EC Number   |
Posttranslational Modification  |
Reference |
|---|
   3.4.22.55 | more |
DNA damage induced by gamma-radiation triggers the phosphorylation of nuclear caspase-2 at S122 site within the prodomain leading to its cleavage and activation |
711715, 711820 |
| 3.4.22.55 | phosphoprotein |
- |
731596 |
| 3.4.22.55 | phosphoprotein |
calcium/calmodulin regulated protein kinase II phosphorylates caspase-2 at Ser-135 |
732592 |
| 3.4.22.55 | phosphoprotein |
phosphorylation at Ser-340 |
732220 |
| 3.4.22.55 | phosphoprotein |
regulatory phosphorylations of (pro)caspase-2 |
713566 |
| 3.4.22.55 | proteolytic modification |
caspase-2 processing occurs in goniothalamin-treated Jurkat cells, cleavage to its active subunit (33 kDa) occurs as early as 3 h |
713545 |
| 3.4.22.55 | proteolytic modification |
caspase-2 undergoes autocatalytic activation to remove the prodomain and linker region to generate a stable dimer consisting of the large subunit p19 and the small subunit p12. This p19/p12 dimer self-associates to form the active caspase-2, forming a dimer, a tetramer, or a dimer-of-dimers |
717846 |
| 3.4.22.55 | proteolytic modification |
pattern of caspase-2 processing differs between its autocatalytic and caspase-8-mediated cleavage |
713152 |
| 3.4.22.55 | proteolytic modification |
PIDD (p53-induced protein with a death domain [DD]), together with the bipartite adapter protein RAIDD (receptor-interacting protein-associated ICH-1/CED-3 homologous protein with a DD), is implicated in the activation of procaspase-2 in a high molecular weight complex called the PIDDosome during apoptosis induction after DNA damage. Processing of caspase-2 is readily detected in the absence of PIDDosome formation in primary lymphocytes |
712540 |
| 3.4.22.55 | proteolytic modification |
the activation site of the caspase is DQQD-/- (P4,P3,P2,P1) |
647429 |
