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O70343 (PRGC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ppargc1a
Synonyms:Pgc1, Pgc1a, Ppargc1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length797 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.8 Ref.12

Subunit structure

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. Ref.7 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15

Subcellular location

Nucleus. NucleusPML body Ref.2 Ref.15.

Tissue specificity

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. Ref.1 Ref.2 Ref.12

Induction

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. Ref.1 Ref.2 Ref.6 Ref.12 Ref.16

Post-translational modification

Phosphorylation by AMPK in skeletal muscle increases activation of its own promoter. Phosphorylated by CLK2. Ref.11 Ref.14

Heavily acetylated by GCN5 and biologically inactive under conditions of high nutrients. Deacetylated by SIRT1 in low nutrients/high NAD conditions. Ref.8

Disruption phenotype

Mice show abnormal diurnal rhythms of activity, body temperature and metabolic rate. Ref.12

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
   LigandRNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to fatty acid

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to nitrite

Inferred from electronic annotation. Source: Ensembl

cellular response to oxidative stress

Inferred from mutant phenotype PubMed 20566846. Source: MGI

cellular response to thyroid hormone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

circadian regulation of gene expression

Inferred from direct assay Ref.12. Source: UniProtKB

flavone metabolic process

Inferred from electronic annotation. Source: Ensembl

galactose metabolic process

Inferred from electronic annotation. Source: Ensembl

mitochondrion organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of glycolytic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 20566846. Source: MGI

negative regulation of receptor activity

Inferred from electronic annotation. Source: Ensembl

neuron death

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ATP biosynthetic process

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

positive regulation of cellular respiration

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

positive regulation of energy homeostasis

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

positive regulation of fatty acid oxidation

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitochondrial DNA metabolic process

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

positive regulation of mitochondrion organization

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

positive regulation of muscle tissue development

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 19651776. Source: BHF-UCL

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 21106753. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.7PubMed 15681609. Source: MGI

regulation of N-methyl-D-aspartate selective glutamate receptor activity

Inferred from electronic annotation. Source: Ensembl

regulation of cell death

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of circadian rhythm

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

respiratory electron transport chain

Inferred from direct assay Ref.7. Source: MGI

response to cold

Inferred from electronic annotation. Source: Ensembl

response to epinephrine

Inferred from electronic annotation. Source: Ensembl

response to leucine

Inferred from electronic annotation. Source: Ensembl

response to muscle activity

Inferred from mutant phenotype PubMed 21106753. Source: BHF-UCL

response to norepinephrine

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

response to statin

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17952069. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15681609. Source: MGI

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin DNA binding

Inferred from direct assay PubMed 17952069. Source: MGI

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

nucleotide binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.9Ref.12Ref.10Ref.13. Source: UniProtKB

sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.12. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 19345188. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: O70343-1)

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.
Isoform 2 (identifier: O70343-2)

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.
Isoform 3 (identifier: O70343-3)

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.
Isoform 4 (identifier: O70343-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 797797Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
PRO_0000081733

Regions

Domain676 – 75277RRM
Region292 – 33847Interaction with PPARG By similarity
Motif142 – 1465LXXLL motif
Compositional bias565 – 59834Arg/Ser-rich
Compositional bias620 – 63213Arg/Ser-rich

Amino acid modifications

Modified residue771N6-acetyllysine Ref.8
Modified residue1441N6-acetyllysine Ref.8
Modified residue1771Phosphothreonine; by AMPK Ref.11
Modified residue1831N6-acetyllysine Ref.8
Modified residue2531N6-acetyllysine Ref.8
Modified residue2701N6-acetyllysine Ref.8
Modified residue2771N6-acetyllysine Ref.8
Modified residue3201N6-acetyllysine Ref.8
Modified residue3461N6-acetyllysine Ref.8
Modified residue4121N6-acetyllysine Ref.8
Modified residue4411N6-acetyllysine Ref.8
Modified residue4501N6-acetyllysine Ref.8
Modified residue5381Phosphoserine; by AMPK Ref.11
Modified residue7571N6-acetyllysine Ref.8
Modified residue7781N6-acetyllysine Ref.8

