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Q9UBK2 (PRGC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
Alternative name(s):
Ligand effect modulator 6
Gene names
Name:PPARGC1A
Synonyms:LEM6, PGC1, PGC1A, PPARGC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length798 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. Ref.3 Ref.12 Ref.13 Ref.14

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.3 Ref.11

Subcellular location

Isoform 1: Nucleus Ref.3 Ref.4 Ref.5. NucleusPML body Ref.3 Ref.4 Ref.5.

Isoform B4: Nucleus Ref.3 Ref.4 Ref.5.

Isoform B4-8a: Cytoplasm. Nucleus Ref.3 Ref.4 Ref.5.

Isoform B5: Nucleus Ref.3 Ref.4 Ref.5. NucleusPML body Ref.3 Ref.4 Ref.5.

Isoform 9: Nucleus Ref.3 Ref.4 Ref.5.

Tissue specificity

Heart, skeletal muscle, liver and kidney. Expressed at lower levels in brain and pancreas and at very low levels in the intestine and white adipose tissue. In skeletal muscle, levels were lower in obese than in lean subjects and fasting induced a 2-fold increase in levels in the skeletal muscle in obese subjects. Ref.1 Ref.2 Ref.3

Induction

Transcription is repressed by ZNF746 which binds to 'insulin response sequences' its promoter. Ref.12 Ref.13

Post-translational modification

Phosphorylation by AMPK in skeletal muscle increases activation of its own promoter By similarity. 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. Ref.12

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

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

Traceable author statement PubMed 12588810. Source: UniProtKB

androgen metabolic process

Inferred from electronic annotation. Source: Ensembl

androgen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

brown fat cell differentiation

Traceable author statement PubMed 12588810. Source: UniProtKB

cellular glucose homeostasis

Non-traceable author statement PubMed 11854298. Source: UniProtKB

cellular respiration

Traceable author statement PubMed 11551810. Source: UniProtKB

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 sequence or structural similarity. Source: UniProtKB

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 sequence or structural similarity. Source: UniProtKB

digestion

Traceable author statement Ref.1. Source: UniProtKB

fatty acid oxidation

Non-traceable author statement PubMed 11854298. Source: UniProtKB

flavone metabolic process

Inferred from electronic annotation. Source: Ensembl

galactose metabolic process

Inferred from electronic annotation. Source: Ensembl

gluconeogenesis

Non-traceable author statement PubMed 11854298. Source: UniProtKB

mRNA processing

Traceable author statement PubMed 12588810. Source: UniProtKB

mitochondrion organization

Non-traceable author statement PubMed 11854298. Source: UniProtKB

negative regulation of glycolysis

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of receptor activity

Inferred from electronic annotation. Source: Ensembl

neuron death

Inferred from direct assay Ref.13. Source: UniProtKB

positive regulation of ATP biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cellular respiration

Inferred from electronic annotation. Source: Ensembl

positive regulation of energy homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fatty acid oxidation

Traceable author statement PubMed 12588810. Source: UniProtKB

positive regulation of gluconeogenesis

Traceable author statement PubMed 12588810. Source: UniProtKB

positive regulation of histone acetylation

Traceable author statement PubMed 14636573. Source: UniProtKB

positive regulation of mitochondrial DNA metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitochondrion organization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of muscle tissue development

Inferred from electronic annotation. Source: Ensembl

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 sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Non-traceable author statement PubMed 15572661. Source: UniProtKB

protein complex assembly

Traceable author statement PubMed 14636573. Source: UniProtKB

protein stabilization

Traceable author statement PubMed 14636573. Source: UniProtKB

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

Inferred from electronic annotation. Source: Ensembl

regulation of cell death

Inferred from direct assay Ref.13. Source: UniProtKB

regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay Ref.14. Source: UniProtKB

respiratory electron transport chain

Inferred from sequence or structural similarity. Source: UniProtKB

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 sequence or structural similarity. Source: BHF-UCL

response to norepinephrine

Inferred from electronic annotation. Source: Ensembl

response to starvation

Non-traceable author statement PubMed 11854298. Source: UniProtKB

response to statin

Inferred from electronic annotation. Source: Ensembl

temperature homeostasis

Traceable author statement PubMed 1258810. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Traceable author statement PubMed 14636573. Source: UniProtKB

   Cellular_componentDNA-directed RNA polymerase II, core complex

Traceable author statement PubMed 12588810. Source: UniProtKB

PML 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 Ref.14. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

RNA binding

Traceable author statement PubMed 12588810. Source: UniProtKB

RNA polymerase II transcription cofactor activity

Traceable author statement PubMed 14636573. Source: UniProtKB

androgen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

chromatin DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

ligand-dependent nuclear receptor binding

Inferred from physical interaction PubMed 18798693. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from direct assay PubMed 16488887. Source: BHF-UCL

nucleotide binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding

Inferred from direct assay Ref.14. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.13. Source: UniProtKB

transcription factor binding

Traceable author statement PubMed 12588810. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ESRRGP625083EBI-765486,EBI-2834260
LRPPRCP427042EBI-765486,EBI-1050853

Alternative products

This entry describes 9 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UBK2-1)

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 NT-7a (identifier: Q9UBK2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     269-271: DPK → LFL
     272-798: Missing.
Isoform B5 (identifier: Q9UBK2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MAWDMCNQDSESVWSDIE → MDETSPRLEEDWKKVLQREAGWQ
Note: Produced by alternative promoter usage.
Isoform B4 (identifier: Q9UBK2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MAWDMCNQDSESVWSDIE → MDEGYF
Note: Produced by alternative promoter usage.
Isoform B4-8a (identifier: Q9UBK2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MAWDMCNQDSESVWSDIE → MDEGYF
     294-301: LTPPTTPP → VKTNLISK
     302-798: Missing.
Note: Produced by alternative promoter usage.
Isoform B5-NT (identifier: Q9UBK2-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MAWDMCNQDSESVWSDIE → MDETSPRLEEDWKKVLQREAGWQ
     269-271: DPK → LFL
     272-798: Missing.
Note: Produced by alternative promoter usage.
Isoform B4-3ext (identifier: Q9UBK2-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MAWDMCNQDSESVWSDIE → MDEGYF
     144-150: LKKLLLA → VRTLPTV
     151-798: Missing.
Note: Produced by alternative promoter usage.
Isoform 8a (identifier: Q9UBK2-8)

The sequence of this isoform differs from the canonical sequence as follows:
     294-301: LTPPTTPP → VKTNLISK
     302-798: Missing.
Isoform 9 (identifier: Q9UBK2-9)

Also known as: L-PGG-1alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     1-127: Missing.
Note: Produced by alternative promoter usage. May be involved in gluconeogenesis, liver-specific.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 798798Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
PRO_0000081732

Regions

Domain677 – 75377RRM
Region293 – 33947Interaction with PPARG
Motif144 – 1485LXXLL motif
Compositional bias566 – 59934Arg/Ser-rich
Compositional bias621 – 63313Arg/Ser-rich

