P19785 (ESR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	599 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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 withN NRIP1 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 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 process	Transcription Transcription regulation
Cellular component	Cell membrane Cytoplasm Golgi apparatus Membrane Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Lipid-binding Metal-binding Steroid-binding Zinc
Molecular function	Activator Receptor
PTM	Glycoprotein Lipoprotein Methylation Palmitate Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	androgen 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 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 estrogen receptor signaling pathway Inferred from electronic annotation. Source: GOC 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 cascade Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of gene expression Inferred from electronic annotation. Source: Compara 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 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 retinoic acid receptor signaling pathway Inferred from electronic annotation. Source: Compara 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 uterus development Inferred from genetic interaction PubMed 10976058. Source: MGI vagina development Inferred from genetic interaction PubMed 10976058. Source: MGI
Cellular_component	Golgi 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_function	chromatin binding Inferred from direct assay PubMed 18202148. Source: MGI core promoter sequence-specific DNA binding Inferred from electronic annotation. Source: Compara estrogen response element binding Inferred from electronic annotation. Source: Compara estrogen-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Inferred from electronic annotation. Source: Compara ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Inferred from direct assay PubMed 15322135. Source: MGI steroid binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCOA1	Q15788	2	EBI-346765,EBI-455189	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 599	599	Estrogen receptor		PRO_0000053621
Regions
	DNA binding	189 – 254	66	Nuclear receptor
	Zinc finger	189 – 209	21	NR C4-type
	Zinc finger	225 – 249	25	NR C4-type
	Region	1 – 188	188	Modulating (transactivation AF-1); mediates interaction with MACROD1 By similarity
	Region	35 – 178	144	Interaction with DDX5; self-association By similarity
	Region	35 – 47	13	Required for interaction with NCOA1 By similarity
	Region	189 – 314	126	Mediates interaction with DNTTIP2 By similarity
	Region	255 – 314	60	Hinge
	Region	266 – 599	334	Interaction with AKAP13 By similarity
	Region	268 – 599	332	Self-association By similarity
	Region	315 – 599	285	Transactivation AF-2 By similarity
	Region	315 – 555	241	Steroid-binding
	Compositional bias	64 – 72	9	Poly-Ala
Amino acid modifications
	Modified residue	108	1	Phosphoserine; by CDK2 By similarity
	Modified residue	110	1	Phosphoserine; by CDK2 By similarity
	Modified residue	122	1	Phosphoserine By similarity
	Modified residue	171	1	Phosphoserine; by CK2 By similarity
	Modified residue	264	1	Asymmetric dimethylarginine; by PRMT1 By similarity
	Modified residue	541	1	Phosphotyrosine; by Tyr-kinases By similarity
	Lipidation	451	1	S-palmitoyl cysteine Ref.16
	Glycosylation	10	1	O-linked (GlcNAc) Ref.10
	Glycosylation	50	1	O-linked (GlcNAc) Ref.10
	Glycosylation	575	1	O-linked (GlcNAc) Ref.9 Ref.10		CAR_000137
Natural variations
	Natural variant	591	1	E → Q in strain: SJL/J. Ref.4
Experimental info
	Mutagenesis	362	1	I → 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
	Mutagenesis	362	1	I → D: Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. Ref.6
	Mutagenesis	366	1	K → A: Greatly reduces transcriptional activity and estrogen-induced interaction with NCOA1. Ref.6
	Mutagenesis	366	1	K → D: Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. Ref.6
	Mutagenesis	366	1	K → L: Reduces transcriptional activity and estrogen-induced interaction with NCOA1. Ref.6
