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. 2017 Jan 17;114(5):E879–E886. doi: 10.1073/pnas.1620315114

Fig. 1.

Fig. 1.

Phosphorylation sites in WNK4 present within a RRXS sequence. (A) Alignment of amino acid sequences of WNK4 from different vertebrate species. The five RRXS motifs present in WNK4 and the phosphorylatable serine in each of them are indicated. Numbering corresponds to mouse WNK4. (B) Schematic representation of WNK4. Known domains and motifs are indicated. Location of the RRXS sites is shown with asterisks. CC, coiled-coil domain (2); CC*, coiled-coil domain that is implicated in WNK homo- and heterodimerization (39); PF2-like, domain similar to the PF2 domain present in SPAK/OSR1 (49); PP1-BS, protein phosphatase 1 binding site (50); SPAK-BS: SPAK binding site (49). PHAII-causing mutations found in WNK4 lie within the acidic box. Only one has been reported outside this region (R1185C; R1164C in mouse WNK4) (2) and its position is indicated. See also Tables S1 and S2.