CASP9
Also known as APAF-3, APAF3, ICE-LAP6, MCH6, PPP1R56, caspase 9
Caspase-9 is an enzyme that in humans is encoded by the CASP9 gene. It is an initiator caspase, critical to the apoptotic pathway found in many tissues. Caspase-9 homologs have been identified in all mammals for which they are known to exist, such as Mus musculus and Pan troglodytes.
Gene data
CASP9- Name
- caspase 9
- Type
- protein-coding
- Position
- 15,490,832–15,526,534 (−)
- Aliases
- APAF-3, APAF3, ICE-LAP6, MCH6, PPP1R56
- Ensembl
- ENSG00000132906
- RefSeq RNA
- NM_001229.5, NM_001278054.2, NM_032996.3, NR_102732.2, NR_102733.2
- RefSeq protein
- NP_001220.2, NP_001264983.1, NP_127463.2, XP_005246071.1, XP_011540575.1
This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein can undergo autoproteolytic processing and activation by the apoptosome, a protein complex of cytochrome c and the apoptotic peptidase activating factor 1; this step is thought to be one of the earliest in the caspase activation cascade. This protein is thought to play a central role in apoptosis and to be a tumor suppressor. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2013].
Gene Ontology
Biological process
Article
21 sectionsContents
- Structure
- Localization
- Protein expression
- Mechanism
- Processing
- Activation
- Catalytic activity
- Regulation
- Deficiencies and mutations
- Clinical significance
- iCasp9
- Alternative transcripts
- Caspase-9α (9L)
- Caspase-9β (9S)
- Caspase-9γ
- Isoform 4
- Interactions
- See also
- References
- Further reading
- External links
Caspase-9 is an enzyme that in humans is encoded by the CASP9 gene. It is an initiator caspase, critical to the apoptotic pathway found in many tissues. Caspase-9 homologs have been identified in all mammals for which they are known to exist, such as Mus musculus and Pan troglodytes.
Caspase-9 belongs to a family of caspases, cysteine-aspartic proteases involved in apoptosis and cytokine signalling. Apoptotic signals cause the release of cytochrome c from mitochondria and activation of apaf-1 (apoptosome), which then cleaves the pro-enzyme of caspase-9 into the active dimer form. Regulation of this enzyme occurs through phosphorylation by an allosteric inhibitor, inhibiting dimerization and inducing a conformational change.