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]
PREP
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
Prolyl oligopeptidase enhances α-synuclein dimerization via direct protein-protein interaction.
Prolyl oligopeptidase (PREP) accelerates the aggregation of α-synuclein (aSyn), a key protein involved in development of Parkinson disease and other synucleinopathies. PREP inhibitors reduce aSyn aggregation, but the mechanism has remained unknown. We have now used protein-fragment complementation assays (PCA) and microscale thermophoresis in parallel to show that PREP interacts directly with aSyn in both intact cells and in a ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| SNCA PREP | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | - |
Curated By
- BioGRID