PPARG
entrez
5468
canonical
uniprot
P37231
canonical
ensembl
ENSG00000132170
resolver
ensp
ENSP00000287820
resolver
ensp
ENSP00000312472
resolver
ensp
ENSP00000380196
resolver
ensp
ENSP00000380205
resolver
ensp
ENSP00000380210
resolver
ensp
ENSP00000380221
resolver
ensp
ENSP00000494873
resolver
ensp
ENSP00000494934
resolver
ensp
ENSP00000495840
resolver
ensp
ENSP00000498313
resolver
ensp
ENSP00000506813
resolver
ensp
ENSP00000507823
resolver
ensp
ENSP00000507893
resolver
ensp
ENSP00000508065
resolver
ensp
ENSP00000562376
resolver
ensp
ENSP00000562377
resolver
ensp
ENSP00000562378
resolver
ensp
ENSP00000562380
resolver
ensp
ENSP00000562381
resolver
ensp
ENSP00000562382
resolver
ensp
ENSP00000562383
resolver
ensp
ENSP00000562384
resolver
ensp
ENSP00000562385
resolver
ensp
ENSP00000562386
resolver
ensp
ENSP00000562387
resolver
ensp
ENSP00000562388
resolver
ensp
ENSP00000562389
resolver
ensp
ENSP00000562390
resolver
ensp
ENSP00000612316
resolver
ensp
ENSP00000612317
resolver
ensp
ENSP00000612318
resolver
ensp
ENSP00000612319
resolver
ensp
ENSP00000612321
resolver
ensp
ENSP00000612322
resolver
ensp
ENSP00000612323
resolver
ensp
ENSP00000612324
resolver
ensp
ENSP00000612325
resolver
ensp
ENSP00000612326
resolver
ensp
ENSP00000612327
resolver
ensp
ENSP00000612328
resolver
ensp
ENSP00000612329
resolver
ensp
ENSP00000612330
resolver
ensp
ENSP00000612331
resolver
ensp
ENSP00000612332
resolver
ensp
ENSP00000612333
resolver
ensp
ENSP00000612334
resolver
ensp
ENSP00000612335
resolver
ensp
ENSP00000612336
resolver
ensp
ENSP00000612338
resolver
ensp
ENSP00000612339
resolver
ensp
ENSP00000612340
resolver
ensp
ENSP00000612341
resolver
ensp
ENSP00000612342
resolver
ensp
ENSP00000671858
resolver
ensp
ENSP00000701867
resolver
ensp
ENSP00000776917
resolver
enst
ENST00000309576
resolver
enst
ENST00000397000
resolver
enst
ENST00000397010
resolver
enst
ENST00000397015
resolver
enst
ENST00000397026
resolver
enst
ENST00000643197
resolver
enst
ENST00000643888
resolver
enst
ENST00000644622
resolver
enst
ENST00000651735
resolver
enst
ENST00000681982
resolver
enst
ENST00000682446
resolver
enst
ENST00000683586
resolver
enst
ENST00000683699
resolver
enst
ENST00000892317
resolver
enst
ENST00000892318
resolver
enst
ENST00000892319
resolver
enst
ENST00000892321
resolver
enst
ENST00000892322
resolver
enst
ENST00000892323
resolver
enst
ENST00000892324
resolver
enst
ENST00000892325
resolver
enst
ENST00000892326
resolver
enst
ENST00000892327
resolver
enst
ENST00000892328
resolver
enst
ENST00000892329
resolver
enst
ENST00000892330
resolver
enst
ENST00000892331
resolver
enst
ENST00000942257
resolver
enst
ENST00000942258
resolver
enst
ENST00000942259
resolver
enst
ENST00000942260
resolver
enst
ENST00000942262
resolver
enst
ENST00000942263
resolver
enst
ENST00000942264
resolver
enst
ENST00000942265
resolver
enst
ENST00000942266
resolver
enst
ENST00000942267
resolver
enst
ENST00000942268
resolver
enst
ENST00000942269
resolver
enst
ENST00000942270
