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
CLTC
CHC, CHC17, CLH-17, CLTCL2, Hc
clathrin, heavy chain (Hc)
GO Process (11)
GO Function (6)
GO Component (15)
Gene Ontology Biological Process
- antigen processing and presentation of exogenous peptide antigen via MHC class II [TAS]
- intracellular protein transport [NAS]
- membrane organization [TAS]
- mitotic nuclear division [IMP]
- negative regulation of hyaluronan biosynthetic process [IDA, IMP]
- negative regulation of protein localization to plasma membrane [IMP]
- osteoblast differentiation [IDA]
- post-Golgi vesicle-mediated transport [TAS]
- receptor internalization [IMP]
- receptor-mediated endocytosis [IMP]
- transferrin transport [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- clathrin coat [NAS]
- clathrin complex [IDA]
- clathrin-coated endocytic vesicle membrane [TAS]
- clathrin-coated vesicle [IDA]
- cytoplasm [IDA]
- cytosol [TAS]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- intracellular membrane-bounded organelle [IDA]
- membrane [IDA]
- plasma membrane [TAS]
- protein complex [IDA]
- spindle [IDA]
- trans-Golgi network membrane [TAS]
- vesicle [IDA]
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