Search Results
Overview
| Uniprot ID | P42574 |
|---|---|
| Protein Name | Caspase-3 |
| Gene Name | CASP3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 11 | TENSVDSKSIKNLEP |
| 14 | SVDSKSIKNLEPKII |
| 57 | INNKNFHKSTGMTSR |
| 88 | LKYEVRNKNDLTREE |
Function
Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis (PubMed:18723680, PubMed:20566630, PubMed:23650375, PubMed:35338844, PubMed:35446120, PubMed:7596430). Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins (PubMed:18723680, PubMed:20566630, PubMed:23650375, PubMed:7596430). At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond (PubMed:10497198, PubMed:16374543, PubMed:7596430, 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 (By similarity). Cleaves and activates caspase-6, -7 and -9 (CASP6, CASP7 and CASP9, respectively) (PubMed:7596430). Cleaves and inactivates interleukin-18 (IL18) (PubMed:37993714, PubMed:9334240). Involved in the cleavage of huntingtin (PubMed:8696339). Triggers cell adhesion in sympathetic neurons through RET cleavage (PubMed:21357690). Also involved in axon pruning during brain development (By similarity). Cleaves DSG2 in response to apoptosis resulting in a loss of full length DSG2 at desmosome cell junctions and subsequent loss of cell-cell adhesion (PubMed:17559062). Also cleaves JUP in response to apoptosis (PubMed:17559062). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress (PubMed:23152800). Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction (PubMed:30878284). Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (PubMed:35338844, PubMed:35446120). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (PubMed:23845944, PubMed:33725486). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (PubMed:36758104, PubMed:36758106)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0031264 | death-inducing signaling complex |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0043025 | neuronal cell body |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0014069 | postsynaptic density |
| Molecular Function | GO:0004190 | aspartic-type endopeptidase activity |
| Molecular Function | GO:0004861 | cyclin-dependent protein serine/threonine kinase inhibitor activity |
| Molecular Function | GO:0004197 | cysteine-type endopeptidase activity |
| Molecular Function | GO:0005123 | death receptor binding |
| Molecular Function | GO:0008047 | enzyme activator activity |
| Molecular Function | GO:0008233 | peptidase activity |
| Molecular Function | GO:0016005 | phospholipase A2 activator activity |
| Molecular Function | GO:0002020 | protease binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:0097190 | apoptotic signaling pathway |
| Biological Process | GO:0007413 | axonal fasciculation |
| Biological Process | GO:0072734 | cellular response to staurosporine |
| Biological Process | GO:0030218 | erythrocyte differentiation |
| Biological Process | GO:0097194 | execution phase of apoptosis |
| Biological Process | GO:0034349 | glial cell apoptotic process |
| Biological Process | GO:0021766 | hippocampus development |
| Biological Process | GO:0097193 | intrinsic apoptotic signaling pathway |
| Biological Process | GO:0008627 | intrinsic apoptotic signaling pathway in response to osmotic stress |
| Biological Process | GO:0030216 | keratinocyte differentiation |
| Biological Process | GO:0007611 | learning or memory |
| Biological Process | GO:0071887 | leukocyte apoptotic process |
| Biological Process | GO:0001554 | luteolysis |
| Biological Process | GO:0001818 | negative regulation of cytokine production |
| Biological Process | GO:0030182 | neuron differentiation |
| Biological Process | GO:0048011 | neurotrophin TRK receptor signaling pathway |
| Biological Process | GO:0030220 | platelet formation |
| Biological Process | GO:1902004 | positive regulation of amyloid-beta formation |
| Biological Process | GO:0043525 | positive regulation of neuron apoptotic process |
| Biological Process | GO:0140639 | positive regulation of pyroptotic inflammatory response |
| Biological Process | GO:0030163 | protein catabolic process |
| Biological Process | GO:0051604 | protein maturation |
| Biological Process | GO:0016485 | protein processing |
| Biological Process | GO:0006508 | proteolysis |
| Biological Process | GO:0070269 | pyroptotic inflammatory response |
| Biological Process | GO:0016241 | regulation of macroautophagy |
| Biological Process | GO:0031647 | regulation of protein stability |
| Biological Process | GO:0098693 | regulation of synaptic vesicle cycle |
| Biological Process | GO:0043200 | response to amino acid |
| Biological Process | GO:0072347 | response to anesthetic |
| Biological Process | GO:0032025 | response to cobalt ion |
| Biological Process | GO:0032355 | response to estradiol |
| Biological Process | GO:0045471 | response to ethanol |
| Biological Process | GO:0051384 | response to glucocorticoid |
| Biological Process | GO:0009749 | response to glucose |
| Biological Process | GO:0042542 | response to hydrogen peroxide |
| Biological Process | GO:0001666 | response to hypoxia |
| Biological Process | GO:1990418 | response to insulin-like growth factor stimulus |
| Biological Process | GO:0032496 | response to lipopolysaccharide |
| Biological Process | GO:0035094 | response to nicotine |
| Biological Process | GO:0034612 | response to tumor necrosis factor |
| Biological Process | GO:0010165 | response to X-ray |
| Biological Process | GO:0009410 | response to xenobiotic stimulus |
| Biological Process | GO:0051146 | striated muscle cell differentiation |
| Biological Process | GO:0036269 | swimming behavior |
| Biological Process | GO:0098883 | synapse pruning |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.