Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peroxisome proliferator-activated receptor gamma

Gene

PPARG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated proinflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of ARNTL/BMAL1 in the blood vessels (By similarity).By similarity4 Publications
(Microbial infection) Upon treatment with M.tuberculosis or its lipoprotein LpqH, phosphorylation of MAPK p38 and IL-6 production are modulated, probably via this protein.1 Publication

Caution

Enzyme regulationi

PDPK1 activates its transcriptional activity independently of its kinase activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei317Synthetic agonist9 Publications1
Binding sitei351Synthetic agonist9 Publications1
Binding sitei477Synthetic agonist9 Publications1
Binding sitei501Synthetic agonist9 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi136 – 210Nuclear receptorPROSITE-ProRule annotationAdd BLAST75
Zinc fingeri139 – 159NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri176 – 198NR C4-typePROSITE-ProRule annotationAdd BLAST23

GO - Molecular functioni

  • activating transcription factor binding Source: BHF-UCL
  • alpha-actinin binding Source: UniProtKB
  • arachidonic acid binding Source: BHF-UCL
  • chromatin binding Source: UniProtKB
  • core promoter sequence-specific DNA binding Source: UniProtKB
  • DBD domain binding Source: CAFA
  • DNA binding Source: UniProtKB
  • DNA binding transcription factor activity Source: BHF-UCL
  • double-stranded DNA binding Source: CAFA
  • drug binding Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • estrogen receptor binding Source: Ensembl
  • identical protein binding Source: IntAct
  • LBD domain binding Source: CAFA
  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • nuclear receptor activity Source: BHF-UCL
  • peptide binding Source: CAFA
  • prostaglandin receptor activity Source: BHF-UCL
  • protein C-terminus binding Source: CAFA
  • protein heterodimerization activity Source: CAFA
  • protein phosphatase binding Source: Ensembl
  • protein self-association Source: CAFA
  • retinoid X receptor binding Source: BHF-UCL
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
  • steroid hormone receptor activity Source: InterPro
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: BHF-UCL
  • zinc ion binding Source: CAFA

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  • animal organ regeneration Source: Ensembl
  • cell fate commitment Source: BHF-UCL
  • cell maturation Source: BHF-UCL
  • cellular response to hyperoxia Source: Ensembl
  • cellular response to insulin stimulus Source: BHF-UCL
  • cellular response to low-density lipoprotein particle stimulus Source: BHF-UCL
  • cellular response to prostaglandin E stimulus Source: Ensembl
  • cellular response to retinoic acid Source: Ensembl
  • cellular response to vitamin E Source: Ensembl
  • epithelial cell differentiation Source: BHF-UCL
  • fatty acid oxidation Source: Ensembl
  • glucose homeostasis Source: BHF-UCL
  • heart development Source: Ensembl
  • innate immune response Source: BHF-UCL
  • lipid homeostasis Source: BHF-UCL
  • lipid metabolic process Source: ProtInc
  • lipoprotein transport Source: BHF-UCL
  • long-chain fatty acid transport Source: BHF-UCL
  • low-density lipoprotein particle receptor biosynthetic process Source: BHF-UCL
  • macrophage derived foam cell differentiation Source: UniProtKB
  • monocyte differentiation Source: BHF-UCL
  • negative regulation of acute inflammatory response Source: Ensembl
  • negative regulation of angiogenesis Source: BHF-UCL
  • negative regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • negative regulation of cell growth Source: Ensembl
  • negative regulation of cholesterol storage Source: BHF-UCL
  • negative regulation of collagen biosynthetic process Source: Ensembl
  • negative regulation of gene silencing by miRNA Source: BHF-UCL
  • negative regulation of interferon-gamma-mediated signaling pathway Source: BHF-UCL
  • negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  • negative regulation of pancreatic stellate cell proliferation Source: Ensembl
  • negative regulation of receptor biosynthetic process Source: BHF-UCL
  • negative regulation of sequestering of triglyceride Source: BHF-UCL
  • negative regulation of smooth muscle cell proliferation Source: BHF-UCL
  • negative regulation of telomerase activity Source: Ensembl
  • negative regulation of transcription, DNA-templated Source: BHF-UCL
  • negative regulation of transcription by RNA polymerase II Source: BHF-UCL
  • negative regulation of vascular endothelial cell proliferation Source: BHF-UCL
  • negative regulation of vascular smooth muscle cell proliferation Source: BHF-UCL
  • peroxisome proliferator activated receptor signaling pathway Source: BHF-UCL
  • placenta development Source: BHF-UCL
  • positive regulation of DNA binding Source: CAFA
  • positive regulation of DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of fat cell differentiation Source: HGNC
  • positive regulation of fatty acid oxidation Source: Ensembl
  • positive regulation of oligodendrocyte differentiation Source: Ensembl
  • positive regulation of phagocytosis, engulfment Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: CAFA
  • positive regulation of transcription by RNA polymerase II Source: UniProtKB
  • positive regulation of vascular associated smooth muscle cell apoptotic process Source: BHF-UCL
  • pri-miRNA transcription by RNA polymerase II Source: BHF-UCL
  • regulation of blood pressure Source: BHF-UCL
  • regulation of cholesterol transporter activity Source: BHF-UCL
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of transcription involved in cell fate commitment Source: UniProtKB
  • response to caffeine Source: Ensembl
  • response to cold Source: Ensembl
  • response to estrogen Source: Ensembl
  • response to immobilization stress Source: Ensembl
  • response to lipid Source: BHF-UCL
  • response to mechanical stimulus Source: Ensembl
  • response to metformin Source: Ensembl
  • response to nutrient Source: ProtInc
  • response to retinoic acid Source: UniProtKB
  • response to starvation Source: Ensembl
  • response to vitamin A Source: Ensembl
  • rhythmic process Source: UniProtKB-KW
  • signal transduction Source: BHF-UCL
  • transcription initiation from RNA polymerase II promoter Source: Reactome
  • white fat cell differentiation Source: HGNC

