KAT7 (gene)

From Wikipedia, the free encyclopedia
  (Redirected from MYST2)
Jump to: navigation, search
Aliases KAT7, HBO1, HBOA, MYST2, ZC2HC7, lysine acetyltransferase 7
External IDs MGI: 2182799 HomoloGene: 5134 GeneCards: KAT7
RNA expression pattern
PBB GE MYST2 200049 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)


RefSeq (protein)


Location (UCSC) Chr 17: 49.79 – 49.84 Mb Chr 11: 95.27 – 95.31 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Histone acetyltransferase KAT7 is an enzyme that in humans is encoded by the KAT7 gene.[3][4][5] It specifically acetylates H4 histones at the lysine12 residue (H4K12)[6] and is necessary for origin licensing and DNA replication.[7][8] KAT7 associates with origins of replication during G1 phase of the cell cycle through complexing with CDT1.[9] Geminin is thought to inhibit the acetyltransferase activity of KAT7 when KAT7 and CDT1 are complexed together.[10]


KAT7 has been shown to interact with:


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b c 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. 
  4. ^ a b 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. 
  5. ^ "Entrez Gene: MYST2 MYST histone acetyltransferase 2". 
  6. ^ 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 98999Freely accessible. PMID 10839822. 
  7. ^ 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. 
  8. ^ 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 1347032Freely accessible. PMID 16428461. 
  9. ^ 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 2559906Freely accessible. PMID 18832067. 
  10. ^ a b 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 2818871Freely accessible. PMID 20129055. 
  11. ^ 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. 
  12. ^ 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. 
  13. ^ 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[edit]