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
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3.4.22.55
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caspases
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bcl-2
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necrosis
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bid
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proapoptotic
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anti-apoptotic
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parp
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raidd
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apoptosis-inducing
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caspase-dependent
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z-vad-fmk
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p53-induced
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tunel
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jurkat
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polyadp-ribose
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casps
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mitochondria-mediated
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non-apoptotic
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pan-caspase
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apaf-1
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apoptosome
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caspase-mediated
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death-inducing
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cpp32
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fasl
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z-devd-fmk
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executioner
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xiap
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damage-induced
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etoposide-induced
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anti-fas
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prodomains
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p53-dependent
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trail-induced
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executor
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bh3-only
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ac-devd-cho
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apoptogenic
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trail-mediated
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procaspase
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caspase-10
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chk1
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beta-converting
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mitochondria-dependent
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medicine
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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
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Subunits
Subunits on EC 3.4.22.55 - caspase-2
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dimer
monomer
oligomer
caspase-2 undergoes autocatalytic activation to remove the prodomain and linker region to generate a stable dimer consisting of the large subunit p19, residues 170-333, and the small subunit p12, residues 348-452. This p19/p12 dimer self-associates to form the active caspase-2
additional information
dimer
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caspase-2 is activated by dimerization, initiator caspases are present in the cell as inactive monomers and their activation is promoted by dimerization. Dimerization results when initiator caspases are recruited to large molecular weight protein complexes that act as signaling platforms
dimer
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caspase-2 is activated by dimerization, initiator caspases are present in the cell as inactive monomers and their activation is promoted by dimerization. Dimerization results when initiator caspases are recruited to large molecular weight protein complexes that act as signaling platforms
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recruitment of caspase-2 to a higher molecular weight protein complex in cell extracts
additional information
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recruitment of caspase-2 to a higher molecular weight protein complex in cell extracts