Aliases for CASP6 Gene
External Ids for CASP6 Gene
This gene encodes a protein which is 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 is processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade. Alternative splicing of this gene results in two transcript variants that encode different isoforms. [provided by RefSeq, Jul 2008]
GeneCards Summary for CASP6 Gene
CASP6 (Caspase 6, Apoptosis-Related Cysteine Peptidase) is a Protein Coding gene. Diseases associated with CASP6 include thoracic cancer and myocardial infarction. Among its related pathways are Akt Signaling and ERK Signaling. GO annotations related to this gene include identical protein binding and cysteine-type endopeptidase activity. An important paralog of this gene is CASP1.
UniProtKB/Swiss-Prot for CASP6 Gene
Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death
Caspases (short for cysteinyl aspartate proteases) are involved in the signal transduction pathways of apoptosis, necrosis and inflammation. These enzymes can be divided into two major classes - initiators and effectors. The initiator isoforms (caspases-1,-4,-5,-8,-9,-10,-11,-12) are activated by, and interact with, upstream adaptor molecules through protein-protein interaction domains known as CARD and DED. Effector caspases (-3,-6,-7) are responsible for cleaving downstream substrates and are sometimes referred to as the executioner caspases. More than 400 caspase substrates have so far been identified (see The Caspase Substrate Database). Initiator caspases, such as caspase 8, may be directly activated by death receptors such as FasR. Caspases can also be found intracellularly as part of large multiprotein complexes. For example, caspase 9 is recruited to the apoptosome formed during apoptosis, whilst caspases-1 and 5 can form part of the inflammasome, a key part of cytokine processing during inflammation. Caspases are regulated by inhibitors of apoptosis and by dominant negative isoforms. They have been implicated in the pathogenesis of many disorders including stroke, Alzheimers disease, myocardial infarction, cancer, and inflammatory disease.