RPL6
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]
- regulation of transcription, DNA-templated [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
DST
Gene Ontology Biological Process
- cell motility [IMP]
- cytoskeleton organization [IMP]
- extracellular matrix organization [TAS]
- hemidesmosome assembly [IDA]
- integrin-mediated signaling pathway [NAS]
- intermediate filament cytoskeleton organization [IEP, ISS, NAS]
- maintenance of cell polarity [IMP]
- microtubule cytoskeleton organization [IDA]
- response to wounding [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- Z disc [IDA]
- actin cytoskeleton [IDA]
- axon [IDA]
- basal plasma membrane [NAS]
- basement membrane [TAS]
- cell leading edge [IDA]
- cytoplasm [IDA, ISS]
- cytoplasmic membrane-bounded vesicle [IDA]
- cytosol [TAS]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- hemidesmosome [IDA, TAS]
- intermediate filament cytoskeleton [IDA]
- microtubule cytoskeleton [IDA]
- microtubule plus-end [IDA]
- nucleus [IDA]
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
Cross-linking mass spectrometry discovers, evaluates, and corroborates structures and protein-protein interactions in the human cell.
Significant recent advances in structural biology, particularly in the field of cryoelectron microscopy, have dramatically expanded our ability to create structural models of proteins and protein complexes. However, many proteins remain refractory to these approaches because of their low abundance, low stability, or-in the case of complexes-simply not having yet been analyzed. Here, we demonstrate the power of using cross-linking ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RPL6 DST | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | 2785204 |
Curated By
- BioGRID