ESR2_HUMAN
ID ESR2_HUMAN Reviewed; 530 AA.
AC Q92731; A8K8K5; G3V5M5; O60608; O60685; O60702; O60703; O75583; O75584;
AC Q0MWT5; Q0MWT6; Q86Z31; Q9UEV6; Q9UHD3; Q9UQK9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 238.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9473491; DOI=10.1006/bbrc.1997.7893;
RA Ogawa S., Inoue S., Watanabe T., Hiroi H., Orimo A., Hosoi T., Ouchi Y.,
RA Muramatsu M.;
RT "The complete primary structure of human estrogen receptor beta (hERbeta)
RT and its heterodimerization with ER alpha in vivo and in vitro.";
RL Biochem. Biophys. Res. Commun. 243:122-126(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 409-482 (ISOFORM 5), NUCLEOTIDE SEQUENCE [MRNA] OF 409-472
RP (ISOFORM 6), AND TISSUE SPECIFICITY (ISOFORMS 1; 2; 4; 5 AND 6).
RC TISSUE=Mammary gland, and Testis;
RX PubMed=9636657; DOI=10.1006/bbrc.1998.8738;
RA Moore J.T., McKee D.D., Slentz-Kesler K., Moore L.B., Jones S.A.,
RA Horne E.L., Su J.-L., Kliewer S.A., Lehmann J.M., Willson T.M.;
RT "Cloning and characterization of human estrogen receptor beta isoforms.";
RL Biochem. Biophys. Res. Commun. 247:75-78(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), AND
RP INTERACTION WITH ESR1 (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=9671811; DOI=10.1093/nar/26.15.3505;
RA Ogawa S., Inoue S., Watanabe T., Orimo A., Hosoi T., Ouchi Y.,
RA Muramatsu M.;
RT "Molecular cloning and characterization of human estrogen receptor beta cx:
RT a potential inhibitor of estrogen action in human.";
RL Nucleic Acids Res. 26:3505-3512(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
RC TISSUE=Prostate;
RX PubMed=16938840; DOI=10.1073/pnas.0605676103;
RA Leung Y.K., Mak P., Hassan S., Ho S.M.;
RT "Estrogen receptor (ER)-beta isoforms: a key to understanding ER-beta
RT signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13162-13167(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RX PubMed=10964723; DOI=10.1006/bbrc.2000.3363;
RA Li L.C., Yeh C.C., Nojima D., Dahiya R.;
RT "Cloning and characterization of human estrogen receptor beta promoter.";
RL Biochem. Biophys. Res. Commun. 275:682-689(2000).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-530 (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Testis;
RX PubMed=8769313; DOI=10.1016/0014-5793(96)00782-x;
RA Mosselman S., Polman J., Dijkema R.;
RT "ER beta: identification and characterization of a novel human estrogen
RT receptor.";
RL FEBS Lett. 392:49-53(1996).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-530 (ISOFORMS 7 AND 8).
RC TISSUE=Endometrium;
RA Brandenberger A.W., Lebovic D., Taylor R.N., Jaffe R.B.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP INTERACTION WITH NCOA3.
RX PubMed=9267036; DOI=10.1016/s0092-8674(00)80516-4;
RA Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L.,
RA Privalsky M.L., Nakatani Y., Evans R.M.;
RT "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and
RT forms a multimeric activation complex with P/CAF and CBP/p300.";
RL Cell 90:569-580(1997).
RN [15]
RP FUNCTION.
RX PubMed=9325313; DOI=10.1074/jbc.272.41.25832;
RA Pace P., Taylor J., Suntharalingam S., Coombes R.C., Ali S.;
RT "Human estrogen receptor beta binds DNA in a manner similar to and
RT dimerizes with estrogen receptor alpha.";
RL J. Biol. Chem. 272:25832-25838(1997).
RN [16]
RP INTERACTION WITH NCOA6.
RX PubMed=10681503; DOI=10.1074/jbc.275.8.5308;
RA Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.;
RT "Cloning and characterization of RAP250, a nuclear receptor coactivator.";
RL J. Biol. Chem. 275:5308-5317(2000).
RN [17]
RP INTERACTION WITH NCOA5.
RX PubMed=11113208; DOI=10.1128/mcb.21.1.343-353.2001;
RA Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F., Giguere V.;
RT "CIA, a novel estrogen receptor coactivator with a bifunctional nuclear
RT receptor interacting determinant.";
RL Mol. Cell. Biol. 21:343-353(2001).
RN [18]
RP INTERACTION WITH AKAP13.
RX PubMed=11579095; DOI=10.1074/jbc.m106927200;
RA Driggers P.H., Segars J.H., Rubino D.M.;
RT "The proto-oncoprotein Brx activates estrogen receptor beta by a p38
RT mitogen-activated protein kinase pathway.";
RL J. Biol. Chem. 276:46792-46797(2001).
RN [19]
RP INTERACTION WITH PRMT2.
