Dual Specificity Tyrosine Phosphorylation Regulated Kinase 3 (DYRK3)

DYRK3 has been shown to autophosphorylate on tyrosine residue and catalyze phosphorylation of histones H3 and H2B in vitro. Human fetal brain DYRK3 cDNAs encode a deduced 553-amino acid protein containing a canonical kinase domain located between a large N-terminal region and a short C-terminal extension, and features specific to DYRK-related kinases. DYRK3 shares 43% identity with DYRK1 in the catalytic domain, but lacks the striking sequence motifs identified in DYRK1. The DYRK2 and DYRK3 proteins are related over their entire sequences except for the N-terminal region. Northern blot analysis of rat tissues detected strong Dyrk3 expression in testis, only after the onset of spermatogenesis, and very weak expression in spleen and adrenal gland.