BAIT
C9ORF78
HCA59, HSPC220, bA409K20.3
chromosome 9 open reading frame 78
GO Process (0)
GO Function (0)
GO Component (2)
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
A multi-factor trafficking site on the spliceosome remodeling enzyme BRR2 recruits C9ORF78 to regulate alternative splicing.
The intrinsically unstructured C9ORF78 protein was detected in spliceosomes but its role in splicing is presently unclear. We find that C9ORF78 tightly interacts with the spliceosome remodeling factor, BRR2, in vitro. Affinity purification/mass spectrometry and RNA UV-crosslinking analyses identify additional C9ORF78 interactors in spliceosomes. Cryogenic electron microscopy structures reveal how C9ORF78 and the spliceosomal B complex protein, FBP21, wrap around ... [more]
Nat Commun Dec. 03, 2021; 13(1);1132 [Pubmed: 35241646]
Throughput
- High Throughput
Curated By
- BioGRID