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]
SUMO1
Gene Ontology Biological Process
- DNA repair [TAS]
- cellular protein metabolic process [TAS]
- cytokine-mediated signaling pathway [TAS]
- interferon-gamma-mediated signaling pathway [TAS]
- negative regulation of DNA binding [IMP]
- negative regulation of sequence-specific DNA binding transcription factor activity [IMP]
- negative regulation of transcription, DNA-templated [IDA, IMP]
- palate development [ISS]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- positive regulation of protein complex assembly [IDA]
- post-translational protein modification [TAS]
- protein sumoylation [IDA, TAS]
- regulation of interferon-gamma-mediated signaling pathway [TAS]
- regulation of protein localization [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
Role of the CBP catalytic core in intramolecular SUMOylation and control of histone H3 acetylation.
The histone acetyl transferases CREB-binding protein (CBP) and its paralog p300 play a critical role in numerous cellular processes. Dysregulation of their catalytic activity is associated with several human diseases. Previous work has elucidated the regulatory mechanisms of p300 acetyltransferase activity, but it is not known whether CBP activity is controlled similarly. Here, we present the crystal structure of the ... [more]
Throughput
- Low Throughput
Additional Notes
- #LPPI
- likely protein-protein interaction
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CREBBP SUMO1 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 1527391 | |
| CREBBP SUMO1 | 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 | 1527392 |
Curated By
- BioGRID