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UniProtKB - P03372 (ESR1_HUMAN)

Protein

Estrogen receptor

Gene

ESR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. 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. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3. Isoform 3 can bind to ERE and inhibit isoform 1.20 Publications

Miscellaneous

Selective estrogen receptor modulators (SERMs), such as tamoxifen, raloxifene, toremifene, lasofoxifene, clomifene, femarelle and ormeloxifene, have tissue selective agonistic and antagonistic effects on the estrogen receptor (ER). They interfere with the ER association with coactivators or corepressors, mainly involving the AF-2 domain.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi185 – 250Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri185 – 205NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri221 – 245NR C4-typePROSITE-ProRule annotationAdd BLAST25

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding, Receptor
Biological processTranscription, Transcription regulation
LigandLipid-binding, Metal-binding, Steroid-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...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-9018519 Estrogen-dependent gene expression

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P03372

SIGNOR Signaling Network Open Resource

More...SIGNORi		P03372

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		P03372 Predicted

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001568

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Estrogen receptor
Short name:
ER
Alternative name(s):
ER-alpha
Estradiol receptor
Nuclear receptor subfamily 3 group A member 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ESR1
Synonyms:ESR, NR3A1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000091831.21

Human Gene Nomenclature Database

More...HGNCi		HGNC:3467 ESR1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		133430 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P03372

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Estrogen resistance (ESTRR)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by partial or complete resistance to estrogens, in the presence of elevated estrogen serum levels. Clinical features include absence of the pubertal growth spurt, delayed bone maturation, unfused epiphyses, reduced bone mineral density, osteoporosis, continued growth into adulthood and very tall adult stature. Glucose intolerance, hyperinsulinemia and lipid abnormalities may also be present.
See also OMIM:615363
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070072375Q → H in ESTRR; results in highly reduced activity. 1 PublicationCorresponds to variant dbSNP:rs397509428EnsemblClinVar.1
Natural variantiVAR_078516394R → H in ESTRR; highly decreased estrogen receptor activity. 1 PublicationCorresponds to variant dbSNP:rs1131692059Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi39L → P: Impairs AF-1 transactivation. 1 Publication1
Mutagenesisi43Y → P: Impairs AF-1 transactivation. 1 Publication1
Mutagenesisi104S → A: Loss of cyclin A-dependent induction of transcriptional activation. 1
Mutagenesisi106S → A: Loss of cyclin A-dependent induction of transcriptional activation. 1
Mutagenesisi118S → A: Decreases phosphorylation and transactivation activity. Abolishes AF-1 transactivation. Insensitive to PPP5C inhibition of transactivation activity. 2 Publications1
Mutagenesisi118S → E: Enhances transactivation activity. Enhances interaction with DDX5. Insensitive to PPP5C inhibition of transactivation activity. 2 Publications1
Mutagenesisi260R → A or K: Loss of methylation. 1 Publication1
Mutagenesisi364V → E: Has higher transcriptional activity in the absence of wild type ER. Inhibits transcriptional activity when coexpressed with the wild type receptor. 1 Publication1
Mutagenesisi386I → 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 Publication1
Mutagenesisi447C → A: Loss of hormone binding capacity and temperature-sensitive loss in DNA-binding. 1 Publication1
Mutagenesisi539L → A: Abolishes interaction with NCOA1, NCOA2 and NCOA3. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		2099

MalaCards human disease database

More...MalaCardsi		ESR1
MIMi615363 phenotype

Open Targets

More...OpenTargetsi		ENSG00000091831

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		785 Estrogen resistance syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA156

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL206

Drug and drug target database

More...DrugBanki		DB06871 17-METHYL-17-ALPHA-DIHYDROEQUILENIN
DB07708 3-CHLORO-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL
DB07712 3-ETHYL-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL
DB06927 [5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-YL]ACETONITRILE
DB04468 Afimoxifene
DB01431 Allylestrenol
DB05233 AP1081
DB05338 atamestane-plus-toremifene
DB06401 Bazedoxifene
DB05487 CC-8490
DB05882 CHF 4227
DB00269 Chlorotrianisene
DB00882 Clomifene
DB02715 Compound 18
DB02615 Compound 19
DB03742 Compound 4-D
DB00286 Conjugated Equine Estrogens
DB01406 Danazol
DB00304 Desogestrel
DB00890 Dienestrol
DB00255 Diethylstilbestrol
DB00783 Estradiol
DB01196 Estramustine
DB04573 Estriol
DB00655 Estrone
DB04574 Estrone sulfate
DB00977 Ethinyl Estradiol
DB00823 Ethynodiol diacetate
DB00294 Etonogestrel
DB01185 Fluoxymesterone
DB00947 Fulvestrant
DB01645 Genistein
DB06202 Lasofoxifene
DB00367 Levonorgestrel
DB00603 Medroxyprogesterone acetate
DB01065 Melatonin
DB01357 Mestranol
DB07991 N-[(1R)-3-(4-HYDROXYPHENYL)-1-METHYLPROPYL]-2-(2-PHENYL-1H-INDOL-3-YL)ACETAMIDE
DB01183 Naloxone
DB00957 Norgestimate
DB05662 NP-50301
DB04938 Ospemifene
DB01708 Prasterone
DB00396 Progesterone
DB04575 Quinestrol
DB00481 Raloxifene
DB08773 RALOXIFENE CORE
DB00675 Tamoxifen
DB09070 Tibolone
DB00539 Toremifene
DB01108 Trilostane

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		620

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ESR1

Domain mapping of disease mutations (DMDM)

More...DMDMi		544257

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000536181 – 595Estrogen receptorAdd BLAST595

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi10O-linked (GlcNAc) serineBy similarity1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei104Phosphoserine; by CDK21 Publication1
Modified residuei106Phosphoserine; by CDK21 Publication1
Modified residuei118Phosphoserine1 Publication1
Modified residuei167Phosphoserine; by CK21 Publication1
Modified residuei260Asymmetric dimethylarginine; by PRMT11 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi447S-palmitoyl cysteineBy similarity1
Modified residuei537Phosphotyrosine; by Tyr-kinases1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably enhances transcriptional activity. Self-association induces phosphorylation. Dephosphorylation at Ser-118 by PPP5C inhibits its transactivation activity. Phosphorylated by LMTK3 in vitro.7 Publications
Glycosylated; contains N-acetylglucosamine, probably O-linked.1 Publication
Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1 proteasomal degradation (PubMed:21602804, PubMed:28068668). Deubiquitinated by OTUB1 (PubMed:19383985).3 Publications
Dimethylated by PRMT1 at Arg-260. The methylation may favor cytoplasmic localization.1 Publication
Palmitoylated (isoform 3). Not biotinylated (isoform 3).1 Publication
Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation, but not for signaling mediated by the nuclear hormone receptor.1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Methylation, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P03372

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P03372

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P03372

PeptideAtlas

More...PeptideAtlasi		P03372

PRoteomics IDEntifications database

More...PRIDEi		P03372

ProteomicsDB human proteome resource

More...ProteomicsDBi		51607
51608 [P03372-2]
51609 [P03372-3]
51610 [P03372-4]

