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 24-JAN-2024, entry version 172. 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/jci21889; 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}. 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; 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; 28. DR IntAct; Q86YN6; 12. DR STRING; 9606.ENSP00000312649; -. DR DrugBank; DB01118; Amiodarone. DR GlyGen; Q86YN6; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000312649; -. DR PeptideAtlas; 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; 154 antibodies from 30 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 AGR; HGNC:30022; -. 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; EPTKPCC; -. DR OrthoDB; 3134278at2759; -. 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; 341 hits in 1159 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 145 other cell types or tissues. DR ExpressionAtlas; Q86YN6; baseline and differential. 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 DNA-templated transcription; IEA:Ensembl. DR GO; GO:0001503; P:ossification; 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: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 DNA-templated transcription; IDA:UniProtKB. 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; IPR034177; PPARGC1B_RRM. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR15528; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1 PGC-1 -RELATED; 1. DR PANTHER; PTHR15528:SF12; PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA COACTIVATOR 1-BETA; 1. DR Pfam; PF00076; RRM_1; 1. DR SMART; SM00360; RRM; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 1. DR Genevisible; Q86YN6; HS. 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 //