PREY
UBE2N
HEL-S-71, UBC13, UBCHBEN; UBC13, UbcH-ben, UbcH13
ubiquitin-conjugating enzyme E2N
GO Process (30)
GO Function (7)
GO Component (8)
Gene Ontology Biological Process
- DNA double-strand break processing [IMP]
- Fc-epsilon receptor signaling pathway [TAS]
- MyD88-dependent toll-like receptor signaling pathway [TAS]
- T cell receptor signaling pathway [IMP, TAS]
- cellular protein modification process [TAS]
- cytokine-mediated signaling pathway [TAS]
- double-strand break repair via homologous recombination [IMP]
- histone ubiquitination [IMP]
- innate immune response [TAS]
- nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [TAS]
- nucleotide-binding oligomerization domain containing signaling pathway [TAS]
- positive regulation of DNA repair [IMP]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IMP, TAS]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of histone modification [IMP]
- positive regulation of ubiquitin-protein transferase activity [IMP]
- postreplication repair [IMP]
- protein K63-linked ubiquitination [IDA]
- protein ubiquitination [IMP, TAS]
- proteolysis [TAS]
- regulation of DNA repair [TAS]
- regulation of histone ubiquitination [IMP]
- toll-like receptor 10 signaling pathway [TAS]
- toll-like receptor 2 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor 5 signaling pathway [TAS]
- toll-like receptor 9 signaling pathway [TAS]
- toll-like receptor TLR1:TLR2 signaling pathway [TAS]
- toll-like receptor TLR6:TLR2 signaling pathway [TAS]
- toll-like receptor signaling pathway [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
E3 ubiquitin ligase RNF123 targets lamin B1 and lamin-binding proteins.
Lamins are key nuclear proteins which are important for maintaining nuclear structure and function. Mutations in lamins cause a spectrum of genetic diseases termed as laminopathies. RING finger containing E3 ubiquitin ligase, RNF123, is transcriptionally upregulated in cells expressing rod domain lamin A mutations. However, the functional relevance of RNF123 in laminopathic cells is not clear. Using a mass spectrometry-based ... [more]
FEBS J. Jun. 01, 2018; 285(12);2243-2262 [Pubmed: 29676528]
Throughput
- High Throughput
Curated By
- BioGRID