RIOK1
RPS19
Gene Ontology Biological Process
- RNA metabolic process [TAS]
- SRP-dependent cotranslational protein targeting to membrane [TAS]
- cellular protein metabolic process [TAS]
- erythrocyte differentiation [IMP]
- gene expression [TAS]
- mRNA metabolic process [TAS]
- maturation of SSU-rRNA [IMP]
- maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
- monocyte chemotaxis [IDA]
- negative regulation of respiratory burst involved in inflammatory response [IDA]
- nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [TAS]
- nucleolus organization [IMP]
- positive regulation of cellular component movement [TAS]
- positive regulation of respiratory burst involved in inflammatory response [IDA]
- protein tetramerization [IDA]
- rRNA processing [IMP]
- response to extracellular stimulus [TAS]
- ribosomal small subunit assembly [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
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.
Publication
RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity.
Protein arginine methylation plays a critical role in differential gene expression through modulating protein-protein and protein-DNA/RNA interactions. Although numerous proteins undergo arginine methylation, only limited information is available on how protein arginine methyltransferases (PRMTs) identify their substrates. The human PRMT5 complex consists of PRMT5, WD45/MEP50 (WD repeat domain 45/methylosome protein 50), and pICln and catalyzes the symmetrical arginine dimethylation of ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RIOK1 RPS19 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 3644903 |
Curated By
- BioGRID