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O70343

- PRGC1_MOUSE

UniProt

O70343 - PRGC1_MOUSE

Protein

Peroxisome proliferator-activated receptor gamma coactivator 1-alpha

Gene

Ppargc1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Transcriptional coactivator for steroid receptors and nuclear receptors. Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter. Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis. Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. Also involved in the integration of the circadian rhythms and energy metabolism. Required for oscillatory expression of clock genes, such as ARNTL/BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK. Isoform 4 specifically activates the expression of IGF1 and suppresses myostatin expression in skeletal muscle leading to muscle fiber hypertrophy.4 Publications

    GO - Molecular functioni

    1. chromatin DNA binding Source: MGI
    2. DNA binding Source: MGI
    3. ligand-dependent nuclear receptor transcription coactivator activity Source: Ensembl
    4. nucleotide binding Source: InterPro
    5. protein binding Source: UniProtKB
    6. RNA binding Source: UniProtKB-KW
    7. sequence-specific DNA binding Source: UniProtKB
    8. transcription coactivator activity Source: UniProtKB
    9. transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. androgen metabolic process Source: Ensembl
    2. cellular response to fatty acid Source: Ensembl
    3. cellular response to hypoxia Source: Ensembl
    4. cellular response to nitrite Source: Ensembl
    5. cellular response to oxidative stress Source: MGI
    6. cellular response to thyroid hormone stimulus Source: Ensembl
    7. cellular response to tumor necrosis factor Source: Ensembl
    8. circadian regulation of gene expression Source: UniProtKB
    9. flavone metabolic process Source: Ensembl
    10. galactose metabolic process Source: Ensembl
    11. mitochondrion organization Source: Ensembl
    12. negative regulation of glycolytic process Source: Ensembl
    13. negative regulation of neuron apoptotic process Source: MGI
    14. negative regulation of receptor activity Source: Ensembl
    15. neuron death Source: UniProtKB
    16. positive regulation of ATP biosynthetic process Source: UniProtKB
    17. positive regulation of cellular respiration Source: UniProtKB
    18. positive regulation of energy homeostasis Source: UniProtKB
    19. positive regulation of fatty acid oxidation Source: Ensembl
    20. positive regulation of mitochondrial DNA metabolic process Source: UniProtKB
    21. positive regulation of mitochondrion organization Source: UniProtKB
    22. positive regulation of muscle tissue development Source: UniProtKB
    23. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    24. positive regulation of smooth muscle cell proliferation Source: Ensembl
    25. positive regulation of transcription, DNA-templated Source: MGI
    26. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    27. regulation of cell death Source: UniProtKB
    28. regulation of circadian rhythm Source: UniProtKB
    29. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: Ensembl
    30. regulation of transcription, DNA-templated Source: UniProtKB
    31. respiratory electron transport chain Source: MGI
    32. response to cold Source: Ensembl
    33. response to epinephrine Source: Ensembl
    34. response to leucine Source: Ensembl
    35. response to muscle activity Source: BHF-UCL
    36. response to norepinephrine Source: Ensembl
    37. response to starvation Source: Ensembl
    38. response to statin Source: Ensembl
    39. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_118837. Rora activates circadian gene expression.
    REACT_198351. RORA activates circadian gene expression.
    REACT_198352. REV-ERBA represses gene expression.
    REACT_198602. PPARA activates gene expression.
    REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_205688. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_24972. Circadian Clock.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
    Short name:
    PGC-1-alpha
    Short name:
    PPAR-gamma coactivator 1-alpha
    Short name:
    PPARGC-1-alpha
    Gene namesi
    Name:Ppargc1a
    Synonyms:Pgc1, Pgc1a, Ppargc1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1342774. Ppargc1a.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. nucleoplasm Source: Reactome
    3. nucleus Source: MGI
    4. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice show abnormal diurnal rhythms of activity, body temperature and metabolic rate.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi142 – 1465LKKLL → AKKAA: Strongly reduces coactivation of RORA activity. 1 Publication
    Mutagenesisi177 – 1771T → A: Abolishes AMPK-mediated phosphorylation; when associated with A-538. 2 Publications
    Mutagenesisi538 – 5381S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-177. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 797797Peroxisome proliferator-activated receptor gamma coactivator 1-alphaPRO_0000081733Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei77 – 771N6-acetyllysine1 Publication
    Modified residuei144 – 1441N6-acetyllysine1 Publication
    Modified residuei177 – 1771Phosphothreonine; by AMPK2 Publications
    Modified residuei183 – 1831N6-acetyllysine1 Publication
    Modified residuei253 – 2531N6-acetyllysine1 Publication
    Modified residuei270 – 2701N6-acetyllysine1 Publication
    Modified residuei277 – 2771N6-acetyllysine1 Publication
    Modified residuei320 – 3201N6-acetyllysine1 Publication
    Modified residuei346 – 3461N6-acetyllysine1 Publication
    Modified residuei412 – 4121N6-acetyllysine1 Publication
    Modified residuei441 – 4411N6-acetyllysine1 Publication
    Modified residuei450 – 4501N6-acetyllysine1 Publication
    Modified residuei538 – 5381Phosphoserine; by AMPK2 Publications
    Modified residuei757 – 7571N6-acetyllysine1 Publication
    Modified residuei778 – 7781N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylation by AMPK in skeletal muscle increases activation of its own promoter. Phosphorylated by CLK2.2 Publications
    Heavily acetylated by GCN5 and biologically inactive under conditions of high nutrients. Deacetylated by SIRT1 in low nutrients/high NAD conditions.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiO70343.
    PRIDEiO70343.

