ASH2L

Set1/Ash2 histone methyltransferase complex subunit ASH2 is an enzyme that in humans is encoded by the ASH2L gene.[5][6]

ASH2L
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3RSN, 3S32, 3TOJ, 4RIQ, 4X8N, 4X8P, 5F6L, 5F6K
Identifiers
Aliases	ASH2L, ASH2, ASH2L1, ASH2L2, Bre2, ASH2 like histone lysine methyltransferase complex subunit, ASH2 like, histone lysine methyltransferase complex subunit
External IDs	OMIM: 604782 MGI: 1344416 HomoloGene: 3436 GeneCards: ASH2L
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8p11.23 Start 38,105,493 bp[1] End 38,144,076 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8|8 A2 Start 25,815,996 bp[2] End 25,847,694 bp[2]
Gene ontology Molecular function • euchromatin binding • beta-catenin binding • histone methyltransferase activity (H3-K4 specific) • metal ion binding • GO:0001948 protein binding • histone-lysine N-methyltransferase activity • DNA binding Cellular component • nuclear euchromatin • nucleoplasm • MLL1 complex • MLL3/4 complex • cell nucleus • histone methyltransferase complex • Set1C/COMPASS complex Biological process • regulation of transcription, DNA-templated • transcription, DNA-templated • cellular response to DNA damage stimulus • response to estrogen • positive regulation of cell proliferation • positive regulation of transcription from RNA polymerase II promoter • beta-catenin-TCF complex assembly • regulation of megakaryocyte differentiation • histone H3-K4 methylation • chromatin organization • haematopoiesis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9070	23808
Ensembl	ENSG00000129691	ENSMUSG00000031575
UniProt	Q9UBL3	Q91X20
RefSeq (mRNA)	NM_001105214 NM_001261832 NM_001282272 NM_004674	NM_001080793 NM_001286207 NM_011791 NM_001359012
RefSeq (protein)	NP_001098684 NP_001248761 NP_001269201 NP_004665	NP_001074262 NP_001273136 NP_035921 NP_001345941
Location (UCSC)	Chr 8: 38.11 – 38.14 Mb	Chr 8: 25.82 – 25.85 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

ASH2L has been shown to interact with MLL.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000129691 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031575 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Ikegawa S, Isomura M, Koshizuka Y, Nakamura Y (Jul 1999). "Cloning and characterization of ASH2L and Ash2l, human and mouse homologs of the Drosophila ash2 gene". Cytogenet. Cell Genet. 84 (3–4): 167–72. doi:10.1159/000015248. PMID 10393421. S2CID 19257499.
6. "Entrez Gene: ASH2L ash2 (absent, small, or homeotic)-like (Drosophila)".
7. Yokoyama A, Wang Z, Wysocka J, Sanyal M, Aufiero DJ, Kitabayashi I, Herr W, Cleary ML (Jul 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.

External links

• Human ASH2L genome location and ASH2L gene details page in the UCSC Genome Browser.

Further reading

• Wang J, Zhou Y, Yin B, Du G, Huang X, Li G, Shen Y, Yuan J, Qiang B (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. S2CID 6719550.
• Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW (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.
• Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W (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.
• Hughes CM, Rozenblatt-Rosen O, Milne TA, Copeland TD, Levine SS, Lee JC, Hayes DN, Shanmugam KS, Bhattacharjee A, Biondi CA, Kay GF, Hayward NK, Hess JL, Meyerson M (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, Sanyal M, Aufiero DJ, Kitabayashi I, Herr W, Cleary ML (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.
• Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Steward MM, Lee JS, O'Donovan A, Wyatt M, Bernstein BE, Shilatifard A (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. S2CID 19384238.