ASH2L

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; OMA:ASH2L - orthologs
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 26,306,024 bp [2] End 26,337,722 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in superficial temporal artery germinal epithelium gonad trabecular bone gingival epithelium ventricular zone tibialis anterior muscle embryo mucosa of paranasal sinus right testis Top expressed in seminiferous tubule spermatocyte maxillary prominence blastocyst mandibular prominence yolk sac ventricular zone medial ganglionic eminence spermatid abdominal wall More reference expression data BioGPS n/a
Gene ontology Molecular function euchromatin binding beta-catenin binding histone methyltransferase activity (H3-K4 specific) metal ion binding protein binding histone-lysine N-methyltransferase activity DNA binding Cellular component nucleoplasm MLL1 complex MLL3/4 complex 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 population proliferation positive regulation of transcription by RNA polymerase II beta-catenin-TCF complex assembly regulation of megakaryocyte differentiation histone H3-K4 methylation chromatin organization hemopoiesis 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: 26.31 – 26.34 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. Bibcode:2005Sci...307.1621B. 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. Bibcode:2005Natur.437.1173R. 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.