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http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/3.4.-.-
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/3.4.22.-
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/3.-.-.-
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#comment"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)."xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#comment"Belongs to peptidase family C14."xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#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."xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#comment"Proteolysis occurs at Asp residues and the preferred substrate for this enzyme is a pentapeptide rather than a tetrapeptide."xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#comment"Two forms of caspase-2 exist that have antagonistic effects: caspase-2L induces programed cell death and caspase-2S suppresses cell death."xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#comment"Caspase-2 is activated by caspase-3 (EC 3.4.22.56), or by a caspase-3-like protease."xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#comment"alphaII-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)."xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2000/01/rdf-schema#comment"Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation."xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2004/02/skos/core#prefLabel"caspase-2"xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7958843
http://purl.uniprot.org/enzyme/3.4.22.55http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8087842
http://purl.uniprot.org/enzyme/3.4.22.55http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10791974
http://purl.uniprot.org/enzyme/3.4.22.55http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11104820
http://purl.uniprot.org/enzyme/3.4.22.55http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15865942
http://purl.uniprot.org/enzyme/3.4.22.55http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9261102
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2004/02/skos/core#altLabel"CASP-2"xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2004/02/skos/core#altLabel"NEDD-2"xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2004/02/skos/core#altLabel"ICH-1"xsd:string
http://purl.uniprot.org/enzyme/3.4.22.55http://www.w3.org/2004/02/skos/core#altLabel"NEDD2 protein"xsd:string