Natural variations

Alternative sequence2 – 1615AWDMC…WSDIE → LGLSSMDSILK in isoform 2 and isoform 4.
VSP_053275
Alternative sequence2 – 1615AWDMC…WSDIE → LL in isoform 3.
VSP_053276
Alternative sequence108 – 274167Missing in isoform 2 and isoform 3.
VSP_053277
Alternative sequence268 – 500233DPKGS…LPVFI → LFL in isoform 4.
VSP_053279
Alternative sequence501 – 797297Missing in isoform 4.
VSP_053281
Alternative sequence545 – 680136PCRDS…RVIYV → LNVIIT in isoform 2 and isoform 3.
VSP_053278
Alternative sequence681 – 797117Missing in isoform 2 and isoform 3.
VSP_053280

Experimental info

Mutagenesis142 – 1465LKKLL → AKKAA: Strongly reduces coactivation of RORA activity. Ref.12
Mutagenesis1771T → A: Abolishes AMPK-mediated phosphorylation; when associated with A-538. Ref.11
Mutagenesis5381S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-177. Ref.11
Sequence conflict5871S → L in AAH66868. Ref.5
Sequence conflict6291R → C in AAH66868. Ref.5

Secondary structure

... 797
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PGC-1a1) [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: AE73EE2B3A622B05

FASTA79790,588
        10         20         30         40         50         60 
MAWDMCSQDS VWSDIECAAL VGEDQPLCPD LPELDLSELD VNDLDTDSFL GGLKWCSDQS 

        70         80         90        100        110        120 
EIISNQYNNE PANIFEKIDE ENEANLLAVL TETLDSLPVD EDGLPSFDAL TDGAVTTDNE 

       130        140        150        160        170        180 
ASPSSMPDGT PPPQEAEEPS LLKKLLLAPA NTQLSYNECS GLSTQNHAAN HTHRIRTNPA 

       190        200        210        220        230        240 
IVKTENSWSN KAKSICQQQK PQRRPCSELL KYLTTNDDPP HTKPTENRNS SRDKCASKKK 

       250        260        270        280        290        300 
SHTQPQSQHA QAKPTTLSLP LTPESPNDPK GSPFENKTIE RTLSVELSGT AGLTPPTTPP 

       310        320        330        340        350        360 
HKANQDNPFK ASPKLKPSCK TVVPPPTKRA RYSECSGTQG SHSTKKGPEQ SELYAQLSKS 

       370        380        390        400        410        420 
SGLSRGHEER KTKRPSLRLF GDHDYCQSLN SKTDILINIS QELQDSRQLD FKDASCDWQG 

       430        440        450        460        470        480 
HICSSTDSGQ CYLRETLEAS KQVSPCSTRK QLQDQEIRAE LNKHFGHPCQ AVFDDKSDKT 

       490        500        510        520        530        540 
SELRDGDFSN EQFSKLPVFI NSGLAMDGLF DDSEDESDKL SYPWDGTQPY SLFDVSPSCS 

       550        560        570        580        590        600 
SFNSPCRDSV SPPKSLFSQR PQRMRSRSRS FSRHRSCSRS PYSRSRSRSP GSRSSSRSCY 

       610        620        630        640        650        660 
YYESSHYRHR THRNSPLYVR SRSRSPYSRR PRYDSYEAYE HERLKRDEYR KEHEKRESER 

       670        680        690        700        710        720 
AKQRERQKQK AIEERRVIYV GKIRPDTTRT ELRDRFEVFG EIEECTVNLR DDGDSYGFIT 

       730        740        750        760        770        780 
YRYTCDAFAA LENGYTLRRS NETDFELYFC GRKQFFKSNY ADLDTNSDDF DPASTKSKYD 

       790 
SLDFDSLLKE AQRSLRR 

« Hide

Isoform 2 (PGC-1a2) [UniParc].

