MKL1
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
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.
Publication
A novel role of Brg1 in the regulation of SRF/MRTFA-dependent smooth muscle-specific gene expression.
Serum response factor (SRF) is a key regulator of smooth muscle differentiation, proliferation, and migration. Myocardin-related transcription factor A (MRTFA) is a co-activator of SRF that can induce expression of SRF-dependent, smooth muscle-specific genes and actin/Rho-dependent genes, but not MAPK-regulated growth response genes. How MRTFA and SRF discriminate between these sets of target genes is still unclear. We hypothesized that ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| MKL1 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