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 (Comment) | Organism |
---|---|
DNA sequence analysis | Homo sapiens |
DNA sequence analysis | Macaca mulatta |
DNA sequence analysis | Pan troglodytes |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Macaca mulatta | - |
- |
- |
Pan troglodytes | - |
- |
- |
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 | 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 |