Pparg
entrez
19016
canonical
uniprot
P37238
canonical
ensembl
ENSMUSG00000000440
resolver
ensp
ENSMUSP00000000450
resolver
ensp
ENSMUSP00000131962
resolver
ensp
ENSMUSP00000145525
resolver
ensp
ENSMUSP00000220731
resolver
ensp
ENSMUSP00000220736
resolver
ensp
ENSMUSP00000220737
resolver
ensp
ENSMUSP00000220757
resolver
enst
ENSMUST00000000450
resolver
enst
ENSMUST00000171644
resolver
enst
ENSMUST00000203732
resolver
genesymbol
Pparg
resolver
genesymbol_syn
Nr1c3
resolver
genesymbol_syn
PPARG
resolver
uniprot
A0A0A0MQN2
resolver
uniprot
F6WTV7
resolver
uniprot
M1VPI1
resolver
uniprot
Q6GU14
resolver
uniprot_entry
A0A0A0MQN2_MOUSE
resolver
uniprot_entry
F6WTV7_MOUSE
resolver
uniprot_entry
M1VPI1_MOUSE
resolver
uniprot_entry
PPARG_MOUSE
resolver
uniprot_entry
Q6GU14_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: PDPK1 activates its transcriptional activity independently of its kinase activity. {ECO:0000250|UniProtKB:P37231}.
uniprot
proteins
amino_acid_sequence
MGETLGDSPVDPEHGAFADALPMSTSQEITMVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISAPHYEDIPFTRADPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNRPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFINLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKNLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKVLQKMTDLRQIVTEHVQLLHVIKKTETDMSLHPLLQEIYKDLY
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 (PubMed:21035761, PubMed:23525231, PubMed:7838715, PubMed:7926726, PubMed:8041794, PubMed:8262913). Activated by lipid ligands: binds peroxisome proliferators, such as hypolipidemic drugs, and fatty acids, such as prostaglandin J2 metabolites (PubMed:21994940, PubMed:27197753, PubMed:8041794, PubMed:8262913). 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 (PubMed:21994940, PubMed:27197753, PubMed:8041794, PubMed:8262913). Specifically binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase (PubMed:8041794, PubMed:8262913). 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 (PubMed:19041764). {ECO:0000250|UniProtKB:P37231, ECO:0000269|PubMed:19041764, ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:27197753, ECO:0000269|PubMed:7838715, ECO:0000269|PubMed:7926726, ECO:0000269|PubMed:8041794, ECO:0000269|PubMed:8262913}.; FUNCTION: [Isoform 2]: Nuclear receptor that acts as the key factor controlling the development of adipocytes (PubMed:10549290, PubMed:10549291, PubMed:10549292, PubMed:18719582, PubMed:21459326, PubMed:23473036, PubMed:7838715, PubMed:7926726, PubMed:8001151, PubMed:8521497, PubMed:8521498). Specifically activated by 15-deoxy-delta12,14-prostaglandin J2 ligand during early adipogenesis, driving differentiation of all types of adipocytes (white, beige and brown) (PubMed:7838715, PubMed:7926726, PubMed:8521497, PubMed:8521498). 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 (PubMed:7838715). Following recruitment of TLE3, promotes differentiation of white adipocytes (PubMed:21459326, PubMed:23473036). 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 (PubMed:18719582, PubMed:24703692, PubMed:40355558). Also mediates diffentiation of white adipocytes into beige adipocytes by mediating recruitment of PRDM16 (PubMed:22405074). {ECO:0000269|PubMed:10549290, ECO:0000269|PubMed:10549291, ECO:0000269|PubMed:10549292, ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:21459326, ECO:0000269|PubMed:22405074, ECO:0000269|PubMed:23473036, ECO:0000269|PubMed:24703692, ECO:0000269|PubMed:40355558, ECO:0000269|PubMed:7838715, ECO:0000269|PubMed:7926726, ECO:0000269|PubMed:8001151, ECO:0000269|PubMed:8521497, ECO:0000269|PubMed:8521498}.
uniprot
proteins
mass_dalton
57598
uniprot
proteins
mutagenesis
MUTAGEN 112; /note="S->A: Increases basal and ligand-induced adipogenic activity. Abolishes repression by PER2 on transactivation activity. No loss of ubiquitination by FBXO9."; /evidence="ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:27197753"; MUTAGEN 112; /note="S->D: No effect on repression by PER2 on transactivation activity."; /evidence="ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21994940"; MUTAGEN 156..159; /note="CEGC->SEGS: Abolished ability to bind DNA."; /evidence="ECO:0000269|PubMed:8001151"; MUTAGEN 273; /note="S->A: No loss of ubiquitination by FBXO9."; /evidence="ECO:0000269|PubMed:27197753
uniprot
proteins
post_translational_modification
PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in adipocytes. {ECO:0000269|PubMed:22226965}.; PTM: Phosphorylated in basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated Ser-112 form is recognized by PER2 and repressed, dephosphorylation at Ser-112 induces adipogenic activity. Ser-112 phosphorylation levels are reduced by 65% in brown adipose tissue compared to white adipose tissue. {ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21994940}.; PTM: Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO9; leading to proteasomal degradation (PubMed:27197753). Ubiquitinated at Lys-252 by TRIM55 leading to proteasomal degradation (By similarity). Ubiquitinated by E3 ubiquitin-protein ligase STUB1/CHIP; leading to proteasomal degradation (PubMed:35710596). Ubiquitinated by E3 ubiquitin-protein ligase ARIH2; leading to proteasomal degradation (PubMed:40355558). {ECO:0000250|UniProtKB:P37231, ECO:0000269|PubMed:27197753, ECO:0000269|PubMed:35710596, ECO:0000269|PubMed:40355558}.
uniprot
proteins
protein_family
NR1 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
10549290
uniprot
proteins
pubmed
10549291
uniprot
proteins
pubmed
10549292
uniprot
proteins
pubmed
10788465
uniprot
proteins
pubmed
15687259
uniprot
proteins
pubmed
17595322
uniprot
proteins
pubmed
18719582
uniprot
proteins
pubmed
19037106
uniprot
proteins
pubmed
19041764
uniprot
proteins
pubmed
20078863
uniprot
proteins
pubmed
20498072
uniprot
proteins
pubmed
21035761
uniprot
proteins
pubmed
21459326
uniprot
proteins
pubmed
21994940
uniprot
proteins
pubmed
22226965
uniprot
proteins
pubmed
22405074
uniprot
proteins
pubmed
23473036
uniprot
proteins
pubmed
23525231
uniprot
proteins
pubmed
24703692
uniprot
proteins
pubmed
25519902
uniprot
proteins
pubmed
27197753
uniprot
proteins
pubmed
28683290
uniprot
proteins
pubmed
35710596
uniprot
proteins
pubmed
40355558
uniprot
proteins
pubmed
7838715
uniprot
proteins
pubmed
7926726
uniprot
proteins
pubmed
8001151
uniprot
proteins
pubmed
8041794
uniprot
proteins
pubmed
8240342
uniprot
proteins
pubmed
8262913
uniprot
proteins
pubmed
8521497
uniprot
proteins
pubmed
8521498
uniprot
proteins
pubmed
8647948
uniprot
proteins
pubmed
9325263
uniprot
proteins
sequence_length
505
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:20498072, ECO:0000269|PubMed:23525231}. 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 (PubMed:20498072). {ECO:0000250|UniProtKB:P37231, ECO:0000269|PubMed:20498072}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:8001151}.
uniprot
proteins