Keywordsi

Molecular functionActivator, DNA-binding, Receptor
Biological processBiological rhythms, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-1989781 PPARA activates gene expression
R-HSA-381340 Transcriptional regulation of white adipocyte differentiation
R-HSA-383280 Nuclear Receptor transcription pathway
R-HSA-8943724 Regulation of PTEN gene transcription
SignaLinkiP37231
SIGNORiP37231

Chemistry databases

SwissLipidsiSLP:000000396

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisome proliferator-activated receptor gamma
Short name:
PPAR-gamma
Alternative name(s):
Nuclear receptor subfamily 1 group C member 3
Gene namesi
Name:PPARG
Synonyms:NR1C3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000132170.19
HGNCiHGNC:9236 PPARG
MIMi601487 gene
neXtProtiNX_P37231

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in PPARG can lead to type 2 insulin-resistant diabetes and hyptertension. PPARG mutations may be associated with colon cancer.1 Publication
Obesity (OBESITY)1 Publication
Disease susceptibility may be associated with variations affecting the gene represented in this entry.
Disease descriptionA condition characterized by an increase of body weight beyond the limitation of skeletal and physical requirements, as the result of excessive accumulation of body fat.
See also OMIM:601665
Lipodystrophy, familial partial, 3 (FPLD3)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of lipodystrophy characterized by marked loss of subcutaneous fat from the extremities. Facial adipose tissue may be increased, decreased or normal. Affected individuals show an increased preponderance of insulin resistance, diabetes mellitus and dyslipidemia.
See also OMIM:604367
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_022700388F → L in FPLD3. 1 PublicationCorresponds to variant dbSNP:rs72551363Ensembl.1
Natural variantiVAR_022701425R → C in FPLD3. 1 PublicationCorresponds to variant dbSNP:rs72551364Ensembl.1
Glioma 1 (GLM1)1 Publication
Disease susceptibility may be associated with variations affecting the gene represented in this entry. Polymorphic PPARG alleles have been found to be significantly over-represented among a cohort of American patients with sporadic glioblastoma multiforme suggesting a possible contribution to disease susceptibility.
Disease descriptionGliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.
See also OMIM:137800

Keywords - Diseasei

Diabetes mellitus, Disease mutation, Obesity

Organism-specific databases

DisGeNETi5468
MalaCardsiPPARG
MIMi137800 phenotype
601665 phenotype
604367 phenotype
606641 phenotype
609338 phenotype
OpenTargetsiENSG00000132170
Orphaneti528 Berardinelli-Seip congenital lipodystrophy
79083 Familial partial lipodystrophy associated with PPARG mutations
251579 Giant cell glioblastoma
251576 Gliosarcoma
PharmGKBiPA281

