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: | Staurosporine |
Drug Info: | "Staurosporine is a potent, naturally occurring alkaloid originally isolated from the bacterium?Streptomyces staurosporeus. It acts as a?non-selective, ATP-competitive inhibitor?of multiple protein kinases (e.g., PKC, PKA) with IC?? values in the nanomolar range and is widely used in research to?induce apoptosis?at higher concentrations or?promote neurite outgrowth?at lower doses ." |
Relation: |
AKT-Ser473
DOWN
+
Staurosporine
➜
Melanoma
Alleviate
|
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.