To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
ENZYME entry: EC 220.127.116.11
View entry in original ENZYME format
View entry in raw text format (no links)
in this entry
|Neural precursor cell expressed developmentally down-regulated protein 2.|
|Strict requirement for an Asp residue at P1, with 316-asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-|
- Caspase-2 is an initiator caspase, as are caspases-8 (EC 18.104.22.168),
caspase-9 (EC 22.214.171.124) and caspase-10 (EC 126.96.36.199).
- Contains a caspase-recruitment domain (CARD) in its N-terminal
prodomain, which plays a role in procaspase activation.
- Two forms of caspase-2 exist that have antagonistic effects: caspase-
2L induces programd cell death and caspase-2S suppresses cell death.
- Caspase-2 is activated by caspase-3 (EC 188.8.131.52), or by a caspase-
- 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.
- Proteolysis occurs at Asp residues and the preferred substrate for
this enzyme is a pentapeptide rather than a tetrapeptide.
- 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
- Alpha-II-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).
- Belongs to peptidase family C14.
|PRIAM enzyme-specific profiles||184.108.40.206|
|KEGG Ligand Database for Enzyme Nomenclature||220.127.116.11|
|IUBMB Enzyme Nomenclature||18.104.22.168|
|MEDLINE||Find literature relating to 22.214.171.124|
, with possibility to download in different formats, align etc.
entries corresponding to 3.4.22.-
entries corresponding to 3.4.-.-
entries corresponding to 3.-.-.-