SR protein-specific kinase 1 is highly expressed in testis and phosphorylates protamine 1.

@article{Papoutsopoulou1999SRPK,
  title={SR protein-specific kinase 1 is highly expressed in testis and phosphorylates protamine 1.},
  author={Stamatia V. Papoutsopoulou and Eleni Nikolakaki and Georges Chalepakis and Volker Kruft and Philippe Chevaillier and Thomas Giannakouros},
  journal={Nucleic acids research},
  year={1999},
  volume={27 14},
  pages={2972-80}
}
Arginine/serine protein kinases constitute a novel class of enzymes that can modify arginine/serine (RS) dipeptide motifs. SR splicing factors that are essential for pre-mRNA splicing are among the best characterized proteins that contain RS domains. TwoSRprotein-specifickinases, SRPK1 and SRPK2, have been considered as highly specific for the phosphorylation of these proteins, thereby contributing to splicing regulation. However, despite the fact that SR proteins are more or less conserved… CONTINUE READING

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