RX PubMed=12039952; DOI=10.1074/jbc.m201053200;
RA Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
RT "Identification of protein arginine methyltransferase 2 as a coactivator
RT for estrogen receptor alpha.";
RL J. Biol. Chem. 277:28624-28630(2002).
RN [20]
RP RETRACTED PAPER.
RX PubMed=12415108; DOI=10.1073/pnas.192569699;
RA Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
RT "Estrogen receptor-interacting protein that modulates its nongenomic
RT activity-crosstalk with Src/Erk phosphorylation cascade.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002).
RN [21]
RP RETRACTION NOTICE OF PUBMED:12415108.
RX PubMed=19666546; DOI=10.1073/pnas.0908685106;
RA Wong C.W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
RL Proc. Natl. Acad. Sci. U.S.A. 106:14180-14180(2009).
RN [22]
RP INTERACTION WITH DNTTIP2.
RX PubMed=15047147; DOI=10.1016/j.bbrc.2004.02.179;
RA Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M.,
RA Zhu Y.-J.;
RT "ERBP, a novel estrogen receptor binding protein enhancing the activity of
RT estrogen receptor.";
RL Biochem. Biophys. Res. Commun. 317:54-59(2004).
RN [23]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [24]
RP INTERACTION WITH TXNRD1.
RX PubMed=15199063; DOI=10.1074/jbc.m402753200;
RA Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A.,
RA Spyrou G.;
RT "An alternative splicing variant of the selenoprotein thioredoxin reductase
RT is a modulator of estrogen signaling.";
RL J. Biol. Chem. 279:38721-38729(2004).
RN [25]
RP PHOSPHORYLATION AT SER-87 AND SER-105, AND MUTAGENESIS OF SER-87 AND
RP SER-105.
RX PubMed=15862947; DOI=10.1016/j.jsbmb.2005.02.001;
RA St-Laurent V., Sanchez M., Charbonneau C., Tremblay A.;
RT "Selective hormone-dependent repression of estrogen receptor beta by a p38-
RT activated ErbB2/ErbB3 pathway.";
RL J. Steroid Biochem. Mol. Biol. 94:23-37(2005).
RN [26]
RP INTERACTION WITH CCDC62, AND SUBCELLULAR LOCATION.
RX PubMed=19126643; DOI=10.1093/carcin/bgn288;
RA Chen M., Ni J., Chang H.C., Lin C.Y., Muyan M., Yeh S.;
RT "CCDC62/ERAP75 functions as a coactivator to enhance estrogen receptor
RT beta-mediated transactivation and target gene expression in prostate cancer
RT cells.";
RL Carcinogenesis 30:841-850(2009).
RN [27]
RP FUNCTION, INTERACTION WITH CCAR2, AND SUBCELLULAR LOCATION.
RX PubMed=20074560; DOI=10.1016/j.bbrc.2010.01.025;
RA Koyama S., Wada-Hiraike O., Nakagawa S., Tanikawa M., Hiraike H.,
RA Miyamoto Y., Sone K., Oda K., Fukuhara H., Nakagawa K., Kato S., Yano T.,
RA Taketani Y.;
RT "Repression of estrogen receptor beta function by putative tumor suppressor
RT DBC1.";
RL Biochem. Biophys. Res. Commun. 392:357-362(2010).
RN [28]
RP FUNCTION, VARIANTS VAL-84; ASN-181 DEL AND ARG-426, AND CHARACTERIZATION OF
RP VARIANTS VAL-84; ASN-181 DEL AND ARG-426.
RX PubMed=29261182; DOI=10.1038/gim.2017.163;
RG ESR2 STUDY GROUP;
RA Baetens D., Gueran T., Mendonca B.B., Gomes N.L., De Cauwer L., Peelman F.,
RA Verdin H., Vuylsteke M., Van der Linden M., Atay Z., Bereket A.,
RA de Krijger R.R., Preter K., Domenice S., Turan S., Stoop H.,
RA Looijenga L.H., De Bosscher K., Cools M., De Baere E.;
RT "Biallelic and monoallelic ESR2 variants associated with 46,XY disorders of
RT sex development.";
RL Genet. Med. 20:717-727(2018).
RN [29]
RP FUNCTION, INVOLVEMENT IN ODG8, VARIANT ODG8 ARG-314, AND CHARACTERIZATION
RP OF VARIANT ODG8 ARG-314.
RX PubMed=30113650; DOI=10.1210/jc.2018-00769;
RA Lang-Muritano M., Sproll P., Wyss S., Kolly A., Huerlimann R., Konrad D.,
RA Biason-Lauber A.;
RT "Early-onset complete ovarian failure and lack of puberty in a woman with
RT mutated estrogen receptor beta (ESR2).";
RL J. Clin. Endocrinol. Metab. 103:3748-3756(2018).
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 (PubMed:20074560). {ECO:0000269|PubMed:20074560,
CC ECO:0000269|PubMed:29261182, ECO:0000269|PubMed:30113650,
CC ECO:0000269|PubMed:9325313}.
