RPL14
Gene Ontology Biological Process
- RNA metabolic process [TAS]
- SRP-dependent cotranslational protein targeting to membrane [TAS]
- cellular protein metabolic process [TAS]
- gene expression [TAS]
- mRNA metabolic process [TAS]
- nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [TAS]
- rRNA processing [IMP]
- ribosomal large subunit biogenesis [IMP]
- translation [NAS, TAS]
- translational elongation [TAS]
- translational initiation [TAS]
- translational termination [TAS]
- viral life cycle [TAS]
- viral process [TAS]
- viral transcription [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
RPL24
Gene Ontology Biological Process
- RNA metabolic process [TAS]
- SRP-dependent cotranslational protein targeting to membrane [TAS]
- cellular protein metabolic process [TAS]
- gene expression [TAS]
- mRNA metabolic process [TAS]
- nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [TAS]
- translation [NAS, TAS]
- translational elongation [TAS]
- translational initiation [TAS]
- translational termination [TAS]
- viral life cycle [TAS]
- viral process [TAS]
- viral transcription [TAS]
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
Protein interaction landscapes revealed by advanced in vivo cross-linking-mass spectrometry.
Defining protein-protein interactions (PPIs) in their native environment is crucial to understanding protein structure and function. Cross-linking-mass spectrometry (XL-MS) has proven effective in capturing PPIs in living cells; however, the proteome coverage remains limited. Here, we have developed a robust in vivo XL-MS platform to facilitate in-depth PPI mapping by integrating a multifunctional MS-cleavable cross-linker with sample preparation strategies and ... [more]
Throughput
- High Throughput
Additional Notes
- In vivo cross-linking-mass spectrometry (XL-MS) was carried out in HEK-293 cells using the cross-linking reagent Alkyne-A-DSBSO (Azide/Alkyne-tagged, acid-cleavable disuccinimidyl bissulfoxide). High confidence protein interactions were identified based on cross-linked peptides having an FDR < 1%.
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
RPL14 RPL24 | 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 | 1 | BioGRID | 741963 | |
RPL14 RPL24 | 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 | 0.9941 | BioGRID | 1269533 | |
RPL14 RPL24 | 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 | - |
Curated By
- BioGRID