    PTM databases

    PhosphoSiteiO70343.

    Expressioni

    Tissue specificityi

    White quadriceps and red tibialis anterior (TA) muscles, liver, kidney and brown adipose tissue (at protein level). Skeletal muscle, brown adipose tissue, heart, kidney and brain.3 Publications

    Inductioni

    Dramatically induced in brown adipose tissue and skeletal muscle by exposure of animals to cold. Up-regulated in brown adipose tissue of obese leptin-deficient (ob/ob) and leptin-unresponsive (db/db) mice. Leptin is required for normal basal and cold-stimulated expression in brown adipose tissue and hyperleptinemia rapidly up-regulates its expression. Induced in muscle by exercise. Oscillates diurnally in liver and skeletal muscle.5 Publications

    Gene expression databases

    ArrayExpressiO70343.
    BgeeiO70343.
    GenevestigatoriO70343.

    Interactioni

    Subunit structurei

    Homooligomer. Interacts with MYBBP1A; inhibits MYBBP1A transcriptional activation. Interacts with LRPPRC, PRDM16, LPIN1 and PML. Interacts (via LXXLL motif) with RORA and RORC (via AF-2 motif); activates RORA and RORC transcriptional activation.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LrpprcQ6PB662EBI-1371053,EBI-1371262
    Sirt1Q923E46EBI-1371053,EBI-1802585

    Protein-protein interaction databases

    BioGridi202321. 11 interactions.
    DIPiDIP-38447N.
    IntActiO70343. 7 interactions.

    Structurei

    Secondary structure

    1
    797
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi141 – 1477

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3F7DX-ray2.20B137-150[»]
    ProteinModelPortaliO70343.
    SMRiO70343. Positions 674-774.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO70343.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini676 – 75277RRMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni292 – 33847Interaction with PPARGBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi142 – 1465LXXLL motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi565 – 59834Arg/Ser-richAdd
    BLAST
    Compositional biasi620 – 63213Arg/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG78353.
    GeneTreeiENSGT00530000063196.
    HOGENOMiHOG000037431.
    HOVERGENiHBG053678.
    InParanoidiO70343.
    KOiK07202.
    OMAiENGYTLR.
    OrthoDBiEOG7S4X5H.
    PhylomeDBiO70343.
    TreeFamiTF343068.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: O70343-1) [UniParc]FASTAAdd to Basket

