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Entry version 221 (03 Jul 2019)
Sequence version 1 (01 Feb 1991)
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Protein

Estrogen receptor

Gene

Esr1

Organism
Mus musculus (Mouse)
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. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi189 – 254Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 fingeri189 – 209NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri225 – 249NR 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

GO - Biological processi

<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-MMU-1251985 Nuclear signaling by ERBB4
R-MMU-1257604 PIP3 activates AKT signaling
R-MMU-383280 Nuclear Receptor transcription pathway
R-MMU-4090294 SUMOylation of intracellular receptors
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-8866910 TFAP2 (AP-2) family regulates transcription of growth factors and their receptors
R-MMU-8931987 RUNX1 regulates estrogen receptor mediated transcription
R-MMU-8939211 ESR-mediated signaling
R-MMU-9009391 Non-genomic estrogen signaling
R-MMU-9018519 Estrogen-dependent gene expression

<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, Estr, Estra, 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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 10

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:1352467 Esr1

<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 & Seán O’Donoghue; 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

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>Mutagenesisi362I → A: No effect on transcriptional activity and estrogen-induced interaction with NCOA1. Abolishes estrogen-induced interaction with NCOA1; when associated with A-376 and A-380. 1 Publication1
Mutagenesisi362I → D: Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. 1 Publication1
Mutagenesisi366K → A: Greatly reduces transcriptional activity and estrogen-induced interaction with NCOA1. 1 Publication1
Mutagenesisi366K → D: Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. 1 Publication1
Mutagenesisi366K → L: Reduces transcriptional activity and estrogen-induced interaction with NCOA1. 1 Publication1
Mutagenesisi371F → A: Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcriptional activity, abolishes estrogen-induced interaction with NCOA1. 1 Publication1
Mutagenesisi376L → A: Reduces transcriptional activity, no effect on estrogen-induced interaction with NCOA1. Abolishes estrogen-induced interaction with NCOA1; when associated with A-362 and A-380. 1 Publication1
Mutagenesisi376L → D: Reduces transcriptional activity and estrogen-induced interaction with NCOA1. 1 Publication1
Mutagenesisi380V → A: No effect on transcriptional activity and estrogen-induced interaction with NCOA1. Abolishes estrogen-induced interaction with NCOA1; when associated with A-362 and A-376. 1 Publication1
Mutagenesisi380V → D: Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. 1 Publication1
Mutagenesisi451C → A: Loss of ZDHHC7 and ZDHHC21 binding. Loss of palmitoylation. 1 Publication1
Mutagenesisi508L → A: Reduces DNA-binding, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression; when associated with E-512 and E-515. 1 Publication1
Mutagenesisi508L → E: Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-512 and E-515. 1 Publication1
Mutagenesisi509A → E: Reduces DNA-binding,, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression. 1 Publication1
Mutagenesisi512L → A: Reduces DNA-binding, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-515. 1 Publication1
Mutagenesisi512L → E: Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-515. 1 Publication1
Mutagenesisi515L → A: Reduces DNA-binding, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-512. 1 Publication1
Mutagenesisi515L → E: Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-512. 1 Publication1
Mutagenesisi525G → R: Abolishes estrogen binding; impairs repression of NF-kappa activity. 1 Publication1
Mutagenesisi542D → N: Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcriptional activity, impairs estrogen-induced interaction with NCOA1; when associated with Q-546 and N-548. 1 Publication1
Mutagenesisi543 – 544LL → AA: Abolishes estrogen-dependent NF-kappa B transcriptional repression, abolishes estrogen-induced interaction with NCOA1. 1 Publication2
Mutagenesisi543L → A: Abolishes estrogen-induced interaction with NCOA1. 1 Publication1
Mutagenesisi546E → Q: Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcriptional activity, impairs estrogen-induced interaction with NCOA1; when associated with N-542 and N-548. 1 Publication1
Mutagenesisi547 – 548ML → AA: No effect on estrogen-dependent NF-kappa B transcriptional repression, greatly impairs transcriptional activity, abolishes estrogen-induced interaction with NCOA1. 1 Publication2
Mutagenesisi549D → N: Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcriptional activity, impairs estrogen-induced interaction with NCOA1; when associated with N-542 and Q-546. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3065

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
620

<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_00000536211 – 599Estrogen receptorAdd BLAST599

