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P19785 (ESR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Estrogen receptor

Short name=ER
Alternative name(s):
ER-alpha
Estradiol receptor
Nuclear receptor subfamily 3 group A member 1
Gene names
Name:Esr1
Synonyms:Esr, Estr, Estra, Nr3a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length599 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Subcellular location

Nucleus By similarity. 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 By similarity. Associated with the plasma membrane when palmitoylated By similarity.

Domain

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.

Post-translational modification

Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably enhances transcriptional activity. Dephosphorylation at Ser-122 by PPP5C inhibits its transactivation activity By similarity.

Ubiquitinated. Deubiquitinated by OTUB1 By similarity.

Dimethylated by PRMT1 at Arg-264. The methylation may favor cytoplasmic localization 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. Ref.16

Sequence similarities

Belongs to the nuclear hormone receptor family. NR3 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
Nucleus
   DomainZinc-finger
   LigandDNA-binding
Lipid-binding
Metal-binding
Steroid-binding
Zinc
   Molecular functionActivator
Receptor
   PTMGlycoprotein
Lipoprotein
Methylation
Palmitate
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen metabolic process

Inferred from mutant phenotype PubMed 18755802. Source: MGI

antral ovarian follicle growth

Inferred from mutant phenotype PubMed 10976058. Source: MGI

cell growth

Non-traceable author statement PubMed 9171231. Source: UniProtKB

cellular response to estradiol stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to estrogen stimulus

Inferred from mutant phenotype PubMed 17901126. Source: MGI

epithelial cell development

Inferred from mutant phenotype PubMed 18755802. Source: MGI

epithelial cell proliferation involved in mammary gland duct elongation

Inferred from mutant phenotype PubMed 12021201. Source: MGI

intracellular steroid hormone receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

male gonad development

Inferred from mutant phenotype PubMed 18755802. Source: MGI

mammary gland alveolus development

Inferred from mutant phenotype PubMed 10919287. Source: MGI

mammary gland branching involved in pregnancy

Inferred from mutant phenotype PubMed 10919287. Source: MGI

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of mitosis

Non-traceable author statement PubMed 12119130. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from mutant phenotype PubMed 18755802. Source: MGI

positive regulation of nitric oxide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of nitric-oxide synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phospholipase C activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of retinoic acid receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17901126. Source: MGI

prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis

Inferred from mutant phenotype PubMed 18535112. Source: MGI

prostate epithelial cord elongation

Inferred from mutant phenotype PubMed 18535112. Source: MGI

regulation of apoptotic process

Inferred from mutant phenotype PubMed 17901126. Source: MGI

regulation of branching involved in prostate gland morphogenesis

Inferred from mutant phenotype PubMed 15665095PubMed 18755802. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15322135. Source: MGI

uterus development

Inferred from genetic interaction PubMed 10976058. Source: MGI

vagina development

Inferred from genetic interaction PubMed 10976058. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 12845704PubMed 14552897. Source: MGI

nucleus

Inferred from direct assay PubMed 11897499PubMed 12845704PubMed 14502087PubMed 14552897PubMed 17065319PubMed 18202148Ref.9. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchromatin binding

Inferred from direct assay PubMed 18202148. Source: MGI

core promoter sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

estrogen response element binding

Inferred from electronic annotation. Source: Ensembl

estrogen-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from electronic annotation. Source: Ensembl

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 15322135. Source: MGI

protein binding

Inferred from physical interaction PubMed 12878603PubMed 8978696. Source: UniProtKB

steroid binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 19797124Ref.15. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCOA1Q157882EBI-346765,EBI-455189From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 599599Estrogen receptor
PRO_0000053621

