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Q9UBK2

- PRGC1_HUMAN

UniProt

Q9UBK2 - PRGC1_HUMAN

Protein

Peroxisome proliferator-activated receptor gamma coactivator 1-alpha

Gene

PPARGC1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. chromatin DNA binding Source: UniProtKB
    3. DNA binding Source: UniProtKB
    4. ligand-dependent nuclear receptor binding Source: UniProtKB
    5. ligand-dependent nuclear receptor transcription coactivator activity Source: BHF-UCL
    6. nucleotide binding Source: InterPro
    7. protein binding Source: IntAct
    8. RNA binding Source: UniProtKB
    9. RNA polymerase II transcription cofactor activity Source: UniProtKB
    10. sequence-specific DNA binding Source: UniProtKB
    11. transcription coactivator activity Source: UniProtKB
    12. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. androgen metabolic process Source: Ensembl
    2. androgen receptor signaling pathway Source: UniProtKB
    3. brown fat cell differentiation Source: UniProtKB
    4. cellular glucose homeostasis Source: UniProtKB
    5. cellular respiration Source: UniProtKB
    6. cellular response to fatty acid Source: Ensembl
    7. cellular response to hypoxia Source: Ensembl
    8. cellular response to nitrite Source: Ensembl
    9. cellular response to oxidative stress Source: UniProtKB
    10. cellular response to thyroid hormone stimulus Source: Ensembl
    11. cellular response to tumor necrosis factor Source: Ensembl
    12. circadian regulation of gene expression Source: UniProtKB
    13. digestion Source: UniProtKB
    14. fatty acid oxidation Source: UniProtKB
    15. flavone metabolic process Source: Ensembl
    16. galactose metabolic process Source: Ensembl
    17. gluconeogenesis Source: UniProtKB
    18. mitochondrion organization Source: UniProtKB
    19. mRNA processing Source: UniProtKB
    20. negative regulation of glycolytic process Source: Ensembl
    21. negative regulation of neuron apoptotic process Source: UniProtKB
    22. negative regulation of receptor activity Source: Ensembl
    23. neuron death Source: UniProtKB
    24. positive regulation of ATP biosynthetic process Source: UniProtKB
    25. positive regulation of cellular respiration Source: Ensembl
    26. positive regulation of energy homeostasis Source: UniProtKB
    27. positive regulation of fatty acid oxidation Source: UniProtKB
    28. positive regulation of gluconeogenesis Source: UniProtKB
    29. positive regulation of histone acetylation Source: UniProtKB
    30. positive regulation of mitochondrial DNA metabolic process Source: Ensembl
    31. positive regulation of mitochondrion organization Source: UniProtKB
    32. positive regulation of muscle tissue development Source: Ensembl
    33. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    34. positive regulation of smooth muscle cell proliferation Source: Ensembl
    35. positive regulation of transcription, DNA-templated Source: UniProtKB
    36. positive regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
    37. protein complex assembly Source: UniProtKB
    38. protein stabilization Source: UniProtKB
    39. regulation of cell death Source: UniProtKB
    40. regulation of circadian rhythm Source: UniProtKB
    41. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: Ensembl
    42. regulation of transcription, DNA-templated Source: UniProtKB
    43. respiratory electron transport chain Source: UniProtKB
    44. response to cold Source: Ensembl
    45. response to epinephrine Source: Ensembl
    46. response to leucine Source: Ensembl
    47. response to muscle activity Source: BHF-UCL
    48. response to norepinephrine Source: Ensembl
    49. response to starvation Source: UniProtKB
    50. response to statin Source: Ensembl
    51. RNA splicing Source: UniProtKB
    52. temperature homeostasis Source: UniProtKB
    53. transcription initiation from RNA polymerase II promoter Source: UniProtKB

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.

    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
    Alternative name(s):
    Ligand effect modulator 6
    Gene namesi
    Name:PPARGC1A
    Synonyms:LEM6, PGC1, PGC1A, PPARGC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:9237. PPARGC1A.

