ERR2_HUMAN
ID ERR2_HUMAN Reviewed; 433 AA.
AC O95718; A2VDJ2; B6ZGU4; Q5F0P7; Q5F0P8; Q9HCB4;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Steroid hormone receptor ERR2 {ECO:0000305};
DE AltName: Full=ERR beta-2;
DE AltName: Full=Estrogen receptor-like 2;
DE AltName: Full=Estrogen-related receptor beta {ECO:0000303|PubMed:16332939};
DE Short=ERR-beta;
DE AltName: Full=Nuclear receptor subfamily 3 group B member 2;
GN Name=ESRRB {ECO:0000312|HGNC:HGNC:3473}; Synonyms=ERRB2, ESRL2, NR3B2;
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 2).
RC TISSUE=Testis;
RX PubMed=10072763; DOI=10.1016/s0378-1119(98)00619-2;
RA Chen F., Zhang Q., McDonald T., Davidoff M.J., Bailey W., Bai C., Liu Q.,
RA Caskey C.T.;
RT "Identification of two hERR2-related novel nuclear receptors utilizing
RT bioinformatics and inverse PCR.";
RL Gene 228:101-109(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND ALTERNATIVE SPLICING.
RC TISSUE=Heart, and Testis;
RX PubMed=16332939; DOI=10.1210/jc.2004-1957;
RA Zhou W., Liu Z., Wu J., Liu J.H., Hyder S.M., Antoniou E., Lubahn D.B.;
RT "Identification and characterization of two novel splicing isoforms of
RT human estrogen-related receptor beta.";
RL J. Clin. Endocrinol. Metab. 91:569-579(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Kobayashi T., Kodani Y., Sawasaki T., Endo Y.;
RT "Comprehensive DNA-binding analysis of human hormone nuclear receptors by
RT fluorescence correlation spectroscopy based on cell-free system.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Kaighin V.A., Martin A.L., Aronstam R.S.;
RT "Isolation of cDNA coding for multiple human nuclear receptor clones.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP FUNCTION (ISOFORM 3), AND INTERACTION WITH NFE2L2.
RX PubMed=17920186; DOI=10.1016/j.mce.2007.08.011;
RA Zhou W., Lo S.C., Liu J.H., Hannink M., Lubahn D.B.;
RT "ERRbeta: a potent inhibitor of Nrf2 transcriptional activity.";
RL Mol. Cell. Endocrinol. 278:52-62(2007).
RN [8]
RP FUNCTION, ALTERNATIVE SPLICING, AND INTERACTION WITH ESR1.
RX PubMed=19755138; DOI=10.1016/j.mce.2009.09.007;
RA Bombail V., Collins F., Brown P., Saunders P.T.;
RT "Modulation of ER alpha transcriptional activity by the orphan nuclear
RT receptor ERR beta and evidence for differential effects of long- and short-
RT form splice variants.";
RL Mol. Cell. Endocrinol. 314:53-61(2010).
RN [9]
RP FUNCTION.
RX PubMed=23836911; DOI=10.1074/jbc.m113.489674;
RA Cho Y., Hazen B.C., Russell A.P., Kralli A.;
RT "Peroxisome proliferator-activated receptor gamma coactivator 1 (PGC-
RT 1)- and estrogen-related receptor (ERR)-induced regulator in muscle 1
RT (Perm1) is a tissue-specific regulator of oxidative capacity in skeletal
RT muscle cells.";
RL J. Biol. Chem. 288:25207-25218(2013).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=18775884; DOI=10.1093/humrep/den298;
RA Bombail V., MacPherson S., Critchley H.O., Saunders P.T.;
RT "Estrogen receptor related beta is expressed in human endometrium
RT throughout the normal menstrual cycle.";
RL Hum. Reprod. 23:2782-2790(2008).
RN [11]
RP ACETYLATION BY PCAF/KAT2B.
RX PubMed=20484414; DOI=10.1210/me.2009-0441;
RA Wilson B.J., Tremblay A.M., Deblois G., Sylvain-Drolet G., Giguere V.;
RT "An acetylation switch modulates the transcriptional activity of estrogen-
RT related receptor alpha.";
RL Mol. Endocrinol. 24:1349-1358(2010).
