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
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]
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
p300/cAMP-responsive element-binding protein interactions with ets-1 and ets-2 in the transcriptional activation of the human stromelysin promoter.
In this paper we show that transcription factors Ets-1 and Ets-2 recruit transcription adapter proteins p300 and CBP (cAMP-responsive element-binding protein) during the transcriptional activation of the human stromelysin promoter, which contains palindromic Ets-binding sites. Ets-2 and p300/CBP exist as a complex in vivo. Two regions of p300/CBP between amino acids (a.a.) 328 and 596 and a. a. 1678 and ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| EP300 ETS1 | Phenotypic Enhancement Phenotypic Enhancement A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | BioGRID | - | |
| ETS1 EP300 | 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 | - | |
| EP300 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