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

Tyr  -  tyrosinase

Rattus norvegicus

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 Tyr


High impact information on Tyr

  • Here we show that another tyrosine phosphorylation site in middle T-antigen (Tyr 250; refs 4, 5) acts as a binding region for the SH2 domain of the transforming protein Shc [6].
  • As a result, middle T-antigen itself is phosphorylated on tyrosine residues, one of which (Tyr 315) acts as a binding site for the SH2 domains of phosphatidylinositol-3'OH kinase 85K subunit [6].
  • These data suggest that the phenolic hydroxyl of Tyr 248 does not act as the requisite general acid catalyst but participates in ligand binding [7].
  • An RHI mutant, with Tyr substituted for Cys at position 374 (as in microliter) confers three properties of TTX-sensitive channels: (i) greater sensitivity to TTX (730-fold); (ii) lower sensitivity to cadmium (28-fold); and (iii) altered additional block by toxin upon repetitive stimulation [8].
  • We conclude that the isoform-specific residue (Tyr/Phe/Cys) in the P-loop of domain I plays an important role in drug access as well as in tetrodotoxin binding [9].

Biological context of Tyr

  • The PC12 hydroxylase exhibited typical kinetics of tyrosine hydroxylation exhibited typical kinetics of tyrosine hydroxylation, both as a function of tyrosine (S0.5 Tyr = 15 microM) and BH4 (apparent Km BH4 = 210 microM) [10].
  • Interestingly, down-regulation of MAP kinase activity can be initiated by multiple Ser/Thr phosphatases, Tyr-specific phosphatases, and dual-specificity phosphatases [11].
  • None of the 24 synthetic peptides alone stimulated anti-AChR production and, when added to cultures along with AChR, [Tyr 100]alpha 100-116 and [Gly 89, Tyr 90]alpha 73-90 suppressed antibody production [12].
  • The importance of the Glu(279) residue in the binding of NAD(+) was further examined by cassette mutagenesis with mutant enzymes containing Arg, Gly, Leu, Met, or Tyr at position 279 [13].
  • Additionally, in CD95-yellow fluorescent protein-transfected Huh7-hepatoma cells, ONOO(-) induced CD95 Tyr nitration and prevented CD95L-induced Tyr phosphorylation and apoptosis [14].

Anatomical context of Tyr

  • Of twelve cloned T cell lines specific to AChR, 4 responded to [Tyr 100]alpha 100-116, indicating the importance of the epitope in alpha 101-116 in Lewis rats [12].
  • Intracellular protein degradation in the rat hepatocyte is regulated by 7 amino acids of which Leu, Gln, and Tyr play major roles [15].
  • We replaced the invariant Gly17 residue in human neutrophil alpha-defensin 2 (HNP2) by L-Ala or one of the D-amino acids Ala, Glu, Phe, Arg, Thr, Val, or Tyr [16].
  • Binding of double-stranded calf thymus DNA brings about a moderate quenching of the Tyr and Trp fluorescence emission of both the 31-kDa fragment and beta-polymerase and induces a 6-nm blue shift in the Trp emission maximum of the intact enzyme, but not in the fragment [17].
  • The amino acid control of macroautophagy in the hepatocyte is accomplished by a small group of direct inhibitors (Leu, Tyr/Phe, Gln, Pro, Met, Trp, and His) and the permissive effect of alanine whereas only leucine is involved in myocytes and adipocytes [18].

