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This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430. |
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Ubiquitin
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Ubiquitin is a very important protein utilized in the degradation of other proteins. It is a highly conserved protein that has not changed much during the evolution of life, so it and its related proteins are found in plant cells, yeast cells, and our own cells.
Function and Mechanism
Ubiquitin functions as a protein that regulates the degradation of other proteins. It consists of 76 amino acids and is found in almost all cells. UBQ functions in the ubiquitin-proteasome system. In this system, ubiquitin binds to an E1 protein. This E1 protein helps transfer the ubiquitin to an E2 protein. The E2 protein then binds to an E3 protein which binds to the targeted substrate protein. After this, ubiquitin binds onto the substrate via a glysine in the . This process must occur multiple times () before the ubiquitin signals for the to bind to the substrate. The proteasome then binds to the substrate and degrades the protein.
Disease
The malfunction of ubiquitination has been related to several diseases such as Alzheimer's, Parkinson's and Huntington's diseases. Ubiquitin also plays a major part in cancer specifically metastasis.
Relevance
Structural highlights
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References
Definition of Ubiquitin. (n.d.). Retrieved February 25, 2018, from https://www.medicinenet.com/script/main/art.asp?articlekey=26110
Goodsell, D. (2004, December). Ubiquitin. Retrieved February 25, 2018, from http://pdb101.rcsb.org/motm/60
The Ubiquitin Proteasome Pathway (UPP). (n.d.). Retrieved February 25, 2018, from http://www.bostonbiochem.com/about/ubiquitin-proteasome-pathway-upp
Varshavsky, A. (2006). The early history of the ubiquitin field. Protein Science : A Publication of the Protein Society, 15(3), 647–654. http://doi.org/10.1110/ps.052012306