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
MTDH
3D3, AEG-1, AEG1, LYRIC, LYRIC/3D3
metadherin
GO Process (8)
GO Function (6)
GO Component (10)
Gene Ontology Biological Process
- lipopolysaccharide-mediated signaling pathway [IMP]
- negative regulation of apoptotic process [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- positive regulation of NF-kappaB transcription factor activity [IDA]
- positive regulation of angiogenesis [IDA]
- positive regulation of autophagy [IDA]
- positive regulation of protein kinase B signaling [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