TWIST1
Gene Ontology Biological Process
- aortic valve morphogenesis [IMP]
- cell proliferation involved in heart valve development [IMP]
- cellular response to hypoxia [IMP]
- cranial suture morphogenesis [TAS]
- embryonic camera-type eye formation [IMP]
- embryonic cranial skeleton morphogenesis [IMP]
- embryonic digit morphogenesis [TAS]
- eyelid development in camera-type eye [IMP]
- negative regulation of DNA damage response, signal transduction by p53 class mediator [IMP]
- negative regulation of cellular senescence [IMP]
- negative regulation of double-strand break repair [IMP]
- negative regulation of histone phosphorylation [IMP]
- negative regulation of osteoblast differentiation [IMP]
- negative regulation of phosphatidylinositol 3-kinase signaling [IMP]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- negative regulation of transcription, DNA-templated [ISS]
- ossification [TAS]
- outer ear morphogenesis [TAS]
- positive regulation of angiogenesis [NAS]
- positive regulation of cell motility [IMP, NAS]
- positive regulation of epithelial to mesenchymal transition [IMP]
- positive regulation of fatty acid beta-oxidation [IMP]
- positive regulation of gene expression [IMP]
- positive regulation of interleukin-6 secretion [IMP]
- positive regulation of monocyte chemotactic protein-1 production [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription regulatory region DNA binding [IMP]
- positive regulation of tumor necrosis factor production [IMP]
- regulation of bone mineralization [IMP]
- transcription from RNA polymerase II promoter [IDA]
Gene Ontology Molecular Function
KAT2B
Gene Ontology Biological Process
- N-terminal peptidyl-lysine acetylation [IDA]
- Notch signaling pathway [TAS]
- cell cycle arrest [TAS]
- cellular response to insulin stimulus [IDA]
- chromatin organization [TAS]
- chromatin remodeling [IDA, NAS]
- gene expression [TAS]
- histone H3 acetylation [IDA]
- internal peptidyl-lysine acetylation [IDA]
- negative regulation of cell proliferation [IDA]
- peptidyl-lysine acetylation [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- protein acetylation [TAS]
- regulation of protein ADP-ribosylation [IDA]
- transcription from RNA polymerase I promoter [TAS]
- transcription initiation from RNA polymerase I promoter [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
Gene Ontology Molecular Function- acetyltransferase activity [IDA]
- cyclin-dependent protein serine/threonine kinase inhibitor activity [ISS]
- histone acetyltransferase activity [IDA]
- histone deacetylase binding [IPI]
- lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [IDA, ISS]
- protein binding [IPI]
- protein complex binding [IDA]
- protein kinase binding [ISS]
- transcription coactivator activity [IDA]
- transcription cofactor activity [IPI]
- transcription factor binding [IPI]
- acetyltransferase activity [IDA]
- cyclin-dependent protein serine/threonine kinase inhibitor activity [ISS]
- histone acetyltransferase activity [IDA]
- histone deacetylase binding [IPI]
- lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [IDA, ISS]
- protein binding [IPI]
- protein complex binding [IDA]
- protein kinase binding [ISS]
- transcription coactivator activity [IDA]
- transcription cofactor activity [IPI]
- transcription factor binding [IPI]
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A.
Histone acetyltransferases (HAT) play a critical role in transcriptional control by relieving repressive effects of chromatin, and yet how HATs themselves are regulated remains largely unknown. Here, it is shown that Twist directly binds two independent HAT domains of acetyltransferases, p300 and p300/CBP-associated factor (PCAF), and directly regulates their HAT activities. The N terminus of Twist is a primary domain ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| KAT2B TWIST1 | 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 | - | |
| TWIST1 KAT2B | 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 | - | |
| TWIST1 KAT2B | 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 | - | |
| KAT2B TWIST1 | Phenotypic Suppression Phenotypic Suppression A genetic interaction is inferred when mutation or over expression of one gene results in suppression of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | BioGRID | - | |
| KAT2B TWIST1 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - |
Curated By
- BioGRID