Aliases for CASP4 Gene
External Ids for CASP4 Gene
This gene encodes a protein that 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 composed of a prodomain and a large and small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This caspase is able to cleave and activate its own precursor protein, as well as caspase 1 precursor. When overexpressed, this gene induces cell apoptosis. Alternative splicing results in transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2008]
GeneCards Summary for CASP4 Gene
CASP4 (Caspase 4, Apoptosis-Related Cysteine Peptidase) is a Protein Coding gene. Diseases associated with CASP4 include myocardial infarction. Among its related pathways are PAK Pathway and Apoptotic Pathways in Synovial Fibroblasts. GO annotations related to this gene include cysteine-type endopeptidase activity. An important paralog of this gene is CASP1.
UniProtKB/Swiss-Prot for CASP4 Gene
Involved in the activation cascade of caspases responsible for apoptosis execution. Involved in ER-stress induced apoptosis. Cleaves caspase-1.
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.