| UniProt ID | PPARG_HUMAN | |
|---|---|---|
| UniProt AC | P37231 | |
| Protein Name | Peroxisome proliferator-activated receptor gamma | |
| Gene Name | PPARG | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 505 | |
| Subcellular Localization | Nucleus. Cytoplasm. Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation. | |
| Protein Description | 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).; (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.. | |
| Protein Sequence | MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 63 | Sumoylation | HSHSFDIKPFTTVDF CCCCCCCCCCEEECH | 35.60 | - | |
| 74 (in isoform 2) | Phosphorylation | - | 37.52 | - | |
| 78 | Phosphorylation | SSISTPHYEDIPFTR HHCCCCCCCCCCCCC | 19.25 | - | |
| 79 (in isoform 2) | Sumoylation | - | 46.56 | - | |
| 84 (in isoform 3) | Phosphorylation | - | 27.57 | - | |
| 84 | O-linked_Glycosylation | HYEDIPFTRTDPVVA CCCCCCCCCCCCCEE | 27.57 | UniProtKB CARBOHYD | |
| 95 | Phosphorylation | PVVADYKYDLKLQEY CCEEECCEEEECHHH | 21.93 | - | |
| 102 | Phosphorylation | YDLKLQEYQSAIKVE EEEECHHHHHCCCCC | 8.53 | 25690035 | |
| 104 | Phosphorylation | LKLQEYQSAIKVEPA EECHHHHHCCCCCCC | 30.93 | 25690035 | |
| 107 | Sumoylation | QEYQSAIKVEPASPP HHHHHCCCCCCCCCC | 40.02 | - | |
| 107 | Sumoylation | QEYQSAIKVEPASPP HHHHHCCCCCCCCCC | 40.02 | - | |
| 112 | Phosphorylation | AIKVEPASPPYYSEK CCCCCCCCCCCCCHH | 36.80 | 16574647 | |
| 115 | Phosphorylation | VEPASPPYYSEKTQL CCCCCCCCCCHHHCC | 24.02 | 28450419 | |
| 116 | Phosphorylation | EPASPPYYSEKTQLY CCCCCCCCCHHHCCC | 19.00 | 28450419 | |
| 117 | Phosphorylation | PASPPYYSEKTQLYN CCCCCCCCHHHCCCC | 27.12 | 28450419 | |
| 123 | Phosphorylation | YSEKTQLYNKPHEEP CCHHHCCCCCCCCCC | 16.01 | 27642862 | |
| 184 | Ubiquitination | DLNCRIHKKSRNKCQ CCCCEEEHHCCCCCC | 50.50 | - | |
| 185 | Ubiquitination | LNCRIHKKSRNKCQY CCCEEEHHCCCCCCC | 40.25 | - | |
| 245 (in isoform 2) | Phosphorylation | - | 24.82 | - | |
| 269 | Phosphorylation | RAILTGKTTDKSPFV HHHHCCCCCCCCCEE | 41.39 | 18452278 | |
| 273 | Phosphorylation | TGKTTDKSPFVIYDM CCCCCCCCCEEEEEC | 26.78 | 20651683 | |
| 364 | Sumoylation | MLASLMNKDGVLISE HHHHHCCCCCCEEEC | 41.72 | - | |
| 367 (in isoform 2) | Sumoylation | - | 6.51 | - | |
| 395 | Sumoylation | FGDFMEPKFEFAVKF CCCCCCCCCEEEEEE | 44.19 | - | |
| 395 | Sumoylation | FGDFMEPKFEFAVKF CCCCCCCCCEEEEEE | 44.19 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 74 | Y | Phosphorylation | Kinase | EGFR | P00533 | PSP |
| 78 | Y | Phosphorylation | Kinase | ABL | P00519 | PSP |
| 102 | Y | Phosphorylation | Kinase | ABL | P00519 | PSP |
| 112 | S | Phosphorylation | Kinase | CDK9 | P50750 | PSP |
| 112 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
| 112 | S | Phosphorylation | Kinase | MAPK8 | P45983 | GPS |
| 112 | S | Phosphorylation | Kinase | MAPK-FAMILY | - | GPS |
| 273 | S | Phosphorylation | Kinase | CDK5 | Q00535 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | NEDD4 | P46934 | PMID:23549616 |
| - | K | Ubiquitination | E3 ubiquitin ligase | SIAH2 | O43255 | PMID:22294748 |
| - | K | Ubiquitination | E3 ubiquitin ligase | AHR | P35869 | PMID:31653699 |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 112 | S | Phosphorylation |
| 23186163 |
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PPARG_HUMAN !! | ||||||
| Kegg Disease | |
|---|---|
| There are no disease associations of PTM sites. | |
| OMIM Disease | |
| Note=Defects in PPARG can lead to type 2 insulin-resistant diabetes and hyptertension. PPARG mutations may be associated with colon cancer. | |
| 601665 | |
| 604367 | Lipodystrophy, familial partial, 3 (FPLD3) |
| 137800 | Glioma 1 (GLM1) |
| Kegg Drug | |
| There are no disease associations of PTM sites. | |
| DrugBank | |
| DB01014 | Balsalazide |
| DB01393 | Bezafibrate |
| DB01067 | Glipizide |
| DB01050 | Ibuprofen |
| DB00159 | Icosapent |
| DB00328 | Indomethacin |
| DB00244 | Mesalazine |
| DB01252 | Mitiglinide |
| DB00731 | Nateglinide |
| DB01132 | Pioglitazone |
| DB00912 | Repaglinide |
| DB00412 | Rosiglitazone |
| DB00795 | Sulfasalazine |
| DB00966 | Telmisartan |
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