Chromatin Regulator | Alias | |||||||||||||||||||||||||||||||||||||||||||||||||
| KAT8 | MYST1;HMOF;MOF;ZC2HC8 | |||||||||||||||||||||||||||||||||||||||||||||||||
External Links: | Wiki GeneCards NCBI UniProt | |||||||||||||||||||||||||||||||||||||||||||||||||
Related histone modifications: | H2AK5ac;H3K4ac;H3K14ac;H3K27ac;H3K56ac;H4K5ac;H4K8ac;H4K12ac;H4K16ac | |||||||||||||||||||||||||||||||||||||||||||||||||
Introduction | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Full name: Lysine Acetyltransferase 8. KAT8 is a member of the MYST histone acetylase protein family,contains a C-terminal MYST domain which has the canonical acetyl CoA binding site,a C2HC-type zinc finger domain and a chromodomain(1).KAT8 has histone acetyltransferase activity directed toward histones H3,H2A and H4,is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac as part of male-specific lethal (MSL)complex(1-5).KAT8 interacts with MLL1 to form a MLL1-WDR5 complex which both have histone methyltransferase activity and acetyltransferase activity(6). | ||||||||||||||||||||||||||||||||||||||||||||||||||
Function and Interaction | ||||||||||||||||||||||||||||||||||||||||||||||||||
| KAT8 is the major enzyme to catalyze acetylation of histone H4 lysine 16(K16) and is highly conserved through evolution,plays important roles in DNA damage repair by modulating recruitment of DNA damage repair protein Mdc1(1,2,7).KAT8 interacts with MLL1 through a physical association,is involved in gene activation events(6).KAT8 regulates antioxidant gene expression by direct binding to promoter regions and acetylating histone H4 preferentially at lysine 16,is essential for female fertility(8). | ||||||||||||||||||||||||||||||||||||||||||||||||||
Disease Association | ||||||||||||||||||||||||||||||||||||||||||||||||||
| NA | ||||||||||||||||||||||||||||||||||||||||||||||||||
ChIP-Seq data
ChIP-Seq data of related histone modifications
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| Notice: For bigwiggle or bed file download, if the browser cannot automatically download the file, users can right click the hyperlink and then click the "Save link as..." button, which will automatically redirect to download dialogue box, or click the "Copy link address" button and access the website in a new tab page. For data analysis in Cistrome, users should first login into the Cistrome website, then press the "Send Bed" or "Send Big wiggle" button. For data download by Cistrome, users can follow this tutorial. | ||||||||||||||||||||||||||||||||||||||||||||||||||
References | ||||||||||||||||||||||||||||||||||||||||||||||||||
| 1.Neal, K.C., Pannuti, A., Smith, E.R., and Lucchesi, J.C. (2000). A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF. Biochim Biophys Acta 1490, 170-174. 2.Cai, Y., Jin, J., Swanson, S.K., Cole, M.D., Choi, S.H., Florens, L., Washburn, M.P., Conaway, J.W., and Conaway, R.C. (2010). Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J Biol Chem 285, 4268-4272. 3.Kadlec, J., Hallacli, E., Lipp, M., Holz, H., Sanchez-Weatherby, J., Cusack, S., and Akhtar, A. (2011). Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1. Nat Struct Mol Biol 18, 142-149. 4.Huang, J., Wan, B., Wu, L., Yang, Y., Dou, Y., and Lei, M. (2012). Structural insight into the regulation of MOF in the male-specific lethal complex and the non-specific lethal complex. Cell Res 22, 1078-1081. 5.Yuan, H., Rossetto, D., Mellert, H., Dang, W., Srinivasan, M., Johnson, J., Hodawadekar, S., Ding, E.C., Speicher, K., Abshiru, N., et al. (2012). MYST protein acetyltransferase activity requires active site lysine autoacetylation. EMBO J 31, 58-70. 6.Dou, Y., Milne, T.A., Tackett, A.J., Smith, E.R., Fukuda, A., Wysocka, J., Allis, C.D., Chait, B.T., Hess, J.L., and Roeder, R.G. (2005). Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell 121, 873-885. 7.Li, X., Corsa, C.A., Pan, P.W., Wu, L., Ferguson, D., Yu, X., Min, J., and Dou, Y. (2010). MOF and H4 K16 acetylation play important roles in DNA damage repair by modulating recruitment of DNA damage repair protein Mdc1. Mol Cell Biol 30, 5335-5347. 8.Yin, S., Jiang, X., Jiang, H., Gao, Q., Wang, F., Fan, S., Khan, T., Jabeen, N., Khan, M., Ali, A., et al. (2017). Histone acetyltransferase KAT8 is essential for mouse oocyte development by regulating reactive oxygen species levels. Development 144, 2165-2174. | ||||||||||||||||||||||||||||||||||||||||||||||||||
Figure Gallery
About Chromatin Regulator
Chromatin Regulator Cistrome
is a unique database integrating curated information of CRs, CR ChIP-seq datasets, CR related HM ChIP-seq datasets, and analysis of the relationship between CRs and HMs ChIP-seq pairs in human and mouse.