ERR3_HUMAN
ID ERR3_HUMAN Reviewed; 458 AA.
AC P62508; A8K4I0; A8K6I2; B3KY84; E9PGB7; F8W8J3; O75454; O96021; Q68DA0;
AC Q6P274; Q6PK28; Q6TS38; Q9R1F3; Q9UNJ4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Estrogen-related receptor gamma;
DE AltName: Full=ERR gamma-2;
DE AltName: Full=Estrogen receptor-related protein 3;
DE AltName: Full=Nuclear receptor subfamily 3 group B member 3;
GN Name=ESRRG; Synonyms=ERR3, ERRG2, KIAA0832, NR3B3;
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).
RC TISSUE=Brain;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=9676434; DOI=10.1006/geno.1998.5345;
RA Eudy J.D., Yao S.F., Weston M.D., Ma-Edmonds M., Talmadge C.B., Cheng J.J.,
RA Kimberling W.J., Sumegi J.;
RT "Isolation of a gene encoding a novel member of the nuclear receptor
RT superfamily from the critical region of Usher syndrome type IIa at 1q41.";
RL Genomics 50:382-384(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, Retina, and Skeletal muscle;
RX PubMed=10707956; DOI=10.1210/mend.14.3.0431;
RA Heard D.J., Norby P.L., Holloway J., Vissing H.;
RT "Human ERRgamma, a third member of the estrogen receptor-related receptor
RT (ERR) subfamily of orphan nuclear receptors: tissue-specific isoforms are
RT expressed during development and in the adult.";
RL Mol. Endocrinol. 14:382-392(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Brain, and Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-50.
RG NIEHS SNPs program;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Eye, and Placenta;
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 [MRNA] OF 1-129 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10428842; DOI=10.1074/jbc.274.32.22618;
RA Hong H., Yang L., Stallcup M.R.;
RT "Hormone-independent transcriptional activation and coactivator binding by
RT novel orphan nuclear receptor ERR3.";
RL J. Biol. Chem. 274:22618-22626(1999).
RN [12]
RP INTERACTION WITH TLE1 AND PNRC2, AND TISSUE SPECIFICITY.
RX PubMed=14651967; DOI=10.1016/j.bbrc.2003.11.025;
RA Hentschke M., Borgmeyer U.;
RT "Identification of PNRC2 and TLE1 as activation function-1 cofactors of the
RT orphan nuclear receptor ERRgamma.";
RL Biochem. Biophys. Res. Commun. 312:975-982(2003).
RN [13]
RP SUMOYLATION AT LYS-40, AND MUTAGENESIS OF LYS-40.
RX PubMed=16371476; DOI=10.1073/pnas.0503698102;
RA Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J.,
RA Nakai A., Sistonen L.;
RT "PDSM, a motif for phosphorylation-dependent SUMO modification.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006).
RN [14]
RP SUMOYLATION AT LYS-40, PHOSPHORYLATION AT SER-45, FUNCTION, AND MUTAGENESIS
RP OF PHE-38; ILE-39; LYS-40; THR-41; GLU-42; SER-44 AND SER-45.
RX PubMed=19067653; DOI=10.1042/bj20081556;
RA Hentschke M., Suesens U., Borgmeyer U.;
RT "Transcriptional ERRgamma2-mediated activation is regulated by sentrin-
RT specific proteases.";
RL Biochem. J. 419:167-176(2009).
RN [15]
RP SUMOYLATION AT LYS-40, PHOSPHORYLATION AT SER-45, FUNCTION, AND MUTAGENESIS
RP OF LYS-40 AND SER-45.
RX PubMed=18063693; DOI=10.1210/me.2007-0357;
RA Tremblay A.M., Wilson B.J., Yang X.-J., Giguere V.;
RT "Phosphorylation-dependent sumoylation regulates estrogen-related receptor-
RT alpha and -gamma transcriptional activity through a synergy control
RT motif.";
RL Mol. Endocrinol. 22:570-584(2008).
