Pparg
entrez
25664
canonical
uniprot
O88275
canonical
ensembl
ENSRNOG00000008839
resolver
ensembl
ENSRNOG00055009152
resolver
ensembl
ENSRNOG00060025849
resolver
ensembl
ENSRNOG00065029023
resolver
ensp
ENSRNOP00000012137
resolver
ensp
ENSRNOP00000073235
resolver
genesymbol
Pparg
resolver
genesymbol_syn
Nr1c3
resolver
uniprot
Q9QWG0
resolver
uniprot
Q9R197
resolver
uniprot_entry
PPARG_RAT
resolver
uniprot_sec
Q9QWG0
resolver
uniprot_sec
Q9R197
resolver
activity_regulation
ACTIVITY REGULATION: PDPK1 activates its transcriptional activity independently of its kinase activity. {ECO:0000250|UniProtKB:P37231}.
uniprot
proteins
amino_acid_sequence
MGETLGDPPVDPEHGAFADALPMSTSQEITMVDTEMPFWPTNFGISSVDLSVMDDHSHSFDIKPFTTVDFSSISAPHYEDIPFTRADPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNRPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFINLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKVLQKMTDLRQIVTEHVQLLHVIKKTETDMSLHPLLQEIYKDLY
uniprot
proteins
function
FUNCTION: Ligand-activated transcription factor that forms obligate heterodimers with the retinoic acid receptor and acts as a key regulator of biological processes, such as adipocyte differentiation, lipid metabolism, glucose homeostasis and beta-oxidation of fatty acids. Activated by lipid ligands: binds peroxisome proliferators, such as hypolipidemic drugs, and fatty acids, such as prostaglandin J2 metabolites. Ligand-binding results in a conformational change in the receptor, promoting dissociation of repressors and recruitment of coactivators, and subsequent activation of target gene expression. Specifically binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase (By similarity). Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses (By similarity). Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels (By similarity). {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.; FUNCTION: [Isoform 2]: Nuclear receptor that acts as the key factor controlling the development of adipocytes. Specifically activated by 15-deoxy-delta12,14-prostaglandin J2 ligand during early adipogenesis, driving differentiation of all types of adipocytes (white, beige and brown). Acts together with retinoic acid receptor RXRA, forming the ARF6 complex, which acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Following recruitment of TLE3, promotes differentiation of white adipocytes. Following recruitment of PRDM16, promotes differentiation of myoblastic precursors into brown adipose cells (BAT), which are specialized in dissipating energy in the form of heat in response to cold or excess feeding. Also mediates diffentiation of white adipocytes into beige adipocytes by mediating recruitment of PRDM16. {ECO:0000250|UniProtKB:P37238}.
uniprot
proteins
mass_dalton
57567
uniprot
proteins
mutagenesis
MUTAGEN 112; /note="S->A: Increases adipogenic activity."; /evidence="ECO:0000269|PubMed:9030579
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by MAPK. The phosphorylation inhibits PPAR gamma activity. {ECO:0000269|PubMed:8943212, ECO:0000269|PubMed:8953045, ECO:0000269|PubMed:9030579}.; PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in adipocytes. {ECO:0000250|UniProtKB:P37238}.; PTM: Phosphorylated at basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated form may be inactive and dephosphorylation at induces adipogenic activity (By similarity). {ECO:0000250|UniProtKB:P37231}.; PTM: Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO9; leading to proteasomal degradation (By similarity). Ubiquitinated at Lys-252 by TRIM55 leading to proteasomal degradation (By similarity). Ubiquitinated by E3 ubiquitin-protein ligase STUB1/CHIP; leading to proteasomal degradation (By similarity). Ubiquitinated by E3 ubiquitin-protein ligase ARIH2; leading to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
uniprot
proteins
protein_family
NR1 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
10438514
uniprot
proteins
pubmed
10797535
uniprot
proteins
pubmed
8943212
uniprot
proteins
pubmed
8953045
uniprot
proteins
pubmed
9030579
uniprot
proteins
sequence_length
505
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P37238}. Cytoplasm {ECO:0000250|UniProtKB:P37231}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner (By similarity). NOCT enhances its nuclear translocation (By similarity). {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000250|UniProtKB:P37238}.
uniprot
proteins