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  Domain Name: UBQ
Ubiquitin-like proteins. Ubiquitin homologs; Includes ubiquitin and ubiquitin-like proteins. Ubiquitin-mediated proteolysis is part of the regulated turnover of proteins required for controlling cell cycle progression. Other family members are protein modifiers that perform a wide range of functions. Ubiquitination usually results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. The three-step mechanism requires an activating enzyme (E1) that forms a thiol ester with the C-terminal carboxy group, a conjugating enzyme (E2) that transiently carries the activated ubiquitin molecule as a thiol ester, and a ligase (E3) that transfers the activated ubiquitin from the E2 to the substrate lysine residue. In poly-ubiquitination, ubiquitin itself is the substrate.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 28
Total Disease Mutations Found: 13
This domain occurred 40 times on human genes (72 proteins).



  DIABETES MELLITUS, INSULIN-DEPENDENT, 5
  MOLYBDENUM COFACTOR DEFICIENCY, COMPLEMENTATION GROUP B
  PARKINSON DISEASE (PARK)
  PARKINSON DISEASE 2 (PARK2)
  PARKINSON DISEASE 2, AUTOSOMAL RECESSIVE JUVENILE


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 Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below.



Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
hydrophobic patch
charged pocket











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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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