Casp9
Function
Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates effector caspases caspase-3 (CASP3) or caspase-7 (CASP7). Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (By similarity).
Post-translational modifications
Cleavages at Asp-353 by granzyme B and at Asp-368 by caspase-3 generate the two active subunits. Caspase-8 and -10 can also be involved in these processing events (By similarity).
Phosphorylated at Thr-163 by MAPK1/ERK2. Phosphorylation at Thr-163 is sufficient to block caspase-9 processing and subsequent caspase-3 activation (By similarity). Phosphorylation on Tyr-191 by ABL1/c-Abl; occurs in the response of cells to DNA damage (PubMed:15657060).
Ubiquitinated by BIRC6; this activity is inhibited by DIABLO/SMAC.
Sequence Similarities
Belongs to the peptidase C14A family.
Alternative names
Mch6, Caspase-9, CASP-9, Apoptotic protease Mch-6, Apoptotic protease-activating factor 3, ICE-like apoptotic protease 6, APAF-3, ICE-LAP6