Statements in which the resource exists.
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http://www.reactome.org/bio...rdf:typebiopax3:BiochemicalReactionlld:biopax3
http://www.reactome.org/bio...biopax3:commentAuthored: Nasi, S, Annibali, D, 2006-10-10 09:07:07lld:biopax3
http://www.reactome.org/bio...biopax3:commentReviewed: Greene, LA, 2007-11-08 15:39:37lld:biopax3
http://www.reactome.org/bio...biopax3:commentPhosphatidylinositides generated by PI3K recruit phosphatidylinositide-dependent protein kinase 1 (PDK1) and AKT (also known as protein kinase B) to the membrane, through their PH (pleckstrin-homology) domains. The binding of PIP3 to the PH domain of AKT is the rate-limiting step in AKT activation. In mammals there are three AKT isoforms (AKT1-3) encoded by three separate genes. The three isoforms share a high degree of amino acid identity and have indistinguishable substrate specificity in vitro. However, isoform-preferred substrates in vivo cannot be ruled out. The relative expression of the three isoforms differs in different mammalian tissues: AKT1 is the predominant isoform in the majority of tissues, AKT2 is the predominant isoform in insulin-responsive tissues, and AKT3 is the predominant isoform in brain and testes. All 3 isoforms are expressed in human and mouse platelets (Yin et al. 2008; O'Brien et al. 2008). Note: all data in the pathway refer to AKT1, which is the most studied.lld:biopax3
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