COPS4
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
RBX1
Gene Ontology Biological Process
- Notch signaling pathway [TAS]
- SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [IDA, ISS]
- cellular response to hypoxia [TAS]
- proteasome-mediated ubiquitin-dependent protein catabolic process [IDA]
- protein monoubiquitination [IDA]
- protein neddylation [IDA]
- protein ubiquitination [IDA]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- viral process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- Cul2-RING ubiquitin ligase complex [IDA]
- Cul3-RING ubiquitin ligase complex [IDA]
- Cul4A-RING E3 ubiquitin ligase complex [IDA]
- Cul4B-RING E3 ubiquitin ligase complex [IDA]
- Cul5-RING ubiquitin ligase complex [IDA]
- Cul7-RING ubiquitin ligase complex [IDA]
- SCF ubiquitin ligase complex [IDA, ISS]
- cullin-RING ubiquitin ligase complex [IDA]
- cytosol [ISS, TAS]
- nucleoplasm [TAS]
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
Structural basis of Cullin 2 RING E3 ligase regulation by the COP9 signalosome.
Cullin-Ring E3 Ligases (CRLs) regulate a multitude of cellular pathways through specific substrate receptors. The COP9 signalosome (CSN) deactivates CRLs by removing NEDD8 from activated Cullins. Here we present structures of the neddylated and deneddylated CSN-CRL2 complexes by combining single-particle cryo-electron microscopy (cryo-EM) with chemical cross-linking mass spectrometry (XL-MS). These structures suggest a conserved mechanism of CSN activation, consisting of ... [more]
Throughput
- Low Throughput
Additional Notes
- assayed using XL-MS (cross-linking coupled to mass spectrometry) and HDX (hydrogen-deuterium exchange)-MS
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RBX1 COPS4 | 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. | High | - | BioGRID | - | |
| COPS4 RBX1 | 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. | High | - | BioGRID | - | |
| RBX1 COPS4 | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | - | BioGRID | 3447466 |
Curated By
- BioGRID