spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

Right arrow Help viewing high resolution images
Right arrow Return to article
(Downloading may take up to 30 seconds.
If the slide opens in your browser, select File -> Save As to save it.)
Click on image to view larger version.


Figure 1


Fig. 1. Domain structure and covalent modifications of human WNK protein kinases. Phosphorylation sites that were identified on endogenous WNK1 isolated from control cells or sorbitol-stimulated cells (Zagorska et al., 2007) are highlighted in green and red, respectively. Further phosphorylation sites are in black and are reported on the PhosphoSitePlus website (http://www.phosphosite.org); the location of additional exons within the neuronal WNK1 splice variants is indicated. In addition, the neuronal isoforms are predicted to lack some of the N-terminal non-catalytic residues. Furthermore, the WNK1 variant that is found in brain and spinal cord reportedly lacks exons 11-12, whereas the variant found in the dorsal root ganglia and sciatic nerve cells lacks exon 11 (Shekarabi et al., 2008). Sequence alignment of the acidic segment of WNK isoforms is illustrated and reported PHAII-associated mutations of WNK4 are highlighted (E562K, D564A, Q565E, R1185C). The positions of domains and residues are drawn approximately to scale in each figure.





Right arrow Return to article