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
ATP1A1
RP4-655J12.1
ATPase, Na+/K+ transporting, alpha 1 polypeptide
GO Process (14)
GO Function (4)
GO Component (10)
Gene Ontology Biological Process
- cardiac muscle contraction [TAS]
- cell communication by electrical coupling involved in cardiac conduction [TAS]
- cellular potassium ion homeostasis [IDA]
- cellular response to steroid hormone stimulus [IDA]
- cellular sodium ion homeostasis [IDA]
- ion transmembrane transport [TAS]
- membrane repolarization [IDA]
- membrane repolarization during cardiac muscle cell action potential [IC]
- potassium ion import [IDA]
- regulation of sodium ion transport [ISS]
- relaxation of cardiac muscle [TAS]
- response to glycoside [IDA]
- sodium ion export from cell [IDA]
- transmembrane transport [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