MYST3

From Wikipedia, the free encyclopedia

MYST histone acetyltransferase (monocytic leukemia) 3

PDB rendering based on 1m36.

Available structures: 1m36, 2ozu

Identifiers

Symbol(s)

MYST3; MOZ; RUNXBP2; ZNF220

External IDs

OMIM: 601408 MGI: 2442415 HomoloGene: 4924

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

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006766 (mRNA)
NP_006757 (protein)

XM_146248 (mRNA)
XP_146248 (protein)

Location

Chr 8: 41.91 - 42.03 Mb

Chr 8: 24.33 - 24.41 Mb

Pubmed search

[1]

[2]

MYST histone acetyltransferase (monocytic leukemia) 3, also known as MYST3, is a human gene.^[1]

[edit] References

^ Entrez Gene: MYST3 MYST histone acetyltransferase (monocytic leukemia) 3.

[edit] Further reading

Schuler GD, Boguski MS, Stewart EA, et al. (1996). "A gene map of the human genome.". Science 274 (5287): 540–6. PMID 8849440.
Borrow J, Stanton VP, Andresen JM, et al. (1996). "The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein.". Nat. Genet. 14 (1): 33–41. doi:10.1038/ng0996-33. PMID 8782817.
Carapeti M, Aguiar RC, Goldman JM, Cross NC (1998). "A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia.". Blood 91 (9): 3127–33. PMID 9558366.
Chaffanet M, Gressin L, Preudhomme C, et al. (2000). "MOZ is fused to p300 in an acute monocytic leukemia with t(8;22).". Genes Chromosomes Cancer 28 (2): 138–44. PMID 10824998.
Champagne N, Pelletier N, Yang XJ (2001). "The monocytic leukemia zinc finger protein MOZ is a histone acetyltransferase.". Oncogene 20 (3): 404–9. doi:10.1038/sj.onc.1204114. PMID 11313971.
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.
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.
Deguchi K, Ayton PM, Carapeti M, et al. (2003). "MOZ-TIF2-induced acute myeloid leukemia requires the MOZ nucleosome binding motif and TIF2-mediated recruitment of CBP.". Cancer Cell 3 (3): 259–71. PMID 12676584.
Bristow CA, Shore P (2003). "Transcriptional regulation of the human MIP-1alpha promoter by RUNX1 and MOZ.". Nucleic Acids Res. 31 (11): 2735–44. PMID 12771199.
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.
Kindle KB, Troke PJ, Collins HM, et al. (2005). "MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by impairment of CBP function.". Mol. Cell. Biol. 25 (3): 988–1002. doi:10.1128/MCB.25.3.988-1002.2005. PMID 15657427.
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.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.
Collins HM, Kindle KB, Matsuda S, et al. (2006). "MOZ-TIF2 alters cofactor recruitment and histone modification at the RARbeta2 promoter: differential effects of MOZ fusion proteins on CBP- and MOZ-dependent activators.". J. Biol. Chem. 281 (25): 17124–33. doi:10.1074/jbc.M602633200. PMID 16613851.
Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
Kim SC, Sprung R, Chen Y, et al. (2006). "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.". Mol. Cell 23 (4): 607–18. doi:10.1016/j.molcel.2006.06.026. PMID 16916647.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
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.