PRGC1_HUMAN
ID PRGC1_HUMAN Reviewed; 798 AA.
AC Q9UBK2; B7Z406; G8DM16; I3RTT5; I3RTT6; I3RTT7; I3RTT8; I3RTT9; Q3LIG1;
AC Q4W5M7; Q9UN32;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Peroxisome proliferator-activated receptor gamma coactivator 1-alpha;
DE Short=PGC-1-alpha {ECO:0000303|PubMed:16753578};
DE Short=PPAR-gamma coactivator 1-alpha {ECO:0000303|PubMed:10585775};
DE Short=PPARGC-1-alpha {ECO:0000303|PubMed:10585775};
DE AltName: Full=Ligand effect modulator 6;
GN Name=PPARGC1A;
GN Synonyms=LEM6, PGC1, PGC1A {ECO:0000303|PubMed:16753578}, 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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RX PubMed=10585775; DOI=10.1006/geno.1999.5977;
RA Esterbauer H., Oberkofler H., Krempler F., Patsch W.;
RT "Human peroxisome proliferator activated receptor gamma coactivator 1
RT (PPARGC1) gene: cDNA sequence, genomic organization, chromosomal
RT localization, and tissue expression.";
RL Genomics 62:98-102(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP SER-482.
RC TISSUE=Skeletal muscle;
RX PubMed=10643692; DOI=10.1038/sj.ijo.0801106;
RA Larrouy D., Vidal H., Andreelli F., Laville M., Langin D.;
RT "Cloning and mRNA tissue distribution of human PPARgamma coactivator-1.";
RL Int. J. Obes. Relat. Metab. Disord. 23:1327-1332(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10713165; DOI=10.1128/mcb.20.7.2411-2422.2000;
RA Knutti D., Kaul A., Kralli A.;
RT "A tissue-specific coactivator of steroid receptors, identified in a
RT functional genetic screen.";
RL Mol. Cell. Biol. 20:2411-2422(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9), AND SUBCELLULAR LOCATION (ISOFORM
RP 9).
RC TISSUE=Liver;
RX PubMed=22009745; DOI=10.1074/jbc.m111.227496;
RA Felder T.K., Soyal S.M., Oberkofler H., Hahne P., Auer S., Weiss R.,
RA Gadermaier G., Miller K., Krempler F., Esterbauer H., Patsch W.;
RT "Characterization of novel peroxisome proliferator-activated receptor gamma
RT coactivator-1alpha (PGC-1alpha) isoform in human liver.";
RL J. Biol. Chem. 286:42923-42936(2011).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B4; B4-3EXT; B4-8A; B5 AND B5-NT),
RP ALTERNATIVE PROMOTER USAGE, ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=22589246; DOI=10.1093/hmg/dds177;
RA Soyal S.M., Felder T.K., Auer S., Hahne P., Oberkofler H., Witting A.,
RA Paulmichl M., Landwehrmeyer G.B., Weydt P., Patsch W.;
RT "A greatly extended PPARGC1A genomic locus encodes several new brain-
RT specific isoforms and influences Huntington disease age of onset.";
RL Hum. Mol. Genet. 21:3461-3473(2012).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NT-7A), AND ALTERNATIVE SPLICING.
RC TISSUE=Skeletal muscle;
RA Endo H.;
RT "Isoform of PGC-1 generated by alternative splicing.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8A).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rieder M.J., Johanson E.J., da Ponte S.H., Stanaway I.B., Ahearn M.O.,
RA Bertucci C.B., Wong M.W., Yi Q., Nickerson D.A.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP INTERACTION WITH LRPPRC.
RX PubMed=17050673; DOI=10.1101/gad.1483906;
RA Cooper M.P., Qu L., Rohas L.M., Lin J., Yang W., Erdjument-Bromage H.,
RA Tempst P., Spiegelman B.M.;
RT "Defects in energy homeostasis in Leigh syndrome French Canadian variant
RT through PGC-1alpha/LRP130 complex.";
RL Genes Dev. 20:2996-3009(2006).
RN [12]
RP FUNCTION, AND ACETYLATION BY KAT2A.
RX PubMed=16753578; DOI=10.1016/j.cmet.2006.04.013;
RA Lerin C., Rodgers J.T., Kalume D.E., Kim S.H., Pandey A., Puigserver P.;
RT "GCN5 acetyltransferase complex controls glucose metabolism through
RT transcriptional repression of PGC-1alpha.";
RL Cell Metab. 3:429-438(2006).