CC -!- FUNCTION: [Isoform 2]: Lacks ligand binding ability and has no or only
CC very low ERE binding activity resulting in the loss of ligand-dependent
CC transactivation ability. {ECO:0000269|PubMed:9671811}.
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 Interacts with AKAP13. Interacts with DNTTIP2. Interacts with isoform 4
CC of TXNRD1. Interacts with CCDC62 in the presence of estradiol/E2; this
CC interaction seems to enhance the transcription of target genes,
CC including cyclin-D1/CCND1 AP-1 promoter. Interacts with DNAAF4 (By
CC similarity). Interacts with PRMT2. Interacts with CCAR2 (via N-
CC terminus) in a ligand-independent manner. Interacts with RBM39, in the
CC presence of estradiol (E2) (By similarity).
CC {ECO:0000250|UniProtKB:O08537, ECO:0000250|UniProtKB:Q62986,
CC ECO:0000269|PubMed:10681503, ECO:0000269|PubMed:11113208,
CC ECO:0000269|PubMed:11579095, ECO:0000269|PubMed:12039952,
CC ECO:0000269|PubMed:15047147, ECO:0000269|PubMed:15199063,
CC ECO:0000269|PubMed:19126643, ECO:0000269|PubMed:20074560,
CC ECO:0000269|PubMed:9267036}.
CC -!- SUBUNIT: [Isoform 2]: Preferentially forms a heterodimer with ESR1
CC rather than ESR2 isoform 1 and inhibits DNA-binding by ESR1.
CC {ECO:0000269|PubMed:9671811}.
CC -!- INTERACTION:
CC Q92731; P38398: BRCA1; NbExp=4; IntAct=EBI-78505, EBI-349905;
CC Q92731; P29279: CCN2; NbExp=5; IntAct=EBI-78505, EBI-2835375;
CC Q92731; P00533: EGFR; NbExp=8; IntAct=EBI-78505, EBI-297353;
CC Q92731; P03372-1: ESR1; NbExp=5; IntAct=EBI-78505, EBI-15606245;
CC Q92731; O43524: FOXO3; NbExp=4; IntAct=EBI-78505, EBI-1644164;
CC Q92731; O15162: PLSCR1; NbExp=4; IntAct=EBI-78505, EBI-740019;
CC Q92731; P53041: PPP5C; NbExp=4; IntAct=EBI-78505, EBI-716663;
CC Q92731; Q16881-4: TXNRD1; NbExp=3; IntAct=EBI-78505, EBI-9080335;
CC Q92731; Q60974: Ncor1; Xeno; NbExp=6; IntAct=EBI-78505, EBI-349004;
CC Q92731-1; Q6P9F0: CCDC62; NbExp=6; IntAct=EBI-11176604, EBI-11176612;
CC Q92731-3; O95273: CCNDBP1; NbExp=3; IntAct=EBI-12259414, EBI-748961;
CC Q92731-3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12259414, EBI-3867333;
CC Q92731-3; P49639: HOXA1; NbExp=3; IntAct=EBI-12259414, EBI-740785;
CC Q92731-3; O00505: KPNA3; NbExp=3; IntAct=EBI-12259414, EBI-358297;
CC Q92731-3; Q5T749: KPRP; NbExp=3; IntAct=EBI-12259414, EBI-10981970;
CC Q92731-3; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-12259414, EBI-11962084;
CC Q92731-3; Q99750: MDFI; NbExp=3; IntAct=EBI-12259414, EBI-724076;
CC Q92731-3; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-12259414, EBI-10271199;
CC Q92731-3; O15162: PLSCR1; NbExp=4; IntAct=EBI-12259414, EBI-740019;
CC Q92731-3; Q12800: TFCP2; NbExp=3; IntAct=EBI-12259414, EBI-717422;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:19126643, ECO:0000269|PubMed:20074560}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1; Synonyms=Beta-1;
CC IsoId=Q92731-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta-2, CX;
CC IsoId=Q92731-2; Sequence=VSP_003689;
CC Name=3; Synonyms=Beta-2A;
CC IsoId=Q92731-3; Sequence=VSP_003684, VSP_003686;
CC Name=4; Synonyms=Beta-3;
CC IsoId=Q92731-4; Sequence=VSP_003690;
CC Name=5; Synonyms=Beta-4;
CC IsoId=Q92731-5; Sequence=VSP_003691;
CC Name=6; Synonyms=Beta-5;
CC IsoId=Q92731-6; Sequence=VSP_003692;
CC Name=7; Synonyms=Beta-5A;
CC IsoId=Q92731-7; Sequence=VSP_003685;
CC Name=8; Synonyms=Beta-6;
CC IsoId=Q92731-8; Sequence=VSP_003687, VSP_003688;
CC Name=9;
CC IsoId=Q92731-9; Sequence=VSP_055746, VSP_055747;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in testis and ovary, and at
CC a lower level in heart, brain, placenta, liver, skeletal muscle,
CC spleen, thymus, prostate, colon, bone marrow, mammary gland and uterus.