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) serine1 Publication1
Glycosylationi50O-linked (GlcNAc) threonine1 Publication1
<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 residuei108Phosphoserine; by CDK2By similarity1
Modified residuei110Phosphoserine; by CDK2By similarity1
Modified residuei122PhosphoserineBy similarity1
Modified residuei171Phosphoserine; by CK2By similarity1
Modified residuei264Asymmetric dimethylarginine; by PRMT1By similarity1
<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>Lipidationi451S-palmitoyl cysteine1 Publication1
Modified residuei541Phosphotyrosine; by Tyr-kinasesBy similarity1
GlycosylationiCAR_000137575O-linked (GlcNAc) threonine2 Publications1

<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. Dephosphorylation at Ser-122 by PPP5C inhibits its transactivation activity (By similarity). Phosphorylated by LMTK3 (in vitro) (By similarity).By similarity
Ubiquitinated. Deubiquitinated by OTUB1 (By similarity).By similarity
Palmitoylated at Cys-451 by ZDHHC7 and ZDHHC21. This modification is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation, but not for signaling mediated by the nuclear hormone receptor.1 Publication
Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1 proteasomal degradation. Deubiquitinated by OTUB1.By similarity
Dimethylated by PRMT1 at Arg-264. The methylation may favor cytoplasmic localization. Demethylated by JMJD6 at Arg-264.By similarity

Keywords - PTMi

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

Proteomic databases

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

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PaxDbi
P19785

PRoteomics IDEntifications database

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PRIDEi
P19785

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
145

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P19785

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

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PhosphoSitePlusi
P19785

SwissPalm database of S-palmitoylation events

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SwissPalmi
P19785

UniCarbKB; an annotated and curated database of glycan structures

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UniCarbKBi
P19785

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000019768 Expressed in 219 organ(s), highest expression level in uterus

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P19785 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P19785 MM

<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

Interacts with BCAS3. Binds DNA as a homodimer (By similarity). Can form a heterodimer with ESR2 (By similarity).

Interacts with coactivator NCOA5.

Interacts with NCOA7; the interaction is ligand-inducible.

Interacts with AKAP13, CUEDC2, HEXIM1, KDM5A, MAP1S, PELP1, SMARD1, and UBE1C.

Interacts with MUC1; the interaction is stimulated by 7 beta-estradiol (E2) and enhances ERS1-mediated transcription.

Interacts with DNTTIP2, and UIMC1.

Interacts with KMT2D/MLL2.

Interacts with ATAD2; the interaction is enhanced by estradiol.

Interacts with KIF18A and LDB1.

Interacts with RLIM (via its C-terminus).

Interacts with MACROD1.

Interacts with SH2D4A and PLCG.

Interacts with SH2D4A; the interaction blocks binding to PLCG and inhibits estrogen-induced cell proliferation.

Interacts with DYNLL1.

Interacts with CCDC62; the interaction requires estradiol and appears to enhance the transcription of target genes.

Interacts with NR2C1; the interaction prevents homodimerization of ESR1 and suppresses its transcriptional activity and cell growth.

Interacts with DNAAF4.

Interacts with PRMT2.

Interacts with PI3KR1 or PIK3R2, SRC and PTK2/FAK1.

Interacts with RBFOX2.

Interacts with EP300; the interaction is estrogen-dependent and enhanced by CITED1.

Interacts with CITED1; the interaction is estrogen-dependent (By similarity).

Interacts with FAM120B, FOXL2, PHB2 and SLC30A9.

Interacts with coactivators NCOA3 and NCOA6.

Interacts with STK3/MST2 only in the presence of SAV1 and vice-versa. Binds to CSNK1D.

Interacts with NCOA2; NCOA2 can interact with ESR1 AF-1 and AF-2 domains simultaneously and mediate their transcriptional synergy.

Interacts with DDX5.

Interacts with NCOA1; the interaction seems to require a self-association of N-terminal and C-terminal regions.

Interacts with ZNF366, DDX17, NFKB1, RELA, SP1 and SP3.

Interacts with NRIP1 (By similarity).

Interacts with GPER1; the interaction occurs in an estrogen-dependent manner.

Interacts with CLOCK and the interaction is stimulated by estrogen (By similarity).

Interacts with BCAS3.

Interacts with TRIP4 (ufmylated); estrogen dependent (By similarity).

Interacts with LMTK3; the interaction phosphorylates ESR1 (in vitro) and protects it against proteasomal degradation.

Interacts with CCAR2 (via N-terminus) in a ligand-independent manner.

Interacts with ZFHX3 (By similarity).

Interacts with SFR1 in a ligand-dependent and -independent manner (By similarity).

Interacts with DCAF13, LATS1 and DCAF1; regulates ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation (By similarity).

