Id: | acc3217 |
Group: | 2sens |
Protein: | Akt |
Gene Symbol: | Akt1 |
Protein Id: | P31750 |
Protein Name: | AKT1_MOUSE |
PTM: | phosphorylation |
Site: | Ser473 |
Site Sequence: | ERRPHFPQFSYSASGTA---- |
Disease Category: | Endocrine and metabolic diseases |
Disease: | Diabetes Mellitus |
Disease Subtype: | testicular oxidative damage |
Disease Cellline: | |
Disease Info: | |
Drug: | TPEN |
Drug Info: | "TPEN is a chelating agent that can bind to metal ions, which is often used in biological and chemical research." |
Effect: | modulate |
Effect Info: | "Zinc deficiency significantly enhanced the decrease in Akt and GSK - 3β phosphorylation (Fig. 1A, B) and the increase in GS phosphorylation caused by diabetes, thus exacerbating the testicular glucose metabolism changes and inflammation induced by diabetes." |
Note: | |
Score: | 4.0 |
Pubmed(PMID): | 22000581 |
Sentence Index: | 22000581_4-5 |
Sentence: | "After diabetes onset induced by streptozotocin, both diabetic and age-matched control mice were given TPEN intraperitoneally for 4 months. Western blotting assay revealed that Akt-mediated glucose metabolism signaling was down-regulated in the diabetic testis and was further decreased in diabetic mice with Zn deficiency, reflected by reduced phosphorylation of both Akt and GSK-3beta and increased phosphorylation of glycogen synthase along with a disarrangement of fatty acid metabolism (increased expression of PPAR-alpha and decreased adenosine-monophosphate-activated protein kinase phosphorylation)." |
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.