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Protein

Peroxisome proliferator-activated receptor gamma coactivator 1-alpha

Gene

Ppargc1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  • adipose tissue development Source: CACAO
  • androgen metabolic process Source: Ensembl
  • cellular respiration Source: GO_Central
  • cellular response to fatty acid Source: Ensembl
  • cellular response to hypoxia Source: Ensembl
  • cellular response to nitrite Source: Ensembl
  • cellular response to oxidative stress Source: MGI
  • cellular response to thyroid hormone stimulus Source: Ensembl
  • cellular response to tumor necrosis factor Source: Ensembl
  • circadian regulation of gene expression Source: UniProtKB
  • circadian rhythm Source: Reactome
  • flavone metabolic process Source: Ensembl
  • galactose metabolic process Source: Ensembl
  • mitochondrion organization Source: Ensembl
  • negative regulation of glycolytic process Source: Ensembl
  • negative regulation of neuron apoptotic process Source: MGI
  • negative regulation of neuron death Source: UniProtKB
  • negative regulation of receptor activity Source: Ensembl
  • negative regulation of smooth muscle cell migration Source: Ensembl
  • positive regulation of ATP biosynthetic process Source: UniProtKB
  • positive regulation of cellular respiration Source: UniProtKB
  • positive regulation of energy homeostasis Source: UniProtKB
  • positive regulation of fatty acid oxidation Source: GO_Central
  • positive regulation of mitochondrial DNA metabolic process Source: UniProtKB
  • positive regulation of mitochondrion organization Source: UniProtKB
  • positive regulation of muscle tissue development Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of smooth muscle cell proliferation Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: CACAO
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: Ensembl
  • regulation of transcription, DNA-templated Source: UniProtKB
  • respiratory electron transport chain Source: MGI
  • response to cold Source: Ensembl
  • response to dietary excess Source: MGI
  • response to epinephrine Source: Ensembl
  • response to leucine Source: Ensembl
  • response to muscle activity Source: BHF-UCL
  • response to norepinephrine Source: Ensembl
  • response to starvation Source: Ensembl
  • response to statin Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_115781. Bmal1:Clock,Npas2 activates circadian gene expression.
REACT_118837. Rora activates gene expression.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
REACT_276725. RORA activates gene expression.
REACT_309805. Transcriptional regulation of white adipocyte differentiation.
REACT_321345. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_328033. Transcriptional activation of mitochondrial biogenesis.
REACT_344843. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_351159. Circadian Clock.

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 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1342774. Ppargc1a.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • PML body Source: UniProtKB-SubCell
Complete GO annotation...

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. 1 Publication
Mutagenesisi538 – 5381S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-177. 1 Publication

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 AMPK1 Publication
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 AMPK1 Publication
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
Ubiquitinated. Ubiquitination by RNF34 induces proteasomal degradation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

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

BgeeiO70343.
ExpressionAtlasiO70343. baseline and differential.
GenevisibleiO70343. MM.

Interactioni

Subunit structurei

Homooligomer (By similarity). Interacts with MYBBP1A; inhibits MYBBP1A transcriptional activation. Interacts with PRDM16, LPIN1 and PML. Interacts (via LXXLL motif) with RORA and RORC (via AF-2 motif); activates RORA and RORC transcriptional activation. Interacts with LRPPRC (By similarity). Interacts with RNF34 (via RING-type zinc finger) (By similarity).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Irf4Q642876EBI-1371053,EBI-6398485
LrpprcQ6PB662EBI-1371053,EBI-1371262
Sirt1Q923E46EBI-1371053,EBI-1802585

Protein-protein interaction databases

BioGridi202321. 12 interactions.
DIPiDIP-38447N.
IntActiO70343. 8 interactions.
STRINGi10090.ENSMUSP00000117040.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3F7DX-ray2.20B137-150[»]
ProteinModelPortaliO70343.
SMRiO70343. Positions 673-737.
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
Regioni349 – 797449Mediates interaction with RNF34By 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. AlignAdd to basket

