IKBKE
Gene Ontology Biological Process
- MyD88-independent toll-like receptor signaling pathway [TAS]
- NIK/NF-kappaB signaling [IDA]
- TRIF-dependent toll-like receptor signaling pathway [TAS]
- immune response [NAS]
- innate immune response [TAS]
- intrinsic apoptotic signaling pathway in response to DNA damage [IMP]
- negative regulation of type I interferon production [TAS]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IEP]
- protein phosphorylation [IDA]
- toll-like receptor 3 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor signaling pathway [TAS]
Gene Ontology Molecular Function
CYLD
Gene Ontology Biological Process
- cytoplasmic translation [IBA]
- innate immune response [TAS]
- necroptotic process [IBA]
- negative regulation of NF-kappaB import into nucleus [IDA]
- negative regulation of NF-kappaB transcription factor activity [IDA]
- negative regulation of canonical Wnt signaling pathway [IMP]
- negative regulation of type I interferon production [TAS]
- nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [TAS]
- nucleotide-binding oligomerization domain containing signaling pathway [TAS]
- positive regulation of extrinsic apoptotic signaling pathway [IMP]
- protein K63-linked deubiquitination [IDA]
- regulation of cilium assembly [ISS]
- regulation of intrinsic apoptotic signaling pathway [IMP]
- regulation of microtubule cytoskeleton organization [IMP]
- regulation of mitotic cell cycle [IMP]
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
The tumour suppressor CYLD is a negative regulator of RIG-I-mediated antiviral response.
On detecting viral RNAs, the RNA helicase retinoic acid-inducible gene I (RIG-I) activates the interferon regulatory factor 3 (IRF3) signalling pathway to induce type I interferon (IFN) gene transcription. How this antiviral signalling pathway might be negatively regulated is poorly understood. Microarray and bioinformatic analysis indicated that the expression of RIG-I and that of the tumour suppressor CYLD (cylindromatosis), a ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CYLD IKBKE | 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 | - | |
| IKBKE CYLD | 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 | 2513541 |
Curated By
- BioGRID