TRAF3
Gene Ontology Biological Process
- MyD88-independent toll-like receptor signaling pathway [TAS]
- TRIF-dependent toll-like receptor signaling pathway [TAS]
- innate immune response [TAS]
- negative regulation of NF-kappaB transcription factor activity [IMP]
- negative regulation of type I interferon production [TAS]
- regulation of cytokine production [ISS]
- regulation of defense response to virus [ISS]
- regulation of interferon-beta production [ISS]
- regulation of proteolysis [IMP]
- signal transduction [TAS]
- toll-like receptor 3 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor signaling pathway [ISS, TAS]
- tumor necrosis factor-mediated signaling pathway [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
TRAF3
Gene Ontology Biological Process
- MyD88-independent toll-like receptor signaling pathway [TAS]
- TRIF-dependent toll-like receptor signaling pathway [TAS]
- innate immune response [TAS]
- negative regulation of NF-kappaB transcription factor activity [IMP]
- negative regulation of type I interferon production [TAS]
- regulation of cytokine production [ISS]
- regulation of defense response to virus [ISS]
- regulation of interferon-beta production [ISS]
- regulation of proteolysis [IMP]
- signal transduction [TAS]
- toll-like receptor 3 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor signaling pathway [ISS, TAS]
- tumor necrosis factor-mediated signaling pathway [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
FRET
An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins.
Publication
TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NF-{kappa}B activation.
FRET experiments utilizing confocal microscopy or flow cytometry assessed homo- and heterotrimeric association of human tumor necrosis factor receptor-associated factors (TRAF) in living cells. Following transfection of HeLa cells with plasmids expressing CFP- or YFP-TRAF fusion proteins, constitutive homotypic association of TRAF2, -3, and -5 was observed, as well as heterotypic association of TRAF1-TRAF2 and TRAF3-TRAF5. A novel heterotypic association ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
TRAF3 TRAF3 | 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 | - | |
TRAF3 TRAF3 | 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 | - | |
TRAF3 TRAF3 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
TRAF3 TRAF3 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
TRAF3 TRAF3 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
TRAF3 TRAF3 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | 2722664 |
Curated By
- BioGRID