RPL36
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
RPS6
Gene Ontology Biological Process
- RNA metabolic process [TAS]
- SRP-dependent cotranslational protein targeting to membrane [TAS]
- TOR signaling [IDA]
- cellular protein metabolic process [TAS]
- gene expression [TAS]
- glucose homeostasis [ISS]
- insulin receptor signaling pathway [TAS]
- mRNA metabolic process [TAS]
- nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [TAS]
- positive regulation of apoptotic process [IDA]
- rRNA processing [IMP]
- ribosomal small subunit biogenesis [IMP]
- translation [IC, TAS]
- translational elongation [TAS]
- translational initiation [TAS]
- translational termination [TAS]
- viral life cycle [TAS]
- viral process [TAS]
- viral transcription [TAS]
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 |
|---|---|---|---|---|---|---|
| RPL36 RPS6 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | 0.9906 | BioGRID | 3134789 | |
| RPL36 RPS6 | 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 | 0.768 | BioGRID | 743342 | |
| RPL36 RPS6 | 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 | 0.9961 | BioGRID | 1271276 | |
| RPS6 RPL36 | 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 | - |
Curated By
- BioGRID