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Ubiquitin can not only be found in the nucleus, but in the cytoplasm and cell-surface membrane as well[1]. Secondary structures found throughout ubiquitin include three and one half turns of ?-helix, a short 310 helix, a mixed ?-sheet with five strands and seven reverse turns.
At first, ubiquitin was believed to be a hormone involed in inducing the differentiation of lymphocytes and activating adenylate cyclase [2]. The first step of ubiquitin activation involves the formation of a ubiquitin-adenylate intermediate. The activated ubiquitin in then transferred to a ubiquitin-conjugating enzyme, E2, through a trans-thiolesteration reaction.


Before degradation is complete, the system must ensure that the protein that has been ubiquitinylated is in fact damaged. If, however, the target protein is found to be damaged, the ubiquitinylated protein is lead to its degradation by the 26S proteasome[5].
Ubiquitinylation simply refers to the isopeptide bond formation between the carboxyl-terminal of ubiquitin and the ?-amino acid side chain of the target protein. This conjugate formation is the most important process in protein degradation as it is believed to signal the protein for degradation.
Alanine (abbreviated as Ala or A)[1] is an ?-amino acid with the chemical formula CH3CH(NH2)COOH.


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This step results in a thioester linkage between the C-terminal carboxyl group of ubiquitin and the E1 cysteine sulfhydryl group[1]. The 20S proteasome than cleaves the polypeptide into short peptides of roughly 7-9 fragment residues.



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