RAB5A
Gene Ontology Biological Process
- GTP catabolic process [IDA]
- Rab protein signal transduction [IBA]
- blood coagulation [TAS]
- early endosome to late endosome transport [IMP]
- endocytosis [IDA]
- intracellular protein transport [IBA]
- positive regulation of exocytosis [IMP]
- receptor internalization involved in canonical Wnt signaling pathway [IMP]
- regulation of endocytosis [IBA]
- regulation of endosome size [IMP]
- regulation of filopodium assembly [IDA]
- regulation of synaptic vesicle exocytosis [IMP]
- synaptic vesicle recycling [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- axon [ISS]
- axon terminus [ISS]
- cytoplasm [IDA]
- cytoplasmic side of early endosome membrane [IMP]
- cytosol [IDA]
- dendrite [ISS]
- early endosome [IDA]
- endocytic vesicle [IBA]
- endosome [ISS]
- endosome membrane [TAS]
- extracellular vesicular exosome [IDA]
- neuronal cell body [ISS]
- plasma membrane [IBA]
- somatodendritic compartment [IDA]
- synaptic vesicle [ISS]
- terminal bouton [IDA]
RABEP1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5.
Rabaptin-5 functions as an effector for the small GTPase Rab5, a regulator of endocytosis and early endosome fusion. We have searched for structural determinants that confer functional specificity on Rabaptin-5. Here we report that native cytosolic Rabaptin-5 is present in a homodimeric state and dimerization depends upon the presence of its coiled-coil predicted sequences. A 73 residue C-terminal region of ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
RAB5A RABEP1 | 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 | - | |
RABEP1 RAB5A | Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps. | Low | - | BioGRID | - | |
RAB5A RABEP1 | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | 72 | BioGRID | 3002776 | |
RAB5A RABEP1 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
RAB5A RABEP1 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
RAB5A RABEP1 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
RAB5A RABEP1 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
RABEP1 RAB5A | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
RABEP1 RAB5A | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - |
Curated By
- BioGRID