The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

UCHL5  -  ubiquitin carboxyl-terminal hydrolase L5

Homo sapiens

Synonyms: AD-019, CGI-70, INO80R, UCH-L5, UCH37, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on UCHL5

  • Following binding, Adrm1 relieves Uch37 autoinhibition, accelerating the hydrolysis of ubiquitin-7-amido-4-methylcoumarin (ubiquitin-AMC) [1].
  • Furthermore, overexpression of UCH37 upregulates TGF-beta-dependent transcription, and this effect is reversed in cells subject to RNAi-mediated knockdown of endogenous UCH37 [2].
  • Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S proteasome in fission yeast [3].
  • The human orthologues of these enzymes are known as Uch37 and Usp14, respectively [3].
  • The activity of the C-terminal hydrolases UCH-L3 and UCH37 was upregulated in the majority of tumor tissues compared to the adjacent normal tissues [4].

Biological context of UCHL5


Physical interactions of UCHL5

  • In addition, we show that UCH37 can deubiquitinate and stabilize the type I TGF-beta receptor [2].

Other interactions of UCHL5

  • The interaction of UCH37 with S14 or UIP1 was confirmed by in vitro binding assay and in vivo co-immunoprecipitation analysis [6].
  • Recently, we have defined a novel interaction between Smads and UCH37 (ubiquitin C-terminal hydrolase 37), a DUB (de-ubiquitinating enzyme) that could potentially counteract Smurf-mediated ubiquitination [5].
  • Recently, USP2 and UCH37 have been shown to deubiquitinate tumor-growth-promoting proteins, and other DUBs have been shown to be overexpressed in cancer cells [7].


  1. Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Yao, T., Song, L., Xu, W., DeMartino, G.N., Florens, L., Swanson, S.K., Washburn, M.P., Conaway, R.C., Conaway, J.W., Cohen, R.E. Nat. Cell Biol. (2006) [Pubmed]
  2. The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-beta signalling. Wicks, S.J., Haros, K., Maillard, M., Song, L., Cohen, R.E., Dijke, P.T., Chantry, A. Oncogene (2005) [Pubmed]
  3. Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S proteasome in fission yeast. Stone, M., Hartmann-Petersen, R., Seeger, M., Bech-Otschir, D., Wallace, M., Gordon, C. J. Mol. Biol. (2004) [Pubmed]
  4. Activity profiling of deubiquitinating enzymes in cervical carcinoma biopsies and cell lines. Rolén, U., Kobzeva, V., Gasparjan, N., Ovaa, H., Winberg, G., Kisseljov, F., Masucci, M.G. Mol. Carcinog. (2006) [Pubmed]
  5. Reversible ubiquitination regulates the Smad/TGF-beta signalling pathway. Wicks, S.J., Grocott, T., Haros, K., Maillard, M., Dijke, P.T., Chantry, A. Biochem. Soc. Trans. (2006) [Pubmed]
  6. Identification of two proteins, S14 and UIP1, that interact with UCH37. Li, T., Duan, W., Yang, H., Lee, M.K., Bte Mustafa, F., Lee, B.H., Teo, T.S. FEBS Lett. (2001) [Pubmed]
  7. A substrate for deubiquitinating enzymes based on time-resolved fluorescence resonance energy transfer between terbium and yellow fluorescent protein. Horton, R.A., Strachan, E.A., Vogel, K.W., Riddle, S.M. Anal. Biochem. (2007) [Pubmed]
WikiGenes - Universities