KAT7 (gene)

K(lysine) acetyltransferase 7
Identifiers
Symbols	KAT7 ; HBO1; HBOA; MYST2; ZC2HC7
External IDs	OMIM: 609880 MGI: 2182799 HomoloGene: 5134 GeneCards: KAT7 Gene
EC number	2.3.1.48
Gene ontology Molecular function • transcription factor activity, sequence-specific DNA binding • histone acetyltransferase activity • protein binding • zinc ion binding Cellular component • histone acetyltransferase complex • nucleoplasm • nucleolus • cytoplasm Biological process • DNA replication • chromatin organization • transcription, DNA-templated • regulation of transcription, DNA-templated • histone H3 acetylation • histone H4-K5 acetylation • histone H4-K8 acetylation • histone H4-K12 acetylation • histone H4-K16 acetylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	11143	217127
Ensembl	ENSG00000136504	ENSMUSG00000038909
UniProt	O95251	Q5SVQ0
RefSeq (mRNA)	NM_001199155	NM_001195003
RefSeq (protein)	NP_001186084	NP_001181932
Location (UCSC)	Chr 17: 49.79 – 49.84 Mb	Chr 11: 95.27 – 95.31 Mb
PubMed search

Histone acetyltransferase KAT7 is an enzyme that in humans is encoded by the KAT7 gene.^[1][2][3] It specifically acetylates H4 histones at the lysine12 residue (H4K12)^[4] and is necessary for origin licensing and DNA replication.^[5][6] KAT7 associates with origins of replication during G1 phase of the cell cycle through complexing with CDT1.^[7] Geminin is thought to inhibit the acetyltransferase activity of KAT7 when KAT7 and CDT1 are complexed together.^[8]

Interactions

KAT7 has been shown to interact with:

• AR,^[2]
• CDT1,^[8]
• MCM2^[9][1]
• ORC1L^[1] and
• VIM,^[10][11]

References

1. Iizuka M, Stillman B (Aug 1999). "Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein". The Journal of Biological Chemistry 274 (33): 23027–34. doi:10.1074/jbc.274.33.23027. PMID 10438470.
2. Sharma M, Zarnegar M, Li X, Lim B, Sun Z (Nov 2000). "Androgen receptor interacts with a novel MYST protein, HBO1". The Journal of Biological Chemistry 275 (45): 35200–8. doi:10.1074/jbc.M004838200. PMID 10930412.
3. "Entrez Gene: MYST2 MYST histone acetyltransferase 2".
4. Sterner DE, Berger SL (Jun 2000). "Acetylation of histones and transcription-related factors". Microbiology and Molecular Biology Reviews 64 (2): 435–59. PMC 98999. PMID 10839822.
5. Doyon Y, Cayrou C, Ullah M, Landry AJ, Côté V, Selleck W, Lane WS, Tan S, Yang XJ, Côté J (Jan 2006). "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation". Molecular Cell 21 (1): 51–64. doi:10.1016/j.molcel.2005.12.007. PMID 16387653.
6. Iizuka M, Matsui T, Takisawa H, Smith MM (Feb 2006). "Regulation of replication licensing by acetyltransferase Hbo1". Molecular and Cellular Biology 26 (3): 1098–108. doi:10.1128/MCB.26.3.1098-1108.2006. PMC 1347032. PMID 16428461.
7. Miotto B, Struhl K (Oct 2008). "HBO1 histone acetylase is a coactivator of the replication licensing factor Cdt1". Genes & Development 22 (19): 2633–8. doi:10.1101/gad.1674108. PMC 2559906. PMID 18832067.
8. Miotto B, Struhl K (Jan 2010). "HBO1 histone acetylase activity is essential for DNA replication licensing and inhibited by Geminin". Molecular Cell 37 (1): 57–66. doi:10.1016/j.molcel.2009.12.012. PMC 2818871. PMID 20129055.
9. Burke TW, Cook JG, Asano M, Nevins JR (May 2001). "Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1". The Journal of Biological Chemistry 276 (18): 15397–408. doi:10.1074/jbc.M011556200. PMID 11278932.
10. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
11. Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.

Further reading

• Kueh AJ, Dixon MP, Voss AK, Thomas T (Feb 2011). "HBO1 is required for H3K14 acetylation and normal transcriptional activity during embryonic development". Molecular and Cellular Biology 31 (4): 845–60. doi:10.1128/MCB.00159-10. PMID 21149574.
• Yanagisawa J, Kitagawa H, Yanagida M, Wada O, Ogawa S, Nakagomi M, Oishi H, Yamamoto Y, Nagasawa H, McMahon SB, Cole MD, Tora L, Takahashi N, Kato S (Mar 2002). "Nuclear receptor function requires a TFTC-type histone acetyl transferase complex". Molecular Cell 9 (3): 553–62. doi:10.1016/S1097-2765(02)00478-1. PMID 11931763.
• Cervoni N, Detich N, Seo SB, Chakravarti D, Szyf M (Jul 2002). "The oncoprotein Set/TAF-1beta, an inhibitor of histone acetyltransferase, inhibits active demethylation of DNA, integrating DNA methylation and transcriptional silencing". The Journal of Biological Chemistry 277 (28): 25026–31. doi:10.1074/jbc.M202256200. PMID 11978794.
• Sharma D, Fondell JD (Jun 2002). "Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo". Proceedings of the National Academy of Sciences of the United States of America 99 (12): 7934–9. doi:10.1073/pnas.122004799. PMC 122998. PMID 12034878.
• Goehler H, Lalowski M, Stelzl U, Waelter S, Stroedicke M, Worm U, Droege A, Lindenberg KS, Knoblich M, Haenig C, Herbst M, Suopanki J, Scherzinger E, Abraham C, Bauer B, Hasenbank R, Fritzsche A, Ludewig AH, Büssow K, Buessow K, Coleman SH, Gutekunst CA, Landwehrmeyer BG, Lehrach H, Wanker EE (Sep 2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease". Molecular Cell 15 (6): 853–65. doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
• Zong H, Li Z, Liu L, Hong Y, Yun X, Jiang J, Chi Y, Wang H, Shen X, Hu Y, Niu Z, Gu J (Jul 2005). "Cyclin-dependent kinase 11(p58) interacts with HBO1 and enhances its histone acetyltransferase activity". FEBS Letters 579 (17): 3579–88. doi:10.1016/j.febslet.2005.05.039. PMID 15963510.
• Cereseto A, Manganaro L, Gutierrez MI, Terreni M, Fittipaldi A, Lusic M, Marcello A, Giacca M (Sep 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.
• Georgiakaki M, Chabbert-Buffet N, Dasen B, Meduri G, Wenk S, Rajhi L, Amazit L, Chauchereau A, Burger CW, Blok LJ, Milgrom E, Lombès M, Guiochon-Mantel A, Loosfelt H (Sep 2006). "Ligand-controlled interaction of histone acetyltransferase binding to ORC-1 (HBO1) with the N-terminal transactivating domain of progesterone receptor induces steroid receptor coactivator 1-dependent coactivation of transcription". Molecular Endocrinology 20 (9): 2122–40. doi:10.1210/me.2005-0149. PMID 16645042.
• Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (Oct 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 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, Mohammed K, Smith L, Muesing MA (Mar 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.