Chromatin reader component of the NuA4 histone acetyltransferase (HAT) complex, a complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A (PubMed:12963728, PubMed:14966270). Specifically recognizes and binds acylated histone H3, with a preference for histone H3 diacetylated at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac) or histone H3 diacetylated at 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac) (PubMed:29437725, PubMed:30071723, PubMed:29900004). Also able to recognize and bind crotonylated histone H3 (PubMed:30071723). May also recognize and bind histone H3 succinylated at 'Lys-122' (H3K122succ); additional evidences are however required to confirm this result in vivo (PubMed:29463709). Plays a key role in histone variant H2AZ1/H2A.Z deposition into specific chromatin regions: recognizes and binds H3K14ac and H3K27ac on the promoters of actively transcribed genes and recruits NuA4-related complex to deposit H2AZ1/H2A.Z (PubMed:29437725). H2AZ1/H2A.Z deposition is required for maintenance of embryonic stem cell (By similarity). Component of numerous complexes with chromatin remodeling and histone acetyltransferase activity (PubMed:12963728, PubMed:14966270). Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6 (PubMed:12963728, PubMed:14966270). The NuA4 complex interacts with MYC and the adenovirus E1A protein (PubMed:12963728, PubMed:14966270). Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41 (PubMed:14966270, PubMed:29437725). Interacts with MLLT10/AF10 (PubMed:11756182). Also interacts with the SWI/SNF component SMARCB1/BAF47, TACC1 and TACC2, and the nuclear matrix protein NUMA1 (PubMed:10913114, PubMed:11903063, PubMed:12620397, PubMed:11756182). Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. The YEATS domain specifically recognizes and binds acylated histones, with a preference for histone H3 diacetylated at 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac). According to a report, recognizes and binds histone H3 succinylated at 'Lys-122' (H3K122succ) (PubMed:29463709). However, another report only observed poor binding with succinylated histone H3 (PubMed:30071723).