Biology:KAT7 (gene)
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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:
References
- ↑ 1.0 1.1 1.2 "Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein". The Journal of Biological Chemistry 274 (33): 23027–34. Aug 1999. doi:10.1074/jbc.274.33.23027. PMID 10438470.
- ↑ 2.0 2.1 "Androgen receptor interacts with a novel MYST protein, HBO1". The Journal of Biological Chemistry 275 (45): 35200–8. Nov 2000. doi:10.1074/jbc.M004838200. PMID 10930412.
- ↑ "Entrez Gene: MYST2 MYST histone acetyltransferase 2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11143.
- ↑ "Acetylation of histones and transcription-related factors". Microbiology and Molecular Biology Reviews 64 (2): 435–59. Jun 2000. doi:10.1128/mmbr.64.2.435-459.2000. PMID 10839822.
- ↑ "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation". Molecular Cell 21 (1): 51–64. Jan 2006. doi:10.1016/j.molcel.2005.12.007. PMID 16387653.
- ↑ "Regulation of replication licensing by acetyltransferase Hbo1". Molecular and Cellular Biology 26 (3): 1098–108. Feb 2006. doi:10.1128/MCB.26.3.1098-1108.2006. PMID 16428461.
- ↑ "HBO1 histone acetylase is a coactivator of the replication licensing factor Cdt1". Genes & Development 22 (19): 2633–8. Oct 2008. doi:10.1101/gad.1674108. PMID 18832067.
- ↑ 8.0 8.1 "HBO1 histone acetylase activity is essential for DNA replication licensing and inhibited by Geminin". Molecular Cell 37 (1): 57–66. Jan 2010. doi:10.1016/j.molcel.2009.12.012. PMID 20129055.
- ↑ "Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1". The Journal of Biological Chemistry 276 (18): 15397–408. May 2001. doi:10.1074/jbc.M011556200. PMID 11278932.
- ↑ "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- ↑ "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. Sep 2005. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
Further reading
- "HBO1 is required for H3K14 acetylation and normal transcriptional activity during embryonic development". Molecular and Cellular Biology 31 (4): 845–60. Feb 2011. doi:10.1128/MCB.00159-10. PMID 21149574.
- "Retracted: Nuclear receptor function requires a TFTC-type histone acetyl transferase complex". Molecular Cell 9 (3): 553–62. Mar 2002. doi:10.1016/S1097-2765(02)00478-1. PMID 11931763.
- "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. Jul 2002. doi:10.1074/jbc.M202256200. PMID 11978794.
- "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. Jun 2002. doi:10.1073/pnas.122004799. PMID 12034878. Bibcode: 2002PNAS...99.7934S.
- "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease". Molecular Cell 15 (6): 853–65. Sep 2004. doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
- "Cyclin-dependent kinase 11(p58) interacts with HBO1 and enhances its histone acetyltransferase activity". FEBS Letters 579 (17): 3579–88. Jul 2005. doi:10.1016/j.febslet.2005.05.039. PMID 15963510.
- "Acetylation of HIV-1 integrase by p300 regulates viral integration". The EMBO Journal 24 (17): 3070–81. Sep 2005. doi:10.1038/sj.emboj.7600770. PMID 16096645.
- "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. Sep 2006. doi:10.1210/me.2005-0149. PMID 16645042.
- "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology 24 (10): 1285–92. Oct 2006. doi:10.1038/nbt1240. PMID 16964243.
- "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. Nov 2006. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- "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. Mar 2007. doi:10.1128/JVI.02257-06. PMID 17182677.
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