EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.22.59 | proteolytic modification |
- |
-, 698177 |
| 3.4.22.59 | proteolytic modification |
activation by proteolytic self-cleavage, during activation, the N-terminal prodomain is removed by cleavage at a TETD site. Double cleavage in an unstructured linker region at a DVVD and a TEVD site gives rise to a large 20-kDa and a small 10-kDa subunit. The two large p20 and two small p10 subunits then assemble to form the active CASP6 complex |
718437 |
| 3.4.22.59 | proteolytic modification |
activation through cleavage mainly by caspase-8, partly by caspase-2 and caspase-9 |
700524 |
| 3.4.22.59 | proteolytic modification |
Casp6 is cleaved after B cell activation |
-, 699336 |
| 3.4.22.59 | proteolytic modification |
caspase-6 activates itself through self-processing, processing at either intersubunit linker sites D23, D179 and D193, the prodomain of Casp6 entirely prevents self-processing and activation in vivo but not in vitro, removal of the pro-domain promotes Casp6 activation. Processing of caspase-6 mutants by recombinant caspase-3, overview |
696453 |
| 3.4.22.59 | proteolytic modification |
caspase-6 is activated by caspase-9 |
698943 |
| 3.4.22.59 | proteolytic modification |
caspase-6 is activated by cleavage |
697069 |
| 3.4.22.59 | proteolytic modification |
caspase-6 is inactive until the short 23 amino acid prodomain is removed |
647462 |
| 3.4.22.59 | proteolytic modification |
pro-forms of caspase-6 isozymes need to be proteolytically self-activated. RCasp1-mediated increased processing of pro-Casp6a, while pro-Casp6b inhibits pro-Casp6a activationinto its active subunits |
717804 |
| 3.4.22.59 | proteolytic modification |
the activation site is TEVD-/- (P4,P3,P2,P1) |
647429 |