Amino acid modifications

Modified residue791N6-acetyllysine By similarity
Modified residue1461N6-acetyllysine By similarity
Modified residue1781Phosphothreonine; by AMPK By similarity
Modified residue1841N6-acetyllysine By similarity
Modified residue2541N6-acetyllysine By similarity
Modified residue2711N6-acetyllysine By similarity
Modified residue2781N6-acetyllysine By similarity
Modified residue3211N6-acetyllysine By similarity
Modified residue3471N6-acetyllysine By similarity
Modified residue4131N6-acetyllysine By similarity
Modified residue4421N6-acetyllysine By similarity
Modified residue4511N6-acetyllysine By similarity
Modified residue5391Phosphoserine; by AMPK By similarity
Modified residue7581N6-acetyllysine By similarity
Modified residue7791N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 127127Missing in isoform 9.
VSP_053770
Alternative sequence1 – 1818MAWDM…WSDIE → MDEGYF in isoform B4, isoform B4-8a and isoform B4-3ext.
VSP_053725
Alternative sequence1 – 1818MAWDM…WSDIE → MDETSPRLEEDWKKVLQREA GWQ in isoform B5 and isoform B5-NT.
VSP_053724
Alternative sequence144 – 1507LKKLLLA → VRTLPTV in isoform B4-3ext.
VSP_053726
Alternative sequence151 – 798648Missing in isoform B4-3ext.
VSP_053727
Alternative sequence269 – 2713DPK → LFL in isoform NT-7a and isoform B5-NT.
VSP_047684
Alternative sequence272 – 798527Missing in isoform NT-7a and isoform B5-NT.
VSP_047685
Alternative sequence294 – 3018LTPPTTPP → VKTNLISK in isoform B4-8a and isoform 8a.
VSP_053728
Alternative sequence302 – 798497Missing in isoform B4-8a and isoform 8a.
VSP_053729
Natural variant4821G → S. Ref.2
Corresponds to variant rs8192678 [ dbSNP | Ensembl ].
VAR_018450
Natural variant6121T → M.
Corresponds to variant rs3736265 [ dbSNP | Ensembl ].
VAR_018451

Secondary structure

..... 798
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 97DDD3643051A5F1

FASTA79891,027
        10         20         30         40         50         60 
MAWDMCNQDS ESVWSDIECA ALVGEDQPLC PDLPELDLSE LDVNDLDTDS FLGGLKWCSD 

        70         80         90        100        110        120 
QSEIISNQYN NEPSNIFEKI DEENEANLLA VLTETLDSLP VDEDGLPSFD ALTDGDVTTD 

       130        140        150        160        170        180 
NEASPSSMPD GTPPPQEAEE PSLLKKLLLA PANTQLSYNE CSGLSTQNHA NHNHRIRTNP 

       190        200        210        220        230        240 
AIVKTENSWS NKAKSICQQQ KPQRRPCSEL LKYLTTNDDP PHTKPTENRN SSRDKCTSKK 

       250        260        270        280        290        300 
KSHTQSQSQH LQAKPTTLSL PLTPESPNDP KGSPFENKTI ERTLSVELSG TAGLTPPTTP 

       310        320        330        340        350        360 
PHKANQDNPF RASPKLKSSC KTVVPPPSKK PRYSESSGTQ GNNSTKKGPE QSELYAQLSK 

       370        380        390        400        410        420 
SSVLTGGHEE RKTKRPSLRL FGDHDYCQSI NSKTEILINI SQELQDSRQL ENKDVSSDWQ 

       430        440        450        460        470        480 
GQICSSTDSD QCYLRETLEA SKQVSPCSTR KQLQDQEIRA ELNKHFGHPS QAVFDDEADK 

       490        500        510        520        530        540 
TGELRDSDFS NEQFSKLPMF INSGLAMDGL FDDSEDESDK LSYPWDGTQS YSLFNVSPSC 

       550        560        570        580        590        600 
SSFNSPCRDS VSPPKSLFSQ RPQRMRSRSR SFSRHRSCSR SPYSRSRSRS PGSRSSSRSC 

       610        620        630        640        650        660 
YYYESSHYRH RTHRNSPLYV RSRSRSPYSR RPRYDSYEEY QHERLKREEY RREYEKRESE 

       670        680        690        700        710        720 
RAKQRERQRQ KAIEERRVIY VGKIRPDTTR TELRDRFEVF GEIEECTVNL RDDGDSYGFI 

       730        740        750        760        770        780 
TYRYTCDAFA ALENGYTLRR SNETDFELYF CGRKQFFKSN YADLDSNSDD FDPASTKSKY 

       790 
DSLDFDSLLK EAQRSLRR 

« Hide

Isoform NT-7a [UniParc].

Checksum: 0F7BB8B4136DE6E3
Show »

FASTA27130,031
Isoform B5 [UniParc].

Checksum: 5AD73310B38C36D8
Show »

FASTA80391,713
Isoform B4 [UniParc].

