Recombinant Human Set1/Ash2 histone methyltransferase complex subunit ASH2 (ASH2L)

1. our results suggest that ASH2L contributes to leukemogenesis by cooperating with other proteins that aberrantly upregulate cellular growth and proliferation pathways. PMID: 28185526
2. different cancer mutations in MLL1 lead to a loss or increase in activity, illustrating the complex and tumor-specific role of MLL1 in carcinogenesis. PMID: 28182322
3. Overall, epigenetic modulation is a promising approach to evaluate the role of chromatin structure for the radioresponsiveness of glioma cell lines. PMID: 28044469
4. Data suggest an interplay between megakaryocytic leukemia 1 (MKL1) and ASH2 protein to promote tumor necrosis factor alpha (TNF-alpha) induced proinflammatory transcription in macrophages. PMID: 28218970
5. the histone methyltransferase core enzyme ASH2L was bound at EGFR in the germinal matrix and in gliomas where levels of H3K4me3 are high, and the histone acetyltransferase P300 was bound in samples with H3K27ac enrichment PMID: 25996283
6. 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. PMID: 25023704
7. ASH2L enhances ERalpha expression as a coactivator of GATA3 in breast cancers PMID: 25258321
8. 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/Ash2L heterodimer. PMID: 24680668
9. H2B dependent regulation of MLL family histone methylatransferases depends on the N-terminal WH motif of ASH2L. PMID: 23453805
10. crystal structure of the C-terminal SPRY domain of human Ash2L PMID: 22231628
11. The structure shows that Ash2L contains an atypical PHD finger that does not have histone tail-binding activity. PMID: 21660059
12. ASH2L binds DNA using a forkhead-like helix-wing-helix (HWH) domain. PMID: 21642971
13. NF-Y acts upstream of H3K4me3 deposition by recruiting Ash2L PMID: 21445285
14. Protein-arginine methyltransferase 1 (PRMT1) methylates Ash2L, a shared component of mammalian histone H3K4 methyltransferase complexes. PMID: 21285357
15. Data suggest that both Ash2L/RbBP5 and the MLL1 SET domain make direct contacts with the substrates and contribute to the formation of a joint catalytic center. PMID: 21124902
16. Results show that Depletion of CHD8 enhances HOXA2 expression and a loss of the WDR5/Ash2L/RbBP5 subcomplex. PMID: 20085832
17. Ash2l and Saf-A are recruited to the inactive X chromosome at the onset of stable X inactivation. PMID: 20150277
18. high dimethylation of histone H3 at lysine 4 expression is rare in hepatocellular carcinoma compared with other carcinomas, possibly due to complex epigenetic regulation involving Ash2 PMID: 19896696
19. These findings offer insight into the molecular role of ASH2L, and by extension that of WDR5, in proper H3K4 trimethylation. PMID: 16892064
20. Although hASH2 expression at the mRNA level was not deregulated, hASH2 protein expression was increased in most human tumors and tumor cell lines. Knockdown of hASH2 inhibited tumor cell proliferation. These show hASH2 as a novel oncoprotein. PMID: 18245475
21. The identified components revealed factors involved in histone methylation and cell cycle control and include Ash2L, RbBP5, WDR5, HCF-1, DBC-1, and EMSY. PMID: 19131338

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HGNC: 744

OMIM: 604782

KEGG: hsa:9070

STRING: 9606.ENSP00000340896

UniGene: Hs.521530