Id: | acc0903 |
Group: | 2sens |
Protein: | JNK |
Gene Symbol: | MAPK8 |
Protein Id: | P45983 |
Protein Name: | MK08_HUMAN |
PTM: | phosphorylation |
Site: | Thr183 |
Site Sequence: | RTAGTSFMMTPYVVTRYYRAP |
Disease Category: | Cancer |
Disease: | Breast Cancer |
Disease Subtype: | |
Disease Cellline: | SK-BR-3 |
Disease Info: | |
Drug: | curcumin + Tricostatin A (TSA) |
Drug Info: | "Curcumin is a natural polyphenolic compound derived from the rhizome of Curcuma longa, known for its anti-inflammatory, antioxidant, and potential anticancer properties. + Tricostatin A (TSA) is a histone deacetylase (HDAC) inhibitor widely used in epigenetic research to modulate gene expression and induce cell differentiation or apoptosis. Tricostatin A (TSA): -" |
Effect: | modulate |
Effect Info: | "The combination of TSA and curcumin reduced the phosphorylation of ERK and Akt, and induced the phosphorylation of p38 and JNK, thereby enhancing the anti - cancer effect of TSA." |
Note: | "drug comb, site unclear" |
Score: | 4.0 |
Pubmed(PMID): | 22290509 |
Sentence Index: | 22290509_5-6 |
Sentence: | "Increasing the concentration of curcumin from 10 to 20 microM enhanced the growth inhibitory effects of the combination in SkBr3 and 435eB breast cancer cells, which was accompanied by decreased viability along with decreased phosphorylation of ERK and Akt. The decreased cell viability observed in SkBr3 cells when curcumin was combined with TSA led to a G0/G1 cell cycle arrest and increased p21 and p27, and decreased Cyclin D1 protein expression." |
Sequence & Structure:
MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLEERTKNGVIRGQPSPLGAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR
Select PDB:
Target | Drug name | MOA | Phase | Status | Disease | Source |
---|---|---|---|---|---|---|
MAPK8 | BENTAMAPIMOD | c-Jun N-terminal kinase, JNK inhibitor | 2 | Completed | endometriosis | ClinicalTrials |
MAPK8 | TANZISERTIB | c-Jun N-terminal kinase 1 inhibitor | 2 | Terminated | idiopathic pulmonary fibrosis | ClinicalTrials |
MAPK8 | TANZISERTIB | c-Jun N-terminal kinase 1 inhibitor | 2 | Terminated | lupus erythematosus | ClinicalTrials |
MAPK8 | CC-401 | c-Jun N-terminal kinase 1 inhibitor | 1 | Terminated | myeloid leukemia | ClinicalTrials |
Note: Only show clinically investigational or approved drugs with protein targets.
Protein Tractability:
source: Open TargetsPTM Intensity:
source: CPTACMAPK8-Thr183 | |
---|---|
Cancer | Intensity |
BRCA | |
COAD | 0.707 |
HGSC | -0.707 |
ccRCC | |
GBM | |
HNSC | |
LUAD | |
LUSC | |
non_ccRCC | |
PDAC | |
UCEC |
PTM-Disease Association:
source: PTMDResidue | Position | State | Disease | Class | PMID |
---|---|---|---|---|---|
T | 183 | D | Chronic myelogenous leukemia/chronic myeloid leukemia | Phosphorylation | 26147002 |
T | 183 | U | Type 2 diabetes | Phosphorylation | 21931634 |
T | 183 | U | Pancreatic cancer | Phosphorylation | 37016317 |
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.