    Also known as: PGC-1a1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAWDMCSQDS VWSDIECAAL VGEDQPLCPD LPELDLSELD VNDLDTDSFL    50
    GGLKWCSDQS EIISNQYNNE PANIFEKIDE ENEANLLAVL TETLDSLPVD 100
    EDGLPSFDAL TDGAVTTDNE ASPSSMPDGT PPPQEAEEPS LLKKLLLAPA 150
    NTQLSYNECS GLSTQNHAAN HTHRIRTNPA IVKTENSWSN KAKSICQQQK 200
    PQRRPCSELL KYLTTNDDPP HTKPTENRNS SRDKCASKKK SHTQPQSQHA 250
    QAKPTTLSLP LTPESPNDPK GSPFENKTIE RTLSVELSGT AGLTPPTTPP 300
    HKANQDNPFK ASPKLKPSCK TVVPPPTKRA RYSECSGTQG SHSTKKGPEQ 350
    SELYAQLSKS SGLSRGHEER KTKRPSLRLF GDHDYCQSLN SKTDILINIS 400
    QELQDSRQLD FKDASCDWQG HICSSTDSGQ CYLRETLEAS KQVSPCSTRK 450
    QLQDQEIRAE LNKHFGHPCQ AVFDDKSDKT SELRDGDFSN EQFSKLPVFI 500
    NSGLAMDGLF DDSEDESDKL SYPWDGTQPY SLFDVSPSCS SFNSPCRDSV 550
    SPPKSLFSQR PQRMRSRSRS FSRHRSCSRS PYSRSRSRSP GSRSSSRSCY 600
    YYESSHYRHR THRNSPLYVR SRSRSPYSRR PRYDSYEAYE HERLKRDEYR 650
    KEHEKRESER AKQRERQKQK AIEERRVIYV GKIRPDTTRT ELRDRFEVFG 700
    EIEECTVNLR DDGDSYGFIT YRYTCDAFAA LENGYTLRRS NETDFELYFC 750
    GRKQFFKSNY ADLDTNSDDF DPASTKSKYD SLDFDSLLKE AQRSLRR 797
    Length:797
    Mass (Da):90,588
    Last modified:August 1, 1998 - v1
    Checksum:iAE73EE2B3A622B05
    GO
    Isoform 2 (identifier: O70343-2) [UniParc]FASTAAdd to Basket

    Also known as: PGC-1a2

    The sequence of this isoform differs from the canonical sequence as follows:
         2-16: AWDMCSQDSVWSDIE → LGLSSMDSILK
         108-274: Missing.
         545-680: PCRDSVSPPK...AIEERRVIYV → LNVIIT
         681-797: Missing.

    Note: Produced by alternative promoter usage and alternative splicing.

    Show »
    Length:379
    Mass (Da):41,921
    Checksum:iF9FC43F94A209D82
    GO
    Isoform 3 (identifier: O70343-3) [UniParc]FASTAAdd to Basket

    Also known as: PGC-1a3

    The sequence of this isoform differs from the canonical sequence as follows:
         2-16: AWDMCSQDSVWSDIE → LL
         108-274: Missing.
         545-680: PCRDSVSPPK...AIEERRVIYV → LNVIIT
         681-797: Missing.

    Note: Produced by alternative promoter usage and alternative splicing.

    Show »
    Length:370
    Mass (Da):41,002
    Checksum:iAA98B0425EE8F122
    GO
    Isoform 4 (identifier: O70343-4) [UniParc]FASTAAdd to Basket

    Also known as: PGC-1a4

    The sequence of this isoform differs from the canonical sequence as follows:
         2-16: AWDMCSQDSVWSDIE → LGLSSMDSILK
         268-500: DPKGSPFENK...EQFSKLPVFI → LFL
         501-797: Missing.

