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
RPL10A
CSA19, Csa-19, L10A, NEDD6
ribosomal protein L10a
GO Process (14)
GO Function (3)
GO Component (8)
Gene Ontology Biological Process
- RNA metabolic process [TAS]
- SRP-dependent cotranslational protein targeting to membrane [TAS]
- anatomical structure morphogenesis [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
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