Literature summary for 3.4.22.55 extracted from

Baliga, B.C.; Colussi, P.A.; Read, S.H.; Dias, M.M.; Jans, D.A.; Kumar, S.
Role of prodomain in importin-mediated nuclear localization and activation of caspase-2 (2003), J. Biol. Chem., 278, 4899-4905.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
K152A	mutant enzyme with strikingly altered caspase-2 localization. Whereas caspase-2 characteristically accumulates in the nucleus forming dots or filaments, the mutant enzyme is mostly localized outside and exclusively of the nucleus forming dot-like aggregates. K152A mutants can also kill transfected cells at comparable levels to the wild-type version	Mus musculus
additional information	caspase prodomain-DELTA25 mutant is slightly less effective than wild-type caspase-2, inducing cell death of about 70% of transfected cells. Caspase prodomain-DELTA25 mutant cannot kill due to its impaired nuclear localization	Mus musculus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
nucleus	the enzyme contains a classical nuclear localization signal at the C terminus of the prodomain which is recognized by the importin alpha/beta dimer	Mus musculus	5634	-

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	-	-

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Release 2023.1 (January 2023)