biostudies-literatureKipreos ETNCI NIH HHSNIGMS NIH HHSREVIEWS3002https://www.ebi.ac.uk/biostudies/studies/S-EPMC138887biostudies-literatureUnknown1(5)<h4>Summary</h4>The F-box is a protein motif of approximately 50 amino acids that functions as a site of protein-protein interaction. F-box proteins were first characterized as components of SCF ubiquitin-ligase complexes (named after their main components, Skp I, Cullin, and an F-box protein), in which they bind substrates for ubiquitin-mediated proteolysis. The F-box motif links the F-box protein to other components of the SCF complex by binding the core SCF component Skp I. F-box proteins have more recently been discovered to function in non-SCF protein complexes in a variety of cellular functions. There are 11 F-box proteins in budding yeast, 326 predicted in Caenorhabditis elegans, 22 in Drosophila, and at least 38 in humans. F-box proteins often include additional carboxy-terminal moGenome biologyThe F-box protein family.PMC138887R01 GM057587P30 CA016087R01-GM55297P30-CA16087R01 GM055297R21-CA66229R01-GM57587R01-CA76584R01 CA076584Pagano MKipreos ETfalseThe F-box protein family.<h4>Summary</h4>The F-box is a protein motif of approximately 50 amino acids that functions as a site of protein-protein interaction. F-box proteins were first characterized as components of SCF ubiquitin-ligase complexes (named after their main components, Skp I, Cullin, and an F-box protein), in which they bind substrates for ubiquitin-mediated proteolysis. The F-box motif links the F-box protein to other components of the SCF complex by binding the core SCF component Skp I. F-box proteins have more recently been discovered to function in non-SCF protein complexes in a variety of cellular functions. There are 11 F-box proteins in budding yeast, 326 predicted in Caenorhabditis elegans, 22 in Drosophila, and at least 38 in humans. F-box proteins often include additional carboxy-terminal mo2000-01-01T00:00:00Z20002026-05-02T21:31:10.753Z2019-03-27T00:17:28ZS-EPMC1388871117826310.1186/gb-2000-1-5-reviews3002