BAIT
SNRNP70
RNPU1Z, RPU1, SNRP70, Snp1, U1-70K, U170K, U1AP, U1RNP
small nuclear ribonucleoprotein 70kDa (U1)
GO Process (5)
GO Function (3)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
RNA-binding proteins with basic-acidic dipeptide (BAD) domains self-assemble and aggregate in Alzheimer's disease.
The U1 small nuclear ribonucleoprotein 70 kDa (U1-70K) and other RNA-binding proteins (RBPs) are mislocalized to cytoplasmic neurofibrillary Tau aggregates in Alzheimer's disease (AD), yet the co-aggregation mechanisms are incompletely understood. U1-70K harbors two disordered low-complexity domains (LC1 and LC2) that are necessary for aggregation in AD brain extracts. The LC1 domain contains highly repetitive basic (Arg/Lys) and acidic (Asp/Glu) ... [more]
J. Biol. Chem. Dec. 13, 2017; 293(28);11047-11066 [Pubmed: 29802200]
Throughput
- High Throughput
Curated By
- BioGRID