BAIT
WDR77
MEP-50, MEP50, Nbla10071, p44, p44/Mep50, HKMT1069
WD repeat domain 77
GO Process (4)
GO Function (2)
GO Component (6)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- Golgi apparatus [IDA]
- cytoplasm [IDA, IGI]
- cytosol [IDA, TAS]
- methylosome [IDA]
- nucleoplasm [IDA]
- nucleus [IGI]
Homo sapiens
PREY
RPSA
37LRP, 67LR, ICAS, LAMBR, LAMR1, LBP, LBP/p40, LRP, LRP/LR, NEM/1CHD4, SA, lamR, p40
ribosomal protein SA
GO Process (17)
GO Function (4)
GO Component (8)
Gene Ontology Biological Process
- RNA metabolic process [TAS]
- SRP-dependent cotranslational protein targeting to membrane [TAS]
- cellular protein metabolic process [TAS]
- endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IBA]
- endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IBA]
- gene expression [TAS]
- mRNA metabolic process [TAS]
- nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [TAS]
- rRNA export from nucleus [IBA]
- ribosomal small subunit assembly [IBA]
- translation [IBA, IC, TAS]
- translational elongation [TAS]
- translational initiation [TAS]
- translational termination [TAS]
- viral life cycle [TAS]
- viral process [TAS]
- viral transcription [TAS]
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
The PRMT5/WDR77 complex regulates alternative splicing through ZNF326 in breast cancer.
We observed overexpression and increased intra-nuclear accumulation of the PRMT5/WDR77 in breast cancer cell lines relative to immortalized breast epithelial cells. Utilizing mass spectrometry and biochemistry approaches we identified the Zn-finger protein ZNF326, as a novel interaction partner and substrate of the nuclear PRMT5/WDR77 complex. ZNF326 is symmetrically dimethylated at arginine 175 (R175) and this modification is lost in a ... [more]
Nucleic Acids Res. Nov. 02, 2017; 45(19);11106-11120 [Pubmed: 28977470]
Throughput
- High Throughput
Curated By
- BioGRID