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Literature summary for 3.4.22.36 extracted from

  • da Cunha, J.P.; Galante, P.A.; de Souza, S.J.
    Different evolutionary strategies for the origin of caspase-1 inhibitors (2008), J. Mol. Evol., 66, 591-597.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme Homo sapiens
additional information association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme Macaca mulatta
additional information association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme Pan troglodytes

Cloned(Commentary)

Cloned (Comment) Organism
DNA sequence analysis Homo sapiens
DNA sequence analysis Macaca mulatta
DNA sequence analysis Pan troglodytes

Inhibitors

Inhibitors Comment Organism Structure
additional information caspase 1 inhibitors share sequence similarity to CASP-1 itself and are all mapped to chr11q22.3, overview Homo sapiens
additional information caspase 1 inhibitors share sequence similarity to CASP-1 itself and are all mapped to chr11q22.3, overview Macaca mulatta
additional information caspase 1 inhibitors share sequence similarity to CASP-1 itself and are all mapped to chr11q22.3, overview Pan troglodytes

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Macaca mulatta
-
-
-
Pan troglodytes
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification CASP-1 is synthesized as an inactive zymogen and active caspase-1 is produced by proteolytic cleavage of its pro domain, which contains the CAspase Recruitment Domain, i.e. CARD, the CARD domain is localized at the amino end of CASP-1 and serves as a protein-protein interaction module that is important in protein recruitment and proteolytic activation, association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme Homo sapiens
proteolytic modification CASP-1 is synthesized as an inactive zymogen and active caspase-1 is produced by proteolytic cleavage of its pro domain, which contains the CAspase Recruitment Domain, i.e. CARD, the CARD domain is localized at the amino end of CASP-1 and serves as a protein-protein interaction module that is important in protein recruitment and proteolytic activation, association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme Macaca mulatta
proteolytic modification CASP-1 is synthesized as an inactive zymogen and active caspase-1 is produced by proteolytic cleavage of its pro domain, which contains the CAspase Recruitment Domain, i.e. CARD, the CARD domain is localized at the amino end of CASP-1 and serves as a protein-protein interaction module that is important in protein recruitment and proteolytic activation, association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme Pan troglodytes

Synonyms

Synonyms Comment Organism
CASP-1
-
Homo sapiens
CASP-1
-
Macaca mulatta
CASP-1
-
Pan troglodytes
IL-1B converting enzyme
-
Homo sapiens
IL-1B converting enzyme
-
Macaca mulatta
IL-1B converting enzyme
-
Pan troglodytes
interleukin-1B converting enzyme
-
Homo sapiens
interleukin-1B converting enzyme
-
Macaca mulatta
interleukin-1B converting enzyme
-
Pan troglodytes