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Protein Page:
PGC-1 alpha (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PGC-1 alpha a transcriptional coactivator for steroid receptors and nuclear receptors. Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor genes. Interacts with, and regulates the activities of, cAMP response element binding protein (CREB) and nuclear respiratory factors (NRFs). Regulates many genes involved in energy metabolism. Provides a direct link between external physiological stimuli and the regulation of mitochondrial biogenesis, and is a major factor that regulates muscle fiber type determination. 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. May be involved in controlling blood pressure, regulating cellular cholesterol homoeostasis, and the development of obesity. Its transcription is repressed by ZNF746 which binds to 'insulin response sequences' in its promoter. Heavily acetylated by GCN5 and biologically inactive under conditions of high nutrients. Deacetylated by SIRT1 in low nutrients/high NAD conditions. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor co-regulator; Transcription, coactivator/corepressor
Chromosomal Location of Human Ortholog: 4p15.1
Cellular Component: cell soma; DNA-directed RNA polymerase II, core complex; nucleoplasm; nucleus; PML body
Molecular Function: alpha-tubulin binding; androgen receptor binding; chromatin DNA binding; DNA binding; estrogen receptor binding; ligand-dependent nuclear receptor binding; ligand-dependent nuclear receptor transcription coactivator activity; nucleotide binding; peroxisome proliferator activated receptor binding; protein binding; RNA binding; sequence-specific DNA binding; transcription coactivator activity; transcription factor binding; ubiquitin protein ligase binding
Biological Process: aging; androgen metabolic process; androgen receptor signaling pathway; brown fat cell differentiation; cell glucose homeostasis; cellular respiration; cerebellum development; circadian regulation of gene expression; circadian rhythm; digestion; fatty acid oxidation; flavone metabolic process; forebrain development; galactose metabolic process; gluconeogenesis; mitochondrion degradation; mitochondrion organization and biogenesis; mRNA processing; negative regulation of glycolysis; negative regulation of neuron apoptosis; negative regulation of protein amino acid phosphorylation; negative regulation of smooth muscle cell migration; negative regulation of smooth muscle cell proliferation; organelle organization and biogenesis; positive regulation of fatty acid oxidation; positive regulation of gluconeogenesis; positive regulation of histone acetylation; positive regulation of smooth muscle cell proliferation; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription from RNA polymerase II promoter by pheromones; positive regulation of transcription, DNA-dependent; protein complex assembly; protein stabilization; regulation of circadian rhythm; regulation of transcription, DNA-dependent; response to cold; response to dietary excess; response to electrical stimulus involved in regulation of muscle adaptation; response to leucine; response to muscle activity; response to reactive oxygen species; response to starvation; RNA splicing; skeletal muscle atrophy; thermoregulation; transcription initiation from RNA polymerase II promoter
Reference #:  Q9UBK2 (UniProtKB)
Alt. Names/Synonyms: LEM6; Ligand effect modulator 6; ligand effect modulator-6; peroxisome proliferative activated receptor, gamma, coactivator 1, alpha; Peroxisome proliferator-activated receptor gamma coactivator 1-alpha; peroxisome proliferator-activated receptor gamma, coactivator 1 alpha; PGC-1(alpha); PGC-1-alpha; PGC-1v; PGC1; PGC1A; PPAR gamma coactivator variant form; PPAR gamma coactivator-1; PPAR-gamma coactivator 1-alpha; PPARGC-1-alpha; PPARGC1; PPARGC1A; PRGC1
Gene Symbols: PPARGC1A
Molecular weight: 91,027 Da
Basal Isoelectric point: 5.71  Predict pI for various phosphorylation states
CST Pathways:  AMPK Signaling  |  mTOR Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PGC-1 alpha

Protein Structure Not Found.


