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Gene Review

PpY-55A  -  Protein phosphatase Y at 55A

Drosophila melanogaster

Synonyms: CG10930, D19, DmPpY-55A, Dmel\CG10930, PPY, ...
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High impact information on PpY-55A

  • We also demonstrate that PPY is a novel testis specific protein phosphatase by analysis of both mRNA and protein distribution [1].
  • Here we show by expression of cDNA in bacteria, that PPY is a protein serine phosphatase and that its biochemical properties are distinct from PP1 in both substrate specificity and regulation by the thermostable inhibitory proteins inhibitor 1 and inhibitor 2 [1].
  • More precise immunolocalisation within the testis, using affinity purified anti-PPY protein and anti-PPY peptide antibodies, shows that PPY is present in somatic cyst cells, which encase the germ cells [1].
  • The distribution of PPY, coupled with its unique biochemical properties, suggests that PPY may be required to prevent cyst cell division, increase transcription for provision of nutrients to the germ cells and/or provide a signal for spermatocyte differentiation [1].
  • The complete amino acid sequences of PPX, PPY and PPZ and an almost complete sequence of PPV are presented [2].

Biological context of PpY-55A

  • The deduced sequence of the protein, designated protein phosphatase-Y, is homologous to the catalytic subunits of Drosophila and rabbit protein phosphatase-1 alpha (64 and 59% identity, respectively) and rabbit protein phosphatase-2A (39% identity) [3].
  • PPYR1 moderately inhibits PPY activity, the inhibitory potential of the protein is slightly increased by phosphorylation [4].

Anatomical context of PpY-55A

  • The predominant location of PPY is in the nuclei of both head and tail cyst cells throughout the length of the testis except for the apical tip [1].

Associations of PpY-55A with chemical compounds


Physical interactions of PpY-55A


Other interactions of PpY-55A

  • The deduced amino acid sequence of PPN 58A exhibits 59-62% identity to D. melanogaster PP1 isoforms, 51% identity to D. melanogaster PPY 55A and < or = 40% identity to other members of the PPP family [5].

Analytical, diagnostic and therapeutic context of PpY-55A

  • The complex formation between PPY and PPYR1 was confirmed under in vitro and in vivo conditions by plasmon resonance spectroscopy, co-immunoprecipitation, and pull down experiments [4].


  1. Drosophila PPY, a novel male specific protein serine/threonine phosphatase localised in somatic cells of the testis. Armstrong, C.G., Mann, D.J., Berndt, N., Cohen, P.T. J. Cell. Sci. (1995) [Pubmed]
  2. Protein serine/threonine phosphatases; an expanding family. Cohen, P.T., Brewis, N.D., Hughes, V., Mann, D.J. FEBS Lett. (1990) [Pubmed]
  3. Molecular cloning and chromosomal localization of a novel Drosophila protein phosphatase. Dombrádi, V., Axton, J.M., Glover, D.M., Cohen, P.T. FEBS Lett. (1989) [Pubmed]
  4. CG15031/PPYR1 is an intrinsically unstructured protein that interacts with protein phosphatase Y. Kókai, E., Tantos, A., Vissi, E., Szöor, B., Tompa, P., Gausz, J., Alphey, L., Friedrich, P., Dombrádi, V. Arch. Biochem. Biophys. (2006) [Pubmed]
  5. Cloning of a novel testis specific protein serine/threonine phosphatase, PPN 58A, from Drosophila melanogaster. Armstrong, C.G., Dombradi, V., Mann, D.J., Cohen, P.T. Biochim. Biophys. Acta (1998) [Pubmed]
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