EC Number   |
Posttranslational Modification |
Reference  |
|---|
   3.4.22.55 | proteolytic modification |
the activation site of the caspase is DQQD-/- (P4,P3,P2,P1) |
647429 |
| 3.4.22.55 | proteolytic modification |
the enzyme is activated during apoptosis by a caspase-3 (CPP32)-like protease. When cells are induced to undergo apoptosis, endogenous caspase-2 is first cleaved into three fragments of 32000-33000 Da and 14000 Da, which are then further processed into 18000 Da and 12000 Da active subunits |
647763 |
| 3.4.22.55 | sumoylation |
- |
711697 |
| 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 | 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 initial activation of caspase 2 seems to be mediated by dimerization not processing, this generates a partially active enzyme that is further activated by autoprocessing (self cleavage). Additional processing, which is presumably mediated by active effector caspases (caspases 3 and 7) results in the generation of caspase 2 p19 and p12 subunits. Given that caspase 2 can be processed by caspases 3 and 7, and that loss or inhibition of these caspases or their upstream activators (caspase 9 and APAF1) leads to an inhibition of caspase 2 cleavage |
713092 |
| 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 |
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 | phosphoprotein |
regulatory phosphorylations of (pro)caspase-2 |
713566 |
| 3.4.22.55 | proteolytic modification |
the topoisomerase-II inhibitor etoposide induces processing of procaspase-2 |
717457 |