CC Also found in uterine bone, breast, and ovarian tumor cell lines, but
CC not in colon and liver tumors. {ECO:0000269|PubMed:9636657}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in spleen, thymus, testis
CC and ovary and at a lower level in skeletal muscle, prostate, colon,
CC small intestine, leukocytes, bone marrow, mammary gland and uterus.
CC {ECO:0000269|PubMed:9636657}.
CC -!- TISSUE SPECIFICITY: [Isoform 4]: Expressed in the testis.
CC {ECO:0000269|PubMed:9636657}.
CC -!- TISSUE SPECIFICITY: [Isoform 5]: Expressed in testis, and at a lower
CC level in spleen, thymus, ovary, mammary gland and uterus.
CC {ECO:0000269|PubMed:9636657}.
CC -!- TISSUE SPECIFICITY: [Isoform 6]: Expressed in testis, placenta,
CC skeletal muscle, spleen and leukocytes, and at a lower level in heart,
CC lung, liver, kidney, pancreas, thymus, prostate, colon, small
CC intestine, bone marrow, mammary gland and uterus. Not expressed in
CC brain. {ECO:0000269|PubMed:9636657}.
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:15862947}.
CC -!- DISEASE: Ovarian dysgenesis 8 (ODG8) [MIM:618187]: An autosomal
CC dominant form of ovarian dysgenesis, a disorder characterized by lack
CC of spontaneous pubertal development, primary amenorrhea, uterine
CC hypoplasia, and hypergonadotropic hypogonadism as a result of streak
CC gonads. {ECO:0000269|PubMed:30113650}. Note=The disease may be caused
CC by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Does not form homodimers. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Does not form homodimers. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Had previously been shown to interact with PELP1. However this
CC paper was retracted as cell-based data was viewed as unreliable.
CC {ECO:0000305|PubMed:12415108, ECO:0000305|PubMed:19666546}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA67555.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ESR2ID40500ch14q23.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Estrogen receptor entry;
CC URL="https://en.wikipedia.org/wiki/Estrogen_receptor";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB006590; BAA24953.1; -; mRNA.
DR EMBL; AF051427; AAC05985.1; -; mRNA.
DR EMBL; AF051428; AAC05751.1; -; mRNA.
DR EMBL; AF061054; AAC39784.1; -; mRNA.
DR EMBL; AF061055; AAC39785.1; -; mRNA.
DR EMBL; AF060555; AAC15234.1; -; mRNA.
DR EMBL; AF124790; AAD32580.1; -; mRNA.
DR EMBL; AF047463; AAC03786.1; -; mRNA.
DR EMBL; AB006589; BAA31966.1; -; mRNA.
DR EMBL; DQ838582; ABH09189.1; -; mRNA.
DR EMBL; DQ838583; ABH09190.1; -; mRNA.
DR EMBL; AY785359; AAV31779.1; -; Genomic_DNA.
DR EMBL; AK292370; BAF85059.1; -; mRNA.
DR EMBL; AL161756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80850.1; -; Genomic_DNA.
DR EMBL; BC024181; AAH24181.1; -; mRNA.
DR EMBL; AF191544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X99101; CAA67555.1; ALT_INIT; mRNA.
DR EMBL; AF074598; AAC25602.1; -; mRNA.
DR EMBL; AF074599; AAC25603.1; -; mRNA.
DR CCDS; CCDS32096.1; -. [Q92731-2]
DR CCDS; CCDS55920.1; -. [Q92731-5]
DR CCDS; CCDS61469.1; -. [Q92731-7]
DR CCDS; CCDS61470.1; -. [Q92731-9]
DR CCDS; CCDS9762.1; -. [Q92731-1]
DR PIR; JC5939; JC5939.
DR PIR; PW0044; PW0044.
DR PIR; S71400; S71400.
DR RefSeq; NP_001035365.1; NM_001040275.1. [Q92731-2]
DR RefSeq; NP_001201831.1; NM_001214902.1. [Q92731-5]
DR RefSeq; NP_001258805.1; NM_001271876.1. [Q92731-9]
DR RefSeq; NP_001258806.1; NM_001271877.1. [Q92731-7]
DR RefSeq; NP_001278641.1; NM_001291712.1. [Q92731-2]
DR RefSeq; NP_001278652.1; NM_001291723.1. [Q92731-2]
DR RefSeq; NP_001428.1; NM_001437.2. [Q92731-1]
DR RefSeq; XP_016876568.1; XM_017021079.1. [Q92731-1]
DR RefSeq; XP_016876569.1; XM_017021080.1. [Q92731-1]
DR RefSeq; XP_016876570.1; XM_017021081.1. [Q92731-1]
DR RefSeq; XP_016876571.1; XM_017021082.1. [Q92731-1]
DR RefSeq; XP_016876572.1; XM_017021083.1. [Q92731-1]
DR RefSeq; XP_016876573.1; XM_017021084.1. [Q92731-2]
DR PDB; 1L2J; X-ray; 2.95 A; A/B=256-505.
