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EC Number
Posttranslational Modification
Commentary
Reference
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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
phosphoprotein
-
phosphoprotein
calcium/calmodulin regulated protein kinase II phosphorylates caspase-2 at Ser-135
phosphoprotein
phosphorylation at Ser-340
phosphoprotein
regulatory phosphorylations of (pro)caspase-2
proteolytic modification
caspase-2 processing occurs in goniothalamin-treated Jurkat cells, cleavage to its active subunit (33 kDa) occurs as early as 3 h
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
proteolytic modification
pattern of caspase-2 processing differs between its autocatalytic and caspase-8-mediated cleavage
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
proteolytic modification
the activation site of the caspase is DQQD-/- (P4,P3,P2,P1)
Results 1 - 10 of 14 > >>