UBE2M
Gene Ontology Biological Process
Gene Ontology Molecular Function
CFL1
Gene Ontology Biological Process
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- Rho protein signal transduction [TAS]
- actin cytoskeleton organization [TAS]
- axon guidance [TAS]
- blood coagulation [TAS]
- cytoskeleton organization [IMP]
- innate immune response [TAS]
- negative regulation of apoptotic process [TAS]
- platelet activation [TAS]
- platelet degranulation [TAS]
- regulation of cell morphogenesis [IMP]
- regulation of dendritic spine morphogenesis [IMP]
- response to virus [IEP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase.
N-terminal acetylation is an abundant modification influencing protein functions. Because ∼80% of mammalian cytosolic proteins are N-terminally acetylated, this modification is potentially an untapped target for chemical control of their functions. Structural studies have revealed that, like lysine acetylation, N-terminal acetylation converts a positively charged amine into a hydrophobic handle that mediates protein interactions; hence, this modification may be a ... [more]
Throughput
- High Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
UBE2M CFL1 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 2900394 |
Curated By
- BioGRID