	Mutagenesis	371	1	F → A: Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcritional activity, abolishes estrogen-induced interaction with NCOA1. Ref.7
	Mutagenesis	376	1	L → 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
	Mutagenesis	376	1	L → D: Reduces transcriptional activity and estrogen-induced interaction with NCOA1. Ref.6
	Mutagenesis	380	1	V → 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
	Mutagenesis	380	1	V → D: Abolishes transcriptional activity and estrogen-induced interaction with NCOA1. Ref.6
	Mutagenesis	451	1	C → A: Loss of ZDHHC7 and ZDHHC21 binding. Loss of palmitoylation. Ref.16
	Mutagenesis	508	1	L → 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
	Mutagenesis	508	1	L → 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
	Mutagenesis	509	1	A → E: Reduces DNA-binding,, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression. Ref.7
	Mutagenesis	512	1	L → 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
	Mutagenesis	512	1	L → 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
	Mutagenesis	515	1	L → 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
	Mutagenesis	515	1	L → 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
	Mutagenesis	525	1	G → R: Abolishes estrogen binding; impairs repression of NF-kappa activity. Ref.7
	Mutagenesis	542	1	D → 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
	Mutagenesis	543 – 544	2	LL → AA: Abolishes estrogen-dependent NF-kappa B transcriptional repression, abolishes estrogen-induced interaction with NCOA1. Ref.6
	Mutagenesis	543	1	L → A: Abolishes estrogen-induced interaction with NCOA1. Ref.6
	Mutagenesis	546	1	E → 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
	Mutagenesis	547 – 548	2	ML → AA: No effect on estrogen-dependent NF-kappa B transcriptional repression, greatly impairs transcritional activity, abolishes estrogen-induced interaction with NCOA1.
	Mutagenesis	549	1	D → 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 conflict	269	1	L → M in AAF22561. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P19785 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 05F5E2FC21CC0A8B	FASTA	599	66,955
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00117980.
PIR	QRMSE. A40061.
RefSeq	NP_031982.1. NM_007956.4.
UniGene	Mm.463262. Mm.489063. Mm.9213.
3D structure databases
ProteinModelPortal	P19785.
SMR	P19785. Positions 184-555.
ModBase	Search...
Protein-protein interaction databases
IntAct	P19785. 5 interactions.
MINT	MINT-2835181.
PTM databases
GlycoSuiteDB	P19785.
PhosphoSite	P19785.
Proteomic databases
PRIDE	P19785.
Protocols and materials databases
DNASU	13982.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000067086; ENSMUSP00000070070; ENSMUSG00000019768. ENSMUST00000105589; ENSMUSP00000101214; ENSMUSG00000019768. ENSMUST00000105590; ENSMUSP00000101215; ENSMUSG00000019768.
GeneID	13982.
KEGG	mmu:13982.
UCSC	uc007egu.2. mouse.
Organism-specific databases
CTD	2099.
MGI	MGI:1352467. Esr1.
Phylogenomic databases
eggNOG	NOG320746.
GeneTree	ENSGT00700000104072.
HOGENOM	HOG000233468.
HOVERGEN	HBG108344.
InParanoid	P19785.
KO	K08550.
OMA	YRPSSDN.
OrthoDB	EOG4JM7PP.
Gene expression databases
ArrayExpress	P19785.
Bgee	P19785.
CleanEx	MM_ESR1.
Genevestigator	P19785.
GermOnline	ENSMUSG00000019768. Mus musculus.
Family and domain databases
Gene3D	1.10.565.10. 2 hits. 3.30.50.10. 1 hit.
InterPro	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]
Pfam	PF12743. ESR1_C. 1 hit. PF00104. Hormone_recep. 1 hit. PF02159. Oest_recep. 1 hit. PF00105. zf-C4. 1 hit. [Graphical view]
PIRSF	PIRSF500101. ER-a. 1 hit. PIRSF002527. ER-like_NR. 1 hit.
PRINTS	PR00543. OESTROGENR. PR00398. STRDHORMONER. PR00047. STROIDFINGER.
SMART	SM00430. HOLI. 1 hit. SM00399. ZnF_C4. 1 hit. [Graphical view]
SUPFAM	SSF48508. Str_ncl_receptor. 1 hit.
PROSITE	PS00031. NUCLEAR_REC_DBD_1. 1 hit. PS51030. NUCLEAR_REC_DBD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P19785.
ChEMBL	CHEMBL3065.
NextBio	284854.
SOURCE	Search...

Entry information

Entry name

ESR1_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 161 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program