The protein encoded by this gene is a cysteine-aspartic acid protease that plays a central role in the execution-phase of cell apoptosis. The encoded protein cleaves and inactivates poly(ADP-ribose) polymerase while it cleaves and activates sterol regulatory element binding proteins as well as caspases 6, 7, and 9. This protein itself is processed by caspases 8, 9, and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. [provided by RefSeq, Aug 2017]
Full Name
Caspase 3
Function
Involved in the activation cascade of caspases responsible for apoptosis execution (PubMed:7596430). At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond (PubMed:7774019). Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9 (PubMed:7596430). Involved in the cleavage of huntingtin (PubMed:8696339). Triggers cell adhesion in sympathetic neurons through RET cleavage (PubMed:21357690). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress (PubMed:23152800).
Biological Process
Anterior neural tube closure Source: Ensembl Apoptotic DNA fragmentation Source: Reactome Apoptotic process Source: UniProtKB Apoptotic signaling pathway Source: BHF-UCL Axonal fasciculation Source: Ensembl B cell homeostasis Source: Ensembl Cell fate commitment Source: Ensembl Cellular response to DNA damage stimulus Source: Ensembl Cellular response to staurosporine Source: CAFA Cytokine-mediated signaling pathway Source: Reactome Erythrocyte differentiation Source: UniProtKB Execution phase of apoptosis Source: UniProtKB Extrinsic apoptotic signaling pathway in absence of ligand Source: Reactome Glial cell apoptotic process Source: Ensembl Heart development Source: Ensembl Hippocampus development Source: Ensembl Hippo signaling Source: Reactome Intrinsic apoptotic signaling pathway in response to osmotic stress Source: Ensembl Keratinocyte differentiation Source: GO_Central Learning or memory Source: Ensembl Leukocyte apoptotic process Source: Ensembl Luteolysis Source: Ensembl Negative regulation of activated T cell proliferation Source: Ensembl Negative regulation of apoptotic process Source: MGI Negative regulation of B cell proliferation Source: Ensembl Neuron apoptotic process Source: Ensembl Neuron differentiation Source: GO_Central Neurotrophin TRK receptor signaling pathway Source: MGI Platelet formation Source: UniProtKB Positive regulation of amyloid-beta formation Source: UniProtKB Positive regulation of apoptotic process Source: GO_Central Positive regulation of neuron apoptotic process Source: Ensembl Protein processing Source: Ensembl Proteolysis Source: UniProtKB Regulation of macroautophagy Source: ParkinsonsUK-UCL Regulation of protein stability Source: UniProtKB Response to amino acid Source: Ensembl Response to antibiotic Source: Ensembl Response to cobalt ion Source: Ensembl Response to drug Source: Ensembl Response to estradiol Source: Ensembl Response to glucocorticoid Source: Ensembl Response to glucose Source: Ensembl Response to hydrogen peroxide Source: Ensembl Response to hypoxia Source: Ensembl Response to lipopolysaccharide Source: Ensembl Response to nicotine Source: Ensembl Response to tumor necrosis factor Source: BHF-UCL Response to UV Source: Ensembl Response to X-ray Source: Ensembl Sensory perception of sound Source: Ensembl Striated muscle cell differentiation Source: Ensembl T cell homeostasis Source: Ensembl Wound healing Source: Ensembl
Cellular Location
Cytoplasm
PTM
Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa. S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol.
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Datasheet