EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.22.36 | more |
caspase-1 is gluthathionylated |
700365 |
| 3.4.22.36 | proteolytic modification |
activation of pro-caspase-1 |
700393 |
| 3.4.22.36 | proteolytic modification |
CASP-1 is synthesized as an inactive zymogen and active caspase-1 is produced by proteolytic cleavage of its pro domain, which contains the CAspase Recruitment Domain, i.e. CARD, the CARD domain is localized at the amino end of CASP-1 and serves as a protein-protein interaction module that is important in protein recruitment and proteolytic activation, association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme |
699610 |
| 3.4.22.36 | proteolytic modification |
caspase-1 is synthesized as an inactive zymogen that becomes activated by cleavage at aspartic residues to generate an enzymatically active 10-20 kDa heterodimer |
698215 |
| 3.4.22.36 | proteolytic modification |
inactive 45000 Da proform of caspase-1 is basally expressed in macrophages, virus infection induces the cleavage of procaspase into the mature 20000 Da form |
647636 |
| 3.4.22.36 | proteolytic modification |
pro-caspase-1 is a 45 kDa molecule that autocatalyzes to form active caspase-1 |
699968 |
| 3.4.22.36 | proteolytic modification |
pro-caspase-1 is a 45 kDa molecule that autocatalyzes to form active caspase-1, it is also activated by caspase-11 |
699968 |
| 3.4.22.36 | proteolytic modification |
pro-caspase-1 is a 45 kDa molecule that autocatalyzes to form active caspase-1, it is also activated by caspase-5 |
699968 |
| 3.4.22.36 | proteolytic modification |
pro-Sf-caspase-1 with a short domain is activated by an apical caspase through proteolytic cleavage, at the caspase-recognition site between the large and small subunits of pro-Sfcaspase-1, when apoptotic signaling is triggered |
695901 |
| 3.4.22.36 | proteolytic modification |
the activation site in caspase is WFKD (P4,P3,P2,P1) |
647429 |
