CEBPA
Gene Ontology Biological Process
Gene Ontology Molecular Function
SMARCA4
Gene Ontology Biological Process
- ATP catabolic process [IGI]
- ATP-dependent chromatin remodeling [IDA]
- chromatin remodeling [IC, IDA]
- negative regulation of G1/S transition of mitotic cell cycle [TAS]
- negative regulation of androgen receptor signaling pathway [IMP]
- negative regulation of cell growth [IMP]
- negative regulation of transcription from RNA polymerase II promoter [TAS]
- negative regulation of transcription from RNA polymerase II promoter during mitosis [TAS]
- negative regulation of transcription, DNA-templated [IDA, IMP]
- neural retina development [IEP]
- nucleosome disassembly [IDA]
- positive regulation by host of viral transcription [IMP]
- positive regulation of Wnt signaling pathway [IMP]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IGI]
- positive regulation of transcription, DNA-templated [IMP]
- regulation of transcription from RNA polymerase II promoter [NAS]
Gene Ontology Molecular Function- DNA polymerase binding [IPI]
- DNA-dependent ATPase activity [IGI]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- RNA polymerase II transcription coactivator activity [IDA]
- Tat protein binding [IPI]
- androgen receptor binding [IPI]
- lysine-acetylated histone binding [IDA]
- nucleosomal DNA binding [IDA]
- p53 binding [IPI]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- transcription coactivator activity [IMP, NAS]
- transcription corepressor activity [IDA]
- DNA polymerase binding [IPI]
- DNA-dependent ATPase activity [IGI]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- RNA polymerase II transcription coactivator activity [IDA]
- Tat protein binding [IPI]
- androgen receptor binding [IPI]
- lysine-acetylated histone binding [IDA]
- nucleosomal DNA binding [IDA]
- p53 binding [IPI]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- transcription coactivator activity [IMP, NAS]
- transcription corepressor activity [IDA]
Gene Ontology Cellular Component
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.
Publication
PRISMA and BioID disclose a motifs-based interactome of the intrinsically disordered transcription factor C/EBP?.
C/EBP? represents a paradigm intrinsically disordered transcription factor containing short linear motifs and post-translational modifications (PTM). Unraveling C/EBP? protein interaction networks is a prerequisite for understanding the multi-modal functions of C/EBP? in hematopoiesis and leukemia. Here, we combined arrayed peptide matrix screening (PRISMA) with BioID to generate an in vivo validated and isoform specific interaction map of C/EBP?. The myeloid C/EBP? ... [more]
Throughput
- High Throughput
Additional Notes
- BioID
- FDR less than 0.05
- PRISMA method
- significance threshold (FDR less than 0.1)
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CEBPA SMARCA4 | 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 | - | |
| CEBPA SMARCA4 | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | High | - | BioGRID | 3695411 | |
| CEBPA SMARCA4 | 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 | - |
Curated By
- BioGRID