    Note: Produced by alternative promoter usage and alternative splicing.

    Show »
    Length:266
    Mass (Da):29,115
    Checksum:i317BEC86DF2E9DFB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti587 – 5871S → L in AAH66868. (PubMed:15489334)Curated
    Sequence conflicti629 – 6291R → C in AAH66868. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 1615AWDMC…WSDIE → LGLSSMDSILK in isoform 2 and isoform 4. 1 PublicationVSP_053275Add
    BLAST
    Alternative sequencei2 – 1615AWDMC…WSDIE → LL in isoform 3. 1 PublicationVSP_053276Add
    BLAST
    Alternative sequencei108 – 274167Missing in isoform 2 and isoform 3. 1 PublicationVSP_053277Add
    BLAST
    Alternative sequencei268 – 500233DPKGS…LPVFI → LFL in isoform 4. 1 PublicationVSP_053279Add
    BLAST
    Alternative sequencei501 – 797297Missing in isoform 4. 1 PublicationVSP_053281Add
    BLAST
    Alternative sequencei545 – 680136PCRDS…RVIYV → LNVIIT in isoform 2 and isoform 3. 1 PublicationVSP_053278Add
    BLAST
    Alternative sequencei681 – 797117Missing in isoform 2 and isoform 3. 1 PublicationVSP_053280Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF049330 mRNA. Translation: AAC13554.1.
    JX866946 mRNA. Translation: AFZ74947.1.
    JX866947 mRNA. Translation: AFZ74948.1.
    JX866948 mRNA. Translation: AFZ74949.1.
    AK138668 mRNA. Translation: BAE23740.1.
    AK143753 mRNA. Translation: BAE25525.1.
    CH466524 Genomic DNA. Translation: EDL37647.1.
    BC066868 mRNA. Translation: AAH66868.1.
    CCDSiCCDS19282.1. [O70343-1]
    RefSeqiNP_032930.1. NM_008904.2. [O70343-1]
    UniGeneiMm.259072.

    Genome annotation databases

    EnsembliENSMUST00000132734; ENSMUSP00000117040; ENSMUSG00000029167. [O70343-1]
    GeneIDi19017.
    KEGGimmu:19017.
    UCSCiuc008xkc.2. mouse. [O70343-1]

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF049330 mRNA. Translation: AAC13554.1 .
    JX866946 mRNA. Translation: AFZ74947.1 .
    JX866947 mRNA. Translation: AFZ74948.1 .
    JX866948 mRNA. Translation: AFZ74949.1 .
    AK138668 mRNA. Translation: BAE23740.1 .
    AK143753 mRNA. Translation: BAE25525.1 .
    CH466524 Genomic DNA. Translation: EDL37647.1 .
    BC066868 mRNA. Translation: AAH66868.1 .
    CCDSi CCDS19282.1. [O70343-1 ]
    RefSeqi NP_032930.1. NM_008904.2. [O70343-1 ]
    UniGenei Mm.259072.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3F7D X-ray 2.20 B 137-150 [» ]
    ProteinModelPortali O70343.
    SMRi O70343. Positions 674-774.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202321. 11 interactions.
    DIPi DIP-38447N.
    IntActi O70343. 7 interactions.

    PTM databases

    PhosphoSitei O70343.

    Proteomic databases

    PaxDbi O70343.
    PRIDEi O70343.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000132734 ; ENSMUSP00000117040 ; ENSMUSG00000029167 . [O70343-1 ]
    GeneIDi 19017.
    KEGGi mmu:19017.
    UCSCi uc008xkc.2. mouse. [O70343-1 ]

    Organism-specific databases

    CTDi 10891.
    MGIi MGI:1342774. Ppargc1a.

    Phylogenomic databases

    eggNOGi NOG78353.
    GeneTreei ENSGT00530000063196.
    HOGENOMi HOG000037431.
    HOVERGENi HBG053678.
    InParanoidi O70343.
    KOi K07202.
    OMAi ENGYTLR.
    OrthoDBi EOG7S4X5H.
    PhylomeDBi O70343.
    TreeFami TF343068.