Associations of Tyr with chemical compounds

  • The most prominent conformational changes that occur in the presence of dicoumarol involve Tyr 128 and Phe 232 that are present on the surface of the NQO1 catalytic pocket [19].
  • The four LHRHs known to occur in nature involve a total of six amino acids (Tyr, His, Leu, Trp, Arg, Gln) in positions 5, 7, and 8 [20].
  • It is found that the aminoacyl-tRNA synthetases (EC 6.1.1.-) with specificity for Arg, Asn, Ile, Leu, Met, Phe, Thr, Trp, and Val attach the amino acid to the 2'-position; those with specificity for Gly, His, Lys, and Ser attach the amino acid to the 3'-position; and that Tyr and Cys can be enzymatically attached to both the 2'- and 3'-positions [21].
  • The aromatic rings of Tyr and Phe are postulated to stabilize carbocation intermediates of the first and second half-reactions, respectively; the acidic Asp residues may be required for substrate binding [22].
  • RL-29 has a 140-amino-acid COOH-terminal carbohydrate-binding domain, a 20-amino-acid NH2-terminal domain, and an intervening domain consisting of 11 repeating elements rich in Pro, Gly, and Tyr (R-domain) [23].

Analytical, diagnostic and therapeutic context of Tyr

  • To test this hypothesis we have modified the rat CPA cDNA by site-directed mutagenesis so that the codon for Tyr 248 is replaced by that for Phe [7].
  • Sequence analysis revealed that within the minimal 18-amino acid peptide of E2F-1 required for RB binding, five residues, Tyr (position 411), Glu (419), and Asp-Leu-Phe (423-425), are critical [24].
  • We now show that proteolytic responses to Phe during liver perfusion differ strikingly from effects of the multiphasic regulators Leu, Gln, and Tyr in eliciting mirror image responses at half-normal and normal plasma concentrations [15].
  • Insulin, biosynthetic human proinsulin and 2 human proinsulin conversion intermediates, des (64, 65) human proinsulin and des (31, 32) human proinsulin, were labelled with 123 I and the derivatives monosubstituted on Tyr A14 were purified by reverse phase high performance liquid chromatography [25].
  • This conformational change can be demonstrated directly by the circular dichroism spectrum of human Thy-1 that detects changes in the environment of Tyr residues located near the antigenic epitopes [26].


