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

Overview
PPAR-gamma a transcription factor, member of the nuclear hormone receptor superfamily. Receptor for hypolipidemic drugs and fatty acids. Preferentially expressed in adipocytes as well as in vascular smooth muscle cells and macrophage. Regulator of adipogenesis and lipid metabolism, modulates insulin sensitivity, cell proliferation and inflammation. Phosphorylated and inhibited by MAP kinase. Heterodimerizes with the retinoid X receptor. Interacts with NCOA6 coactivator, leading to a strong increase in transcription of target genes. Two splice-variant isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor; DNA binding protein
Chromosomal Location of Human Ortholog: 3p25
Cellular Component: nucleoplasm; perinuclear region of cytoplasm; cytosol; nucleus
Molecular Function: ligand-dependent nuclear receptor activity; transcription activator binding; zinc ion binding; drug binding; alpha-actinin binding; protein phosphatase binding; retinoid X receptor binding; arachidonic acid binding; protein binding; enzyme binding; ligand-dependent nuclear receptor transcription coactivator activity; DNA binding; prostaglandin receptor activity; sequence-specific DNA binding; steroid hormone receptor activity; estrogen receptor binding; chromatin binding; transcription factor activity
Biological Process: positive regulation of transcription, DNA-dependent; negative regulation of collagen biosynthetic process; heart development; cell maturation; rhythmic process; lipid homeostasis; glucose homeostasis; response to lipid; response to vitamin A; response to caffeine; positive regulation of oligodendrocyte differentiation; placenta development; long-chain fatty acid transport; organ regeneration; cell fate commitment; monocyte differentiation; negative regulation of acute inflammatory response; regulation of circadian rhythm; response to starvation; negative regulation of telomerase activity; cellular response to insulin stimulus; lipoprotein transport; response to estrogen stimulus; response to mechanical stimulus; brown fat cell differentiation; positive regulation of fat cell differentiation; positive regulation of transcription factor activity; steroid hormone mediated signaling; positive regulation of transcription from RNA polymerase II promoter; fatty acid oxidation; negative regulation of transcription, DNA-dependent; positive regulation of phagocytosis, engulfment; negative regulation of smooth muscle cell proliferation; low-density lipoprotein receptor biosynthetic process; negative regulation of transcription from RNA polymerase II promoter; signal transduction; epithelial cell differentiation; regulation of blood pressure; response to nutrient; caspase activation; transcription initiation from RNA polymerase II promoter; response to retinoic acid; G-protein coupled receptor protein signaling pathway; response to low density lipoprotein stimulus; positive regulation of fatty acid oxidation; white fat cell differentiation; innate immune response; gene expression; response to cold; negative regulation of cell growth; lipid metabolic process
Disease: Obesity; Lipodystrophy, Familial Partial, Type 3; Carotid Intimal Medial Thickness 1; Diabetes Mellitus, Noninsulin-dependent
Reference #:  P37231 (UniProtKB)
Alt. Names/Synonyms: CIMT1; GLM1; NR1C3; Nuclear receptor subfamily 1 group C member 3; peroxisome proliferative activated receptor gamma; Peroxisome proliferator-activated receptor gamma; peroxisome proliferator-activated receptor gamma 1; PPAR gamma; PPAR-gamma; PPARG; PPARG1; PPARG2; PPARgamma
Gene Symbols: PPARG
Molecular weight: 57,620 Da
Basal Isoelectric point: 5.61  Predict pI for various phosphorylation states
CST Pathways:  Growth And Differentiation Control by MAPKs  |  mTOR Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PPAR-gamma

Protein Structure Not Found.


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Sites Implicated In
cell differentiation, altered: S112‑p
cell growth, altered: S112‑p
transcription, altered: S112‑p
transcription, inhibited: S112‑p
protein degradation: S112‑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

