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
DNAJA3
HCA57, TID1, hTID-1
DnaJ (Hsp40) homolog, subfamily A, member 3
GO Process (18)
GO Function (7)
GO Component (13)
Gene Ontology Biological Process
- activation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- mitochondrion organization [IBA]
- negative regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- negative regulation of NF-kappaB transcription factor activity [IDA]
- negative regulation of apoptotic process [IDA]
- negative regulation of cell proliferation [IDA]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- negative regulation of interferon-gamma-mediated signaling pathway [IDA]
- negative regulation of protein kinase activity [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- neuromuscular junction development [IDA]
- positive regulation of apoptotic process [IDA]
- positive regulation of protein ubiquitination [IDA]
- protein folding [IDA]
- protein refolding [IBA]
- protein stabilization [IDA]
- response to interferon-gamma [IDA]
- skeletal muscle acetylcholine-gated channel clustering [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- I-kappaB/NF-kappaB complex [IDA]
- IkappaB kinase complex [IDA]
- actin filament [IDA]
- cytoplasm [IDA]
- cytosol [IMP]
- extrinsic component of plasma membrane [ISS]
- intracellular membrane-bounded organelle [IDA]
- mitochondrial matrix [IDA]
- mitochondrial nucleoid [IDA]
- mitochondrion [IDA]
- neuromuscular junction [ISS]
- nucleus [IDA]
- postsynaptic membrane [ISS]
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