EC Number   |
General Information |
Reference |
|---|
   3.4.22.29 | malfunction |
a catalytic mutant of 2A (2Amut) fails to cleave GAB2. Deletion of GAB1 causes a decrease in phosphorylated ERK1/2, but knockdown of GAB2 has no effect on virus-mediated ERK1/2 phosphorylation |
753654 |
| 3.4.22.29 | malfunction |
a PV 2Apro variant deficient in eukaryotic initiation factor (eIF) 4GI cleavage does not increase picornavirus IRES-driven translation |
717992 |
| 3.4.22.29 | malfunction |
CVB3 mutants, that arise with passage in polyamine-depleted conditions, contain mutations in the 2A protease (EC 3.4.22.29) and 3C protease (EC 3.4.22.28). These mutant proteases confer resistance to polyamine depletion. The 2A and 3C protease mutations also enhance reporter protease activity in polyamine-depleted conditions. The mutations promote cleavage of cellular eIF4G during infection of polyamine-depleted cells |
-, 755655 |
| 3.4.22.29 | malfunction |
infection of 2A protease activity-inactivated recombinant EV71 (EV71-2AC110S) failed to induce atypical stress granule (aSG) formation and only induced typical stress granule (tSG) formation, which is PKR and eIF2alpha phosphorylation-dependent. When the protease activity of 2A in EV71 is blocked (EV71-2AC110S), the tSGs but not aSGs appear in infected cells |
-, 755212 |
| 3.4.22.29 | malfunction |
overexpression of these DAP5 truncates (45 kDa N-terminal (DAP5-N) and 52 kDa C-terminal (DAP5-C) fragments) demonstrates that DAP5-N retains the capability of initiating IRES-driven translation of apoptosis-associated p53, but not the prosurvival Bcl-2 (B-cell lymphoma 2) when compared with the full-length DAP5 |
753178 |
| 3.4.22.29 | malfunction |
viral 2Apro proteolytic activity is key process by disrupting the ERK signaling cascade. Disruption of the ERK signaling cascade interrupts viral 2Aprocatalysed processing of eIF4GI, overview. Inhibition of the ERK signaling cascade decreases 2Apro-mediated vIRES-dependent translation in other enteroviruses |
752515 |
| 3.4.22.29 | metabolism |
regulation of enterovirus 2A protease-associated viral IRES activities by the cell's ERK signaling cascade. The positive regulation of virus replication by the ERK cascade is mediated through effects on both the cis-cleavage of the viral polyprotein by 2Apro and its trans-cleavage of cellular eIF4GI. The ERK cascade positively regulates EV-A71-mediated cleavage of eIF4GI that establishes the cellular conditions which favour vIRES-dependent translation. This ERK-2Apro linked network coordinating vIRES efficiency is also found in other important human enteroviruses |
752515 |
| 3.4.22.29 | more |
structure-function analysis of poliovirus 2A protease, three-dimensional structure homology modelling using the crystal structure of coxsakievirus B4 as a template. Protein structure and protein-ligand-drug binding site predictions. Mutation pattern, intrinsic disorder regions (IDRs), hydrophobic regions, drug binding sites (DBS) and subcellular localization are identified, overview |
755620 |
| 3.4.22.29 | more |
the 2A proteases of other picornaviruses such as poliovirus and coxsackievirus also induce aSG formation and blocked tSG formation |
-, 755212 |
| 3.4.22.29 | more |
the enzyme structure contains a conserved His-Asp-Cys catalytic triad and a Zn2+-binding site. Comparison with other 2Apro structures from enteroviruses reveals that the substrate-binding cleft of 2Apro from HRV-C15 exhibits a more open conformation, which presumably favours substrate binding, structure comparisons, overview |
752401 |
