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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

USP17L2  -  ubiquitin specific peptidase 17-like...

Homo sapiens

Synonyms: DUB-3, DUB3, Deubiquitinating enzyme 17-like protein 2, Deubiquitinating protein 3, USP17, ...
 
 
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High impact information on DUB3

  • Finally, we have demonstrated that constitutive expression of DUB-3 blocks proliferation and can initiate apoptosis in both IL-3-dependent Ba/F3 cells and NIH3T3 fibroblasts [1].
  • We have also demonstrated that DUB-3, which was shown to be an active deubiquitinating enzyme, is induced in response to interleukin-4 and interleukin-6 stimulation [1].
  • DUB-3, a cytokine-inducible deubiquitinating enzyme that blocks proliferation [1].
  • In addition, human DUB enzyme DUB-3, highly homologous to USP17 and induced by cytokines interleukin (IL)-4 and IL-6, has been recently isolated and showed that it has significant homology to the known murine DUB subfamily members [2].
 

Anatomical context of DUB3

  • RESULTS: While identifying putative ubiquitin specific protease (USP) enzymes that contain a conserved Asp (I) domain in humans, 4 USP17 subfamily members, highly homologous to DUB-3, have been found (USP17K, USP17L, USP17M, and USP17N), from human chorionic villi [3].

References

  1. DUB-3, a cytokine-inducible deubiquitinating enzyme that blocks proliferation. Burrows, J.F., McGrattan, M.J., Rascle, A., Humbert, M., Baek, K.H., Johnston, J.A. J. Biol. Chem. (2004) [Pubmed]
  2. Cytokine-regulated protein degradation by the ubiquitination system. Baek, K.H. Curr. Protein Pept. Sci. (2006) [Pubmed]
  3. Hyaluronan- and RNA-binding deubiquitinating enzymes of USP17 family members associated with cell viability. Shin, J.M., Yoo, K.J., Kim, M.S., Kim, D., Baek, K.H. BMC Genomics (2006) [Pubmed]
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