EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.22.56 | more |
caspase-3 is S-nitrosylated under basal conditions to prevent activation |
699097 |
| 3.4.22.56 | proteolytic modification |
activation site is IETD (P4,P3,P2,P1) |
647429 |
| 3.4.22.56 | proteolytic modification |
both Mch4 and granzyme B cleave recombinant proCPP32 at a conserved IXXD-S sequence to produce the large and small subunits of the active protease. Granzyme B cleaves at Asp175 to generate the small C-terminal subunit, 12000 Da, and te large N-terminal subunit. Cleavage of the prodomain is an autocatalytic activity of the activated CPP32 |
647431 |
| 3.4.22.56 | proteolytic modification |
caspase-3 is activated by cleavage |
695950 |
| 3.4.22.56 | proteolytic modification |
caspase-3 is activated from procaspase-3 by cleavage |
699751, 699937 |
| 3.4.22.56 | proteolytic modification |
caspase-3 is expressed as an inactive 32 kDa precursor from which the p20 and p11 subunits are proteolytically generated during onset of apoptosis |
701188 |
| 3.4.22.56 | proteolytic modification |
caspase-8 is activated when procaspase-8 is cleaved subsequently from the recruitment of Fas associated protein with death domain, FADD, to the death-effector domain site of procaspase-8 during the oligomerization of death receptor and its ligand |
695620 |
| 3.4.22.56 | proteolytic modification |
caspase-9 and caspase-8 activate procaspase-3 to caspase-3 by cleavage |
698258 |
| 3.4.22.56 | proteolytic modification |
caspases are synthesized in the cell as single-chain precursors and are activated by cleavage at the conserved Asp297 residue, where a conformational change occurs bringing it into the correct alignment for catalysis |
695681 |
| 3.4.22.56 | proteolytic modification |
cleavage of procaspase-3 to the active 17 kDa form. Caspase-3 activation occurs after TNF stimulation at later time points and is not associated with TNF receptosomes |
717539 |
