Fig. 4

PLK4 and MPS1 protein sequence alignment in humans and other vertebrate species. A PLK4 protein sequence alignment in vertebrates. Red letters show homology within a subgroup; the blue boxes show similarity, and red highlights identity. The conserved (blue boxes) and identical (red highlighted white letter) amino acids between species are shown, and residues susceptible to be phosphorylated by MPS1 (yellow) are also indicated. B–D MPS1 protein sequence alignment in vertebrates. The conserved amino acids between species are shown (blue boxes); identical conserved amino acids are shown (red highlighted white letter), and the residues are susceptible to being phosphorylated by PLK4 (yellow). E PLK4 and MPS1 kinase domains. I) PLK4 kinase domains. Four different domains reported earlier, and the possible phosphorylation sites mediated by MPS1 (P red), as well as the reported autophosphorylation sites [45] (P black), are indicated. II) MPS1 kinase domains. Seven domains were previously identified, and the possible phosphorylation sites mediated by PLK4 (P red) as well as the autophosphorylation site [46] (P black) are shown