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P19785

- ESR1_MOUSE

UniProt

P19785 - ESR1_MOUSE

Protein

Estrogen receptor

Gene

Esr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi189 – 25466Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri189 – 20921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri225 – 24925NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. core promoter sequence-specific DNA binding Source: Ensembl
    3. estrogen-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: Ensembl
    4. estrogen response element binding Source: Ensembl
    5. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
    6. protein binding Source: UniProtKB
    7. steroid binding Source: UniProtKB
    8. transcription factor binding Source: UniProtKB
    9. zinc ion binding Source: InterPro

    GO - Biological processi

    1. androgen metabolic process Source: MGI
    2. antral ovarian follicle growth Source: MGI
    3. cell growth Source: UniProtKB
    4. cellular response to estradiol stimulus Source: UniProtKB
    5. cellular response to estrogen stimulus Source: MGI
    6. epithelial cell development Source: MGI
    7. epithelial cell proliferation involved in mammary gland duct elongation Source: MGI
    8. intracellular steroid hormone receptor signaling pathway Source: UniProtKB
    9. male gonad development Source: MGI
    10. mammary gland alveolus development Source: MGI
    11. mammary gland branching involved in pregnancy Source: MGI
    12. negative regulation of gene expression Source: Ensembl
    13. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    14. negative regulation of mitosis Source: UniProtKB
    15. negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    16. phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
    17. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    18. positive regulation of fibroblast proliferation Source: MGI
    19. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
    20. positive regulation of nitric-oxide synthase activity Source: UniProtKB
    21. positive regulation of phospholipase C activity Source: UniProtKB
    22. positive regulation of retinoic acid receptor signaling pathway Source: Ensembl
    23. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    24. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    25. prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis Source: MGI
    26. prostate epithelial cord elongation Source: MGI
    27. regulation of apoptotic process Source: MGI
    28. regulation of branching involved in prostate gland morphogenesis Source: MGI
    29. regulation of transcription, DNA-templated Source: MGI
    30. uterus development Source: MGI
    31. vagina development Source: MGI

    Keywords - Molecular functioni

    Activator, Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Lipid-binding, Metal-binding, Steroid-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198574. Nuclear signaling by ERBB4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Estrogen receptor
    Short name:
    ER
    Alternative name(s):
    ER-alpha
    Estradiol receptor
    Nuclear receptor subfamily 3 group A member 1
    Gene namesi
    Name:Esr1
    Synonyms:Esr, Estr, Estra, Nr3a1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1352467. Esr1.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation. Cytoplasm By similarity. Golgi apparatus By similarity. Cell membrane By similarity
    Note: Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus where most probably palmitoylation occurs. Associated with the plasma membrane when palmitoylated.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. Golgi apparatus Source: UniProtKB-SubCell
    3. nucleus Source: MGI
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi362 – 3621I → 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 Publication
    Mutagenesisi362 – 3621I → D: Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. 1 Publication
    Mutagenesisi366 – 3661K → A: Greatly reduces transcriptional activity and estrogen-induced interaction with NCOA1. 1 Publication
    Mutagenesisi366 – 3661K → D: Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. 1 Publication
    Mutagenesisi366 – 3661K → L: Reduces transcriptional activity and estrogen-induced interaction with NCOA1. 1 Publication
    Mutagenesisi371 – 3711F → A: Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcritional activity, abolishes estrogen-induced interaction with NCOA1. 1 Publication
    Mutagenesisi376 – 3761L → 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 Publication
    Mutagenesisi376 – 3761L → D: Reduces transcriptional activity and estrogen-induced interaction with NCOA1. 1 Publication
    Mutagenesisi380 – 3801V → 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 Publication
    Mutagenesisi380 – 3801V → D: Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. 1 Publication
    Mutagenesisi451 – 4511C → A: Loss of ZDHHC7 and ZDHHC21 binding. Loss of palmitoylation. 1 Publication
    Mutagenesisi508 – 5081L → 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 Publication
    Mutagenesisi508 – 5081L → E: Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-512 and E-515. 1 Publication
    Mutagenesisi509 – 5091A → E: Reduces DNA-binding,, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression. 1 Publication
    Mutagenesisi512 – 5121L → 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 Publication
    Mutagenesisi512 – 5121L → E: Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-515. 1 Publication
    Mutagenesisi515 – 5151L → 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 Publication
    Mutagenesisi515 – 5151L → E: Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-512. 1 Publication
    Mutagenesisi525 – 5251G → R: Abolishes estrogen binding; impairs repression of NF-kappa activity. 1 Publication
    Mutagenesisi542 – 5421D → N: Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcritional activity, impairs estrogen-induced interaction with NCOA1; when associated with Q-546 and N-548. 1 Publication
    Mutagenesisi543 – 5442LL → AA: Abolishes estrogen-dependent NF-kappa B transcriptional repression, abolishes estrogen-induced interaction with NCOA1. 1 Publication
    Mutagenesisi543 – 5431L → A: Abolishes estrogen-induced interaction with NCOA1. 1 Publication
    Mutagenesisi546 – 5461E → Q: Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcritional activity, impairs estrogen-induced interaction with NCOA1; when associated with N-542 and N-548. 1 Publication
    Mutagenesisi547 – 5482ML → AA: No effect on estrogen-dependent NF-kappa B transcriptional repression, greatly impairs transcritional activity, abolishes estrogen-induced interaction with NCOA1.
    Mutagenesisi549 – 5491D → N: Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcritional activity, impairs estrogen-induced interaction with NCOA1; when associated with N-542 and Q-546. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 599599Estrogen receptorPRO_0000053621Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi10 – 101O-linked (GlcNAc)1 Publication
    Glycosylationi50 – 501O-linked (GlcNAc)1 Publication
    Modified residuei108 – 1081Phosphoserine; by CDK2By similarity
    Modified residuei110 – 1101Phosphoserine; by CDK2By similarity
    Modified residuei122 – 1221PhosphoserineBy similarity
    Modified residuei171 – 1711Phosphoserine; by CK2By similarity
    Modified residuei264 – 2641Asymmetric dimethylarginine; by PRMT1By similarity
    Lipidationi451 – 4511S-palmitoyl cysteine1 Publication
    Modified residuei541 – 5411Phosphotyrosine; by Tyr-kinasesBy similarity
    Glycosylationi575 – 5751O-linked (GlcNAc)2 PublicationsCAR_000137

