MYST1

From Wikipedia, the free encyclopedia

MYST histone acetyltransferase 1

PDB rendering based on 1wgs.

Available structures: 1wgs, 2giv, 2pq8

Identifiers

Symbol(s)

MYST1; FLJ14040; MOF; hMOF

External IDs

OMIM: 609912 MGI: 1915023 HomoloGene: 41676

Gene ontology
Molecular Function:	• chromatin binding • histone acetyltransferase activity • transcription factor binding • zinc ion binding • acetyltransferase activity • transferase activity • metal ion binding
Cellular Component:	• chromatin • nucleus
Biological Process:	• chromatin assembly or disassembly • transcription • regulation of transcription, DNA-dependent • negative regulation of transcription • chromatin modification • histone acetylation • myeloid cell differentiation • positive regulation of transcription

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_032188 (mRNA)
NP_115564 (protein)

NM_026370 (mRNA)
NP_080646 (protein)

Location

Chr 16: 31.04 - 31.05 Mb

Chr 7: 127.7 - 127.72 Mb

Pubmed search

[1]

[2]

MYST histone acetyltransferase 1, also known as MYST1, is a human gene.^[1]

The MYST family of histone acetyltransferases, which includes MYST1, is named for the founding members MOZ (MYST3; MIM 601408), yeast YBF2 and SAS2, and TIP60 (HTATIP; MIM 601409). All members of this family contain a MYST region of about 240 amino acids with a canonical acetyl-CoA-binding site and a C2HC-type zinc finger motif. Most MYST proteins also have a chromodomain involved in protein-protein interactions and targeting transcriptional regulators to chromatin (Neal et al., 2000).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: MYST1 MYST histone acetyltransferase 1.

[edit] Further reading

Rea S, Xouri G, Akhtar A (2007). "Males absent on the first (MOF): from flies to humans.". Oncogene 26 (37): 5385-94. doi:10.1038/sj.onc.1210607. PMID 17694080.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.
Neal KC, Pannuti A, Smith ER, Lucchesi JC (2000). "A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF.". Biochim. Biophys. Acta 1490 (1-2): 170-4. PMID 10786633.
Kitabayashi I, Aikawa Y, Nguyen LA, et al. (2002). "Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein.". EMBO J. 20 (24): 7184-96. doi:10.1093/emboj/20.24.7184. PMID 11742995.
Pelletier N, Champagne N, Stifani S, Yang XJ (2002). "MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2.". Oncogene 21 (17): 2729-40. doi:10.1038/sj.onc.1205367. PMID 11965546.
Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM (2003). "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation.". J. Biol. Chem. 277 (52): 50860-6. doi:10.1074/jbc.M203839200. PMID 12397079.
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.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039.
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.
Wan D, Gong Y, Qin W, et al. (2004). "Large-scale cDNA transfection screening for genes related to cancer development and progression.". Proc. Natl. Acad. Sci. U.S.A. 101 (44): 15724-9. doi:10.1073/pnas.0404089101. PMID 15498874.
Gupta A, Sharma GG, Young CS, et al. (2005). "Involvement of human MOF in ATM function.". Mol. Cell. Biol. 25 (12): 5292-305. doi:10.1128/MCB.25.12.5292-5305.2005. PMID 15923642.
Dou Y, Milne TA, Tackett AJ, et al. (2005). "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.". Cell 121 (6): 873-85. doi:10.1016/j.cell.2005.04.031. PMID 15960975.
Taipale M, Rea S, Richter K, et al. (2005). "hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells.". Mol. Cell. Biol. 25 (15): 6798-810. doi:10.1128/MCB.25.15.6798-6810.2005. PMID 16024812.
Cereseto A, Manganaro L, Gutierrez MI, et al. (2005). "Acetylation of HIV-1 integrase by p300 regulates viral integration.". EMBO J. 24 (17): 3070-81. doi:10.1038/sj.emboj.7600770. PMID 16096645.
Smith ER, Cayrou C, Huang R, et al. (2005). "A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16.". Mol. Cell. Biol. 25 (21): 9175-88. doi:10.1128/MCB.25.21.9175-9188.2005. PMID 16227571.
Topper M, Luo Y, Zhadina M, et al. (2007). "Posttranslational acetylation of the human immunodeficiency virus type 1 integrase carboxyl-terminal domain is dispensable for viral replication.". J. Virol. 81 (6): 3012-7. doi:10.1128/JVI.02257-06. PMID 17182677.