DR PDB; 1NDE; X-ray; 3.00 A; A=256-501.
DR PDB; 1QKM; X-ray; 1.80 A; A=255-509.
DR PDB; 1U3Q; X-ray; 2.40 A; A/B/C/D=261-500.
DR PDB; 1U3R; X-ray; 2.21 A; A/B=261-501.
DR PDB; 1U3S; X-ray; 2.50 A; A/B=261-500.
DR PDB; 1U9E; X-ray; 2.40 A; A/B=261-501.
DR PDB; 1X76; X-ray; 2.20 A; A/B=261-500.
DR PDB; 1X78; X-ray; 2.30 A; A/B=261-500.
DR PDB; 1X7B; X-ray; 2.30 A; A/B=261-500.
DR PDB; 1X7J; X-ray; 2.30 A; A/B=261-500.
DR PDB; 1YY4; X-ray; 2.70 A; A/B=263-530.
DR PDB; 1YYE; X-ray; 2.03 A; A/B=263-530.
DR PDB; 1ZAF; X-ray; 2.20 A; A/B=263-500.
DR PDB; 2FSZ; X-ray; 2.20 A; A/B=257-502.
DR PDB; 2GIU; X-ray; 2.20 A; A=260-500.
DR PDB; 2I0G; X-ray; 2.50 A; A/B=256-505.
DR PDB; 2JJ3; X-ray; 2.28 A; A/B=256-505.
DR PDB; 2NV7; X-ray; 2.10 A; A/B=263-500.
DR PDB; 2QTU; X-ray; 2.53 A; A/B=256-505.
DR PDB; 2YJD; X-ray; 1.93 A; A/B=261-500.
DR PDB; 2YLY; X-ray; 3.20 A; A/B=260-500.
DR PDB; 2Z4B; X-ray; 2.34 A; A/B=256-505.
DR PDB; 3OLL; X-ray; 1.50 A; A/B=261-500.
DR PDB; 3OLS; X-ray; 2.20 A; A/B=261-500.
DR PDB; 3OMO; X-ray; 2.21 A; A/B=261-500.
DR PDB; 3OMP; X-ray; 2.05 A; A/B=261-500.
DR PDB; 3OMQ; X-ray; 1.97 A; A/B=261-500.
DR PDB; 4J24; X-ray; 2.10 A; A/B/C/D=261-500.
DR PDB; 4J26; X-ray; 2.30 A; A/B=261-500.
DR PDB; 4ZI1; X-ray; 2.10 A; A=262-509.
DR PDB; 5TOA; X-ray; 2.50 A; A/B=262-509.
DR PDBsum; 1L2J; -.
DR PDBsum; 1NDE; -.
DR PDBsum; 1QKM; -.
DR PDBsum; 1U3Q; -.
DR PDBsum; 1U3R; -.
DR PDBsum; 1U3S; -.
DR PDBsum; 1U9E; -.
DR PDBsum; 1X76; -.
DR PDBsum; 1X78; -.
DR PDBsum; 1X7B; -.
DR PDBsum; 1X7J; -.
DR PDBsum; 1YY4; -.
DR PDBsum; 1YYE; -.
DR PDBsum; 1ZAF; -.
DR PDBsum; 2FSZ; -.
DR PDBsum; 2GIU; -.
DR PDBsum; 2I0G; -.
DR PDBsum; 2JJ3; -.
DR PDBsum; 2NV7; -.
DR PDBsum; 2QTU; -.
DR PDBsum; 2YJD; -.
DR PDBsum; 2YLY; -.
DR PDBsum; 2Z4B; -.
DR PDBsum; 3OLL; -.
DR PDBsum; 3OLS; -.
DR PDBsum; 3OMO; -.
DR PDBsum; 3OMP; -.
DR PDBsum; 3OMQ; -.
DR PDBsum; 4J24; -.
DR PDBsum; 4J26; -.
DR PDBsum; 4ZI1; -.
DR PDBsum; 5TOA; -.
DR AlphaFoldDB; Q92731; -.
DR SMR; Q92731; -.
DR BioGRID; 108404; 2282.
DR CORUM; Q92731; -.
DR DIP; DIP-5966N; -.
DR ELM; Q92731; -.
DR IntAct; Q92731; 461.
DR MINT; Q92731; -.
DR STRING; 9606.ENSP00000343925; -.
DR BindingDB; Q92731; -.
DR ChEMBL; CHEMBL242; -.
DR DrugBank; DB07638; (3AS,4R,9BR)-2,2-DIFLUORO-4-(4-HYDROXYPHENYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-8-OL.
DR DrugBank; DB07036; (3aS,4R,9bR)-2,2-difluoro-4-(4-hydroxyphenyl)-6-(methoxymethyl)-1,2,3,3a,4,9b-hexahydrocyclopenta[c]chromen-8-ol.
DR DrugBank; DB08020; (3AS,4R,9BR)-4-(4-HYDROXYPHENYL)-6-(METHOXYMETHYL)-1,2,3,3A,4,9B-HEXAHYDROCYCLOPENTA[C]CHROMEN-8-OL.
DR DrugBank; DB07757; (9aS)-4-bromo-9a-butyl-7-hydroxy-1,2,9,9a-tetrahydro-3H-fluoren-3-one.
DR DrugBank; DB07119; 1-CHLORO-6-(4-HYDROXYPHENYL)-2-NAPHTHOL.
DR DrugBank; DB07702; 17alpha-Estriol.
DR DrugBank; DB07032; 2-(4-HYDROXY-PHENYL)BENZOFURAN-5-OL.
DR DrugBank; DB07009; 2-(5-HYDROXY-NAPHTHALEN-1-YL)-1,3-BENZOOXAZOL-6-OL.
DR DrugBank; DB13869; 2-Methoxy-6-{(E)-[(4-methylphenyl)imino]methyl}phenol.
DR DrugBank; DB07236; 3-(6-HYDROXY-NAPHTHALEN-2-YL)-BENZO[D]ISOOXAZOL-6-OL.
DR DrugBank; DB07230; 3-BROMO-6-HYDROXY-2-(4-HYDROXYPHENYL)-1H-INDEN-1-ONE.
DR DrugBank; DB04020; 4-(2-{[4-{[3-(4-Chlorophenyl)Propyl]Sulfanyl}-6-(1-Piperazinyl)-1,3,5-Triazin-2-Yl]Amino}Ethyl)Phenol.
DR DrugBank; DB07150; 4-(4-HYDROXYPHENYL)-1-NAPHTHALDEHYDE OXIME.
DR DrugBank; DB06937; 4-(6-HYDROXY-BENZO[D]ISOXAZOL-3-YL)BENZENE-1,3-DIOL.
DR DrugBank; DB03882; 5-Alpha-Androstane-3-Beta,17beta-Diol.
DR DrugBank; DB07198; 5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-CARBONITRILE.
DR DrugBank; DB06927; [5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-YL]ACETONITRILE.
DR DrugBank; DB04468; Afimoxifene.
DR DrugBank; DB06249; Arzoxifene.
DR DrugBank; DB06401; Bazedoxifene.
DR DrugBank; DB01878; Benzophenone.
DR DrugBank; DB05882; CHF 4227.
DR DrugBank; DB00286; Conjugated estrogens.
DR DrugBank; DB00255; Diethylstilbestrol.
DR DrugBank; DB11219; Enzacamene.
DR DrugBank; DB11674; Equol.
DR DrugBank; DB06875; ERB-196.
DR DrugBank; DB07933; Erteberel.
DR DrugBank; DB12235; Estetrol.
DR DrugBank; DB00783; Estradiol.
DR DrugBank; DB13952; Estradiol acetate.
DR DrugBank; DB13953; Estradiol benzoate.
DR DrugBank; DB13954; Estradiol cypionate.
DR DrugBank; DB13955; Estradiol dienanthate.
DR DrugBank; DB13956; Estradiol valerate.
DR DrugBank; DB01196; Estramustine.
DR DrugBank; DB04573; Estriol.
DR DrugBank; DB14641; Estriol tripropionate.
DR DrugBank; DB00655; Estrone.
DR DrugBank; DB04574; Estrone sulfate.
DR DrugBank; DB09086; Eugenol.
DR DrugBank; DB15690; Fluoroestradiol F-18.
DR DrugBank; DB01645; Genistein.
DR DrugBank; DB03860; ICI-164384.
DR DrugBank; DB06202; Lasofoxifene.
DR DrugBank; DB05052; MF101.
DR DrugBank; DB03467; Naringenin.
DR DrugBank; DB09535; Octocrylene.
DR DrugBank; DB01428; Oxybenzone.
DR DrugBank; DB02983; Para-Mercury-Benzenesulfonic Acid.
DR DrugBank; DB02746; Phthalic Acid.
DR DrugBank; DB01708; Prasterone.
DR DrugBank; DB06832; Prinaberel.
DR DrugBank; DB00396; Progesterone.
DR DrugBank; DB02757; Pyrazole.
DR DrugBank; DB04216; Quercetin.
DR DrugBank; DB00481; Raloxifene.
DR DrugBank; DB00675; Tamoxifen.
DR DrugBank; DB05966; TAS-108.
DR DrugBank; DB01108; Trilostane.
DR DrugCentral; Q92731; -.
DR GuidetoPHARMACOLOGY; 621; -.
DR MoonDB; Q92731; Predicted.
DR iPTMnet; Q92731; -.
DR PhosphoSitePlus; Q92731; -.
DR SwissPalm; Q92731; -.
DR BioMuta; ESR2; -.
DR DMDM; 6166154; -.
DR MassIVE; Q92731; -.
DR PaxDb; Q92731; -.
DR PeptideAtlas; Q92731; -.
DR PRIDE; Q92731; -.
DR ProteomicsDB; 33568; -.