RN [13]
RP FUNCTION, AND REGULATION BY ACETYLATION.
RX PubMed=20005308; DOI=10.1016/j.bbapap.2009.11.023;
RA Dominy J.E. Jr., Lee Y., Gerhart-Hines Z., Puigserver P.;
RT "Nutrient-dependent regulation of PGC-1alpha's acetylation state and
RT metabolic function through the enzymatic activities of Sirt1/GCN5.";
RL Biochim. Biophys. Acta 1804:1676-1683(2010).
RN [14]
RP FUNCTION, AND INDUCTION.
RX PubMed=21376232; DOI=10.1016/j.cell.2011.02.010;
RA Shin J.H., Ko H.S., Kang H., Lee Y., Lee Y.I., Pletinkova O.,
RA Troconso J.C., Dawson V.L., Dawson T.M.;
RT "PARIS (ZNF746) repression of PGC-1alpha contributes to neurodegeneration
RT in Parkinson's disease.";
RL Cell 144:689-702(2011).
RN [15]
RP FUNCTION, AND ACETYLATION BY KAT2A.
RX PubMed=23142079; DOI=10.1016/j.molcel.2012.09.030;
RA Dominy J.E. Jr., Lee Y., Jedrychowski M.P., Chim H., Jurczak M.J.,
RA Camporez J.P., Ruan H.B., Feldman J., Pierce K., Mostoslavsky R.,
RA Denu J.M., Clish C.B., Yang X., Shulman G.I., Gygi S.P., Puigserver P.;
RT "The deacetylase Sirt6 activates the acetyltransferase GCN5 and suppresses
RT hepatic gluconeogenesis.";
RL Mol. Cell 48:900-913(2012).
RN [16]
RP UBIQUITINATION BY RNF34.
RX PubMed=22064484; DOI=10.1128/mcb.05674-11;
RA Wei P., Pan D., Mao C., Wang Y.X.;
RT "RNF34 is a cold-regulated E3 ubiquitin ligase for PGC-1alpha and modulates
RT brown fat cell metabolism.";
RL Mol. Cell. Biol. 32:266-275(2012).
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).
CC -!- FUNCTION: Transcriptional coactivator for steroid receptors and nuclear
CC receptors (PubMed:10713165, PubMed:20005308, PubMed:21376232). Greatly
CC increases the transcriptional activity of PPARG and thyroid hormone
CC receptor on the uncoupling protein promoter (PubMed:10713165,
CC PubMed:20005308, PubMed:21376232). Can regulate key mitochondrial genes
CC that contribute to the program of adaptive thermogenesis
CC (PubMed:10713165, PubMed:20005308, PubMed:21376232). Plays an essential
CC role in metabolic reprogramming in response to dietary availability
CC through coordination of the expression of a wide array of genes
CC involved in glucose and fatty acid metabolism (PubMed:10713165,
CC PubMed:20005308, PubMed:21376232). Acts as a key regulator of
CC gluconeogenesis: stimulates hepatic gluconeogenesis by increasing the
CC expression of gluconeogenic enzymes, and acting together with FOXO1 to
CC promote the fasting gluconeogenic program (PubMed:16753578,
CC PubMed:23142079). Induces the expression of PERM1 in the skeletal
CC muscle in an ESRRA-dependent manner (PubMed:23836911). Also involved in
CC the integration of the circadian rhythms and energy metabolism (By
CC similarity). Required for oscillatory expression of clock genes, such
CC as ARNTL/BMAL1 and NR1D1, through the coactivation of RORA and RORC,
CC and metabolic genes, such as PDK4 and PEPCK (By similarity).
CC {ECO:0000250|UniProtKB:O70343, ECO:0000269|PubMed:10713165,
CC ECO:0000269|PubMed:16753578, ECO:0000269|PubMed:20005308,
CC ECO:0000269|PubMed:21376232, ECO:0000269|PubMed:23142079,
CC ECO:0000269|PubMed:23836911}.
CC -!- SUBUNIT: Homooligomer (PubMed:10713165). Interacts with MYBBP1A;
CC inhibits MYBBP1A transcriptional activation (By similarity). Interacts
CC with PRDM16, LPIN1 and PML (By similarity). Interacts (via LXXLL motif)
CC with RORA and RORC (via AF-2 motif); activates RORA and RORC
CC transcriptional activation (By similarity). Interacts with LRPPRC
CC (PubMed:17050673). Interacts with FOXO1 (By similarity).