RN [12]
RP STRUCTURE BY NMR OF 97-194, SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF
RP TYR-185.
RX PubMed=12654265; DOI=10.1016/s0022-2836(03)00183-9;
RA Gearhart M.D., Holmbeck S.M., Evans R.M., Dyson H.J., Wright P.E.;
RT "Monomeric complex of human orphan estrogen related receptor-2 with DNA: a
RT pseudo-dimer interface mediates extended half-site recognition.";
RL J. Mol. Biol. 327:819-832(2003).
RN [13]
RP VARIANTS DFNB35 VAL-110; PRO-320; LEU-342; PRO-347 AND MET-389, AND VARIANT
RP SER-386.
RX PubMed=18179891; DOI=10.1016/j.ajhg.2007.09.008;
RA Collin R.W.J., Kalay E., Tariq M., Peters T., van der Zwaag B.,
RA Venselaar H., Oostrik J., Lee K., Ahmed Z.M., Caylan R., Li Y.,
RA Spierenburg H.A., Eyupoglu E., Heister A., Riazuddin S., Bahat E.,
RA Ansar M., Arslan S., Wollnik B., Brunner H.G., Cremers C.W.R.J.,
RA Karaguzel A., Ahmad W., Cremers F.P.M., Vriend G., Friedman T.B.,
RA Riazuddin S., Leal S.M., Kremer H.;
RT "Mutations of ESRRB encoding estrogen-related receptor beta cause
RT autosomal-recessive nonsyndromic hearing impairment DFNB35.";
RL Am. J. Hum. Genet. 82:125-138(2008).
CC -!- FUNCTION: [Isoform 3]: Transcription factor that binds a canonical
CC ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter
CC and enhancer of targets genes regulating their expression or their
CC transcription activity (PubMed:17920186, PubMed:19755138). Plays a
CC role, in a LIF-independent manner, in maintainance of self-renewal and
CC pluripotency of embryonic and trophoblast stem cells through different
CC signaling pathways including FGF signaling pathway and Wnt signaling
CC pathways. Upon FGF signaling pathway activation, interacts with KDM1A
CC by directly binding to enhancer site of ELF5 and EOMES and activating
CC their transcription leading to self-renewal of trophoblast stem cells.
CC Also regulates expression of multiple rod-specific genes and is
CC required for survival of this cell type (By similarity). Plays a role
CC as transcription factor activator of GATA6, NR0B1, POU5F1 and PERM1
CC (PubMed:23836911). Plays a role as transcription factor repressor of
CC NFE2L2 transcriptional activity and ESR1 transcriptional activity
CC (PubMed:17920186, PubMed:19755138). During mitosis remains bound to a
CC subset of interphase target genes, including pluripotency regulators,
CC through the canonical ESRRB recognition (ERRE) sequence, leading to
CC their transcriptional activation in early G1 phase. Can coassemble on
CC structured DNA elements with other transcription factors like SOX2,
CC POU5F1, KDM1A and NCOA3 to trigger ESRRB-dependent gene activation.
CC This mechanism, in the case of SOX2 corecruitment prevents the
CC embryonic stem cells (ESCs) to epiblast stem cells (EpiSC) transition
CC through positive regulation of NR0B1 that inhibits the EpiSC
CC transcriptional program. Also plays a role inner ear development by
CC controlling expression of ion channels and transporters and in early
CC placentation (By similarity). {ECO:0000250|UniProtKB:Q61539,
CC ECO:0000269|PubMed:17920186, ECO:0000269|PubMed:19755138,
CC ECO:0000269|PubMed:23836911}.
CC -!- FUNCTION: [Isoform 1]: Transcription factor that binds a canonical
CC ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter
CC and enhancer of targets genes regulating their expression or their
CC transcription activity. Positively regulates ESR1 transcriptional
CC activity upon E2 stimulation. {ECO:0000269|PubMed:19755138}.