Checksum: 61A006A08CD2862C
Show »

FASTA78689,641
Isoform B4-8a [UniParc].

Checksum: 7551B9318C4F7BA9
Show »

FASTA28931,772
Isoform B5-NT [UniParc].

Checksum: 6818E49B958E2F21
Show »

FASTA27630,717
Isoform B4-3ext [UniParc].

Checksum: 913391C42BA4D8B2
Show »

FASTA13814,964
Isoform 8a [UniParc].

Checksum: 31AACF20FC3B29F9
Show »

FASTA30133,157
Isoform 9 (L-PGG-1alpha) [UniParc].

Checksum: D84936587B7C36CF
Show »

FASTA67177,139

References

« Hide 'large scale' references
[1]"Human peroxisome proliferator activated receptor gamma coactivator 1 (PPARGC1) gene: cDNA sequence, genomic organization, chromosomal localization, and tissue expression."
Esterbauer H., Oberkofler H., Krempler F., Patsch W.
Genomics 62:98-102(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"Cloning and mRNA tissue distribution of human PPARgamma coactivator-1."
Larrouy D., Vidal H., Andreelli F., Laville M., Langin D.
Int. J. Obes. Relat. Metab. Disord. 23:1327-1332(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT SER-482.
Tissue: Skeletal muscle.
[3]"A tissue-specific coactivator of steroid receptors, identified in a functional genetic screen."
Knutti D., Kaul A., Kralli A.
Mol. Cell. Biol. 20:2411-2422(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Characterization of novel peroxisome proliferator-activated receptor gamma coactivator-1alpha (PGC-1alpha) isoform in human liver."
Felder T.K., Soyal S.M., Oberkofler H., Hahne P., Auer S., Weiss R., Gadermaier G., Miller K., Krempler F., Esterbauer H., Patsch W.
J. Biol. Chem. 286:42923-42936(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9), SUBCELLULAR LOCATION (ISOFORM 9).
Tissue: Liver.
[5]"A greatly extended PPARGC1A genomic locus encodes several new brain-specific isoforms and influences Huntington disease age of onset."
Soyal S.M., Felder T.K., Auer S., Hahne P., Oberkofler H., Witting A., Paulmichl M., Landwehrmeyer G.B., Weydt P., Patsch W.
Hum. Mol. Genet. 21:3461-3473(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B4; B4-3EXT; B4-8A; B5 AND B5-NT), ALTERNATIVE PROMOTER USAGE, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
Tissue: Brain.
[6]"Isoform of PGC-1 generated by alternative splicing."
Endo H.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NT-7A), ALTERNATIVE SPLICING.
Tissue: Skeletal muscle.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8A).
[8]Rieder M.J., Johanson E.J., da Ponte S.H., Stanaway I.B., Ahearn M.O., Bertucci C.B., Wong M.W., Yi Q., Nickerson D.A.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"Defects in energy homeostasis in Leigh syndrome French Canadian variant through PGC-1alpha/LRP130 complex."
Cooper M.P., Qu L., Rohas L.M., Lin J., Yang W., Erdjument-Bromage H., Tempst P., Spiegelman B.M.
Genes Dev. 20:2996-3009(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRPPRC.
[12]"Nutrient-dependent regulation of PGC-1alpha's acetylation state and metabolic function through the enzymatic activities of Sirt1/GCN5."
Dominy J.E. Jr., Lee Y., Gerhart-Hines Z., Puigserver P.
Biochim. Biophys. Acta 1804:1676-1683(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, REGULATION BY ACETYLATION.
[13]"PARIS (ZNF746) repression of PGC-1alpha contributes to neurodegeneration in Parkinson's disease."
Shin J.H., Ko H.S., Kang H., Lee Y., Lee Y.I., Pletinkova O., Troconso J.C., Dawson V.L., Dawson T.M.
Cell 144:689-702(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[14]"Peroxisome proliferator-activated receptor gamma coactivator 1 (PGC-1)- and estrogen-related receptor (ERR)-induced regulator in muscle 1 (Perm1) is a tissue-specific regulator of oxidative capacity in skeletal muscle cells."
Cho Y., Hazen B.C., Russell A.P., Kralli A.
J. Biol. Chem. 288:25207-25218(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF108205 expand/collapse EMBL AC list , AF108193, AF108194, AF108195, AF108196, AF108197, AF108198, AF108199, AF108200, AF108201, AF108202, AF108203, AF108204 Genomic DNA. Translation: AAF19083.1.
AF106698 mRNA. Translation: AAF18573.1.
AF159714 mRNA. Translation: AAD51615.1.
AF186379 mRNA. Translation: AAD56250.1.
HQ695733 mRNA. Translation: ADW77180.1.
JQ772116 mRNA. Translation: AFK29753.1.
JQ772117 mRNA. Translation: AFK29754.1.
JQ772118 mRNA. Translation: AFK29755.1.
JQ772119 mRNA. Translation: AFK29756.1.
JQ772120 mRNA. Translation: AFK29757.1.
AB061325 mRNA. Translation: BAE46508.1.
EU280319 Genomic DNA. Translation: ABX44665.1.
AK296591 mRNA. Translation: BAH12392.1.
AC092834 Genomic DNA. Translation: AAY41058.1.
AC097508 Genomic DNA. No translation available.
CH471069 Genomic DNA. Translation: EAW92811.1.
RefSeqNP_037393.1. NM_013261.3.
XP_005248187.1. XM_005248130.1.
UniGeneHs.527078.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XB7X-ray2.50P205-216[»]
3B1MX-ray1.60B136-154[»]
3CS8X-ray2.30B141-152[»]
3D24X-ray2.11B/D198-219[»]
3U9QX-ray1.52B142-150[»]
3V9TX-ray1.65C136-154[»]
3V9VX-ray1.60C136-154[»]
ProteinModelPortalQ9UBK2.
SMRQ9UBK2. Positions 675-738.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116097. 51 interactions.
DIPDIP-38449N.
IntActQ9UBK2. 7 interactions.
MINTMINT-6824612.
STRING9606.ENSP00000264867.