CC {ECO:0000250|UniProtKB:O70343, ECO:0000269|PubMed:10713165,
CC ECO:0000269|PubMed:17050673}.
CC -!- INTERACTION:
CC Q9UBK2; P11474: ESRRA; NbExp=20; IntAct=EBI-765486, EBI-372412;
CC Q9UBK2; P62508: ESRRG; NbExp=4; IntAct=EBI-765486, EBI-2834260;
CC Q9UBK2; P62508-3: ESRRG; NbExp=5; IntAct=EBI-765486, EBI-12001340;
CC Q9UBK2; P41235: HNF4A; NbExp=4; IntAct=EBI-765486, EBI-1049011;
CC Q9UBK2; P42704: LRPPRC; NbExp=2; IntAct=EBI-765486, EBI-1050853;
CC Q9UBK2; P37231: PPARG; NbExp=2; IntAct=EBI-765486, EBI-781384;
CC Q9UBK2; P10826-2: RARB; NbExp=3; IntAct=EBI-765486, EBI-8583223;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:10713165}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:O70343}.
CC -!- SUBCELLULAR LOCATION: [Isoform B4]: Nucleus
CC {ECO:0000269|PubMed:22589246}.
CC -!- SUBCELLULAR LOCATION: [Isoform B4-8a]: Cytoplasm
CC {ECO:0000269|PubMed:22589246}. Nucleus {ECO:0000269|PubMed:22589246}.
CC -!- SUBCELLULAR LOCATION: [Isoform B5]: Nucleus
CC {ECO:0000269|PubMed:22589246}. Nucleus, PML body
CC {ECO:0000269|PubMed:22589246}.
CC -!- SUBCELLULAR LOCATION: [Isoform 9]: Nucleus
CC {ECO:0000269|PubMed:22009745}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q9UBK2-1; Sequence=Displayed;
CC Name=NT-7a;
CC IsoId=Q9UBK2-2; Sequence=VSP_047684, VSP_047685;
CC Name=B5;
CC IsoId=Q9UBK2-3; Sequence=VSP_053724;
CC Name=B4;
CC IsoId=Q9UBK2-4; Sequence=VSP_053725;
CC Name=B4-8a;
CC IsoId=Q9UBK2-5; Sequence=VSP_053725, VSP_053728, VSP_053729;
CC Name=B5-NT;
CC IsoId=Q9UBK2-6; Sequence=VSP_053724, VSP_047684, VSP_047685;
CC Name=B4-3ext;
CC IsoId=Q9UBK2-7; Sequence=VSP_053725, VSP_053726, VSP_053727;
CC Name=8a;
CC IsoId=Q9UBK2-8; Sequence=VSP_053728, VSP_053729;
CC Name=9; Synonyms=L-PGG-1alpha;
CC IsoId=Q9UBK2-9; Sequence=VSP_053770;
CC -!- TISSUE SPECIFICITY: Heart, skeletal muscle, liver and kidney. Expressed
CC at lower levels in brain and pancreas and at very low levels in the
CC intestine and white adipose tissue. In skeletal muscle, levels were
CC lower in obese than in lean subjects and fasting induced a 2-fold
CC increase in levels in the skeletal muscle in obese subjects.
CC {ECO:0000269|PubMed:10585775, ECO:0000269|PubMed:10643692,
CC ECO:0000269|PubMed:10713165}.
CC -!- INDUCTION: Transcription is repressed by ZNF746 which binds to 'insulin
CC response sequences' its promoter. {ECO:0000269|PubMed:21376232}.
CC -!- PTM: Phosphorylation by AMPK in skeletal muscle increases activation of
CC its own promoter. Phosphorylated by CLK2.
CC {ECO:0000250|UniProtKB:O70343}.
CC -!- PTM: Heavily acetylated by KAT2A/GCN5 under conditions of high
CC nutrients, leading to inactivation of PPARGC1A (PubMed:16753578,
CC PubMed:20005308, PubMed:23142079). Deacetylated by SIRT1 in low
CC nutrients/high NAD conditions, leading to its activation
CC (PubMed:20005308). {ECO:0000269|PubMed:16753578,
CC ECO:0000269|PubMed:20005308, ECO:0000269|PubMed:23142079}.
CC -!- PTM: Ubiquitinated. Ubiquitination by RNF34 induces proteasomal
CC degradation. {ECO:0000269|PubMed:22064484}.
