http://purl.uniprot.org/enzyme/3.4.22.55 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.4.-.- |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.4.22.- |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.-.-.- |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://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/3.4.22.55 | http://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/3.4.22.55 | http://www.w3.org/2000/01/rdf-schema#comment | "Belongs to peptidase family C14."xsd:string |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://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/3.4.22.55 | http://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/3.4.22.55 | http://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/3.4.22.55 | http://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/3.4.22.55 | http://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/3.4.22.55 | http://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/3.4.22.55 | http://www.w3.org/2004/02/skos/core#prefLabel | "caspase-2"xsd:string |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7958843 |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8087842 |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10791974 |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11104820 |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15865942 |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9261102 |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://www.w3.org/2004/02/skos/core#altLabel | "CASP-2"xsd:string |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://www.w3.org/2004/02/skos/core#altLabel | "NEDD-2"xsd:string |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://www.w3.org/2004/02/skos/core#altLabel | "ICH-1"xsd:string |
http://purl.uniprot.org/enzyme/3.4.22.55 | http://www.w3.org/2004/02/skos/core#altLabel | "NEDD2 protein"xsd:string |