REL
Gene Ontology Biological Process
Gene Ontology Molecular Function- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [NAS]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [NAS]
Gene Ontology Cellular Component
- cytosol [TAS]
- nucleoplasm [TAS]
RELA
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- MyD88-dependent toll-like receptor signaling pathway [TAS]
- MyD88-independent toll-like receptor signaling pathway [TAS]
- T cell receptor signaling pathway [TAS]
- TRIF-dependent toll-like receptor signaling pathway [TAS]
- cellular defense response [NAS]
- cellular response to hydrogen peroxide [IDA]
- cellular response to interleukin-1 [IDA]
- cellular response to interleukin-6 [IMP]
- cellular response to nicotine [IMP]
- cellular response to peptide hormone stimulus [IMP]
- cellular response to tumor necrosis factor [IDA]
- cytokine-mediated signaling pathway [IDA]
- defense response to virus [NAS]
- inflammatory response [IDA]
- innate immune response [TAS]
- membrane protein intracellular domain proteolysis [TAS]
- negative regulation of apoptotic process [IDA, TAS]
- negative regulation of extrinsic apoptotic signaling pathway [IMP]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- neurotrophin TRK receptor signaling pathway [TAS]
- nucleotide-binding oligomerization domain containing 2 signaling pathway [IDA]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IEP]
- positive regulation of NF-kappaB transcription factor activity [IDA, TAS]
- positive regulation of cell proliferation [IDA]
- positive regulation of miRNA metabolic process [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription, DNA-templated [IDA]
- positive regulation of type I interferon production [TAS]
- regulation of inflammatory response [ISS]
- response to UV-B [IDA]
- response to interleukin-1 [IGI]
- response to organic substance [IDA]
- toll-like receptor 10 signaling pathway [TAS]
- toll-like receptor 2 signaling pathway [TAS]
- toll-like receptor 3 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor 5 signaling pathway [TAS]
- toll-like receptor 9 signaling pathway [TAS]
- toll-like receptor TLR1:TLR2 signaling pathway [TAS]
- toll-like receptor TLR6:TLR2 signaling pathway [TAS]
- toll-like receptor signaling pathway [TAS]
Gene Ontology Molecular Function- DNA binding [IDA]
- NF-kappaB binding [IPI]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA]
- activating transcription factor binding [IPI]
- chromatin binding [IDA]
- identical protein binding [IDA, IPI]
- phosphate ion binding [IDA]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein kinase binding [IPI]
- repressing transcription factor binding [IPI]
- sequence-specific DNA binding transcription factor activity [IDA]
- transcription factor binding [IPI]
- transcription regulatory region DNA binding [IDA]
- ubiquitin protein ligase binding [IPI]
- DNA binding [IDA]
- NF-kappaB binding [IPI]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA]
- activating transcription factor binding [IPI]
- chromatin binding [IDA]
- identical protein binding [IDA, IPI]
- phosphate ion binding [IDA]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein kinase binding [IPI]
- repressing transcription factor binding [IPI]
- sequence-specific DNA binding transcription factor activity [IDA]
- transcription factor binding [IPI]
- transcription regulatory region DNA binding [IDA]
- ubiquitin protein ligase binding [IPI]
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.
Publication
Mutational analysis of the v-Rel dimerization interface reveals a critical role for v-Rel homodimers in transformation.
The v-rel oncogene encoded by reticuloendotheliosis virus strain T is the acutely transforming member of the Rel/NF-kappaB family of transcription factors. In v-Rel-transformed cells, v-Rel exists as homodimers or heterodimers with the endogenous Rel/NF-kappaB proteins c-Rel, NF-kappaB1, NF-kappaB2, and RelA. To examine the contribution of these complexes to v-Rel-mediated transformation, mutations were introduced into the dimerization interface of v-Rel to ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| REL RELA | Affinity Capture-MS 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. | High | - | BioGRID | - | |
| RELA REL | Affinity Capture-MS 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. | High | - | BioGRID | - | |
| RELA REL | Affinity Capture-MS 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. | Low | - | BioGRID | 2474333 | |
| REL RELA | Affinity Capture-MS 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. | High | - | BioGRID | - | |
| RELA REL | Affinity Capture-MS 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. | High | - | BioGRID | - | |
| RELA REL | Affinity Capture-MS 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. | High | - | BioGRID | 3367244 | |
| REL RELA | Affinity Capture-MS 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. | High | 1 | BioGRID | 1198067 | |
| REL RELA | Affinity Capture-MS 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. | High | 1 | BioGRID | 2219129 | |
| REL RELA | Affinity Capture-MS 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. | High | 1 | BioGRID | 3081719 | |
| RELA REL | 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 | - | |
| RELA REL | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | - | BioGRID | 3448634 | |
| REL RELA | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
| REL RELA | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
| REL RELA | 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 | - | |
| RELA REL | 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 | - |
Curated By
- BioGRID