CC -!- MISCELLANEOUS: [Isoform B5]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform B4]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform B4-8a]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform B5-NT]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform B4-3ext]: Produced by alternative promoter
CC usage. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 9]: Produced by alternative promoter usage. May
CC be involved in gluconeogenesis, liver-specific. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/ppargc1a/";
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DR EMBL; AF108205; AAF19083.1; -; Genomic_DNA.
DR EMBL; AF108193; AAF19083.1; JOINED; Genomic_DNA.
DR EMBL; AF108194; AAF19083.1; JOINED; Genomic_DNA.
DR EMBL; AF108195; AAF19083.1; JOINED; Genomic_DNA.
DR EMBL; AF108196; AAF19083.1; JOINED; Genomic_DNA.
DR EMBL; AF108197; AAF19083.1; JOINED; Genomic_DNA.
DR EMBL; AF108198; AAF19083.1; JOINED; Genomic_DNA.
DR EMBL; AF108199; AAF19083.1; JOINED; Genomic_DNA.
DR EMBL; AF108200; AAF19083.1; JOINED; Genomic_DNA.
DR EMBL; AF108201; AAF19083.1; JOINED; Genomic_DNA.
DR EMBL; AF108202; AAF19083.1; JOINED; Genomic_DNA.
DR EMBL; AF108203; AAF19083.1; JOINED; Genomic_DNA.
DR EMBL; AF108204; AAF19083.1; JOINED; Genomic_DNA.
DR EMBL; AF106698; AAF18573.1; -; mRNA.
DR EMBL; AF159714; AAD51615.1; -; mRNA.
DR EMBL; AF186379; AAD56250.1; -; mRNA.
DR EMBL; HQ695733; ADW77180.1; -; mRNA.
DR EMBL; JQ772116; AFK29753.1; -; mRNA.
DR EMBL; JQ772117; AFK29754.1; -; mRNA.
DR EMBL; JQ772118; AFK29755.1; -; mRNA.
DR EMBL; JQ772119; AFK29756.1; -; mRNA.
DR EMBL; JQ772120; AFK29757.1; -; mRNA.
DR EMBL; AB061325; BAE46508.1; -; mRNA.
DR EMBL; EU280319; ABX44665.1; -; Genomic_DNA.
DR EMBL; AK296591; BAH12392.1; -; mRNA.
DR EMBL; AC092834; AAY41058.1; -; Genomic_DNA.
DR EMBL; AC097508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471069; EAW92811.1; -; Genomic_DNA.
DR CCDS; CCDS3429.1; -. [Q9UBK2-1]
DR CCDS; CCDS87211.1; -. [Q9UBK2-9]
DR RefSeq; NP_001317680.1; NM_001330751.1. [Q9UBK2-3]
DR RefSeq; NP_001317681.1; NM_001330752.1. [Q9UBK2-4]
DR RefSeq; NP_001317682.1; NM_001330753.1. [Q9UBK2-9]
DR RefSeq; NP_037393.1; NM_013261.4. [Q9UBK2-1]
DR RefSeq; XP_011512073.1; XM_011513771.1. [Q9UBK2-9]
DR PDB; 1XB7; X-ray; 2.50 A; P=205-216.
DR PDB; 3B1M; X-ray; 1.60 A; B=136-154.
DR PDB; 3CS8; X-ray; 2.30 A; B=141-152.
DR PDB; 3D24; X-ray; 2.11 A; B/D=198-219.
DR PDB; 3U9Q; X-ray; 1.52 A; B=142-150.
DR PDB; 3V9T; X-ray; 1.65 A; C=136-154.
DR PDB; 3V9V; X-ray; 1.60 A; C=136-154.
DR PDB; 4QJR; X-ray; 2.40 A; B=139-152.
DR PDB; 4QK4; X-ray; 2.81 A; B=139-152.
DR PDB; 5Q0I; X-ray; 1.70 A; B=141-152.
DR PDB; 5TWO; X-ray; 1.93 A; B=138-152.
DR PDB; 5UNJ; X-ray; 1.96 A; C=139-152.
DR PDB; 5Z5S; X-ray; 1.80 A; C=136-154.
DR PDB; 5Z6S; X-ray; 1.80 A; C=136-154.
DR PDB; 6AD9; X-ray; 2.20 A; B=141-152.
