| Id: | acc0204 |
| Group: | 1sens |
| Protein: | FAK |
| Gene Symbol: | Ptk2 |
| Protein Id: | P34152 |
| Protein Name: | FAK1_MOUSE |
| PTM: | phosphorylation |
| Site: | Tyr397 |
| Site Sequence: | AVSVSETDDYAEIIDEEDTYT |
| Disease Category: | Cancer |
| Disease: | Ovarian Cancer |
| Disease Subtype: | |
| Disease Cellline: | ID8 |
| Disease Info: | |
| Drug: | PND-1186 |
| Drug Info: | "PND-1186 is a reversible inhibitor of focal adhesion kinase (FAK) with an IC50 of 1.5 nM, intended for scientific research use only and not for clinical applications. " |
| Effect: | modulate |
| Effect Info: | "Adding PND - 1186 to the drinking water of mice is well - tolerated and can inhibit the growth of ascites and peritoneum - related ovarian cancer tumors, which is associated with the inhibition of FAK Tyr - 397 phosphorylation." |
| Note: | |
| Score: | 4.0 |
| Pubmed(PMID): | 20234191 |
| Sentence Index: | 20234191_11 |
| Sentence: | Addition of PND-1186 to the drinking water of mice was well tolerated and inhibited ascites- and peritoneal membrane-associated ovarian carcinoma tumor growth associated with the inhibition of FAK Tyr-397 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.