    Subcellular locationi

    Isoform 9 : Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. DNA-directed RNA polymerase II, core complex Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti803. Amyotrophic lateral sclerosis.
    PharmGKBiPA33558.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 798798Peroxisome proliferator-activated receptor gamma coactivator 1-alphaPRO_0000081732Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791N6-acetyllysineBy similarity
    Modified residuei146 – 1461N6-acetyllysineBy similarity
    Modified residuei178 – 1781Phosphothreonine; by AMPKBy similarity
    Modified residuei184 – 1841N6-acetyllysineBy similarity
    Modified residuei254 – 2541N6-acetyllysineBy similarity
    Modified residuei271 – 2711N6-acetyllysineBy similarity
    Modified residuei278 – 2781N6-acetyllysineBy similarity
    Modified residuei321 – 3211N6-acetyllysineBy similarity
    Modified residuei347 – 3471N6-acetyllysineBy similarity
    Modified residuei413 – 4131N6-acetyllysineBy similarity
    Modified residuei442 – 4421N6-acetyllysineBy similarity
    Modified residuei451 – 4511N6-acetyllysineBy similarity
    Modified residuei539 – 5391Phosphoserine; by AMPKBy similarity
    Modified residuei758 – 7581N6-acetyllysineBy similarity
    Modified residuei779 – 7791N6-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.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ9UBK2.
    PRIDEiQ9UBK2.

    PTM databases

    PhosphoSiteiQ9UBK2.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Inductioni

    Transcription is repressed by ZNF746 which binds to 'insulin response sequences' its promoter.1 Publication

    Gene expression databases

    ArrayExpressiQ9UBK2.
    BgeeiQ9UBK2.
    CleanExiHS_PPARGC1A.
    GenevestigatoriQ9UBK2.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ESRRGP625083EBI-765486,EBI-2834260
    LRPPRCP427042EBI-765486,EBI-1050853

    Protein-protein interaction databases

    BioGridi116097. 53 interactions.
    DIPiDIP-38449N.
    IntActiQ9UBK2. 8 interactions.
    MINTiMINT-6824612.
    STRINGi9606.ENSP00000264867.

    Structurei

    Secondary structure

    1
    798
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi143 – 1497
    Helixi208 – 2147

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ9UBK2.
    SMRiQ9UBK2. Positions 675-738.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UBK2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini677 – 75377RRMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni293 – 33947Interaction with PPARGAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi144 – 1485LXXLL motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi566 – 59934Arg/Ser-richAdd
    BLAST
    Compositional biasi621 – 63313Arg/Ser-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG78353.
    HOGENOMiHOG000037431.
    HOVERGENiHBG053678.
    InParanoidiQ9UBK2.
    KOiK07202.
    OMAiENGYTLR.
    OrthoDBiEOG7S4X5H.
    PhylomeDBiQ9UBK2.
    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 (9)i

    Sequence statusi: Complete.

    This entry describes 9 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: Q9UBK2-1) [UniParc]FASTAAdd to Basket

    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

    MAWDMCNQDS ESVWSDIECA ALVGEDQPLC PDLPELDLSE LDVNDLDTDS    50
    FLGGLKWCSD QSEIISNQYN NEPSNIFEKI DEENEANLLA VLTETLDSLP 100
    VDEDGLPSFD ALTDGDVTTD NEASPSSMPD GTPPPQEAEE PSLLKKLLLA 150
    PANTQLSYNE CSGLSTQNHA NHNHRIRTNP AIVKTENSWS NKAKSICQQQ 200
    KPQRRPCSEL LKYLTTNDDP PHTKPTENRN SSRDKCTSKK KSHTQSQSQH 250
    LQAKPTTLSL PLTPESPNDP KGSPFENKTI ERTLSVELSG TAGLTPPTTP 300
    PHKANQDNPF RASPKLKSSC KTVVPPPSKK PRYSESSGTQ GNNSTKKGPE 350
    QSELYAQLSK SSVLTGGHEE RKTKRPSLRL FGDHDYCQSI NSKTEILINI 400
    SQELQDSRQL ENKDVSSDWQ GQICSSTDSD QCYLRETLEA SKQVSPCSTR 450
    KQLQDQEIRA ELNKHFGHPS QAVFDDEADK TGELRDSDFS NEQFSKLPMF 500
    INSGLAMDGL FDDSEDESDK LSYPWDGTQS YSLFNVSPSC SSFNSPCRDS 550
    VSPPKSLFSQ RPQRMRSRSR SFSRHRSCSR SPYSRSRSRS PGSRSSSRSC 600
    YYYESSHYRH RTHRNSPLYV RSRSRSPYSR RPRYDSYEEY QHERLKREEY 650
    RREYEKRESE RAKQRERQRQ KAIEERRVIY VGKIRPDTTR TELRDRFEVF 700
    GEIEECTVNL RDDGDSYGFI TYRYTCDAFA ALENGYTLRR SNETDFELYF 750
    CGRKQFFKSN YADLDSNSDD FDPASTKSKY DSLDFDSLLK EAQRSLRR 798
    Length:798
    Mass (Da):91,027
    Last modified:May 1, 2000 - v1
    Checksum:i97DDD3643051A5F1
    GO
    Isoform NT-7a (identifier: Q9UBK2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         269-271: DPK → LFL
         272-798: Missing.

