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P19785

- ESR1_MOUSE

UniProt

P19785 - ESR1_MOUSE

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Protein

Estrogen receptor

Gene

Esr1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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)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. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  7. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  8. steroid binding Source: UniProtKB
  9. transcription factor binding Source: UniProtKB
  10. 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
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

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-KW
  3. nucleus Source: MGI
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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. 1 Publication
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

BgeeiP19785.
CleanExiMM_ESR1.
ExpressionAtlasiP19785. baseline and differential.
GenevestigatoriP19785.

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).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.
GeneTreeiENSGT00760000118887.
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

        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)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 ENSGT00760000118887.
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

Bgeei P19785.
CleanExi MM_ESR1.
ExpressionAtlasi P19785. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 177 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