CC -!- SUBUNIT: Binds DNA as a monomer (PubMed:12654265). Interacts with
CC NR0B1; represses ESRRB activity at the GATA6 promoter. Interacts with
CC NANOG; reciprocally modulates their transcriptional activities and
CC activates POU5F1 expression. Interacts with NCOA3; mediates the
CC interaction between ESRRB and RNA polymerase II complexes and allows
CC NCOA3 corecruitment to ESRRB, KLF4, NANOG, and SOX2 enhancer regions to
CC trigger ESRRB-dependent gene activation involved in self-renewal and
CC pluripotency. Interacts with KDM1A; co-occupes the core set of ESRRB
CC targets including ELF5 and EOMES. Interacts with the multiprotein
CC complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4,
CC INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and
CC INTS12; ESRRB is probably not a core component of the integrator
CC complex and associates to integrator via its interaction with INTS1 and
CC INTS9; attracts the transcriptional machinery. Interacts with JARID2.
CC Interacts with POU5F1; recruits ESRRB near the POU5F1-SOX2 element in
CC the NANOG proximal promoter leading to activation of NANOG expression;
CC the interaction is DNA independent (By similarity). Interacts with
CC NFE2L2; represses NFE2L2 transcriptional activity (PubMed:17920186).
CC Isoform 1 interacts with ESR1 (PubMed:19755138).
CC {ECO:0000250|UniProtKB:Q61539, ECO:0000269|PubMed:12654265,
CC ECO:0000269|PubMed:17920186, ECO:0000269|PubMed:19755138}.
CC -!- INTERACTION:
CC O95718-2; P62508-3: ESRRG; NbExp=3; IntAct=EBI-13303537, EBI-12001340;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18775884}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q61539}. Chromosome
CC {ECO:0000250|UniProtKB:Q61539}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3; Synonyms=ERRbeta-short-form {ECO:0000303|PubMed:16332939};
CC IsoId=O95718-3; Sequence=Displayed;
CC Name=1; Synonyms=ERRbeta2-delta10 {ECO:0000303|PubMed:16332939};
CC IsoId=O95718-1; Sequence=VSP_058967;
CC Name=2; Synonyms=ERRbeta2 {ECO:0000303|PubMed:16332939};
CC IsoId=O95718-2; Sequence=VSP_058968;
CC -!- PTM: Acetylated by PCAF/KAT2 (in vitro). {ECO:0000269|PubMed:20484414}.
CC -!- DISEASE: Deafness, autosomal recessive, 35 (DFNB35) [MIM:608565]: A
CC form of non-syndromic deafness characterized by non-progressive,
CC prelingual hearing loss. {ECO:0000269|PubMed:18179891}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 1]: Primate-specific splicing isoform.
CC {ECO:0000303|PubMed:16332939}.
CC -!- MISCELLANEOUS: [Isoform 2]: Primate-specific splicing isoform.
CC {ECO:0000303|PubMed:16332939}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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DR EMBL; AF094517; AAC99409.1; -; mRNA.
DR EMBL; AY451389; AAS15571.1; -; mRNA.
DR EMBL; AY451390; AAS15572.1; -; mRNA.
DR EMBL; AB307714; BAH02305.1; -; mRNA.
DR EMBL; HQ692852; ADZ17363.1; -; mRNA.
DR EMBL; AC008050; AAG17472.1; -; Genomic_DNA.
DR EMBL; AC016543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC131517; AAI31518.1; -; mRNA.
DR CCDS; CCDS9850.2; -. [O95718-1]
DR RefSeq; NP_004443.3; NM_004452.3. [O95718-1]
DR RefSeq; XP_016876575.1; XM_017021086.1.
DR PDB; 1LO1; NMR; -; A=97-192.
DR PDB; 6LIT; X-ray; 2.00 A; A/B=204-433.
DR PDB; 6LN4; X-ray; 2.61 A; A=204-432.
DR PDBsum; 1LO1; -.
DR PDBsum; 6LIT; -.
DR PDBsum; 6LN4; -.
DR AlphaFoldDB; O95718; -.
DR BMRB; O95718; -.
DR SMR; O95718; -.
DR BioGRID; 108406; 104.
DR IntAct; O95718; 3.
DR STRING; 9606.ENSP00000422488; -.
DR BindingDB; O95718; -.
DR ChEMBL; CHEMBL3751; -.
DR DrugBank; DB00255; Diethylstilbestrol.
