3.4.22.55	additional information	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 pro–caspase-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