DR ProteomicsDB; 75421; -. [Q92731-1]
DR ProteomicsDB; 75422; -. [Q92731-2]
DR ProteomicsDB; 75423; -. [Q92731-3]
DR ProteomicsDB; 75424; -. [Q92731-4]
DR ProteomicsDB; 75425; -. [Q92731-5]
DR ProteomicsDB; 75426; -. [Q92731-6]
DR ProteomicsDB; 75427; -. [Q92731-7]
DR ProteomicsDB; 75428; -. [Q92731-8]
DR Antibodypedia; 11874; 1767 antibodies from 45 providers.
DR DNASU; 2100; -.
DR Ensembl; ENST00000267525.10; ENSP00000267525.6; ENSG00000140009.19. [Q92731-7]
DR Ensembl; ENST00000341099.6; ENSP00000343925.4; ENSG00000140009.19. [Q92731-1]
DR Ensembl; ENST00000344288.10; ENSP00000345616.6; ENSG00000140009.19. [Q92731-3]
DR Ensembl; ENST00000353772.7; ENSP00000335551.4; ENSG00000140009.19. [Q92731-2]
DR Ensembl; ENST00000358599.9; ENSP00000351412.5; ENSG00000140009.19. [Q92731-2]
DR Ensembl; ENST00000553796.5; ENSP00000452426.1; ENSG00000140009.19. [Q92731-9]
DR Ensembl; ENST00000554572.5; ENSP00000450699.1; ENSG00000140009.19. [Q92731-2]
DR Ensembl; ENST00000555278.5; ENSP00000450488.1; ENSG00000140009.19. [Q92731-5]
DR Ensembl; ENST00000557772.5; ENSP00000451582.1; ENSG00000140009.19. [Q92731-6]
DR GeneID; 2100; -.
DR KEGG; hsa:2100; -.
DR MANE-Select; ENST00000341099.6; ENSP00000343925.4; NM_001437.3; NP_001428.1.
DR UCSC; uc001xgu.4; human. [Q92731-1]
DR CTD; 2100; -.
DR DisGeNET; 2100; -.
DR GeneCards; ESR2; -.
DR HGNC; HGNC:3468; ESR2.
DR HPA; ENSG00000140009; Tissue enhanced (adrenal).
DR MalaCards; ESR2; -.
DR MIM; 601663; gene.
DR MIM; 618187; phenotype.
DR neXtProt; NX_Q92731; -.
DR OpenTargets; ENSG00000140009; -.
DR Orphanet; 99361; Familial medullary thyroid carcinoma.
DR PharmGKB; PA27886; -.
DR VEuPathDB; HostDB:ENSG00000140009; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000156116; -.
DR HOGENOM; CLU_862048_0_0_1; -.
DR InParanoid; Q92731; -.
DR OMA; SHKEFSQ; -.
DR PhylomeDB; Q92731; -.
DR TreeFam; TF323751; -.
DR PathwayCommons; Q92731; -.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-8939211; ESR-mediated signaling.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR SignaLink; Q92731; -.
DR SIGNOR; Q92731; -.
DR BioGRID-ORCS; 2100; 15 hits in 1092 CRISPR screens.
DR ChiTaRS; ESR2; human.
DR EvolutionaryTrace; Q92731; -.
DR GeneWiki; Estrogen_receptor_beta; -.
DR GenomeRNAi; 2100; -.
DR Pharos; Q92731; Tclin.
DR PRO; PR:Q92731; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q92731; protein.
DR Bgee; ENSG00000140009; Expressed in right adrenal gland and 117 other tissues.
DR ExpressionAtlas; Q92731; baseline and differential.
DR Genevisible; Q92731; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0034056; F:estrogen response element binding; IDA:CAFA.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IDA:CAFA.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003707; F:nuclear steroid receptor activity; TAS:ProtInc.
DR GO; GO:0048019; F:receptor antagonist activity; NAS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:CAFA.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:CAFA.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:CAFA.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR DisProt; DP00079; -.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID00091; -.
