AC T05295
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ID T05295
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DT 22.10.2002 (created); oke.
CO Copyright (C), QIAGEN.
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FA PGC-1-isoform1
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SY Ligand effect modulator 6; peroxisome-proliferator-activated receptor gamma, co-activator 1; PGC-1; PGC-1-alpha; PGC1; PPAR gamma coactivator 1-alpha; PPAR-gamma co-activator 1; PPARGC-1-alpha; PPARGC1.
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OS human, Homo sapiens
OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; primates
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GE G004832 PPARGC1A; HGNC: PPARGC1A.
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SZ 798 AA; 91.0 kDa (cDNA) (calc.).
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SQ MAWDMCNQDSESVWSDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSD
SQ QSEIISNQYNNEPSNIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGDVTTD
SQ NEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHANHNHRIRTNP
SQ AIVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTENRNSSRDKCTSKK
SQ KSHTQSQSQHLQAKPTTLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTP
SQ PHKANQDNPFRASPKLKSSCKTVVPPPSKKPRYSESSGTQGNNSTKKGPEQSELYAQLSK
SQ SSVLTGGHEERKTKRPSLRLFGDHDYCQSINSKTEILINISQELQDSRQLENKDVSSDWQ
SQ GQICSSTDSDQCYLRETLEASKQVSPCSTRKQLQDQEIRAELNKHFGHPSQAVFDDEADK
SQ TGELRDSDFSNEQFSKLPMFINSGLAMDGLFDDSEDESDKLSYPWDGTQSYSLFNVSPSC
SQ SSFNSPCRDSVSPPKSLFSQRPQRMRSRSRSFSRHRSCSRSPYSRSRSRSPGSRSSSRSC
SQ YYYESSHYRHRTHRNSPLYVRSRSRSPYSRRPRYDSYEEYQHERLKREEYRREYEKRESE
SQ RAKQRERQRQKAIEERRVIYVGKIRPDTTRTELRDRFEVFGEIEECTVNLRDDGDSYGFI
SQ TYRYTCDAFAALENGYTLRRSNETDFELYFCGRKQFFKSNYADLDSNSDDFDPASTKSKY
SQ DSLDFDSLLKEAQRSLRR
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SC translated from EMBL #AF106698
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FT 146 586 
PF00478; IMP dehydrogenase / GMP reductase domain.
FT 677 753 
PS50102; RRM.
FT 678 747 
SM00360; rrm1_1.
FT 679 745 
PF00076; RNA recognition motif. (a.k.a. RRM, RBD, or.
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SF the amino-terminal 190 amino acids of PGC-1-isoform1 are sufficient to mediate a strong interaction with HNF-4alpha transactivation domain [1];
SF the same region is shown to mediate ligand-dependent interactions with AF-2 domains of ERalpha, PPARalpha, GR;
SF PGC-1-isoform1 interacts with PPARgamma in a ligand-independent fashion;
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FF It co-activates the LXR/RXR-mediated expression of SREBP-1c T01558, and dexamethasone-stimulated expression of SREBP-2 T01560 [4];
FF co-activator of PPARgamma, PPARalpha, ERalpha;
FF co-activator of HNF-4alpha and GR [1];
FF may regulate aspects of hepatic glucose metabolism [1];
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IN T05682 ERR1-isoform1; human, Homo sapiens.
IN T17105 FXR; Mammalia.
IN T03828 HNF-4alpha; human, Homo sapiens.
IN T00851 T3R-beta1; human, Homo sapiens.
IN T08482 VDR-isoform1; human, Homo sapiens.
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BS R32255.
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DR TRANSPATH: MO000033776.
DR EMBL: AF106698; AF106698.
DR EMBL: AF186379;
DR UniProtKB: Q9UBK2;
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RN [1]; RE0018079.
RX PUBMED: 11557972.
RA Yoon J. C., Puigserver P., Chen G., Donovan J., Wu Z., Rhee J., Adelmant G., Stafford J., Kahn C. R., Granner D. K., Newgard C. B., Spiegelman B. M.
RT Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1.
RL Nature 413:131-138 (2001).
RN [2]; RE0047400.
RX PUBMED: 15908514.
RA Savkur R. S., Bramlett K. S., Stayrook K. R., Nagpal S., Burris T. P.
RT Coactivation of the human vitamin D receptor by the peroxisome proliferator-activated receptor gamma coactivator-1 alpha.
RL Mol. Pharmacol. 68:511-517 (2005).
RN [3]; RE0047758.
RX PUBMED: 11751919.
RA Wu Y., Delerive P., Chin W. W., Burris T. P.
RT Requirement of helix 1 and the AF-2 domain of the thyroid hormone receptor for coactivation by PGC-1.
RL J. Biol. Chem. 277:8898-8905 (2002).
RN [4]; RE0048535.
RX PUBMED: 16282353.
RA Oberkofler H., Klein K., Felder T. K., Krempler F., Patsch W.
RT Role of peroxisome proliferator-activated receptor-gamma coactivator-1alpha in the transcriptional regulation of the human uncoupling protein 2 gene in INS-1E cells.
RL Endocrinology 147:966-976 (2006).
RN [5]; RE0051163.
RX PUBMED: 15329387.
RA Savkur R. S., Thomas J. S., Bramlett K. S., Gao Y., Michael L. F., Burris T. P.
RT Ligand-dependent coactivation of the human bile acid receptor FXR by the peroxisome proliferator-activated receptor gamma coactivator-1alpha.
RL J. Pharmacol. Exp. Ther. 312:170-178 (2005).
RN [6]; RE0053654.
RX PUBMED: 18441008.
RA Greschik H., Althage M., Flaig R., Sato Y., Peluso-Iltis C., Chavant V., Choulier L., Cronet P., Rochel N., Schule R., Stromstedt P. E., Moras D.
RT Communication between the ERR alpha homodimer interface and the PGC-1alpha binding surface vie the helix 8-9 loop.
RL J. Biol. Chem. 283:20220-20230 (2008).
RN [7]; RE0067583.
RX PUBMED: 20661474.
RA Kong X., Wang R., Xue Y., Liu X., Zhang H., Chen Y., Fang F., Chang Y.
RT Sirtuin 3, a New Target of PGC-1alpha, Plays an Important Role in the Suppression of ROS and Mitochondrial Biogenesis.
RL PLoS ONE 5:e11707 (2010).
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