FBXO2
Gene Ontology Biological Process
- ER-associated ubiquitin-dependent protein catabolic process [IDA]
- SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [IDA]
- glycoprotein catabolic process [IDA]
- negative regulation of cell proliferation [ISO]
- protein ubiquitination [IDA]
- regulation of protein ubiquitination [IDA]
- ubiquitin-dependent protein catabolic process [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
FBXO2
Gene Ontology Biological Process
- ER-associated ubiquitin-dependent protein catabolic process [IDA]
- SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [IDA]
- glycoprotein catabolic process [IDA]
- negative regulation of cell proliferation [ISO]
- protein ubiquitination [IDA]
- regulation of protein ubiquitination [IDA]
- ubiquitin-dependent protein catabolic process [IDA]
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
Structural analysis of a function-associated loop mutant of the substrate-recognition domain of Fbs1 ubiquitin ligase.
The SCF ubiquitin ligase comprises four components: Skp1, Cul1, Rbx1 and a variable-subunit F-box protein. The F-box protein Fbs1, which recognizes the N-linked glycoproteins, is involved in the endoplasmic reticulum-associated degradation pathway. Although FBG3, another F-box protein, shares 51% sequence identity with Fbs1, FBG3 does not bind glycoproteins. To investigate the sequence-structure relationship of the substrate-binding pocket, the crystal structure ... [more]
Throughput
- Low Throughput
Additional Notes
- dimer
Curated By
- BioGRID