Chemistry

ChEMBLCHEMBL6116.

PTM databases

PhosphoSiteQ9UBK2.

Polymorphism databases

DMDM47117335.

Proteomic databases

PaxDbQ9UBK2.
PRIDEQ9UBK2.

Protocols and materials databases

DNASU10891.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264867; ENSP00000264867; ENSG00000109819. [Q9UBK2-1]
ENST00000506055; ENSP00000423075; ENSG00000109819. [Q9UBK2-2]
ENST00000513205; ENSP00000421632; ENSG00000109819. [Q9UBK2-8]
GeneID10891.
KEGGhsa:10891.
UCSCuc003gqs.3. human. [Q9UBK2-1]

Organism-specific databases

CTD10891.
GeneCardsGC04M023793.
HGNCHGNC:9237. PPARGC1A.
MIM604517. gene.
neXtProtNX_Q9UBK2.
Orphanet803. Amyotrophic lateral sclerosis.
PharmGKBPA33558.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG78353.
HOGENOMHOG000037431.
HOVERGENHBG053678.
InParanoidQ9UBK2.
KOK07202.
OMAENGYTLR.
OrthoDBEOG7S4X5H.
PhylomeDBQ9UBK2.
TreeFamTF343068.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_24941. Circadian Clock.

Gene expression databases

ArrayExpressQ9UBK2.
BgeeQ9UBK2.
CleanExHS_PPARGC1A.
GenevestigatorQ9UBK2.

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

EvolutionaryTraceQ9UBK2.
GeneWikiPPARGC1A.
GenomeRNAi10891.
NextBio35479358.
PROQ9UBK2.
SOURCESearch...

Entry information

Entry namePRGC1_HUMAN
AccessionPrimary (citable) accession number: Q9UBK2
Secondary accession number(s): B7Z406 expand/collapse secondary AC list , G8DM16, I3RTT5, I3RTT6, I3RTT7, I3RTT8, I3RTT9, Q3LIG1, Q4W5M7, Q9UN32
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM