| Id: | acc3305 |
| Group: | 2sens |
| Protein: | Akt |
| Gene Symbol: | Akt1 |
| Protein Id: | P47196 |
| Protein Name: | AKT1_RAT |
| PTM: | phosphorylation |
| Site: | Ser473 |
| Site Sequence: | ERRPHFPQFSYSASGTA---- |
| Disease Category: | Cardiovascular and circulatory system diseases |
| Disease: | Myocardial I/R Injury |
| Disease Subtype: | |
| Disease Cellline: | "Neonatal rat Cardiomyocytes, NRCMs" |
| Disease Info: | |
| Drug: | glucose |
| Drug Info: | "Glucose is a simple sugar that serves as a primary energy source for the body, often used in medical settings to treat hypoglycemia." |
| Effect: | modulate |
| Effect Info: | The article aims to verify the protective effect of insulin on cardiomyocytes and finds that high glucose causes damage in the MI/R model. High glucose environment → Increased O-GlcNAc glycosylation of IRS-1 → Hindrance of insulin-stimulated IRS-1/Akt phosphorylation → Impairment of the insulin signaling pathway in cardiomyocytes → Weakened cardioprotective effect |
| Note: | |
| Score: | 4.0 |
| Pubmed(PMID): | 24845581 |
| Sentence Index: | 24845581_7-8 |
| Sentence: | "However, these cardioprotective effects of insulin were markedly blunted in hyperglycaemic animals (HI/HG). In vitro mechanistic study in neonatal rat cardiomyocytes revealed that insulin-stimulated tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and Akt was significantly attenuated by high glucose, accompanied by markedly increased IRS-1 O-GlcNAc glycosylation following hypoxia/reoxygenation." |
Sequence & Structure:
MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVEQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKRQEEETMDFRSGSPSDNSGAEEMEVALAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA
No data.
No data.
Protein Tractability:
source: Open TargetsNo data.
PTM Intensity:
source: CPTACNo data.
PTM-Disease Association:
source: PTMD| Residue | Position | State | Disease | Class | PMID |
|---|---|---|---|---|---|
| S | 473 | D | Major depressive disorder | Phosphorylation | 16959794 |
| S | 473 | D | Type 2 diabetes | Phosphorylation | 34057658 ; 36374861 |
| S | 473 | U | Status epilepticus | Phosphorylation | 35562960 |
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.