RN [16]
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 [17]
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 [18]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 229-458 IN COMPLEXES WITH INVERSE
RP AGONISTS AND NCOA1, FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11864604; DOI=10.1016/s1097-2765(02)00444-6;
RA Greschik H., Wurtz J.-M., Sanglier S., Bourguet W., van Dorsselaer A.,
RA Moras D., Renaud J.-P.;
RT "Structural and functional evidence for ligand-independent transcriptional
RT activation by the estrogen-related receptor 3.";
RL Mol. Cell 9:303-313(2002).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 233-458 IN COMPLEX WITH INVERSE
RP AGONIST.
RX PubMed=16307879; DOI=10.1016/j.bmcl.2005.11.030;
RA Chao E.Y.H., Collins J.L., Gaillard S., Miller A.B., Wang L.,
RA Orband-Miller L.A., Nolte R.T., McDonnell D.P., Willson T.M.,
RA Zuercher W.J.;
RT "Structure-guided synthesis of tamoxifen analogs with improved selectivity
RT for the orphan ERRgamma.";
RL Bioorg. Med. Chem. Lett. 16:821-824(2006).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 229-458 IN COMPLEXES WITH AGONIST
RP AND INVERSE AGONIST; NRIP1 AND NCOR2, AND SUBUNIT.
RX PubMed=16990259; DOI=10.1074/jbc.m608410200;
RA Wang L., Zuercher W.J., Consler T.G., Lambert M.H., Miller A.B.,
RA Orband-Miller L.A., McKee D.D., Willson T.M., Nolte R.T.;
RT "X-ray crystal structures of the estrogen-related receptor-gamma ligand
RT binding domain in three functional states reveal the molecular basis of
RT small molecule regulation.";
RL J. Biol. Chem. 281:37773-37781(2006).
CC -!- FUNCTION: Orphan receptor that acts as transcription activator in the
CC absence of bound ligand. Binds specifically to an estrogen response
CC element and activates reporter genes controlled by estrogen response
CC elements (By similarity). Induces the expression of PERM1 in the
CC skeletal muscle. {ECO:0000250, ECO:0000269|PubMed:11864604,
CC ECO:0000269|PubMed:18063693, ECO:0000269|PubMed:19067653,
CC ECO:0000269|PubMed:23836911}.
CC -!- SUBUNIT: Homodimer. Binds TLE1, PNRC1 and PNRC2. Binds GRIP1 (By
CC similarity). Interacts with NRIP1, NCOA1 and NCOR2. {ECO:0000250,
CC ECO:0000269|PubMed:14651967, ECO:0000269|PubMed:16307879,
CC ECO:0000269|PubMed:16990259}.
CC -!- INTERACTION:
CC P62508; Q05D60: DEUP1; NbExp=3; IntAct=EBI-2834260, EBI-748597;
CC P62508; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-2834260, EBI-2125614;
CC P62508; P50222: MEOX2; NbExp=3; IntAct=EBI-2834260, EBI-748397;
CC P62508; P51843: NR0B1; NbExp=3; IntAct=EBI-2834260, EBI-946109;
CC P62508; Q12769: NUP160; NbExp=3; IntAct=EBI-2834260, EBI-295715;
CC P62508; Q9UBK2: PPARGC1A; NbExp=4; IntAct=EBI-2834260, EBI-765486;
CC P62508; A0MZ66: SHTN1; NbExp=3; IntAct=EBI-2834260, EBI-308778;
CC P62508; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-2834260, EBI-10175576;
CC P62508-3; Q8NFM4: ADCY4; NbExp=6; IntAct=EBI-12001340, EBI-2838710;
CC P62508-3; Q13315: ATM; NbExp=3; IntAct=EBI-12001340, EBI-495465;
CC P62508-3; Q86WA6-2: BPHL; NbExp=3; IntAct=EBI-12001340, EBI-21843491;
CC P62508-3; Q9BZE7: C22orf23; NbExp=3; IntAct=EBI-12001340, EBI-10303102;