DR PDB; 6FZF; X-ray; 1.95 A; C/D=139-152.
DR PDB; 6FZP; X-ray; 2.30 A; C=139-152.
DR PDB; 6IZM; X-ray; 1.80 A; C=136-154.
DR PDB; 6IZN; X-ray; 1.75 A; C=136-154.
DR PDB; 6K0T; X-ray; 1.84 A; B/D=139-150.
DR PDB; 6KXX; X-ray; 1.95 A; B=135-156.
DR PDB; 6KXY; X-ray; 2.00 A; B=135-156.
DR PDB; 6LN4; X-ray; 2.61 A; B=207-216.
DR PDB; 6MS7; X-ray; 1.43 A; B=141-151.
DR PDB; 6NWK; X-ray; 1.65 A; B=141-152.
DR PDB; 6NWL; X-ray; 1.59 A; B=141-152.
DR PDB; 6T1V; X-ray; 2.21 A; C=139-152.
DR PDB; 6W9K; X-ray; 1.60 A; B=142-151.
DR PDB; 6W9L; X-ray; 1.45 A; B=141-152.
DR PDB; 7E2E; X-ray; 2.70 A; P/Q=205-216.
DR PDB; 7KHT; X-ray; 2.50 A; B=139-152.
DR PDBsum; 1XB7; -.
DR PDBsum; 3B1M; -.
DR PDBsum; 3CS8; -.
DR PDBsum; 3D24; -.
DR PDBsum; 3U9Q; -.
DR PDBsum; 3V9T; -.
DR PDBsum; 3V9V; -.
DR PDBsum; 4QJR; -.
DR PDBsum; 4QK4; -.
DR PDBsum; 5Q0I; -.
DR PDBsum; 5TWO; -.
DR PDBsum; 5UNJ; -.
DR PDBsum; 5Z5S; -.
DR PDBsum; 5Z6S; -.
DR PDBsum; 6AD9; -.
DR PDBsum; 6FZF; -.
DR PDBsum; 6FZP; -.
DR PDBsum; 6IZM; -.
DR PDBsum; 6IZN; -.
DR PDBsum; 6K0T; -.
DR PDBsum; 6KXX; -.
DR PDBsum; 6KXY; -.
DR PDBsum; 6LN4; -.
DR PDBsum; 6MS7; -.
DR PDBsum; 6NWK; -.
DR PDBsum; 6NWL; -.
DR PDBsum; 6T1V; -.
DR PDBsum; 6W9K; -.
DR PDBsum; 6W9L; -.
DR PDBsum; 7E2E; -.
DR PDBsum; 7KHT; -.
DR AlphaFoldDB; Q9UBK2; -.
DR SMR; Q9UBK2; -.
DR BioGRID; 116097; 71.
DR CORUM; Q9UBK2; -.
DR DIP; DIP-38449N; -.
DR ELM; Q9UBK2; -.
DR IntAct; Q9UBK2; 20.
DR MINT; Q9UBK2; -.
DR STRING; 9606.ENSP00000264867; -.
DR ChEMBL; CHEMBL6116; -.
DR GlyGen; Q9UBK2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UBK2; -.
DR PhosphoSitePlus; Q9UBK2; -.
DR BioMuta; PPARGC1A; -.
DR DMDM; 47117335; -.
DR jPOST; Q9UBK2; -.
DR MassIVE; Q9UBK2; -.
DR MaxQB; Q9UBK2; -.
DR PaxDb; Q9UBK2; -.
DR PeptideAtlas; Q9UBK2; -.
DR PRIDE; Q9UBK2; -.
DR Antibodypedia; 10142; 357 antibodies from 40 providers.
DR DNASU; 10891; -.
DR Ensembl; ENST00000264867.7; ENSP00000264867.2; ENSG00000109819.9. [Q9UBK2-1]
DR Ensembl; ENST00000506055.5; ENSP00000423075.1; ENSG00000109819.9. [Q9UBK2-2]
DR Ensembl; ENST00000513205.5; ENSP00000421632.1; ENSG00000109819.9. [Q9UBK2-8]
DR Ensembl; ENST00000613098.4; ENSP00000481498.1; ENSG00000109819.9. [Q9UBK2-9]
DR GeneID; 10891; -.
DR KEGG; hsa:10891; -.
DR MANE-Select; ENST00000264867.7; ENSP00000264867.2; NM_013261.5; NP_037393.1.
