ASH2L

From Wikipedia, the free encyclopedia

Ash2 (absent, small, or homeotic)-like (Drosophila)

Identifiers

ASH2L; ASH2; ASH2L1; ASH2L2

External IDs

OMIM: 604782 MGI: 1344416 HomoloGene: 3436

Gene ontology
Molecular Function:	• DNA binding • protein binding • zinc ion binding • transcription regulator activity • metal ion binding
Cellular Component:	• nucleus • histone methyltransferase complex
Biological Process:	• transcription • regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter • hemopoiesis

Orthologs

Human

Mouse

Refseq

NM_004674 (mRNA)
NP_004665 (protein)

NM_001080793 (mRNA)
NP_001074262 (protein)

Location

Chr 8: 38.08 - 38.12 Mb

Chr 8: 27.28 - 27.31 Mb

Pubmed search

[1]

[2]

Ash2 (absent, small, or homeotic)-like (Drosophila), also known as ASH2L, is a human gene.^[1]

[edit] References

^ Entrez Gene: ASH2L ash2 (absent, small, or homeotic)-like (Drosophila).

[edit] Further reading

Ikegawa S, Isomura M, Koshizuka Y, Nakamura Y (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. PMID 10393421.
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. 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. PMID 12477932.
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. PMID 12482968.
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. PMID 12670868.
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. 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. PMID 15199122.
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. PMID 15231748.
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. PMID 15489334.
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.