Chemistry databases

ChEMBLiCHEMBL235
DrugBankiDB08760 (2S)-2-(4-chlorophenoxy)-3-phenylpropanoic acid
DB07842 (2S)-2-(4-ethylphenoxy)-3-phenylpropanoic acid
DB08121 (2S)-2-(biphenyl-4-yloxy)-3-phenylpropanoic acid
DB07675 (2S)-2-ETHOXY-3-{4-[2-(10H-PHENOXAZIN-10-YL)ETHOXY]PHENYL}PROPANOIC ACID
DB04270 (S)-3-(4-(2-Carbazol-9-Yl-Ethoxy)-Phenyl)-2-Ethoxy-Propionic Acid
DB07863 2-chloro-5-nitro-N-phenylbenzamide
DB04689 2-{5-[3-(6-BENZOYL-1-PROPYLNAPHTHALEN-2-YLOXY)PROPOXY]INDOL-1-YL}ETHANOIC ACID
DB07053 2-{5-[3-(7-PROPYL-3-TRIFLUOROMETHYLBENZO[D]ISOXAZOL-6-YLOXY)PROPOXY]INDOL-1-YL}ETHANOIC ACID
DB07723 3-(5-methoxy-1H-indol-3-yl)propanoic acid
DB08302 3-[5-(2-nitropent-1-en-1-yl)furan-2-yl]benzoic acid
DB08560 3-FLUORO-N-[1-(4-FLUOROPHENYL)-3-(2-THIENYL)-1H-PYRAZOL-5-YL]BENZENESULFONAMIDE
DB07724 3-{5-methoxy-1-[(4-methoxyphenyl)sulfonyl]-1H-indol-3-yl}propanoic acid
DB08915 Aleglitazar
DB01014 Balsalazide
DB01393 Bezafibrate
DB05854 CLX-0921
DB07509 difluoro(5-{2-[(5-octyl-1H-pyrrol-2-yl-kappaN)methylidene]-2H-pyrrol-5-yl-kappaN}pentanoato)boron
DB05187 GFT505
DB01067 Glipizide
DB01050 Ibuprofen
DB00159 Icosapent
DB00328 Indomethacin
DB00244 Mesalazine
DB01252 Mitiglinide
DB00731 Nateglinide
DB01132 Pioglitazone
DB04971 Reglixane
DB00912 Repaglinide
DB00412 Rosiglitazone
DB00795 Sulfasalazine
DB05490 T131
DB00966 Telmisartan
DB00197 Troglitazone
GuidetoPHARMACOLOGYi595

Polymorphism and mutation databases

BioMutaiPPARG
DMDMi13432234

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000534921 – 505Peroxisome proliferator-activated receptor gammaAdd BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi84O-linked (GlcNAc) threonineBy similarity1
Modified residuei112PhosphoserineCombined sources1

Post-translational modificationi

O-GlcNAcylation at Thr-84 reduces transcriptional activity in adipocytes.By similarity
Phosphorylated in basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated form may be inactive and dephosphorylation at Ser-112 induces adipogenic activity (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP37231
MaxQBiP37231
PaxDbiP37231
PeptideAtlasiP37231
PRIDEiP37231

PTM databases

iPTMnetiP37231
PhosphoSitePlusiP37231

Expressioni

Tissue specificityi

Highest expression in adipose tissue. Lower in skeletal muscle, spleen, heart and liver. Also detectable in placenta, lung and ovary.1 Publication

Inductioni

(Microbial infection) Expression increases when incubated with M.tuberculosis or its lipoprotein LpqH; induction is TLR2-dependent (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000132170
ExpressionAtlasiP37231 baseline and differential
GenevisibleiP37231 HS

