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
ERCC8
CKN1, CSA, UVSS2
excision repair cross-complementation group 8
GO Process (10)
GO Function (5)
GO Component (6)
Gene Ontology Biological Process
- DNA repair [TAS]
- cellular response to DNA damage stimulus [IDA]
- nucleotide-excision repair [IMP, TAS]
- positive regulation of DNA repair [IMP]
- proteasome-mediated ubiquitin-dependent protein catabolic process [IDA]
- protein autoubiquitination [IDA]
- protein polyubiquitination [IDA]
- response to UV [IDA, IMP]
- response to oxidative stress [IDA, IMP]
- transcription-coupled nucleotide-excision repair [IDA, IMP, 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
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