UniProtSummary | FUNCTION:NAD-dependentproteindeacetylase,whichregulatesprocessessuchasapoptosisandmuscledifferentiationbydeacetylatingkeyproteins.Deacetylates"Lys-382"ofp53/TP53andimpairsitsabilitytoinduceproapoptoticprogramandmodulatecellsenescence.DeacetylatesTAF1BandtherebyrepressesrDNAtranscriptionbytheRNApolymeraseI.InvolvedinHES1-andHEY2-mediatedtranscriptionalrepression.InhibitsskeletalmuscledifferentiationbydeacetylatingPCAFandMYOD1.MayserveasasensorofthecytosolicratioofNAD+/NADH,whichisessentialinskeletalmusclecelldifferentiation.Deacetylates"Lys-16"ofhistoneH4(invitro).ComponentoftheeNoSC(energy-dependentnucleolarsilencing)complex,acomplexthatmediatessilencingofrDNAinresponsetointracellularenergystatusandactsbyrecruitinghistone-modifyingenzymes.TheeNoSCcomplexisabletosensetheenergystatusofcell:uponglucosestarvation,elevationofNAD+/NADP+ratioactivatesSIRT1,leADIngtohistoneH3deacetylationfollowedbydimethylationofH3at"Lys-9"(H3K9me2)bySUV39H1andtheformationofsilentchromatinintherDNAlocus.IncaseofHIV-1infection,interactswithanddeacetylatestheviralTatprotein. CATALYTICACTIVITY:NAD++anacetylprotein=nicotinamide+O-acetyl-ADP-ribose+aprotein. COFACTOR:Binds1zincionpersubunitBysimilarity. ENZYMEREGULATION:Inhibitedbynicotinamide.Activatedbyresveratrol(3,5,4"-trihydroxy-trans-stilbene),butein(3,4,2",4"-tetrahydroxychalcone),piceatannol(3,5,3",4"-tetrahydroxy-trans-stilbene),Isoliquiritigenin(4,2",4"-trihydroxychalcone),fisetin(3,7,3",4"-tetrahydroxyflavone)andquercetin(3,5,7,3",4"-pentahydroxyflavone).RPS19BP1/AROSactsasapositiveregulatorofdeacetylationactivity.NegativelyregulatedbyKIAA1967/DBC1. SUBUNITSTRUCTURE:InteractswithTAF1B.FoundinacomplexwithPCAFandMYOD1Bysimilarity.ComponentoftheeNoSCcomplex,composedofSIRT1,SUV39H1andRRP8.InteractswithMLLT7/FOXO4,HES1,HEY2,p53/TP53andPML.InteractswithRPS19BP1/AROS.InteractswithKIAA1967/DBC1(viaN-terminus). SUBCELLULARLOCATION:Nucleus›PMLbody.Note:RecruitedtothenuclearbodiesviaitsinteractionwithPML. TISSUESPECIFICITY:Widelyexpressed. MISCELLANEOUS:Redwine,whichcontainsresveratrol,mayparticipateinactivationofsirtuinproteins,andmaythereforeparticipateinanextendedLifespanasithasbeenobservedinyeast. SEQUENCESIMILARITIES:Belongstothesirtuinfamily. Contains1deacetylasesirtuin-typedomain. SEQUENCECAUTIONS:ThesequenceAAH12499.1differsfromthatshown.Reason:Erroneousinitiation. |