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Chemical Compound Review

PHOSPHOTYROSINE     (2S)-2-amino-3-(4- phosphonooxyphenyl)propa...

Synonyms: AmbotzHAA7420, SureCN1152, CHEMBL286939, AG-E-59448, CHEBI:37788, ...
 
 
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Disease relevance of PHOSPHOTYROSINE

 

Psychiatry related information on PHOSPHOTYROSINE

 

High impact information on PHOSPHOTYROSINE

 

Chemical compound and disease context of PHOSPHOTYROSINE

 

Biological context of PHOSPHOTYROSINE

  • Signaling by tyrosine kinase receptors is mediated by selective interactions between individual Src homology 2 (SH2) domains of cytoplasmic effectors and specific phosphotyrosine residues in the activated receptor [19].
  • However, the binding site for residues C-terminal to the phosphotyrosine (pTyr) is an extended groove that contacts peptide residues at the +1 to +6 positions relative to the pTyr [20].
  • This demonstrates that the TCR-CD3 complex can engage selective intracellular biochemical signaling pathways as a direct consequence of the nature of the ligand recognized and the initial phosphotyrosine pattern of the TCR-CD3 proteins, leading to different phenotypes [21].
  • Phosphotyrosine in cdc2 is detectable at the onset of DNA synthesis and becomes maximal in the G2 phase of the cell cycle [22].
  • SH2 regions are protein motifs capable of binding target protein sequences that contain a phosphotyrosine [23].
 

Anatomical context of PHOSPHOTYROSINE

 

Associations of PHOSPHOTYROSINE with other chemical compounds

  • Prior to this work, C2 domains were thought to bind only to phospholipids or to unphosphorylated proteins, and the SH2 and PTB domains were the only signaling domains known to recognize phosphotyrosine [28].
  • Experiments indicate that, in vivo, many of these viruses or growth factors induce an increase in cellular phosphotyrosine, as well as an increase in the phosphorylation of serine residues on proteins, including ribosomal protein S6 [29].
  • A PDGFR mutant (F5) that lacks high-affinity binding sites for the Src homology 2 domain-containing proteins phosphatidylinositol-3 kinase (PI-3 kinase), Ras guanosine triphosphatase activating protein, phospholipase C-gamma, and a phosphotyrosine phosphatase (Syp) remained at the cell periphery [30].
  • Lack of significant incorporation of label from [alpha-32P]adenosine triphosphate into the copolymer or endogenous yeast proteins demonstrated that nucleotide interconversion, adenylylation, and subsequent hydrolysis could not account for the generation of phosphotyrosine observed [31].
  • The APS SH2 dimer engages two kinase molecules, with pTyr-1158 of the kinase activation loop bound in the canonical phosphotyrosine binding pocket of the SH2 domain and a second phosphotyrosine, pTyr-1162, coordinated by two lysine residues in beta strand D [32].
 

Gene context of PHOSPHOTYROSINE

 

