EP300
Gene Ontology Biological Process
- G2/M transition of mitotic cell cycle [TAS]
- N-terminal peptidyl-lysine acetylation [IDA]
- Notch signaling pathway [TAS]
- apoptotic process [IMP]
- cellular response to hypoxia [TAS]
- chromatin organization [TAS]
- circadian rhythm [ISS]
- histone H2B acetylation [IDA]
- histone H4 acetylation [IMP]
- innate immune response [TAS]
- internal peptidyl-lysine acetylation [IDA]
- internal protein amino acid acetylation [IDA]
- intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [IDA]
- mitotic cell cycle [TAS]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- nervous system development [TAS]
- positive regulation by host of viral transcription [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response [ISS]
- positive regulation of type I interferon production [TAS]
- protein stabilization [ISS]
- regulation of androgen receptor signaling pathway [IDA]
- regulation of cell cycle [TAS]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- regulation of transcription, DNA-templated [IDA]
- regulation of tubulin deacetylation [IDA]
- response to estrogen [IDA]
- response to hypoxia [IDA]
Gene Ontology Molecular Function- DNA binding [IDA]
- RNA polymerase II activating transcription factor binding [IPI]
- acetyltransferase activity [IDA, IMP]
- activating transcription factor binding [IPI]
- androgen receptor binding [IPI]
- beta-catenin binding [IPI]
- chromatin binding [IMP]
- core promoter binding [IDA]
- histone acetyltransferase activity [IDA]
- lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [IDA]
- nuclear hormone receptor binding [IPI]
- protein binding [IPI]
- transcription coactivator activity [IDA]
- transcription factor binding [IPI]
- transferase activity, transferring acyl groups [IDA]
- DNA binding [IDA]
- RNA polymerase II activating transcription factor binding [IPI]
- acetyltransferase activity [IDA, IMP]
- activating transcription factor binding [IPI]
- androgen receptor binding [IPI]
- beta-catenin binding [IPI]
- chromatin binding [IMP]
- core promoter binding [IDA]
- histone acetyltransferase activity [IDA]
- lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [IDA]
- nuclear hormone receptor binding [IPI]
- protein binding [IPI]
- transcription coactivator activity [IDA]
- transcription factor binding [IPI]
- transferase activity, transferring acyl groups [IDA]
NEUROD1
Gene Ontology Biological Process
- amacrine cell differentiation [ISS]
- cerebellum development [ISS]
- dentate gyrus development [ISS]
- embryonic organ morphogenesis [ISS]
- endocrine pancreas development [ISS, TAS]
- enteroendocrine cell differentiation [ISS]
- glucose homeostasis [ISS]
- inner ear development [ISS]
- insulin secretion [IDA]
- negative regulation of type B pancreatic cell apoptotic process [ISS]
- neurogenesis [TAS]
- nitric oxide mediated signal transduction [IDA]
- positive regulation of apoptotic process [ISS]
- positive regulation of cell differentiation [ISS]
- positive regulation of neuron differentiation [ISS]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of transcription regulatory region DNA binding [IDA]
- positive regulation of transcription, DNA-templated [ISS]
- regulation of cell cycle arrest [ISS]
- regulation of insulin secretion [IC]
- regulation of intestinal epithelial structure maintenance [ISS]
- response to glucose [IMP]
Gene Ontology Molecular Function- E-box binding [IDA]
- RNA polymerase II activating transcription factor binding [IPI]
- RNA polymerase II transcription coactivator activity [IDA]
- chromatin binding [ISS]
- protein binding [IPI]
- protein heterodimerization activity [IDA, IPI]
- sequence-specific DNA binding [IDA]
- sequence-specific DNA binding transcription factor activity [IDA]
- transcription coactivator activity [IDA]
- transcription factor binding [IPI]
- E-box binding [IDA]
- RNA polymerase II activating transcription factor binding [IPI]
- RNA polymerase II transcription coactivator activity [IDA]
- chromatin binding [ISS]
- protein binding [IPI]
- protein heterodimerization activity [IDA, IPI]
- sequence-specific DNA binding [IDA]
- sequence-specific DNA binding transcription factor activity [IDA]
- transcription coactivator activity [IDA]
- transcription factor binding [IPI]
Gene Ontology Cellular Component
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
Insulin gene transcription is mediated by interactions between the p300 coactivator and PDX-1, BETA2, and E47.
Pancreatic beta-cell-type-specific expression of the insulin gene requires both ubiquitous and cell-enriched activators, which are organized within the enhancer region into a network of protein-protein and protein-DNA interactions to promote transcriptional synergy. Protein-protein-mediated communication between DNA-bound activators and the RNA polymerase II transcriptional machinery is inhibited by the adenovirus E1A protein as a result of E1A's binding to the p300 ... [more]
Throughput
- Low Throughput
Additional Notes
- Figure 8
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NEUROD1 EP300 | 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 | - | |
| EP300 NEUROD1 | 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 | - | |
| NEUROD1 EP300 | 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 | 1055582 |
Curated By
- BioGRID