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Ubiquitin ligase is a protein which is found in all eukaryotic cells. Ubiqiutin allows cells to recognise the proteins that need to be degraded by binding on the protein. This binding of ubiquitin to the protein labels the proteins for destruction. The enzymes are involved in the binding of ubiquitin to a protein, ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2) and ubiquitin-protein ligase (E3)[1].

Ubiquitin is a protein with a globular structure[2], consisting of 76 amino acid residues[3], linked by peptide bonds, that have been folded tightly into a compact structure. Ubiquitin is a part of the Ubiquitin system, which involves the process of ubiquitination which is the reversible[4] alteration of the function of the location of a protein by the attachment of ubiquitin or leads to protein degradation.


  1. Jeremy M. Berg,John L. Tymoczko, Lubert Stryer, 2011, Biochemistry,7 th edition,W.H. Freeman and Company.pg 699-700
  2. The University of Nottingham. The Pathway of Protein Ubiquitylation. [18/11/18]. Available from: https://www.Nottingham.ac.uk/biochemcourses/students/ub/ubpath.html
  3. European Bioinformatics Institute. Jennifer McDowall. Ubiquitin. [15/11/18]. Available from: https://www.ebi.ac.uk/interpro/potm/2004_12/Page1.htm
  4. NCBI. Viduth K. Chaugule and Helen Walden. Specificity and Disease in the Ubiquitin System. 2016. [18/11/18]. Available from: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5264512/
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