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
EEF2
Gene Ontology Biological Process
Gene Ontology Molecular Function
Cross-Linking-MS (XL-MS)
An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071).
Publication
Exploring an Alternative Cysteine-Reactive Chemistry to Enable Proteome-Wide PPI Analysis by Cross-Linking Mass Spectrometry.
The development of MS-cleavable cross-linking mass spectrometry (XL-MS) has enabled the effective capture and identification of endogenous protein-protein interactions (PPIs) and their residue contacts at the global scale without cell engineering. So far, only lysine-reactive cross-linkers have been successfully applied for proteome-wide PPI profiling. However, lysine cross-linkers alone cannot uncover the complete PPI map in cells. Previously, we have developed ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| EEF2 FLNA | Co-fractionation 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. | High | - | BioGRID | 3438035 |
Curated By
- BioGRID