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]
UBTF
Gene Ontology Biological Process
- chromatin remodeling [IBA]
- gene expression [TAS]
- positive regulation of transcription from RNA polymerase I promoter [ISS]
- regulation of transcription from RNA polymerase I promoter [TAS]
- regulation of transcription, DNA-templated [IBA]
- termination of RNA polymerase I transcription [TAS]
- transcription elongation from RNA polymerase I promoter [TAS]
- transcription from RNA polymerase I promoter [TAS]
- transcription initiation from RNA polymerase I promoter [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- nucleolus [IDA, ISS]
- nucleoplasm [TAS]
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
DNA-dependent acetylation of p53 by the transcription coactivator p300.
Reconstitution of the stages in the assembly of the p300.p53 transcription complex has identified a novel type of DNA-dependent regulation of p300-catalyzed acetylation. Phosphorylation at the CHK2 site (Ser(20)) in the N-terminal activation domain of p53 stabilized p300 binding. The phosphopeptide binding activity of p300 was mapped in vitro to two domains: the C-terminal IBiD domain and the N-terminal IHD ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID