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. 2017 Jan 26;292(11):4544–4555. doi: 10.1074/jbc.M116.765743

FIGURE 2.

FIGURE 2.

Domain graphic for human PPIP5Ks. Domain graphics are shown for the human PPIP5Ks used in this study (type 1, BC057395.1; type 2, XM_005271938). For PPIP5K1, amino acid residues defining each domain are numbered as in a previous study, which also defined the intrinsically disordered domain (IDR) (49). These boundaries were matched to those of the corresponding domains in PPIP5K2 by sequence alignments using Clustal Omega. The aligned intrinsically disordered domain boundaries in PPIP5K2 are consistent with those independently predicted from the PSIPRED Protein Sequence Analysis Workbench. The percent sequence identities across each of the three domains are also indicated. Also indicated are the nature and the locations of our engineered mutations in the kinase and phosphatase domains.