MYB
Gene Ontology Biological Process
- blood coagulation [TAS]
- chromatin remodeling [IMP]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- negative regulation of transcription, DNA-templated [IMP]
- positive regulation of T-helper cell differentiation [IMP]
- positive regulation of histone H3-K4 methylation [IMP]
- positive regulation of histone H3-K9 methylation [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription, DNA-templated [IMP, NAS]
- regulation of transcription, DNA-templated [NAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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]
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.
Publication
Inhibition of cyclin A/Cdk2 phosphorylation impairs B-Myb transactivation function without affecting interactions with DNA or the CBP coactivator.
Expression of the B-Myb transcription factor is directed by an E2F-dependent transcriptional mechanism to late G1 and S phases of the cell cycle, where its transactivation properties are enhanced post-translationally by cyclin A/Cdk2-mediated phosphorylation. Other experiments have shown that removal of the B-Myb C-terminus constitutively activates both transactivation and DNA-binding activities, suggesting that autoregulation by this inhibitory domain is counteracted ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CREBBP MYB | 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 MYB | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 511487 | |
| CREBBP MYB | 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 | - | |
| CREBBP MYB | 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 | 263365 | |
| MYB CREBBP | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | 3316943 | |
| CREBBP MYB | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
| CREBBP MYB | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
| CREBBP MYB | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
| CREBBP MYB | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
| CREBBP MYB | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - |
Curated By
- BioGRID