Fig. 2: Sequence alignment of human HIPK1–4 and DYRK1A kinase domains. | Nature Communications

Fig. 2: Sequence alignment of human HIPK1–4 and DYRK1A kinase domains.

From: Abemaciclib is a potent inhibitor of DYRK1A and HIP kinases involved in transcriptional regulation

Fig. 2

Sequence alignment of the kinase ___domain of human HIPKs and DYRK1A over the entire length of the crystallized HIPK3 construct (159–562). Secondary structure elements are indicated for HIPK3 as determined for the apo-HIPK3 structure. Characteristic sequence motifs, including the phosphorylated T-loop tyrosine, and functional regions are indicated. Serine/threonine or tyrosine residues found to be phosphorylated are circled magenta or green, respectively. Residues conserved in all kinases are boxed red, and those that are similar have red characters. The sequence alignment was prepared with MultAlin. The secondary structure alignment was prepared with ESPript. UniProt accession numbers are: Q86Z02 (HIPK1), Q9H2X6 (HIPK2), Q9H422 (HIPK3), Q8NE63 (HIPK4), and Q13627 (DYRK1A).

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