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

        10         20         30         40         50
MAWDMCSQDS VWSDIECAAL VGEDQPLCPD LPELDLSELD VNDLDTDSFL
60 70 80 90 100
GGLKWCSDQS EIISNQYNNE PANIFEKIDE ENEANLLAVL TETLDSLPVD
110 120 130 140 150
EDGLPSFDAL TDGAVTTDNE ASPSSMPDGT PPPQEAEEPS LLKKLLLAPA
160 170 180 190 200
NTQLSYNECS GLSTQNHAAN HTHRIRTNPA IVKTENSWSN KAKSICQQQK
210 220 230 240 250
PQRRPCSELL KYLTTNDDPP HTKPTENRNS SRDKCASKKK SHTQPQSQHA
260 270 280 290 300
QAKPTTLSLP LTPESPNDPK GSPFENKTIE RTLSVELSGT AGLTPPTTPP
310 320 330 340 350
HKANQDNPFK ASPKLKPSCK TVVPPPTKRA RYSECSGTQG SHSTKKGPEQ
360 370 380 390 400
SELYAQLSKS SGLSRGHEER KTKRPSLRLF GDHDYCQSLN SKTDILINIS
410 420 430 440 450
QELQDSRQLD FKDASCDWQG HICSSTDSGQ CYLRETLEAS KQVSPCSTRK
460 470 480 490 500
QLQDQEIRAE LNKHFGHPCQ AVFDDKSDKT SELRDGDFSN EQFSKLPVFI
510 520 530 540 550
NSGLAMDGLF DDSEDESDKL SYPWDGTQPY SLFDVSPSCS SFNSPCRDSV
560 570 580 590 600
SPPKSLFSQR PQRMRSRSRS FSRHRSCSRS PYSRSRSRSP GSRSSSRSCY
610 620 630 640 650
YYESSHYRHR THRNSPLYVR SRSRSPYSRR PRYDSYEAYE HERLKRDEYR
660 670 680 690 700
KEHEKRESER AKQRERQKQK AIEERRVIYV GKIRPDTTRT ELRDRFEVFG
710 720 730 740 750
EIEECTVNLR DDGDSYGFIT YRYTCDAFAA LENGYTLRRS NETDFELYFC
760 770 780 790
GRKQFFKSNY ADLDTNSDDF DPASTKSKYD SLDFDSLLKE AQRSLRR
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:
EMBLi
GenBanki
DDBJi
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]
ENSMUST00000151104; ENSMUSP00000116566; ENSMUSG00000029167. [O70343-4]
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3F7DX-ray2.20B137-150[»]
ProteinModelPortaliO70343.
SMRiO70343. Positions 673-737.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202321. 12 interactions.
DIPiDIP-38447N.
IntActiO70343. 8 interactions.
STRINGi10090.ENSMUSP00000117040.

PTM databases

PhosphoSiteiO70343.

Proteomic databases

PaxDbiO70343.
PRIDEiO70343.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000132734; ENSMUSP00000117040; ENSMUSG00000029167. [O70343-1]
ENSMUST00000151104; ENSMUSP00000116566; ENSMUSG00000029167. [O70343-4]
GeneIDi19017.
KEGGimmu:19017.
UCSCiuc008xkc.2. mouse. [O70343-1]

Organism-specific databases

CTDi10891.
MGIiMGI:1342774. Ppargc1a.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_115781. Bmal1:Clock,Npas2 activates circadian gene expression.
REACT_118837. Rora activates gene expression.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
REACT_276725. RORA activates gene expression.
REACT_309805. Transcriptional regulation of white adipocyte differentiation.
REACT_321345. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_328033. Transcriptional activation of mitochondrial biogenesis.
REACT_344843. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_351159. Circadian Clock.

Miscellaneous databases

EvolutionaryTraceiO70343.
NextBioi295448.
PROiO70343.
SOURCEiSearch...

Gene expression databases

BgeeiO70343.
ExpressionAtlasiO70343. baseline and differential.
GenevisibleiO70343. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 MYBBP1A.
  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: July 22, 2015
This is version 141 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.