EXOC2
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
RALA
Gene Ontology Biological Process
- Ras protein signal transduction [TAS]
- actin cytoskeleton reorganization [IDA]
- chemotaxis [TAS]
- cytokinesis [IDA]
- membrane organization [TAS]
- membrane raft localization [IDA]
- neurotrophin TRK receptor signaling pathway [TAS]
- positive regulation of filopodium assembly [IDA]
- regulation of exocytosis [IDA]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Structure of the GTPase-binding domain of Sec5 and elucidation of its Ral binding site.
The exocyst complex is involved in the final stages of exocytosis, when vesicles are targeted to the plasma membrane and dock. The regulation of exocytosis is vital for a number of processes, for example, cell polarity, embryogenesis, and neuronal growth formation. Regulation of the exocyst complex in mammals was recently shown to be dependent upon binding of the small G ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
EXOC2 RALA | 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 | - | |
EXOC2 RALA | 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 | - |
Curated By
- BioGRID