Organism-specific databases

HPAiCAB004282
HPA051239
HPA063663

Interactioni

Subunit structurei

Interacts with FOXO1 (acetylated form) (By similarity). Heterodimer with other nuclear receptors, such as RXRA. The heterodimer with the retinoic acid receptor RXRA is called adipocyte-specific transcription factor ARF6. Interacts with NCOA6 coactivator, leading to a strong increase in transcription of target genes. Interacts with coactivator PPARBP, leading to a mild increase in transcription of target genes. Interacts with NOCA7 in a ligand-inducible manner. Interacts with NCOA1 and NCOA2 LXXLL motifs. Interacts with ASXL1, ASXL2, DNTTIP2, FAM120B, MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and TGFB1I1. Interacts (when activated by agonist) with PPP5C. Interacts with HELZ2 and THRAP3; the interaction stimulates the transcriptional activity of PPARG. Interacts with PER2, the interaction is ligand dependent and blocks PPARG recruitment to target promoters. Interacts with NOCT. Interacts with ACTN4. Interacts (when in the liganded conformation) with GPS2 (By similarity).By similarity21 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • activating transcription factor binding Source: BHF-UCL
  • alpha-actinin binding Source: UniProtKB
  • DBD domain binding Source: CAFA
  • enzyme binding Source: UniProtKB
  • estrogen receptor binding Source: Ensembl
  • identical protein binding Source: IntAct
  • LBD domain binding Source: CAFA
  • protein C-terminus binding Source: CAFA
  • protein heterodimerization activity Source: CAFA
  • protein phosphatase binding Source: Ensembl
  • protein self-association Source: CAFA
  • retinoid X receptor binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111464138 interactors.
DIPiDIP-35528N
ELMiP37231
IntActiP37231 37 interactors.
MINTiP37231
STRINGi9606.ENSP00000287820