Interacts (via DNA-binding domain) with POU4F2 isoform 2 (C-terminus); this interaction increases the estrogen receptor ESR1 transcriptional activity in a DNA- and ligand 17-beta-estradiol-independent manner (PubMed:9448000).

Interacts with ESRRB isoform 1 (By similarity).

Interacts with UBE3A and WBP2 (By similarity).

Interacts with GTF2B (By similarity).

Interacts with RBM39 (PubMed:11704680). In the absence of hormonal ligand, interacts with TACC1 (By similarity).

By similarity10 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
199521, 25 interactors

Protein interaction database and analysis system

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IntActi
P19785, 9 interactors

Molecular INTeraction database

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MINTi
P19785

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000070070

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P19785

<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

3D structure databases

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

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SMRi
P19785

Database of comparative protein structure models

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ModBasei
Search...

<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>Domaini315 – 551NR 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 – 188Modulating (transactivation AF-1); mediates interaction with MACROD1By similarityAdd BLAST188
Regioni35 – 178Interaction with DDX5; self-associationBy similarityAdd BLAST144
Regioni35 – 47Required for interaction with NCOA1By similarityAdd BLAST13
Regioni189 – 314Mediates interaction with DNTTIP2By similarityAdd BLAST126
Regioni255 – 314HingeAdd BLAST60
Regioni266 – 599Interaction with AKAP13By similarityAdd BLAST334
Regioni268 – 599Self-associationBy similarityAdd BLAST332
Regioni315 – 599Transactivation AF-2By similarityAdd BLAST285

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi64 – 72Poly-Ala9

<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 (By similarity).By similarity

<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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri189 – 209NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri225 – 249NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3575 Eukaryota
ENOG410XRZC LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158133

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233468

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P19785

KEGG Orthology (KO)

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KOi
K08550

Identification of Orthologs from Complete Genome Data

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OMAi
HSQQVPY

Database of Orthologous Groups

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OrthoDBi
487299at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P19785

TreeFam database of animal gene trees

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TreeFami
TF323751

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.565.10, 1 hit
3.30.50.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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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

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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00543 OESTROGENR
PR00398 STRDHORMONER
PR00047 STROIDFINGER

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48508 SSF48508, 1 hit

PROSITE; a protein domain and family database

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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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P19785-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKMPMERALG EVYVDNSKPT
60 70 80 90 100
VFNYPEGAAY EFNAAAAAAA AASAPVYGQS GIAYGPGSEA AAFSANSLGA
110 120 130 140 150
FPQLNSVSPS PLMLLHPPPQ LSPFLHPHGQ QVPYYLENEP SAYAVRDTGP
160 170 180 190 200
PAFYRSNSDN RRQNGRERLS SSNEKGNMIM ESAKETRYCA VCNDYASGYH
210 220 230 240 250
YGVWSCEGCK AFFKRSIQGH NDYMCPATNQ CTIDKNRRKS CQACRLRKCY
260 270 280 290 300
EVGMMKGGIR KDRRGGRMLK HKRQRDDLEG RNEMGASGDM RAANLWPSPL
310 320 330 340 350
VIKHTKKNSP ALSLTADQMV SALLDAEPPM IYSEYDPSRP FSEASMMGLL
360 370 380 390 400
TNLADRELVH MINWAKRVPG FGDLNLHDQV HLLECAWLEI LMIGLVWRSM
410 420 430 440 450
EHPGKLLFAP NLLLDRNQGK CVEGMVEIFD MLLATSSRFR MMNLQGEEFV
460 470 480 490 500
CLKSIILLNS GVYTFLSSTL KSLEEKDHIH RVLDKITDTL IHLMAKAGLT
510 520 530 540 550
LQQQHRRLAQ LLLILSHIRH MSNKGMEHLY NMKCKNVVPL YDLLLEMLDA
560 570 580 590
HRLHAPASRM GVPPEEPSQT QLATTSSTSA HSLQTYYIPP EAEGFPNTI
Length:599
Mass (Da):66,955
Last modified:February 1, 1991 - v1
<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:i05F5E2FC21CC0A8B
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3Z6V3D3Z6V3_MOUSE
Estrogen receptor
Esr1
499Annotation 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>

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 conflicti269L → M in AAF22561 (Ref. 4) Curated1

Natural variant

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 varianti591E → Q in strain: SJL/J. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M38651 mRNA Translation: AAA37580.1
AK036627 mRNA Translation: BAC29510.1
AK041525 mRNA Translation: BAC30973.1
AJ276597 Genomic DNA Translation: CAB85618.1
AF128221 mRNA Translation: AAF22562.1
AF128220 mRNA Translation: AAF22561.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS56678.1

