3.4.22.55: caspase-2
This is an abbreviated version!
For detailed information about caspase-2, go to the full flat file.
Word Map on EC 3.4.22.55
-
3.4.22.55
-
caspases
-
bcl-2
-
necrosis
-
bid
-
proapoptotic
-
anti-apoptotic
-
parp
-
raidd
-
apoptosis-inducing
-
caspase-dependent
-
z-vad-fmk
-
p53-induced
-
tunel
-
jurkat
-
polyadp-ribose
-
casps
-
mitochondria-mediated
-
non-apoptotic
-
pan-caspase
-
apaf-1
-
apoptosome
-
caspase-mediated
-
death-inducing
-
cpp32
-
fasl
-
z-devd-fmk
-
executioner
-
xiap
-
damage-induced
-
etoposide-induced
-
anti-fas
-
prodomains
-
p53-dependent
-
trail-induced
-
executor
-
bh3-only
-
ac-devd-cho
-
apoptogenic
-
trail-mediated
-
procaspase
-
caspase-10
-
chk1
-
beta-converting
-
mitochondria-dependent
-
medicine
-
diagnostics
- 3.4.22.55
-
caspases
- bcl-2
- necrosis
- bid
-
proapoptotic
-
anti-apoptotic
- parp
- raidd
-
apoptosis-inducing
-
caspase-dependent
- z-vad-fmk
-
p53-induced
-
tunel
-
jurkat
-
polyadp-ribose
-
casps
-
mitochondria-mediated
-
non-apoptotic
-
pan-caspase
- apaf-1
- apoptosome
-
caspase-mediated
-
death-inducing
- cpp32
- fasl
- z-devd-fmk
-
executioner
- xiap
-
damage-induced
-
etoposide-induced
-
anti-fas
- prodomains
-
p53-dependent
-
trail-induced
-
executor
-
bh3-only
- ac-devd-cho
-
apoptogenic
-
trail-mediated
-
procaspase
- caspase-10
- chk1
-
beta-converting
-
mitochondria-dependent
- medicine
- diagnostics
Reaction
strict requirement for an Asp residue at P1, with Asp316 being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-/- =
Synonyms
AjCASP, C14.006, CASP-2, Casp2, caspase 2, caspase-2, caspase-2L, caspase-2S, ICH-1, ICH-1 protease, ICH-1L/1S, NEDD-2
ECTree
Advanced search results
Posttranslational Modification
Posttranslational Modification on EC 3.4.22.55 - caspase-2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
phosphoprotein
proteolytic modification
additional information
phosphoprotein
calcium/calmodulin regulated protein kinase II phosphorylates caspase-2 at Ser-135
-
the enzyme is activated during apoptosis by a caspase-3 (CPP32)-like protease. When cells are induced to undergo apoptosis, endogenous caspase-2 is first cleaved into three fragments of 32000-33000 Da and 14000 Da, which are then further processed into 18000 Da and 12000 Da active subunits
proteolytic modification
-
the activation site of the caspase is DQQD-/- (P4,P3,P2,P1)
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
-
pattern of caspase-2 processing differs between its autocatalytic and caspase-8-mediated cleavage
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
-
the topoisomerase-II inhibitor etoposide induces processing of procaspase-2
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 procaspase-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 initial activation of caspase 2 seems to be mediated by dimerization not processing, this generates a partially active enzyme that is further activated by autoprocessing (self cleavage). Additional processing, which is presumably mediated by active effector caspases (caspases 3 and 7) results in the generation of caspase 2 p19 and p12 subunits. Given that caspase 2 can be processed by caspases 3 and 7, and that loss or inhibition of these caspases or their upstream activators (caspase 9 and APAF1) leads to an inhibition of caspase 2 cleavage
-
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
additional information
-
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
additional information
-
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