Dual specificity tyrosine-phosphorylation-regulated kinase 2 is an
enzyme, in particular a
dual-specificity kinase, that in humans is encoded by the DYRK2gene.[5][6]
DYRK2 belongs to a family of protein
kinases whose members are presumed to be involved in cellular growth and development. The family is defined by structural similarity of their kinase domains and their capability to
autophosphorylate on tyrosine residues. DYRK2 has demonstrated tyrosine autophosphorylation and catalyzed phosphorylation of
histones H3 and H2B in vitro. Two
isoforms of DYRK2 have been isolated. The predominant isoform, isoform 1, lacks a 5' terminal insert.[6]
Dual specificity tyrosine-phosphorylation-regulated kinase 2 is an
enzyme, in particular a
dual-specificity kinase, that in humans is encoded by the DYRK2gene.[5][6]
DYRK2 belongs to a family of protein
kinases whose members are presumed to be involved in cellular growth and development. The family is defined by structural similarity of their kinase domains and their capability to
autophosphorylate on tyrosine residues. DYRK2 has demonstrated tyrosine autophosphorylation and catalyzed phosphorylation of
histones H3 and H2B in vitro. Two
isoforms of DYRK2 have been isolated. The predominant isoform, isoform 1, lacks a 5' terminal insert.[6]