FBXO3
Gene Ontology Molecular Function
Gene Ontology Cellular Component
SMURF1
Gene Ontology Biological Process
- BMP signaling pathway [IDA, TAS]
- cell differentiation [IDA]
- ectoderm development [TAS]
- negative regulation of BMP signaling pathway [TAS]
- negative regulation of transforming growth factor beta receptor signaling pathway [IDA, TAS]
- proteasome-mediated ubiquitin-dependent protein catabolic process [IDA]
- protein export from nucleus [IDA]
- protein localization to cell surface [IDA]
- protein polyubiquitination [IDA]
- protein ubiquitination [IDA]
- protein ubiquitination involved in ubiquitin-dependent protein catabolic process [IDA]
- receptor catabolic process [IDA]
- transforming growth factor beta receptor signaling pathway [TAS]
- ubiquitin-dependent SMAD protein catabolic process [IDA]
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
F-box protein Fbxo3 targets Smurf1 ubiquitin ligase for ubiquitination and degradation.
It has been demonstrated previously that F-box protein Fbxl15 targets HECT-type E3 Smurf1 and forms a functionally active SCF complex for ubiquitination and proteasomal degradation. Here we show that another F-box protein Fbxo3, belonging to the FBXO type protein family, also interacts with and targets Smurf1 for poly-ubiquitination and proteasomal degradation. Different from Fbxl15, Fbxo3 targets all the Nedd4 family ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| FBXO3 SMURF1 | 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 | - | |
| SMURF1 FBXO3 | 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 | - | |
| FBXO3 SMURF1 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 1256995 |
Curated By
- BioGRID