ID:BAZ1B_HUMAN DESCRIPTION: RecName: Full=Tyrosine-protein kinase BAZ1B; EC=2.7.10.2; AltName: Full=Bromodomain adjacent to zinc finger domain protein 1B; AltName: Full=Williams syndrome transcription factor; AltName: Full=Williams-Beuren syndrome chromosomal region 10 protein; AltName: Full=Williams-Beuren syndrome chromosomal region 9 protein; AltName: Full=hWALp2; FUNCTION: Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR- mediated transrepression of the CYP27B1 gene. In the WINAC complex, plays an essential role by targeting the complex to acetylated histones, an essential step for VDR-promoter association. CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. COFACTOR: Manganese. SUBUNIT: Interacts with MYO1C (By similarity). Interacts with CDT1. Interacts with SMARCA5/SNF2H; the interaction is direct and forms the WICH complex. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with VDR; in a ligand-dependent manner. Interacts with PCNA; the interaction is direct. INTERACTION: O60264:SMARCA5; NbExp=6; IntAct=EBI-927482, EBI-352588; SUBCELLULAR LOCATION: Nucleus. Note=Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase via its association with PCNA. TISSUE SPECIFICITY: Ubiquitously expressed with high levels of expression in heart, brain, placenta, skeletal muscle and ovary. DEVELOPMENTAL STAGE: Expressed at equal levels in 19-23 weeks old fetal tissues. DOMAIN: The N-terminal part (1-345), including the WAC domain and the C motif, mediates the tyrosine-protein kinase activity. DOMAIN: The bromo domain mediates the specific interaction with acetylated histones. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. DISEASE: Note=BAZ1B is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of BAZ1B may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. SIMILARITY: Belongs to the WAL family. BAZ1B subfamily. SIMILARITY: Contains 1 bromo domain. SIMILARITY: Contains 1 DDT domain. SIMILARITY: Contains 1 PHD-type zinc finger. SIMILARITY: Contains 1 WAC domain. SEQUENCE CAUTION: Sequence=AAC97879.1; Type=Frameshift; Positions=1031, 1042, 1422; Sequence=AAD04720.1; Type=Erroneous gene model prediction; Sequence=AAH65029.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; Sequence=BAA89210.1; Type=Frameshift; Positions=1478;
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 Q9UIG0
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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.
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
