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Q9QYK2

- PRGC1_RAT

UniProt

Q9QYK2 - PRGC1_RAT

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Protein

Peroxisome proliferator-activated receptor gamma coactivator 1-alpha

Gene

Ppargc1a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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 (By similarity).By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. androgen metabolic process Source: RGD
  2. cellular response to fatty acid Source: RGD
  3. cellular response to hypoxia Source: RGD
  4. cellular response to nitrite Source: RGD
  5. cellular response to oxidative stress Source: UniProtKB
  6. cellular response to thyroid hormone stimulus Source: RGD
  7. cellular response to tumor necrosis factor Source: RGD
  8. circadian regulation of gene expression Source: UniProtKB
  9. flavone metabolic process Source: RGD
  10. galactose metabolic process Source: RGD
  11. mitochondrion organization Source: RGD
  12. negative regulation of glycolytic process Source: RGD
  13. negative regulation of neuron apoptotic process Source: UniProtKB
  14. negative regulation of neuron death Source: UniProtKB
  15. negative regulation of receptor activity Source: RGD
  16. negative regulation of smooth muscle cell migration Source: RGD
  17. neuron death Source: Ensembl
  18. positive regulation of ATP biosynthetic process Source: UniProtKB
  19. positive regulation of cellular metabolic process Source: RGD
  20. positive regulation of cellular respiration Source: Ensembl
  21. positive regulation of energy homeostasis Source: UniProtKB
  22. positive regulation of fatty acid oxidation Source: RGD
  23. positive regulation of mitochondrial DNA metabolic process Source: Ensembl
  24. positive regulation of mitochondrion organization Source: UniProtKB
  25. positive regulation of muscle tissue development Source: Ensembl
  26. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  27. positive regulation of smooth muscle cell proliferation Source: RGD
  28. positive regulation of transcription, DNA-templated Source: RGD
  29. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  30. regulation of circadian rhythm Source: UniProtKB
  31. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: RGD
  32. regulation of transcription, DNA-templated Source: UniProtKB
  33. respiratory electron transport chain Source: UniProtKB
  34. response to activity Source: RGD
  35. response to cold Source: RGD
  36. response to drug Source: RGD
  37. response to epinephrine Source: RGD
  38. response to hypoxia Source: RGD
  39. response to leucine Source: RGD
  40. response to muscle activity Source: UniProtKB
  41. response to norepinephrine Source: RGD
  42. response to nutrient levels Source: RGD
  43. response to organic cyclic compound Source: RGD
  44. response to starvation Source: RGD
  45. response to statin Source: RGD
  46. 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_196405. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_196408. PPARA activates gene expression.
REACT_196852. REV-ERBA represses gene expression.
REACT_196856. RORA activates circadian gene expression.
REACT_209077. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_216049. Transcriptional activation of mitochondrial biogenesis.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 14

Organism-specific databases

RGDi620925. Ppargc1a.

Subcellular locationi

Nucleus By similarity. NucleusPML body By similarity

GO - Cellular componenti

  1. cytosol Source: RGD
  2. nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 796796Peroxisome proliferator-activated receptor gamma coactivator 1-alphaPRO_0000081735Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771N6-acetyllysineBy similarity
Modified residuei144 – 1441N6-acetyllysineBy similarity
Modified residuei176 – 1761Phosphothreonine; by AMPKBy similarity
Modified residuei182 – 1821N6-acetyllysineBy similarity
Modified residuei252 – 2521N6-acetyllysineBy similarity
Modified residuei269 – 2691N6-acetyllysineBy similarity
Modified residuei276 – 2761N6-acetyllysineBy similarity
Modified residuei319 – 3191N6-acetyllysineBy similarity
Modified residuei345 – 3451N6-acetyllysineBy similarity
Modified residuei411 – 4111N6-acetyllysineBy similarity
Modified residuei440 – 4401N6-acetyllysineBy similarity
Modified residuei449 – 4491N6-acetyllysineBy similarity
Modified residuei537 – 5371Phosphoserine; by AMPKBy similarity
Modified residuei756 – 7561N6-acetyllysineBy similarity
Modified residuei777 – 7771N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylation by AMPK in skeletal muscle increases activation of its own promoter. Phosphorylated by CLK2.By similarity
Heavily acetylated by GCN5 and biologically inactive under conditions of high nutrients. Deacetylated by SIRT1 in low nutrients/high NAD conditions (By similarity).By similarity
Ubiquitinated. Ubiquitination by RNF34 induces proteasomal degradation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9QYK2.

PTM databases

PhosphoSiteiQ9QYK2.

Expressioni

Inductioni

Up-regulated in brown adipose tissue of diabetic fatty (fa/fa) rats. Exposure of fa/fa rats to cold resulted in a much smaller increase as compared to lean rats in which a 2.6 fold increase was seen. Leptin is required for normal basal and cold-stimulated expression in brown adipose tissue and hyperleptinemia rapidly up-regulates its expression. It is induced not only by cold exposure but also by prolonged low-intensity physical exercise in epitrochlearis muscle.2 Publications

Gene expression databases

GenevestigatoriQ9QYK2.

Interactioni

Subunit structurei

Homooligomer. 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. Interacts with RNF34 (via RING-type zinc finger).By similarity

Protein-protein interaction databases

IntActiQ9QYK2. 1 interaction.
STRINGi10116.ENSRNOP00000006071.

