Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation.
| Predicate | Object |
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| rdf:type | |
| rdfs:comment |
Activation involves cleavage of the N-terminal prodomain, followed by self-proteolysis between the large and small subunits of pro-caspase-2 and further proteolysis into smaller fragments.,
Apart from itself, the enzyme can cleave golgin-16, which is present in the Golgi complex and has a cleavage site that is unique for caspase-2.,
Belongs to peptidase family C14.,
Caspase-2 is activated by caspase-3 (EC 3.4.22.56), or by a caspase-3-like protease.,
Caspase-2 is an initiator caspase, as are caspases-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63).,
Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation.,
Proteolysis occurs at Asp residues and the preferred substrate for this enzyme is a pentapeptide rather than a tetrapeptide.,
Two forms of caspase-2 exist that have antagonistic effects: caspase-2L induces programd cell death and caspase-2S suppresses cell death.,
alpha-II-spectrin, a component of the membrane cytoskeleton, is a substrate of the large isoform of pro-caspase-2 (caspase-2L) but not of the short isoform (caspase-2S).
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| rdfs:subClassOf | |
| skos:broaderTransitive | |
| uniprot:name |
CASP-2,
Caspase-2,
ICH-1,
NEDD-2,
NEDD2 protein,
Neural precursor cell expressed developmentally down-regulated protein 2
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| uniprot:activity |
Strict requirement for an Asp residue at P1, with 316-asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-.
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