@prefix this: . @prefix sub: . @prefix beldoc: . @prefix rdfs: . @prefix rdf: . @prefix xsd: . @prefix dct: . @prefix dce: . @prefix pav: . @prefix np: . @prefix belv: . @prefix prov: . @prefix sfam: . @prefix proteinModification: . @prefix psimod: . @prefix go: . @prefix Protein: . @prefix geneProductOf: . @prefix hasAgent: . @prefix species: . @prefix occursIn: . @prefix pubmed: . @prefix orcid: . sub:Head { this: np:hasAssertion sub:assertion; np:hasProvenance sub:provenance; np:hasPublicationInfo sub:pubinfo; a np:Nanopublication . } sub:assertion { sub:_1 belv:variantOf sfam:AKT%20Family; a proteinModification:, psimod:00696 . sub:_2 hasAgent: sub:_3; a go:0016301 . sub:_3 geneProductOf: sfam:AKT%20Family; a Protein: . sub:_4 occursIn: species:9606; rdf:object sub:_2; rdf:predicate belv:directlyIncreases; rdf:subject sub:_1; a rdf:Statement . sub:assertion rdfs:label "p(SFAM:\"AKT Family\",pmod(P,T,308)) => kin(p(SFAM:\"AKT Family\"))" . } sub:provenance { beldoc: dce:description "Approximately 61,000 statements."; dce:rights "Copyright (c) 2011-2012, Selventa. All rights reserved."; dce:title "BEL Framework Large Corpus Document"; pav:authoredBy sub:_6; pav:version "20131211" . sub:_5 prov:value "We next examined the Akt T-loop Thr308 phosphorylation in wild-type and SIN1-/- cells. We found that although Ser473 phosphorylation was completely abolished in the SIN1-/- cells, Thr308 phosphorylation of Akt was not blocked (Figure 3A). These results indicate that SIN1 is not essential for Akt Thr308 phosphorylation and that the Ser473 phosphorylation is not a prerequisite for Thr308 phosphorylation. Akt, Singly Phosphorylated at Thr308, Remains Active and Functional in Response to Growth Factor Stimulation in SIN1-/- Cells Since Akt Thr308 phosphorylation was not dependent on Ser473 phosphorylation in SIN1-/- cells, we then asked whether this Thr308 singly phosphorylated Akt is still active and whether lack of Ser473 phosphorylation would have a global effect on the phosphorylation of Akt targets. Using an in vitro kinase assay, we found that Akt retained a substantial amount of enzymatic activity in SIN1-/- cells, although lower than that in wild-type cells (Figure 3B). Thus, singly phosphorylated (Thr308) Akt is an active but weaker enzyme."; prov:wasQuotedFrom pubmed:16962653 . sub:_6 rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:16962653; prov:wasDerivedFrom beldoc:, sub:_5 . } sub:pubinfo { this: dct:created "2014-07-03T14:33:03.254+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }