Id: | acc0733 |
Group: | 2sens |
Protein: | FOXO1 |
Gene Symbol: | FOXO1 |
Protein Id: | Q12778 |
Protein Name: | FOXO1_HUMAN |
PTM: | acetylation |
Site: | Thr24 |
Site Sequence: | EPLPRPRSCTWPLPRPEFSQS |
Disease Category: | Cancer |
Disease: | Lung Cancer |
Disease Subtype: | NSCLC |
Disease Cellline: | H1650 |
Disease Info: | |
Drug: | Ku0063794 + Erlotinib |
Drug Info: | "Ku-0063794 is a cell-permeable, selective dual inhibitor of mTORC1 and mTORC2 with an IC50 of 10 nM, which induces G1-cell cycle arrest and autophagy, and inhibits tumor growth in renal cell carcinoma xenograft models. Erlotinib is a direct-acting EGFR tyrosine kinase inhibitor with an IC50 of 2 nM for human EGFR, used in the treatment of non-small cell lung cancer (NSCLC) by reducing EGFR autophosphorylation in intact tumor cells. " |
Effect: | modulate |
Effect Info: | These drugs affect the growth and apoptosis of tumor cells by regulating the phosphorylation and acetylation states of FOXO1. |
Note: | drug comb |
Score: | 4.0 |
Pubmed(PMID): | 26036758 |
Sentence Index: | 26036758_10-11 |
Sentence: | "Importantly, increasing FOXO1 acetylation by a HDAC inhibitor, depsipeptide, overcomes TKI resistance to effectively induce TKI-resistant NSCLC cell apoptosis. Together, FOXO1 plays dual roles in TKI resistance through posttranslational modifications in NSCLC and this study provides a possible strategy for treatment of TKI-resistant NSCLC patients." |
Sequence & Structure:
MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGSAAANPDAAAGLPSASAAAVSADFMSNLSLLEESEDFPQAPGSVAAAVAAAAAAAATGGLCGDFQGPEAGCLHPAPPQPPPPGPLSQHPPVPPAAAGPLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRSRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGEGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTMMQQTPCYSFAPPNTSLNSPSPNYQKYTYGQSSMSPLPQMPIQTLQDNKSSYGGMSQYNCAPGLLKELLTSDSPPHNDIMTPVDPGVAQPNSRVLGQNVMMGPNSVMSTYGSQASHNKMMNPSSHTHPGHAQQTSAVNGRPLPHTVSTMPHTSGMNRLTQVKTPVQVPLPHPMQMSALGGYSSVSSCNGYGRMGLLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG
Select PDB:
No data.
Protein Tractability:
source: Open TargetsPTM Intensity:
source: CPTACNo data.
PTM-Disease Association:
source: PTMDResidue | Position | State | Disease | Class | PMID |
---|---|---|---|---|---|
T | 24 | D | Head and neck squamous cell carcinoma | Phosphorylation | 21281788 |
T | 24 | U | Breast cancer | Phosphorylation | 36797347 |
T | 24 | U | Prostate cancer | Phosphorylation | 36720852 |
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.