BCL2L1
Gene Ontology Biological Process
- apoptotic mitochondrial changes [TAS]
- apoptotic process [TAS]
- cytokinesis [IMP]
- extrinsic apoptotic signaling pathway in absence of ligand [IBA]
- innate immune response [TAS]
- intrinsic apoptotic signaling pathway [TAS]
- mitotic cell cycle checkpoint [IMP]
- negative regulation of anoikis [IMP]
- negative regulation of apoptotic process [IDA, IMP]
- negative regulation of autophagy [TAS]
- negative regulation of establishment of protein localization to plasma membrane [IDA]
- negative regulation of execution phase of apoptosis [IDA]
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [TAS]
- negative regulation of intrinsic apoptotic signaling pathway [IDA]
- negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [IDA]
- negative regulation of release of cytochrome c from mitochondria [IC, IDA]
- nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [TAS]
- positive regulation of intrinsic apoptotic signaling pathway [TAS]
- regulation of mitochondrial membrane permeability [IDA]
- regulation of mitochondrial membrane potential [IDA]
- release of cytochrome c from mitochondria [IDA]
- response to cytokine [IDA]
- suppression by virus of host apoptotic process [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
TP53BP2
Gene Ontology Biological Process
Gene Ontology Molecular Function
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Molecular basis of the interaction between the antiapoptotic Bcl-2 family proteins and the proapoptotic protein ASPP2.
We have characterized the molecular basis of the interaction between ASPP2 and Bcl-2, which are key proteins in the apoptotic pathway. The C-terminal ankyrin repeats and SH3 domain of ASPP2 (ASPP2(Ank-SH3)) mediate its interactions with the antiapoptotic protein Bcl-2. We used biophysical and computational methods to identify the interaction sites of Bcl-2 and its homologues with ASPP2. Using peptide array ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| BCL2L1 TP53BP2 | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | - | |
| BCL2L1 TP53BP2 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | - |
Curated By
- BioGRID