    Show »
    Length:271
    Mass (Da):30,031
    Checksum:i0F7BB8B4136DE6E3
    GO
    Isoform B5 (identifier: Q9UBK2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: MAWDMCNQDSESVWSDIE → MDETSPRLEEDWKKVLQREAGWQ

    Note: Produced by alternative promoter usage.

    Show »
    Length:803
    Mass (Da):91,713
    Checksum:i5AD73310B38C36D8
    GO
    Isoform B4 (identifier: Q9UBK2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: MAWDMCNQDSESVWSDIE → MDEGYF

    Note: Produced by alternative promoter usage.

    Show »
    Length:786
    Mass (Da):89,641
    Checksum:i61A006A08CD2862C
    GO
    Isoform B4-8a (identifier: Q9UBK2-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:289
    Mass (Da):31,772
    Checksum:i7551B9318C4F7BA9
    GO
    Isoform B5-NT (identifier: Q9UBK2-6) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:276
    Mass (Da):30,717
    Checksum:i6818E49B958E2F21
    GO
    Isoform B4-3ext (identifier: Q9UBK2-7) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:138
    Mass (Da):14,964
    Checksum:i913391C42BA4D8B2
    GO
    Isoform 8a (identifier: Q9UBK2-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         294-301: LTPPTTPP → VKTNLISK
         302-798: Missing.

    Show »
    Length:301
    Mass (Da):33,157
    Checksum:i31AACF20FC3B29F9
    GO
    Isoform 9 (identifier: Q9UBK2-9) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:671
    Mass (Da):77,139
    Checksum:iD84936587B7C36CF
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti482 – 4821G → S.1 Publication
    Corresponds to variant rs8192678 [ dbSNP | Ensembl ].
    VAR_018450
    Natural varianti612 – 6121T → M.
    Corresponds to variant rs3736265 [ dbSNP | Ensembl ].
    VAR_018451

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 127127Missing in isoform 9. 1 PublicationVSP_053770Add
    BLAST
    Alternative sequencei1 – 1818MAWDM…WSDIE → MDEGYF in isoform B4, isoform B4-8a and isoform B4-3ext. 1 PublicationVSP_053725Add
    BLAST
    Alternative sequencei1 – 1818MAWDM…WSDIE → MDETSPRLEEDWKKVLQREA GWQ in isoform B5 and isoform B5-NT. 1 PublicationVSP_053724Add
    BLAST
    Alternative sequencei144 – 1507LKKLLLA → VRTLPTV in isoform B4-3ext. 1 PublicationVSP_053726
    Alternative sequencei151 – 798648Missing in isoform B4-3ext. 1 PublicationVSP_053727Add
    BLAST
    Alternative sequencei269 – 2713DPK → LFL in isoform NT-7a and isoform B5-NT. 2 PublicationsVSP_047684
    Alternative sequencei272 – 798527Missing in isoform NT-7a and isoform B5-NT. 2 PublicationsVSP_047685Add
    BLAST
    Alternative sequencei294 – 3018LTPPTTPP → VKTNLISK in isoform B4-8a and isoform 8a. 2 PublicationsVSP_053728
    Alternative sequencei302 – 798497Missing in isoform B4-8a and isoform 8a. 2 PublicationsVSP_053729Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF108205
    , 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.
    CCDSiCCDS3429.1. [Q9UBK2-1]
    RefSeqiNP_037393.1. NM_013261.3. [Q9UBK2-1]
    XP_005248187.1. XM_005248130.1. [Q9UBK2-3]
    UniGeneiHs.527078.

