RBBP4
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- ATP-dependent chromatin remodeling [IDA]
- CENP-A containing nucleosome assembly [TAS]
- DNA replication-dependent nucleosome assembly [IDA]
- DNA replication-independent nucleosome assembly [IDA]
- G2/M transition of mitotic cell cycle [TAS]
- chromatin assembly [IDA]
- chromatin remodeling [IDA]
- mitotic cell cycle [TAS]
- negative regulation of cell proliferation [TAS]
- nucleosome assembly [TAS]
- regulation of cell cycle [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
BCL11A
Gene Ontology Biological Process
- negative regulation of axon extension [ISS]
- negative regulation of collateral sprouting [IMP]
- negative regulation of dendrite development [IMP]
- negative regulation of neuron projection development [IDA]
- negative regulation of protein homooligomerization [IC]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of collateral sprouting [IMP]
- positive regulation of neuron projection development [IDA]
- positive regulation of transcription from RNA polymerase II promoter [ISS]
- protein sumoylation [ISS]
- regulation of dendrite development [IMP]
Gene Ontology Molecular Function- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [IDA]
- protein heterodimerization activity [IPI]
- protein homodimerization activity [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [IDA]
- protein heterodimerization activity [IPI]
- protein homodimerization activity [TAS]
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.
Publication
Probing the interaction between the histone methyltransferase/deacetylase subunit RBBP4/7 and the transcription factor BCL11A in epigenetic complexes.
The transcription factor BCL11A has recently been reported to be a driving force in triple-negative breast cancer (TNBC), contributing to the maintenance of a chemoresistant breast cancer stem cell (BCSC) population. Although BCL11A was shown to suppress γ-globin and p21 and to induce MDM2 expression in the hematopoietic system, its downstream targets in TNBC are still unclear. For its role ... [more]
Throughput
- Low Throughput
Additional Notes
- crystal structure of BCL11A peptide bound to RBBP4 protein
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RBBP4 BCL11A | Affinity Capture-MS Affinity Capture-MS 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 is identified by mass spectrometric methods. | High | - | BioGRID | - | |
| RBBP4 BCL11A | Affinity Capture-MS Affinity Capture-MS 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 is identified by mass spectrometric methods. | High | 1 | BioGRID | 3039685 | |
| RBBP4 BCL11A | Affinity Capture-MS Affinity Capture-MS 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 is identified by mass spectrometric methods. | High | 22.4139 | BioGRID | 2945702 | |
| BCL11A RBBP4 | Affinity Capture-MS Affinity Capture-MS 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 is identified by mass spectrometric methods. | High | 0.9818 | BioGRID | 3832773 | |
| RBBP4 BCL11A | 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 | 2595062 | |
| BCL11A RBBP4 | 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 | 2595064 |
Curated By
- BioGRID