Aliases for CASP1 Gene
- Caspase 1, Apoptosis-Related Cysteine Peptidase 2 3
- IL1BC 3 4 6
- Caspase 1, Apoptosis-Related Cysteine Peptidase (Interleukin 1, Beta, Convertase) 2 3
- IL-1 Beta-Converting Enzyme 3 4
- EC 188.8.131.52 4 63
- Caspase-1 2 3
- P45 3 4
- ICE 3 4
- Caspase 1, Apoptosis-Related Cysteine Protease (Interleukin 1, Beta, Convertase) 2
- Interleukin-1 Beta-Converting Enzyme 4
- Interleukin 1-B Converting Enzyme 3
- Interleukin 1, Beta, Convertase 3
External Ids for CASP1 Gene
Previous Symbols for CASP1 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 2 subunits, large and small, that dimerize to form the active enzyme. This gene was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. This gene has been shown to induce cell apoptosis and may function in various developmental stages. Studies of a similar gene in mouse suggest a role in the pathogenesis of Huntington disease. Alternative splicing results in transcript variants encoding distinct isoforms. [provided by RefSeq, Mar 2012]
GeneCards Summary for CASP1 Gene
CASP1 (Caspase 1, Apoptosis-Related Cysteine Peptidase) is a Protein Coding gene. Diseases associated with CASP1 include shigellosis and cowpox. Among its related pathways are PAK Pathway and Apoptotic Pathways in Synovial Fibroblasts. GO annotations related to this gene include cysteine-type endopeptidase activity and cysteine-type endopeptidase activator activity involved in apoptotic process. An important paralog of this gene is CASP2.
UniProtKB/Swiss-Prot for CASP1 Gene
Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Can also promote apoptosis.
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.