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
EEA1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
CYLD Regulates Centriolar Satellites Proteostasis by Counteracting the E3 Ligase MIB1.
The tumor suppressor CYLD is a deubiquitinating enzyme that removes non-degradative ubiquitin linkages bound to a variety of signal transduction adaptors. CYLD participates in the formation of primary cilia, a microtubule-based structure that protrudes from the cell body to act as a "sensing antenna." Yet, how exactly CYLD regulates ciliogenesis is not fully understood. Here, we conducted an unbiased proteomic ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CYLD EEA1 | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3791861 |
Curated By
- BioGRID