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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

Dyrk1a  -  dual-specificity tyrosine-(Y)...

Rattus norvegicus

Synonyms: Dual specificity YAK1-related kinase, Dual specificity tyrosine-phosphorylation-regulated kinase 1A, Dyrk, MNBH, PSK47, ...
 
 
 
 
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High impact information on Dyrk1a

  • The data suggest that Dyrk is a dual specificity protein kinase that is regulated by tyrosine phosphorylation in the activation loop and might be a component of a signaling pathway regulating nuclear functions [1].
  • A recombinant glutathione S-transferase-Dyrk fusion protein catalyzed autophosphorylation and histone phosphorylation on tyrosine and serine/threonine residues with an apparent Km of approximately 3.4 microM [1].
  • The cDNA of a novel, ubiquitously expressed protein kinase (Dyrk) was cloned from a rat brain cDNA library [1].
  • Exchange of two tyrosine residues in the "activation loop" between subdomains VII and VIII for phenylalanine almost completely suppressed the activity and tyrosine autophosphorylation of Dyrk [1].
 

Associations of Dyrk1a with chemical compounds

  • Dyrk, a dual specificity protein kinase with unique structural features whose activity is dependent on tyrosine residues between subdomains VII and VIII [1].

References

  1. Dyrk, a dual specificity protein kinase with unique structural features whose activity is dependent on tyrosine residues between subdomains VII and VIII. Kentrup, H., Becker, W., Heukelbach, J., Wilmes, A., Schürmann, A., Huppertz, C., Kainulainen, H., Joost, H.G. J. Biol. Chem. (1996) [Pubmed]
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