PRGC2_HUMAN
ID PRGC2_HUMAN Reviewed; 1023 AA.
AC Q86YN6; A2RUM8; A2RUN0; B3KVW0; Q86YN3; Q86YN4; Q86YN5; Q8N1N9; Q8TDE4;
AC Q8TDE5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Peroxisome proliferator-activated receptor gamma coactivator 1-beta;
DE Short=PGC-1-beta;
DE Short=PPAR-gamma coactivator 1-beta;
DE Short=PPARGC-1-beta;
DE AltName: Full=PGC-1-related estrogen receptor alpha coactivator;
GN Name=PPARGC1B; Synonyms=PERC, PGC1, PGC1B, PPARGC1;
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] (ISOFORMS 1 AND 5), SUBCELLULAR LOCATION, MOTIF,
RP TISSUE SPECIFICITY, MUTAGENESIS OF 92-LEU--LEU-96; 155-LEU--LEU-160 AND
RP 343-LEU--LEU-347, INTERACTION WITH ESR1, AND FUNCTION.
RX PubMed=11854298; DOI=10.1074/jbc.m201134200;
RA Kressler D., Schreiber S.N., Knutti D., Kralli A.;
RT "The PGC-1-related protein PERC is a selective coactivator of estrogen
RT receptor alpha.";
RL J. Biol. Chem. 277:13918-13925(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY,
RP FUNCTION, AND VARIANT GLN-265.
RX PubMed=12678921; DOI=10.1042/bj20030200;
RA Meirhaeghe A., Crowley V., Lenaghan C., Lelliott C., Green K., Stewart A.,
RA Hart K., Schinner S., Sethi J.K., Yeo G., Brand M.D., Cortright R.N.,
RA O'Rahilly S., Montague C., Vidal-Puig A.J.;
RT "Characterization of the human, mouse and rat PGC1 beta (peroxisome-
RT proliferator-activated receptor-gamma co-activator 1 beta) gene in vitro
RT and in vivo.";
RL Biochem. J. 373:155-165(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
RC TISSUE=Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-292.
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 INDUCTION.
RX PubMed=12832613; DOI=10.1073/pnas.1032913100;
RA Patti M.E., Butte A.J., Crunkhorn S., Cusi K., Berria R., Kashyap S.,
RA Miyazaki Y., Kohane I., Costello M., Saccone R., Landaker E.J.,
RA Goldfine A.B., Mun E., DeFronzo R., Finlayson J., Kahn C.R.,
RA Mandarino L.J.;
RT "Coordinated reduction of genes of oxidative metabolism in humans with
RT insulin resistance and diabetes: potential role of PGC1 and NRF1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8466-8471(2003).
RN [8]
RP FUNCTION, AND INDUCTION BY INSULIN AND AGING.
RX PubMed=15546003; DOI=10.1172/jci200421889;
RA Ling C., Poulsen P., Carlsson E., Ridderstrale M., Almgren P.,
RA Wojtaszewski J., Beck-Nielsen H., Groop L., Vaag A.;
RT "Multiple environmental and genetic factors influence skeletal muscle PGC-
RT 1alpha and PGC-1beta gene expression in twins.";
RL J. Clin. Invest. 114:1518-1526(2004).
RN [9]
RP POLYMORPHISM, AND VARIANTS PRO-203; ILE-279 AND SER-292.
RX PubMed=15863669; DOI=10.1136/jmg.2004.026278;
RA Andersen G., Wegner L., Yanagisawa K., Rose C.S., Lin J., Gluemer C.,
RA Drivsholm T., Borch-Johnsen K., Jorgensen T., Hansen T., Spiegelman B.M.,
RA Pedersen O.;
RT "Evidence of an association between genetic variation of the coactivator
RT PGC-1beta and obesity.";
RL J. Med. Genet. 42:402-407(2005).
RN [10]
RP REGULATION BY FATTY ACIDS.
RX PubMed=16132959; DOI=10.1007/s00125-005-1895-z;
RA Staiger H., Staiger K., Haas C., Weisser M., Machicao F., Haering H.-U.;
RT "Fatty acid-induced differential regulation of the genes encoding
RT peroxisome proliferator-activated receptor-gamma coactivator-1alpha and
RT -1beta in human skeletal muscle cells that have been differentiated in
RT vitro.";
RL Diabetologia 48:2115-2118(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384; SER-524 AND SER-638, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Plays a role of stimulator of transcription factors and
CC nuclear receptors activities. Activates transcriptional activity of
CC estrogen receptor alpha, nuclear respiratory factor 1 (NRF1) and
CC glucocorticoid receptor in the presence of glucocorticoids. May play a
CC role in constitutive non-adrenergic-mediated mitochondrial biogenesis
CC as suggested by increased basal oxygen consumption and mitochondrial
CC number when overexpressed. May be involved in fat oxidation and non-
CC oxidative glucose metabolism and in the regulation of energy
CC expenditure. Induces the expression of PERM1 in the skeletal muscle in
CC an ESRRA-dependent manner. {ECO:0000269|PubMed:11854298,
CC ECO:0000269|PubMed:12678921, ECO:0000269|PubMed:15546003,
CC ECO:0000269|PubMed:23836911}.