CC P62508-3; Q13555-5: CAMK2G; NbExp=3; IntAct=EBI-12001340, EBI-12020154;
CC P62508-3; Q05D60: DEUP1; NbExp=3; IntAct=EBI-12001340, EBI-748597;
CC P62508-3; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-12001340, EBI-2349927;
CC P62508-3; P11474: ESRRA; NbExp=3; IntAct=EBI-12001340, EBI-372412;
CC P62508-3; O95718-2: ESRRB; NbExp=3; IntAct=EBI-12001340, EBI-13303537;
CC P62508-3; P62508-3: ESRRG; NbExp=3; IntAct=EBI-12001340, EBI-12001340;
CC P62508-3; Q15024: EXOSC7; NbExp=3; IntAct=EBI-12001340, EBI-371841;
CC P62508-3; O95990-4: FAM107A; NbExp=3; IntAct=EBI-12001340, EBI-11977223;
CC P62508-3; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-12001340, EBI-8468186;
CC P62508-3; Q14296: FASTK; NbExp=3; IntAct=EBI-12001340, EBI-1754067;
CC P62508-3; P23508: MCC; NbExp=3; IntAct=EBI-12001340, EBI-307531;
CC P62508-3; Q6IN84: MRM1; NbExp=5; IntAct=EBI-12001340, EBI-5454865;
CC P62508-3; P51843: NR0B1; NbExp=6; IntAct=EBI-12001340, EBI-946109;
CC P62508-3; Q15466: NR0B2; NbExp=3; IntAct=EBI-12001340, EBI-3910729;
CC P62508-3; P48552: NRIP1; NbExp=3; IntAct=EBI-12001340, EBI-746484;
CC P62508-3; P26367: PAX6; NbExp=3; IntAct=EBI-12001340, EBI-747278;
CC P62508-3; Q9NPJ4: PNRC2; NbExp=3; IntAct=EBI-12001340, EBI-726549;
CC P62508-3; P01189: POMC; NbExp=3; IntAct=EBI-12001340, EBI-12219503;
CC P62508-3; Q9UBK2: PPARGC1A; NbExp=5; IntAct=EBI-12001340, EBI-765486;
CC P62508-3; P62195: PSMC5; NbExp=3; IntAct=EBI-12001340, EBI-357745;
CC P62508-3; Q8N0T1-2: RBIS; NbExp=3; IntAct=EBI-12001340, EBI-13380894;
CC P62508-3; Q04864-2: REL; NbExp=3; IntAct=EBI-12001340, EBI-10829018;
CC P62508-3; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-12001340, EBI-726876;
CC P62508-3; A0MZ66-4: SHTN1; NbExp=3; IntAct=EBI-12001340, EBI-12097232;
CC P62508-3; Q8TAD8: SNIP1; NbExp=3; IntAct=EBI-12001340, EBI-749336;
CC P62508-3; P19237: TNNI1; NbExp=3; IntAct=EBI-12001340, EBI-746692;
CC P62508-3; P48788: TNNI2; NbExp=3; IntAct=EBI-12001340, EBI-7746394;
CC P62508-3; Q96PN7: TRERF1; NbExp=3; IntAct=EBI-12001340, EBI-3505166;
CC P62508-3; Q96S82: UBL7; NbExp=3; IntAct=EBI-12001340, EBI-348604;
CC P62508-3; Q5SQQ9-2: VAX1; NbExp=3; IntAct=EBI-12001340, EBI-12227803;
CC P62508-3; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-12001340, EBI-11962468;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Long;
CC IsoId=P62508-1, O75454-1;
CC Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P62508-2, O75454-2;
CC Sequence=VSP_003702;
CC Name=3;
CC IsoId=P62508-3; Sequence=VSP_003702, VSP_013301;
CC Name=4;
CC IsoId=P62508-4; Sequence=VSP_003702, VSP_045980;
CC Name=5;
CC IsoId=P62508-5; Sequence=VSP_047156, VSP_013301;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, kidney, brain, lung, bone
CC marrow, adrenal gland, trachea, spinal cord and thyroid gland.
CC {ECO:0000269|PubMed:14651967, ECO:0000269|PubMed:9676434}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in fetal brain and also
CC in the fetal kidney, lung and liver. {ECO:0000269|PubMed:9676434}.
CC -!- PTM: Acetylated by PCAF/KAT2 (in vitro). {ECO:0000269|PubMed:20484414}.
