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 detected between purified proteins in vitro.
Publication
Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones.
The HIV-1 Tat protein is required for viral replication and is a potent stimulator of viral transcription. Although Tat has been extensively studied in various reductive paradigms, to date there is little information as to how this activator mediates transcription from natural nucleosomally packaged long terminal repeats. Here we show that CREB-binding protein (CBP)/p300 interacts with the HIV-1 Tat protein ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
CREBBP TAT | 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 | - | |
TAT 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 | - | |
CREBBP TAT | 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 | - | |
TAT 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 | 504177 | |
TAT CREBBP | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 1054475 | |
CREBBP TAT | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 483209 | |
TAT CREBBP | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 483210 |
Curated By
- BioGRID