CASP3
Gene Ontology Biological Process
- activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [TAS]
- apoptotic DNA fragmentation [TAS]
- apoptotic process [TAS]
- apoptotic signaling pathway [TAS]
- cellular component disassembly involved in execution phase of apoptosis [TAS]
- erythrocyte differentiation [IDA, TAS]
- execution phase of apoptosis [IDA, IMP]
- extracellular matrix disassembly [TAS]
- extracellular matrix organization [TAS]
- hippo signaling [TAS]
- intrinsic apoptotic signaling pathway [TAS]
- keratinocyte differentiation [IBA]
- negative regulation of apoptotic process [IGI]
- neuron differentiation [IBA]
- neurotrophin TRK receptor signaling pathway [TAS]
- platelet formation [TAS]
- positive regulation of apoptotic process [TAS]
- proteolysis [IDA]
- regulation of apoptotic process [TAS]
- regulation of cysteine-type endopeptidase activity involved in apoptotic process [TAS]
- response to tumor necrosis factor [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- cytosol [IDA, TAS]
- nucleoplasm [TAS]
- nucleus [IDA]
- plasma membrane [TAS]
PTGES3
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Proteolytic Processing)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
Caspase-7 uses an exosite to promote poly(ADP ribose) polymerase 1 proteolysis.
During apoptosis, hundreds of proteins are cleaved by caspases, most of them by the executioner caspase-3. However, caspase-7, which shares the same substrate primary sequence preference as caspase-3, is better at cleaving poly(ADP ribose) polymerase 1 (PARP) and Hsp90 cochaperone p23, despite a lower intrinsic activity. Here, we identified key lysine residues (K(38)KKK) within the N-terminal domain of caspase-7 as ... [more]
Throughput
- Low Throughput
Additional Notes
- partial P23 cleavage by caspase-3 in vitro
Curated By
- BioGRID