PDLIM7
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
PCA
A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.
Publication
Characterization of the latent membrane protein 1 signaling complex of Epstein-Barr virus in the membrane of mammalian cells with bimolecular fluorescence complementation.
Bimolecular fluorescence complementation (BiFC) is a novel technique to examine protein-protein interaction through the assembly of fluorescent proteins. In the present study, BiFC was used to study the assembly of the Epstein-Barr virus latent membrane protein 1 (LMP1) signaling complex within the membrane of mammalian cells. LMP1 signaling requires oligomerization, localization to lipid rafts, and association of the cytoplasmic domain ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRAF2 PDLIM7 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | - |
Curated By
- BioGRID