BAIT
RIOK1
AD034, RRP10, bA288G3.1, RP11-288G3.1
RIO kinase 1
GO Process (0)
GO Function (0)
GO Component (0)
Homo sapiens
PREY
PPP2R1A
PP2A-Aalpha, PP2AAALPHA, PR65A
protein phosphatase 2, regulatory subunit A, alpha
GO Process (25)
GO Function (4)
GO Component (8)
Gene Ontology Biological Process
- G2/M transition of mitotic cell cycle [TAS]
- RNA metabolic process [TAS]
- RNA splicing [NAS]
- apoptotic process [TAS]
- ceramide metabolic process [NAS]
- chromosome segregation [IDA]
- fibroblast growth factor receptor signaling pathway [TAS]
- gene expression [TAS]
- inactivation of MAPK activity [NAS]
- mRNA metabolic process [TAS]
- mitotic cell cycle [TAS]
- mitotic nuclear envelope reassembly [TAS]
- negative regulation of cell growth [NAS]
- negative regulation of tyrosine phosphorylation of Stat3 protein [NAS]
- nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [TAS]
- protein complex assembly [TAS]
- protein dephosphorylation [TAS]
- regulation of DNA replication [NAS]
- regulation of Wnt signaling pathway [NAS]
- regulation of cell adhesion [NAS]
- regulation of cell differentiation [NAS]
- regulation of growth [NAS]
- regulation of transcription, DNA-templated [NAS]
- response to organic substance [NAS]
- second-messenger-mediated signaling [NAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
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]
J. Biol. Chem. Jan. 21, 2011; 286(3);1976-86 [Pubmed: 21081503]
Throughput
- High Throughput
Curated By
- BioGRID