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
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
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8).
Ubiquitin-specific protease 8 (USP8) hydrolyzes mono and polyubiquitylated targets such as epidermal growth factor receptors and is involved in clathrin-mediated internalization. In 1182 residues, USP8 contains multiple domains, including coiled-coil, rhodanese, and catalytic domains. We report the first high-resolution crystal structures of these domains and discuss their implications for USP8 function. The amino-terminal domain is a homodimer with a novel ... [more]
Throughput
- Low Throughput
Additional Notes
- dimerization shown only using N-terminal peptide
Curated By
- BioGRID