    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.By similarity
    Ubiquitinated. Deubiquitinated by OTUB1 By similarity.By similarity
    Dimethylated by PRMT1 at Arg-264. The methylation may favor cytoplasmic localization 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

    Keywords - PTMi

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

    Proteomic databases

    PRIDEiP19785.

    PTM databases

    PhosphoSiteiP19785.
    UniCarbKBiP19785.

    Expressioni

    Gene expression databases

    ArrayExpressiP19785.
    BgeeiP19785.
    CleanExiMM_ESR1.
    GenevestigatoriP19785.

    Interactioni

    Subunit structurei

    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 DYX1C1. 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 ESE1 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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCOA1Q157882EBI-346765,EBI-455189From a different organism.

    Protein-protein interaction databases

    BioGridi199521. 22 interactions.
    IntActiP19785. 6 interactions.
    MINTiMINT-2835181.

    Structurei

    3D structure databases

    ProteinModelPortaliP19785.
    SMRiP19785. Positions 184-555.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 188188Modulating (transactivation AF-1); mediates interaction with MACROD1By similarityAdd
    BLAST
    Regioni35 – 178144Interaction with DDX5; self-associationBy similarityAdd
    BLAST
    Regioni35 – 4713Required for interaction with NCOA1By similarityAdd
    BLAST
    Regioni189 – 314126Mediates interaction with DNTTIP2By similarityAdd
    BLAST
    Regioni255 – 31460HingeAdd
    BLAST
    Regioni266 – 599334Interaction with AKAP13By similarityAdd
    BLAST
    Regioni268 – 599332Self-associationBy similarityAdd
    BLAST
    Regioni315 – 599285Transactivation AF-2By similarityAdd
    BLAST
    Regioni315 – 555241Steroid-bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi64 – 729Poly-Ala

    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

    Sequence similaritiesi

    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri189 – 20921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri225 – 24925NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG320746.
    GeneTreeiENSGT00730000110346.
    HOGENOMiHOG000233468.
    HOVERGENiHBG108344.
    InParanoidiP19785.
    KOiK08550.
    OMAiHSQQVPY.
    OrthoDBiEOG7288S1.
    PhylomeDBiP19785.
    TreeFamiTF323751.