Chemistry databases

BindingDBiP37231

Structurei

Secondary structure

1505
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi140 – 142Combined sources3
Beta strandi148 – 150Combined sources3
Beta strandi151 – 154Combined sources4
Helixi157 – 167Combined sources11
Turni168 – 170Combined sources3
Helixi186 – 188Combined sources3
Helixi191 – 200Combined sources10
Helixi205 – 207Combined sources3
Turni214 – 217Combined sources4
Helixi218 – 220Combined sources3
Turni222 – 226Combined sources5
Turni228 – 231Combined sources4
Helixi237 – 253Combined sources17
Helixi258 – 265Combined sources8
Beta strandi266 – 268Combined sources3
Beta strandi269 – 271Combined sources3
Beta strandi275 – 277Combined sources3
Helixi280 – 286Combined sources7
Turni287 – 289Combined sources3
Beta strandi290 – 292Combined sources3
Beta strandi294 – 296Combined sources3
Helixi298 – 300Combined sources3
Beta strandi301 – 303Combined sources3
Helixi305 – 329Combined sources25
Helixi334 – 336Combined sources3
Helixi339 – 360Combined sources22
Beta strandi361 – 363Combined sources3
Beta strandi366 – 369Combined sources4
Turni370 – 373Combined sources4
Beta strandi374 – 377Combined sources4
Helixi378 – 383Combined sources6
Turni385 – 387Combined sources3
Helixi388 – 390Combined sources3
Helixi393 – 403Combined sources11
Helixi409 – 420Combined sources12
Beta strandi423 – 425Combined sources3
Helixi431 – 452Combined sources22
Beta strandi454 – 456Combined sources3
Helixi459 – 486Combined sources28
Beta strandi488 – 490Combined sources3
Helixi491 – 493Combined sources3
Helixi495 – 501Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FM6X-ray2.10D/X234-505[»]
1FM9X-ray2.10D234-505[»]
1I7IX-ray2.35A/B225-505[»]
1K74X-ray2.30D234-505[»]
1KNUX-ray2.50A/B232-505[»]
1NYXX-ray2.65A/B230-505[»]
1PRGX-ray2.20A/B235-504[»]
1RDTX-ray2.40D235-505[»]
1WM0X-ray2.90X232-505[»]
1ZEOX-ray2.50A/B231-505[»]
1ZGYX-ray1.80A234-505[»]
2ATHX-ray2.28A/B235-505[»]
2F4BX-ray2.07A/B235-505[»]
2FVJX-ray1.99A235-505[»]
2G0GX-ray2.54A/B235-505[»]
2G0HX-ray2.30A/B235-505[»]
2GTKX-ray2.10A235-505[»]
2HFPX-ray2.00A234-505[»]
2HWQX-ray1.97A/B235-505[»]
2HWRX-ray2.34A/B235-505[»]
2I4JX-ray2.10A/B223-504[»]
2I4PX-ray2.10A/B223-504[»]
2I4ZX-ray2.25A/B223-504[»]
2OM9X-ray2.80A/B/C/D232-505[»]
2P4YX-ray2.25A/B231-505[»]
2POBX-ray2.30A/B234-505[»]
2PRGX-ray2.30A/B235-505[»]
2Q59X-ray2.20A/B233-505[»]
2Q5PX-ray2.30A/B233-505[»]
2Q5SX-ray2.05A/B233-505[»]
2Q61X-ray2.20A/B233-505[»]
2Q6RX-ray2.41A/B233-505[»]
2Q6SX-ray2.40A/B233-505[»]
2Q8SX-ray2.30A/B235-505[»]
2QMVNMR-A235-504[»]
2VSRX-ray2.05A/B232-505[»]
2VSTX-ray2.35A/B232-505[»]
2VV0X-ray2.55A/B232-505[»]
2VV1X-ray2.20A/B232-505[»]
2VV2X-ray2.75A/B232-505[»]
2VV3X-ray2.85A/B232-505[»]
2VV4X-ray2.35A/B232-505[»]
2XKWX-ray2.02A/B232-505[»]
2YFEX-ray2.00A/B223-505[»]
2ZK0X-ray2.36A/B223-504[»]
2ZK1X-ray2.61A/B223-504[»]
2ZK2X-ray2.26A/B223-504[»]
2ZK3X-ray2.58A/B223-504[»]
2ZK4X-ray2.57A/B223-504[»]
2ZK5X-ray2.45A/B223-504[»]
2ZK6X-ray2.41A/B223-504[»]
2ZNOX-ray2.40A/B223-504[»]
2ZVTX-ray1.90A/B223-504[»]
3ADSX-ray2.25A/B223-505[»]
3ADTX-ray2.70A/B223-505[»]
