The Effects of Changing the Site of Activating Phosphorylation in CDK2 from Threonine to Serine*
Kaldis P, Cheng A, Solomon M. The Effects of Changing the Site of Activating Phosphorylation in CDK2 from Threonine to Serine*. Journal Of Biological Chemistry 2000, 275: 32578-32584. PMID: 10931829, DOI: 10.1074/jbc.m003212200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionCDC2-CDC28 KinasesCyclin-Dependent Kinase 2Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesHumansKineticsMutagenesis, Site-DirectedPhosphorylationProtein Serine-Threonine KinasesRecombinant Fusion ProteinsRecombinant ProteinsSerineSubstrate SpecificityThreonineConceptsWild-type Cdk2Cyclin-dependent kinasesThreonine residuesRNA polymerase IIDegradation of cyclinsHeLa cell extractsCell cycle progressionEssential phosphorylationHuman CDK2Efficient phosphorylationActivating PhosphorylationPolymerase IICyclin HTerminal domainHistone H1Cycle progressionCell extractsPhosphorylationCyclinCDK2General defectCAKKinaseSerineThreonineAnalysis of CAK activities from human cells
Kaldis P, Solomon M. Analysis of CAK activities from human cells. The FEBS Journal 2000, 267: 4213-4221. PMID: 10866826, DOI: 10.1046/j.1432-1327.2000.01455.x.Peer-Reviewed Original ResearchConceptsCdk-activating kinaseCAK activityHuman cellsTranscription factor IIHRNA polymerase IICyclin-dependent kinasesCell cycle progressionPolymerase IIThreonine residuesLarge subunitCyclin HTerminal domainSubstrate specificityCak1pKinase activityMonomeric enzymeMO15HeLa cellsATP analogKinaseSubunits