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)
 

Links

 

Gene Review

USP33  -  ubiquitin specific peptidase 33

Homo sapiens

Synonyms: Deubiquitinating enzyme 33, KIAA1097, Ubiquitin carboxyl-terminal hydrolase 33, Ubiquitin thioesterase 33, Ubiquitin-specific-processing protease 33, ...
 
 
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.
 

Disease relevance of USP33

  • In particular we identified two novel genes not previously reported: endomucin (EMCN) and ubiquitin specific protease 33 (USP33) that appear to be over-expressed in B-ALL relative to their expression in T-ALL [1].
 

High impact information on USP33

 

Other interactions of USP33

  • Targeted degradation of VDU1 by pVHL could be crucial for regulating the ubiquitin-proteasome degradation pathway [3].
  • Based on human and mouse cDNA sequences, VDU1 and VDU2 are identical in approximately 59% of the amino acids with strong homology in the N-terminus and C-terminus and a weaker similarity in the middle region [4].

References

  1. A leukemia-enriched cDNA microarray platform identifies new transcripts with relevance to the biology of pediatric acute lymphoblastic leukemia. De Pittà, C., Tombolan, L., Campo Dell'Orto, M., Accordi, B., te Kronnie, G., Romualdi, C., Vitulo, N., Basso, G., Lanfranchi, G. Haematologica (2005) [Pubmed]
  2. Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation. Curcio-Morelli, C., Zavacki, A.M., Christofollete, M., Gereben, B., de Freitas, B.C., Harney, J.W., Li, Z., Wu, G., Bianco, A.C. J. Clin. Invest. (2003) [Pubmed]
  3. Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein. Li, Z., Na, X., Wang, D., Schoen, S.R., Messing, E.M., Wu, G. J. Biol. Chem. (2002) [Pubmed]
  4. Identification of a deubiquitinating enzyme subfamily as substrates of the von Hippel-Lindau tumor suppressor. Li, Z., Wang, D., Na, X., Schoen, S.R., Messing, E.M., Wu, G. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
 
WikiGenes - Universities