Id: | acc2203 |
Group: | 2sens |
Protein: | NF-kappaB |
Gene Symbol: | NFKBIA |
Protein Id: | P25963 |
Protein Name: | IKBA_HUMAN |
PTM: | phosphorylation |
Site: | Ser276 |
Site Sequence: | QQLGQLTLENLQMLPESEDEE |
Disease Category: | Cancer |
Disease: | Colorectal Cancer |
Disease Subtype: | |
Disease Cellline: | CT26 |
Disease Info: | |
Drug: | rottlerin |
Drug Info: | "Rottlerin is a natural product derived from *Mallotus Philippinensis*, functioning as a specific protein kinase C delta (PKCdelta) inhibitor with an IC50 of 3-6 μM, a mitochondrial uncoupler that stimulates autophagy through mTORC1 upstream signaling, and an inducer of apoptosis via caspase-3 activation, while also exhibiting inhibitory effects on HIV-1 integration and rabies virus infection. " |
Effect: | modulate |
Effect Info: | "Both magnolol and the PKCdelta inhibitor rottlerin can reduce the activity of NF-κB, decrease the phosphorylation of proteins related to tumor progression, and weaken the invasive ability of CRC cells." |
Note: | |
Score: | 4.0 |
Pubmed(PMID): | 32429376 |
Sentence Index: | 32429376_6-7 |
Sentence: | Results from Western blotting also indicated that phosphorylation of PKCdelta and NF-kappaB -related proteins involved in tumor progression were effectively decreased by magnolol treatment. The invasion capacity of CRC cells was also attenuated by both magnolol and rottlerin. |
Sequence & Structure:
MFQAAERPQEWAMEGPRDGLKKERLLDDRHDSGLDSMKDEEYEQMVKELQEIRLEPQEVPRGSEPWKQQLTEDGDSFLHLAIIHEEKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHSILKATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQLTWGRPSTRIQQQLGQLTLENLQMLPESEDEESYDTESEFTEFTEDELPYDDCVFGGQRLTL
Select PDB:
No data.
Protein Tractability:
source: Open TargetsPTM Intensity:
source: CPTACNo data.
PTM-Disease Association:
source: PTMDResidue | Position | State | Disease | Class | PMID |
---|---|---|---|---|---|
- | - | N | Autosomal dominant anhidrotic ectodermal dysplasia | Phosphorylation | 14523047 |
S | 32 | U | Head and neck squamous cell carcinoma | Phosphorylation | 21281788 |
T | 32 | U | Head and neck squamous cell carcinoma | Phosphorylation | 21281788 |
T | 291 | U | Breast cancer | Phosphorylation | 37377974 |
Y | 305 | U | Chronic lymphocytic leukemia | Phosphorylation | 30887112 |
- | - | U | Colorectal cancer | Ubiquitination | 31685801 |
- | - | U | Squamous cell carcinoma | Ubiquitination | 35128752 |
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.