DR UCSC; uc003gqs.3; human. [Q9UBK2-1]
DR CTD; 10891; -.
DR DisGeNET; 10891; -.
DR GeneCards; PPARGC1A; -.
DR HGNC; HGNC:9237; PPARGC1A.
DR HPA; ENSG00000109819; Tissue enhanced (liver).
DR MalaCards; PPARGC1A; -.
DR MIM; 604517; gene.
DR neXtProt; NX_Q9UBK2; -.
DR OpenTargets; ENSG00000109819; -.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR PharmGKB; PA33558; -.
DR VEuPathDB; HostDB:ENSG00000109819; -.
DR eggNOG; ENOG502QSXU; Eukaryota.
DR GeneTree; ENSGT00950000183137; -.
DR HOGENOM; CLU_020104_0_0_1; -.
DR InParanoid; Q9UBK2; -.
DR OMA; KCPSKKK; -.
DR OrthoDB; 94418at2759; -.
DR PhylomeDB; Q9UBK2; -.
DR TreeFam; TF343068; -.
DR PathwayCommons; Q9UBK2; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; Q9UBK2; -.
DR SIGNOR; Q9UBK2; -.
DR BioGRID-ORCS; 10891; 12 hits in 1075 CRISPR screens.
DR ChiTaRS; PPARGC1A; human.
DR EvolutionaryTrace; Q9UBK2; -.
DR GeneWiki; PPARGC1A; -.
DR GenomeRNAi; 10891; -.
DR Pharos; Q9UBK2; Tbio.
DR PRO; PR:Q9UBK2; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UBK2; protein.
DR Bgee; ENSG00000109819; Expressed in renal medulla and 177 other tissues.
DR ExpressionAtlas; Q9UBK2; baseline and differential.
DR Genevisible; Q9UBK2; HS.
DR GO; GO:0000785; C:chromatin; IC:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; TAS:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; TAS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; TAS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0050873; P:brown fat cell differentiation; TAS:UniProtKB.
DR GO; GO:0001678; P:cellular glucose homeostasis; NAS:UniProtKB.
DR GO; GO:0045333; P:cellular respiration; TAS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007586; P:digestion; TAS:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:0019395; P:fatty acid oxidation; NAS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; IDA:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; NAS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; TAS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:1901215; P:negative regulation of neuron death; IGI:UniProtKB.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISS:UniProtKB.
DR GO; GO:1901857; P:positive regulation of cellular respiration; 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; IDA:BHF-UCL.
DR GO; GO:0046321; P:positive regulation of fatty acid oxidation; TAS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ARUK-UCL.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; TAS:UniProtKB.
DR GO; GO:0035066; P:positive regulation of histone acetylation; TAS:UniProtKB.
DR GO; GO:1901860; P:positive regulation of mitochondrial DNA metabolic process; IEA:Ensembl.
DR GO; GO:0010822; P:positive regulation of mitochondrion organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:1901863; P:positive regulation of muscle tissue development; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; TAS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; ISS:UniProtKB.
DR GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
DR GO; GO:0014850; P:response to muscle activity; ISS:BHF-UCL.
DR GO; GO:0042594; P:response to starvation; NAS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
DR GO; GO:0001659; P:temperature homeostasis; TAS:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:UniProtKB.
DR CDD; cd12623; RRM_PPARGC1A; 1.
DR DisProt; DP01489; -.
DR Gene3D; 3.30.70.330; -; 1.
DR IDEAL; IID00103; -.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034605; PGC-1.
DR InterPro; IPR034625; PGC-1alpha.
DR InterPro; IPR034833; PPARGC1A_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR15528; PTHR15528; 1.
