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The protein encoded by ZMYND11 was first identified by its ability to bind the adenovirus E1A protein. Additionally we are shipping ZMYND11 Antibodies (55) and many more products for this protein.
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This study identifies the BS69 C-terminal domains as an inhibitor of EBNA2.
BS69 has roles in gene repression and chromatin remodeling
In this study, we show that this translocation results in an in-frame translocation fusing exon 12 of the tumor suppressor gene ZMYND11 to exon 3 of the chromatin protein MBTD1 (show MBTD1 Proteins), encoding a protein of 1,054 amino acids
ZMYND11 represses gene expression by binding H3.3K36me3 and preventing transcription elongation.
We propose that BS69 specifically associates with H3K36me3-enriched chromatin through the PWWP domain, which facilitates the recruitment of MYND-bound transcription and chromatin remodeling factors
this study identifies an H3.3K36me3-specific reader and a regulator of intron retention and reveals that BS69 connects histone H3.3K36me3 to regulated RNA splicing, providing significant, important insights into chromatin regulation of pre-mRNA processing (show PRPF39 Proteins).
identification of ZMYND11 as an H3.3-specific reader of H3K36me3 that links the histone-variant-mediated transcription elongation control to tumor suppression
BRAM1 acts as a negative signal regulator located at the very proximal end of lymphotoxin beta receptor (show LTBR Proteins) complex assembly.
Data show significant association between the copy number variations of BS69 and some hematological malignancies.
Data found that BS69 directly interacted with TRAF3 (show TRAF3 Proteins), a negative regulator of NF-kappaB (show NFKB1 Proteins) activation. Results revealed that TRAF3 (show TRAF3 Proteins) was involved in the BS69-mediated suppression of LMP1 (show PDLIM7 Proteins)/CTAR1-induced NF-kappaB (show NFKB1 Proteins) activation.
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.
the C-terminal Mynd domain of BS69 (amino acids 516-561) or Mynd domains of the Caenorhabditis elegans proteins Bra-1 and Bra-2 bind not only to E1A but also to the Epstein-Barr virus EBNA2 oncoprotein and the Myc-related cellular protein MGA
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.
zinc finger, MYND-type containing 11
, zinc finger MYND domain-containing protein 11
, adenovirus 5 E1A-binding protein
, bone morphogenetic protein receptor-associated molecule 1
, zinc finger, MYND domain containing 11