BAIT
UBE2M
UBC-RS2, UBC12, hUbc12
ubiquitin-conjugating enzyme E2M
GO Process (4)
GO Function (6)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Homo sapiens
PREY
XRCC5
KARP-1, KARP1, KU80, KUB2, Ku86, NFIV
X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining)
GO Process (10)
GO Function (10)
GO Component (9)
Gene Ontology Biological Process
- DNA duplex unwinding [TAS]
- DNA repair [TAS]
- double-strand break repair [TAS]
- double-strand break repair via nonhomologous end joining [IMP, TAS]
- establishment of integrated proviral latency [TAS]
- innate immune response [TAS]
- negative regulation of transcription, DNA-templated [IMP]
- positive regulation of type I interferon production [TAS]
- telomere maintenance [TAS]
- viral process [TAS]
Gene Ontology Molecular Function- 5'-deoxyribose-5-phosphate lyase activity [IMP]
- DNA binding [NAS]
- double-stranded DNA binding [TAS]
- double-stranded telomeric DNA binding [IDA]
- poly(A) RNA binding [IDA]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- telomeric DNA binding [IDA]
- transcription regulatory region DNA binding [IDA]
- ubiquitin protein ligase binding [IPI]
- 5'-deoxyribose-5-phosphate lyase activity [IMP]
- DNA binding [NAS]
- double-stranded DNA binding [TAS]
- double-stranded telomeric DNA binding [IDA]
- poly(A) RNA binding [IDA]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- telomeric DNA binding [IDA]
- transcription regulatory region DNA binding [IDA]
- ubiquitin protein ligase binding [IPI]
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
Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase.
N-terminal acetylation is an abundant modification influencing protein functions. Because ∼80% of mammalian cytosolic proteins are N-terminally acetylated, this modification is potentially an untapped target for chemical control of their functions. Structural studies have revealed that, like lysine acetylation, N-terminal acetylation converts a positively charged amine into a hydrophobic handle that mediates protein interactions; hence, this modification may be a ... [more]
Nat. Chem. Biol. Aug. 01, 2017; 13(8);850-857 [Pubmed: 28581483]
Throughput
- High Throughput
Curated By
- BioGRID