EC Number   |
Protein Variants |
Reference |
|---|
   2.7.11.10 | C179A |
berberine does not have any effect on mutant IKK beta C179A. This proves that berberine inhibits IKK beta activity through the modification of Cys179 |
691616 |
| 2.7.11.10 | C179A |
mutant, not susceptible to the inhibitor N-tosyl-L-phenylalanine chloromethyl ketone |
702333 |
| 2.7.11.10 | C179A |
site-directed mutagenesis of IKKbeta at the activation loop, the mutant shows reduced activation and activity compared to the wild-type enzyme, which is not restorable by TNF stimulation, activity of the mutant is partially recovered when its phosphorylation is enforced by coexpression with mitogen-activated protein kinase kinase kinases such as NF-kappaB inducing kinase, NIK, and MAPK/extracellular signal-regulated kinase kinase kinase 1, MEKK1, or when the serine residues are replaced with phospho-mimetic glutamate, the mutant is normal in dimer formation, while its activity abnormally responds to the change in the concentration of substrate ATP, overview |
673483 |
| 2.7.11.10 | C99S |
the mutation partially abolishes (E)-2-methoxy-4-(3-(4-methoxyphenyl)prop-1-en-1-yl)phenol-induced cell growth inhibition and enhances expression of death receptors 5 and 6 |
762079 |
| 2.7.11.10 | D145A |
site-directed mutagenesis, the IKK-2 is devoid of kinase activity despite its ability to bind ATP with high affinity and is not phosphorylated at the T loop. mutant binds a diverse collection of inhibitors with comparable binding affinities to wild-type IKK-2, inhibition by PHA-408 is reduced compared to the wild-type enzyme |
723696 |
| 2.7.11.10 | DELTA1-640 |
deletion mutant containing residues 640-756, which contains the entire C-terminal region after the HLH domain, interacts well with NEMO |
690938 |
| 2.7.11.10 | DELTA1-680 |
deletion mutant wich stably interacts with NEMO |
690938 |
| 2.7.11.10 | DELTA1-705 |
deletion mutant comprising just the predicted alpha-helical and coiled-coil region and the NEMO binding domain (NPD) residues 734-745 is sufficient for a stable interaction with NEMO |
690938 |
| 2.7.11.10 | DELTA1-734 |
deletion mutant containing only the 11-residues of the NEMO-binding region (NBD) is not sufficient for interaction with NEMO |
690938 |
| 2.7.11.10 | DELTA307-384 |
mutant protein consisting of a deletion of the ubiquitin-like domain that is present only in IKKbeta fails to activate NFkappaB in response to IL-1 or TNF. Deletion mutant is incorporated into the IKK complex, indicating that this domain is not important for the intermolecular interaction between the IKKs and NEMO. Deletion mutant strongly associate with the NF-kappaB p65 subunit in the absence or presence of stimuli, whereas wild-type IKKbeta can not be detected in a complex with p65. This indicates that the to propose a model in which the ubiquitin-like domain plays a role in release of NF-kappaB following IkappaBalpha phosphorylation |
692591 |
