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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Zinc finger, MYND-type containing 11

The protein encoded by this gene was first identified by its ability to bind the adenovirus E1A protein. The protein localizes to the nucleus. It functions as a transcriptional repressor, and expression of E1A inhibits this repression. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: E1A, Barr, LMP1, CAN, NF-kappaB
Papers on BS69
Recurrent translocation t(10;17)(p15;q21) in minimally differentiated acute myeloid leukemia results in ZMYND11/MBTD1 fusion.
Zwaan et al., Rotterdam, Netherlands. In Genes Chromosomes Cancer, Mar 2016
ZMYND11, also known as BS69, is a tumor suppressor that specifically recognizes H3K36me3, which is linked to aberrant HOXA expression in leukemogenesis.
The identification of loci for polydactyly in chickens using a genome-wide association study.
Guo et al., Beijing, China. In Gene, Oct 2015
The strongest association signal (rs317674023, P=5.48×10(-8)) residing nearby Bone Morphogenetic Protein Receptor-Associated Molecule 1 (BRAM1) was identified in the genomic region.
Histone H3.3 and cancer: A potential reader connection.
Shi et al., Shanghai, China. In Proc Natl Acad Sci U S A, Jul 2015
Interestingly, two recent studies identified BS69/ZMYND11, which was proposed to be a candidate tumor suppressor, as a specific reader for a modified form of H3.3 (H3.3K36me3).
BS69/ZMYND11 reads and connects histone H3.3 lysine 36 trimethylation-decorated chromatin to regulated pre-mRNA processing.
Shi et al., Shanghai, China. In Mol Cell, 2014
BS69 (also called ZMYND11) contains tandemly arranged PHD, BROMO, and PWWP domains, which are chromatin recognition modalities.
Cancer-testis antigen HCA587/MAGE-C2 interacts with BS69 and promotes its degradation in the ubiquitin-proteasome pathway.
Yin et al., Beijing, China. In Biochem Biophys Res Commun, 2014
We immunopurified HCA587-containing complex from HEK293 cells and identified BS69, a potential tumor suppressor, as an associated protein by mass spectrometry, and the following Immunoprecipitation and GST pull-down assays confirmed HCA587 interaction with BS69.
Structural and functional analysis of the DEAF-1 and BS69 MYND domains.
Sattler et al., München, Germany. In Plos One, 2012
The ligand binding and molecular functions of the related BS69 MYND domain were studied based on a homology model and mutational analysis.
Loss of Xenopus tropicalis EMSY causes impairment of gastrulation and upregulation of p53.
Smith et al., Cambridge, United Kingdom. In N Biotechnol, 2011
It also interacts with BS69 and HP1b, both of which are involved in chromatin remodelling, and with NIF-1 and DBC-1 in the regulation of nuclear receptor-mediated transcription.
High resolution ArrayCGH and expression profiling identifies PTPRD and PCDH17/PCH68 as tumor suppressor gene candidates in laryngeal squamous cell carcinoma.
Jarmuz et al., Poznań, Poland. In Genes Chromosomes Cancer, 2011
These were ATG7 (1/10 cell line), ZMYND11 (BS69) (1/10 cell line), PCDH17/PCH68 (9/10 cell lines), and PTPRD (7/10 cell lines).
The MYND domain-containing protein BRAM1 inhibits lymphotoxin beta receptor-mediated signaling through affecting receptor oligomerization.
Chang et al., Taiwan. In Cell Signal, 2011
BRAM1 acts as a negative signal regulator located at the very proximal end of lymphotoxin beta receptor complex assembly.
Analysis of copy number variations of BS69 in multiple types of hematological malignancies.
Huang et al., Shenzhen, China. In Ann Hematol, 2010
Data show significant association between the copy number variations of BS69 and some hematological malignancies.
BS69 cooperates with TRAF3 in the regulation of Epstein-Barr virus-derived LMP1/CTAR1-induced NF-kappaB activation.
Matsuda et al., Sapporo, Japan. In Febs Lett, 2010
Data found that BS69 directly interacted with TRAF3, a negative regulator of NF-kappaB activation. Results revealed that TRAF3 was involved in the BS69-mediated suppression of LMP1/CTAR1-induced NF-kappaB activation.
BS69 undergoes SUMO modification and plays an inhibitory role in muscle and neuronal differentiation.
Wan et al., Shenzhen, China. In Exp Cell Res, 2010
BS69 forms oligomers. The PHD and MYND domains are important for the cellular localization of BS69. PIAS1 and Ubc9 interact with BS69 and promote the sumoylation of BS69. BS69 plays inhibitory roles in both muscle and neuron differentiation.
Oligomerized TICAM-1 (TRIF) in the cytoplasm recruits nuclear BS69 to enhance NF-kappaB activation and type I IFN induction.
Seya et al., Sapporo, Japan. In Eur J Immunol, 2009
Knockdown of BS69 resulted in a decrease of IFN-beta induction, suggesting that BS69 is a positive regulator for the TLR3-TICAM-1 pathway and negative regulatory properties in NF-kappaB activation.
LMP1 TRAFficking activates growth and survival pathways.
Kieff et al., Boston, United States. In Adv Exp Med Biol, 2006
LMP1 TES1/CTAR1 directly recruits TRAFs 1, 2, 3 and 5 whereas LMP1 TES2/CTAR2 indirectly recruits TRAF6 via BS69.
EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer.
Kouzarides et al., Cambridge, United Kingdom. In Cell, 2003
EMSY is capable of silencing the activation potential of BRCA2 exon 3, associates with chromatin regulators HP1beta and BS69, and localizes to sites of repair following DNA damage.
Epstein-Barr virus latent membrane protein 1: structure and functions.
Chang et al., Taiwan. In J Biomed Sci, 2003
TRAFs, TRADD, RIP, JAK3, BRAM1, and p85.
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