Sandbox Reserved 1450: Difference between revisions

Ubiquitin is one of the most highly conserved proteins known at this time and so the relevance is very important for the cell to encode it properly.  This protein is expressed throughout the body but mostly where lots of growth hormones occur most frequently.  These places include liver, reproductive organs, kidney, brain & bone marrow.  Being in places of growth and starting so low in the evolutionary tree suggests that Ubiquitin is crucial for homeostatic functions.  Because it is so important for the cell, it is highly regulated with a half life between ten and twenty hours but usually closer to ten.   

Ubiquitin has lots of lysine residues throughout the protein.  The lysine residues play a large part in the binding ability of the protein due to its basic properties.  It is made up of three domains with a total of 229 residues.  The TRAF6 RING dimer forms a catalytic complex with RING interacting with the Ubiquitin conjugate and a zinc finger domain that opposes it in the Ubiquitin contact.  The TRAF5 enables Ubiquitin to transfer from a TRAF6 bound conjugate.  The TRAF RING domains can synthesize Ubiquitin chains for tagging the cellular proteins for degradation.   

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http://www.uniprot.org/uniprot/P0CG47  

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2776765/