MYST3

K(lysine) acetyltransferase 6A

PDB rendering based on 1m36.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1M36, 2LN0, 2OZU, 2RC4, 3V43, 4LJN, 4LK9, 4LKA, 4LLB

Identifiers

Symbols

KAT6A ; MOZ; MRD32; MYST-3; MYST3; RUNXBP2; ZC2HC6A; ZNF220

External IDs

OMIM: 601408 MGI: 2442415 HomoloGene: 4924 IUPHAR: 2665 GeneCards: KAT6A Gene

EC number

2.3.1.48

Gene ontology
Molecular function	• DNA binding • chromatin binding • transcription coactivator activity • histone acetyltransferase activity • protein binding • transcription factor binding • zinc ion binding • acetyltransferase activity
Cellular component	• nucleosome • nucleus • nucleoplasm • nucleolus • Golgi apparatus • PML body • MOZ/MORF histone acetyltransferase complex
Biological process	• heart morphogenesis • DNA packaging • chromatin organization • nucleosome assembly • transcription, DNA-templated • protein acetylation • histone acetylation • myeloid cell differentiation • somatic stem cell maintenance • embryonic hemopoiesis • aorta morphogenesis • negative regulation of sequence-specific DNA binding transcription factor activity • histone H3 acetylation • negative regulation of transcription, DNA-templated • positive regulation of transcription, DNA-templated • face morphogenesis • cellular senescence
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 8:
41.93 – 42.05 Mb

Chr 8:
22.86 – 22.94 Mb

PubMed search

MYST histone acetyltransferase (monocytic leukemia) 3, also known as MYST3, is an enzyme that, in humans, is encoded by the MYST3 gene.^[1]^[2]

Function

MYST3 contains two nuclear localization domains, a C₂HC₃ zinc finger and an acetyltransferase domain. This structure suggests that MYST3 functions as a chromatin-bound acetyltransferase.^[2] MYST3 is important for proper development of hematopoietic stem cells.^[3]

References

↑ "Entrez Gene: MYST3 MYST histone acetyltransferase (monocytic leukemia) 3".
1 2 Borrow J, Stanton VP, Andresen JM, Becher R, Behm FG, Chaganti RS, Civin CI, Disteche C, Dubé I, Frischauf AM, Horsman D, Mitelman F, Volinia S, Watmore AE, Housman DE (September 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.
↑ Yang XJ, Ullah M (August 2007). "MOZ and MORF, two large MYSTic HATs in normal and cancer stem cells". Oncogene 26 (37): 5408–19. doi:10.1038/sj.onc.1210609. PMID 17694082.

Schuler GD, Boguski MS, Stewart EA, et al. (1996). "A gene map of the human genome.". Science 274 (5287): 540–6. doi:10.1126/science.274.5287.540. 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. doi:10.1002/(SICI)1098-2264(200006)28:2<138::AID-GCC2>3.0.CO;2-2. 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. PMC 125775. 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. PMC 139241. 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. doi:10.1016/S1535-6108(03)00051-5. 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. doi:10.1093/nar/gkg401. PMC 156734. 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. PMC 544007. 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. PMC 1201351. 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. PMC 1356129. 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. PMC 1865993. PMID 17182677.

PDB gallery

1m36: Solution Structure of a CCHC Zinc Finger from MOZ

2ozu: Crystal structure of human MYST histone acetyltransferase 3 in complex with acetylcoenzyme A

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MYST3

Function

References

Further reading