UniProt Summary: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates (PubMed:23886940, PubMed:27462458). Through an ubiquitination-dependent mechanism plays for instance a role in the incorporation of SLC11A2 into extracellular vesicles (PubMed:27462458). More generally, plays a role in the extracellular transport of proteins between cells through the release in the extracellular space of microvesicles (PubMed:22315426). By participating to the ITCH-mediated ubiquitination and subsequent degradation of NOTCH1, negatively regulates the NOTCH signaling pathway (PubMed:23886940). {ECO:0000269|PubMed:22315426, ECO:0000269|PubMed:23886940, ECO:0000269|PubMed:27462458}.
Pfam DomainsGO Terms
Pfam Domains
Arrestin C
Arrestin N
GO Terms
protein binding, bridging involved in substrate recognition for ubiquitination
extracellular vesicle biogenesis
arrestin family protein binding
extracellular transport
negative regulation of Notch signaling pathway
extracellular vesicle
regulation of Notch signaling pathway
cytoplasmic vesicle
ubiquitin protein ligase binding
ubiquitin-dependent protein catabolic process
modification-dependent protein catabolic process
modification-dependent macromolecule catabolic process
proteolysis involved in cellular protein catabolic process
cellular protein catabolic process
protein catabolic process
protein ubiquitination
protein modification by small protein conjugation
cellular macromolecule catabolic process
protein modification by small protein conjugation or removal
macromolecule catabolic process
organonitrogen compound catabolic process
identical protein binding
negative regulation of signal transduction
proteolysis
negative regulation of cell communication
negative regulation of signaling
protein transport
peptide transport
amide transport
establishment of protein localization
negative regulation of response to stimulus
organic substance catabolic process
cellular catabolic process
nitrogen compound transport
CRISPR Data
Compound HitMost Correlated Genes in ChemogenomicsTissues where Essential in the Avana Dataset (DepMap 20Q1)