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
C1QBP
GC1QBP, HABP1, SF2p32, gC1Q-R, gC1qR, p32
complement component 1, q subcomponent binding protein
GO Process (21)
GO Function (9)
GO Component (7)
Gene Ontology Biological Process
- blood coagulation [TAS]
- blood coagulation, intrinsic pathway [TAS]
- immune response [TAS]
- mature ribosome assembly [IMP]
- negative regulation of MDA-5 signaling pathway [IDA]
- negative regulation of RIG-I signaling pathway [IDA]
- negative regulation of defense response to virus [IMP]
- negative regulation of interferon-gamma production [IDA]
- negative regulation of interleukin-12 production [IDA]
- negative regulation of mRNA splicing, via spliceosome [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- phosphatidylinositol 3-kinase signaling [IMP]
- positive regulation of apoptotic process [IMP]
- positive regulation of cell adhesion [IMP]
- positive regulation of dendritic cell chemotaxis [IMP]
- positive regulation of mitochondrial translation [ISS]
- positive regulation of neutrophil chemotaxis [IDA]
- positive regulation of protein kinase B signaling [IMP]
- positive regulation of substrate adhesion-dependent cell spreading [IMP]
- positive regulation of trophoblast cell migration [IMP]
- regulation of complement activation [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
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