    Genome annotation databases

    EnsembliENST00000264867; ENSP00000264867; ENSG00000109819. [Q9UBK2-1]
    ENST00000506055; ENSP00000423075; ENSG00000109819. [Q9UBK2-2]
    ENST00000513205; ENSP00000421632; ENSG00000109819. [Q9UBK2-8]
    GeneIDi10891.
    KEGGihsa:10891.
    UCSCiuc003gqs.3. human. [Q9UBK2-1]

    Polymorphism databases

    DMDMi47117335.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF108205
    , 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 .
    CCDSi CCDS3429.1. [Q9UBK2-1 ]
    RefSeqi NP_037393.1. NM_013261.3. [Q9UBK2-1 ]
    XP_005248187.1. XM_005248130.1. [Q9UBK2-3 ]
    UniGenei Hs.527078.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XB7 X-ray 2.50 P 205-216 [» ]
    3B1M X-ray 1.60 B 136-154 [» ]
    3CS8 X-ray 2.30 B 141-152 [» ]
    3D24 X-ray 2.11 B/D 198-219 [» ]
    3U9Q X-ray 1.52 B 142-150 [» ]
    3V9T X-ray 1.65 C 136-154 [» ]
    3V9V X-ray 1.60 C 136-154 [» ]
    ProteinModelPortali Q9UBK2.
    SMRi Q9UBK2. Positions 675-738.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116097. 53 interactions.
    DIPi DIP-38449N.
    IntActi Q9UBK2. 8 interactions.
    MINTi MINT-6824612.
    STRINGi 9606.ENSP00000264867.

    Chemistry

    ChEMBLi CHEMBL6116.

    PTM databases

    PhosphoSitei Q9UBK2.

    Polymorphism databases

    DMDMi 47117335.

    Proteomic databases

    PaxDbi Q9UBK2.
    PRIDEi Q9UBK2.

    Protocols and materials databases

    DNASUi 10891.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264867 ; ENSP00000264867 ; ENSG00000109819 . [Q9UBK2-1 ]
    ENST00000506055 ; ENSP00000423075 ; ENSG00000109819 . [Q9UBK2-2 ]
    ENST00000513205 ; ENSP00000421632 ; ENSG00000109819 . [Q9UBK2-8 ]
    GeneIDi 10891.
    KEGGi hsa:10891.
    UCSCi uc003gqs.3. human. [Q9UBK2-1 ]

    Organism-specific databases

    CTDi 10891.
    GeneCardsi GC04M023793.
    HGNCi HGNC:9237. PPARGC1A.
    MIMi 604517. gene.
    neXtProti NX_Q9UBK2.
    Orphaneti 803. Amyotrophic lateral sclerosis.
    PharmGKBi PA33558.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG78353.
    HOGENOMi HOG000037431.
    HOVERGENi HBG053678.
    InParanoidi Q9UBK2.
    KOi K07202.
    OMAi ENGYTLR.
    OrthoDBi EOG7S4X5H.
    PhylomeDBi Q9UBK2.
    TreeFami TF343068.

    Enzyme and pathway databases

    Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.

    Miscellaneous databases

    EvolutionaryTracei Q9UBK2.
    GeneWikii PPARGC1A.
    GenomeRNAii 10891.
    NextBioi 35479358.
    PROi Q9UBK2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBK2.
    Bgeei Q9UBK2.
    CleanExi HS_PPARGC1A.
    Genevestigatori Q9UBK2.

    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. "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.
      , 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.
      , 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. 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.

    Entry informationi

    Entry nameiPRGC1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBK2
    Secondary accession number(s): B7Z406
    , G8DM16, I3RTT5, I3RTT6, I3RTT7, I3RTT8, I3RTT9, Q3LIG1, Q4W5M7, Q9UN32
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3