Analytical, diagnostic and therapeutic context of PHOSPHOTYROSINE

References

  1. Transformation by Rous sarcoma virus: a cellular substrate for transformation-specific protein phosphorylation contains phosphotyrosine. Radke, K., Gilmore, T., Martin, G.S. Cell (1980) [Pubmed]
  2. HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase. Gallay, P., Swingler, S., Song, J., Bushman, F., Trono, D. Cell (1995) [Pubmed]
  3. Crystal structure of a complex of a type IA DNA topoisomerase with a single-stranded DNA molecule. Changela, A., DiGate, R.J., Mondragón, A. Nature (2001) [Pubmed]
  4. Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling. Frischknecht, F., Moreau, V., Röttger, S., Gonfloni, S., Reckmann, I., Superti-Furga, G., Way, M. Nature (1999) [Pubmed]
  5. Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cells. White, M.F., Maron, R., Kahn, C.R. Nature (1985) [Pubmed]
  6. The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled. Ermekova, K.S., Zambrano, N., Linn, H., Minopoli, G., Gertler, F., Russo, T., Sudol, M. J. Biol. Chem. (1997) [Pubmed]
  7. Proteomic analysis of phosphotyrosyl proteins in morphine-dependent rat brains. Kim, S.Y., Chudapongse, N., Lee, S.M., Levin, M.C., Oh, J.T., Park, H.J., Ho, I.K. Brain Res. Mol. Brain Res. (2005) [Pubmed]
  8. Protein tyrosine phosphatase activity in insulin-resistant rodent Psammomys obesus. Meyerovitch, J., Balta, Y., Ziv, E., Sack, J., Shafrir, E. Int. J. Exp. Diabetes Res. (2002) [Pubmed]
  9. The C2 domain of PKCdelta is a phosphotyrosine binding domain. Benes, C.H., Wu, N., Elia, A.E., Dharia, T., Cantley, L.C., Soltoff, S.P. Cell (2005) [Pubmed]
  10. Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Pawson, T. Cell (2004) [Pubmed]
  11. Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome. Tartaglia, M., Mehler, E.L., Goldberg, R., Zampino, G., Brunner, H.G., Kremer, H., van der Burgt, I., Crosby, A.H., Ion, A., Jeffery, S., Kalidas, K., Patton, M.A., Kucherlapati, R.S., Gelb, B.D. Nat. Genet. (2001) [Pubmed]
  12. The SH2 tyrosine phosphatase shp2 is required for mammalian limb development. Saxton, T.M., Ciruna, B.G., Holmyard, D., Kulkarni, S., Harpal, K., Rossant, J., Pawson, T. Nat. Genet. (2000) [Pubmed]
  13. Daughter of sevenless is a substrate of the phosphotyrosine phosphatase Corkscrew and functions during sevenless signaling. Herbst, R., Carroll, P.M., Allard, J.D., Schilling, J., Raabe, T., Simon, M.A. Cell (1996) [Pubmed]
  14. A yeast protein phosphatase related to the vaccinia virus VH1 phosphatase is induced by nitrogen starvation. Guan, K., Hakes, D.J., Wang, Y., Park, H.D., Cooper, T.G., Dixon, J.E. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  15. Detection of phosphotyrosine-containing proteins in polyomavirus middle tumor antigen-transformed cells after treatment with a phosphotyrosine phosphatase inhibitor. Yonemoto, W., Filson, A.J., Queral-Lustig, A.E., Wang, J.Y., Brugge, J.S. Mol. Cell. Biol. (1987) [Pubmed]
  16. Phosphotyrosine-containing lactate dehydrogenase is restricted to the nuclei of PC12 pheochromocytoma cells. Zhong, X.H., Howard, B.D. Mol. Cell. Biol. (1990) [Pubmed]
  17. Mechanism of reversion of Rous sarcoma virus transformation by herbimycin A: reduction of total phosphotyrosine levels due to reduced kinase activity and increased turnover of p60v-src1. Uehara, Y., Murakami, Y., Sugimoto, Y., Mizuno, S. Cancer Res. (1989) [Pubmed]
  18. Discovery of JSI-124 (cucurbitacin I), a selective Janus kinase/signal transducer and activator of transcription 3 signaling pathway inhibitor with potent antitumor activity against human and murine cancer cells in mice. Blaskovich, M.A., Sun, J., Cantor, A., Turkson, J., Jove, R., Sebti, S.M. Cancer Res. (2003) [Pubmed]
  19. A multifunctional docking site mediates signaling and transformation by the hepatocyte growth factor/scatter factor receptor family. Ponzetto, C., Bardelli, A., Zhen, Z., Maina, F., dalla Zonca, P., Giordano, S., Graziani, A., Panayotou, G., Comoglio, P.M. Cell (1994) [Pubmed]
  20. Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide. Pascal, S.M., Singer, A.U., Gish, G., Yamazaki, T., Shoelson, S.E., Pawson, T., Kay, L.E., Forman-Kay, J.D. Cell (1994) [Pubmed]