Checksum: F9FC43F94A209D82
Show »

FASTA37941,921
Isoform 3 (PGC-1a3) [UniParc].

Checksum: AA98B0425EE8F122
Show »

FASTA37041,002
Isoform 4 (PGC-1a4) [UniParc].

Checksum: 317BEC86DF2E9DFB
Show »

FASTA26629,115

References

« Hide 'large scale' references
[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]"A PGC-1alpha isoform induced by resistance training regulates skeletal muscle hypertrophy."
Ruas J.L., White J.P., Rao R.R., Kleiner S., Brannan K.T., Harrison B.C., Greene N.P., Wu J., Estall J.L., Irving B.A., Lanza I.R., Rasbach K.A., Okutsu M., Nair K.S., Yan Z., Leinwand L.A., Spiegelman B.M.
Cell 151:1319-1331(2012) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Transcriptional control of brown fat determination by PRDM16."
Seale P., Kajimura S., Yang W., Chin S., Rohas L.M., Uldry M., Tavernier G., Langin D., Spiegelman B.M.
Cell Metab. 6:38-54(2007) [PubMed] [Europe PMC] [Abstract]
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]"A metabolic prosurvival role for PML in breast cancer."
Carracedo A., Weiss D., Leliaert A.K., Bhasin M., de Boer V.C., Laurent G., Adams A.C., Sundvall M., Song S.J., Ito K., Finley L.S., Egia A., Libermann T., Gerhart-Hines Z., Puigserver P., Haigis M.C., Maratos-Flier E., Richardson A.L., Schafer Z.T., Pandolfi P.P.
J. Clin. Invest. 122:3088-3100(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PML.
[16]"A PGC1-alpha-dependent myokine that drives brown-fat-like development of white fat and thermogenesis."
Bostrom P., Wu J., Jedrychowski M.P., Korde A., Ye L., Lo J.C., Rasbach K.A., Bostrom E.A., Choi J.H., Long J.Z., Kajimura S., Zingaretti M.C., Vind B.F., Tu H., Cinti S., Hojlund K., Gygi S.P., Spiegelman B.M.
Nature 481:463-468(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS19282.1. [O70343-1]
RefSeqNP_032930.1. NM_008904.2. [O70343-1]
UniGeneMm.259072.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3F7DX-ray2.20B137-150[»]
ProteinModelPortalO70343.
SMRO70343. Positions 674-774.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202321. 11 interactions.
DIPDIP-38447N.
IntActO70343. 7 interactions.

PTM databases

PhosphoSiteO70343.

Proteomic databases

PaxDbO70343.
PRIDEO70343.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000132734; ENSMUSP00000117040; ENSMUSG00000029167. [O70343-1]
GeneID19017.
KEGGmmu:19017.
UCSCuc008xkc.2. mouse. [O70343-1]

Organism-specific databases

CTD10891.
MGIMGI:1342774. Ppargc1a.

Phylogenomic databases

eggNOGNOG78353.
GeneTreeENSGT00530000063196.
HOGENOMHOG000037431.
HOVERGENHBG053678.
InParanoidO70343.
KOK07202.
OMAENGYTLR.
OrthoDBEOG7S4X5H.
PhylomeDBO70343.
TreeFamTF343068.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.
REACT_200794. Mus musculus biological processes.
REACT_224594. Organelle biogenesis and maintenance.

Gene expression databases

ArrayExpressO70343.
BgeeO70343.
GenevestigatorO70343.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO70343.
NextBio295448.
PROO70343.
SOURCESearch...

Entry information

Entry namePRGC1_MOUSE
AccessionPrimary (citable) accession number: O70343
Secondary accession number(s): L0AM20 expand/collapse secondary AC list , L0AN96, L0APB0, Q3UP72
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot