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The endogenous sequence encoding threonine residues at positions 305 and 306 was modified to encode valine and alanine by homologous recombination of a site directed mutagenized construct. The replacement of the threonine residues with nonphosphorylatable amino acids was designed to inhibit autophosphorylation of the targeted residues. Western blot analysis of homozygous mutant mice showed that normal sized protein was present at a level approximately two fold lower than that observed in wild-type mice. Further analysis using antibodies directed against phosphorylated threonine residues 305 and 286 showed immunoreactivity for only the latter. A single loxP site was left within the locus. (J:79714)