Petroski, Matthew D. Signal Transduction Program, Burnham Institute for Medical Research, La Jolla, California.
Last reviewed:January 2021
- Process of ubiquitination
- Ubiquitin ligases
- Ubiquitin-conjugating and ubiquitin-activating enzymes
- Deubiquitinating enzymes
- Different types of ubiquitin modifications
- Physiological functions of ubiquitination
- Links between disease and ubiquitination
- Targeting aspects of ubiquitination for human therapies
- Related Primary Literature
- Additional Reading
The conjugation of ubiquitin to cellular proteins, which regulates a broad range of eukaryotic cell functions and in particular targets proteins for degradation. All eukaryotic cells express a 76-amino-acid protein known as ubiquitin. This protein has the unique ability to be covalently attached to other proteins in an enzymatic process known as ubiquitination (alternatively, ubiquitylation). Ubiquitination is involved in the posttranslational regulation of a wide array of cellular processes, and different types of ubiquitin modifications exist that in turn can promote distinct protein fates. The most well understood role for ubiquitination is to target modified proteins for destruction by the large proteolytic enzyme complex known as the 26S proteasome. Ubiquitination is also involved in altering protein localization, promoting protein–protein interactions, regulating gene expression, and changing the activity of cellular enzymes. See also: Biochemistry; Cell biology; Enzyme; Molecular biology; Proteasome; Protein; Protein degradation
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