KAT8

K(lysine) acetyltransferase 8 (KAT8) is an enzyme that in humans is encoded by the KAT8 gene.

KAT8
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2GIV, 2PQ8, 2Y0M, 3QAH, 3TOA, 3TOB, 4DNC
Identifiers
Aliases	KAT8, MOF, MYST1, ZC2HC8, hMOF, lysine acetyltransferase 8, LIGOWS
External IDs	OMIM: 609912; MGI: 1915023; HomoloGene: 41676; GeneCards: KAT8; OMA:KAT8 - orthologs
Gene location (Human) Chr. Chromosome 16 (human) Band 16p11.2 Start 31,114,489 bp End 31,131,393 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7 F3|7 69.83 cM Start 127,511,688 bp End 127,525,009 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in cerebellar hemisphere right hemisphere of cerebellum right ovary left ovary corpus epididymis cerebellar vermis paraflocculus of cerebellum left uterine tube external globus pallidus apex of heart Top expressed in seminiferous tubule spermatocyte spermatid primary oocyte neural layer of retina hand muscle of thigh otolith organ tail of embryo utricle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity transcription factor binding metal ion binding histone acetyltransferase activity (H4-K8 specific) histone acetyltransferase activity histone acetyltransferase activity (H4-K5 specific) methylated histone binding protein binding histone acetyltransferase activity (H4-K16 specific) enzyme binding acetyltransferase activity acyltransferase activity histone binding Cellular component nucleoplasm chromosome MLL1 complex histone acetyltransferase complex nucleus kinetochore MSL complex nuclear matrix Biological process myeloid cell differentiation regulation of transcription, DNA-templated transcription, DNA-templated histone H4-K5 acetylation positive regulation of transcription, DNA-templated regulation of autophagy histone H4-K16 acetylation negative regulation of transcription, DNA-templated histone H4-K8 acetylation histone acetylation chromatin organization positive regulation of transcription by RNA polymerase II Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 84148 67773 Ensembl ENSG00000103510 ENSMUSG00000030801 UniProt Q9H7Z6 Q9D1P2 RefSeq (mRNA) NM_032188 NM_182958 NM_026370 NM_001360699 RefSeq (protein) NP_115564 NP_892003 NP_080646 NP_001347628 Location (UCSC) Chr 16: 31.11 – 31.13 Mb Chr 7: 127.51 – 127.53 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

The MYST family of histone acetyltransferases, which includes KAT8, was 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.

KAT8 is also known as MOF, and in humans hMOF. Given its fundamental role in modulating higher-order chromatin structure, hMOF is involved in many of the steps of the DNA damage response. The human hMOF gene encodes an enzyme that specifically acetylates histone H4 at lysine 16. The depletion of hMOF greatly decreases DNA double-strand break repair by both non-homologous end joining and homologous recombination. Thus MOF activity is critical for double-strand break repair.

Interactions

KAT8 has been shown to interact with MORF4L1.

Further reading

• Rea S, Xouri G, Akhtar A (August 2007). "Males absent on the first (MOF): from flies to humans". Oncogene. 26 (37): 5385–94. doi:10.1038/sj.onc.1210607. PMID 17694080. S2CID 12302768.
• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Kitabayashi I, Aikawa Y, Nguyen LA, Yokoyama A, Ohki M (December 2001). "Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein". The EMBO Journal. 20 (24): 7184–96. doi:10.1093/emboj/20.24.7184. PMC 125775. PMID 11742995.
• Pelletier N, Champagne N, Stifani S, Yang XJ (April 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. S2CID 19597517.
• Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM (December 2002). "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation". The Journal of Biological Chemistry. 277 (52): 50860–6. doi:10.1074/jbc.M203839200. PMID 12397079.
• Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J (November 2004). "Large-scale cDNA transfection screening for genes related to cancer development and progression". Proceedings of the National Academy of Sciences of the United States of America. 101 (44): 15724–9. Bibcode:2004PNAS..10115724W. doi:10.1073/pnas.0404089101. PMC 524842. PMID 15498874.
• Gupta A, Sharma GG, Young CS, Agarwal M, Smith ER, Paull TT, Lucchesi JC, Khanna KK, Ludwig T, Pandita TK (June 2005). "Involvement of human MOF in ATM function". Molecular and Cellular Biology. 25 (12): 5292–5305. doi:10.1128/MCB.25.12.5292-5305.2005. PMC 1140595. PMID 15923642.
• Dou Y, Milne TA, Tackett AJ, Smith ER, Fukuda A, Wysocka J, Allis CD, Chait BT, Hess JL, Roeder RG (June 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. S2CID 14717470.
• Taipale M, Rea S, Richter K, Vilar A, Lichter P, Imhof A, Akhtar A (August 2005). "hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells". Molecular and Cellular Biology. 25 (15): 6798–810. doi:10.1128/MCB.25.15.6798-6810.2005. PMC 1190338. PMID 16024812.
• Cereseto A, Manganaro L, Gutierrez MI, Terreni M, Fittipaldi A, Lusic M, Marcello A, Giacca M (September 2005). "Acetylation of HIV-1 integrase by p300 regulates viral integration". The EMBO Journal. 24 (17): 3070–81. doi:10.1038/sj.emboj.7600770. PMC 1201351. PMID 16096645.
• Smith ER, Cayrou C, Huang R, Lane WS, Côté J, Lucchesi JC (Nov 2005). "A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16". Molecular and Cellular Biology. 25 (21): 9175–88. doi:10.1128/MCB.25.21.9175-9188.2005. PMC 1265810. PMID 16227571.
• Topper M, Luo Y, Zhadina M, Mohammed K, Smith L, Muesing MA (March 2007). "Posttranslational acetylation of the human immunodeficiency virus type 1 integrase carboxyl-terminal domain is dispensable for viral replication". Journal of Virology. 81 (6): 3012–7. doi:10.1128/JVI.02257-06. PMC 1865993. PMID 17182677.

External links

• Overview of all the structural information available in the PDB for UniProt: Q9H7Z6 (Human Histone acetyltransferase KAT8) at the PDBe-KB.
• Overview of all the structural information available in the PDB for UniProt: Q9D1P2 (Mouse Histone acetyltransferase KAT8) at the PDBe-KB.