Aliases for CASP12 Gene
External Ids for CASP12 Gene
Previous HGNC Symbols for CASP12 Gene
Previous GeneCards Identifiers for CASP12 Gene
Caspases are cysteine proteases that cleave C-terminal aspartic acid residues on their substrate molecules. This gene is most highly related to members of the ICE subfamily of caspases that process inflammatory cytokines. In rodents, the homolog of this gene mediates apoptosis in response to endoplasmic reticulum stress. However, in humans this gene contains a polymorphism for the presence or absence of a premature stop codon. The majority of human individuals have the premature stop codon and produce a truncated non-functional protein. The read-through codon occurs primarily in individuals of African descent and carriers have endotoxin hypo-responsiveness and an increased susceptibility to severe sepsis. Several alternatively spliced transcript variants have been noted for this gene. [provided by RefSeq, Feb 2011]
GeneCards Summary for CASP12 Gene
CASP12 (Caspase 12 (Gene/Pseudogene)) is a Protein Coding gene. Diseases associated with CASP12 include prion disease and myocardial infarction. Among its related pathways are Apoptotic Pathways in Synovial Fibroblasts and Apoptosis Pathway. GO annotations related to this gene include cysteine-type endopeptidase activity. An important paralog of this gene is CASP1.
UniProtKB/Swiss-Prot for CASP12 Gene
Has no protease activity. May reduce cytokine release in response to bacterial lipopolysaccharide during infections. Reduces activation of NF-kappa-B in response to TNF.
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, Alzheimer's disease, myocardial infarction, cancer, and inflammatory disease.