DR PANTHER; PTHR15528:SF10; PTHR15528:SF10; 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; Acetylation; Activator; Alternative promoter usage;
KW Alternative splicing; Biological rhythms; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..798
FT /note="Peroxisome proliferator-activated receptor gamma
FT coactivator 1-alpha"
FT /id="PRO_0000081732"
FT DOMAIN 677..753
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 100..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..339
FT /note="Interaction with PPARG"
FT /evidence="ECO:0000269|PubMed:10713165"
FT REGION 350..798
FT /note="Mediates interaction with RNF34"
FT /evidence="ECO:0000269|PubMed:22064484"
FT REGION 542..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 144..148
FT /note="LXXLL motif"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT COMPBIAS 222..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 178
FT /note="Phosphothreonine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 184
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 254
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 271
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 278
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 321
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 347
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 413
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 442
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 451
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 539
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 758
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 779
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT VAR_SEQ 1..127
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:22009745"
FT /id="VSP_053770"
FT VAR_SEQ 1..18
FT /note="MAWDMCNQDSESVWSDIE -> MDEGYF (in isoform B4, isoform
FT B4-8a and isoform B4-3ext)"
FT /evidence="ECO:0000303|PubMed:22589246"
FT /id="VSP_053725"
FT VAR_SEQ 1..18
FT /note="MAWDMCNQDSESVWSDIE -> MDETSPRLEEDWKKVLQREAGWQ (in
FT isoform B5 and isoform B5-NT)"
FT /evidence="ECO:0000303|PubMed:22589246"
FT /id="VSP_053724"
FT VAR_SEQ 144..150
FT /note="LKKLLLA -> VRTLPTV (in isoform B4-3ext)"
FT /evidence="ECO:0000303|PubMed:22589246"
FT /id="VSP_053726"
FT VAR_SEQ 151..798
FT /note="Missing (in isoform B4-3ext)"
FT /evidence="ECO:0000303|PubMed:22589246"
FT /id="VSP_053727"
FT VAR_SEQ 269..271
FT /note="DPK -> LFL (in isoform NT-7a and isoform B5-NT)"
FT /evidence="ECO:0000303|PubMed:22589246, ECO:0000303|Ref.6"
FT /id="VSP_047684"
FT VAR_SEQ 272..798
FT /note="Missing (in isoform NT-7a and isoform B5-NT)"
FT /evidence="ECO:0000303|PubMed:22589246, ECO:0000303|Ref.6"
FT /id="VSP_047685"
FT VAR_SEQ 294..301
FT /note="LTPPTTPP -> VKTNLISK (in isoform B4-8a and isoform
FT 8a)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:22589246"
FT /id="VSP_053728"
FT VAR_SEQ 302..798
FT /note="Missing (in isoform B4-8a and isoform 8a)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:22589246"
FT /id="VSP_053729"
FT VARIANT 482
FT /note="G -> S (in dbSNP:rs8192678)"
FT /evidence="ECO:0000269|PubMed:10643692"
FT /id="VAR_018450"
FT VARIANT 612
FT /note="T -> M (in dbSNP:rs3736265)"
FT /id="VAR_018451"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:6MS7"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:3D24"
SQ SEQUENCE 798 AA; 91027 MW; 97DDD3643051A5F1 CRC64;
MAWDMCNQDS ESVWSDIECA ALVGEDQPLC PDLPELDLSE LDVNDLDTDS FLGGLKWCSD
QSEIISNQYN NEPSNIFEKI DEENEANLLA VLTETLDSLP VDEDGLPSFD ALTDGDVTTD
NEASPSSMPD GTPPPQEAEE PSLLKKLLLA PANTQLSYNE CSGLSTQNHA NHNHRIRTNP
AIVKTENSWS NKAKSICQQQ KPQRRPCSEL LKYLTTNDDP PHTKPTENRN SSRDKCTSKK
KSHTQSQSQH LQAKPTTLSL PLTPESPNDP KGSPFENKTI ERTLSVELSG TAGLTPPTTP
PHKANQDNPF RASPKLKSSC KTVVPPPSKK PRYSESSGTQ GNNSTKKGPE QSELYAQLSK
SSVLTGGHEE RKTKRPSLRL FGDHDYCQSI NSKTEILINI SQELQDSRQL ENKDVSSDWQ
GQICSSTDSD QCYLRETLEA SKQVSPCSTR KQLQDQEIRA ELNKHFGHPS QAVFDDEADK
TGELRDSDFS NEQFSKLPMF INSGLAMDGL FDDSEDESDK LSYPWDGTQS YSLFNVSPSC
SSFNSPCRDS VSPPKSLFSQ RPQRMRSRSR SFSRHRSCSR SPYSRSRSRS PGSRSSSRSC
YYYESSHYRH RTHRNSPLYV RSRSRSPYSR RPRYDSYEEY QHERLKREEY RREYEKRESE
RAKQRERQRQ KAIEERRVIY VGKIRPDTTR TELRDRFEVF GEIEECTVNL RDDGDSYGFI
TYRYTCDAFA ALENGYTLRR SNETDFELYF CGRKQFFKSN YADLDSNSDD FDPASTKSKY
DSLDFDSLLK EAQRSLRR
