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

USP14  -  ubiquitin specific peptidase 14 (tRNA...

Homo sapiens

Synonyms: Deubiquitinating enzyme 14, TGT, Ubiquitin carboxyl-terminal hydrolase 14, Ubiquitin thioesterase 14, Ubiquitin-specific-processing protease 14
 
 
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 USP14

  • In 18 of 99 (18.2%) colorectal cancer patients, USP14/TGT60 kD was strongly detected in the cytoplasm of cancer cells [1].
  • Our results suggest that USP14/TGT60 kD also controls the fate of proteins that regulate tumor invasion and metastasis [1].
  • To investigate the functional significance of TGT haplotype, a stable CHO transfectant expressing a P238S-L-selectin variant (CHO-varL) and a recombinant adenovirus vector containing an H468Y-E-selectin variant (Ad-varE) were established and compared to their Wt counterparts [2].
  • In an Italian patient with severe factor XIII deficiency, a novel mutation, Y283C (TAT to TGT), was identified heterozygously by nucleotide sequencing analysis in exon VII of the gene for the A subunit [3].
 

High impact information on USP14

  • Here, we report the crystal structures of the 45-kDa catalytic domain of USP14 in isolation and in a complex with ubiquitin aldehyde, which reveal distinct structural features [4].
  • In the absence of ubiquitin binding, the catalytic cleft leading to the active site of USP14 is blocked by two surface loops [4].
  • These three SNPs are in one major haplotype block, with TGT representing 78.4% of alleles [5].
  • The TGT/TGT diplotype found in 62.2% of samples was the major genotype seen to modify eye color, with a frequency of 0.905 in blue or green compared with only 0.095 in brown eye color [5].
  • This genotype was also at highest frequency in subjects with light brown hair and was more frequent in fair and medium skin types, consistent with the TGT haplotype acting as a recessive modifier of lighter pigmentary phenotypes [5].
 

Biological context of USP14

 

Anatomical context of USP14

 

Associations of USP14 with chemical compounds

  • The rabbit TGT 60-kDa subunit shares significant sequence similarity with the deubiquitinating enzyme family (F. R. Papa and M. Hochstrasser, 1993, nature 366, 313-319), especially with sequence elements that include conserved Cys and His residues [8].
  • Eukaryotes synthesize queuosine (nucleoside Q) by the irreversible base-for-base exchange of queuine (Q base) for guanine at tRNA position 34, a reaction catalyzed by tRNA-guanine transglycosylase (TGT) [8].
  • Change of the TGA codon to TGT gave a mutant enzyme form in which selenocysteine was replaced with cysteine [9].
 

Other interactions of USP14

  • Furthermore, the percentage of patients strongly positive for USP14/TGT60 kD expression increased with pathological stage [1].
  • The human orthologues of these enzymes are known as Uch37 and Usp14, respectively [10].

References

  1. Ubiquitin-specific protease 14 expression in colorectal cancer is associated with liver and lymph node metastases. Shinji, S., Naito, Z., Ishiwata, S., Ishiwata, T., Tanaka, N., Furukawa, K., Suzuki, H., Seya, T., Matsuda, A., Katsuta, M., Tajiri, T. Oncol. Rep. (2006) [Pubmed]
  2. Functional impact of IgA nephropathy-associated selectin gene haplotype on leukocyte-endothelial interaction. Takei, T., Hiraoka, M., Nitta, K., Uchida, K., Deushi, M., Yu, T., Nitta, N., Tsuchiya, K., Yumura, W., Nihei, H., Nakamura, Y., Yoshida, M. Immunogenetics (2006) [Pubmed]
  3. Novel Y283C mutation of the A subunit for coagulation factor XIII: molecular modelling predicts its impaired protein folding and dimer formation. Souri, M., Yee, V.C., Kasai, K., Kaneshiro, T., Narasaki, K., Castaman, G., Ichinose, A. Br. J. Haematol. (2001) [Pubmed]
  4. Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. Hu, M., Li, P., Song, L., Jeffrey, P.D., Chenova, T.A., Wilkinson, K.D., Cohen, R.E., Shi, Y. EMBO J. (2005) [Pubmed]
  5. A Three-Single-Nucleotide Polymorphism Haplotype in Intron 1 of OCA2 Explains Most Human Eye-Color Variation. Duffy, D.L., Montgomery, G.W., Chen, W., Zhao, Z.Z., Le, L., James, M.R., Hayward, N.K., Martin, N.G., Sturm, R.A. Am. J. Hum. Genet. (2007) [Pubmed]
  6. Segmental duplication associated with the human-specific inversion of chromosome 18: a further example of the impact of segmental duplications on karyotype and genome evolution in primates. Goidts, V., Szamalek, J.M., Hameister, H., Kehrer-Sawatzki, H. Hum. Genet. (2004) [Pubmed]
  7. Molecular basis of a hereditary type I protein S deficiency caused by a substitution of Cys for Arg474. Yamazaki, T., Katsumi, A., Kagami, K., Okamoto, Y., Sugiura, I., Hamaguchi, M., Kojima, T., Takamatsu, J., Saito, H. Blood (1996) [Pubmed]
  8. Cloning and characterization of cDNA encoding the rabbit tRNA-guanine transglycosylase 60-kilodalton subunit. Deshpande, K.L., Seubert, P.H., Tillman, D.M., Farkas, W.R., Katze, J.R. Arch. Biochem. Biophys. (1996) [Pubmed]
  9. Overexpression of wild type and SeCys/Cys mutant of human thioredoxin reductase in E. coli: the role of selenocysteine in the catalytic activity. Bar-Noy, S., Gorlatov, S.N., Stadtman, T.C. Free Radic. Biol. Med. (2001) [Pubmed]
  10. 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]
 
WikiGenes - Universities