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
EIF2AK2
EIF2AK1, PKR, PPP1R83, PRKR
eukaryotic translation initiation factor 2-alpha kinase 2
GO Process (22)
GO Function (7)
GO Component (4)
Gene Ontology Biological Process
- activation of MAPKK activity [IMP]
- evasion or tolerance by virus of host immune response [TAS]
- modulation by virus of host morphology or physiology [TAS]
- modulation by virus of host process [TAS]
- negative regulation of cell proliferation [TAS]
- negative regulation of osteoblast proliferation [IMP]
- negative regulation of translation [IDA, IMP]
- negative regulation of viral genome replication [IMP]
- positive regulation of NF-kappaB transcription factor activity [IDA]
- positive regulation of NIK/NF-kappaB signaling [ISS]
- positive regulation of chemokine production [ISS]
- positive regulation of cytokine production [ISS]
- positive regulation of stress-activated MAPK cascade [ISS]
- protein autophosphorylation [IDA, IMP]
- protein phosphorylation [IDA]
- regulation of NLRP3 inflammasome complex assembly [ISS]
- regulation of hematopoietic progenitor cell differentiation [ISS]
- regulation of hematopoietic stem cell differentiation [ISS]
- regulation of hematopoietic stem cell proliferation [ISS]
- response to interferon-alpha [IDA]
- response to virus [IMP]
- viral life cycle [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