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Gene Review

STYX  -  serine/threonine/tyrosine interacting protein

Homo sapiens

Synonyms: Protein tyrosine phosphatase-like protein, Serine/threonine/tyrosine-interacting protein
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Disease relevance of STYX


High impact information on STYX

  • STYX is a unique modular domain found within proteins implicated in mediating the effects of tyrosine phosphorylation in vivo [3].
  • The archetype STYX/dead-phosphatase complexes with a spermatid mRNA-binding protein and is essential for normal sperm production [4].
  • We demonstrate that the phosphoserine, -threonine or -tyrosine, interaction protein, Styx, complexes with a testicular RNA-binding protein and is essential for normal spermiogenesis [4].
  • Ablation of Styx expression in mouse disrupts round and elongating spermatid development, resulting in a >1,000-fold decrease in spermatozoa production [4].
  • Immunoprecipitation of Styx with Crhsp-24, a phosphorylated RNA-binding protein implicated in translational repression of histone mRNAs, provides a strategy for regulating posttranscriptional gene expression [4].

Biological context of STYX

  • Bacterially expressed STYX is incapable of hydrolyzing Tyr(P)-containing substrates; however, mutation of Gly120 to Cys (G120C), which structurally mimics the active site of dsPTPases, confers phosphatase activity to this molecule [5].
  • Thus, the STYX domain adds to the repertoire of modular domains that can mediate intracellular signaling in response to protein phosphorylation [3].
  • Pasticcino2 is a protein tyrosine phosphatase-like involved in cell proliferation and differentiation in Arabidopsis [6].
  • Macronuclear DNA synthesis occupies a substantial part of the interdivision interval, and micronuclear DNA synthesis in Styx sp. takes place in early prophase at a time when macronuclear DNA synthesis is in its terminal phase [7].

Anatomical context of STYX


Associations of STYX with chemical compounds


Other interactions of STYX


Analytical, diagnostic and therapeutic context of STYX


  1. Protein tyrosine phosphatase-like protein IA2-antibodies plus glutamic acid decarboxylase 65 antibodies (GADA) indicates autoimmunity as frequently as islet cell antibodies assay in children with recently diagnosed diabetes mellitus. Borg, H., Fernlund, P., Sundkvist, G. Clin. Chem. (1997) [Pubmed]
  2. Evaluation of two nonisotopic immunoassays for determination of glutamic acid decarboxylase and tyrosine phosphatase autoantibodies in serum. Palomer, X., Mauricio, D., Rodríguez-Espinosa, J., Zapico, E., Mayoral, C., González-Sastre, F., de Leiva, A., Blanco-Vaca, F. Clin. Chem. (2004) [Pubmed]
  3. Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains. Wishart, M.J., Dixon, J.E. Trends Biochem. Sci. (1998) [Pubmed]
  4. The archetype STYX/dead-phosphatase complexes with a spermatid mRNA-binding protein and is essential for normal sperm production. Wishart, M.J., Dixon, J.E. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  5. A single mutation converts a novel phosphotyrosine binding domain into a dual-specificity phosphatase. Wishart, M.J., Denu, J.M., Williams, J.A., Dixon, J.E. J. Biol. Chem. (1995) [Pubmed]
  6. Pasticcino2 is a protein tyrosine phosphatase-like involved in cell proliferation and differentiation in Arabidopsis. Bellec, Y., Harrar, Y., Butaeye, C., Darnet, S., Bellini, C., Faure, J.D. Plant J. (2002) [Pubmed]
  7. Electron microscope autoradiography of DNA synthesis in the replication band of two hypotrichous ciliates. Lin, M., Prescott, D.M. J. Protozool. (1985) [Pubmed]
  8. The yeast split-ubiquitin membrane protein two-hybrid screen identifies BAP31 as a regulator of the turnover of endoplasmic reticulum-associated protein tyrosine phosphatase-like B. Wang, B., Pelletier, J., Massaad, M.J., Herscovics, A., Shore, G.C. Mol. Cell. Biol. (2004) [Pubmed]
  9. Identification of protein tyrosine phosphatase-like IA2 (islet cell antigen 512) as the insulin-dependent diabetes-related 37/40K autoantigen and a target of islet-cell antibodies. Bonifacio, E., Lampasona, V., Genovese, S., Ferrari, M., Bosi, E. J. Immunol. (1995) [Pubmed]
  10. Localisation of high Acid phosphotyrosine phosphatase activity in afferent arterioles and glomeruli of human kidney. Partanen, S. Journal of molecular histology. (2005) [Pubmed]
  11. High levels of antigen-specific islet antibodies predict future beta-cell failure in patients with onset of diabetes in adult age. Borg, H., Gottsäter, A., Landin-Olsson, M., Fernlund, P., Sundkvist, G. J. Clin. Endocrinol. Metab. (2001) [Pubmed]
  12. Molecular cloning, chromosomal mapping, and developmental expression of a novel protein tyrosine phosphatase-like gene. Uwanogho, D.A., Hardcastle, Z., Balogh, P., Mirza, G., Thornburg, K.L., Ragoussis, J., Sharpe, P.T. Genomics (1999) [Pubmed]
  13. Identification of novel iso/anteiso nonacosadienoic acids from the phospholipids of the sponges Chondrosia remiformis and Myrmekioderma styx. Carballeira, N.M., Reyes, E.D., Shalabi, F. J. Nat. Prod. (1993) [Pubmed]
  14. Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated in myotubular myopathy and type 4B Charcot-Marie-Tooth disease. Kim, S.A., Taylor, G.S., Torgersen, K.M., Dixon, J.E. J. Biol. Chem. (2002) [Pubmed]
  15. Autoantibodies in insulin-dependent diabetes recognize distinct cytoplasmic domains of the protein tyrosine phosphatase-like IA-2 autoantigen. Lampasona, V., Bearzatto, M., Genovese, S., Bosi, E., Ferrari, M., Bonifacio, E. J. Immunol. (1996) [Pubmed]
  16. Islet cell antibody frequency differs from that of glutamic acid decarboxylase antibodies/IA2 antibodies after diagnosis of diabetes. Borg, H., Marcus, C., Sjöblad, S., Fernlund, P., Sundkvist, G. Acta Paediatr. (2000) [Pubmed]
  17. Diagnostic value of carboxypeptidase-H autoantibodies in detecting latent autoimmune diabetes in adults. Zhou, Z.G., Yang, L., Huang, G. Hunan Yi Ke Da Xue Xue Bao (2003) [Pubmed]
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