期刊
GENOME BIOLOGY
卷 1, 期 5, 页码 -出版社
BIOMED CENTRAL LTD
DOI: 10.1186/gb-2000-1-5-reviews3002
关键词
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资金
- NIH [R01-GM55297, R01-CA76584, R01-GM57587, P30-CA16087, R21-CA66229]
- HFSPO [RG-229, RG0229]
- Irma T. Hirschl scholarship
- NATIONAL CANCER INSTITUTE [R21CA066229, R01CA076584, P30CA016087] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM055297, R01GM057587] Funding Source: NIH RePORTER
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, Skp1, 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 Skp1. 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 motifs capable of protein-protein interaction; the most common secondary motifs in yeast and human F-box proteins are WD repeats and leucine-rich repeats, both of which have been found to bind phosphorylated substrates to the SCF complex. The majority of F-box proteins have other associated motifs, and the functions of most of these proteins have not yet been defined.
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