Protein sequence database of the Protein Information Resource

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PIRi
A40061 QRMSE

NCBI Reference Sequences

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RefSeqi
NP_001289460.1, NM_001302531.1
NP_001289461.1, NM_001302532.1
NP_031982.1, NM_007956.5
XP_006512496.1, XM_006512433.3
XP_006512497.1, XM_006512434.3
XP_006512498.1, XM_006512435.2
XP_011241368.1, XM_011243066.2
XP_011241369.1, XM_011243067.2
XP_011241370.1, XM_011243068.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000067086; ENSMUSP00000070070; ENSMUSG00000019768
ENSMUST00000105589; ENSMUSP00000101214; ENSMUSG00000019768
ENSMUST00000105590; ENSMUSP00000101215; ENSMUSG00000019768

Database of genes from NCBI RefSeq genomes

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GeneIDi
13982

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:13982

UCSC genome browser

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UCSCi
uc007egu.3 mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38651 mRNA Translation: AAA37580.1
AK036627 mRNA Translation: BAC29510.1
AK041525 mRNA Translation: BAC30973.1
AJ276597 Genomic DNA Translation: CAB85618.1
AF128221 mRNA Translation: AAF22562.1
AF128220 mRNA Translation: AAF22561.1
CCDSiCCDS56678.1
PIRiA40061 QRMSE
RefSeqiNP_001289460.1, NM_001302531.1
NP_001289461.1, NM_001302532.1
NP_031982.1, NM_007956.5
XP_006512496.1, XM_006512433.3
XP_006512497.1, XM_006512434.3
XP_006512498.1, XM_006512435.2
XP_011241368.1, XM_011243066.2
XP_011241369.1, XM_011243067.2
XP_011241370.1, XM_011243068.2

3D structure databases

SMRiP19785
ModBaseiSearch...

Protein-protein interaction databases

BioGridi199521, 25 interactors
IntActiP19785, 9 interactors
MINTiP19785
STRINGi10090.ENSMUSP00000070070

Chemistry databases

BindingDBiP19785
ChEMBLiCHEMBL3065
GuidetoPHARMACOLOGYi620

PTM databases

GlyConnecti145
iPTMnetiP19785
PhosphoSitePlusiP19785
SwissPalmiP19785
UniCarbKBiP19785

Proteomic databases

PaxDbiP19785
PRIDEiP19785

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
13982
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067086; ENSMUSP00000070070; ENSMUSG00000019768
ENSMUST00000105589; ENSMUSP00000101214; ENSMUSG00000019768
ENSMUST00000105590; ENSMUSP00000101215; ENSMUSG00000019768
GeneIDi13982
KEGGimmu:13982
UCSCiuc007egu.3 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2099
MGIiMGI:1352467 Esr1

Phylogenomic databases

eggNOGiKOG3575 Eukaryota
ENOG410XRZC LUCA
GeneTreeiENSGT00940000158133
HOGENOMiHOG000233468
InParanoidiP19785
KOiK08550
OMAiHSQQVPY
OrthoDBi487299at2759
PhylomeDBiP19785
TreeFamiTF323751

Enzyme and pathway databases

ReactomeiR-MMU-1251985 Nuclear signaling by ERBB4
R-MMU-1257604 PIP3 activates AKT signaling
R-MMU-383280 Nuclear Receptor transcription pathway
R-MMU-4090294 SUMOylation of intracellular receptors
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-8866910 TFAP2 (AP-2) family regulates transcription of growth factors and their receptors
R-MMU-8931987 RUNX1 regulates estrogen receptor mediated transcription
R-MMU-8939211 ESR-mediated signaling
R-MMU-9009391 Non-genomic estrogen signaling
R-MMU-9018519 Estrogen-dependent gene expression

Miscellaneous databases

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

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ChiTaRSi
Esr1 mouse

Protein Ontology

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PROi
PR:P19785

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000019768 Expressed in 219 organ(s), highest expression level in uterus
ExpressionAtlasiP19785 baseline and differential
GenevisibleiP19785 MM

Family and domain databases

Gene3Di1.10.565.10, 1 hit
3.30.50.10, 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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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_MOUSE
<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: P19785
Secondary accession number(s): Q9JJT5, Q9QY51, Q9QY52
<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: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 3, 2019
This is version 221 of the entry and version 1 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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