KAT6A

K(lysine) acetyltransferase 6A (KAT6A), is an enzyme that, in humans, is encoded by the KAT6A gene.[5][6] This gene is located on the back wing of human chromosome 8, band 8p11.21. [7]

KAT6A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1M36, 2LN0, 2OZU, 2RC4, 3V43, 4LJN, 4LK9, 4LKA, 4LLB
Identifiers
Aliases	KAT6A, MOZ, MYST3, RUNXBP2, ZC2HC6A, ZNF220, MRD32, MYST-3, lysine acetyltransferase 6A, ARTHS
External IDs	OMIM: 601408 MGI: 2442415 HomoloGene: 4924 GeneCards: KAT6A
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8p11.21 Start 41,929,479 bp[1] End 42,051,994 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8|8 A2 Start 22,859,535 bp[2] End 22,943,259 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • DNA binding • GO:0001105 transcription coactivator activity • transcription factor binding • metal ion binding • histone acetyltransferase activity • GO:0001948 protein binding • transferase activity, transferring acyl groups • acetyltransferase activity • zinc ion binding • H4 histone acetyltransferase activity • histone binding Cellular component • PML body • nucleosome • MOZ/MORF histone acetyltransferase complex • cell nucleus • nucleoplasm • nucleolus • cytosol • nuclear speck • histone acetyltransferase complex • nuclear chromatin Biological process • animal organ development • nucleosome assembly • myeloid cell differentiation • regulation of transcription, DNA-templated • DNA packaging • transcription, DNA-templated • positive regulation of transcription, DNA-templated • cellular senescence • histone H3 acetylation • negative regulation of transcription, DNA-templated • protein acetylation • regulation of signal transduction by p53 class mediator • histone acetylation • chromatin organization • histone H4 acetylation • positive regulation of transcription from RNA polymerase II promoter Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	7994	244349
Ensembl	ENSG00000083168	ENSMUSG00000031540
UniProt	Q92794	Q8BZ21
RefSeq (mRNA)	NM_001099412 NM_001099413 NM_001305878 NM_006766	NM_001081149 NM_001364449
RefSeq (protein)	NP_001292807 NP_006757	NP_001074618 NP_001351378
Location (UCSC)	Chr 8: 41.93 – 42.05 Mb	Chr 8: 22.86 – 22.94 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

KAT6A contains two nuclear localization domains, a C₂HC₃ zinc finger and an acetyltransferase domain. This structure suggests that KAT6A functions as a chromatin-bound acetyltransferase.[6] KAT6A is important for proper development of hematopoietic stem cells.[8]

Alternative names

• MYST3
• MOZ
• MRD32
• ZNF220
• RUNXBP2
• ZC2HC6A

References

1. GRCh38: Ensembl release 89: ENSG00000083168 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031540 - 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. "Entrez Gene: MYST3 MYST histone acetyltransferase (monocytic leukemia) 3".
6. 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.
7. - KAT6A NCBI
8. 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.

Further reading

• 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. doi:10.1182/blood.V91.9.3127. 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.