| Id: | acc3206 |
| 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: | High Glucose |
| Disease Subtype: | |
| Disease Cellline: | 3T3L1 |
| Disease Info: | |
| Drug: | "H(2)S, L-cysteine (LC)" |
| Drug Info: | H(2)S is a chemical molecule potentially having biological effects. | L-cysteine (LC) is an amino acid with various physiological functions. |
| Effect: | modulate |
| Effect Info: | "Under hyperglycemic conditions such as diabetes, H?S or its precursor L-cysteine (LC) enhances the phosphorylation of key insulin signaling proteins such as IRS1, Akt, and PKCζ → enhances the GLUT4 pathway and improves the cellular glucose utilization ability." |
| Note: | |
| Score: | 4.0 |
| Pubmed(PMID): | 21953448 |
| Sentence Index: | 21953448_9-10 |
| Sentence: | "Comparative signal silencing studies with siAKT2 or siPKCzeta revealed that PKCzeta phosphorylation is more effective for the GLUT4 activation and glucose utilization in LC-, H(2)S-, or PIP3-treated cells exposed to HG. This is the first report to demonstrate that H(2)S or LC can increase cellular levels of PIP3, a positive regulator of glucose metabolism." |
Sequence & Structure:
MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWATAIQTVADGLKRQEEETMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA
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 | 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.
