MYBL2
Gene Ontology Biological Process
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 positive regulation of transcription [IDA]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor 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 positive regulation of transcription [IDA]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [TAS]
Gene Ontology Cellular Component
- nucleoplasm [IDA, TAS]
FLNA
Gene Ontology Biological Process
- actin crosslink formation [IDA]
- actin cytoskeleton reorganization [IDA]
- adenylate cyclase-inhibiting dopamine receptor signaling pathway [IMP]
- blood coagulation [TAS]
- cell junction assembly [TAS]
- cilium assembly [IMP]
- cytoplasmic sequestering of protein [IMP]
- establishment of protein localization [IDA]
- negative regulation of protein catabolic process [IMP]
- negative regulation of sequence-specific DNA binding transcription factor activity [IDA]
- platelet activation [TAS]
- platelet aggregation [IMP]
- platelet degranulation [TAS]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IMP]
- positive regulation of transcription factor import into nucleus [IMP]
- protein localization to cell surface [IDA]
- protein stabilization [IMP]
- receptor clustering [IDA]
- spindle assembly involved in mitosis [IDA]
Gene Ontology Molecular Function- Fc-gamma receptor I complex binding [IDA]
- Rac GTPase binding [IDA]
- Ral GTPase binding [IDA]
- Rho GTPase binding [IDA]
- actin filament binding [IDA]
- glycoprotein binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein homodimerization activity [IDA]
- signal transducer activity [IMP]
- small GTPase binding [IDA]
- transcription factor binding [IPI]
- Fc-gamma receptor I complex binding [IDA]
- Rac GTPase binding [IDA]
- Ral GTPase binding [IDA]
- Rho GTPase binding [IDA]
- actin filament binding [IDA]
- glycoprotein binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein homodimerization activity [IDA]
- signal transducer activity [IMP]
- small GTPase binding [IDA]
- transcription factor binding [IPI]
Gene Ontology Cellular Component
Co-fractionation
Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.
Publication
A B-Myb complex containing clathrin and filamin is required for mitotic spindle function.
B-Myb is one member of the vertebrate Myb family of transcription factors and is ubiquitously expressed. B-Myb activates transcription of a group of genes required for the G2/M cell cycle transition by forming the dREAM/Myb-MuvB-like complex, which was originally identified in Drosophila. Mutants of zebrafish B-myb and Drosophila myb exhibit defects in cell cycle progression and genome instability. Although the ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| MYBL2 FLNA | 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. | Low | - | BioGRID | - | |
| MYBL2 FLNA | 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 | - |
Curated By
- BioGRID