BIRC5
Gene Ontology Biological Process
- G2/M transition of mitotic cell cycle [IDA]
- cell division [IMP]
- cytokinesis [IMP]
- establishment of chromosome localization [IMP]
- inhibition of cysteine-type endopeptidase activity involved in apoptotic process [IBA]
- mitotic cell cycle [TAS]
- mitotic nuclear division [TAS]
- negative regulation of apoptotic process [IDA, IMP]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IDA, IMP]
- negative regulation of transcription, DNA-templated [IMP]
- positive regulation of cell proliferation [TAS]
- positive regulation of exit from mitosis [IMP]
- positive regulation of mitotic cell cycle [IMP]
- protein complex localization [IMP]
- protein phosphorylation [IDA]
- protein ubiquitination [IBA]
- regulation of signal transduction [IBA]
- spindle assembly involved in mitosis [IBA]
- spindle checkpoint [IMP]
Gene Ontology Molecular Function- Ran GTPase binding [IPI]
- chaperone binding [IPI]
- cobalt ion binding [NAS]
- cofactor binding [IDA]
- cysteine-type endopeptidase inhibitor activity involved in apoptotic process [IMP]
- enzyme binding [IPI]
- identical protein binding [IPI]
- microtubule binding [IDA, TAS]
- protein binding [IPI]
- protein heterodimerization activity [IDA]
- protein homodimerization activity [IDA, IPI]
- tubulin binding [IDA]
- ubiquitin-protein transferase activity [IBA]
- zinc ion binding [IDA, NAS]
- Ran GTPase binding [IPI]
- chaperone binding [IPI]
- cobalt ion binding [NAS]
- cofactor binding [IDA]
- cysteine-type endopeptidase inhibitor activity involved in apoptotic process [IMP]
- enzyme binding [IPI]
- identical protein binding [IPI]
- microtubule binding [IDA, TAS]
- protein binding [IPI]
- protein heterodimerization activity [IDA]
- protein homodimerization activity [IDA, IPI]
- tubulin binding [IDA]
- ubiquitin-protein transferase activity [IBA]
- zinc ion binding [IDA, NAS]
Gene Ontology Cellular Component
- centriole [IDA]
- chromosome passenger complex [IPI]
- chromosome, centromeric region [IDA]
- condensed chromosome kinetochore [IDA]
- cytoplasm [IDA]
- cytoplasmic microtubule [IDA]
- cytosol [IDA, TAS]
- interphase microtubule organizing center [IDA]
- midbody [IDA]
- nuclear chromosome [IDA]
- nucleus [IDA]
- spindle microtubule [IDA]
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]
Biochemical Activity
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
An anti-apoptotic protein human survivin is a direct inhibitor of caspase-3 and -7.
Survivin, an apoptosis inhibitor/cell-cycle regulator, is critically required for suppression of apoptosis and ensuring normal cell division in the G2/M phase of the cell cycle. It is highly expressed in a cell cycle-regulated manner and localizes together with caspase-3 on microtubules within centrosomes. Whether survivin is a physiologically relevant caspase inhibitor has been unclear due to the difficulties with obtaining ... [more]
Throughput
- Low Throughput
Additional Notes
- Survivin/BIRC5 inhibits caspase-3 and caspase-7.
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| BIRC5 CASP3 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | 315831 | |
| BIRC5 CASP3 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - |
Curated By
- BioGRID