► Hide Isoforms
 
1 0 S46 WPTNFGISSVDLSVM
1 0 S51 GISSVDLSVMEDHSH
2 0 K63 HSHSFDIKPFTTVDF
1 0 Y78-p SSISTPHyEDIPFTR
1 0 K94 DPVVADYKyDLKLQE
0 1 Y95-p PVVADYKyDLKLQEy
1 0 K98 ADYKyDLKLQEyQSA
1 1 Y102-p yDLKLQEyQSAIkVE
9 0 K107-sm QEyQSAIkVEPAsPP
18 2 S112-p AIkVEPAsPPYYSEK
1 1 S133 PHEEPSNSLMAIECR
0 1 Y173 TIRLKLIYDRCDLNC
1 0 K184-ub DLNCRIHkkSRNKCQ
1 0 K185-ub LNCRIHkkSRNKCQY
1 1 K268 ARAILTGKTTDKsPF
5 2 S273-p TGKTTDKsPFVIYDM
1 1 K293 GEDKIKFKHITPLQE
1 1 T296 KIKFKHITPLQEQSK
0 1 S317 FQGCQFRSVEAVQEI
3 0 K395-sm FGDFMEPkFEFAVKF
1 0 K462 ESSQLFAKLLQKMTD
  PPAR-gamma iso2  
S18 WPTNFGISSVDLSVM
S23 GISSVDLSVMEDHSH
K35 HSHSFDIKPFTTVDF
Y50 SSISTPHYEDIPFTR
K66 DPVVADYKYDLKLQE
Y67 PVVADYKYDLKLQEY
K70 ADYKYDLKLQEYQSA
Y74 YDLKLQEYQSAIkVE
K79-sm QEYQSAIkVEPASPP
S84 AIkVEPASPPYYSEK
S105 PHEEPSNSLMAIECR
Y145 TIRLKLIYDRCDLNC
K156 DLNCRIHKKSRNKCQ
K157 LNCRIHKKSRNKCQY
K240 ARAILTGKTTDKSPF
S245 TGKTTDKSPFVIYDM
K265 GEDKIKFKHITPLQE
T268 KIKFKHITPLQEQSK
S289 FQGCQFRSVEAVQEI
K367-sm FGDFMEPkFEFAVKF
K434 ESSQLFAKLLQKMTD
  PPAR-gamma iso3  
S18 WPTNFGISSVDLSVM
S23 GISSVDLSVMEDHSH
K35 HSHSFDIKPFTTVDF
Y50 SSISTPHYEDIPFTR
K66 DPVVADYKYDLKLQE
Y67 PVVADYKYDLKLQEY
K70 ADYKYDLKLQEYQSA
Y74 YDLKLQEYQSAIKVE
K79 QEYQSAIKVEPAsPP
S84-p AIKVEPAsPPYYSEK
S105 PHEEPSNSLMAIECR
Y145 TIRLKLIYDRCDLNC
K156 DLNCRIHKKSRNKCQ
K157 LNCRIHKKSRNKCQY
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  mouse

► Hide Isoforms
 
S46 WPTNFGISSVDLSVM
S51 GISSVDLSVMEDHSH
K63-sm HSHSFDIkPFTTVDF
Y78 SSISAPHYEDIPFTR
K94 DPMVADYKYDLKLQE
Y95 PMVADYKYDLKLQEY
K98 ADYKYDLKLQEYQSA
Y102 YDLKLQEYQSAIkVE
K107-sm QEYQSAIkVEPAsPP
S112-p AIkVEPAsPPYYSEK
S133-p PHEEPSNsLMAIECR
Y173-p TIRLKLIyDRCDLNC
K184 DLNCRIHKKSRNKCQ
K185 LNCRIHKKSRNKCQY
K268-ac ARAILTGkTTDKsPF
S273-p TGkTTDKsPFVIYDM
K293-ac GEDKIKFkHItPLQE
T296-p KIKFkHItPLQEQSK
S317-p FQGCQFRsVEAVQEI
K395 FGDFMEPKFEFAVKF
K462 ESSQLFAKVLQKMTD
  PPAR-gamma iso2  
S16-p WPTNFGIsSVDLsVM
S21-p GIsSVDLsVMEDHSH
K33-sm HSHSFDIkPFTTVDF
Y48 SSISAPHYEDIPFTR
K64-sm DPMVADYkYDLkLQE
Y65 PMVADYkYDLkLQEY
K68-sm ADYkYDLkLQEYQSA
Y72 YDLkLQEYQSAIkVE
K77-sm QEYQSAIkVEPAsPP
S82-p AIkVEPAsPPYYSEK
S103 PHEEPSNSLMAIECR
Y143 TIRLKLIYDRCDLNC
K154 DLNCRIHKKSRNKCQ
K155 LNCRIHKKSRNKCQY
K238 ARAILTGKTTDKSPF
S243 TGKTTDKSPFVIYDM
K263 GEDKIKFKHITPLQE
T266 KIKFKHITPLQEQSK
S287 FQGCQFRSVEAVQEI
K365-sm FGDFMEPkFEFAVKF
K432-ub ESSQLFAkVLQKMTD
  rat

 
S46 WPTNFGISSVDLSVM
S51 GISSVDLSVMDDHSH
K63 HSHSFDIKPFTTVDF
Y78 SSISAPHYEDIPFTR
K94 DPMVADYKYDLKLQE
Y95 PMVADYKYDLKLQEY
K98 ADYKYDLKLQEYQSA
Y102 YDLKLQEYQSAIKVE
K107 QEYQSAIKVEPASPP
S112 AIKVEPASPPYYSEK
S133 PHEEPSNSLMAIECR
Y173 TIRLKLIYDRCDLNC
K184 DLNCRIHKKSRNKCQ
K185 LNCRIHKKSRNKCQY
K268 ARAILTGKTTDKSPF
S273 TGKTTDKSPFVIYDM
K293 GEDKIKFKHITPLQE
T296 KIKFKHITPLQEQSK
S317 FQGCQFRSVEAVQEI
K395 FGDFMEPKFEFAVKF
K462 ESSQLFAKVLQKMTD
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