PFN1
Gene Ontology Biological Process
- blood coagulation [TAS]
- negative regulation of actin filament bundle assembly [IMP]
- negative regulation of actin filament polymerization [IDA]
- negative regulation of stress fiber assembly [IMP]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of ATPase activity [IDA]
- positive regulation of actin filament polymerization [IGI]
- positive regulation of epithelial cell migration [IMP]
- positive regulation of ruffle assembly [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
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
Cysteine-enabled cleavability to advance cross-linking mass spectrometry for global analysis of endogenous protein-protein interactions.
Cross-linking mass spectrometry (XL-MS) is a powerful technology for probing protein-protein interactions (PPIs) and elucidating architectures of protein complexes at the systems level. While successful, the proteome coverage remains limited. To expand the scope of global PPI profiling, we introduce an innovative cysteine-based cleavable XL-MS platform using non-cleavable heterobifunctional lysine-cysteine (K-C) cross-linkers. The oxidation-induced transformation of cysteine cleavability enables unambiguous ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PFN1 CFL1 | 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 | 0.0905 | BioGRID | 1259928 |
Curated By
- BioGRID