3ADUX-ray2.77A/B223-505[»]
3ADVX-ray2.27A/B223-505[»]
3ADWX-ray2.07A/B223-505[»]
3ADXX-ray1.95A/B223-505[»]
3AN3X-ray2.30A/B223-504[»]
3AN4X-ray2.30A/B223-504[»]
3B0QX-ray2.10A/B231-504[»]
3B0RX-ray2.15A/B231-504[»]
3B1MX-ray1.60A234-505[»]
3B3KX-ray2.60A/B223-504[»]
3BC5X-ray2.27A231-505[»]
3CDPX-ray2.80A/B223-504[»]
3CDSX-ray2.65A/B223-504[»]
3CS8X-ray2.30A234-504[»]
3CWDX-ray2.40A/B236-505[»]
3D6DX-ray2.40A/B223-504[»]
3DZUX-ray3.20D102-505[»]
3DZYX-ray3.10D102-505[»]
3E00X-ray3.10D102-505[»]
3ET0X-ray2.40A/B235-505[»]
3ET3X-ray1.95A235-505[»]
3FEJX-ray2.01A235-505[»]
3FURX-ray2.30A234-505[»]
3G9EX-ray2.30A235-505[»]
3GBKX-ray2.30A/B235-505[»]
3H0AX-ray2.10D234-505[»]
3HO0X-ray2.60A/B223-504[»]
3HODX-ray2.10A/B223-504[»]
3IA6X-ray2.31A/B235-505[»]
3K8SX-ray2.55A/B234-505[»]
3KMGX-ray2.10A/D234-505[»]
3LMPX-ray1.90A234-505[»]
3NOAX-ray1.98A/B235-505[»]
3OSIX-ray2.70A/B224-504[»]
3OSWX-ray2.55A/B224-504[»]
3PBAX-ray2.30A/B224-505[»]
3PO9X-ray2.35A/B224-505[»]
3PRGX-ray2.90A232-505[»]
3QT0X-ray2.50A235-505[»]
3R5NX-ray2.00A232-505[»]
3R8AX-ray2.41A/B235-505[»]
3R8IX-ray2.30A/B223-505[»]
3S9SX-ray2.55A234-505[»]
3SZ1X-ray2.30A/B232-505[»]
3T03X-ray2.10A/B234-505[»]
3TY0X-ray2.00A/B231-505[»]
3U9QX-ray1.52A236-504[»]
3V9TX-ray1.65A234-505[»]
3V9VX-ray1.60A234-505[»]
3V9YX-ray2.10A234-505[»]
3VJHX-ray2.22A/B223-504[»]
3VJIX-ray2.61A/B223-504[»]
3VN2X-ray2.18A225-505[»]
3VSOX-ray2.00A/B223-504[»]
3VSPX-ray2.40A/B223-504[»]
3WJ4X-ray1.95A/B235-505[»]
3WJ5X-ray1.89A/B235-505[»]
3WMHX-ray2.10A/B223-504[»]
3X1HX-ray2.30A/B232-505[»]
3X1IX-ray2.40A/B232-505[»]
4A4VX-ray2.00A/B223-505[»]
4A4WX-ray2.00A/B223-505[»]
4CI5X-ray1.77A/B234-505[»]
4E4KX-ray2.50A/B223-505[»]
4E4QX-ray2.50A/B223-505[»]
4EM9X-ray2.10A/B235-505[»]
4EMAX-ray2.54A/B235-505[»]
4F9MX-ray1.90A234-505[»]
4FGYX-ray2.84A235-504[»]
4HEEX-ray2.50X235-505[»]
4JAZX-ray2.85A/B223-505[»]
4JL4X-ray2.50A/B223-505[»]
4L96X-ray2.38A235-505[»]
4L98X-ray2.28A/B235-505[»]
4O8FX-ray2.60A/B223-505[»]
4OJ4X-ray2.30A232-505[»]
4PRGX-ray2.90A/B/C/D235-504[»]
4PVUX-ray2.60A/B223-505[»]
4PWLX-ray2.60A/B223-505[»]
4R06X-ray2.22A/B233-505[»]
4R2UX-ray2.30A/D231-505[»]
4R6SX-ray2.30A/B231-505[»]
4XLDX-ray2.45A231-505[»]
4XTAX-ray2.50A/B232-505[»]
4XUHX-ray2.22A/B232-505[»]
4XUMX-ray2.40A/B232-505[»]
4Y29X-ray1.98A236-504[»]
4YT1X-ray2.20A/B223-504[»]
5AZVX-ray2.70A/B232-505[»]
5DSHX-ray2.95A223-505[»]
5DV3X-ray2.75A223-505[»]
5DV6X-ray2.80A223-505[»]
5DV8X-ray2.75A223-505[»]
5DVCX-ray2.30A223-505[»]
5DWLX-ray2.20A223-505[»]
5F9BX-ray2.25A/B223-505[»]
5GTNX-ray1.85A223-505[»]
5GTOX-ray2.10A223-505[»]
5GTPX-ray2.35A223-505[»]
5HZCX-ray2.00A/B223-505[»]
5JI0X-ray1.98D234-505[»]
5LSGX-ray2.00A/B223-505[»]
5TTOX-ray2.25A/B233-505[»]
5TWOX-ray1.93A234-505[»]
5U5LX-ray2.55A/B233-505[»]
5UGMX-ray2.10A/B235-505[»]
5WQXX-ray2.29A/B232-505[»]
5WR0X-ray2.85A/B232-505[»]
5WR1X-ray2.34A/B232-505[»]
5Y2OX-ray1.80A/B235-505[»]
5Y2TX-ray1.70A/B235-505[»]
6AN1X-ray2.69A/B224-505[»]
6ENQX-ray2.20A/B224-505[»]
6F2LX-ray2.10A/B223-505[»]
DisProtiDP00718
ProteinModelPortaliP37231
SMRiP37231
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37231

