| Id: | acc3898 |
| Group: | 1sens |
| Protein: | ERK2 |
| Gene Symbol: | Mapk1 |
| Protein Id: | P63086 |
| Protein Name: | MK01_RAT |
| PTM: | phosphorylation |
| Site: | Tyr187 |
| Site Sequence: | HTGFLTEYVATRWYRAPEIML |
| Disease Category: | Cardiovascular and circulatory system diseases |
| Disease: | Ischemia |
| Disease Subtype: | "Ischemic Neuronal Injury, diabetes mellitus" |
| Disease Cellline: | |
| Disease Info: | |
| Drug: | Monosialotetrahexosy-1 ganglioside (GM1) |
| Drug Info: | Monosialotetrahexosy - 1 ganglioside (GM1) is a ganglioside that is involved in various biological processes in the nervous system. It has potential applications in the treatment of neurological disorders. |
| Effect: | modulate |
| Effect Info: | "Monosialotetrahexosylganglioside (GM1) alleviates ischemic brain injury in diabetic rats, especially in the hippocampal CA3 region and cingulate cortex, and its neuroprotective effect is associated with the inhibition of ERK1/2 phosphorylation." |
| Note: | |
| Score: | 4.0 |
| Pubmed(PMID): | 20546707 |
| Sentence Index: | 20546707_6 |
| Sentence: | The results suggest that GM1 attenuates diabetic-augmented ischemic neuronal injuries probably through suppression of ERK1/2 phosphorylation. |
Sequence & Structure:
MAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
Select PDB:
No data.
Protein Tractability:
source: Open TargetsNo data.
PTM Intensity:
source: CPTACNo data.
PTM-Disease Association:
source: PTMD| Residue | Position | State | Disease | Class | PMID |
|---|---|---|---|---|---|
| - | - | A | Basophilic leukemia | Phosphorylation | 11971018 |
| T | 183 | D | Major depressive disorder | Phosphorylation | 16959794 |
| Y | 185 | D | Major depressive disorder | Phosphorylation | 16959794 |
| T | 183 | U | Uteroplacental insufficiency | Phosphorylation | 16940436 |
| Y | 185 | U | Uteroplacental insufficiency | Phosphorylation | 16940436 |
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.
