Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity; hexamerization is thoughtto be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity. Component of the NuA4 histone acetyltransferasecomplex which is involved in transcriptional activation of select genesprincipally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNAinteractions and promote interaction of the modified histones withother proteins which positively regulate transcription. This complex may be required for the activation oftranscriptional programs associated with oncogene and proto-oncogenemediated growth induction, tumor suppressor mediated growth arrest andreplicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least inpart, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sitesof DNA damage. Component of a SWR1-like complex thatspecifically mediates the removal of histone H2A. Z/H2AZ1 from thenucleosome. Proposed core component of the chromatinremodeling INO80 complex which exhibits DNA- and nucleosome-activatedATPase activity and catalyzes ATP-dependent nucleosome sliding. Plays an essential role inoncogenic transformation by MYC and also modulates transcriptionalactivation by the LEF1/TCF1-CTNNB1 complex. Essential for cell proliferation. May be able to bind plasminogen at cell surface and enhance plasminogenactivation. [1-3]

MKIEEVKSTTKTQRIASHSHVKGLGLDESGLAKQAASGLVGQENAREACGVIVELIKSKKMAGRAVLLAGPPGTGKTALALAIAQELGSKVPFCPMVGSEVYSTEIKKTEVLMENFRRAIGLRIKETKEVYEGEVTELTPCETENPMGGYGKTISHVIIGLKTAKGTKQLKLDPSIFESLQKERVEAGDVIYIEANSGAVKRQGRCDTYATEFDLEAEEYVPLPKGDVHKKKEIIQDVTLHDLDVANARPQGGQDILSMMGQLMKPKKTEITDKLRGEINKVVNKYIDQGIAELVPGVLFVDEVHMLDIECFTYLHRALESSIAPIVIFASNRGNCVIRGTEDITSPHGIPLDLLDRVMIIRTMLYTPQEMKQIIKIRAQTEGINISEEALNHLGEIGTKTTLRYSVQLLTPANLLAKINGKDSIEKEHVEEISELFYDAKSSAKILADQQDKYMK