Ubiquitin is involved in
In animals, many proteins are degraded by the ubiquitin- protease pathway. This pathway was discovered by Aaron Ciechanover, A Hershko and Irwin Roose who got Nobel Prize. Proteosome 26s Protein * Comprises more than 30 polypeptide subunits, which are arranged in the form of a hollow cylinder. * Active sites of its proteolytic subunits face the interior of the cylinder, thus preventing the indiscriminate degradation of cellular proteins. * Proteins requiring degradation are targeted to the proteasome by "Ubiquitination"--the process in which there is covalent attachment of one or more ubiquitin molecules. Ubiquitin: It is a small, approximately 7s residue protein that is highly conserved among eukaryotes. Ubiquitination: It is catalyzed by a large family of enzymes called "E3 Ligases", which attach ubiquitin to the side chain amino group of lysyl residues.Ref: Textbook of medical biochemistry, MN Chatterji, 8th edition, page no: 131
Protein folding
Protein degradation
Synthesis of nucleic acid
Glycosylation of proteins
Structure and function of protein