TSG101
Gene Ontology Biological Process
- endosomal transport [TAS]
- intracellular transport of virus [TAS]
- membrane organization [TAS]
- positive regulation of exosomal secretion [IMP]
- regulation of extracellular vesicular exosome assembly [IMP]
- ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [IC, IDA, IMP]
- viral budding [IMP, ISS]
- viral life cycle [TAS]
- viral process [TAS]
- viral protein processing [TAS]
- virion assembly [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
NEDD4
Gene Ontology Biological Process
- cellular response to UV [IMP]
- cytokine-mediated signaling pathway [TAS]
- development involved in symbiotic interaction [IMP]
- glucocorticoid receptor signaling pathway [IDA]
- lysosomal transport [IDA]
- negative regulation of sodium ion transport [IDA]
- negative regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage [IMP]
- negative regulation of vascular endothelial growth factor receptor signaling pathway [ISS]
- neuron projection development [IEP]
- positive regulation of nucleocytoplasmic transport [IDA]
- positive regulation of phosphatidylinositol 3-kinase signaling [IMP]
- positive regulation of protein catabolic process [IDA]
- progesterone receptor signaling pathway [IDA]
- protein K63-linked ubiquitination [ISS]
- protein targeting to lysosome [IDA]
- protein ubiquitination [IDA]
- protein ubiquitination involved in ubiquitin-dependent protein catabolic process [IDA, IMP]
- receptor catabolic process [IDA]
- receptor internalization [IDA]
- regulation of dendrite morphogenesis [ISS]
- regulation of ion transmembrane transport [IDA]
- regulation of membrane potential [IDA]
- regulation of potassium ion transmembrane transporter activity [IDA]
- response to calcium ion [TAS]
- transmission of virus [IMP]
- ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [IMP]
Gene Ontology Molecular Function- RNA polymerase binding [IPI]
- beta-2 adrenergic receptor binding [IDA]
- phosphoserine binding [ISS]
- phosphothreonine binding [ISS]
- proline-rich region binding [IMP, IPI]
- protein binding [IPI]
- protein domain specific binding [IPI]
- sodium channel inhibitor activity [IDA]
- ubiquitin binding [IDA]
- ubiquitin-protein transferase activity [IDA]
- RNA polymerase binding [IPI]
- beta-2 adrenergic receptor binding [IDA]
- phosphoserine binding [ISS]
- phosphothreonine binding [ISS]
- proline-rich region binding [IMP, IPI]
- protein binding [IPI]
- protein domain specific binding [IPI]
- sodium channel inhibitor activity [IDA]
- ubiquitin binding [IDA]
- ubiquitin-protein transferase activity [IDA]
Gene Ontology Cellular Component
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
The functionally exchangeable L domains in RSV and HIV-1 Gag direct particle release through pathways linked by Tsg101.
The functionally exchangeable L domains of HIV-1 and Rous sarcoma virus (RSV) Gag bind Tsg101 and Nedd4, respectively. Tsg101 and Nedd4 function in endocytic trafficking, and studies show that expression of Tsg101 or Nedd4 fragments interfere with release of HIV-1 or RSV Gag, respectively, as virus-like particles (VLPs). To determine whether functional exchangeability reflects use of the same trafficking pathway, ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NEDD4 TSG101 | 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