CRYAB
Gene Ontology Biological Process
Gene Ontology Molecular Function
APP
Gene Ontology Biological Process
- adult locomotory behavior [ISS]
- axon cargo transport [ISS]
- axon midline choice point recognition [ISS]
- axonogenesis [ISS]
- blood coagulation [TAS]
- cellular copper ion homeostasis [ISS]
- collateral sprouting in absence of injury [ISS]
- dendrite development [ISS]
- endocytosis [ISS]
- extracellular matrix organization [ISS, TAS]
- innate immune response [TAS]
- ionotropic glutamate receptor signaling pathway [ISS]
- locomotory behavior [ISS]
- mRNA polyadenylation [ISS]
- mating behavior [ISS]
- negative regulation of endopeptidase activity [IDA]
- neuron apoptotic process [IMP]
- neuron projection development [ISS]
- neuron remodeling [ISS]
- nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [TAS]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of mitotic cell cycle [ISS]
- protein phosphorylation [ISS]
- regulation of epidermal growth factor-activated receptor activity [ISS]
- regulation of multicellular organism growth [ISS]
- regulation of synapse structure or activity [ISS]
- regulation of translation [ISS]
- visual learning [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- Golgi apparatus [IDA, ISS]
- axon [ISS]
- cell surface [IDA]
- cytoplasm [IDA, ISS]
- cytosol [TAS]
- dendritic shaft [IDA]
- dendritic spine [IDA]
- endosome [IDA]
- extracellular region [TAS]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- integral component of membrane [ISS]
- integral component of plasma membrane [TAS]
- intracellular membrane-bounded organelle [IDA]
- membrane raft [IDA]
- nuclear envelope lumen [IDA]
- perinuclear region of cytoplasm [IDA]
- plasma membrane [IDA]
- platelet alpha granule lumen [TAS]
- receptor complex [IDA]
- synapse [IDA]
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
The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.
Small heat-shock proteins, including αB-crystallin (αB), play an important part in protein homeostasis, because their ATP-independent chaperone activity inhibits uncontrolled protein aggregation. Mechanistic details of human αB, particularly in its client-bound state, have been elusive so far, owing to the high molecular weight and the heterogeneity of these complexes. Here we provide structural insights into this highly dynamic assembly and ... [more]
Throughput
- Low Throughput
Additional Notes
- NMR
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| APP CRYAB | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | Low | - | BioGRID | - | |
| APP CRYAB | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| CRYAB APP | 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 | 728540 | |
| CRYAB APP | 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 | 2209270 | |
| APP CRYAB | 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 | - | |
| CRYAB APP | 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