ESR2_MOUSE
ID ESR2_MOUSE Reviewed; 530 AA.
AC O08537; B2RUC6; E9QKX7; O35635; O70519; Q8BG65; Q91Z86;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Estrogen receptor beta;
DE Short=ER-beta;
DE AltName: Full=Nuclear receptor subfamily 3 group A member 2;
GN Name=Esr2; Synonyms=Estrb, Nr3a2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Ovary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-530, AND MUTAGENESIS OF SER-105 AND
RP SER-139.
RC STRAIN=129/Sv; TISSUE=Ovary;
RX PubMed=9058381; DOI=10.1210/mend.11.3.9902;
RA Tremblay G.B., Tremblay A., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Labrie F., Giguere V.;
RT "Cloning, chromosomal localization, and functional analysis of the murine
RT estrogen receptor beta.";
RL Mol. Endocrinol. 11:353-365(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-530, AND CHARACTERIZATION.
RC TISSUE=Ovary;
RX PubMed=9280064; DOI=10.1210/mend.11.10.9989;
RA Pettersson K., Grandien K., Kuiper G.G.J.M., Gustafsson J.-A.;
RT "Mouse estrogen receptor beta forms estrogen response element-binding
RT heterodimers with estrogen receptor alpha.";
RL Mol. Endocrinol. 11:1486-1496(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-530 (ISOFORM 2), AND INDUCTION.
RC STRAIN=ddY; TISSUE=Calvaria;
RX PubMed=11878304; DOI=10.1359/jbmr.2002.17.3.394;
RA Dang Z.C., van Bezooijen R.L., Karperien M., Papapoulos S.E., Lowik C.W.;
RT "Exposure of KS483 cells to estrogen enhances osteogenesis and inhibits
RT adipogenesis.";
RL J. Bone Miner. Res. 17:394-405(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
RC TISSUE=Ovary;
RA Leygue E., Lu B., Dotzlaw H., Glor C., Watson P.H., Murphy L.C.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
RC TISSUE=Ovary;
RA Rosenfeld C.S., Lubahn D.B.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INTERACTION WITH NCOA3.
RX PubMed=9192892; DOI=10.1038/42652;
RA Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K.,
RA Rosenfeld M.G.;
RT "The transcriptional co-activator p/CIP binds CBP and mediates nuclear-
RT receptor function.";
RL Nature 387:677-684(1997).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=9607809; DOI=10.1210/endo.139.6.6028;
RA Rosenfeld C.S., Ganjam V.K., Taylor J.A., Yuan X., Stiehr J.R., Hardy M.P.,
RA Lubahn D.B.;
RT "Transcription and translation of estrogen receptor-beta in the male
RT reproductive tract of estrogen receptor-alpha knock-out and wild-type
RT mice.";
RL Endocrinology 139:2982-2987(1998).
RN [11]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
RC TISSUE=Ovary;
RX PubMed=9685228; DOI=10.1016/s0303-7207(98)00050-1;
RA Lu B., Leygue E., Dotzlaw H., Murphy L.J., Murphy L.C., Watson P.H.;
RT "Estrogen receptor-beta mRNA variants in human and murine tissues.";
RL Mol. Cell. Endocrinol. 138:199-203(1998).
RN [12]
RP PHOSPHORYLATION AT SER-87 AND SER-105.
RX PubMed=10230404; DOI=10.1016/s1097-2765(00)80479-7;
RA Tremblay A., Tremblay G.B., Labrie F., Giguere V.;
RT "Ligand-independent recruitment of SRC-1 to estrogen receptor beta through
RT phosphorylation of activation function AF-1.";
RL Mol. Cell 3:513-519(1999).
RN [13]
RP GLYCOSYLATION AT SER-61, AND PHOSPHORYLATION AT SER-61.
RX PubMed=10995228; DOI=10.1021/bi000755i;
RA Cheng X., Cole R.N., Zaia J., Hart G.W.;
RT "Alternative O-glycosylation/O-phosphorylation of the murine estrogen
RT receptor beta.";
RL Biochemistry 39:11609-11620(2000).
RN [14]
RP INTERACTION WITH NCOA6.
RX PubMed=10788465; DOI=10.1074/jbc.275.18.13510;
RA Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K.;
RT "Isolation and characterization of peroxisome proliferator-activated
RT receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR.";
RL J. Biol. Chem. 275:13510-13516(2000).
RN [15]
RP INTERACTION WITH RBM39.
RX PubMed=11704680; DOI=10.1074/jbc.m110417200;
RA Jung D.-J., Na S.-Y., Na D.S., Lee J.W.;
RT "Molecular cloning and characterization of CAPER, a novel coactivator of
RT activating protein-1 and estrogen receptors.";
RL J. Biol. Chem. 277:1229-1234(2002).
CC -!- FUNCTION: Nuclear hormone receptor. Binds estrogens with an affinity
CC similar to that of ESR1/ER-alpha, and activates expression of reporter
CC genes containing estrogen response elements (ERE) in an estrogen-
CC dependent manner. {ECO:0000250|UniProtKB:Q92731}.
CC -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ESR1.
