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
FLNC
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
Two-Dimensional Fractionation Method for Proteome-Wide Cross-Linking Mass Spectrometry Analysis.
Cross-linking mass spectrometry (XL-MS) is an emergent technology for studying protein-protein interactions (PPIs) and elucidating architectures of protein complexes. The development of various MS-cleavable cross-linkers has facilitated the identification of cross-linked peptides, enabling XL-MS studies at the systems level. However, the scope and depth of cellular networks revealed by current XL-MS technologies remain limited. Due to the inherently broad dynamic ... [more]
Throughput
- High Throughput
Additional Notes
- In vitro cross-linking-mass spectrometry (XL-MS) was carried out using HEK-293 cell lysates and the cross-linking reagent DSSO (disuccinimidyl sulfoxide). High confidence protein interactions were identified based on cross-linked peptides having an FDR =< 0.3%.
- In vitro cross-linking-mass spectrometry (XL-MS) was carried out using HEK-293 cell lysates and the cross-linking reagent DSSO (disuccinimidyl sulfoxide). High confidence protein interactions were identified based on cross-linked peptides having an FDR =< 0.3%.
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| FLNA FLNC | 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 | 3439801 | |
| FLNA FLNC | Cross-Linking-MS (XL-MS) 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). | High | - | BioGRID | 3720463 |
Curated By
- BioGRID