SNAP25
Gene Ontology Biological Process
- energy reserve metabolic process [TAS]
- glutamate secretion [TAS]
- neurotransmitter secretion [TAS]
- neurotransmitter uptake [NAS]
- regulation of insulin secretion [TAS]
- small molecule metabolic process [TAS]
- synaptic transmission [NAS, TAS]
- synaptic vesicle docking [NAS]
- synaptic vesicle exocytosis [TAS]
- synaptic vesicle fusion to presynaptic membrane [IBA]
- synaptic vesicle priming [IBA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
GOSR1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
N-Ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment proteins (SNAP) mediate dissociation of GS28-syntaxin 5 Golgi SNAP receptors (SNARE) complex.
Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) GS28 and syntaxin 5 can be reciprocally coimmunoprecipitated from Golgi extracts, suggesting that they exist in a protein complex. When Golgi extract is preincubated with soluble NSF attachment proteins (alpha-SNAP) and N-ethylmaleimide-sensitive factor (NSF) under conditions that allow ATP hydrolysis by NSF, GS28 and syntaxin 5 become dissociated. GS28 and syntaxin 5 ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID