BAIT
RIOK1
AD034, RRP10, bA288G3.1, RP11-288G3.1
RIO kinase 1
GO Process (0)
GO Function (0)
GO Component (0)
Homo sapiens
PREY
C1QBP
GC1QBP, HABP1, SF2p32, gC1Q-R, gC1qR, p32
complement component 1, q subcomponent binding protein
GO Process (21)
GO Function (9)
GO Component (7)
Gene Ontology Biological Process
- blood coagulation [TAS]
- blood coagulation, intrinsic pathway [TAS]
- immune response [TAS]
- mature ribosome assembly [IMP]
- negative regulation of MDA-5 signaling pathway [IDA]
- negative regulation of RIG-I signaling pathway [IDA]
- negative regulation of defense response to virus [IMP]
- negative regulation of interferon-gamma production [IDA]
- negative regulation of interleukin-12 production [IDA]
- negative regulation of mRNA splicing, via spliceosome [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- phosphatidylinositol 3-kinase signaling [IMP]
- positive regulation of apoptotic process [IMP]
- positive regulation of cell adhesion [IMP]
- positive regulation of dendritic cell chemotaxis [IMP]
- positive regulation of mitochondrial translation [ISS]
- positive regulation of neutrophil chemotaxis [IDA]
- positive regulation of protein kinase B signaling [IMP]
- positive regulation of substrate adhesion-dependent cell spreading [IMP]
- positive regulation of trophoblast cell migration [IMP]
- regulation of complement activation [IDA]
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