ID:BAZ2A_HUMAN DESCRIPTION: RecName: Full=Bromodomain adjacent to zinc finger domain protein 2A; AltName: Full=Transcription termination factor I-interacting protein 5; Short=TTF-I-interacting protein 5; Short=Tip5; AltName: Full=hWALp3; FUNCTION: Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. 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. 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. 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). SUBUNIT: Component of the NoRC complex, at least composed of SMARCA5/SNF2H and BAZ2A/TIP5. Interacts with TTF1; required for recruitment of the NoRC complex to rDNA. Interacts with DNMT1, DNM3B, HDAC1 and SIN3A (By similarity). INTERACTION: P16333:NCK1; NbExp=2; IntAct=EBI-934890, EBI-389883; SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity). Note=Colocalizes with the basal RNA polymerase I transcription factor UBF in the nucleolus (By similarity). TISSUE SPECIFICITY: Expressed at moderate levels in most tissues analyzed, including heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. DOMAIN: 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 recritment of chromatin silencing proteins such as DNMT1, DNMT3B and HDAC1. DOMAIN: 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 (By similarity). PTM: 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). PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. SIMILARITY: Belongs to the WAL family. SIMILARITY: Contains 4 A.T hook DNA-binding domains. SIMILARITY: Contains 1 bromo domain. SIMILARITY: Contains 1 DDT domain. SIMILARITY: Contains 1 MBD (methyl-CpG-binding) domain. SIMILARITY: Contains 1 PHD-type zinc finger. SEQUENCE CAUTION: Sequence=AAB60864.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; Sequence=BAG51228.1; Type=Erroneous termination; Positions=168; Note=Translated as Tyr;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9UIF9
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.