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		144

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P03372

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P03372

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P03372

UniCarbKB; an annotated and curated database of glycan structures

More...UniCarbKBi		P03372

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed. Isoform 3 is not expressed in the pituitary gland.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000091831 Expressed in 152 organ(s), highest expression level in endometrium

CleanEx database of gene expression profiles

More...CleanExi		HS_ESR1

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P03372 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P03372 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB000037
CAB055099
CAB072858
HPA000449
HPA000450

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Binds DNA as a homodimer. Can form a heterodimer with ESR2. Isoform 3 can probably homodimerize or heterodimerize with isoform 1 and ESR2. Interacts with FOXC2, MAP1S, SLC30A9, UBE1C and NCOA3 coactivator (By similarity). 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, PELP1 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 ERS1-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 PI3KR1 or PI3KR2, SRC and PTK2/FAK1. 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. 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).By similarity60 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-78473,EBI-78473
AKAP13Q128023EBI-78473,EBI-1373806
ARID5AQ039899EBI-78473,EBI-948603
ASF1AQ9Y2942EBI-78473,EBI-749553
ASXL1Q8IXJ92EBI-78473,EBI-1646500
Asxl1P595982EBI-78473,EBI-5743705From Mus musculus.
ATAD2Q6PL183EBI-78473,EBI-6598454
BLCAPP629522EBI-78473,EBI-3895726
BRCA1P3839812EBI-78473,EBI-349905
BTF3P20290-25EBI-78473,EBI-1054703
CACUL1Q86Y375EBI-78473,EBI-8168227
CITED1Q999663EBI-78473,EBI-2624951
CTGFP292797EBI-78473,EBI-2835375
CUEDC2Q9H4672EBI-78473,EBI-1248228
DNM1LO004292EBI-78473,EBI-724571
EGFRP005334EBI-4309277,EBI-297353
EP300Q094722EBI-78473,EBI-447295
ESR2Q927315EBI-15606245,EBI-78505
FOXO1Q127782EBI-78473,EBI-1108782
GRIP1Q9Y3R02EBI-78473,EBI-5349621
HAX1O001652EBI-78473,EBI-357001
JMJD6Q6NYC18EBI-78473,EBI-8464037
JunP056276EBI-78473,EBI-764369From Mus musculus.
KAT5Q929933EBI-15606245,EBI-399080
KDM6BO150542EBI-78473,EBI-2831260
KMT2DO146863EBI-78473,EBI-996065
LMTK3Q96Q043EBI-78473,EBI-720814
MACROD1Q9BQ696EBI-78473,EBI-5324932
MDM2Q009872EBI-78473,EBI-389668
MYL6P606603EBI-78473,EBI-300817
NCOA1Q157888EBI-78473,EBI-455189
NCOA2Q155965EBI-78473,EBI-81236
NCOA3Q9Y6Q94EBI-78473,EBI-81196
Ncoa6Q9JLI42EBI-78473,EBI-286271From Rattus norvegicus.
NDRG2Q9UN362EBI-78473,EBI-3895741
NFKB1P198383EBI-78473,EBI-697771
NR1H4Q96RI1-32EBI-78473,EBI-10921781
PAGR1Q9BTK65EBI-78473,EBI-2372223
PBXIP1Q96AQ6-15EBI-15606245,EBI-15606280
Pfn1P629623EBI-78473,EBI-647096From Mus musculus.
PGRP0640120EBI-78473,EBI-78539
PGRP06401-14EBI-78473,EBI-12590474
PHB2Q996234EBI-78473,EBI-358348
PIK3R1P279867EBI-78473,EBI-79464
PPP5CP530414EBI-78473,EBI-716663
PRMT2P553459EBI-78473,EBI-78458
RAC3P607635EBI-78473,EBI-767084
RBFOX2O432514EBI-78473,EBI-746056
RELAQ042067EBI-78473,EBI-73886
SAFB2Q141512EBI-78473,EBI-352869
SENP5Q96HI02EBI-78473,EBI-3895753
SHC1P293532EBI-4309277,EBI-78835
SP1P080472EBI-78473,EBI-298336
SP3Q024472EBI-78473,EBI-348158
SRCP005232EBI-78473,EBI-848039From Gallus gallus.
SRCP1293112EBI-78473,EBI-621482
TRIM24O151643EBI-78473,EBI-2130378
TXNRD1Q16881-44EBI-78473,EBI-9080335
UXTQ9UBK92EBI-78473,EBI-357355
ZNF366Q8N8956EBI-78473,EBI-2813661

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108403, 737 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P03372

Database of interacting proteins

More...DIPi		DIP-5965N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P03372

Protein interaction database and analysis system

More...IntActi		P03372, 478 interactors

Molecular INTeraction database

More...MINTi		P03372

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000206249

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P03372

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1595
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A52X-ray2.80A/B297-554[»]
1AKFmodel-A309-547[»]
1EREX-ray3.10A/B/C/D/E/F301-553[»]
1ERRX-ray2.60A/B301-553[»]
1G50X-ray2.90A/B/C304-550[»]
1GWQX-ray2.45A/B301-548[»]
1GWRX-ray2.40A/B305-549[»]
1HCPNMR-A180-254[»]
1HCQX-ray2.40A/B/E/F180-262[»]
1L2IX-ray1.95A/B297-554[»]
1PCGX-ray2.70A/B304-547[»]
1QKTX-ray2.20A304-551[»]
1QKUX-ray3.20A/B/C301-550[»]
1R5KX-ray2.70A/B/C297-554[»]
1SJ0X-ray1.90A307-554[»]
1UOMX-ray2.28A301-553[»]
1X7EX-ray2.80A/B305-549[»]
1X7RX-ray2.00A305-549[»]
1XP1X-ray1.80A307-554[»]
1XP6X-ray1.70A307-554[»]
1XP9X-ray1.80A307-554[»]
1XPCX-ray1.60A307-554[»]
1XQCX-ray2.05A/B/C/D301-553[»]
1YIMX-ray1.90A307-554[»]
1YINX-ray2.20A307-554[»]
1ZKYX-ray2.25A/B298-554[»]
2AYRX-ray1.90A304-551[»]
2B1VX-ray1.80A/B298-554[»]
2B1ZX-ray1.78A/B298-554[»]
2B23X-ray2.10A/B298-554[»]
2BJ4X-ray2.00A/B305-533[»]
2FAIX-ray2.10A/B298-554[»]
2G44X-ray2.65A/B298-554[»]
2G5OX-ray2.30A/B298-554[»]
2I0JX-ray2.90A/B/C/D304-547[»]
2IOGX-ray1.60A309-554[»]
2IOKX-ray2.40A/B301-554[»]
2JF9X-ray2.10A/B/C304-533[»]
2JFAX-ray2.55A/B304-533[»]
2LLONMR-B287-305[»]
2LLQNMR-B287-305[»]
2OCFX-ray2.95A298-595[»]
2OUZX-ray2.00A301-553[»]
2P15X-ray1.94A/B298-554[»]
2POGX-ray1.84A/B304-551[»]
2Q6JX-ray2.70A/B298-554[»]
2Q70X-ray1.95A/B304-551[»]
2QA6X-ray2.60A/B298-554[»]
2QA8X-ray1.85A/B298-554[»]
2QABX-ray1.89A/B298-554[»]
2QE4X-ray2.40A/B304-551[»]
2QGTX-ray2.15A/B298-554[»]
2QGWX-ray2.39A/B298-554[»]
2QH6X-ray2.70A/B298-554[»]
2QR9X-ray2.00A/B298-554[»]
2QSEX-ray1.85A/B298-554[»]
2QXMX-ray2.30A/B298-554[»]
2QXSX-ray1.70A/B298-554[»]
2QZOX-ray1.72A/B298-554[»]
2R6WX-ray2.00A/B304-551[»]
2R6YX-ray2.00A/B304-551[»]
2YATX-ray2.60A301-551[»]
2YJAX-ray1.82B299-551[»]
3CBMX-ray1.69B298-307[»]
3CBOX-ray1.65B298-307[»]
3CBPX-ray1.42B298-307[»]
3DT3X-ray2.40A/B299-551[»]
3ERDX-ray2.03A/B297-554[»]
3ERTX-ray1.90A297-554[»]
3HLVX-ray3.00A/B298-550[»]
3HM1X-ray2.33A/B298-550[»]
3L03X-ray1.90A/B298-550[»]
3OS8X-ray2.03A/B/C/D299-553[»]
3OS9X-ray2.30A/B/C/D299-553[»]
3OSAX-ray2.30A/B/C/D299-553[»]
3Q95X-ray2.05A/B298-554[»]
3UU7X-ray2.20A/B302-552[»]
3UUAX-ray2.05A/B302-552[»]
3UUCX-ray2.10A/B/C/D302-552[»]
3UUDX-ray1.60A/B302-552[»]
4AA6X-ray2.60A/B/E/F182-252[»]
4DMAX-ray2.30A/B303-549[»]
4IU7X-ray2.29A/B303-549[»]
4IUIX-ray2.30A/B303-549[»]
4IV2X-ray2.14A/B303-549[»]
4IV4X-ray2.30A/B303-549[»]
4IVWX-ray2.06A/B303-549[»]
4IVYX-ray1.95A/B303-549[»]
4IW6X-ray1.98A/B303-549[»]
4IW8X-ray2.04A/B303-549[»]
4IWCX-ray2.24A/B303-549[»]
4IWFX-ray1.93A/B303-549[»]
4JC3X-ray2.05B585-595[»]
4JDDX-ray2.10B585-595[»]
4MG5X-ray2.05A/B302-552[»]
4MG6X-ray2.10A/B302-552[»]
4MG7X-ray2.15A/B302-552[»]
4MG8X-ray1.85A/B302-552[»]
4MG9X-ray2.00A/B302-552[»]
4MGAX-ray1.80A/B302-552[»]
4MGBX-ray1.85A/B302-552[»]
4MGCX-ray2.15A/B302-552[»]
4MGDX-ray1.90A/B302-552[»]
4O6FX-ray2.82B261-271[»]
4PP6X-ray2.20A/B305-548[»]
4PPPX-ray2.69A/B305-548[»]
4PPSX-ray1.93A/B305-548[»]
4PXMX-ray1.90A/B299-554[»]
4Q13X-ray2.24A/B299-554[»]
4Q50X-ray3.07A/B/C/D/E/F/G/H299-554[»]
4TUZX-ray1.90A/B302-552[»]
4TV1X-ray1.85A/B302-552[»]
4XI3X-ray2.49A/B/C/D306-548[»]
4ZN7X-ray1.93A/B301-559[»]
4ZN9X-ray2.21A/B301-559[»]
4ZNHX-ray1.93A/B301-559[»]
4ZNSX-ray1.86A/B301-559[»]
4ZNTX-ray1.90A/B301-559[»]
4ZNUX-ray2.40A/B301-559[»]
4ZNVX-ray1.77A/B301-559[»]
4ZNWX-ray2.31A/B301-559[»]
5AAUX-ray1.90A/B307-554[»]
5AAVX-ray1.95A307-554[»]
B306-554[»]
5ACCX-ray1.88A307-554[»]
5AK2X-ray2.19A/B307-554[»]
5DI7X-ray2.24A/B298-554[»]
5DIDX-ray2.24A/B298-554[»]
5DIEX-ray2.24A/B298-554[»]
5DIGX-ray2.24A/B298-554[»]
5DK9X-ray2.28A/B298-554[»]
5DKBX-ray2.40A/B298-554[»]
5DKEX-ray2.60A/B298-554[»]
5DKGX-ray2.15A/B298-554[»]
5DKSX-ray2.60A/B298-554[»]
5DL4X-ray2.10A/B298-554[»]
5DLRX-ray2.26A/B298-554[»]
5DMCX-ray2.40A/B298-554[»]
5DMFX-ray2.40A/B298-554[»]
5DP0X-ray2.38A/B298-554[»]
5DRJX-ray2.07A/B298-554[»]
5DRMX-ray2.24A/B298-554[»]
5DTVX-ray2.29A/B298-554[»]
5DU5X-ray2.19A/B298-554[»]
5DUEX-ray2.09A/B298-554[»]
5DUGX-ray2.25A/B298-554[»]
5DUHX-ray2.24A/B298-554[»]
5DVSX-ray2.28A/B298-554[»]
5DVVX-ray2.50A/B298-554[»]
5DWEX-ray1.92A/B298-554[»]
5DWGX-ray2.30A/B298-554[»]
5DWIX-ray2.43A/B298-554[»]
5DWJX-ray2.00A/B298-554[»]
5DX3X-ray2.09A/B297-554[»]
5DXBX-ray2.08A/B297-554[»]
5DXEX-ray1.50A/B297-554[»]
5DXGX-ray1.86A/B297-554[»]
5DXKX-ray2.23A/B298-554[»]
5DXMX-ray2.37A/B298-554[»]
5DXPX-ray2.20A/B298-554[»]
5DXQX-ray2.40A/B298-554[»]
5DXRX-ray2.28A/B298-554[»]
5DY8X-ray2.03A/B298-554[»]
5DYBX-ray2.27A/B298-554[»]
5DYDX-ray2.48A/B298-554[»]
5DZ0X-ray2.24A/B298-554[»]
5DZ1X-ray2.20A/B298-554[»]
5DZ3X-ray2.15A/B298-554[»]
5DZHX-ray2.11A/B298-554[»]
5DZIX-ray1.90A/B298-554[»]
5E0WX-ray2.00A/B298-554[»]
5E0XX-ray2.01A/B298-554[»]
5E14X-ray2.22A/B298-554[»]
5E15X-ray2.10A/B298-554[»]
5E19X-ray2.24A/B298-554[»]
5E1CX-ray1.98A/B298-554[»]
5EGVX-ray2.86A/B298-554[»]
5EHJX-ray2.50A/B298-554[»]
5EI1X-ray2.40A/B298-554[»]
5EITX-ray2.68A/B298-554[»]
5FQPX-ray1.88A307-554[»]
5FQRX-ray1.88A307-554[»]
5FQSX-ray1.94A307-554[»]
5FQTX-ray1.99A307-554[»]
5FQVX-ray1.74A307-554[»]
5GS4X-ray2.40A305-547[»]
5GTRX-ray2.80A305-547[»]
5HYRX-ray2.27A/B302-559[»]
5JMMX-ray2.10A/B302-552[»]
5KCCX-ray2.39A/B298-554[»]
A/B304-549[»]
5KCDX-ray1.82A/B298-554[»]
A/B305-549[»]
5KCEX-ray1.85A/B298-554[»]
A/B303-549[»]
5KCFX-ray2.07A/B298-554[»]
A/B303-549[»]
5KCTX-ray1.60A/B298-554[»]
A/B303-548[»]
5KCUX-ray2.03A/B298-554[»]
A/B303-548[»]
5KCWX-ray1.91A/B303-549[»]
A/B298-554[»]
5KD9X-ray1.78A/B298-554[»]
A/B303-549[»]
5KR9X-ray2.25A/B298-554[»]
5KRAX-ray2.40A/B/E/F298-554[»]
5KRCX-ray2.40A/B298-554[»]
5KRFX-ray2.19A/B298-554[»]
5KRHX-ray2.24A/B298-554[»]
5KRIX-ray2.25A/B298-554[»]
5KRJX-ray2.70A/B298-554[»]
5KRKX-ray2.39A/B298-554[»]
5KRLX-ray2.40A/B298-554[»]
5KRMX-ray2.24A/B298-554[»]
5KROX-ray2.10A/B298-554[»]
5N10X-ray1.60C/D/F584-595[»]
5T0XNMR-B/C287-305[»]
5T1ZX-ray2.10A/B298-554[»]
5T92X-ray2.22A/B301-553[»]
5T97X-ray3.00A/B301-553[»]
5TLDX-ray2.38A/B298-554[»]
5TLFX-ray2.20A/B298-554[»]
5TLGX-ray2.23A/B298-554[»]
5TLLX-ray2.42A/B298-554[»]
5TLMX-ray2.50A/B298-554[»]
5TLOX-ray2.28A/B298-554[»]
5TLPX-ray2.08A/B298-554[»]
5TLTX-ray1.90A/B298-554[»]
5TLUX-ray2.22A/B298-554[»]
5TLVX-ray2.32A/B298-554[»]
5TLXX-ray2.10A/B298-554[»]
5TLYX-ray2.14A/B298-554[»]
5TM1X-ray2.23A/B298-554[»]
5TM2X-ray2.60A/B298-554[»]
5TM3X-ray2.19A/B298-554[»]
5TM4X-ray2.25A/B298-554[»]
5TM5X-ray2.24A/B298-554[»]
5TM6X-ray2.54A/B298-554[»]
5TM7X-ray2.40A/B298-554[»]
5TM8X-ray1.99A/B298-554[»]
5TM9X-ray2.50A/B298-554[»]
5TMLX-ray2.25A/B298-554[»]
5TMMX-ray2.20A/B298-554[»]
5TMOX-ray2.17A/B298-554[»]
5TMQX-ray2.24A/B298-554[»]
5TMRX-ray2.30A/B298-554[»]
5TMSX-ray2.24A/B298-554[»]
5TMTX-ray2.05A/B298-554[»]
5TMUX-ray2.43A/B298-554[»]
5TMVX-ray2.38A/B298-554[»]
5TMWX-ray2.29A/B298-554[»]
5TMZX-ray2.21A/B298-554[»]
5TN1X-ray2.06A/B298-554[»]
5TN3X-ray2.54A/B298-554[»]
5TN4X-ray1.86A/B298-554[»]
5TN5X-ray1.89A/B298-554[»]
5TN6X-ray2.09A/B298-554[»]
5TN7X-ray2.24A/B298-554[»]
5TN8X-ray2.65A/B298-554[»]
5TN9X-ray2.25A/B/C/D298-554[»]
5TNBX-ray2.08A/B/C/D298-554[»]
5U2BX-ray2.22A/B/C/D/E/F298-554[»]
5U2DX-ray1.86A/B298-554[»]
5UFWX-ray1.58A/B306-554[»]
5UFXX-ray1.55A/B306-554[»]
5W9CX-ray1.80A/B/C/D306-554[»]
5W9DX-ray1.65A/B306-554[»]
5WGDX-ray1.80A/B297-554[»]
5WGQX-ray2.30A/B297-554[»]
6B0FX-ray2.86A/B301-553[»]
6C42X-ray2.00A/B307-554[»]
6CBZX-ray1.65A/B305-554[»]
6CHWX-ray1.89A306-551[»]
6CHZX-ray1.68A307-554[»]