CC Interacts with NCOA1, NCOA3, NCOA5 and NCOA6 coactivators, leading to a
CC strong increase of transcription of target genes. Interacts with UBE1C
CC and AKAP13. Interacts with DNTTIP2 (By similarity). Interacts with
CC CCDC62 in the presence of estradiol/E2; this interaction seems to
CC enhance the transcription of target genes. Interacts with DNAAF4.
CC Interacts with PRMT2. Interacts with CCAR2 (via N-terminus) in a
CC ligand-independent manner (By similarity). Interacts with RBM39, in the
CC presence of estradiol (E2) (PubMed:11704680).
CC {ECO:0000250|UniProtKB:Q62986, ECO:0000250|UniProtKB:Q92731,
CC ECO:0000269|PubMed:11704680}.
CC -!- INTERACTION:
CC O08537; P01101: Fos; NbExp=2; IntAct=EBI-2526214, EBI-4288185;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92731}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Beta-1;
CC IsoId=O08537-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta-2;
CC IsoId=O08537-2; Sequence=VSP_003693;
CC Name=3; Synonyms=Beta-5A;
CC IsoId=O08537-4; Sequence=VSP_003696;
CC Name=4;
CC IsoId=O08537-6; Sequence=VSP_042429, VSP_042430;
CC Name=5;
CC IsoId=O08537-7; Sequence=VSP_042431, VSP_042432;
CC -!- TISSUE SPECIFICITY: Expressed in prostate, ovary, Leydig cells and in
CC epithelium of the efferent ductules and of the initial segment of the
CC epididymis. {ECO:0000269|PubMed:9607809}.
CC -!- INDUCTION: Isoforms 1 and 2 are down-regulated by 17-beta-estradiol.
CC {ECO:0000269|PubMed:11878304}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- PTM: Phosphorylation at Ser-87 and Ser-105 recruits NCOA1.
CC {ECO:0000269|PubMed:10230404, ECO:0000269|PubMed:10995228}.
CC -!- MISCELLANEOUS: [Isoform 3]: Corresponds to exons 5 and 6 deletion.
CC {ECO:0000305|PubMed:9685228}.
CC -!- MISCELLANEOUS: [Isoform 4]: Corresponds to exon 5 deletion
CC (PubMed:9685228). May be produced at very low levels due to a premature
CC stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No
CC experimental confirmation available. {ECO:0000305|PubMed:9685228}.
CC -!- MISCELLANEOUS: [Isoform 5]: Corresponds to exon 6 deletion
CC (PubMed:9685228). May be produced at very low levels due to a premature
CC stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No
CC experimental confirmation available. {ECO:0000305|PubMed:9685228}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17919.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI41076.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI45330.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL15175.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC35719.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC35770.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK054290; BAC35719.1; ALT_INIT; mRNA.
DR EMBL; AK054413; BAC35770.1; ALT_INIT; mRNA.
DR EMBL; AC164121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141075; AAI41076.1; ALT_INIT; mRNA.
DR EMBL; BC145329; AAI45330.1; ALT_INIT; mRNA.
DR EMBL; U81451; AAB51132.1; -; mRNA.
DR EMBL; AJ000220; CAA03949.1; -; Genomic_DNA.
DR EMBL; AY054413; AAL15175.1; ALT_INIT; mRNA.
DR EMBL; AF067422; AAC17919.1; ALT_INIT; mRNA.
DR EMBL; AF063853; AAC16656.1; -; mRNA.
DR RefSeq; NP_034287.3; NM_010157.3.
DR RefSeq; NP_997590.1; NM_207707.1.
DR AlphaFoldDB; O08537; -.
DR SMR; O08537; -.
DR BioGRID; 199522; 3.
DR IntAct; O08537; 2.
DR STRING; 10090.ENSMUSP00000098849; -.
DR BindingDB; O08537; -.
DR ChEMBL; CHEMBL2995; -.
DR DrugCentral; O08537; -.
DR GuidetoPHARMACOLOGY; 621; -.
DR GlyConnect; 146; 1 O-Linked glycan (1 site).
DR GlyGen; O08537; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O08537; -.
DR PhosphoSitePlus; O08537; -.
DR PaxDb; O08537; -.
DR PRIDE; O08537; -.
DR Antibodypedia; 11874; 1767 antibodies from 45 providers.
DR DNASU; 13983; -.
DR Ensembl; ENSMUST00000101291; ENSMUSP00000098849; ENSMUSG00000021055. [O08537-2]
DR Ensembl; ENSMUST00000110421; ENSMUSP00000106051; ENSMUSG00000021055. [O08537-1]
DR Ensembl; ENSMUST00000133564; ENSMUSP00000138637; ENSMUSG00000021055. [O08537-6]
DR GeneID; 13983; -.
DR KEGG; mmu:13983; -.
DR UCSC; uc007nxu.1; mouse. [O08537-2]
DR UCSC; uc007nxv.1; mouse. [O08537-1]
DR CTD; 2100; -.
DR MGI; MGI:109392; Esr2.
DR VEuPathDB; HostDB:ENSMUSG00000021055; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000156116; -.
DR InParanoid; O08537; -.
DR OMA; SHKEFSQ; -.