CC -!- SUBUNIT: Interacts with hepatocyte nuclear factor 4-alpha/HNF4A, Sterol
CC regulatory binding transcription factor 1/SREBF1, PPAR-alpha/PPARA,
CC thyroid hormone receptor beta/THRB and host cell factor/HCFC1.
CC Interacts with estrogen-related receptor gamma/ESRRG and alpha/ESRRA.
CC Interacts with PRDM16 (By similarity). Interacts with estrogen receptor
CC alpha/ESR1. {ECO:0000250, ECO:0000269|PubMed:11854298}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11854298}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=PGC1beta-1a;
CC IsoId=Q86YN6-1; Sequence=Displayed;
CC Name=2; Synonyms=PGC1beta-2a;
CC IsoId=Q86YN6-2; Sequence=VSP_019299;
CC Name=3; Synonyms=PGC1beta-1b;
CC IsoId=Q86YN6-3; Sequence=VSP_019301;
CC Name=4; Synonyms=PGC1beta-2b;
CC IsoId=Q86YN6-4; Sequence=VSP_019299, VSP_019301;
CC Name=5; Synonyms=PERC-s;
CC IsoId=Q86YN6-5; Sequence=VSP_019300;
CC Name=6;
CC IsoId=Q86YN6-6; Sequence=VSP_043374, VSP_019300;
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher expression in heart, brain
CC and skeletal muscle. {ECO:0000269|PubMed:11854298,
CC ECO:0000269|PubMed:12678921}.
CC -!- INDUCTION: Repressed by saturated fatty acids such as palmitate and
CC stearate in skeletal muscle cells. Induced by insulin and reduced by
CC aging in skeletal muscle biopsies. Down-regulated in type 2 diabetes
CC mellitus subjects as well as in pre-diabetics.
CC {ECO:0000269|PubMed:12832613, ECO:0000269|PubMed:15546003}.
CC -!- DOMAIN: Contains 2 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which are usually
CC required for the association with nuclear receptors. {ECO:0000250}.
CC -!- POLYMORPHISM: Variation of PPARGC1B may contribute to the pathogenesis
CC of obesity, with a widespread Ala-203 allele being a risk factor for
CC the development of this common disorders.
CC {ECO:0000269|PubMed:15863669}.
CC -!- MISCELLANEOUS: [Isoform 5]: Lacks LXXLL motif 1 and has a reduced
CC ability to enhance the hormone-dependent activity of estrogen receptor
CC alpha. {ECO:0000305}.
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DR EMBL; AF468496; AAL78633.1; -; mRNA.
DR EMBL; AF468497; AAL78634.1; -; mRNA.
DR EMBL; AY188947; AAO40022.1; -; mRNA.
DR EMBL; AY188948; AAO40023.1; -; mRNA.
DR EMBL; AY188949; AAO40024.1; -; mRNA.
DR EMBL; AY188950; AAO40025.1; -; mRNA.
DR EMBL; AK095391; BAC04541.1; -; mRNA.
DR EMBL; AK123614; BAG53922.1; -; mRNA.
DR EMBL; AC008545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61759.1; -; Genomic_DNA.
DR EMBL; BC132971; AAI32972.1; -; mRNA.
DR EMBL; BC132973; AAI32974.1; -; mRNA.
DR CCDS; CCDS4298.1; -. [Q86YN6-1]
DR CCDS; CCDS54933.1; -. [Q86YN6-5]
DR CCDS; CCDS54934.1; -. [Q86YN6-6]
DR RefSeq; NP_001166169.1; NM_001172698.1. [Q86YN6-5]
DR RefSeq; NP_001166170.1; NM_001172699.1. [Q86YN6-6]
DR RefSeq; NP_573570.3; NM_133263.3. [Q86YN6-1]
DR RefSeq; XP_005268429.1; XM_005268372.4. [Q86YN6-2]
DR PDB; 3SP6; X-ray; 2.21 A; B=153-163.
DR PDB; 6D0Y; X-ray; 2.68 A; B=994-1023.
DR PDBsum; 3SP6; -.
DR PDBsum; 6D0Y; -.
DR AlphaFoldDB; Q86YN6; -.
DR SMR; Q86YN6; -.
DR BioGRID; 126361; 26.
DR IntAct; Q86YN6; 13.
DR STRING; 9606.ENSP00000312649; -.
DR DrugBank; DB01118; Amiodarone.
DR iPTMnet; Q86YN6; -.
DR PhosphoSitePlus; Q86YN6; -.
DR BioMuta; PPARGC1B; -.
DR DMDM; 116242724; -.
DR EPD; Q86YN6; -.
DR jPOST; Q86YN6; -.
DR MassIVE; Q86YN6; -.
DR MaxQB; Q86YN6; -.
DR PaxDb; Q86YN6; -.
DR PeptideAtlas; Q86YN6; -.
DR PRIDE; Q86YN6; -.
DR ProteomicsDB; 70440; -. [Q86YN6-1]
DR ProteomicsDB; 70441; -. [Q86YN6-2]
DR ProteomicsDB; 70442; -. [Q86YN6-3]
DR ProteomicsDB; 70443; -. [Q86YN6-4]
DR ProteomicsDB; 70444; -. [Q86YN6-5]
DR ProteomicsDB; 70445; -. [Q86YN6-6]
DR Antibodypedia; 27863; 124 antibodies from 29 providers.
DR DNASU; 133522; -.
DR Ensembl; ENST00000309241.10; ENSP00000312649.5; ENSG00000155846.17. [Q86YN6-1]
DR Ensembl; ENST00000360453.8; ENSP00000353638.4; ENSG00000155846.17. [Q86YN6-5]
DR Ensembl; ENST00000394320.7; ENSP00000377855.3; ENSG00000155846.17. [Q86YN6-3]
DR Ensembl; ENST00000403750.5; ENSP00000384403.1; ENSG00000155846.17. [Q86YN6-6]
DR GeneID; 133522; -.
DR KEGG; hsa:133522; -.
DR MANE-Select; ENST00000309241.10; ENSP00000312649.5; NM_133263.4; NP_573570.3.
DR UCSC; uc003lrb.3; human. [Q86YN6-1]
DR CTD; 133522; -.
DR DisGeNET; 133522; -.
DR GeneCards; PPARGC1B; -.
DR HGNC; HGNC:30022; PPARGC1B.
DR HPA; ENSG00000155846; Tissue enhanced (retina).
DR MIM; 608886; gene.
DR neXtProt; NX_Q86YN6; -.
DR OpenTargets; ENSG00000155846; -.
DR PharmGKB; PA134953410; -.
DR VEuPathDB; HostDB:ENSG00000155846; -.
DR eggNOG; ENOG502QTA7; Eukaryota.
DR GeneTree; ENSGT00950000183137; -.
DR HOGENOM; CLU_014202_0_0_1; -.
DR InParanoid; Q86YN6; -.
DR OMA; PTKPCCH; -.
DR OrthoDB; 94418at2759; -.
DR PhylomeDB; Q86YN6; -.
DR TreeFam; TF343068; -.
DR PathwayCommons; Q86YN6; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR SignaLink; Q86YN6; -.
DR BioGRID-ORCS; 133522; 336 hits in 1081 CRISPR screens.
DR ChiTaRS; PPARGC1B; human.
DR EvolutionaryTrace; Q86YN6; -.
DR GeneWiki; PPARGC1B; -.
DR GenomeRNAi; 133522; -.
DR Pharos; Q86YN6; Tbio.
DR PRO; PR:Q86YN6; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q86YN6; protein.
DR Bgee; ENSG00000155846; Expressed in endothelial cell and 143 other tissues.
DR ExpressionAtlas; Q86YN6; baseline and differential.
DR Genevisible; Q86YN6; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0050682; F:AF-2 domain binding; IPI:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006390; P:mitochondrial transcription; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IEA:Ensembl.
DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR CDD; cd12356; RRM_PPARGC1B; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034605; PGC-1.
DR InterPro; IPR034621; PGC-1beta.
DR InterPro; IPR034177; PPARGC1B_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR15528; PTHR15528; 1.
DR PANTHER; PTHR15528:SF12; PTHR15528:SF12; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..1023
FT /note="Peroxisome proliferator-activated receptor gamma
FT coactivator 1-beta"
FT /id="PRO_0000240158"
FT DOMAIN 902..976
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..91
FT /note="Abolishes DNA transcriptional activity when missing"
FT REGION 122..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 156..160
FT /note="LXXLL motif 1"
FT MOTIF 343..347
FT /note="LXXLL motif 2"
FT MOTIF 691..694
FT /note="HCFC1-binding-motif (HBM)"
FT COMPBIAS 131..145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..826
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..26
FT /note="MAGNDCGALLDEELSSFFLNYLADTQ -> MGVYK (in isoform 2
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12678921"
FT /id="VSP_019299"
FT VAR_SEQ 1..26
FT /note="MAGNDCGALLDEELSSFFLNYLADTQ -> M (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043374"
FT VAR_SEQ 156..194
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11854298,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_019300"
FT VAR_SEQ 991..1023
FT /note="DSNSEEALPASGKSKYEAMDFDSLLKEAQQSLH -> GKPLKPSHSLVRLKA
FT WEAVPSLNKTQS (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12678921"
FT /id="VSP_019301"
FT VARIANT 203
FT /note="A -> P (in dbSNP:rs7732671)"
FT /evidence="ECO:0000269|PubMed:15863669"
FT /id="VAR_026698"
FT VARIANT 265
FT /note="R -> Q (in dbSNP:rs45520937)"
FT /evidence="ECO:0000269|PubMed:12678921"
FT /id="VAR_026699"
FT VARIANT 279
FT /note="V -> I (in dbSNP:rs17572019)"
FT /evidence="ECO:0000269|PubMed:15863669"
FT /id="VAR_026700"
FT VARIANT 292
FT /note="R -> S (in dbSNP:rs11959820)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15863669"
FT /id="VAR_026701"
FT MUTAGEN 92..96
FT /note="LLAEL->AAAEA: Reduces DNA transcriptional activity."
FT /evidence="ECO:0000269|PubMed:11854298"
FT MUTAGEN 155..160
FT /note="LLQKLL->AAQKAA: Reduces interaction and activation
FT of ESR1. Loss of interaction and activation of ESR1; when
FT associated with 343-AREAA-347."
FT /evidence="ECO:0000269|PubMed:11854298"
FT MUTAGEN 343..347
FT /note="LRELL->AREAA: Reduces interaction and activation of
FT ESR1. Loss of interaction and activation of ESR1; when
FT associated with 155-AAQKAA-160."
FT /evidence="ECO:0000269|PubMed:11854298"
FT CONFLICT 558
FT /note="E -> G (in Ref. 3; BAC04541)"
FT /evidence="ECO:0000305"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:3SP6"
FT HELIX 1011..1021
FT /evidence="ECO:0007829|PDB:6D0Y"
SQ SEQUENCE 1023 AA; 113222 MW; DC37FCDE4D3CD239 CRC64;
MAGNDCGALL DEELSSFFLN YLADTQGGGS GEEQLYADFP ELDLSQLDAS DFDSATCFGE
LQWCPENSET EPNQYSPDDS ELFQIDSENE ALLAELTKTL DDIPEDDVGL AAFPALDGGD
ALSCTSASPA PSSAPPSPAP EKPSAPAPEV DELSLLQKLL LATSYPTSSS DTQKEGTAWR
QAGLRSKSQR PCVKADSTQD KKAPMMQSQS RSCTELHKHL TSAQCCLQDR GLQPPCLQSP
RLPAKEDKEP GEDCPSPQPA PASPRDSLAL GRADPGAPVS QEDMQAMVQL IRYMHTYCLP
QRKLPPQTPE PLPKACSNPS QQVRSRPWSR HHSKASWAEF SILRELLAQD VLCDVSKPYR
LATPVYASLT PRSRPRPPKD SQASPGRPSS VEEVRIAASP KSTGPRPSLR PLRLEVKREV
RRPARLQQQE EEDEEEEEEE EEEEKEEEEE WGRKRPGRGL PWTKLGRKLE SSVCPVRRSR
RLNPELGPWL TFADEPLVPS EPQGALPSLC LAPKAYDVER ELGSPTDEDS GQDQQLLRGP
QIPALESPCE SGCGDMDEDP SCPQLPPRDS PRCLMLALSQ SDPTFGKKSF EQTLTVELCG
TAGLTPPTTP PYKPTEEDPF KPDIKHSLGK EIALSLPSPE GLSLKATPGA AHKLPKKHPE
RSELLSHLRH ATAQPASQAG QKRPFSCSFG DHDYCQVLRP EGVLQRKVLR SWEPSGVHLE
DWPQQGAPWA EAQAPGREED RSCDAGAPPK DSTLLRDHEI RASLTKHFGL LETALEEEDL
ASCKSPEYDT VFEDSSSSSG ESSFLPEEEE EEGEEEEEDD EEEDSGVSPT CSDHCPYQSP
PSKANRQLCS RSRSSSGSSP CHSWSPATRR NFRCESRGPC SDRTPSIRHA RKRREKAIGE
GRVVYIQNLS SDMSSRELKR RFEVFGEIEE CEVLTRNRRG EKYGFITYRC SEHAALSLTK
GAALRKRNEP SFQLSYGGLR HFCWPRYTDY DSNSEEALPA SGKSKYEAMD FDSLLKEAQQ
SLH
