BAIT
BAX
BCL2L4
BCL2-associated X protein
GO Process (36)
GO Function (7)
GO Component (13)
Gene Ontology Biological Process
- B cell apoptotic process [IDA]
- B cell receptor apoptotic signaling pathway [IDA]
- activation of cysteine-type endopeptidase activity involved in apoptotic process [IDA, IMP]
- activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [IDA]
- apoptotic mitochondrial changes [IDA]
- apoptotic process [NAS, TAS]
- apoptotic signaling pathway [IDA]
- endoplasmic reticulum calcium ion homeostasis [TAS]
- establishment or maintenance of transmembrane electrochemical gradient [IDA]
- extrinsic apoptotic signaling pathway [IDA]
- extrinsic apoptotic signaling pathway in absence of ligand [IBA]
- extrinsic apoptotic signaling pathway via death domain receptors [IC]
- intrinsic apoptotic signaling pathway [IDA, TAS]
- intrinsic apoptotic signaling pathway in response to DNA damage [IBA]
- intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [IMP]
- mitochondrial fragmentation involved in apoptotic process [IDA]
- mitochondrial fusion [IDA]
- negative regulation of protein binding [IDA]
- positive regulation of apoptotic DNA fragmentation [IMP]
- positive regulation of apoptotic process [IMP]
- positive regulation of endoplasmic reticulum unfolded protein response [IMP]
- positive regulation of intrinsic apoptotic signaling pathway [IMP]
- positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [TAS]
- positive regulation of neuron apoptotic process [IDA]
- positive regulation of protein oligomerization [IDA]
- positive regulation of release of cytochrome c from mitochondria [IDA]
- protein homooligomerization [IDA]
- protein oligomerization [IDA]
- regulation of mitochondrial membrane potential [IDA]
- regulation of protein heterodimerization activity [IPI]
- regulation of protein homodimerization activity [IDA]
- release of cytochrome c from mitochondria [IDA]
- release of matrix enzymes from mitochondria [IDA]
- response to toxic substance [IDA]
- retinal cell apoptotic process [IMP]
- transformed cell apoptotic process [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- BAX complex [IDA]
- Bcl-2 family protein complex [IDA]
- cytosol [IDA, TAS]
- endoplasmic reticulum [IDA]
- endoplasmic reticulum membrane [IDA]
- extracellular vesicular exosome [IDA]
- membrane [IDA]
- mitochondrial outer membrane [IBA, TAS]
- mitochondrial permeability transition pore complex [IDA]
- mitochondrion [IDA]
- nuclear envelope [IDA]
- nucleus [IDA, IMP]
- pore complex [IDA]
Homo sapiens
PREY
CYCS
CYC, HCS, THC4
cytochrome c, somatic
GO Process (11)
GO Function (4)
GO Component (6)
Gene Ontology Biological Process
- activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [TAS]
- apoptotic DNA fragmentation [IMP]
- apoptotic process [TAS]
- cellular metabolic process [TAS]
- cellular respiration [TAS]
- dephosphorylation [TAS]
- intrinsic apoptotic signaling pathway [TAS]
- mitochondrial electron transport, cytochrome c to oxygen [IBA]
- mitochondrial electron transport, ubiquinol to cytochrome c [IBA]
- respiratory electron transport chain [TAS]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Co-fractionation
Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.
Publication
Association of active caspase 8 with the mitochondrial membrane during apoptosis: potential roles in cleaving BAP31 and caspase 3 and mediating mitochondrion-endoplasmic reticulum cross talk in etoposide-induced cell death.
It was recently demonstrated that during apoptosis, active caspase 9 and caspase 3 rapidly accumulate in the mitochondrion-enriched membrane fraction (D. Chandra and D. G. Tang, J. Biol. Chem.278:17408-17420, 2003). We now show that active caspase 8 also becomes associated with the membranes in apoptosis caused by multiple stimuli. In MDA-MB231 breast cancer cells treated with etoposide (VP16), active caspase ... [more]
Mol. Cell. Biol. Aug. 01, 2004; 24(15);6592-607 [Pubmed: 15254227]
Throughput
- Low Throughput
Curated By
- BioGRID