Database of protein disorder

More...DisProti		DP00074

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P03372

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P03372

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P03372

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini311 – 547NR LBDPROSITE-ProRule annotationAdd BLAST237

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 184Modulating (transactivation AF-1); mediates interaction with MACROD11 PublicationAdd BLAST184
Regioni35 – 174Interaction with DDX5; self-associationAdd BLAST140
Regioni35 – 47Required for interaction with NCOA1Add BLAST13
Regioni185 – 310Mediates interaction with DNTTIP21 PublicationAdd BLAST126
Regioni251 – 310HingeAdd BLAST60
Regioni262 – 595Interaction with AKAP131 PublicationAdd BLAST334
Regioni264 – 595Self-associationAdd BLAST332
Regioni311 – 595Transactivation AF-2Add BLAST285

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. The modulating domain, also known as A/B or AF-1 domain has a ligand-independent transactivation function. The C-terminus contains a ligand-dependent transactivation domain, also known as E/F or AF-2 domain which overlaps with the ligand binding domain. AF-1 and AF-2 activate transcription independently and synergistically and act in a promoter- and cell-specific manner. AF-1 seems to provide the major transactivation function in differentiated cells.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the nuclear hormone receptor family. NR3 subfamily.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri185 – 205NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri221 – 245NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Transmembrane, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3575 Eukaryota
ENOG410XRZC LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000158133

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG108344

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P03372

KEGG Orthology (KO)

More...KOi		K08550

Identification of Orthologs from Complete Genome Data

More...OMAi		HSQQVPY

Database of Orthologous Groups

More...OrthoDBi		926074at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P03372

TreeFam database of animal gene trees

More...TreeFami		TF323751

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.50.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR035500 NHR_like_dom_sf
IPR000536 Nucl_hrmn_rcpt_lig-bd
IPR001723 Nuclear_hrmn_rcpt
IPR024178 Oest_rcpt/oest-rel_rcp
IPR001292 Oestr_rcpt
IPR024736 Oestrogen-typ_rcpt_final_C_dom
IPR001628 Znf_hrmn_rcpt
IPR013088 Znf_NHR/GATA

Pfam protein domain database

More...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

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF500101 ER-a, 1 hit
PIRSF002527 ER-like_NR, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00543 OESTROGENR
PR00398 STRDHORMONER
PR00047 STROIDFINGER

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00430 HOLI, 1 hit
SM00399 ZnF_C4, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48508 SSF48508, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51843 NR_LBD, 1 hit
PS00031 NUCLEAR_REC_DBD_1, 1 hit
PS51030 NUCLEAR_REC_DBD_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P03372-1) [UniParc]FASTAAdd to basket
Also known as: Long, hER-alpha66, ER66

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        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
Length:595
Mass (Da):66,216
Last modified:June 1, 1994 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5455C57AB0CCCAA7
GO
Isoform 2 (identifier: P03372-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     255-366: Missing.