DR DrugBank; DB07776; Flavone.
DR DrugBank; DB01645; Genistein.
DR DrugCentral; O95718; -.
DR GuidetoPHARMACOLOGY; 623; -.
DR iPTMnet; O95718; -.
DR PhosphoSitePlus; O95718; -.
DR BioMuta; ESRRB; -.
DR MassIVE; O95718; -.
DR MaxQB; O95718; -.
DR PaxDb; O95718; -.
DR PeptideAtlas; O95718; -.
DR PRIDE; O95718; -.
DR ProteomicsDB; 51011; -. [O95718-1]
DR ProteomicsDB; 51012; -. [O95718-2]
DR ProteomicsDB; 51013; -. [O95718-3]
DR Antibodypedia; 13059; 325 antibodies from 35 providers.
DR DNASU; 2103; -.
DR Ensembl; ENST00000380887.7; ENSP00000370270.2; ENSG00000119715.15. [O95718-1]
DR Ensembl; ENST00000505752.6; ENSP00000423004.1; ENSG00000119715.15. [O95718-2]
DR Ensembl; ENST00000509242.5; ENSP00000422488.1; ENSG00000119715.15. [O95718-1]
DR GeneID; 2103; -.
DR KEGG; hsa:2103; -.
DR UCSC; uc001xsq.2; human. [O95718-3]
DR CTD; 2103; -.
DR DisGeNET; 2103; -.
DR GeneCards; ESRRB; -.
DR GeneReviews; ESRRB; -.
DR HGNC; HGNC:3473; ESRRB.
DR HPA; ENSG00000119715; Tissue enriched (retina).
DR MalaCards; ESRRB; -.
DR MIM; 602167; gene.
DR MIM; 608565; phenotype.
DR neXtProt; NX_O95718; -.
DR OpenTargets; ENSG00000119715; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA27889; -.
DR VEuPathDB; HostDB:ENSG00000119715; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000153433; -.
DR HOGENOM; CLU_007368_11_0_1; -.
DR InParanoid; O95718; -.
DR OrthoDB; 669799at2759; -.
DR TreeFam; TF323751; -.
DR PathwayCommons; O95718; -.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR SignaLink; O95718; -.
DR SIGNOR; O95718; -.
DR BioGRID-ORCS; 2103; 13 hits in 1100 CRISPR screens.
DR ChiTaRS; ESRRB; human.
DR EvolutionaryTrace; O95718; -.
DR GeneWiki; Estrogen-related_receptor_beta; -.
DR GenomeRNAi; 2103; -.
DR Pharos; O95718; Tchem.
DR PRO; PR:O95718; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O95718; protein.
DR Bgee; ENSG00000119715; Expressed in metanephros cortex and 88 other tissues.
DR ExpressionAtlas; O95718; baseline and differential.
DR Genevisible; O95718; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0005496; F:steroid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043697; P:cell dedifferentiation; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB.
DR GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0090282; P:positive regulation of transcription involved in G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:2000035; P:regulation of stem cell division; ISS: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; IDA:UniProtKB.
DR GO; GO:0017145; P:stem cell division; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; IDA:UniProtKB.
DR DisProt; DP01764; -.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID00011; -.
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; IPR027289; Oest-rel_rcp.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PIRSF; PIRSF002527; ER-like_NR; 1.