resolver
enst
ENST00000942271
resolver
enst
ENST00000942272
resolver
enst
ENST00000942273
resolver
enst
ENST00000942274
resolver
enst
ENST00000942275
resolver
enst
ENST00000942276
resolver
enst
ENST00000942277
resolver
enst
ENST00000942279
resolver
enst
ENST00000942280
resolver
enst
ENST00000942281
resolver
enst
ENST00000942282
resolver
enst
ENST00000942283
resolver
genesymbol
PPARG
resolver
genesymbol
PPARG1D5
resolver
genesymbol
PPARG2D5
resolver
genesymbol
PPARG5
resolver
genesymbol_syn
NR1C3
resolver
genesymbol_syn
PPAR gamma
resolver
genesymbol_syn
PPARG
resolver
genesymbol_syn
PPARG3D5
resolver
hgnc
HGNC:9236
resolver
uniprot
A0A3P3ZKM0
resolver
uniprot
A0A494C1F9
resolver
uniprot
A0A6F8P0E0
resolver
uniprot
A0A804HK89
resolver
uniprot
A0ACM8Q7H3
resolver
uniprot
A8K3G6
resolver
uniprot
B5BUA1
resolver
uniprot
D2KUA6
resolver
uniprot
E9PFV2
resolver
uniprot
E9PFX5
resolver
uniprot
O00684
resolver
uniprot
O00710
resolver
uniprot
O14515
resolver
uniprot
Q0QJH8
resolver
uniprot
Q15178
resolver
uniprot
Q15179
resolver
uniprot
Q15180
resolver
uniprot
Q15832
resolver
uniprot
Q4W448
resolver
uniprot
Q86U60
resolver
uniprot
Q96J12
resolver
uniprot_entry
A0A3P3ZKM0_HUMAN
resolver
uniprot_entry
A0A494C1F9_HUMAN
resolver
uniprot_entry
A0A6F8P0E0_HUMAN
resolver
uniprot_entry
A0A804HK89_HUMAN
resolver
uniprot_entry
A0ACM8Q7H3_HUMAN
resolver
uniprot_entry
D2KUA6_HUMAN
resolver
uniprot_entry
E9PFV2_HUMAN
resolver
uniprot_entry
E9PFX5_HUMAN
resolver
uniprot_entry
PPARG_HUMAN
resolver
uniprot_sec
A8K3G6
resolver
uniprot_sec
B5BUA1
resolver
uniprot_sec
O00684
resolver
uniprot_sec
O00710
resolver
uniprot_sec
O14515
resolver
uniprot_sec
Q0QJH8
resolver
uniprot_sec
Q15178
resolver
uniprot_sec
Q15179
resolver
uniprot_sec
Q15180
resolver
uniprot_sec
Q15832
resolver
uniprot_sec
Q4W448
resolver
uniprot_sec
Q86U60
resolver
uniprot_sec
Q96J12
resolver
activity_regulation
ACTIVITY REGULATION: PDPK1 activates its transcriptional activity independently of its kinase activity. {ECO:0000269|PubMed:16150867}.
uniprot
proteins
amino_acid_sequence
MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in PPARG can lead to type 2 insulin-resistant diabetes and hyptertension. PPARG mutations may be associated with colon cancer. {ECO:0000269|PubMed:10394368}.; DISEASE: Obesity (OBESITY) [MIM:601665]: A 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. {ECO:0000269|PubMed:9753710}. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry.; DISEASE: Lipodystrophy, familial partial, 3 (FPLD3) [MIM:604367]: An autosomal dominant 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. {ECO:0000269|PubMed:11788685, ECO:0000269|PubMed:12453919}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Glioma 1 (GLM1) [MIM:137800]: Gliomas 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. {ECO:0000269|PubMed:10851250}. Note=Disease susceptibility may be associated with variants 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.
