CASP8
Gene Ontology Biological Process
- B cell activation [TAS]
- MyD88-independent toll-like receptor signaling pathway [TAS]
- T cell activation [TAS]
- TRAIL-activated apoptotic signaling pathway [IDA]
- TRIF-dependent toll-like receptor signaling pathway [TAS]
- activation of cysteine-type endopeptidase activity [IDA]
- activation of cysteine-type endopeptidase activity involved in apoptotic process [TAS]
- apoptotic process [IGI, IMP, TAS]
- apoptotic signaling pathway [IMP, TAS]
- cellular component disassembly involved in execution phase of apoptosis [TAS]
- cellular response to mechanical stimulus [IEP]
- execution phase of apoptosis [IMP]
- extrinsic apoptotic signaling pathway [IDA]
- extrinsic apoptotic signaling pathway via death domain receptors [IBA]
- innate immune response [TAS]
- intrinsic apoptotic signaling pathway [TAS]
- macrophage differentiation [TAS]
- natural killer cell activation [TAS]
- negative regulation of I-kappaB kinase/NF-kappaB signaling [IMP]
- nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [TAS]
- nucleotide-binding oligomerization domain containing signaling pathway [TAS]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IEP, IMP]
- positive regulation of macrophage differentiation [IMP]
- positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [TAS]
- positive regulation of proteolysis [IDA]
- proteolysis [IDA]
- proteolysis involved in cellular protein catabolic process [IMP]
- regulation of extrinsic apoptotic signaling pathway in absence of ligand [TAS]
- response to tumor necrosis factor [IMP]
- syncytiotrophoblast cell differentiation involved in labyrinthine layer development [TAS]
- toll-like receptor 3 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor signaling pathway [TAS]
Gene Ontology Molecular Function- cysteine-type endopeptidase activity [IDA, TAS]
- cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- cysteine-type endopeptidase activity involved in apoptotic signaling pathway [IMP]
- cysteine-type peptidase activity [TAS]
- death effector domain binding [IPI]
- peptidase activity [IMP]
- protein binding [IPI]
- scaffold protein binding [IPI]
- ubiquitin protein ligase binding [IPI]
- cysteine-type endopeptidase activity [IDA, TAS]
- cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- cysteine-type endopeptidase activity involved in apoptotic signaling pathway [IMP]
- cysteine-type peptidase activity [TAS]
- death effector domain binding [IPI]
- peptidase activity [IMP]
- protein binding [IPI]
- scaffold protein binding [IPI]
- ubiquitin protein ligase binding [IPI]
Gene Ontology Cellular Component
MAPT
Gene Ontology Biological Process
- apoptotic process [TAS]
- cellular component disassembly involved in execution phase of apoptosis [TAS]
- generation of neurons [NAS]
- microtubule cytoskeleton organization [IDA]
- positive regulation of axon extension [IDA]
- positive regulation of microtubule polymerization [IDA]
- regulation of autophagy [IGI]
- regulation of microtubule polymerization [NAS]
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 cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease.
The principal pathological features of Alzheimer's disease (AD) are extracellular amyloid plaques and intracellular neurofibrillary tangles, the latter composed of the microtubule-binding protein tau assembled into paired helical and straight filaments. Recent studies suggest that these pathological entities may be functionally linked, although the mechanisms by which amyloid deposition promotes pathological tau filament assembly are poorly understood. Here, we report ... [more]
Throughput
- Low Throughput
Additional Notes
- Caspase cleaves Tau in vitro
Curated By
- BioGRID