Note: No experimental confirmation available.
Show »
Length:483
Mass (Da):53,687
Checksum:i449BC03EF22E80A5
GO
Isoform 3 (identifier: P03372-3) [UniParc]FASTAAdd to basket
Also known as: hER-alpha46, ER46

The sequence of this isoform differs from the canonical sequence as follows:
     1-173: Missing.

Note: Produced by alternative promoter usage.
Show »
Length:422
Mass (Da):47,629
Checksum:iC51DF9A9644127C0
GO
Isoform 4 (identifier: P03372-4) [UniParc]FASTAAdd to basket
Also known as: hER-alpha36, ER36

The sequence of this isoform differs from the canonical sequence as follows:
     1-173: Missing.
     458-595: VYTFLSSTLK...GEAEGFPATV → FTISHVEAKKRILNLHPKIFGNKWFPRV

Note: Produced by alternative splicing of isoform 3.
Show »
Length:312
Mass (Da):35,547
Checksum:i85C8DEAD873F9AEC
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y4W6H0Y4W6_HUMAN
Estrogen receptor
ESR1
310Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q9H2M1Q9H2M1_HUMAN
Estrogen receptor alpha
ESR1
334Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B0QYW7B0QYW7_HUMAN
Estrogen receptor
ESR1
107Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q9UE35Q9UE35_HUMAN
Estrogen receptor protein
ESR1 estrogen receptor
115Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q9H2M2Q9H2M2_HUMAN
Estrogen receptor alpha
ESR1
152Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5T5H8Q5T5H8_HUMAN
Estrogen receptor
ESR1
84Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1W2PP92A0A1W2PP92_HUMAN
Estrogen receptor
ESR1
44Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB00115 differs from that shown. contains an in-frame duplication of exons 6 and 7.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti452I → L in CAE45969 (PubMed:17974005).Curated1

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Genetic variations in ESR1 are correlated with bone mineral density (BMD). Low BMD is a risk factor for osteoporotic fracture. Osteoporosis is characterized by reduced bone mineral density, disruption of bone microarchitecture, and the alteration of the amount and variety of non-collagenous proteins in bone. Osteoporotic bones are more at risk of fracture.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0330286H → Y in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs139960913Ensembl.1
Natural variantiVAR_01890577G → S. Corresponds to variant dbSNP:rs9340773Ensembl.1
Natural variantiVAR_004671160G → C1 PublicationCorresponds to variant dbSNP:rs149308960Ensembl.1
Natural variantiVAR_033029264M → I in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_070072375Q → H in ESTRR; results in highly reduced activity. 1 PublicationCorresponds to variant dbSNP:rs397509428EnsemblClinVar.1
Natural variantiVAR_078516394R → H in ESTRR; highly decreased estrogen receptor activity. 1 PublicationCorresponds to variant dbSNP:rs1131692059Ensembl.1
Natural variantiVAR_004673400G → V Destabilizes the receptor and decreases its affinity for estradiol at 25 degrees Celsius, but not at 4 degrees Celsius. 3 Publications1
Natural variantiVAR_010143411D → 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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0424601 – 173Missing in isoform 3 and isoform 4. 2 PublicationsAdd BLAST173
Alternative sequenceiVSP_003680255 – 366Missing in isoform 2. 1 PublicationAdd BLAST112
Alternative sequenceiVSP_042461458 – 595VYTFL…FPATV → FTISHVEAKKRILNLHPKIF GNKWFPRV in isoform 4. 2 PublicationsAdd BLAST138

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X03635 mRNA Translation: CAA27284.1
M12674 mRNA Translation: AAA52399.1
U47678 mRNA Translation: AAB00115.1 Sequence problems.
AY425004 Genomic DNA Translation: AAQ91815.1
BX640939 mRNA Translation: CAE45969.1
AL049821 Genomic DNA No translation available.
AL078582 Genomic DNA No translation available.
AL356311 Genomic DNA No translation available.
AL590993 Genomic DNA No translation available.
CH471051 Genomic DNA Translation: EAW47740.1
BC128573 mRNA Translation: AAI28574.1
BC128574 mRNA Translation: AAI28575.1
AH008151 Genomic DNA Translation: AAD52984.1
X73067 mRNA Translation: CAA51528.1
Z75126 mRNA Translation: CAA99436.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS5234.1 [P03372-1]

Protein sequence database of the Protein Information Resource

More...PIRi		S64737

NCBI Reference Sequences

More...RefSeqi		NP_000116.2, NM_000125.3 [P03372-1]
NP_001116212.1, NM_001122740.1 [P03372-1]
NP_001116213.1, NM_001122741.1 [P03372-1]
NP_001116214.1, NM_001122742.1 [P03372-1]
NP_001278159.1, NM_001291230.1
NP_001278170.1, NM_001291241.1
NP_001315029.1, NM_001328100.1
XP_006715438.1, XM_006715375.3 [P03372-3]
XP_011533845.1, XM_011535543.2 [P03372-1]
XP_011533846.1, XM_011535544.2 [P03372-1]
XP_011533847.1, XM_011535545.2 [P03372-1]
XP_016865865.1, XM_017010376.1 [P03372-1]
XP_016865866.1, XM_017010377.1 [P03372-1]
XP_016865867.1, XM_017010378.1 [P03372-1]
XP_016865868.1, XM_017010379.1 [P03372-1]
XP_016865869.1, XM_017010380.1 [P03372-1]
XP_016865870.1, XM_017010381.1 [P03372-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.208124
Hs.744830

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000206249; ENSP00000206249; ENSG00000091831 [P03372-1]
ENST00000338799; ENSP00000342630; ENSG00000091831 [P03372-1]
ENST00000440973; ENSP00000405330; ENSG00000091831 [P03372-1]
ENST00000443427; ENSP00000387500; ENSG00000091831 [P03372-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2099

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2099

UCSC genome browser

More...UCSCi		uc003qom.5 human [P03372-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs
Wikipedia