    Enzyme and pathway databases

    Reactomei REACT_118837. Rora activates circadian gene expression.
    REACT_198351. RORA activates circadian gene expression.
    REACT_198352. REV-ERBA represses gene expression.
    REACT_198602. PPARA activates gene expression.
    REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_205688. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_24972. Circadian Clock.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Miscellaneous databases

    EvolutionaryTracei O70343.
    NextBioi 295448.
    PROi O70343.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O70343.
    Bgeei O70343.
    Genevestigatori O70343.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis."
      Puigserver P., Wu Z., Park C.W., Graves R., Wright M., Spiegelman B.M.
      Cell 92:829-839(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, TISSUE SPECIFICITY.
      Strain: C57BL/6J.
      Tissue: Brown adipose tissue.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, INDUCTION.
      Strain: C57BL/6.
      Tissue: Skeletal muscle.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Spinal cord and Spleen.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: CD-1.
      Tissue: Neural stem cell.
    6. "Role of leptin in peroxisome proliferator-activated receptor gamma coactivator-1 expression."
      Kakuma T., Wang Z.-W., Pan W., Unger R.H., Zhou Y.-T.
      Endocrinology 141:4576-4582(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. "Suppression of mitochondrial respiration through recruitment of p160 myb binding protein to PGC-1alpha: modulation by p38 MAPK."
      Fan M., Rhee J., St Pierre J., Handschin C., Puigserver P., Lin J., Jaeger S., Erdjument-Bromage H., Tempst P., Spiegelman B.M.
      Genes Dev. 18:278-289(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYBBP1.
    8. "Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1."
      Rodgers J.T., Lerin C., Haas W., Gygi S.P., Spiegelman B.M., Puigserver P.
      Nature 434:113-118(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ACETYLATION AT LYS-77; LYS-144; LYS-183; LYS-253; LYS-270; LYS-277; LYS-320; LYS-346; LYS-412; LYS-441; LYS-450; LYS-757 AND LYS-778, DEACETYLATION BY SIRT1.
    9. "Lipin 1 is an inducible amplifier of the hepatic PGC-1alpha/PPARalpha regulatory pathway."
      Finck B.N., Gropler M.C., Chen Z., Leone T.C., Croce M.A., Harris T.E., Lawrence J.C. Jr., Kelly D.P.
      Cell Metab. 4:199-210(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LPIN1.
    10. Cited for: INTERACTION WITH PRDM16.
    11. "AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha."
      Jager S., Handschin C., St-Pierre J., Spiegelman B.M.
      Proc. Natl. Acad. Sci. U.S.A. 104:12017-12022(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-177 AND SER-538, MUTAGENESIS OF THR-177 AND SER-538.
    12. "Transcriptional coactivator PGC-1alpha integrates the mammalian clock and energy metabolism."
      Liu C., Li S., Liu T., Borjigin J., Lin J.D.
      Nature 447:477-481(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN RHYTHMS, INTERACTION WITH RORA AND RORC, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 142-LEU--LEU-146.
    13. "Regulation of the brown and white fat gene programs through a PRDM16/CtBP transcriptional complex."
      Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P., Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.
      Genes Dev. 22:1397-1409(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRDM16.
    14. "Cdc2-like kinase 2 is an insulin-regulated suppressor of hepatic gluconeogenesis."
      Rodgers J.T., Haas W., Gygi S.P., Puigserver P.
      Cell Metab. 11:23-34(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CLK2.
    15. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PML.
    16. Cited for: INDUCTION.

    Entry informationi

    Entry nameiPRGC1_MOUSE
    AccessioniPrimary (citable) accession number: O70343
    Secondary accession number(s): L0AM20
    , L0AN96, L0APB0, Q3UP72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3