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini238 – 503NR LBDPROSITE-ProRule annotationAdd BLAST266

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni205 – 280Interaction with FAM120BBy similarityAdd BLAST76

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri139 – 159NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri176 – 198NR C4-typePROSITE-ProRule annotationAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575 Eukaryota
ENOG410XRZC LUCA
GeneTreeiENSGT00870000136388
HOGENOMiHOG000119407
HOVERGENiHBG106004
InParanoidiP37231
KOiK08530
OMAiPLQEQSK
OrthoDBiEOG091G05U8
PhylomeDBiP37231
TreeFamiTF316304

Family and domain databases

Gene3Di3.30.50.101 hit
InterProiView protein in InterPro
IPR003074 1Cnucl_rcpt
IPR035500 NHR_like_dom_sf
IPR000536 Nucl_hrmn_rcpt_lig-bd
IPR001723 Nuclear_hrmn_rcpt
IPR003077 PPAR-gamma
IPR022590 PPARgamma_N
IPR001628 Znf_hrmn_rcpt
IPR013088 Znf_NHR/GATA
PfamiView protein in Pfam
PF00104 Hormone_recep, 1 hit
PF12577 PPARgamma_N, 1 hit
PF00105 zf-C4, 1 hit
PRINTSiPR01288 PROXISOMEPAR
PR01291 PROXISOMPAGR
PR00398 STRDHORMONER
PR00047 STROIDFINGER
SMARTiView protein in SMART
SM00430 HOLI, 1 hit
SM00399 ZnF_C4, 1 hit
SUPFAMiSSF48508 SSF48508, 1 hit
PROSITEiView protein in PROSITE
PS51843 NR_LBD, 1 hit
PS00031 NUCLEAR_REC_DBD_1, 1 hit
PS51030 NUCLEAR_REC_DBD_2, 1 hit

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform 2 (identifier: P37231-1) [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

        10         20         30         40         50
MGETLGDSPI DPESDSFTDT LSANISQEMT MVDTEMPFWP TNFGISSVDL
60 70 80 90 100
SVMEDHSHSF DIKPFTTVDF SSISTPHYED IPFTRTDPVV ADYKYDLKLQ
110 120 130 140 150
EYQSAIKVEP ASPPYYSEKT QLYNKPHEEP SNSLMAIECR VCGDKASGFH
160 170 180 190 200
YGVHACEGCK GFFRRTIRLK LIYDRCDLNC RIHKKSRNKC QYCRFQKCLA
210 220 230 240 250
VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR ALAKHLYDSY
260 270 280 290 300
IKSFPLTKAK ARAILTGKTT DKSPFVIYDM NSLMMGEDKI KFKHITPLQE
310 320 330 340 350
QSKEVAIRIF QGCQFRSVEA VQEITEYAKS IPGFVNLDLN DQVTLLKYGV
360 370 380 390 400
HEIIYTMLAS LMNKDGVLIS EGQGFMTREF LKSLRKPFGD FMEPKFEFAV
410 420 430 440 450
KFNALELDDS DLAIFIAVII LSGDRPGLLN VKPIEDIQDN LLQALELQLK
460 470 480 490 500
LNHPESSQLF AKLLQKMTDL RQIVTEHVQL LQVIKKTETD MSLHPLLQEI

YKDLY
Length:505
Mass (Da):57,620
Last modified:April 27, 2001 - v3
Checksum:i3933EFF36A0E4CAF
GO
Isoform 1 (identifier: P37231-2) [UniParc]FASTAAdd to basket
Also known as: PPARgamma1(wt)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Show »
Length:477
Mass (Da):54,681
Checksum:i1061C2074B739E0A
GO
Isoform 3 (identifier: P37231-3) [UniParc]FASTAAdd to basket
Also known as: PPARgamma1(tr)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.
     207-213: AIRFGRM → EELQKDS
     214-504: Missing.

Note: Exhibits dominant negative activity over isoform 1.
Show »
Length:186
Mass (Da):21,580
Checksum:i10E780305F860A5D
GO

Sequence cautioni

The sequence AAN38992 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA23354 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAF83270 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA62153 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti36 – 37MP → IA in BAA18949 (PubMed:9144532).Curated2
Sequence conflicti213 – 214MP → IA in BAA18949 (PubMed:9144532).Curated2
Sequence conflicti240R → RQ in BAA18949 (PubMed:9144532).Curated1