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 3D-structure; Activator; Alternative splicing; Disease variant;
KW DNA-binding; Lipid-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Steroid-binding; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..530
FT /note="Estrogen receptor beta"
FT /id="PRO_0000053642"
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 507..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15862947"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15862947"
FT VAR_SEQ 319..409
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|Ref.13"
FT /id="VSP_003685"
FT VAR_SEQ 319..323
FT /note="FVELS -> MRGNA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9685228"
FT /id="VSP_003684"
FT VAR_SEQ 324..530
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9685228"
FT /id="VSP_003686"
FT VAR_SEQ 365..375
FT /note="DEGKCVEGILE -> YVPSGHSDPGC (in isoform 8)"
FT /evidence="ECO:0000303|Ref.13"
FT /id="VSP_003687"
FT VAR_SEQ 376..530
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|Ref.13"
FT /id="VSP_003688"
FT VAR_SEQ 469..530
FT /note="SNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKS
FT KEGSQNPQSQ -> RAEKASQTLTSFGMKMETLLPEATMEQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9636657, ECO:0000303|PubMed:9671811"
FT /id="VSP_003689"
FT VAR_SEQ 469..530
FT /note="SNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKS
FT KEGSQNPQSQ -> SSLSLSWRLFMLREASCHGVRQTPGGAHMSVSRSRSFEACQQPRE
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9636657"
FT /id="VSP_003690"
FT VAR_SEQ 469..530
FT /note="SNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKS
FT KEGSQNPQSQ -> RWGEKQFIHLKLS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16938840,
FT ECO:0000303|PubMed:9636657"
FT /id="VSP_003691"
FT VAR_SEQ 469..530
FT /note="SNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKS
FT KEGSQNPQSQ -> RYAP (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16938840,
FT ECO:0000303|PubMed:9636657"
FT /id="VSP_003692"
FT VAR_SEQ 469..474
FT /note="SNKGME -> RSCVYK (in isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_055746"
FT VAR_SEQ 475..530
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_055747"
FT VARIANT 84
FT /note="G -> V (found in a patient with a 46,XY disorder of
FT sex development; unknown pathological significance; no
FT change in positive regulation of DNA-binding transcription
FT factor activity; dbSNP:rs1460814363)"
FT /evidence="ECO:0000269|PubMed:29261182"
FT /id="VAR_081786"
FT VARIANT 181
FT /note="Missing (found in a patient with a 46,XY disorder of
FT sex development; unknown pathological significance; shows
FT increased positive regulation of DNA-binding transcription
FT factor activity; dbSNP:rs750091675)"
FT /evidence="ECO:0000269|PubMed:29261182"
FT /id="VAR_081787"
FT VARIANT 314
FT /note="K -> R (in ODG8; completely inactive in positive
FT regulation of DNA-binding transcription factor activity;
FT dbSNP:rs1567753148)"
FT /evidence="ECO:0000269|PubMed:30113650"
FT /id="VAR_081788"
FT VARIANT 426
FT /note="L -> R (found in a patient with a 46,XY disorder of
FT sex development; unknown pathological significance; shows a
FT higher positive regulation of DNA-binding transcription
FT factor activity; dbSNP:rs1217623435)"
FT /evidence="ECO:0000269|PubMed:29261182"
FT /id="VAR_081789"
FT MUTAGEN 87
FT /note="S->A: Enhances repression by activated ErbB2/ErbB3;
FT when associated with A-105."
FT /evidence="ECO:0000269|PubMed:15862947"
FT MUTAGEN 87
FT /note="S->D: Abolishes repression by activated ErbB2/ErbB3;
FT when associated with D-105."
FT /evidence="ECO:0000269|PubMed:15862947"
FT MUTAGEN 105
FT /note="S->A: Enhances repression by activated ErbB2/ErbB3;
FT when associated with A-87."
FT /evidence="ECO:0000269|PubMed:15862947"
FT MUTAGEN 105
FT /note="S->D: Abolishes repression by activated ErbB2/ErbB3;
FT when associated with D-87."
FT /evidence="ECO:0000269|PubMed:15862947"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:1L2J"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:2FSZ"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:3OLL"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:2FSZ"
FT HELIX 291..314
FT /evidence="ECO:0007829|PDB:3OLL"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:3OLL"
FT HELIX 324..347
FT /evidence="ECO:0007829|PDB:3OLL"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1L2J"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:3OLL"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:3OLL"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:3OLL"
FT HELIX 373..389
FT /evidence="ECO:0007829|PDB:3OLL"
FT HELIX 394..406
FT /evidence="ECO:0007829|PDB:3OLL"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:1NDE"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:1QKM"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:1L2J"
FT HELIX 421..442
FT /evidence="ECO:0007829|PDB:3OLL"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:1U3Q"
FT HELIX 448..481
FT /evidence="ECO:0007829|PDB:3OLL"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:5TOA"
FT HELIX 489..497
FT /evidence="ECO:0007829|PDB:3OLL"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:4ZI1"
SQ SEQUENCE 530 AA; 59216 MW; 8CAE34215992418A CRC64;
MDIKNSPSSL NSPSSYNCSQ SILPLEHGSI YIPSSYVDSH HEYPAMTFYS PAVMNYSIPS
NVTNLEGGPG RQTTSPNVLW PTPGHLSPLV VHRQLSHLYA EPQKSPWCEA RSLEHTLPVN
RETLKRKVSG NRCASPVTGP GSKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH
NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRLVR RQRSADEQLH
CAGKAKRSGG HAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFT EASMMMSLTK
LADKELVHMI SWAKKIPGFV ELSLFDQVRL LESCWMEVLM MGLMWRSIDH PGKLIFAPDL
VLDRDEGKCV EGILEIFDML LATTSRFREL KLQHKEYLCV KAMILLNSSM YPLVTATQDA
DSSRKLAHLL NAVTDALVWV IAKSGISSQQ QSMRLANLLM LLSHVRHASN KGMEHLLNMK
CKNVVPVYDL LLEMLNAHVL RGCKSSITGS ECSPAEDSKS KEGSQNPQSQ
