VPS28
Gene Ontology Biological Process
- endosomal transport [TAS]
- intracellular transport of virus [TAS]
- membrane organization [TAS]
- negative regulation of protein ubiquitination [IDA]
- protein targeting to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [IBA]
- ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [IC, IMP]
- viral life cycle [TAS]
- viral process [TAS]
- viral protein processing [TAS]
- virion assembly [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
VPS36
Gene Ontology Biological Process
Gene Ontology Molecular Function
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.
Publication
Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex.
ESCRT-II plays a pivotal role in receptor downregulation and multivesicular body biogenesis and is conserved from yeast to humans. The crystal structures of two human ESCRT-II complex structures have been determined at 2.6 and 2.9 A resolution, respectively. The complex has three lobes and contains one copy each of VPS22 and VPS36 and two copies of VPS25. The structure reveals ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| VPS28 VPS36 | 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