Regions

DNA binding189 – 25466Nuclear receptor
Zinc finger189 – 20921NR C4-type
Zinc finger225 – 24925NR C4-type
Region1 – 188188Modulating (transactivation AF-1); mediates interaction with MACROD1 By similarity
Region35 – 178144Interaction with DDX5; self-association By similarity
Region35 – 4713Required for interaction with NCOA1 By similarity
Region189 – 314126Mediates interaction with DNTTIP2 By similarity
Region255 – 31460Hinge
Region266 – 599334Interaction with AKAP13 By similarity
Region268 – 599332Self-association By similarity
Region315 – 599285Transactivation AF-2 By similarity
Region315 – 555241Steroid-binding
Compositional bias64 – 729Poly-Ala

Amino acid modifications

Modified residue1081Phosphoserine; by CDK2 By similarity
Modified residue1101Phosphoserine; by CDK2 By similarity
Modified residue1221Phosphoserine By similarity
Modified residue1711Phosphoserine; by CK2 By similarity
Modified residue2641Asymmetric dimethylarginine; by PRMT1 By similarity
Modified residue5411Phosphotyrosine; by Tyr-kinases By similarity
Lipidation4511S-palmitoyl cysteine Ref.16
Glycosylation101O-linked (GlcNAc) Ref.10
Glycosylation501O-linked (GlcNAc) Ref.10
Glycosylation5751O-linked (GlcNAc) Ref.9 Ref.10
CAR_000137

Natural variations

Natural variant5911E → Q in strain: SJL/J. Ref.4

Experimental info

Mutagenesis3621I → 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. Ref.6
Mutagenesis3621I → D: Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. Ref.6
Mutagenesis3661K → A: Greatly reduces transcriptional activity and estrogen-induced interaction with NCOA1. Ref.6
Mutagenesis3661K → D: Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. Ref.6
Mutagenesis3661K → L: Reduces transcriptional activity and estrogen-induced interaction with NCOA1. Ref.6
Mutagenesis3711F → A: Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcritional activity, abolishes estrogen-induced interaction with NCOA1. Ref.7
Mutagenesis3761L → 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. Ref.6
Mutagenesis3761L → D: Reduces transcriptional activity and estrogen-induced interaction with NCOA1. Ref.6
Mutagenesis3801V → 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. Ref.6
Mutagenesis3801V → D: Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. Ref.6
Mutagenesis4511C → A: Loss of ZDHHC7 and ZDHHC21 binding. Loss of palmitoylation. Ref.16
Mutagenesis5081L → 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. Ref.7
Mutagenesis5081L → E: Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-512 and E-515. Ref.7
Mutagenesis5091A → E: Reduces DNA-binding,, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression. Ref.7
Mutagenesis5121L → 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. Ref.7
Mutagenesis5121L → E: Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-515. Ref.7
Mutagenesis5151L → 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. Ref.7
Mutagenesis5151L → E: Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-512. Ref.7
Mutagenesis5251G → R: Abolishes estrogen binding; impairs repression of NF-kappa activity. Ref.7
Mutagenesis5421D → 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. Ref.7
Mutagenesis543 – 5442LL → AA: Abolishes estrogen-dependent NF-kappa B transcriptional repression, abolishes estrogen-induced interaction with NCOA1. Ref.6
Mutagenesis5431L → A: Abolishes estrogen-induced interaction with NCOA1. Ref.6
Mutagenesis5461E → 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. Ref.7
Mutagenesis547 – 5482ML → AA: No effect on estrogen-dependent NF-kappa B transcriptional repression, greatly impairs transcritional activity, abolishes estrogen-induced interaction with NCOA1.
Mutagenesis5491D → 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. Ref.7
Sequence conflict2691L → M in AAF22561. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P19785 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 05F5E2FC21CC0A8B

FASTA59966,955
        10         20         30         40         50         60 
MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKMPMERALG EVYVDNSKPT VFNYPEGAAY 

        70         80         90        100        110        120 
EFNAAAAAAA AASAPVYGQS GIAYGPGSEA AAFSANSLGA FPQLNSVSPS PLMLLHPPPQ 

       130        140        150        160        170        180 
LSPFLHPHGQ QVPYYLENEP SAYAVRDTGP PAFYRSNSDN RRQNGRERLS SSNEKGNMIM 

       190        200        210        220        230        240 
ESAKETRYCA VCNDYASGYH YGVWSCEGCK AFFKRSIQGH NDYMCPATNQ CTIDKNRRKS 

       250        260        270        280        290        300 
CQACRLRKCY EVGMMKGGIR KDRRGGRMLK HKRQRDDLEG RNEMGASGDM RAANLWPSPL 

       310        320        330        340        350        360 
VIKHTKKNSP ALSLTADQMV SALLDAEPPM IYSEYDPSRP FSEASMMGLL TNLADRELVH 

       370        380        390        400        410        420 
MINWAKRVPG FGDLNLHDQV HLLECAWLEI LMIGLVWRSM EHPGKLLFAP NLLLDRNQGK 

       430        440        450        460        470        480 
CVEGMVEIFD MLLATSSRFR MMNLQGEEFV CLKSIILLNS GVYTFLSSTL KSLEEKDHIH 

       490        500        510        520        530        540 
RVLDKITDTL IHLMAKAGLT LQQQHRRLAQ LLLILSHIRH MSNKGMEHLY NMKCKNVVPL 

       550        560        570        580        590 
YDLLLEMLDA HRLHAPASRM GVPPEEPSQT QLATTSSTSA HSLQTYYIPP EAEGFPNTI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Somatic sex reprogramming of adult ovaries to testes by FOXL2 ablation."
Uhlenhaut N.H., Jakob S., Anlag K., Eisenberger T., Sekido R., Kress J., Treier A.C., Klugmann C., Klasen C., Holter N.I., Riethmacher D., Schutz G., Cooney A.J., Lovell-Badge R., Treier M.
Cell 139:1130-1142(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS56678.1.
PIRQRMSE. A40061.
RefSeqNP_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.
UniGeneMm.463262.
Mm.489063.
Mm.9213.

3D structure databases

ProteinModelPortalP19785.
SMRP19785. Positions 184-555.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199521. 22 interactions.
IntActP19785. 6 interactions.
MINTMINT-2835181.

Chemistry

BindingDBP19785.
ChEMBLCHEMBL3065.
GuidetoPHARMACOLOGY620.

PTM databases

PhosphoSiteP19785.
UniCarbKBP19785.

Proteomic databases

PRIDEP19785.

Protocols and materials databases

DNASU13982.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067086; ENSMUSP00000070070; ENSMUSG00000019768.
ENSMUST00000105589; ENSMUSP00000101214; ENSMUSG00000019768.
ENSMUST00000105590; ENSMUSP00000101215; ENSMUSG00000019768.
GeneID13982.
KEGGmmu:13982.
UCSCuc007egu.2. mouse.

Organism-specific databases

CTD2099.
MGIMGI:1352467. Esr1.

Phylogenomic databases

eggNOGNOG320746.
GeneTreeENSGT00730000110346.
HOGENOMHOG000233468.
HOVERGENHBG108344.
InParanoidP19785.
KOK08550.
OMAHSQQVPY.
OrthoDBEOG7288S1.
PhylomeDBP19785.
TreeFamTF323751.

Gene expression databases

ArrayExpressP19785.
BgeeP19785.
CleanExMM_ESR1.
GenevestigatorP19785.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR008946. 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]
PfamPF12743. ESR1_C. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF02159. Oest_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFPIRSF500101. ER-a. 1 hit.
PIRSF002527. ER-like_NR. 1 hit.
PRINTSPR00543. OESTROGENR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 2 hits.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284854.
PROP19785.
SOURCESearch...

Entry information

Entry nameESR1_MOUSE
AccessionPrimary (citable) accession number: P19785
Secondary accession number(s): Q9JJT5, Q9QY51, Q9QY52
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot