ETS1
Gene Ontology Biological Process
- PML body organization [IDA]
- cell motility [IMP]
- immune response [TAS]
- negative regulation of cell cycle [IDA, IMP]
- negative regulation of cell proliferation [TAS]
- positive regulation of cellular component movement [IMP]
- positive regulation of endothelial cell migration [IMP]
- positive regulation of erythrocyte differentiation [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of transcription, DNA-templated [IDA]
- regulation of angiogenesis [IMP]
- regulation of apoptotic process [IDA]
- response to antibiotic [IDA]
- transcription from RNA polymerase II promoter [IBA, IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
CREBBP
Gene Ontology Biological Process
- N-terminal peptidyl-lysine acetylation [IDA]
- Notch signaling pathway [TAS]
- cellular lipid metabolic process [TAS]
- cellular response to hypoxia [TAS]
- chromatin organization [TAS]
- embryonic digit morphogenesis [TAS]
- gene expression [TAS]
- histone acetylation [IDA]
- homeostatic process [NAS]
- innate immune response [TAS]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of transcription, DNA-templated [IDA, ISS]
- positive regulation of type I interferon production [TAS]
- protein complex assembly [TAS]
- regulation of smoothened signaling pathway [TAS]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- regulation of transcription, DNA-templated [IDA, TAS]
- response to hypoxia [TAS]
- signal transduction [NAS]
- small molecule metabolic process [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
Gene Ontology Molecular Function- MRF binding [IDA]
- RNA polymerase II activating transcription factor binding [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [IDA]
- RNA polymerase II transcription coactivator activity [TAS]
- RNA polymerase II transcription factor binding [IPI]
- RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription [IDA]
- acetyltransferase activity [IDA]
- core promoter proximal region sequence-specific DNA binding [IDA]
- histone acetyltransferase activity [IDA]
- p53 binding [IPI]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [TAS]
- signal transducer activity [TAS]
- transcription coactivator activity [IDA, IPI]
- transcription factor binding [IPI]
- MRF binding [IDA]
- RNA polymerase II activating transcription factor binding [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [IDA]
- RNA polymerase II transcription coactivator activity [TAS]
- RNA polymerase II transcription factor binding [IPI]
- RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription [IDA]
- acetyltransferase activity [IDA]
- core promoter proximal region sequence-specific DNA binding [IDA]
- histone acetyltransferase activity [IDA]
- p53 binding [IPI]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [TAS]
- signal transducer activity [TAS]
- transcription coactivator activity [IDA, IPI]
- transcription factor binding [IPI]
Gene Ontology Cellular Component
- cytoplasm [IDA]
- nuclear body [IDA]
- nuclear chromatin [IDA]
- nucleoplasm [IDA, TAS]
- nucleus [IC, IDA]
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.
Publication
Assembly and function of a TCR alpha enhancer complex is dependent on LEF-1-induced DNA bending and multiple protein-protein interactions.
In this study we examine the molecular basis for the synergistic regulation of the minimal TCR alpha enhancer by multiple proteins. We find that reconstitution of TCR alpha enhancer function in nonlymphoid cells requires expression of the lymphoid-specific proteins LEF-1, Ets-1 and PEBP2 alpha (CBF alpha), and a specific arrangement of their binding sites in the enhancer. We show that ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CREBBP ETS1 | 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 | 1053975 | |
| ETS1 CREBBP | 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 | - | |
| ETS1 CREBBP | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | - | |
| ETS1 CREBBP | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | 3313923 | |
| ETS1 CREBBP | 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 | - | |
| CREBBP ETS1 | 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 | - |
Curated By
- BioGRID