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Protein

Estrogen receptor

Gene

Esr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
DNA bindingi189 – 254Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
Zinc fingeri189 – 209NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri225 – 249NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

GO - Biological processi

  • androgen metabolic process Source: MGI
  • antral ovarian follicle growth Source: MGI
  • cell growth Source: UniProtKB
  • cellular response to estradiol stimulus Source: UniProtKB
  • cellular response to estrogen stimulus Source: MGI
  • epithelial cell development Source: MGI
  • epithelial cell proliferation involved in mammary gland duct elongation Source: MGI
  • intracellular steroid hormone receptor signaling pathway Source: UniProtKB
  • male gonad development Source: MGI
  • mammary gland alveolus development Source: MGI
  • mammary gland branching involved in pregnancy Source: MGI
  • negative regulation of gene expression Source: MGI
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • negative regulation of mitotic nuclear division Source: UniProtKB
  • negative regulation of production of miRNAs involved in gene silencing by miRNA Source: MGI
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  • positive regulation of fibroblast proliferation Source: MGI
  • positive regulation of nitric oxide biosynthetic process Source: UniProtKB
  • positive regulation of nitric-oxide synthase activity Source: UniProtKB
  • positive regulation of phospholipase C activity Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis Source: MGI
  • prostate epithelial cord elongation Source: MGI
  • protein localization to chromatin Source: MGI
  • regulation of apoptotic process Source: MGI
  • regulation of branching involved in prostate gland morphogenesis Source: MGI
  • regulation of inflammatory response Source: MGI
  • regulation of toll-like receptor signaling pathway Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • response to estradiol Source: MGI
  • response to estrogen Source: MGI
  • transcription from RNA polymerase II promoter Source: MGI
  • uterus development Source: MGI
  • vagina development Source: MGI
Complete GO annotation...

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

ReactomeiR-MMU-1251985. Nuclear signaling by ERBB4.
R-MMU-383280. Nuclear Receptor transcription pathway.
R-MMU-5689896. Ovarian tumor domain proteases.

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
Proteomesi
  • UP000000589 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

ChEMBLiCHEMBL3065.
GuidetoPHARMACOLOGYi620.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000536211 – 599Estrogen receptorAdd BLAST599

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi10O-linked (GlcNAc)1 Publication1
Glycosylationi50O-linked (GlcNAc)1 Publication1
Modified residuei108Phosphoserine; by CDK2By similarity1
Modified residuei110Phosphoserine; by CDK2By similarity1
Modified residuei122PhosphoserineBy similarity1
Modified residuei171Phosphoserine; by CK2By similarity1
Modified residuei264Asymmetric dimethylarginine; by PRMT1By similarity1
Lipidationi451S-palmitoyl cysteine1 Publication1
Modified residuei541Phosphotyrosine; by Tyr-kinasesBy similarity1
GlycosylationiCAR_000137575O-linked (GlcNAc)2 Publications1

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
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

PaxDbiP19785.
PRIDEiP19785.

PTM databases

iPTMnetiP19785.
PhosphoSitePlusiP19785.
SwissPalmiP19785.
UniCarbKBiP19785.

Expressioni

Gene expression databases

BgeeiENSMUSG00000019768.
CleanExiMM_ESR1.
ExpressionAtlasiP19785. baseline and differential.
GenevisibleiP19785. MM.

Interactioni

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 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 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).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCOA1Q157882EBI-346765,EBI-455189From a different organism.
URI1O947632EBI-346765,EBI-357067From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199521. 25 interactors.
IntActiP19785. 7 interactors.
MINTiMINT-2835181.
STRINGi10090.ENSMUSP00000070070.

Chemistry databases

BindingDBiP19785.

Structurei

3D structure databases

ProteinModelPortaliP19785.
SMRiP19785.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Regioni315 – 555Steroid-bindingAdd BLAST241

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi64 – 72Poly-Ala9

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

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000233468.
HOVERGENiHBG108344.
InParanoidiP19785.
KOiK08550.
OMAiAFYRPNS.
OrthoDBiEOG091G03V4.
PhylomeDBiP19785.
TreeFamiTF323751.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR000536. 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.
[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

        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
Checksum:i05F5E2FC21CC0A8B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti269L → M in AAF22561 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti591E → Q in strain: SJL/J. 1 Publication1

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.
UniGeneiMm.463262.
Mm.489063.
Mm.9213.

Genome annotation databases

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

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.
UniGeneiMm.463262.
Mm.489063.
Mm.9213.

3D structure databases

ProteinModelPortaliP19785.
SMRiP19785.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199521. 25 interactors.
IntActiP19785. 7 interactors.
MINTiMINT-2835181.
STRINGi10090.ENSMUSP00000070070.

Chemistry databases

BindingDBiP19785.
ChEMBLiCHEMBL3065.
GuidetoPHARMACOLOGYi620.

PTM databases

iPTMnetiP19785.
PhosphoSitePlusiP19785.
SwissPalmiP19785.
UniCarbKBiP19785.

Proteomic databases

PaxDbiP19785.
PRIDEiP19785.

Protocols and materials databases

DNASUi13982.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2099.
MGIiMGI:1352467. Esr1.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000233468.
HOVERGENiHBG108344.
InParanoidiP19785.
KOiK08550.
OMAiAFYRPNS.
OrthoDBiEOG091G03V4.
PhylomeDBiP19785.
TreeFamiTF323751.

Enzyme and pathway databases

ReactomeiR-MMU-1251985. Nuclear signaling by ERBB4.
R-MMU-383280. Nuclear Receptor transcription pathway.
R-MMU-5689896. Ovarian tumor domain proteases.

Miscellaneous databases

PROiP19785.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000019768.
CleanExiMM_ESR1.
ExpressionAtlasiP19785. baseline and differential.
GenevisibleiP19785. MM.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR000536. 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.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 198 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.