DR OrthoDB; 487299at2759; -.
DR TreeFam; TF323751; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-8939211; ESR-mediated signaling.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR BioGRID-ORCS; 13983; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Esr2; mouse.
DR PRO; PR:O08537; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O08537; protein.
DR Bgee; ENSMUSG00000021055; Expressed in animal zygote and 67 other tissues.
DR ExpressionAtlas; O08537; baseline and differential.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:1903924; F:estradiol binding; ISO:MGI.
DR GO; GO:0099130; F:estrogen binding; ISO:MGI.
DR GO; GO:0034056; F:estrogen response element binding; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0042562; F:hormone binding; ISO:MGI.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; ISO:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:MGI.
DR GO; GO:0003707; F:nuclear steroid receptor activity; ISO:MGI.
DR GO; GO:0097159; F:organic cyclic compound binding; ISO:MGI.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
DR GO; GO:1990239; F:steroid hormone binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IMP:MGI.
DR GO; GO:0001662; P:behavioral fear response; ISO:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:MGI.
DR GO; GO:0060743; P:epithelial cell maturation involved in prostate gland development; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0044849; P:estrous cycle; ISO:MGI.
DR GO; GO:0008628; P:hormone-mediated apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IMP:MGI.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISO:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IMP:MGI.
DR GO; GO:0048521; P:negative regulation of behavior; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:2000252; P:negative regulation of feeding behavior; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0033574; P:response to testosterone; ISO:MGI.
DR GO; GO:0060011; P:Sertoli cell proliferation; ISO:MGI.
DR GO; GO:0060065; P:uterus development; IGI:MGI.
DR GO; GO:0060068; P:vagina development; IGI:MGI.
DR GO; GO:0042311; P:vasodilation; ISO:MGI.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR021064; ER-beta-like_N.
DR InterPro; IPR028355; ER-beta/gamma.
DR InterPro; IPR024178; Est_rcpt/est-rel_rcp.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF12497; ERbeta_N; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PIRSF; PIRSF500102; ER-b; 1.
DR PIRSF; PIRSF002527; ER-like_NR; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Glycoprotein; Lipid-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome;
KW Steroid-binding; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..530
FT /note="Estrogen receptor beta"
FT /id="PRO_0000053644"
FT DOMAIN 264..498
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 149..214
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 149..169
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 185..209
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..148
FT /note="Modulating"
FT REGION 506..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000269|PubMed:10995228"
FT MOD_RES 87
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:10230404"
FT MOD_RES 105
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:10230404"
FT CARBOHYD 61
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000269|PubMed:10995228"
FT /id="CAR_000201"
FT VAR_SEQ 319..409
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003696"
FT VAR_SEQ 319..343
FT /note="FVELSLLDQVRLLESCWMEVLMVGL -> MRGSAWKGFWKSLTCSWRRRHGS
FT VS (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_042429"
FT VAR_SEQ 344..530
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_042430"
FT VAR_SEQ 364
FT /note="R -> RSSEDPHWHVAQTKSAVPR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11878304,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_003693"
FT VAR_SEQ 365..377
FT /note="DEGKCVEGILEIF -> YVPLGYRKPGSRE (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_042431"
FT VAR_SEQ 378..530
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_042432"
FT MUTAGEN 105
FT /note="S->A: Abolishes stimulatory effect of Ras."
FT /evidence="ECO:0000269|PubMed:9058381"
FT MUTAGEN 139
FT /note="S->A: No loss of the stimulatory effect of Ras."
FT /evidence="ECO:0000269|PubMed:9058381"
FT CONFLICT 47
FT /note="T -> A (in Ref. 5; CAA03949)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="A -> T (in Ref. 5; CAA03949)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="S -> N (in Ref. 5; CAA03949)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="D -> G (in Ref. 1; AAB51132 and 6; AAL15175)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="P -> H (in Ref. 5; CAA03949)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="G -> R (in Ref. 5; CAA03949)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="E -> G (in Ref. 5; CAA03949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 59070 MW; BEFA25F62650A8D4 CRC64;
MEIKNSPSSL TSPASYNCSQ SILPLEHGPI YIPSSYVESR HEYSAMTFYS PAVMNYSVPS
STGNLEGGPV RQTASPNVLW PTSGHLSPLA THCQSSLLYA EPQKSPWCEA RSLEHTLPVN
RETLKRKLGG SGCASPVTSP SAKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH
NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRIVR RQRSASEQVH
CLNKAKRTSG HTPRVKELLL NSLSPEQLVL TLLEAEPPNV LVSRPSMPFT EASMMMSLTK
LADKELVHMI GWAKKIPGFV ELSLLDQVRL LESCWMEVLM VGLMWRSIDH PGKLIFAPDL
VLDRDEGKCV EGILEIFDML LATTARFREL KLQHKEYLCV KAMILLNSSM YPLATASQEA
ESSRKLTHLL NAVTDALVWV ISKSGISSQQ QSVRLANLLM LLSHVRHISN KGMEHLLSMK
CKNVVPVYDL LLEMLNAHTL RGYKSSISGS ECCSTEDSKS KEGSQNLQSQ
