Thesmallregulatoryproteinubiquitinisoftencovalentlylinkedtomanycellularproteins,labelingthesetargetedproteinsforproteasome-mediateddegradation.UbiquitinisfirstactivatedbyformingathiolestercomplexwiththeE1activationcomponent.Activatedubiquitinissubsequentlytransferredtotheubiquitin-carrierproteinE2,andthentoanE3ubiquitinligaseforfinaldeliverytotheepsilon-NH2ofthetargetproteinlysineresidue.Theubiquitin-proteasomepathwayhasbeenimplicatedinawiderangeofbothnormalBIOLOGicalprocessesanddiseases.Theubiquitin-likeproteinfamilycontainsthreesmallubiquitin-relatedmodifierproteins(SUMO-1,-2and-3),neuralprecursorcell-expresseddevelopmentallydown-regulatedprotein8(NEDD8)andinterferon-stimulated15kDprotein(ISG15).TheircovalentattachmenttotargetproteinsisareversIBLe,multi-stepprocessthatisanalogoustoproteinubiquitination.MaturemoleculesarelinkedtotheactivatingenzymeE1,conjugatedtoE2andligatedtothetargetproteinsbyE3.UbiquitinisthepredominantregulatorforthedegradationofawiderangeoftargetproteinswhileSUMO,NEDD8andISG15modifyalimitedsetofsubstratestoregulatevariousotherbiologicalprocesses.Duringubiquitination,thecombinatorialinteractionofdifferentE2andE3proteinsproducesvariablesubstratespecificity.UBC3andUBC3BareE2ubiquitin-carrierproteins.TheSCF(Skp1/CUL1/F-box)E3ubiquitinligaseproteincomplexiscomposedofthreeproteincomponents,includingtheSphasekinaseassociatedprotein1(Skp1),Cullinhomolog1(CUL1)andtheSkp2F-boxprotein.

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