ASH2L

Ash2 (absent, small, or homeotic)-like (Drosophila)
Identifiers
Symbols	ASH2L; ASH2; ASH2L1; ASH2L2; Bre2
External IDs	OMIM: 604782 MGI: 1344416 HomoloGene: 3436 GeneCards: ASH2L Gene
Gene Ontology Molecular function • DNA binding • protein binding • histone methyltransferase activity (H3-K4 specific) • transcription regulatory region DNA binding • metal ion binding Cellular component • nucleus • histone methyltransferase complex • histone methyltransferase complex • Set1C/COMPASS complex • MLL1 complex Biological process • transcription, DNA-dependent • regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter • response to DNA damage stimulus • positive regulation of cell proliferation • chromatin modification • hemopoiesis • response to estrogen stimulus • histone H3-K4 methylation Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9070	23808
Ensembl	ENSG00000129691	ENSMUSG00000031575
UniProt	Q9UBL3	Q3UJ62
RefSeq (mRNA)	NM_001105214.1	NM_001080793
RefSeq (protein)	NP_001098684.1	NP_001074262
Location (UCSC)	Chr 8: 37.96 – 38 Mb	Chr 8: 26.93 – 26.96 Mb
PubMed search	[1]	[2]

Set1/Ash2 histone methyltransferase complex subunit ASH2 is an enzyme that in humans is encoded by the ASH2L gene.

Interactions

ASH2L has been shown to interact with MLL.

Further reading

• Wang J, Zhou Y, Yin B, et al. (2001). "ASH2L: alternative splicing and downregulation during induced megakaryocytic differentiation of multipotential leukemia cell lines". J. Mol. Med. 79 (7): 399–405. doi:10.1007/s001090100222. PMID 11466562. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Goo YH, Sohn YC, Kim DH, et al. (2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. 23 (1): 140–9. doi:10.1128/MCB.23.1.140-149.2003. PMC 140670. PMID 12482968. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=140670. 
• Wysocka J, Myers MP, Laherty CD, et al. (2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes Dev. 17 (7): 896–911. doi:10.1101/gad.252103. PMC 196026. PMID 12670868. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=196026. 
• Hughes CM, Rozenblatt-Rosen O, Milne TA, et al. (2004). "Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus". Mol. Cell 13 (4): 587–97. doi:10.1016/S1097-2765(04)00081-4. PMID 14992727. 
• Yokoyama A, Wang Z, Wysocka J, et al. (2004). "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression". Mol. Cell. Biol. 24 (13): 5639–49. doi:10.1128/MCB.24.13.5639-5649.2004. PMC 480881. PMID 15199122. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=480881. 
• Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442148. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153. 
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• Steward MM, Lee JS, O'Donovan A, et al. (2006). "Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes". Nat. Struct. Mol. Biol. 13 (9): 852–4. doi:10.1038/nsmb1131. PMID 16892064.