| Id: | acc0680 |
| Group: | 1sens |
| Protein: | p125FAK |
| Gene Symbol: | Ptk2 |
| Protein Id: | P34152 |
| Protein Name: | FAK1_MOUSE |
| PTM: | phosphorylation |
| Site: | Tyr397 |
| Site Sequence: | AVSVSETDDYAEIIDEEDTYT |
| Disease Category: | Other |
| Disease: | Mouse Embryonic Fibroblast |
| Disease Subtype: | Mouse Embryonic Fibroblast |
| Disease Cellline: | Swiss 3T3 |
| Disease Info: | |
| Drug: | thapsigargin |
| Drug Info: | "Thapsigargin is a plant-derived sesquiterpene lactone that acts as a potent and non-competitive inhibitor of the sarco/endoplasmic reticulum Ca??-ATPase (SERCA), inducing endoplasmic reticulum stress, disrupting intracellular calcium homeostasis, and exhibiting broad-spectrum antiviral activity against coronaviruses including HCoV-229E, MERS-CoV, and SARS-CoV-2." |
| Effect: | modulate |
| Effect Info: | Bombinin protease activates the adhesion-related signaling pathway by promoting the tyrosine phosphorylation of p125FAK and may play a role in the migration and invasion of tumor cells. |
| Note: | no tumor effct |
| Score: | 3.0 |
| Pubmed(PMID): | 8314789 |
| Sentence Index: | 8314789_8 |
| Sentence: | Depletion of the intracellular Ca2+ pool by treatment with the tumor promoter thapsigargin completely blocked the ability of bombesin to transiently increase the cytosolic Ca2+ concentration but had no effect on bombesin stimulation of p125FAK tyrosine phosphorylation. |
Sequence & Structure:
MAAAYLDPNLNHTPSSSTKTHLGTGMERSPGAMERVLKVFHYFESSSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMQEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGVYLSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKVQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGIPAMAGSIYQGQASLLDQTELWNHRPQEMSMWQPSVEDSAALDLRGMGQVLPPHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSFQGPTGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLSNLSSISSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPALPASTHREIEMAQKLLNSDLGELISKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH
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 |
|---|---|---|---|---|---|
| Y | 956 | A | Lung cancer | Phosphorylation | 18606490 |
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.
