USP8
Gene Ontology Biological Process
- cell proliferation [TAS]
- endosome organization [IMP]
- mitotic cytokinesis [IMP]
- proteasome-mediated ubiquitin-dependent protein catabolic process [IBA]
- protein K48-linked deubiquitination [IDA]
- protein K63-linked deubiquitination [IDA]
- protein deubiquitination [IMP]
- regulation of proteasomal protein catabolic process [IBA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
NBR1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover.
Nbr1, a ubiquitous kinase scaffold protein, contains a PB1, and a ubiquitin-associated (UBA) domain. We show here that the nbr1 UBA domain binds to lysine-48 and -63 linked polyubiquitin-B chains. Nbr1 also binds to the autophagic effector protein LC3-A via a novel binding site. Ubiquitin-binding, but not PB1-mediated p62/SQSTM1 interaction, is required to target nbr1 to LC3 and polyubiquitin-positive bodies. ... [more]
Throughput
- Low Throughput
Related interactions
Curated By
- BioGRID