Reactome | Substitution of histidine residue with arginine at position ...

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created	[InstanceEdit:2399638] Orlic-Milacic, M, 2012-07-11
dbId	2399644
displayName	Substitution of histidine residue with arginine at position ...
literatureReference	[LiteratureReference:2399575] The oncogenic properties of mutant p110alpha and p110beta phosphatidylinositol 3-kinases in human mammary epithelial cells [LiteratureReference:2399562] The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations [LiteratureReference:2399617] Mutations in the catalytic subunit of class IA PI3K confer leukemogenic potential to hematopoietic cells [LiteratureReference:2399642] Regulation of lipid binding underlies the activation mechanism of class IA PI3-kinases
schemaClass	Summation
text	Substitution of histidine residue with arginine at position 1047 in the kinase domain of PIK3CA is predicted, based on PIK3CA crystal structure, to change the conformation of the activation loop (Huang et al. 2007). The PI3K complex containing PIK3CA H1047R mutant is constitutively active, in the absence of growth factors (Zhao et al. 2005, Horn et al. 2008), but its activity may be additional boosted by binding of PIK3R1 regulatory subunit to phosphopeptides generated by activated receptor tyrosine kinases (Hon et al. 2011).

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