Estrogen receptor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03635 mRNA Translation: CAA27284.1
M12674 mRNA Translation: AAA52399.1
U47678 mRNA Translation: AAB00115.1 Sequence problems.
AY425004 Genomic DNA Translation: AAQ91815.1
BX640939 mRNA Translation: CAE45969.1
AL049821 Genomic DNA No translation available.
AL078582 Genomic DNA No translation available.
AL356311 Genomic DNA No translation available.
AL590993 Genomic DNA No translation available.
CH471051 Genomic DNA Translation: EAW47740.1
BC128573 mRNA Translation: AAI28574.1
BC128574 mRNA Translation: AAI28575.1
AH008151 Genomic DNA Translation: AAD52984.1
X73067 mRNA Translation: CAA51528.1
Z75126 mRNA Translation: CAA99436.1
CCDSiCCDS5234.1 [P03372-1]
PIRiS64737
RefSeqiNP_000116.2, NM_000125.3 [P03372-1]
NP_001116212.1, NM_001122740.1 [P03372-1]
NP_001116213.1, NM_001122741.1 [P03372-1]
NP_001116214.1, NM_001122742.1 [P03372-1]
NP_001278159.1, NM_001291230.1
NP_001278170.1, NM_001291241.1
NP_001315029.1, NM_001328100.1
XP_006715438.1, XM_006715375.3 [P03372-3]
XP_011533845.1, XM_011535543.2 [P03372-1]
XP_011533846.1, XM_011535544.2 [P03372-1]
XP_011533847.1, XM_011535545.2 [P03372-1]
XP_016865865.1, XM_017010376.1 [P03372-1]
XP_016865866.1, XM_017010377.1 [P03372-1]
XP_016865867.1, XM_017010378.1 [P03372-1]
XP_016865868.1, XM_017010379.1 [P03372-1]
XP_016865869.1, XM_017010380.1 [P03372-1]
XP_016865870.1, XM_017010381.1 [P03372-1]
UniGeneiHs.208124
Hs.744830

