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KAT7
Identifiers
Aliases	KAT7, HBO1, HBOA, MYST2, ZC2HC7, lysine acetyltransferase 7
External IDs	OMIM: 609880; MGI: 2182799; HomoloGene: 5134; GeneCards: KAT7; OMA:KAT7 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17q21.33 Start 49,788,648 bp End 49,835,026 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 D Start 95,165,085 bp End 95,201,072 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sural nerve testicle left testis Achilles tendon right testis ventricular zone gonad epithelium of colon popliteal artery tibial arteries Top expressed in spermatocyte ankle joint Rostral migratory stream zygote spermatid secondary oocyte seminiferous tubule tail of embryo cumulus cell granulocyte More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity DNA-binding transcription factor activity zinc ion binding metal ion binding histone acetyltransferase activity protein binding acyltransferase activity DNA replication origin binding DNA-binding transcription factor activity, RNA polymerase II-specific H4 histone acetyltransferase activity histone binding Cellular component nucleoplasm nucleolus histone acetyltransferase complex nucleus cytoplasm cytosol Biological process regulation of transcription, DNA-templated transcription, DNA-templated histone H4-K5 acetylation DNA replication histone H3 acetylation histone H4-K16 acetylation histone H4-K8 acetylation histone H4-K12 acetylation positive regulation of protein localization to nucleus stress-activated protein kinase signaling cascade positive regulation of transcription by RNA polymerase II response to sorbitol response to hydroxyurea response to actinomycin D response to dithiothreitol response to anisomycin positive regulation of histone H4 acetylation histone acetylation chromatin organization negative regulation of transcription, DNA-templated internal peptidyl-lysine acetylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11143 217127 Ensembl ENSG00000136504 ENSMUSG00000038909 UniProt O95251 Q5SVQ0 RefSeq (mRNA) NM_001199155 NM_001199156 NM_001199157 NM_001199158 NM_007067 NM_001346706 NM_001195003 NM_001195004 NM_177619 RefSeq (protein) NP_001186084 NP_001186085 NP_001186086 NP_001186087 NP_001333635 NP_008998 NP_001181932 NP_001181933 NP_808287 NP_001392123 NP_001392124 NP_001392125 NP_001392126 NP_001392127 NP_001392128 NP_001392129 NP_001392130 NP_001392131 NP_001392132 NP_001392133 NP_001392134 NP_001392135 NP_001392136 NP_001392137 NP_001392138 NP_001392139 NP_001392140 NP_001392141 NP_001392142 NP_001392143 NP_001392144 NP_001392145 NP_001392146 NP_001392147 NP_001392148 NP_001392149 NP_001392150 NP_001392151 NP_001392152 NP_001392153 NP_001392154 NP_001392155 NP_001392156 Location (UCSC) Chr 17: 49.79 – 49.84 Mb Chr 11: 95.17 – 95.2 Mb PubMed search
Wikidata
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Histone acetyltransferase KAT7 is an enzyme that in humans is encoded by the KAT7 gene. It specifically acetylates H4 histones at the lysine12 residue (H4K12) and is necessary for origin licensing and DNA replication. KAT7 associates with origins of replication during G1 phase of the cell cycle through complexing with CDT1. Geminin is thought to inhibit the acetyltransferase activity of KAT7 when KAT7 and CDT1 are complexed together.

Interactions

KAT7 has been shown to interact with:

• AR,
• CDT1,
• MCM2
• ORC1L and
• VIM,

References

1. ^ GRCh38: Ensembl release 89: ENSG00000136504 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000038909 – 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. ^ 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.
6. ^ 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.
7. "Entrez Gene: MYST2 MYST histone acetyltransferase 2".
8. Sterner DE, Berger SL (Jun 2000). "Acetylation of histones and transcription-related factors". Microbiology and Molecular Biology Reviews. 64 (2): 435–59. doi:10.1128/mmbr.64.2.435-459.2000. PMC 98999. PMID 10839822.
9. 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.
10. 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.
11. 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.
12. ^ 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.
13. 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.
14. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
15. 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. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.

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. PMC 3028655. PMID 21149574.
• 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. Bibcode:2002PNAS...99.7934S. 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. S2CID 23462168.
• 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. S2CID 9870877.
• 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. S2CID 14294292.
• 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. S2CID 7827573.
• 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.

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