Polymorphismi

Genetic variations in PPARG define the body mass index quantitative trait locus 1 (BMIQ1) [MIMi:606641]. The body max index (BMI) reflects the amount of fat, lean mass, and body build.2 Publications
Genetic variations in PPARG influence the carotid intimal medial thickness (CIMT) [MIMi:609338]. CIMT is a measure of atherosclerosis that is independently associated with traditional atherosclerotic cardiovascular disease risk factors and coronary atherosclerotic burden. 35 to 45% of the variability in multivariable-adjusted CIMT is explained by genetic factors.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01072312P → A Polymorphism; significant independent determinant of CIMT; may protect from early atherosclerosis in subject at risk for diabetes; associated with BMI. 5 PublicationsCorresponds to variant dbSNP:rs1801282Ensembl.1
Natural variantiVAR_01611640P → A. Corresponds to variant dbSNP:rs1805192Ensembl.1
Natural variantiVAR_010724113P → Q in obesity. 1 PublicationCorresponds to variant dbSNP:rs1800571Ensembl.1
Natural variantiVAR_010725314Q → P in colon cancer; sporadic; somatic mutation; loss of ligand-binding. 1 PublicationCorresponds to variant dbSNP:rs28936407Ensembl.1
Natural variantiVAR_010726316R → H in colon cancer; sporadic; somatic mutation; partial loss of ligand-binding. 1 PublicationCorresponds to variant dbSNP:rs28936407Ensembl.1
Natural variantiVAR_010727318V → M in diabetes. 1 PublicationCorresponds to variant dbSNP:rs72551362Ensembl.1
Natural variantiVAR_022700388F → L in FPLD3. 1 PublicationCorresponds to variant dbSNP:rs72551363Ensembl.1
Natural variantiVAR_022701425R → C in FPLD3. 1 PublicationCorresponds to variant dbSNP:rs72551364Ensembl.1
Natural variantiVAR_010728495P → L in diabetes. 1 PublicationCorresponds to variant dbSNP:rs121909244Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0036451 – 28Missing in isoform 1 and isoform 3. 7 PublicationsAdd BLAST28
Alternative sequenceiVSP_043906207 – 213AIRFGRM → EELQKDS in isoform 3. 1 Publication7
Alternative sequenceiVSP_043907214 – 504Missing in isoform 3. 1 PublicationAdd BLAST291

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U79012 mRNA Translation: AAC51248.1
U63415 mRNA Translation: AAB04028.1
D83233 mRNA Translation: BAA18949.1
L40904 mRNA Translation: AAA80314.2
AB005526 Genomic DNA Translation: BAA23354.1 Sequence problems.
X90563 mRNA Translation: CAA62152.1
X90563 mRNA Translation: CAA62153.1 Different initiation.
DQ356894 mRNA Translation: ABC97372.1
BT007281 mRNA Translation: AAP35945.1
AK290581 mRNA Translation: BAF83270.1 Different initiation.
AB451337 mRNA Translation: BAG70151.1
AB451486 mRNA Translation: BAG70300.1
AY157024 Genomic DNA Translation: AAN38992.2 Different initiation.
AC090947 Genomic DNA No translation available.
AC091492 Genomic DNA No translation available.
AC093174 Genomic DNA No translation available.
CH471055 Genomic DNA Translation: EAW64124.1
BC006811 mRNA Translation: AAH06811.1
CCDSiCCDS2609.1 [P37231-1]
CCDS2610.2 [P37231-2]
PIRiJC4859
PC4290
PC4429
RefSeqiNP_005028.4, NM_005037.5 [P37231-2]
NP_056953.2, NM_015869.4 [P37231-1]
NP_619725.2, NM_138711.3 [P37231-2]
NP_619726.2, NM_138712.3 [P37231-2]
XP_011532143.1, XM_011533841.2
UniGeneiHs.162646

Genome annotation databases

EnsembliENST00000287820; ENSP00000287820; ENSG00000132170 [P37231-1]
ENST00000309576; ENSP00000312472; ENSG00000132170 [P37231-2]
ENST00000396999; ENSP00000380195; ENSG00000132170 [P37231-3]
ENST00000397010; ENSP00000380205; ENSG00000132170 [P37231-2]
ENST00000397012; ENSP00000380207; ENSG00000132170 [P37231-2]
ENST00000397015; ENSP00000380210; ENSG00000132170 [P37231-2]
GeneIDi5468
KEGGihsa:5468
UCSCiuc003bwr.4 human [P37231-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPPARG_HUMAN
AccessioniPrimary (citable) accession number: P37231
Secondary accession number(s): A8K3G6
, B5BUA1, O00684, O00710, O14515, Q0QJH8, Q15178, Q15179, Q15180, Q15832, Q86U60, Q96J12
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: April 27, 2001
Last modified: April 25, 2018
This is version 242 of the entry and version 3 of the sequence. See 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