  1. Insulin stimulates PKCzeta -mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteins. Liu, Y.F., Paz, K., Herschkovitz, A., Alt, A., Tennenbaum, T., Sampson, S.R., Ohba, M., Kuroki, T., LeRoith, D., Zick, Y. J. Biol. Chem. (2001) [Pubmed]
  2. SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in Rat-2 fibroblasts. Briggs, S.D., Smithgall, T.E. J. Biol. Chem. (1999) [Pubmed]
  3. Inhibition of tyrosine protein kinases by the antineoplastic agent adriamycin. Donella-Deana, A., Monti, E., Pinna, L.A. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  4. Corneal organ cultures in tyrosinemia release chemotactic factors. Lohr, K.M., Hyndiuk, R.A., Hatchell, D.L., Kurth, C.E. J. Lab. Clin. Med. (1985) [Pubmed]
  5. Amino acid utilization during apoptosis in HL-60 cells. Sakagami, H., Yokote, Y., Kochi, M., Hara, E., Akahane, K. Anticancer Res. (1999) [Pubmed]
  6. Transformation by polyoma virus middle T-antigen involves the binding and tyrosine phosphorylation of Shc. Dilworth, S.M., Brewster, C.E., Jones, M.D., Lanfrancone, L., Pelicci, G., Pelicci, P.G. Nature (1994) [Pubmed]
  7. Site-directed mutagenesis shows that tyrosine 248 of carboxypeptidase A does not play a crucial role in catalysis. Gardell, S.J., Craik, C.S., Hilvert, D., Urdea, M.S., Rutter, W.J. Nature (1985) [Pubmed]
  8. A mutant of TTX-resistant cardiac sodium channels with TTX-sensitive properties. Satin, J., Kyle, J.W., Chen, M., Bell, P., Cribbs, L.L., Fozzard, H.A., Rogart, R.B. Science (1992) [Pubmed]
  9. A critical residue for isoform difference in tetrodotoxin affinity is a molecular determinant of the external access path for local anesthetics in the cardiac sodium channel. Sunami, A., Glaaser, I.W., Fozzard, H.A. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  10. The hydroxylation of phenylalanine and tyrosine by tyrosine hydroxylase from cultured pheochromocytoma cells. Ribeiro, P., Pigeon, D., Kaufman, S. J. Biol. Chem. (1991) [Pubmed]
  11. The activity of the extracellular signal-regulated kinase 2 is regulated by differential phosphorylation in the activation loop. Zhou, B., Zhang, Z.Y. J. Biol. Chem. (2002) [Pubmed]
  12. Specificity of the T cell immune response to acetylcholine receptor in experimental autoimmune myasthenia gravis. Response to subunits and synthetic peptides. Fujii, Y., Lindstrom, J. J. Immunol. (1988) [Pubmed]
  13. Importance of glutamate 279 for the coenzyme binding of human glutamate dehydrogenase. Yoon, H.Y., Cho, E.H., Kwon, H.Y., Choi, S.Y., Cho, S.W. J. Biol. Chem. (2002) [Pubmed]
  14. CD95-tyrosine nitration inhibits hyperosmotic and CD95 ligand-induced CD95 activation in rat hepatocytes. Reinehr, R., Görg, B., Höngen, A., Häussinger, D. J. Biol. Chem. (2004) [Pubmed]
  15. Parallel control of hepatic proteolysis by phenylalanine and phenylpyruvate through independent inhibitory sites at the plasma membrane. Kadowaki, M., Pösö, A.R., Mortimore, G.E. J. Biol. Chem. (1992) [Pubmed]
  16. Reconstruction of the conserved beta-bulge in mammalian defensins using D-amino acids. Xie, C., Prahl, A., Ericksen, B., Wu, Z., Zeng, P., Li, X., Lu, W.Y., Lubkowski, J., Lu, W. J. Biol. Chem. (2005) [Pubmed]
  17. Spectroscopic studies of the structural domains of mammalian DNA beta-polymerase. Casas-Finet, J.R., Kumar, A., Morris, G., Wilson, S.H., Karpel, R.L. J. Biol. Chem. (1991) [Pubmed]
  18. Intracellular protein catabolism and its control during nutrient deprivation and supply. Mortimore, G.E., Pösö, A.R. Annu. Rev. Nutr. (1987) [Pubmed]
  19. The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol. Asher, G., Dym, O., Tsvetkov, P., Adler, J., Shaul, Y. Biochemistry (2006) [Pubmed]
  20. Decapeptides as effective agonists from L-amino acids biologically equivalent to the luteinizing hormone-releasing hormone. Folkers, K., Bowers, C.Y., Tang, P.F., Kubota, M. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  21. Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2'- or 3'-hydroxyl group of the terminal adenosine. Sprinzl, M., Cramer, F. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  22. Squalene synthase: structure and regulation. Tansey, T.R., Shechter, I. Prog. Nucleic Acid Res. Mol. Biol. (2001) [Pubmed]
  23. Primary structure of the soluble lactose binding lectin L-29 from rat and dog and interaction of its non-collagenous proline-, glycine-, tyrosine-rich sequence with bacterial and tissue collagenase. Herrmann, J., Turck, C.W., Atchison, R.E., Huflejt, M.E., Poulter, L., Gitt, M.A., Burlingame, A.L., Barondes, S.H., Leffler, H. J. Biol. Chem. (1993) [Pubmed]
  24. Disruption of RB/E2F-1 interaction by single point mutations in E2F-1 enhances S-phase entry and apoptosis. Shan, B., Durfee, T., Lee, W.H. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  25. Scintigraphic distribution of 123 I labelled proinsulin, split conversion intermediates and insulin in rats. Sodoyez-Goffaux, F., Sodoyez, J.C., Koch, M., De Vos, C.J., Frank, B.H. Diabetologia (1988) [Pubmed]
  26. The glycophosphatidylinositol anchor affects the conformation of Thy-1 protein. Barboni, E., Rivero, B.P., George, A.J., Martin, S.R., Renoup, D.V., Hounsell, E.F., Barber, P.C., Morris, R.J. J. Cell. Sci. (1995) [Pubmed]
WikiGenes - Universities