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Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. Additionally we are shipping ASH2L Antibodies (108) and many more products for this protein.
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our results suggest that ASH2L contributes to leukemogenesis by cooperating with other proteins that aberrantly upregulate cellular growth and proliferation pathways.
Data suggest an interplay between megakaryocytic leukemia 1 (MKL1) and ASH2 protein to promote tumor necrosis factor alpha (TNF-alpha (show TNF Proteins)) induced proinflammatory transcription in macrophages.
the histone methyltransferase core enzyme ASH2L was bound at EGFR (show EGFR Proteins) in the germinal matrix and in gliomas where levels of H3K4me3 are high, and the histone acetyltransferase P300 (show EP300 Proteins) was bound in samples with H3K27ac enrichment
Ash2L acts in concert with P53 promoter occupancy to activate RNA Polymerase II by aiding formation of a stable transcription pre-initiation complex required for its activation.
ASH2L enhances ERalpha (show ESR1 Proteins) expression as a coactivator of GATA3 (show GATA3 Proteins) in breast cancers
Non active site mutations in the MLL1 SET domain render the protein defective for H3K4 dimethylation by the MLL1 core complex, which is associated with a loss of the ability of MLL1 to interact with WRAD or with the RbBP5 (show RBBP5 Proteins)/Ash2L heterodimer.
Data indicate that MLL1 methylates Ash2L in the absence of histone H3 (show HIST3H3 Proteins), but only when assembled within a complex with WDR5 (show WDR5 Proteins) and RbBP5 (show RBBP5 Proteins).
H2B dependent regulation of MLL (show MLL Proteins) family histone methylatransferases depends on the N-terminal WH motif of ASH2L.
crystal structure of the C-terminal SPRY domain of human Ash2L
The structure shows that Ash2L contains an atypical PHD (show PDC Proteins) finger that does not have histone tail-binding activity.
Ash2l-1 and Ash2l-2 are involved in the maintenance of mESCs pluripotency and the regulation of genomic H3K4me3.
We discuss the implications of these results to understand the role of ASH2L and Xist repeat E for histone modifications and escape gene regulation during random X-chromosome inactivation.
Ash2l is essential for pluripotency and maintaining open chromatin in embryonic stem cells
Tbx1 (show TBX1 Proteins) and Ash2l have overlapping mRNA and protein expression patterns during development.
Several candidate targets of complexes containing Ap2delta and Ash2l were identified that can be used to further elucidate their roles during development and showed that Fgfr3 (show FGFR3 Proteins) is a novel direct target of these complexes.
Ap2delta associates with ASH2L and MLL2 (ALR), forming a complex that methylates lysine 4 of histone H3.
Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis (By similarity).
, set1/Ash2 histone methyltransferase complex subunit ASH2