CC -!- PTM: Sumoylation on Lys-40 is enhanced by phosphorylation at Ser-45 and
CC represses transcriptional activity. {ECO:0000269|PubMed:16371476,
CC ECO:0000269|PubMed:18063693, ECO:0000269|PubMed:19067653}.
CC -!- PTM: Phosphorylation on Ser-45 enhances sumoylation on Lys-40 thus
CC repressing transcriptional activity. {ECO:0000269|PubMed:16371476,
CC ECO:0000269|PubMed:18063693, ECO:0000269|PubMed:19067653}.
CC -!- MISCELLANEOUS: No physiological activating ligand is known for this
CC orphan receptor, but 4-hydroxytamoxifen and diethylstilbestrol act as
CC inverse agonists and deactivate ESRRG.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08218.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA74855.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/esrrg/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ESRRGID45840ch1q41.html";
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DR EMBL; AF094518; AAC99410.1; -; mRNA.
DR EMBL; AB020639; BAA74855.2; ALT_INIT; mRNA.
DR EMBL; AF058291; AAC39899.1; -; mRNA.
DR EMBL; AY388456; AAQ93376.1; -; mRNA.
DR EMBL; AY388457; AAQ93377.1; -; mRNA.
DR EMBL; AY388458; AAQ93378.1; -; mRNA.
DR EMBL; AY388459; AAQ93379.1; -; mRNA.
DR EMBL; AY388460; AAQ93380.1; -; mRNA.
DR EMBL; AY388461; AAQ93381.1; -; mRNA.
DR EMBL; AK131193; BAG54746.1; -; mRNA.
DR EMBL; AK290945; BAF83634.1; -; mRNA.
DR EMBL; AK291028; BAF83717.1; -; mRNA.
DR EMBL; AK291647; BAF84336.1; -; mRNA.
DR EMBL; CR749497; CAH18320.1; -; mRNA.
DR EMBL; AY528719; AAS00098.1; -; Genomic_DNA.
DR EMBL; AC096635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL603752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93335.1; -; Genomic_DNA.
DR EMBL; BC008218; AAH08218.1; ALT_SEQ; mRNA.
DR EMBL; BC064700; AAH64700.1; -; mRNA.
DR EMBL; AF117255; AAD48370.1; -; mRNA.
DR CCDS; CCDS1517.1; -. [P62508-2]
DR CCDS; CCDS41468.1; -.
DR CCDS; CCDS58060.1; -. [P62508-4]
DR CCDS; CCDS58061.1; -. [P62508-5]
DR RefSeq; NP_001127757.1; NM_001134285.2. [P62508-2]
DR RefSeq; NP_001230434.1; NM_001243505.1.
DR RefSeq; NP_001230435.1; NM_001243506.1.
DR RefSeq; NP_001230436.1; NM_001243507.1. [P62508-4]
DR RefSeq; NP_001230438.1; NM_001243509.1. [P62508-2]
DR RefSeq; NP_001230439.1; NM_001243510.2. [P62508-2]
DR RefSeq; NP_001230440.1; NM_001243511.2. [P62508-2]
DR RefSeq; NP_001230441.1; NM_001243512.1. [P62508-2]
DR RefSeq; NP_001230442.1; NM_001243513.1. [P62508-2]
DR RefSeq; NP_001230443.1; NM_001243514.1. [P62508-2]
DR RefSeq; NP_001230444.1; NM_001243515.1. [P62508-2]
DR RefSeq; NP_001230447.1; NM_001243518.1. [P62508-5]
DR RefSeq; NP_001230448.1; NM_001243519.1. [P62508-2]
DR RefSeq; NP_001429.2; NM_001438.3. [P62508-1]
