943, Testosterone cypionate DB13944, Testosterone enanthate DB13946, Testosterone undecanoate DB09070, Tibolone DB00539, Toremifene DB01108, Trilostane DB11478, Zeranol DB01593, Zinc DB14487, Zinc acetate DB14533, Zinc chloride DB14548, Zinc sulfate, unspecified form |
DrugCentrali | P03372 |
GuidetoPHARMACOLOGYi | 620 |
SwissLipidsi | SLP:000001568 |
Protein family/group databases
MoonDBi | P03372, Predicted |
PTM databases
GlyConnecti | 144, 1 O-Linked glycan |
GlyGeni | P03372, 2 sites, 1 O-linked glycan (1 site) |
iPTMneti | P03372 |
PhosphoSitePlusi | P03372 |
SwissPalmi | P03372 |
Genetic variation databases
BioMutai | ESR1 |
DMDMi | 544257 |
Proteomic databases
CPTACi | CPTAC-1241 CPTAC-145 |
EPDi | P03372 |
jPOSTi | P03372 |
MassIVEi | P03372 |
PaxDbi | P03372 |
PeptideAtlasi | P03372 |
PRIDEi | P03372 |
ProteomicsDBi | 51607 [P03372-1] 51608 [P03372-2] 51609 [P03372-3] 51610 [P03372-4] |
Protocols and materials databases
ABCDi | P03372, 5 sequenced antibodies |
Antibodypediai | 739, 4120 antibodies from 53 providers |
DNASUi | 2099 |
Genome annotation databases
Ensembli | ENST00000206249; ENSP00000206249; ENSG00000091831 ENST00000338799; ENSP00000342630; ENSG00000091831 ENST00000440973; ENSP00000405330; ENSG00000091831 ENST00000443427; ENSP00000387500; ENSG00000091831 |
GeneIDi | 2099 |
KEGGi | hsa:2099 |
MANE-Selecti | ENST00000206249.8; ENSP00000206249.3; NM_000125.4; NP_000116.2 |
UCSCi | uc003qom.5, human [P03372-1] |
Organism-specific databases
CTDi | 2099 |
DisGeNETi | 2099 |
GeneCardsi | ESR1 |
HGNCi | HGNC:3467, ESR1 |
HPAi | ENSG00000091831, Tissue enhanced (cervix, endometrium, fallopian tube) |
MalaCardsi | ESR1 |
MIMi | 133430, gene 615363, phenotype |
neXtProti | NX_P03372 |
OpenTargetsi | ENSG00000091831 |
Orphaneti | 785, Estrogen resistance syndrome |
PharmGKBi | PA156 |
VEuPathDBi | HostDB:ENSG00000091831 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3575, Eukaryota |
GeneTreei | ENSGT00940000158133 |
InParanoidi | P03372 |
OMAi | NRPYTEV |
OrthoDBi | 487299at2759 |
PhylomeDBi | P03372 |
TreeFami | TF323751 |
Enzyme and pathway databases
PathwayCommonsi | P03372 |
Reactomei | R-HSA-1251985, Nuclear signaling by ERBB4 R-HSA-1257604, PIP3 activates AKT signaling R-HSA-2219530, Constitutive Signaling by Aberrant PI3K in Cancer R-HSA-383280, Nuclear Receptor transcription pathway R-HSA-4090294, SUMOylation of intracellular receptors R-HSA-5689896, Ovarian tumor domain proteases R-HSA-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling R-HSA-8866910, TFAP2 (AP-2) family regulates transcription of growth factors and their receptors R-HSA-8931987, RUNX1 regulates estrogen receptor mediated transcription R-HSA-8939211, ESR-mediated signaling R-HSA-8939256, RUNX1 regulates transcription of genes involved in WNT signaling R-HSA-8939902, Regulation of RUNX2 expression and activity R-HSA-9009391, Extra-nuclear estrogen signaling R-HSA-9018519, Estrogen-dependent gene expression |
SignaLinki | P03372 |
SIGNORi | P03372 |
Miscellaneous databases
BioGRID-ORCSi | 2099, 23 hits in 1063 CRISPR screens |
ChiTaRSi | ESR1, human |
EvolutionaryTracei | P03372 |
GeneWikii | Estrogen_receptor_alpha |
GenomeRNAii | 2099 |
Pharosi | P03372, Tclin |
PROi | PR:P03372 |
RNActi | P03372, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000091831, Expressed in endometrium and 168 other tissues |
ExpressionAtlasi | P03372, baseline and differential |
Genevisiblei | P03372, HS |
Family and domain databases
DisProti | DP00074 |
Gene3Di | 1.10.565.10, 1 hit 3.30.50.10, 1 hit |
IDEALi | IID00013 |
InterProi | View protein in InterPro IPR024178, Est_rcpt/est-rel_rcp IPR001292, Estr_rcpt IPR035500, NHR-like_dom_sf IPR000536, Nucl_hrmn_rcpt_lig-bd IPR001723, Nuclear_hrmn_rcpt IPR024736, Oestrogen-typ_rcpt_final_C_dom IPR001628, Znf_hrmn_rcpt IPR013088, Znf_NHR/GATA |
Pfami | View protein in Pfam PF12743, ESR1_C, 1 hit PF00104, Hormone_recep, 1 hit PF02159, Oest_recep, 1 hit PF00105, zf-C4, 1 hit |
PIRSFi | PIRSF500101, ER-a, 1 hit PIRSF002527, ER-like_NR, 1 hit |
PRINTSi | PR00543, OESTROGENR PR00398, STRDHORMONER PR00047, STROIDFINGER |
SMARTi | View protein in SMART SM00430, HOLI, 1 hit SM00399, ZnF_C4, 1 hit |
SUPFAMi | SSF48508, SSF48508, 1 hit |
PROSITEi | View protein in PROSITE PS51843, NR_LBD, 1 hit PS00031, NUCLEAR_REC_DBD_1, 1 hit PS51030, NUCLEAR_REC_DBD_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ESR1_HUMAN | |
Accessioni | P03372Primary (citable) accession number: P03372 Secondary accession number(s): Q13511 Q9UIS7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | June 1, 1994 | |
Last modified: | February 23, 2022 | |
This is version 280 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 6
Human chromosome 6: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families