Histone chaperone that specifically mediates the genome-wide removal of histone H2A.Z/H2AZ1 from the nucleosome: removes H2A.Z/H2AZ1 from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AZ1 in the nucleosome. May stabilize the evicted H2A.Z/H2AZ1-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state (PubMed:24463511). Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis. Component of a SWR1-like complex, composed of EP400, KAT5/TIP60, TRRAP, BRD8, RUVBL1, RUVBL2, ING3 and ANP32E; the complex does not contain SRCAP. Interacts with H2A.Z/H2AZ1 (By similarity). Interacts with the importin alpha KPNA1 and KPNA2. Expressed at highest levels in cerebellum and spleen. In the cerebellum, expressed mainly in granule cells and, to a lesser extent, in Purkinje cells. Low levels are found at postnatal day 4. Levels increase from postnatal day 7 to postnatal day 17. Levels decrease and remain low in the adult. The H2A.Z-interacting domain (ZID) mediates a direct interaction with H2A.Z/H2AZ1. Phosphorylated. The phosphorylation is nuclear localization signal (NLS)-dependent (By similarity). No visible phenotype. Mice are viable and fertile (PubMed:20844742, PubMed:21049064, PubMed:23675506). They display a subtle neurological clasping phenotype and mild motor deficits (PubMed:20844742). Motor defects were not confirmed by a subsequent analysis (PubMed:23675506). Deletion in embryonic fibroblasts results in the appearance of a significant number of new H2A.Z/H2AZ1 around the transcription start site as well as at other chromatin regions (PubMed:24463511). Belongs to the ANP32 family.