DR RefSeq; NP_996317.1; NM_206594.2. [P62508-2]
DR RefSeq; NP_996318.1; NM_206595.2. [P62508-2]
DR RefSeq; XP_011507569.1; XM_011509267.1. [P62508-5]
DR RefSeq; XP_011507570.1; XM_011509268.2. [P62508-5]
DR RefSeq; XP_011507571.1; XM_011509269.2. [P62508-5]
DR RefSeq; XP_011507576.1; XM_011509274.1. [P62508-3]
DR RefSeq; XP_011507577.1; XM_011509275.1. [P62508-3]
DR RefSeq; XP_011507578.1; XM_011509276.1. [P62508-3]
DR RefSeq; XP_011507579.1; XM_011509277.1. [P62508-3]
DR RefSeq; XP_011507580.1; XM_011509278.1. [P62508-3]
DR RefSeq; XP_011507581.1; XM_011509279.1. [P62508-3]
DR RefSeq; XP_011507582.1; XM_011509280.2. [P62508-3]
DR RefSeq; XP_016856120.1; XM_017000631.1. [P62508-3]
DR RefSeq; XP_016856121.1; XM_017000632.1. [P62508-3]
DR RefSeq; XP_016856122.1; XM_017000633.1. [P62508-3]
DR RefSeq; XP_016856123.1; XM_017000634.1. [P62508-3]
DR RefSeq; XP_016856124.1; XM_017000635.1. [P62508-3]
DR RefSeq; XP_016856125.1; XM_017000636.1. [P62508-3]
DR RefSeq; XP_016856126.1; XM_017000637.1. [P62508-3]
DR RefSeq; XP_016856127.1; XM_017000638.1. [P62508-2]
DR RefSeq; XP_016856128.1; XM_017000639.1. [P62508-2]
DR RefSeq; XP_016856129.1; XM_017000640.1.
DR RefSeq; XP_016856130.1; XM_017000641.1. [P62508-2]
DR RefSeq; XP_016856131.1; XM_017000642.1.
DR RefSeq; XP_016856132.1; XM_017000643.1.
DR RefSeq; XP_016856133.1; XM_017000644.1. [P62508-2]
DR RefSeq; XP_016856134.1; XM_017000645.1. [P62508-2]
DR RefSeq; XP_016856135.1; XM_017000646.1.
DR RefSeq; XP_016856136.1; XM_017000647.1.
DR RefSeq; XP_016856137.1; XM_017000648.1.
DR RefSeq; XP_016856138.1; XM_017000649.1.
DR PDB; 1KV6; X-ray; 2.70 A; A/B=229-458.
DR PDB; 1TFC; X-ray; 2.40 A; A/B=229-458.
DR PDB; 1VJB; X-ray; 3.20 A; A/B=229-458.
DR PDB; 2E2R; X-ray; 1.60 A; A=222-458.
DR PDB; 2EWP; X-ray; 2.30 A; A/B/C/D/E=233-458.
DR PDB; 2GP7; X-ray; 2.45 A; A/B/C/D=229-458.
DR PDB; 2GPO; X-ray; 1.95 A; A=229-458.
DR PDB; 2GPP; X-ray; 2.60 A; A/B=229-458.
DR PDB; 2GPU; X-ray; 1.70 A; A=229-458.
DR PDB; 2GPV; X-ray; 2.85 A; A/B/C/D/E/F=229-458.
DR PDB; 2P7A; X-ray; 2.30 A; A=229-458.
DR PDB; 2P7G; X-ray; 2.10 A; A=229-458.
DR PDB; 2P7Z; X-ray; 2.50 A; A=229-458.
DR PDB; 2ZAS; X-ray; 2.00 A; A=222-458.
DR PDB; 2ZBS; X-ray; 1.80 A; A=222-458.
DR PDB; 2ZKC; X-ray; 1.70 A; A=222-458.
DR PDB; 5YSO; X-ray; 2.50 A; A/B/C=221-458.
DR PDB; 6A6K; X-ray; 2.90 A; A/B/C=221-458.
DR PDB; 6I61; X-ray; 1.65 A; A=222-458.
DR PDB; 6I62; X-ray; 1.65 A; A=222-458.
DR PDB; 6I63; X-ray; 2.23 A; A=222-458.
DR PDB; 6I64; X-ray; 1.91 A; A=222-458.
DR PDB; 6I65; X-ray; 1.50 A; A=222-458.
DR PDB; 6I66; X-ray; 1.60 A; A=222-458.
DR PDB; 6I67; X-ray; 1.75 A; A=222-458.
DR PDB; 6K3N; X-ray; 1.97 A; A=232-458.
DR PDB; 6KNR; X-ray; 2.80 A; A/B=222-458.
DR PDB; 6XXC; X-ray; 1.30 A; B=174-182.
DR PDB; 6XY5; X-ray; 1.30 A; B=174-182.
DR PDB; 6Y18; X-ray; 1.30 A; B=174-182.
DR PDB; 6Y1D; X-ray; 1.38 A; B=174-182.
DR PDB; 6Y3W; X-ray; 1.34 A; B=174-182.
DR PDB; 6Y58; X-ray; 1.90 A; P=314-321.
DR PDBsum; 1KV6; -.
DR PDBsum; 1TFC; -.
DR PDBsum; 1VJB; -.
DR PDBsum; 2E2R; -.
DR PDBsum; 2EWP; -.
DR PDBsum; 2GP7; -.
DR PDBsum; 2GPO; -.
DR PDBsum; 2GPP; -.
DR PDBsum; 2GPU; -.
DR PDBsum; 2GPV; -.
DR PDBsum; 2P7A; -.
DR PDBsum; 2P7G; -.
DR PDBsum; 2P7Z; -.
DR PDBsum; 2ZAS; -.
DR PDBsum; 2ZBS; -.
DR PDBsum; 2ZKC; -.
DR PDBsum; 5YSO; -.
DR PDBsum; 6A6K; -.
DR PDBsum; 6I61; -.
DR PDBsum; 6I62; -.
DR PDBsum; 6I63; -.
DR PDBsum; 6I64; -.
DR PDBsum; 6I65; -.
DR PDBsum; 6I66; -.
DR PDBsum; 6I67; -.
DR PDBsum; 6K3N; -.
DR PDBsum; 6KNR; -.
DR PDBsum; 6XXC; -.
DR PDBsum; 6XY5; -.
DR PDBsum; 6Y18; -.
DR PDBsum; 6Y1D; -.
DR PDBsum; 6Y3W; -.
DR PDBsum; 6Y58; -.
DR AlphaFoldDB; P62508; -.
DR SASBDB; P62508; -.
DR SMR; P62508; -.
DR BioGRID; 108407; 67.
DR IntAct; P62508; 52.
DR MINT; P62508; -.
DR STRING; 9606.ENSP00000355904; -.
DR BindingDB; P62508; -.
DR ChEMBL; CHEMBL4245; -.
DR DrugBank; DB06884; 4-HYDROXY-N'-(4-ISOPROPYLBENZYL)BENZOHYDRAZIDE.
DR DrugBank; DB04468; Afimoxifene.
DR DrugBank; DB06973; Bisphenol A.
DR DrugBank; DB07485; Bisphenol Z.
DR DrugBank; DB02659; Cholic Acid.
DR DrugBank; DB00255; Diethylstilbestrol.
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; DB06902; p-Cumylphenol.
DR DrugBank; DB00675; Tamoxifen.
DR DrugBank; DB00197; Troglitazone.
DR DrugCentral; P62508; -.
DR GuidetoPHARMACOLOGY; 624; -.
DR iPTMnet; P62508; -.
DR PhosphoSitePlus; P62508; -.
DR BioMuta; ESRRG; -.
DR DMDM; 50402102; -.
DR MassIVE; P62508; -.
DR MaxQB; P62508; -.
DR PaxDb; P62508; -.
DR PeptideAtlas; P62508; -.
DR PRIDE; P62508; -.
DR ProteomicsDB; 20283; -.
DR ProteomicsDB; 30159; -.
DR ProteomicsDB; 57405; -.
DR ProteomicsDB; 57406; -. [P62508-2]
DR ProteomicsDB; 57407; -. [P62508-3]
DR Antibodypedia; 20728; 525 antibodies from 39 providers.
DR DNASU; 2104; -.
DR Ensembl; ENST00000359162.6; ENSP00000352077.2; ENSG00000196482.18. [P62508-2]
DR Ensembl; ENST00000360012.7; ENSP00000353108.3; ENSG00000196482.18. [P62508-2]
DR Ensembl; ENST00000361395.6; ENSP00000354584.2; ENSG00000196482.18. [P62508-2]
DR Ensembl; ENST00000361525.7; ENSP00000355225.3; ENSG00000196482.18. [P62508-2]
DR Ensembl; ENST00000366937.5; ENSP00000355904.1; ENSG00000196482.18. [P62508-5]
DR Ensembl; ENST00000366938.6; ENSP00000355905.2; ENSG00000196482.18. [P62508-2]
DR Ensembl; ENST00000366940.6; ENSP00000355907.2; ENSG00000196482.18. [P62508-2]
DR Ensembl; ENST00000391890.7; ENSP00000375761.4; ENSG00000196482.18. [P62508-2]
DR Ensembl; ENST00000408911.8; ENSP00000386171.3; ENSG00000196482.18. [P62508-1]
DR Ensembl; ENST00000463665.5; ENSP00000418629.1; ENSG00000196482.18. [P62508-4]
DR Ensembl; ENST00000487276.5; ENSP00000419155.1; ENSG00000196482.18. [P62508-2]
DR Ensembl; ENST00000493603.5; ENSP00000419594.1; ENSG00000196482.18. [P62508-2]
DR Ensembl; ENST00000493748.5; ENSP00000417374.1; ENSG00000196482.18. [P62508-2]
DR Ensembl; ENST00000616180.4; ENSP00000481528.1; ENSG00000196482.18. [P62508-2]
DR Ensembl; ENST00000673908.1; ENSP00000500992.1; ENSG00000196482.18. [P62508-3]
DR GeneID; 2104; -.
DR KEGG; hsa:2104; -.
DR MANE-Select; ENST00000408911.8; ENSP00000386171.3; NM_001438.4; NP_001429.2.
DR UCSC; uc001hkw.3; human.
DR CTD; 2104; -.
DR DisGeNET; 2104; -.
DR GeneCards; ESRRG; -.
DR HGNC; HGNC:3474; ESRRG.
DR HPA; ENSG00000196482; Tissue enhanced (brain, parathyroid gland, retina, stomach).
DR MIM; 602969; gene.
DR neXtProt; NX_P62508; -.
DR OpenTargets; ENSG00000196482; -.
DR PharmGKB; PA27891; -.
DR VEuPathDB; HostDB:ENSG00000196482; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000153433; -.
DR InParanoid; P62508; -.
DR OMA; MDPVELC; -.
DR OrthoDB; 669799at2759; -.
DR PhylomeDB; P62508; -.
DR TreeFam; TF323751; -.
DR PathwayCommons; P62508; -.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR SignaLink; P62508; -.
DR SIGNOR; P62508; -.
DR BioGRID-ORCS; 2104; 19 hits in 1097 CRISPR screens.
DR ChiTaRS; ESRRG; human.
DR EvolutionaryTrace; P62508; -.
DR GeneWiki; Estrogen-related_receptor_gamma; -.
DR GenomeRNAi; 2104; -.
DR Pharos; P62508; Tchem.
DR PRO; PR:P62508; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P62508; protein.
DR Bgee; ENSG00000196482; Expressed in pons and 176 other tissues.
DR ExpressionAtlas; P62508; baseline and differential.
DR Genevisible; P62508; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0050682; F:AF-2 domain binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0034056; F:estrogen response element binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IBA:GO_Central.
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:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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:0048384; P:retinoic acid receptor signaling pathway; IEA:InterPro.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID00057; -.
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; IPR003078; Retinoic_acid_rcpt.
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; PR01292; RETNOICACIDR.
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; Activator; Alternative splicing; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Receptor;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..458
FT /note="Estrogen-related receptor gamma"
FT /id="PRO_0000053665"
FT DOMAIN 233..457
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 125..200
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 128..148
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 164..188
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 42..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:18063693,
FT ECO:0000305|PubMed:19067653"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10707956,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:9676434"
FT /id="VSP_003702"
FT VAR_SEQ 1..19
FT /note="MDSVELCLPESFSLHYEEE -> MWRECDWGLGAVKSDLACVPSAKR (in
FT isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_047156"
FT VAR_SEQ 158..196
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045980"
FT VAR_SEQ 234
FT /note="Y -> LLWSDPAD (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013301"
FT VARIANT 50
FT /note="T -> M (in dbSNP:rs11572693)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_019229"
FT MUTAGEN 38
FT /note="F->A,E: No effect on transcriptional activity."
FT /evidence="ECO:0000269|PubMed:19067653"
FT MUTAGEN 39
FT /note="I->A: 4-fold increase in transcriptional activity."
FT /evidence="ECO:0000269|PubMed:19067653"
FT MUTAGEN 40
FT /note="K->R: Abolishes sumoylation. 7-fold increase in
FT transcriptional activity."
FT /evidence="ECO:0000269|PubMed:16371476,
FT ECO:0000269|PubMed:18063693, ECO:0000269|PubMed:19067653"
FT MUTAGEN 41
FT /note="T->A: No effect on transcriptional activity."
FT /evidence="ECO:0000269|PubMed:19067653"
FT MUTAGEN 42
FT /note="E->A: 4-fold increase in transcriptional activity."
FT /evidence="ECO:0000269|PubMed:19067653"
FT MUTAGEN 44
FT /note="S->A,E: No effect on transcriptional activity."
FT /evidence="ECO:0000269|PubMed:19067653"
FT MUTAGEN 45
FT /note="S->A: Abolishes sumoylation. Increased
FT transcriptional activity."
FT /evidence="ECO:0000269|PubMed:18063693,
FT ECO:0000269|PubMed:19067653"
FT MUTAGEN 45
FT /note="S->D: No change in sumoylation nor transcriptional
FT activity."
FT /evidence="ECO:0000269|PubMed:18063693,
FT ECO:0000269|PubMed:19067653"
FT CONFLICT 19
FT /note="E -> K (in Ref. 4; AAQ93376)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="F -> S (in Ref. 3; AAC39899)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="T -> K (in Ref. 3; AAC39899)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="G -> A (in Ref. 3; AAC39899)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="V -> A (in Ref. 5; BAG54746)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="L -> C (in Ref. 3; AAC39899)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="V -> F (in Ref. 3; AAC39899)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="L -> P (in Ref. 5; CAH18320)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="V -> VC (in Ref. 3; AAC39899)"
FT /evidence="ECO:0000305"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:6I65"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1TFC"
FT HELIX 261..283
FT /evidence="ECO:0007829|PDB:6I65"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:6I65"
FT HELIX 294..316
FT /evidence="ECO:0007829|PDB:6I65"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:6I65"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:6I65"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:6I65"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6I65"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:6I65"
FT HELIX 343..359
FT /evidence="ECO:0007829|PDB:6I65"
FT HELIX 363..375
FT /evidence="ECO:0007829|PDB:6I65"
FT HELIX 385..406
FT /evidence="ECO:0007829|PDB:6I65"
FT HELIX 413..418
FT /evidence="ECO:0007829|PDB:6I65"
FT HELIX 421..441
FT /evidence="ECO:0007829|PDB:6I65"
FT HELIX 448..454
FT /evidence="ECO:0007829|PDB:6I65"
SQ SEQUENCE 458 AA; 51306 MW; 63D36CFD37573152 CRC64;
MDSVELCLPE SFSLHYEEEL LCRMSNKDRH IDSSCSSFIK TEPSSPASLT DSVNHHSPGG
SSDASGSYSS TMNGHQNGLD SPPLYPSAPI LGGSGPVRKL YDDCSSTIVE DPQTKCEYML
NSMPKRLCLV CGDIASGYHY GVASCEACKA FFKRTIQGNI EYSCPATNEC EITKRRRKSC
QACRFMKCLK VGMLKEGVRL DRVRGGRQKY KRRIDAENSP YLNPQLVQPA KKPYNKIVSH
LLVAEPEKIY AMPDPTVPDS DIKALTTLCD LADRELVVII GWAKHIPGFS TLSLADQMSL
LQSAWMEILI LGVVYRSLSF EDELVYADDY IMDEDQSKLA GLLDLNNAIL QLVKKYKSMK
LEKEEFVTLK AIALANSDSM HIEDVEAVQK LQDVLHEALQ DYEAGQHMED PRRAGKMLMT
LPLLRQTSTK AVQHFYNIKL EGKVPMHKLF LEMLEAKV