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Sites Implicated In
activity, inhibited: S571‑p
protein stabilization: T263‑p, S266‑p, T299‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 0 T178 NHNHRIRTNPAIVKT
1 0 K184 RTNPAIVKTENSWSN
1 0 S195 SWSNKAKSICQQQKP
0 1 K201 KSICQQQKPQRRPCs
0 2 S208‑p KPQRRPCsELLKYLT
0 1 K224 NDDPPHTKPTENRNS
0 1 S232 PTENRNSSRDKCTSK
2 0 S242 KCTSKKKSHTQsQSQ
0 1 S246‑p KKKSHTQsQSQHLQA
1 0 T257 HLQAKPTTLSLPLtP
2 0 T263‑p TTLSLPLtPEsPNDP
3 3 S266‑p SLPLtPEsPNDPKGs
0 2 S273‑p sPNDPKGsPFENKTI
1 2 S285‑p KTIERTLsVELSGTA
0 3 T295‑p LSGTAGLtPPTtPPH
2 2 T299‑p AGLtPPTtPPHKANQ
0 6 S313‑p QDNPFRAsPKLKSSC
0 1 S334 PSKKPRYSESSGTQG
0 1 S359 SELYAQLSkSSVLTG
0 1 K360‑ac ELYAQLSkSSVLTGG
0 1 S361 LYAQLSkSSVLTGGH
0 1 S362 YAQLSkSSVLTGGHE
0 1 T365 LSkSSVLTGGHEERK
0 1 G366 SkSSVLTGGHEERKT
0 1 S416‑p QLENKDVssDWQGQI
0 1 S417‑p LENKDVssDWQGQIC
0 1 S445 LEASKQVSPCSTRKQ
1 0 S539 SLFNVSPSCSSFNSP
2 0 S569 PQRMRSRSRsFSRHR
3 0 S571‑p RMRSRSRsFSRHRSC
1 0 S573 RSRSRsFSRHRSCSR
1 3 S616‑p RHRTHRNsPLYVRSR
0 1 Y634‑p PYSRRPRyDsYEEYQ
0 4 S636‑p SRRPRyDsYEEYQHE
0 2 S768‑p YADLDSNsDDFDPAS
0 4 S782‑p STKSKYDsLDFDsLL
0 1 S787‑p YDsLDFDsLLKEAQR
  mouse

 
T177‑p NHTHRIRtNPAIVkT
K183‑sm RtNPAIVkTENSWSN
S194‑p SWSNKAKsICQQQkP
K200‑ac KsICQQQkPQRRPCS
S207 kPQRRPCSELLKYLT
K223‑ac NDDPPHTkPTENRNS
S231‑p PTENRNSsRDKCASK
S241‑p KCASKKKsHTQPQSQ
P245 KKKsHTQPQSQHAQA
T256‑p HAQAKPTtLSLPLTP
T262 TtLSLPLTPEsPNDP
S265‑p SLPLTPEsPNDPKGs
S272‑p sPNDPKGsPFENKTI
S284‑p KTIERTLsVELSGTA
T294‑p LSGTAGLtPPTtPPH
T298‑p AGLtPPTtPPHKANQ
S312‑p QDNPFKAsPKLKPSC
S333‑gl PTKRARYsECSGTQG
S358‑p SELYAQLsKssGLsr
K359 ELYAQLsKssGLsrG
S360‑p LYAQLsKssGLsrGH
S361‑p YAQLsKssGLsrGHE
S364‑p LsKssGLsrGHEERK
R365‑m1 sKssGLsrGHEERKT
S415 QLDFKDASCDWQGHI
C416 LDFKDASCDWQGHIC
S444‑p LEASKQVsPCSTRKQ
S538‑p SLFDVSPsCSSFNSP
S568‑p PQRMRSRsRsFsRHR
S570‑p RMRSRsRsFsRHRSC
S572‑p RSRsRsFsRHRSCSR
S615‑p RHRTHRNsPLYVRSR
Y633 PYSRRPRYDSYEAYE
S635 SRRPRYDSYEAYEHE
S767 YADLDTNSDDFDPAS
S781 STKSKYDSLDFDSLL
S786 YDSLDFDSLLKEAQR
  rat

 
T176 NHTHRIRTNPAIVKT
K182 RTNPAIVKTENSWSN
S193 SWSNKAKSICQQQKP
K199 KSICQQQKPQRRPCS
S206 KPQRRPCSELLKYLT
K222 NDDPPHTKPTENRNS
S230 PTENRNSSRDKCASK
S240 KCASKKKSHTQPQSQ
P244 KKKSHTQPQSQHAQA
T255 HAQAKPTTLSLPLTP
T261 TTLSLPLTPESPNDP
S264 SLPLTPESPNDPKGS
S271 SPNDPKGSPFENKTI
S283 KTIERTLSVELSGTA
T293 LSGTAGLTPPTTPPH
T297 AGLTPPTTPPHKANQ
S311 QDNPFKASPKLKPSC
S332 PTKRARYSECSGTQG
S357 SELYAQLSKSSVLSR
K358 ELYAQLSKSSVLSRG
S359 LYAQLSKSSVLSRGH
S360 YAQLSKSSVLSRGHE
S363 LSKSSVLSRGHEERK
R364 SKSSVLSRGHEERKT
S414 QLDFKDASCDWQGHI
C415 LDFKDASCDWQGHIC
S443 LEASKQVSPCSTRKQ
S537 SLFDVSPSCSSFNSP
S567 PQRMRSRSRsFSRHR
S569‑p RMRSRSRsFSRHRSC
S571 RSRSRsFSRHRSCSR
S614 RHRTHRNSPLYVRSR
Y632 PYSRRPRYDSYEANE
S634 SRRPRYDSYEANEHE
S766 YADLDSNSDDFDPAS
S780 STKSKYDSLDFDSLL
S785 YDSLDFDSLLKEAQR
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