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A52X-ray2.80A/B297-554[»]
1AKFmodel-A309-547[»]
1EREX-ray3.10A/B/C/D/E/F301-553[»]
1ERRX-ray2.60A/B301-553[»]
1G50X-ray2.90A/B/C304-550[»]
1GWQX-ray2.45A/B301-548[»]
1GWRX-ray2.40A/B305-549[»]
1HCPNMR-A180-254[»]
1HCQX-ray2.40A/B/E/F180-262[»]
1L2IX-ray1.95A/B297-554[»]
1PCGX-ray2.70A/B304-547[»]
1QKTX-ray2.20A304-551[»]
1QKUX-ray3.20A/B/C301-550[»]
1R5KX-ray2.70A/B/C297-554[»]
1SJ0X-ray1.90A307-554[»]
1UOMX-ray2.28A301-553[»]
1X7EX-ray2.80A/B305-549[»]
1X7RX-ray2.00A305-549[»]
1XP1X-ray1.80A307-554[»]
1XP6X-ray1.70A307-554[»]
1XP9X-ray1.80A307-554[»]
1XPCX-ray1.60A307-554[»]
1XQCX-ray2.05A/B/C/D301-553[»]
1YIMX-ray1.90A307-554[»]
1YINX-ray2.20A307-554[»]
1ZKYX-ray2.25A/B298-554[»]
2AYRX-ray1.90A304-551[»]
2B1VX-ray1.80A/B298-554[»]
2B1ZX-ray1.78A/B298-554[»]
2B23X-ray2.10A/B298-554[»]
2BJ4X-ray2.00A/B305-533[»]
2FAIX-ray2.10A/B298-554[»]
2G44X-ray2.65A/B298-554[»]
2G5OX-ray2.30A/B298-554[»]
2I0JX-ray2.90A/B/C/D304-547[»]
2IOGX-ray1.60A309-554[»]
2IOKX-ray2.40A/B301-554[»]
2JF9X-ray2.10A/B/C304-533[»]
2JFAX-ray2.55A/B304-533[»]
2LLONMR-B287-305[»]
2LLQNMR-B287-305[»]
2OCFX-ray2.95A298-595[»]
2OUZX-ray2.00A301-553[»]
2P15X-ray1.94A/B298-554[»]
2POGX-ray1.84A/B304-551[»]
2Q6JX-ray2.70A/B298-554[»]
2Q70X-ray1.95A/B304-551[»]
2QA6X-ray2.60A/B298-554[»]
2QA8X-ray1.85A/B298-554[»]
2QABX-ray1.89A/B298-554[»]
2QE4X-ray2.40A/B304-551[»]
2QGTX-ray2.15A/B298-554[»]
2QGWX-ray2.39A/B298-554[»]
2QH6X-ray2.70A/B298-554[»]
2QR9X-ray2.00A/B298-554[»]
2QSEX-ray1.85A/B298-554[»]
2QXMX-ray2.30A/B298-554[»]
2QXSX-ray1.70A/B298-554[»]
2QZOX-ray1.72A/B298-554[»]
2R6WX-ray2.00A/B304-551[»]
2R6YX-ray2.00A/B304-551[»]
2YATX-ray2.60A301-551[»]
2YJAX-ray1.82B299-551[»]
3CBMX-ray1.69B298-307[»]
3CBOX-ray1.65B298-307[»]
3CBPX-ray1.42B298-307[»]
3DT3X-ray2.40A/B299-551[»]
3ERDX-ray2.03A/B297-554[»]
3ERTX-ray1.90A297-554[»]
3HLVX-ray3.00A/B298-550[»]
3HM1X-ray2.33A/B298-550[»]
3L03X-ray1.90A/B298-550[»]
3OS8X-ray2.03A/B/C/D299-553[»]
3OS9X-ray2.30A/B/C/D299-553[»]
3OSAX-ray2.30A/B/C/D299-553[»]
3Q95X-ray2.05A/B298-554[»]
3UU7X-ray2.20A/B302-552[»]
3UUAX-ray2.05A/B302-552[»]
3UUCX-ray2.10A/B/C/D302-552[»]
3UUDX-ray1.60A/B302-552[»]
4AA6X-ray2.60A/B/E/F182-252[»]
4DMAX-ray2.30A/B303-549[»]
4IU7X-ray2.29A/B303-549[»]
4IUIX-ray2.30A/B303-549[»]
4IV2X-ray2.14A/B303-549[»]
4IV4X-ray2.30A/B303-549[»]
4IVWX-ray2.06A/B303-549[»]
4IVYX-ray1.95A/B303-549[»]
4IW6X-ray1.98A/B303-549[»]
4IW8X-ray2.04A/B303-549[»]
4IWCX-ray2.24A/B303-549[»]
4IWFX-ray1.93A/B303-549[»]
4JC3X-ray2.05B585-595[»]
4JDDX-ray2.10B585-595[»]
4MG5X-ray2.05A/B302-552[»]
4MG6X-ray2.10A/B302-552[»]
4MG7X-ray2.15A/B302-552[»]
4MG8X-ray1.85A/B302-552[»]
4MG9X-ray2.00A/B302-552[»]
4MGAX-ray1.80A/B302-552[»]
4MGBX-ray1.85A/B302-552[»]
4MGCX-ray2.15A/B302-552[»]
4MGDX-ray1.90A/B302-552[»]
4O6FX-ray2.82B261-271[»]
4PP6X-ray2.20A/B305-548[»]
4PPPX-ray2.69A/B305-548[»]
4PPSX-ray1.93A/B305-548[»]
4PXMX-ray1.90A/B299-554[»]
4Q13X-ray2.24A/B299-554[»]
4Q50X-ray3.07A/B/C/D/E/F/G/H299-554[»]
4TUZX-ray1.90A/B302-552[»]
4TV1X-ray1.85A/B302-552[»]
4XI3X-ray2.49A/B/C/D306-548[»]
4ZN7X-ray1.93A/B301-559[»]
4ZN9X-ray2.21A/B301-559[»]
4ZNHX-ray1.93A/B301-559[»]
4ZNSX-ray1.86A/B301-559[»]
4ZNTX-ray1.90A/B301-559[»]
4ZNUX-ray2.40A/B301-559[»]
4ZNVX-ray1.77A/B301-559[»]
4ZNWX-ray2.31A/B301-559[»]
5AAUX-ray1.90A/B307-554[»]
5AAVX-ray1.95A307-554[»]
B306-554[»]
5ACCX-ray1.88A307-554[»]
5AK2X-ray2.19A/B307-554[»]
5DI7X-ray2.24A/B298-554[»]
5DIDX-ray2.24A/B298-554[»]
5DIEX-ray2.24A/B298-554[»]
5DIGX-ray2.24A/B298-554[»]
5DK9X-ray2.28A/B298-554[»]
5DKBX-ray2.40A/B298-554[»]
5DKEX-ray2.60A/B298-554[»]
5DKGX-ray2.15A/B298-554[»]
5DKSX-ray2.60A/B298-554[»]
5DL4X-ray2.10A/B298-554[»]
5DLRX-ray2.26A/B298-554[»]
5DMCX-ray2.40A/B298-554[»]
5DMFX-ray2.40A/B298-554[»]
5DP0X-ray2.38A/B298-554[»]
5DRJX-ray2.07A/B298-554[»]
5DRMX-ray2.24A/B298-554[»]
5DTVX-ray2.29A/B298-554[»]
5DU5X-ray2.19A/B298-554[»]
5DUEX-ray2.09A/B298-554[»]
5DUGX-ray2.25A/B298-554[»]
5DUHX-ray2.24A/B298-554[»]
5DVSX-ray2.28A/B298-554[»]
5DVVX-ray2.50A/B298-554[»]
5DWEX-ray1.92A/B298-554[»]
5DWGX-ray2.30A/B298-554[»]
5DWIX-ray2.43A/B298-554[»]
5DWJX-ray2.00A/B298-554[»]
5DX3X-ray2.09A/B297-554[»]
5DXBX-ray2.08A/B297-554[»]
5DXEX-ray1.50A/B297-554[»]
5DXGX-ray1.86A/B297-554[»]
5DXKX-ray2.23A/B298-554[»]
5DXMX-ray2.37A/B298-554[»]
5DXPX-ray2.20A/B298-554[»]
5DXQX-ray2.40A/B298-554[»]
5DXRX-ray2.28A/B298-554[»]
5DY8X-ray2.03A/B298-554[»]
5DYBX-ray2.27A/B298-554[»]
5DYDX-ray2.48A/B298-554[»]
5DZ0X-ray2.24A/B298-554[»]
5DZ1X-ray2.20A/B298-554[»]
5DZ3X-ray2.15A/B298-554[»]
5DZHX-ray2.11A/B298-554[»]
5DZIX-ray1.90A/B298-554[»]
5E0WX-ray2.00A/B298-554[»]
5E0XX-ray2.01A/B298-554[»]
5E14X-ray2.22A/B298-554[»]
5E15X-ray2.10A/B298-554[»]
5E19X-ray2.24A/B298-554[»]
5E1CX-ray1.98A/B298-554[»]
5EGVX-ray2.86A/B298-554[»]
5EHJX-ray2.50A/B298-554[»]
5EI1X-ray2.40A/B298-554[»]
5EITX-ray2.68A/B298-554[»]
5FQPX-ray1.88A307-554[»]
5FQRX-ray1.88A307-554[»]
5FQSX-ray1.94A307-554[»]
5FQTX-ray1.99A307-554[»]
5FQVX-ray1.74A307-554[»]
5GS4X-ray2.40A305-547[»]
5GTRX-ray2.80A305-547[»]
5HYRX-ray2.27A/B302-559[»]
5JMMX-ray2.10A/B302-552[»]
5KCCX-ray2.39A/B298-554[»]
A/B304-549[»]
5KCDX-ray1.82A/B298-554[»]
A/B305-549[»]
5KCEX-ray1.85A/B298-554[»]
A/B303-549[»]
5KCFX-ray2.07A/B298-554[»]
A/B303-549[»]
5KCTX-ray1.60A/B298-554[»]
A/B303-548[»]
5KCUX-ray2.03A/B298-554[»]
A/B303-548[»]
5KCWX-ray1.91A/B303-549[»]
A/B298-554[»]
5KD9X-ray1.78A/B298-554[»]
A/B303-549[»]
5KR9X-ray2.25A/B298-554[»]
5KRAX-ray2.40A/B/E/F298-554[»]
5KRCX-ray2.40A/B298-554[»]
5KRFX-ray2.19A/B298-554[»]
5KRHX-ray2.24A/B298-554[»]
5KRIX-ray2.25A/B298-554[»]
5KRJX-ray2.70A/B298-554[»]
5KRKX-ray2.39A/B298-554[»]
5KRLX-ray2.40A/B298-554[»]
5KRMX-ray2.24A/B298-554[»]
5KROX-ray2.10A/B298-554[»]
5N10X-ray1.60C/D/F584-595[»]
5T0XNMR-B/C287-305[»]
5T1ZX-ray2.10A/B298-554[»]
5T92X-ray2.22A/B301-553[»]
5T97X-ray3.00A/B301-553[»]
5TLDX-ray2.38A/B298-554[»]
5TLFX-ray2.20A/B298-554[»]
5TLGX-ray2.23A/B298-554[»]
5TLLX-ray2.42A/B298-554[»]
5TLMX-ray2.50A/B298-554[»]
5TLOX-ray2.28A/B298-554[»]
5TLPX-ray2.08A/B298-554[»]
5TLTX-ray1.90A/B298-554[»]
5TLUX-ray2.22A/B298-554[»]
5TLVX-ray2.32A/B298-554[»]
5TLXX-ray2.10A/B298-554[»]
5TLYX-ray2.14A/B298-554[»]
5TM1X-ray2.23A/B298-554[»]
5TM2X-ray2.60A/B298-554[»]
5TM3X-ray2.19A/B298-554[»]
5TM4X-ray2.25A/B298-554[»]
5TM5X-ray2.24A/B298-554[»]
5TM6X-ray2.54A/B298-554[»]
5TM7X-ray2.40A/B298-554[»]
5TM8X-ray1.99A/B298-554[»]
5TM9X-ray2.50A/B298-554[»]
5TMLX-ray2.25A/B298-554[»]
5TMMX-ray2.20A/B298-554[»]
5TMOX-ray2.17A/B298-554[»]
5TMQX-ray2.24A/B298-554[»]
5TMRX-ray2.30A/B298-554[»]
5TMSX-ray2.24A/B298-554[»]
5TMTX-ray2.05A/B298-554[»]
5TMUX-ray2.43A/B298-554[»]
5TMVX-ray2.38A/B298-554[»]
5TMWX-ray2.29A/B298-554[»]
5TMZX-ray2.21A/B298-554[»]
5TN1X-ray2.06A/B298-554[»]
5TN3X-ray2.54A/B298-554[»]
5TN4X-ray1.86A/B298-554[»]
5TN5X-ray1.89A/B298-554[»]
5TN6X-ray2.09A/B298-554[»]
5TN7X-ray2.24A/B298-554[»]
5TN8X-ray2.65A/B298-554[»]
5TN9X-ray2.25A/B/C/D298-554[»]
5TNBX-ray2.08A/B/C/D298-554[»]
5U2BX-ray2.22A/B/C/D/E/F298-554[»]
5U2DX-ray1.86A/B298-554[»]
5UFWX-ray1.58A/B306-554[»]
5UFXX-ray1.55A/B306-554[»]
5W9CX-ray1.80A/B/C/D306-554[»]
5W9DX-ray1.65A/B306-554[»]
5WGDX-ray1.80A/B297-554[»]
5WGQX-ray2.30A/B297-554[»]
6B0FX-ray2.86A/B301-553[»]
6C42X-ray2.00A/B307-554[»]
6CBZX-ray1.65A/B305-554[»]
6CHWX-ray1.89A306-551[»]
6CHZX-ray1.68A307-554[»]
DisProtiDP00074
ProteinModelPortaliP03372
SMRiP03372
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108403, 737 interactors
CORUMiP03372
DIPiDIP-5965N
ELMiP03372
IntActiP03372, 478 interactors
MINTiP03372
STRINGi9606.ENSP00000206249

