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 27-MAR-2024, entry version 247. 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). Interacts with STUB1/CHIP CC (By similarity). {ECO:0000250|UniProtKB:O08537, CC ECO:0000250|UniProtKB:Q62986, ECO:0000269|PubMed:10681503, CC ECO:0000269|PubMed:11113208, ECO:0000269|PubMed:11579095, CC ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:15047147, CC ECO:0000269|PubMed:15199063, ECO:0000269|PubMed:19126643, CC ECO:0000269|PubMed:20074560, 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="https://atlasgeneticsoncology.org/gene/40500/ESR2"; 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. DR RefSeq; XP_016876569.1; XM_017021080.1. DR RefSeq; XP_016876570.1; XM_017021081.1. DR RefSeq; XP_016876571.1; XM_017021082.1. DR RefSeq; XP_016876572.1; XM_017021083.1. DR RefSeq; XP_016876573.1; XM_017021084.1. 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 PDB; 7XVY; X-ray; 1.54 A; A/B=261-500. DR PDB; 7XVZ; X-ray; 2.08 A; A/B=261-500. DR PDB; 7XWP; X-ray; 1.92 A; A/B=261-500. DR PDB; 7XWQ; X-ray; 1.89 A; A/B=261-500. DR PDB; 7XWR; X-ray; 2.16 A; A/B=261-500. 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 PDBsum; 7XVY; -. DR PDBsum; 7XVZ; -. DR PDBsum; 7XWP; -. DR PDBsum; 7XWQ; -. DR PDBsum; 7XWR; -. DR AlphaFoldDB; Q92731; -. DR SMR; Q92731; -. DR BioGRID; 108404; 2291. 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; DB13310; Ormeloxifene. 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; 9606-ENSP00000343925; -. DR PeptideAtlas; 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; 1947 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 AGR; HGNC:3468; -. DR CTD; 2100; -. DR DisGeNET; 2100; -. DR GeneCards; ESR2; -. DR HGNC; HGNC:3468; ESR2. DR HPA; ENSG00000140009; Tissue enhanced (adrenal gland, testis). 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; HRNSEDQ; -. DR OrthoDB; 5387678at2759; -. 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; 16 hits in 1181 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 118 other cell types or tissues. DR ExpressionAtlas; Q92731; baseline and differential. 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:0071391; P:cellular response to estrogen stimulus; IBA:GO_Central. DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:CAFA. 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:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:CAFA. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd07171; NR_DBD_ER; 1. DR CDD; cd06949; NR_LBD_ER; 1. DR DisProt; DP00079; -. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1. DR Gene3D; 1.10.565.10; Retinoid X Receptor; 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 PANTHER; PTHR48092:SF12; ESTROGEN RECEPTOR BETA; 1. DR PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1. 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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1. DR PROSITE; PS51843; NR_LBD; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. DR Genevisible; Q92731; HS. 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; uncertain significance; no change in FT positive regulation of DNA-binding transcription factor FT 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; uncertain significance; shows increased FT positive regulation of DNA-binding transcription factor FT 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; uncertain significance; shows a higher FT positive regulation of DNA-binding transcription factor FT 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:7XVY" 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:7XVZ" 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 //