Table 2.

Sequence alignments of the PH domain of AKT

Alignment of human AKT PH domain isoforms
AA numbers14 20 23 25 27 52 55
AKT1 PHMSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVA58
AKT2 PHMSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVA58
AKT3 PHMSDVTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLP-YPLNNFSVA57
AA numbers71 74 76
AKT1 PHQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGL110
AKT2 PHQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGL110
AKT3 PHKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVADRL109
Alignment of human (h) and mouse (m) AKT PH domains
AA numbers14 20 23 25 27 52 55
hAKT PHMSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQC
mAKT PHMNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQRESPLNNFSVAQC
AA numbers71 74 76
hAKT PHQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGL110
mAKT PHQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWATAIQTVADGL110
  • The PH domain binding residues are shown underlined in the sequence alignment above obtained using CLUSTAL W (1.82) multiple sequence alignment.