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Q9UBK2

- PRGC1_HUMAN

UniProt

Q9UBK2 - PRGC1_HUMAN

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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

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. RNA binding Source: UniProtKB
  8. RNA polymerase II transcription cofactor activity Source: UniProtKB
  9. sequence-specific DNA binding Source: UniProtKB
  10. transcription coactivator activity Source: UniProtKB
  11. transcription factor binding Source: UniProtKB
  12. ubiquitin protein ligase 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 neuron death Source: UniProtKB
  23. negative regulation of receptor activity Source: Ensembl
  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 circadian rhythm Source: UniProtKB
  40. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: Ensembl
  41. regulation of transcription, DNA-templated Source: UniProtKB
  42. respiratory electron transport chain Source: UniProtKB
  43. response to cold Source: Ensembl
  44. response to epinephrine Source: Ensembl
  45. response to leucine Source: Ensembl
  46. response to muscle activity Source: BHF-UCL
  47. response to norepinephrine Source: Ensembl
  48. response to starvation Source: UniProtKB
  49. response to statin Source: Ensembl
  50. RNA splicing Source: UniProtKB
  51. temperature homeostasis Source: UniProtKB
  52. transcription initiation from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

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
Complete GO annotation...

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.
Ubiquitinated. Ubiquitination by RNF34 induces proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UBK2.
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

BgeeiQ9UBK2.
CleanExiHS_PPARGC1A.
ExpressionAtlasiQ9UBK2. baseline and differential.
GenevestigatoriQ9UBK2.

Interactioni

Subunit structurei

Homooligomer. Interacts with MYBBP1A; inhibits MYBBP1A transcriptional activation (By similarity). Interacts with PRDM16, LPIN1 and PML (By similarity). Interacts (via LXXLL motif) with RORA and RORC (via AF-2 motif); activates RORA and RORC transcriptional activation (By similarity). Interacts with LRPPRC. Interacts with RNF34 (via RING-type zinc finger).By similarity3 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 – 1497Combined sources
Helixi208 – 2147Combined sources

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[»]
4QJRX-ray2.40B139-152[»]
4QK4X-ray2.81B139-152[»]
ProteinModelPortaliQ9UBK2.
SMRiQ9UBK2. Positions 677-738.
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
Regioni350 – 798449Mediates interaction with RNF341 PublicationAdd
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.
GeneTreeiENSGT00530000063196.
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) [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

        10         20         30         40         50
MAWDMCNQDS ESVWSDIECA ALVGEDQPLC PDLPELDLSE LDVNDLDTDS
60 70 80 90 100
FLGGLKWCSD QSEIISNQYN NEPSNIFEKI DEENEANLLA VLTETLDSLP
110 120 130 140 150
VDEDGLPSFD ALTDGDVTTD NEASPSSMPD GTPPPQEAEE PSLLKKLLLA
160 170 180 190 200
PANTQLSYNE CSGLSTQNHA NHNHRIRTNP AIVKTENSWS NKAKSICQQQ
210 220 230 240 250
KPQRRPCSEL LKYLTTNDDP PHTKPTENRN SSRDKCTSKK KSHTQSQSQH
260 270 280 290 300
LQAKPTTLSL PLTPESPNDP KGSPFENKTI ERTLSVELSG TAGLTPPTTP
310 320 330 340 350
PHKANQDNPF RASPKLKSSC KTVVPPPSKK PRYSESSGTQ GNNSTKKGPE
360 370 380 390 400
QSELYAQLSK SSVLTGGHEE RKTKRPSLRL FGDHDYCQSI NSKTEILINI
410 420 430 440 450
SQELQDSRQL ENKDVSSDWQ GQICSSTDSD QCYLRETLEA SKQVSPCSTR
460 470 480 490 500
KQLQDQEIRA ELNKHFGHPS QAVFDDEADK TGELRDSDFS NEQFSKLPMF
510 520 530 540 550
INSGLAMDGL FDDSEDESDK LSYPWDGTQS YSLFNVSPSC SSFNSPCRDS
560 570 580 590 600
VSPPKSLFSQ RPQRMRSRSR SFSRHRSCSR SPYSRSRSRS PGSRSSSRSC
610 620 630 640 650
YYYESSHYRH RTHRNSPLYV RSRSRSPYSR RPRYDSYEEY QHERLKREEY
660 670 680 690 700
RREYEKRESE RAKQRERQRQ KAIEERRVIY VGKIRPDTTR TELRDRFEVF
710 720 730 740 750
GEIEECTVNL RDDGDSYGFI TYRYTCDAFA ALENGYTLRR SNETDFELYF
760 770 780 790
CGRKQFFKSN YADLDSNSDD FDPASTKSKY DSLDFDSLLK EAQRSLRR
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]
ENST00000613098; ENSP00000481498; ENSG00000109819. [Q9UBK2-9]
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 [» ]
4QJR X-ray 2.40 B 139-152 [» ]
4QK4 X-ray 2.81 B 139-152 [» ]
ProteinModelPortali Q9UBK2.
SMRi Q9UBK2. Positions 677-738.
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

MaxQBi Q9UBK2.
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 ]
ENST00000613098 ; ENSP00000481498 ; ENSG00000109819 . [Q9UBK2-9 ]
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.
GeneTreei ENSGT00530000063196.
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

Bgeei Q9UBK2.
CleanExi HS_PPARGC1A.
ExpressionAtlasi Q9UBK2. baseline and differential.
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

« Hide 'large scale' publications
  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. "RNF34 is a cold-regulated E3 ubiquitin ligase for PGC-1alpha and modulates brown fat cell metabolism."
    Wei P., Pan D., Mao C., Wang Y.X.
    Mol. Cell. Biol. 32:266-275(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY RNF34, INTERACTION WITH RNF34.
  15. "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 29, 2014
This is version 132 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