Id: | acc1043 |
Group: | 2sens |
Protein: | AKT |
Gene Symbol: | Akt1 |
Protein Id: | P31750 |
Protein Name: | AKT1_MOUSE |
PTM: | phosphorylation |
Site: | Ser473 |
Site Sequence: | ERRPHFPQFSYSASGTA---- |
Disease Category: | Cancer |
Disease: | Melanoma |
Disease Subtype: | MM |
Disease Cellline: | B16F10 |
Disease Info: | |
Drug: | fenofibrate |
Drug Info: | "Fenofibrate is a third-generation fibric acid derivative and peroxisome proliferator-activated receptor alpha (PPARalpha) agonist, primarily used as a lipid-lowering agent to treat hypertriglyceridemia and mixed dyslipidemia in adults, particularly effective in reducing triglycerides and improving cholesterol profiles while also exhibiting uric acid-lowering effects." |
Effect: | inhibit |
Effect Info: | "The PPAR-dependent anti-metastatic activity of fenofibrate involves the downregulation of Akt phosphorylation, and supplementation with this drug can enhance the efficacy of melanoma chemotherapy." |
Note: | |
Score: | 5.0 |
Pubmed(PMID): | 16707598 |
Sentence Index: | 16707598_12-13 |
Sentence: | "In addition, fenofibrate strongly sensitized BI6FIO cells to the proapoptotic drug staurosporine, further supporting the possibility that fenofibrate-induced down-regulation of Akt function contributes to fenofibrate-mediated inhibition of metastatic potential in this experimental model. CONCLUSIONS: Our results show that the PPAR-dependent antimetastatic activity of fenofibrate involves down-regulation of Akt phosphorylation and suggest that supplementation with this drug may improve the effectiveness of melanoma chemotherapy." |
Sequence & Structure:
MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWATAIQTVADGLKRQEEETMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA
No data.
No data.
Protein Tractability:
source: Open TargetsNo data.
PTM Intensity:
source: CPTACNo data.
PTM-Disease Association:
source: PTMDResidue | Position | State | Disease | Class | PMID |
---|---|---|---|---|---|
S | 473 | D | Alzheimer's disease | Phosphorylation | 35834993 ;  36843923 |
S | 473 | D | Colonic inflammation | Phosphorylation | 36735734 |
S | 473 | D | Diabetes mellitus | Phosphorylation | 17130464 ;  16777975 ;  15033922 ;  15033922 ;  16777975 ;  17130464 ;  35739993 |
S | 473 | D | Turner syndrome | Phosphorylation | 33910978 |
S | 473 | U | Cardiomyopathy | Phosphorylation | 35358489 |
S | 473 | U | Diabetes mellitus | Phosphorylation | 35358489 |
S | 473 | U | Endometrial cancer/carcinoma | Phosphorylation | 16585156 |
S | 473 | U | Melanoma | Phosphorylation | 26565903 |
S | 473 | U | Non-small cell lung cancer | Phosphorylation | 35961388 |
S | 473 | U | Hepatocellular carcinoma | Phosphorylation | 33500384 |
State Note: Based on the distinct PTM states in diseases, PTMD classified all disease-associated PTMs into six classes, including whether the up-regulation (U) or down-regulation (D) of PTM levels, the absence (A) or presence (P) of PTMs, and the creation (C) or disruption (N) of PTM sites are associated with diseases.
PTM-Drug Perturbation Response:
source: DecryptMNo data.
Function score:
source: funscoRNo data.