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Bromodomain adjacent to zinc finger domain, 1B

WSTF, Williams syndrome transcription factor, BAZ1B, WBSCR9
This gene encodes a member of the bromodomain protein family. The bromodomain is a structural motif characteristic of proteins involved in chromatin-dependent regulation of transcription. This gene is deleted in Williams-Beuren syndrome, a developmental disorder caused by deletion of multiple genes at 7q11.23. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: SWI, Histone, POLYMERASE, V1a, CAN
Papers on WSTF
Haploinsufficiency of BAZ1B contributes to Williams syndrome through transcriptional dysregulation of neurodevelopmental pathways.
Kosik et al., Santa Barbara, United States. In Hum Mol Genet, Feb 2016
We show that haploinsufficiency of the ATP-dependent chromatin remodeler, BAZ1B, which is deleted in WS, significantly contributes to this differentiation defect.
Subnuclear domain proteins in cancer cells support the functions of RUNX2 in the DNA damage response.
Stein et al., Worcester, United States. In J Cell Sci, Mar 2015
We used proteomic analysis to identify RUNX2-dependent protein-protein interactions associated with the nuclear matrix in bone, breast and prostate tumor cell types and found that RUNX2 interacts with three distinct proteins that respond to DNA damage - RUVBL2, INTS3 and BAZ1B.
A cis-acting element in the promoter of human ether à go-go 1 potassium channel gene mediates repression by calcitriol in human cervical cancer cells.
Avila et al., Mexico. In Biochem Cell Biol, Feb 2015
The described mechanism in this work implies that a protein complex formed by the vitamin D receptor-interacting repressor, the vitamin D receptor, the retinoid X receptor, and the Williams syndrome transcription factor interact with the nVDRE in the hEAG1 promoter in the absence of ligand.
Genetic Variants Associated with Lipid Profiles in Chinese Patients with Type 2 Diabetes.
Yang et al., Beijing, China. In Plos One, 2014
Among 4,908 Chinese T2D patients who were not taking lipid-lowering medications, single nucleotide polymorphisms (SNPs) in seven genes previously found to be associated with lipid traits in genome-wide association studies conducted in populations of European ancestry (ABCA1, GCKR, BAZ1B, TOMM40, DOCK7, HNF1A, and HNF4A) were genotyped.
Nuclear myosin 1 contributes to a chromatin landscape compatible with RNA polymerase II transcription activation.
Percipalle et al., Stockholm, Sweden. In Bmc Biol, 2014
NM1 also co-localizes with the nucleosome remodeler SNF2h at class II promoters where they assemble together with WSTF as part of the B-WICH complex.
BAZ1B is dispensable for H2AX phosphorylation on Tyrosine 142 during spermatogenesis.
Namekawa et al., Cincinnati, United States. In Biol Open, 2014
Here we investigate the meiotic functions of BAZ1B (WSTF), the only known Tyr142 kinase in somatic cells, using mice possessing a conditional deletion of BAZ1B.
Importance of dietary calcium and vitamin D in the treatment of hypercalcaemia in Williams-Beuren syndrome.
Schreuder et al., In J Pediatr Endocrinol Metab, 2014
In the light of this new development we discuss the role of one of the deleted genes in WBS, Williams syndrome transcription factor (WSTF), in the etiology of hypercalcaemia in WBS.
Genome-wide association analyses identify 18 new loci associated with serum urate concentrations.
Gieger et al., Freiburg, Germany. In Nat Genet, 2013
By combining data from >140,000 individuals of European ancestry within the Global Urate Genetics Consortium (GUGC), we identified and replicated 28 genome-wide significant loci in association with serum urate concentrations (18 new regions in or near TRIM46, INHBB, SFMBT1, TMEM171, VEGFA, BAZ1B, PRKAG2, STC1, HNF4G, A1CF, ATXN2, UBE2Q2, IGF1R, NFAT5, MAF, HLF, ACVR1B-ACVRL1 and B3GNT4).
WSTF does it all: a multifunctional protein in transcription, repair, and replication.
Krebs et al., Anchorage, United States. In Biochem Cell Biol, 2011
This review describes the three known WSTF-containing complexes and discuss their various roles as well as mechanisms of regulating WSTF activity.
Williams syndrome is an epigenome-regulator disease.
Kato et al., Tokyo, Japan. In Endocr J, 2010
A human multi-protein complex (WINAC), composed of SWI/SNF components and DNA replication-related factors, that directly interacts with the vitamin D receptor (VDR) through the Williams syndrome transcription factor (WSTF), was identified with an ATP-dependent chromatin remodeling activity.
Animal models of Williams syndrome.
Osborne, Toronto, Canada. In Am J Med Genet C Semin Med Genet, 2010
The existing mouse models certainly seem to implicate hemizygosity for ELN, BAZ1B, CLIP2, and GTF2IRD1 in WS, and new mice with large deletions of the WS region are helping us to understand both the additive and potential combinatorial effects of hemizygosity for specific genes.
Phosphorylation of Williams syndrome transcription factor by MAPK induces a switching between two distinct chromatin remodeling complexes.
Kitagawa et al., Tokyo, Japan. In J Biol Chem, 2009
Phosphorylation of Williams syndrome transcription factor by MAPK induces a switching between two distinct chromatin remodeling complexes
Distinct function of 2 chromatin remodeling complexes that share a common subunit, Williams syndrome transcription factor (WSTF).
Kato et al., Tokyo, Japan. In Proc Natl Acad Sci U S A, 2009
Findings suggest that WSTF is shared and is a functionally indispensable subunit of 2 distinct chromatin remodeling complexes; WICH for DNA repair and WINAC for transcriptional control.
WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity.
Allis et al., New York City, United States. In Nature, 2009
WSTF phosphorylates Tyr 142 of H2A.X, and that WSTF activity has an important role in regulating several events that are critical for the DNA damage response
The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription.
Farrants et al., Stockholm, Sweden. In J Biol Chem, 2006
WSTF-SNF2h-NM1 forms a platform in transcription while providing chromatin remodeling
Chromatin remodelling and transcription: be-WICHed by nuclear myosin 1.
Farrants et al., Stockholm, Sweden. In Curr Opin Cell Biol, 2006
Insights into how these structural changes might be coordinated for RNA polymerase I (pol I) genes come from the discoveries of the nucleolar-remodelling complex (NoRC) and B-WICH--a high molecular weight fraction of the WSTF/SNF2h chromatin-remodelling complex.
The Williams syndrome transcription factor interacts with PCNA to target chromatin remodelling by ISWI to replication foci.
Varga-Weisz et al., Maglie, Italy. In Nat Cell Biol, 2004
Here we provide evidence that the Williams syndrome transcription factor (WSTF) is targeted to replication foci through direct interaction with the DNA clamp PCNA, an important coordinator of DNA and chromatin replication.
The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome.
Kato et al., Tokyo, Japan. In Cell, 2003
We identified a human multiprotein complex (WINAC) that directly interacts with the vitamin D receptor (VDR) through the Williams syndrome transcription factor (WSTF).
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