DR PIRSF; PIRSF500939; ERR1-2-3; 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; Acetylation; Alternative splicing; Chromosome; Cytoplasm;
KW Deafness; Disease variant; DNA-binding; Metal-binding;
KW Non-syndromic deafness; Nucleus; Receptor; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..433
FT /note="Steroid hormone receptor ERR2"
FT /id="PRO_0000053662"
FT DOMAIN 208..432
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 100..186
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 103..123
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 139..163
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..211
FT /note="Interaction with NANOG"
FT /evidence="ECO:0000250|UniProtKB:Q61539"
FT REGION 203..433
FT /note="Essential for ESRRB transcriptional activity and
FT interaction with NCOA3"
FT /evidence="ECO:0000250|UniProtKB:Q61539"
FT SITE 185
FT /note="Important for stabilizing DNA-binding"
FT VAR_SEQ 433
FT /note="V -> VGQEQLRGSPKDERMSSHDGKCPFQSAAFTSRDQSNSPGIPNPRPSS
FT PTPLNERGRQISPSTRTPGGQGKHLWLTM (in isoform 1)"
FT /id="VSP_058967"
FT VAR_SEQ 433
FT /note="V -> AWARADSLQEWRPLEQVPSPLHRATKRQHVHFLTPLPPPPSVAWVGT
FT AQAGYHLEVFLPQRAGWPRAA (in isoform 2)"
FT /id="VSP_058968"
FT VARIANT 110
FT /note="A -> V (in DFNB35; dbSNP:rs121909110)"
FT /evidence="ECO:0000269|PubMed:18179891"
FT /id="VAR_043503"
FT VARIANT 320
FT /note="L -> P (in DFNB35)"
FT /evidence="ECO:0000269|PubMed:18179891"
FT /id="VAR_043504"
FT VARIANT 342
FT /note="V -> L (in DFNB35; dbSNP:rs121909111)"
FT /evidence="ECO:0000269|PubMed:18179891"
FT /id="VAR_043505"
FT VARIANT 347
FT /note="L -> P (in DFNB35)"
FT /evidence="ECO:0000269|PubMed:18179891"
FT /id="VAR_043506"
FT VARIANT 386
FT /note="P -> S (in dbSNP:rs61742642)"
FT /evidence="ECO:0000269|PubMed:18179891"
FT /id="VAR_043507"
FT VARIANT 389
FT /note="T -> M (in DFNB35; uncertain pathological
FT significance; dbSNP:rs201714970)"
FT /evidence="ECO:0000269|PubMed:18179891"
FT /id="VAR_043508"
FT MUTAGEN 185
FT /note="Y->A: 6-fold decrease in DNA-binding affinity."
FT /evidence="ECO:0000269|PubMed:12654265"
FT CONFLICT 248
FT /note="D -> E (in Ref. 3; BAH02305)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="L -> V (in Ref. 6; AAI31518)"
FT /evidence="ECO:0000305"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:1LO1"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:1LO1"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:1LO1"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:1LO1"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:1LO1"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1LO1"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:6LN4"
FT HELIX 236..258
FT /evidence="ECO:0007829|PDB:6LIT"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6LIT"
FT HELIX 269..292
FT /evidence="ECO:0007829|PDB:6LIT"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6LIT"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:6LIT"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:6LIT"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:6LIT"
FT HELIX 318..334
FT /evidence="ECO:0007829|PDB:6LIT"
FT HELIX 338..350
FT /evidence="ECO:0007829|PDB:6LIT"
FT HELIX 360..381
FT /evidence="ECO:0007829|PDB:6LIT"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:6LN4"
FT HELIX 388..393
FT /evidence="ECO:0007829|PDB:6LIT"
FT HELIX 396..416
FT /evidence="ECO:0007829|PDB:6LIT"
FT HELIX 423..430
FT /evidence="ECO:0007829|PDB:6LIT"
SQ SEQUENCE 433 AA; 48054 MW; ED1D3F87E2798DD1 CRC64;
MSSDDRHLGS SCGSFIKTEP SSPSSGIDAL SHHSPSGSSD ASGGFGLALG THANGLDSPP
MFAGAGLGGT PCRKSYEDCA SGIMEDSAIK CEYMLNAIPK RLCLVCGDIA SGYHYGVASC
EACKAFFKRT IQGNIEYSCP ATNECEITKR RRKSCQACRF MKCLKVGMLK EGVRLDRVRG
GRQKYKRRLD SESSPYLSLQ ISPPAKKPLT KIVSYLLVAE PDKLYAMPPP GMPEGDIKAL
TTLCDLADRE LVVIIGWAKH IPGFSSLSLG DQMSLLQSAW MEILILGIVY RSLPYDDKLV
YAEDYIMDEE HSRLAGLLEL YRAILQLVRR YKKLKVEKEE FVTLKALALA NSDSMYIEDL
EAVQKLQDLL HEALQDYELS QRHEEPWRTG KLLLTLPLLR QTAAKAVQHF YSVKLQGKVP
MHKLFLEMLE AKV
