TRAF2
Gene Ontology Biological Process
- activation of NF-kappaB-inducing kinase activity [IMP]
- activation of cysteine-type endopeptidase activity involved in apoptotic process [TAS]
- apoptotic process [TAS]
- apoptotic signaling pathway [TAS]
- cellular protein complex assembly [ISS]
- innate immune response [TAS]
- negative regulation of neuron death [TAS]
- positive regulation of JUN kinase activity [IDA]
- positive regulation of NF-kappaB transcription factor activity [IDA, IMP]
- positive regulation of T cell activation [IC]
- positive regulation of T cell cytokine production [IMP]
- positive regulation of extrinsic apoptotic signaling pathway [IMP]
- positive regulation of interleukin-2 production [IMP]
- positive regulation of protein homodimerization activity [IMP]
- positive regulation of sequence-specific DNA binding transcription factor activity [IMP]
- protein K63-linked ubiquitination [IDA]
- protein autoubiquitination [IDA, TAS]
- protein complex assembly [TAS]
- protein homotrimerization [IPI]
- regulation of apoptotic process [IDA]
- regulation of extrinsic apoptotic signaling pathway in absence of ligand [TAS]
- signal transduction [TAS]
- tumor necrosis factor-mediated signaling pathway [IDA]
Gene Ontology Molecular Function- CD40 receptor binding [ISS]
- enzyme binding [IPI]
- identical protein binding [IPI]
- protein binding [IPI]
- protein phosphatase binding [IPI]
- signal transducer activity [NAS]
- sphingolipid binding [IDA]
- thioesterase binding [IPI]
- tumor necrosis factor receptor binding [IPI]
- ubiquitin protein ligase binding [IPI]
- ubiquitin-protein transferase activity [IDA]
- CD40 receptor binding [ISS]
- enzyme binding [IPI]
- identical protein binding [IPI]
- protein binding [IPI]
- protein phosphatase binding [IPI]
- signal transducer activity [NAS]
- sphingolipid binding [IDA]
- thioesterase binding [IPI]
- tumor necrosis factor receptor binding [IPI]
- ubiquitin protein ligase binding [IPI]
- ubiquitin-protein transferase activity [IDA]
Gene Ontology Cellular Component
ELAVL1
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
IL-17 promotes melanoma through TRAF2 as a scaffold protein recruiting PIAS2 and ELAVL1 to induce EPHA5.
An abnormal immune response induces melanoma development. IL-17 and the classical downstream signal STAT1 are associated with melanoma development. TRAF2 also mediates the downstream signaling of IL-17; however, its role in IL-17-stimulated melanoma remains unclear. Bioinformatic analysis revealed that TRAF2 can bind to PIAS2 (a SUMO E3 ligase), ELAVL1 (an RNA-binding protein), and EPHA5 (an ephrin receptor of the tyrosine ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRAF2 ELAVL1 | 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 | - |
Curated By
- BioGRID