Structurei

3D structure databases

ProteinModelPortaliQ9QYK2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini675 – 75177RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni291 – 33747Interaction with PPARGBy similarityAdd
BLAST
Regioni348 – 796449Mediates interaction with RNF34By similarityAdd
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi564 – 59734Arg/Ser-richAdd
BLAST
Compositional biasi619 – 63113Arg/Ser-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG78353.
GeneTreeiENSGT00530000063196.
HOGENOMiHOG000037431.
HOVERGENiHBG053678.
InParanoidiQ9QYK2.
KOiK07202.
OMAiENGYTLR.
OrthoDBiEOG7S4X5H.
PhylomeDBiQ9QYK2.
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]

Sequencei

Sequence statusi: Complete.

Q9QYK2-1 [UniParc]FASTAAdd to Basket

« 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 TDGDVTTDNE ASPSSMPDGT PPPQEAEEPS LLKKLLLAPA
160 170 180 190 200
NTQLSYNECS GLSTQNHANH THRIRTNPAI VKTENSWSNK AKSICQQQKP
210 220 230 240 250
QRRPCSELLK YLTTNDDPPH TKPTENRNSS RDKCASKKKS HTQPQSQHAQ
260 270 280 290 300
AKPTTLSLPL TPESPNDPKG SPFENKTIER TLSVELSGTA GLTPPTTPPH
310 320 330 340 350
KANQDNPFKA SPKLKPSCKT VVPPPTKRAR YSECSGTQGS HSTKKGPEQS
360 370 380 390 400
ELYAQLSKSS VLSRGHEERK TKRPSLRLFG DHDYCQSVNS KTDILINISQ
410 420 430 440 450
ELQDSRQLDF KDASCDWQGH ICSSTDSSQC YLRETLEASK QVSPCSTRKQ
460 470 480 490 500
LQDQEIRAEL NKHFGHPSQA VFDDKVDKTS ELRDGNFSNE QFSKLPVFIN
510 520 530 540 550
SGLAMDGLFD DSEDENDKLS YPWDGTQSYS LFDVSPSCSS FNSPCRDSVS
560 570 580 590 600
PPKSLFSQRP QRMRSRSRSF SRHRSCSRSP YSRSRSRSPG SRSSSRSCYY
610 620 630 640 650
YESSHYRHRT HRNSPLYVRS RSRSPYSRRP RYDSYEANEH ERLKRDEYRR
660 670 680 690 700
EYEKRESERA KQRERQKQKA IEERRVIYVG KIRPDTTRTE LRDRFEVFGE
710 720 730 740 750
IEECTVNLRD DGDSYGFITY RYTCDAFAAL ENGYTLRRSN ETDFELYFCG
760 770 780 790
RKQFFKSNYA DLDSNSDDFD PASTKSKYDS LDFDSLLKEA QRSLRR
Length:796
Mass (Da):90,622
Last modified:May 1, 2000 - v1
Checksum:iCF30A35F95088240
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti427 – 4271S → L(PubMed:10913342)Curated
Sequence conflicti564 – 5641R → H(PubMed:10913342)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB025784 mRNA. Translation: BAA88982.1.
AY237127 mRNA. Translation: AAO89279.1.
PIRiJC7355.
RefSeqiNP_112637.1. NM_031347.1.
UniGeneiRn.19172.

Genome annotation databases

EnsembliENSRNOT00000006071; ENSRNOP00000006071; ENSRNOG00000004473.
GeneIDi83516.
KEGGirno:83516.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB025784 mRNA. Translation: BAA88982.1 .
AY237127 mRNA. Translation: AAO89279.1 .
PIRi JC7355.
RefSeqi NP_112637.1. NM_031347.1.
UniGenei Rn.19172.

3D structure databases

ProteinModelPortali Q9QYK2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9QYK2. 1 interaction.
STRINGi 10116.ENSRNOP00000006071.

PTM databases

PhosphoSitei Q9QYK2.

Proteomic databases

PaxDbi Q9QYK2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000006071 ; ENSRNOP00000006071 ; ENSRNOG00000004473 .
GeneIDi 83516.
KEGGi rno:83516.

Organism-specific databases

CTDi 10891.
RGDi 620925. Ppargc1a.

Phylogenomic databases

eggNOGi NOG78353.
GeneTreei ENSGT00530000063196.
HOGENOMi HOG000037431.
HOVERGENi HBG053678.
InParanoidi Q9QYK2.
KOi K07202.
OMAi ENGYTLR.
OrthoDBi EOG7S4X5H.
PhylomeDBi Q9QYK2.
TreeFami TF343068.

Enzyme and pathway databases

Reactomei REACT_196405. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_196408. PPARA activates gene expression.
REACT_196852. REV-ERBA represses gene expression.
REACT_196856. RORA activates circadian gene expression.
REACT_209077. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_216049. Transcriptional activation of mitochondrial biogenesis.

Miscellaneous databases

NextBioi 615978.
PROi Q9QYK2.

Gene expression databases

Genevestigatori Q9QYK2.

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. "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: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Strain: Zucker.
    Tissue: Heart.
  2. "cDNA cloning and mRNA analysis of PGC-1 in epitrochlearis muscle in swimming-exercised rats."
    Goto M., Terada S., Kato M., Katoh M., Yokozeki T., Tabata I., Shimokawa T.
    Biochem. Biophys. Res. Commun. 274:350-354(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
  3. "Rattus norvegicus PGC1 mRNA."
    Kofman A.V.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPRGC1_RAT
AccessioniPrimary (citable) accession number: Q9QYK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 109 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3