  21. Partial T cell signaling: altered phospho-zeta and lack of zap70 recruitment in APL-induced T cell anergy. Sloan-Lancaster, J., Shaw, A.S., Rothbard, J.B., Allen, P.M. Cell (1994) [Pubmed]
  22. Reversible tyrosine phosphorylation of cdc2: dephosphorylation accompanies activation during entry into mitosis. Morla, A.O., Draetta, G., Beach, D., Wang, J.Y. Cell (1989) [Pubmed]
  23. Three-dimensional solution structure of the src homology 2 domain of c-abl. Overduin, M., Rios, C.B., Mayer, B.J., Baltimore, D., Cowburn, D. Cell (1992) [Pubmed]
  24. Vinculin: a cytoskeletal target of the transforming protein of Rous sarcoma virus. Sefton, B.M., Hunter, T., Ball, E.H., Singer, S.J. Cell (1981) [Pubmed]
  25. Epidermal growth factor induces rapid tyrosine phosphorylation of proteins in A431 human tumor cells. Hunter, T., Cooper, J.A. Cell (1981) [Pubmed]
  26. The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and alpha 2-6 sialyltransferase, CD75, on B cells. Stamenkovic, I., Sgroi, D., Aruffo, A., Sy, M.S., Anderson, T. Cell (1991) [Pubmed]
  27. Transformation of cells by an inhibitor of phosphatases acting on phosphotyrosine in proteins. Klarlund, J.K. Cell (1985) [Pubmed]
  28. C2 can do it, too. Sondermann, H., Kuriyan, J. Cell (2005) [Pubmed]
  29. Increased phosphorylation of ribosomal protein S6 following microinjection of insulin receptor-kinase into Xenopus oocytes. Maller, J.L., Pike, L.J., Freidenberg, G.R., Cordera, R., Stith, B.J., Olefsky, J.M., Krebs, E.G. Nature (1986) [Pubmed]
  30. Disruption of PDGF receptor trafficking by mutation of its PI-3 kinase binding sites. Joly, M., Kazlauskas, A., Fay, F.S., Corvera, S. Science (1994) [Pubmed]
  31. Protein-tyrosine kinase activity in Saccharomyces cerevisiae. Schieven, G., Thorner, J., Martin, G.S. Science (1986) [Pubmed]
  32. Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor. Hu, J., Liu, J., Ghirlando, R., Saltiel, A.R., Hubbard, S.R. Mol. Cell (2003) [Pubmed]
  33. A target for Src in mitosis. Fumagalli, S., Totty, N.F., Hsuan, J.J., Courtneidge, S.A. Nature (1994) [Pubmed]
  34. Role of IRS-2 in insulin and cytokine signalling. Sun, X.J., Wang, L.M., Zhang, Y., Yenush, L., Myers, M.G., Glasheen, E., Lane, W.S., Pierce, J.H., White, M.F. Nature (1995) [Pubmed]
  35. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1. Rozakis-Adcock, M., Fernley, R., Wade, J., Pawson, T., Bowtell, D. Nature (1993) [Pubmed]
  36. Interaction between Gab1 and the c-Met receptor tyrosine kinase is responsible for epithelial morphogenesis. Weidner, K.M., Di Cesare, S., Sachs, M., Brinkmann, V., Behrens, J., Birchmeier, W. Nature (1996) [Pubmed]
  37. The discoidin domain receptor tyrosine kinases are activated by collagen. Vogel, W., Gish, G.D., Alves, F., Pawson, T. Mol. Cell (1997) [Pubmed]
  38. EGF induces tyrosine phosphorylation of phospholipase C-II: a potential mechanism for EGF receptor signaling. Margolis, B., Rhee, S.G., Felder, S., Mervic, M., Lyall, R., Levitzki, A., Ullrich, A., Zilberstein, A., Schlessinger, J. Cell (1989) [Pubmed]
  39. Coexpression of a PDGF-like growth factor and PDGF receptors in a human osteosarcoma cell line: implications for autocrine receptor activation. Betsholtz, C., Westermark, B., Ek, B., Heldin, C.H. Cell (1984) [Pubmed]
  40. Phosphotyrosine-containing proteins isolated by affinity chromatography with antibodies to a synthetic hapten. Ross, A.H., Baltimore, D., Eisen, H.N. Nature (1981) [Pubmed]
  41. Sequential involvement of Lck and SHP-1 with MHC-recognizing receptors on NK cells inhibits FcR-initiated tyrosine kinase activation. Binstadt, B.A., Brumbaugh, K.M., Dick, C.J., Scharenberg, A.M., Williams, B.L., Colonna, M., Lanier, L.L., Kinet, J.P., Abraham, R.T., Leibson, P.J. Immunity (1996) [Pubmed]
  42. Constitutive activation of different Jak tyrosine kinases in human T cell leukemia virus type 1 (HTLV-1) tax protein or virus-transformed cells. Xu, X., Kang, S.H., Heidenreich, O., Okerholm, M., O'Shea, J.J., Nerenberg, M.I. J. Clin. Invest. (1995) [Pubmed]
 
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