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
PCNA
ATLD2
proliferating cell nuclear antigen
GO Process (18)
GO Function (8)
GO Component (9)
Gene Ontology Biological Process
- DNA repair [TAS]
- DNA strand elongation involved in DNA replication [TAS]
- G1/S transition of mitotic cell cycle [TAS]
- base-excision repair [TAS]
- cell proliferation [TAS]
- epithelial cell differentiation [IEP]
- leading strand elongation [IBA]
- mismatch repair [IDA]
- mitotic cell cycle [TAS]
- nucleotide-excision repair [TAS]
- nucleotide-excision repair, DNA gap filling [TAS]
- positive regulation of deoxyribonuclease activity [IDA]
- regulation of transcription involved in G1/S transition of mitotic cell cycle [TAS]
- telomere maintenance [TAS]
- telomere maintenance via recombination [TAS]
- telomere maintenance via semi-conservative replication [TAS]
- transcription-coupled nucleotide-excision repair [TAS]
- translesion synthesis [IDA]
Gene Ontology Molecular Function- DNA polymerase binding [IPI]
- DNA polymerase processivity factor activity [IBA]
- MutLalpha complex binding [IDA]
- dinucleotide insertion or deletion binding [IDA]
- identical protein binding [IPI]
- protein binding [IPI]
- purine-specific mismatch base pair DNA N-glycosylase activity [IDA]
- receptor tyrosine kinase binding [IPI]
- DNA polymerase binding [IPI]
- DNA polymerase processivity factor activity [IBA]
- MutLalpha complex binding [IDA]
- dinucleotide insertion or deletion binding [IDA]
- identical protein binding [IPI]
- protein binding [IPI]
- purine-specific mismatch base pair DNA N-glycosylase activity [IDA]
- receptor tyrosine kinase 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