    Family and domain databases

    Gene3Di1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR024178. Oest_rcpt/oest-rel_rcp.
    IPR001292. Oestr_rcpt.
    IPR024736. Oestrogen-typ_rcpt_final_C_dom.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    PfamiPF12743. ESR1_C. 1 hit.
    PF00104. Hormone_recep. 1 hit.
    PF02159. Oest_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500101. ER-a. 1 hit.
    PIRSF002527. ER-like_NR. 1 hit.
    PRINTSiPR00543. OESTROGENR.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTiSM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view]
    SUPFAMiSSF48508. SSF48508. 2 hits.
    PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19785-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKMPMERALG EVYVDNSKPT    50
    VFNYPEGAAY EFNAAAAAAA AASAPVYGQS GIAYGPGSEA AAFSANSLGA 100
    FPQLNSVSPS PLMLLHPPPQ LSPFLHPHGQ QVPYYLENEP SAYAVRDTGP 150
    PAFYRSNSDN RRQNGRERLS SSNEKGNMIM ESAKETRYCA VCNDYASGYH 200
    YGVWSCEGCK AFFKRSIQGH NDYMCPATNQ CTIDKNRRKS CQACRLRKCY 250
    EVGMMKGGIR KDRRGGRMLK HKRQRDDLEG RNEMGASGDM RAANLWPSPL 300
    VIKHTKKNSP ALSLTADQMV SALLDAEPPM IYSEYDPSRP FSEASMMGLL 350
    TNLADRELVH MINWAKRVPG FGDLNLHDQV HLLECAWLEI LMIGLVWRSM 400
    EHPGKLLFAP NLLLDRNQGK CVEGMVEIFD MLLATSSRFR MMNLQGEEFV 450
    CLKSIILLNS GVYTFLSSTL KSLEEKDHIH RVLDKITDTL IHLMAKAGLT 500
    LQQQHRRLAQ LLLILSHIRH MSNKGMEHLY NMKCKNVVPL YDLLLEMLDA 550
    HRLHAPASRM GVPPEEPSQT QLATTSSTSA HSLQTYYIPP EAEGFPNTI 599
    Length:599
    Mass (Da):66,955
    Last modified:February 1, 1991 - v1
    Checksum:i05F5E2FC21CC0A8B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti269 – 2691L → M in AAF22561. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti591 – 5911E → Q in strain: SJL/J. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_031982.1. NM_007956.4.
    XP_006512495.1. XM_006512432.1.
    XP_006512496.1. XM_006512433.1.
    XP_006512497.1. XM_006512434.1.
    XP_006512498.1. XM_006512435.1.
    UniGeneiMm.463262.
    Mm.489063.
    Mm.9213.

    Genome annotation databases

    EnsembliENSMUST00000067086; ENSMUSP00000070070; ENSMUSG00000019768.
    ENSMUST00000105589; ENSMUSP00000101214; ENSMUSG00000019768.
    ENSMUST00000105590; ENSMUSP00000101215; ENSMUSG00000019768.
    GeneIDi13982.
    KEGGimmu:13982.
    UCSCiuc007egu.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS56678.1.
    PIRi A40061. QRMSE.
    RefSeqi NP_031982.1. NM_007956.4.
    XP_006512495.1. XM_006512432.1.
    XP_006512496.1. XM_006512433.1.
    XP_006512497.1. XM_006512434.1.
    XP_006512498.1. XM_006512435.1.
    UniGenei Mm.463262.
    Mm.489063.
    Mm.9213.

    3D structure databases

    ProteinModelPortali P19785.
    SMRi P19785. Positions 184-555.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199521. 22 interactions.
    IntActi P19785. 6 interactions.
    MINTi MINT-2835181.

    Chemistry

    BindingDBi P19785.
    ChEMBLi CHEMBL3065.
    GuidetoPHARMACOLOGYi 620.

    PTM databases

    PhosphoSitei P19785.
    UniCarbKBi P19785.

    Proteomic databases

    PRIDEi P19785.

    Protocols and materials databases

    DNASUi 13982.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000067086 ; ENSMUSP00000070070 ; ENSMUSG00000019768 .
    ENSMUST00000105589 ; ENSMUSP00000101214 ; ENSMUSG00000019768 .
    ENSMUST00000105590 ; ENSMUSP00000101215 ; ENSMUSG00000019768 .
    GeneIDi 13982.
    KEGGi mmu:13982.
    UCSCi uc007egu.2. mouse.

    Organism-specific databases

    CTDi 2099.
    MGIi MGI:1352467. Esr1.

    Phylogenomic databases

    eggNOGi NOG320746.
    GeneTreei ENSGT00730000110346.
    HOGENOMi HOG000233468.
    HOVERGENi HBG108344.
    InParanoidi P19785.
    KOi K08550.
    OMAi HSQQVPY.
    OrthoDBi EOG7288S1.
    PhylomeDBi P19785.
    TreeFami TF323751.

    Enzyme and pathway databases

    Reactomei REACT_198574. Nuclear signaling by ERBB4.

    Miscellaneous databases

    NextBioi 284854.
    PROi P19785.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19785.
    Bgeei P19785.
    CleanExi MM_ESR1.
    Genevestigatori P19785.

    Family and domain databases

    Gene3Di 1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR024178. Oest_rcpt/oest-rel_rcp.
    IPR001292. Oestr_rcpt.
    IPR024736. Oestrogen-typ_rcpt_final_C_dom.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view ]
    Pfami PF12743. ESR1_C. 1 hit.
    PF00104. Hormone_recep. 1 hit.
    PF02159. Oest_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500101. ER-a. 1 hit.
    PIRSF002527. ER-like_NR. 1 hit.
    PRINTSi PR00543. OESTROGENR.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTi SM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48508. SSF48508. 2 hits.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural organization and expression of the mouse estrogen receptor."
      White R., Lees J.A., Needham M., Ham J., Parker M.
      Mol. Endocrinol. 1:735-744(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Uterus.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone and Thymus.
    3. "Tissue-specific expression of multiple mRNA variants of the mouse estrogen receptor alpha gene."
      Kos M., O'Brien S., Flouriot G., Gannon F.
      FEBS Lett. 477:15-20(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
      Strain: C57BL/6J.
      Tissue: Liver.
    4. "Screening for candidate genes of mouse autoimmune diseases."
      Ma R.Z., Teuscher C.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 269-599, VARIANT GLN-591.
      Strain: B10.S/J and SJL/J.
      Tissue: Spleen.
    5. "Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor."
      Cavailles V., Dauvois S., L'Horset F., Lopez G., Hoare S., Kushner P.J., Parker M.G.
      EMBO J. 14:3741-3751(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NRIP1.
    6. "Molecular determinants of the estrogen receptor-coactivator interface."
      Mak H.Y., Hoare S., Henttu P.M., Parker M.G.
      Mol. Cell. Biol. 19:3895-3903(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NCOA1, MUTAGENESIS OF ILE-362; LYS-366; LEU-376; VAL-380 AND LEU-543.
    7. "Mutations in the estrogen receptor ligand binding domain discriminate between hormone-dependent transactivation and transrepression."
      Valentine J.E., Kalkhoven E., White R., Hoare S., Parker M.G.
      J. Biol. Chem. 275:25322-25329(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NCOA1, MUTAGENESIS OF PHE-371; LEU-508; ALA-509; LEU-512; LEU-515; GLY-525; ASP-542; 543-LEU-LEU-544; GLU-546; 547-MET-LEU-548 AND ASP-549.
    8. "Constitutive coactivator of peroxisome proliferator-activated receptor (PPARgamma), a novel coactivator of PPARgamma that promotes adipogenesis."
      Li D., Kang Q., Wang D.-M.
      Mol. Endocrinol. 21:2320-2333(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FAM120B.
    9. "A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine."
      Jiang M.S., Hart G.W.
      J. Biol. Chem. 272:2421-2428(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-575.
    10. "Glycosylation of the murine estrogen receptor-alpha."
      Cheng X., Hart G.W.
      J. Steroid Biochem. Mol. Biol. 75:147-158(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-10; THR-50 AND THR-575.
    11. "The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function."
      Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G.
      Nature 387:677-684(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA3.
    12. "Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR."
      Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K.
      J. Biol. Chem. 275:13510-13516(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA6.
    13. "Transcriptional regulation by the repressor of estrogen receptor activity via recruitment of histone deacetylases."
      Kurtev V., Margueron R., Kroboth K., Ogris E., Cavailles V., Seiser C.
      J. Biol. Chem. 279:24834-24843(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHB2.
    14. "GAC63, a GRIP1-dependent nuclear receptor coactivator."
      Chen Y.-H., Kim J.H., Stallcup M.R.
      Mol. Cell. Biol. 25:5965-5972(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC30A9.
    15. Cited for: INTERACTION WITH FOXL2.
    16. "DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors."
      Pedram A., Razandi M., Deschenes R.J., Levin E.R.
      Mol. Biol. Cell 23:188-199(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-451, MUTAGENESIS OF CYS-451.

    Entry informationi

    Entry nameiESR1_MOUSE
    AccessioniPrimary (citable) accession number: P19785
    Secondary accession number(s): Q9JJT5, Q9QY51, Q9QY52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 176 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3