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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 Proteins (2) and many more products for this protein.
Showing 10 out of 55 products:
Human Polyclonal ZMYND11 Primary Antibody for IHC, ELISA - ABIN1533904
Deloukas, Earthrowl, Grafham, Rubenfield, French, Steward, Sims, Jones, Searle, Scott, Howe, Hunt, Andrews, Gilbert, Swarbreck, Ashurst, Taylor, Battles, Bird, Ainscough, Almeida, Ashwell, Ambrose et al.: The DNA sequence and comparative analysis of human chromosome 10. ... in Nature 2004
Show all 2 references for ABIN1533904
Human Polyclonal ZMYND11 Primary Antibody for EIA, WB - ABIN453880
Yu, Shao, Zhang, Chen, Zhong, Zhang, Yang, Zhang, Wan: BS69 undergoes SUMO modification and plays an inhibitory role in muscle and neuronal differentiation. in Experimental cell research 2009
Show all 2 references for ABIN453880
Human Polyclonal ZMYND11 Primary Antibody for ELISA, WB - ABIN184908
Hateboer, Gennissen, Ramos, Kerkhoven, Sonntag-Buck, Stunnenberg, Bernards: BS69, a novel adenovirus E1A-associated protein that inhibits E1A transactivation. in The EMBO journal 1995
This study identifies the BS69 C-terminal domains as an inhibitor of EBNA2.
BS69 has roles in gene repression and chromatin remodeling
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 Antibodies).
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 Antibodies) 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 Antibodies), a negative regulator of NF-kappaB (show NFKB1 Antibodies) activation. Results revealed that TRAF3 (show TRAF3 Antibodies) was involved in the BS69-mediated suppression of LMP1 (show PDLIM7 Antibodies)/CTAR1-induced NF-kappaB (show NFKB1 Antibodies) 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 (show BCKDHA Antibodies) but also to the Epstein-Barr virus EBNA2 oncoprotein and the Myc (show MYC Antibodies)-related cellular protein MGA (show AGLU Antibodies)
BS69 controls E1A (show BCKDHA Antibodies) stability via inhibition of ubiquitination.
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