Vav1 mutations identified in human cancers give rise to different oncogenic phenotypes

a Vav1 encodes the following domains: a calponin-homology (CH) domain; an acidic (AC) motif, which contains three tyrosine residues; a DBL homology (DH) domain; a pleckstrin homology (PH) domain; a C1 domain; two SRC-homology-3 (SH3) domains; and one SRC-homology-2 (SH2) domain. The location of mutations introduced in Vav1 is indicated above the protein structure and the location of truncation of oncVav1. b–d Sequence comparisons of the various domains of Vav1 in which mutations were introduced: CH (b), C1 (c), and carboxy SH3 (d) to the same domains in other members of the human Vav1 proteins, as well as to additional proteins that encode the same domains. Below the protein sequences is a key denoting positions which have a single, fully conserved residue (*), (:) indicates conservation between groups of strongly similar properties, semi-conservative mutations, and (.) indicates conservation between groups of weakly similar properties. [Clustal FAQ #Symbols. Clustal. Retrieved 8 December 2014]. A black arrow points to the residue mutated in each domain represented in this figure. Each residue in the alignment is assigned a color if the amino acid profile of the alignment at that position meets some minimum criteria specific for the residue type as described (http://www.jalview.org/help/html/colourSchemes/clustal.html