Chemistry databases

BindingDBiP03372
ChEMBLiCHEMBL206
DrugBankiDB06871 17-METHYL-17-ALPHA-DIHYDROEQUILENIN
DB07708 3-CHLORO-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL
DB07712 3-ETHYL-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL
DB06927 [5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-YL]ACETONITRILE
DB04468 Afimoxifene
DB01431 Allylestrenol
DB05233 AP1081
DB05338 atamestane-plus-toremifene
DB06401 Bazedoxifene
DB05487 CC-8490
DB05882 CHF 4227
DB00269 Chlorotrianisene
DB00882 Clomifene
DB02715 Compound 18
DB02615 Compound 19
DB03742 Compound 4-D
DB00286 Conjugated Equine Estrogens
DB01406 Danazol
DB00304 Desogestrel
DB00890 Dienestrol
DB00255 Diethylstilbestrol
DB00783 Estradiol
DB01196 Estramustine
DB04573 Estriol
DB00655 Estrone
DB04574 Estrone sulfate
DB00977 Ethinyl Estradiol
DB00823 Ethynodiol diacetate
DB00294 Etonogestrel
DB01185 Fluoxymesterone
DB00947 Fulvestrant
DB01645 Genistein
DB06202 Lasofoxifene
DB00367 Levonorgestrel
DB00603 Medroxyprogesterone acetate
DB01065 Melatonin
DB01357 Mestranol
DB07991 N-[(1R)-3-(4-HYDROXYPHENYL)-1-METHYLPROPYL]-2-(2-PHENYL-1H-INDOL-3-YL)ACETAMIDE
DB01183 Naloxone
DB00957 Norgestimate
DB05662 NP-50301
DB04938 Ospemifene
DB01708 Prasterone
DB00396 Progesterone
DB04575 Quinestrol
DB00481 Raloxifene
DB08773 RALOXIFENE CORE
DB00675 Tamoxifen
DB09070 Tibolone
DB00539 Toremifene
DB01108 Trilostane
GuidetoPHARMACOLOGYi620
SwissLipidsiSLP:000001568

Protein family/group databases

MoonDBiP03372 Predicted

PTM databases

GlyConnecti144
iPTMnetiP03372
PhosphoSitePlusiP03372
SwissPalmiP03372
UniCarbKBiP03372

Polymorphism and mutation databases

BioMutaiESR1
DMDMi544257

Proteomic databases

EPDiP03372
jPOSTiP03372
PaxDbiP03372
PeptideAtlasiP03372
PRIDEiP03372
ProteomicsDBi51607
51608 [P03372-2]
51609 [P03372-3]
51610 [P03372-4]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2099
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000206249; ENSP00000206249; ENSG00000091831 [P03372-1]
ENST00000338799; ENSP00000342630; ENSG00000091831 [P03372-1]
ENST00000440973; ENSP00000405330; ENSG00000091831 [P03372-1]
ENST00000443427; ENSP00000387500; ENSG00000091831 [P03372-1]
GeneIDi2099
KEGGihsa:2099
UCSCiuc003qom.5 human [P03372-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2099
DisGeNETi2099
EuPathDBiHostDB:ENSG00000091831.21

GeneCards: human genes, protein and diseases

More...GeneCardsi		ESR1
HGNCiHGNC:3467 ESR1
HPAiCAB000037
CAB055099
CAB072858
HPA000449
HPA000450
MalaCardsiESR1
MIMi133430 gene
615363 phenotype
neXtProtiNX_P03372
OpenTargetsiENSG00000091831
Orphaneti785 Estrogen resistance syndrome
PharmGKBiPA156

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3575 Eukaryota
ENOG410XRZC LUCA
GeneTreeiENSGT00940000158133
HOVERGENiHBG108344
InParanoidiP03372
KOiK08550
OMAiHSQQVPY
OrthoDBi926074at2759
PhylomeDBiP03372
TreeFamiTF323751

Enzyme and pathway databases

ReactomeiR-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-9018519 Estrogen-dependent gene expression
SignaLinkiP03372
SIGNORiP03372

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		ESR1 human
EvolutionaryTraceiP03372

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Estrogen_receptor_alpha

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2099

Protein Ontology

More...PROi		PR:P03372

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000091831 Expressed in 152 organ(s), highest expression level in endometrium
CleanExiHS_ESR1
ExpressionAtlasiP03372 baseline and differential
GenevisibleiP03372 HS

Family and domain databases

Gene3Di3.30.50.10, 1 hit
InterProiView protein in InterPro
IPR035500 NHR_like_dom_sf
IPR000536 Nucl_hrmn_rcpt_lig-bd
IPR001723 Nuclear_hrmn_rcpt
IPR024178 Oest_rcpt/oest-rel_rcp
IPR001292 Oestr_rcpt
IPR024736 Oestrogen-typ_rcpt_final_C_dom
IPR001628 Znf_hrmn_rcpt
IPR013088 Znf_NHR/GATA
PfamiView protein in Pfam
PF12743 ESR1_C, 1 hit
PF00104 Hormone_recep, 1 hit
PF02159 Oest_recep, 1 hit
PF00105 zf-C4, 1 hit
PIRSFiPIRSF500101 ER-a, 1 hit
PIRSF002527 ER-like_NR, 1 hit
PRINTSiPR00543 OESTROGENR
PR00398 STRDHORMONER
PR00047 STROIDFINGER
SMARTiView protein in SMART
SM00430 HOLI, 1 hit
SM00399 ZnF_C4, 1 hit
SUPFAMiSSF48508 SSF48508, 1 hit
PROSITEiView protein in PROSITE
PS51843 NR_LBD, 1 hit
PS00031 NUCLEAR_REC_DBD_1, 1 hit
PS51030 NUCLEAR_REC_DBD_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiESR1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P03372
Secondary accession number(s): Q13511
, Q14276, Q5T5H7, Q6MZQ9, Q9NU51, Q9UDZ7, Q9UIS7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 1994
Last modified: January 16, 2019
This is version 259 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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