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
SEC31A
ABP125, ABP130, HSPC334, SEC31L1, HSPC275
SEC31 homolog A (S. cerevisiae)
GO Process (11)
GO Function (2)
GO Component (12)
Gene Ontology Biological Process
- COPII vesicle coating [TAS]
- ER to Golgi vesicle-mediated transport [NAS, TAS]
- activation of signaling protein activity involved in unfolded protein response [TAS]
- antigen processing and presentation of exogenous peptide antigen via MHC class II [TAS]
- antigen processing and presentation of peptide antigen via MHC class I [TAS]
- cellular protein metabolic process [TAS]
- endoplasmic reticulum unfolded protein response [TAS]
- membrane organization [TAS]
- post-translational protein modification [TAS]
- protein N-linked glycosylation via asparagine [TAS]
- response to calcium ion [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- COPII vesicle coat [NAS]
- ER to Golgi transport vesicle [IDA]
- ER to Golgi transport vesicle membrane [TAS]
- Golgi membrane [TAS]
- cytoplasm [IDA]
- cytosol [TAS]
- endoplasmic reticulum [IDA]
- endoplasmic reticulum exit site [IMP]
- endoplasmic reticulum membrane [TAS]
- intracellular membrane-bounded organelle [IDA]
- perinuclear region of cytoplasm [IDA]
- vesicle coat [IDA]
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