CUL1
Gene Ontology Biological Process
- G1/S transition of mitotic cell cycle [TAS]
- G2/M transition of mitotic cell cycle [TAS]
- Notch signaling pathway [TAS]
- SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [IDA, ISS]
- anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [TAS]
- cell cycle arrest [TAS]
- intrinsic apoptotic signaling pathway [TAS]
- mitotic cell cycle [TAS]
- negative regulation of cell proliferation [TAS]
- positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- protein ubiquitination [IDA]
- regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
NEDD8
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
Herpes virus deneddylases interrupt the cullin-RING ligase neddylation cycle by inhibiting the binding of CAND1.
The conserved N-terminal domains of the major tegument proteins of herpes viridae encode cysteine proteases with potent ubiquitin and NEDD8-specific deconjugase activity. Here we show that the Epstein-Barr virus-encoded member of this enzyme family, BPLF1, is targeted to cullin-RING ubiquitin ligases (CRLs) via the interaction of the conserved helix-2 with helix-23 of the C-terminal domain (CTD) of cullins, at a ... [more]
Throughput
- Low Throughput
Additional Notes
- #LPPI
- Figure 5
- Likely protein-protein interaction
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NEDD8 CUL1 | 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 | 691042 | |
| CUL1 NEDD8 | 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 | 688886 | |
| NEDD8 CUL1 | 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 | 675486 | |
| CUL1 NEDD8 | 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 | - | |
| CUL1 NEDD8 | 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 | 3450344 |
Curated By
- BioGRID