SNCA
Gene Ontology Biological Process
- activation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- calcium ion homeostasis [IDA]
- cellular response to copper ion [IDA]
- cellular response to epinephrine stimulus [TAS]
- cellular response to oxidative stress [IC]
- dopamine biosynthetic process [TAS]
- dopamine uptake involved in synaptic transmission [TAS]
- extracellular fibril organization [TAS]
- microglial cell activation [TAS]
- negative regulation of apoptotic process [IMP]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- negative regulation of dopamine uptake involved in synaptic transmission [IDA]
- negative regulation of exocytosis [IMP]
- negative regulation of histone acetylation [IDA]
- negative regulation of microtubule polymerization [IDA]
- negative regulation of mitochondrial electron transport, NADH to ubiquinone [TAS]
- negative regulation of monooxygenase activity [IDA]
- negative regulation of norepinephrine uptake [IDA]
- negative regulation of platelet-derived growth factor receptor signaling pathway [IDA]
- negative regulation of serotonin uptake [IDA]
- negative regulation of thrombin receptor signaling pathway [IDA]
- negative regulation of transcription from RNA polymerase II promoter [TAS]
- negative regulation of transporter activity [IDA]
- oxidation-reduction process [IDA]
- positive regulation of apoptotic process [TAS]
- positive regulation of endocytosis [IDA]
- positive regulation of glutathione peroxidase activity [IDA]
- positive regulation of hydrogen peroxide catabolic process [IDA]
- positive regulation of inositol phosphate biosynthetic process [IDA]
- positive regulation of peptidyl-serine phosphorylation [ISS]
- positive regulation of protein serine/threonine kinase activity [IDA]
- positive regulation of receptor recycling [IDA]
- positive regulation of release of sequestered calcium ion into cytosol [IDA]
- protein destabilization [IDA]
- receptor internalization [IDA]
- regulation of dopamine secretion [TAS]
- regulation of phospholipase activity [IDA]
- regulation of reactive oxygen species biosynthetic process [TAS]
- regulation of synaptic vesicle recycling [TAS]
- response to interferon-gamma [IDA]
- response to interleukin-1 [IDA]
- response to iron(II) ion [IDA]
- response to lipopolysaccharide [IDA]
- response to magnesium ion [IDA]
- synaptic vesicle endocytosis [ISS]
Gene Ontology Molecular Function- Hsp70 protein binding [IPI]
- alpha-tubulin binding [IPI]
- calcium ion binding [IDA]
- copper ion binding [IDA]
- cysteine-type endopeptidase inhibitor activity involved in apoptotic process [IDA]
- dynein binding [IPI]
- fatty acid binding [IDA]
- ferrous iron binding [IDA]
- histone binding [IDA]
- identical protein binding [IPI]
- kinesin binding [IPI]
- magnesium ion binding [IDA]
- oxidoreductase activity [IDA]
- phospholipase D inhibitor activity [IDA]
- phospholipid binding [IDA]
- phosphoprotein binding [IDA]
- protein binding [IPI]
- tau protein binding [IDA]
- transcription regulatory region DNA binding [TAS]
- zinc ion binding [IDA]
- Hsp70 protein binding [IPI]
- alpha-tubulin binding [IPI]
- calcium ion binding [IDA]
- copper ion binding [IDA]
- cysteine-type endopeptidase inhibitor activity involved in apoptotic process [IDA]
- dynein binding [IPI]
- fatty acid binding [IDA]
- ferrous iron binding [IDA]
- histone binding [IDA]
- identical protein binding [IPI]
- kinesin binding [IPI]
- magnesium ion binding [IDA]
- oxidoreductase activity [IDA]
- phospholipase D inhibitor activity [IDA]
- phospholipid binding [IDA]
- phosphoprotein binding [IDA]
- protein binding [IPI]
- tau protein binding [IDA]
- transcription regulatory region DNA binding [TAS]
- zinc ion binding [IDA]
Gene Ontology Cellular Component
- actin cytoskeleton [IDA]
- axon [IDA]
- cell cortex [IDA]
- cytoplasm [IDA]
- cytosol [IDA]
- extracellular region [TAS]
- fibril [IDA]
- growth cone [IDA]
- inclusion body [IDA]
- lysosome [TAS]
- mitochondrial respiratory chain complex I [TAS]
- mitochondrion [TAS]
- nucleus [IDA]
- perinuclear region of cytoplasm [IDA]
- plasma membrane [IDA]
- platelet alpha granule membrane [IDA]
CRYAB
Gene Ontology Biological Process
Gene Ontology Molecular Function
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.
Publication
Interaction of the chaperones alpha B-crystallin and CHIP with fibrillar alpha-synuclein: Effects on internalization by cells and identification of interacting interfaces.
The spread of fibrillar alpha-synuclein from affected to naive neuronal cells is thought to contribute to the progression of synucleinopathies. The binding of fibrillar alpha-synuclein to the plasma membrane is key in this process. We and others previously showed that coating fibrillar alpha-synuclein by the molecular chaperone Hsc70 affects fibrils properties. Here we assessed the effect of the two molecular ... [more]
Throughput
- Low Throughput
Additional Notes
- Fibrils formation
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| SNCA CRYAB | Co-crystal Structure 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. | Low | - | BioGRID | 724249 | |
| CRYAB SNCA | Co-fractionation 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. | Low | - | BioGRID | 736572 | |
| SNCA 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 | 727055 | |
| SNCA 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 | 724248 | |
| CRYAB SNCA | 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 | 736573 |
Curated By
- BioGRID