Regulatory subunit of the ATP-dependent NoRC-1 and NoRC-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:28801535). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). Directly stimulates the ATPase activity of SMARCA5 in the NoRC-5 ISWI chromatin remodeling complex (PubMed:28801535). The NoRC-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the NoRC-5 ISWI chromatin remodeling complex (PubMed:28801535). Within the NoRC-5 ISWI chromatin remodeling complex, mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing (By similarity). In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription (By similarity). Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac (By similarity). Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA-binding is required for heterochromatin formation and rDNA silencing (By similarity). Component of the NoRC-1 ISWI chromatin remodeling complex at least composed of SMARCA1 and BAZ2A/TIP5, which regulates the spacing of histone octamers on the DNA template to facilitate access to DNA (PubMed:28801535). Within the NoRC-1 ISWI chromatin remodeling complex interacts with SMARCA1; the interaction is direct (PubMed:28801535). Component of the NoRC-5 ISWI chromatin remodeling complex (also called the NoRC nucleolar-remodeling complex), at least composed of SMARCA5/SNF2H and BAZ2A/TIP5, which regulates the spacing of histone octamers on the DNA template to facilitate access to DNA (PubMed:28801535). Within the NoRC-5 ISWI chromatin remodeling complexes interacts with SMARCA5/SNF2H; the interaction is direct (PubMed:28801535). Interacts with TTF1; the interaction is required for recruitment of the NoRC-5 ISWI chromatin remodeling complex to rDNA (By similarity). Interacts with HDAC1 (By similarity). Interacts with SIN3A (By similarity). Interacts with DNMT1 and DNM3B (By similarity). Interacts with BEND3 and USP21 (PubMed:26100909). Colocalizes with the basal RNA polymerase I transcription factor UBF in the nucleolus. Expressed at moderate levels in most tissues analyzed, including heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. The bromo domain and the PHD-type zinc finger recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac). These 2 domains play a central role in the recruitment of chromatin silencing proteins such as DNMT1, DNMT3B and HDAC1. The MBD (methyl-CpG-binding) domain, also named TAM domain, specifically recognizes and binds a conserved stem-loop structure the association within pRNA. Binding to pRNA induces a conformational change of BAZ2A/TIP5 and is essential for targeting the NoRC complex to the nucleolus. Acetylation at Lys-680 by KAT8/MOF promotes its dissociation from pRNA, affecting heterochromatin formation, nucleosome positioning and rDNA silencing. Deacetylation by SIRT1 in late S phase enhances pRNA-binding, allowing de novo DNA methylation and heterochromatin formation. Acetylation is high during S phase and declines to background levels in late S phase when the silent copies of rRNA genes are replicated (By similarity). Ubiquitinated. Deubiquitinated by USP21 leading to its stabilization. Belongs to the WAL family. Contaminating sequence. Potential poly-A sequence. Truncated C-terminus.