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:16150867, PubMed:20829347, PubMed:23525231, PubMed:8702406, PubMed:8706692, PubMed:9065481). Activated by lipid ligands: binds peroxisome proliferators, such as hypolipidemic drugs, and fatty acids, such as prostaglandin J2 metabolites (PubMed:16150867, PubMed:20829347, PubMed:23525231, PubMed:8702406, PubMed:8706692, PubMed:9065481). 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:16150867, PubMed:20829347, PubMed:23525231, PubMed:8702406, PubMed:8706692, PubMed:9065481). 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 (PubMed:20829347). 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:P37238, ECO:0000269|PubMed:16150867, ECO:0000269|PubMed:20829347, ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:8702406, ECO:0000269|PubMed:8706692, ECO:0000269|PubMed:9065481}.; FUNCTION: [Isoform 2]: Nuclear receptor that acts as the key factor controlling the development of adipocytes (By similarity). Specifically activated by 15-deoxy-delta12,14-prostaglandin J2 ligand during early adipogenesis, driving differentiation of all types of adipocytes (white, beige and brown) (By similarity). 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 (By similarity). Following recruitment of TLE3, promotes differentiation of white adipocytes (By similarity). 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 (By similarity). Also mediates diffentiation of white adipocytes into beige adipocytes by mediating recruitment of PRDM16 (By similarity). {ECO:0000250|UniProtKB:P37238}.; FUNCTION: (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. {ECO:0000269|PubMed:25504154}.
uniprot
proteins
mass_dalton
57620
uniprot
proteins
mutagenesis
MUTAGEN 252; /note="K->R: More than 50% loss of ubiquitination."; /evidence="ECO:0000269|PubMed:36737649
uniprot
proteins
post_translational_modification
PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in adipocytes. {ECO:0000250|UniProtKB:P37238}.; PTM: 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). {ECO:0000250}.; 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 (PubMed:36737649). 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:P37238, ECO:0000269|PubMed:36737649}.
uniprot
proteins
protein_family
NR1 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
10394368
uniprot
proteins
pubmed
10407229
uniprot
proteins
pubmed
10523018
uniprot
proteins
pubmed
10622252
uniprot
proteins
pubmed
10681503
uniprot
proteins
pubmed
10851250
uniprot
proteins
pubmed
10882139
uniprot
proteins
pubmed
11587644
uniprot
proteins
pubmed
11698662
uniprot
proteins
pubmed
11788685
uniprot
proteins
pubmed
11971969
uniprot
proteins
pubmed
12039952
uniprot
proteins
pubmed
12453919
uniprot
proteins
pubmed
12672231
uniprot
proteins
pubmed
14569127
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15047147
uniprot
proteins
pubmed
15056000
uniprot
proteins
pubmed
15258145
uniprot
proteins
pubmed
15356014
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15562396
uniprot
proteins
pubmed
15687259
uniprot
proteins
pubmed
15974597
uniprot
proteins
pubmed
15976031
uniprot
proteins
pubmed
16150867
uniprot
proteins
pubmed
16239304
uniprot
proteins
pubmed
16451087
uniprot
proteins
pubmed
16640330
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16842753
uniprot
proteins
pubmed
16919947
uniprot
proteins
pubmed
17101779
uniprot
proteins
pubmed
20078863
uniprot
proteins
pubmed
20829347
uniprot
proteins
pubmed
21047783
uniprot
proteins
pubmed
22351778
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23525231
uniprot
proteins
pubmed
25504154
uniprot
proteins
pubmed
30468856
uniprot
proteins
pubmed
36737649
uniprot
proteins
pubmed
7787419
uniprot
proteins
pubmed
8702406
uniprot
proteins
pubmed
8706692
uniprot
proteins
pubmed
9065481
uniprot
proteins
pubmed
9144532
uniprot
proteins
pubmed
9356045
uniprot
proteins
pubmed
9425261
uniprot
proteins
pubmed
9744270
uniprot
proteins
pubmed
9753710
uniprot
proteins
pubmed
9806549
uniprot
proteins
pubmed
9813012
uniprot
proteins
sequence_length
505
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17101779, ECO:0000269|PubMed:23525231}. Cytoplasm {ECO:0000269|PubMed:17101779}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner (PubMed:17101779). NOCT enhances its nuclear translocation (By similarity). {ECO:0000250|UniProtKB:P37238, ECO:0000269|PubMed:17101779}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000250|UniProtKB:P37238}.
uniprot
proteins