This gene encodes a subunit of several, distinct complexes involved in the repression or activation of transcription. The encoded protein can independently repress transcription and is targeted to replication foci throughout S phase by interacting directly with the N-terminus of DNA methyltransferase 1. During late S phase, histone deacetylase 2 is added to this complex, providing a means to deacetylate histones in transcriptionally inactive heterochromatin following replication. The encoded protein is also a component of the nucleosome acetyltransferase of H4 complex and interacts with the transcriptional corepressor tumor susceptibility gene 101 and the pro-apoptotic death-associated protein 6, among others. Alternatively spliced transcript variants encoding the same protein have been described.[3]
↑Rountree MR, Bachman KE, Baylin SB (Aug 2000). "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci". Nat Genet. 25 (3): 269–77. doi:10.1038/77023. PMID10888872.
↑Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O (Apr 2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (1): 65–73. doi:10.1093/dnares/7.1.65. PMID10718198.
↑Rountree MR, Bachman KE, Baylin SB (Jul 2000). "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci". Nat. Genet. 25 (3): 269–77. doi:10.1038/77023. PMID10888872.
↑Xin H, Yoon HG, Singh PB, Wong J, Qin J (Mar 2004). "Components of a pathway maintaining histone modification and heterochromatin protein 1 binding at the pericentric heterochromatin in Mammalian cells". J. Biol. Chem. 279 (10): 9539–46. doi:10.1074/jbc.M311587200. PMID14665632.
↑Liu Z, Fisher RA (Apr 2004). "RGS6 interacts with DMAP1 and DNMT1 and inhibits DMAP1 transcriptional repressor activity". J. Biol. Chem. 279 (14): 14120–8. doi:10.1074/jbc.M309547200. PMID14734556.
Further reading
Doyon Y, Côté J (2004). "The highly conserved and multifunctional NuA4 HAT complex". Curr. Opin. Genet. Dev. 14 (2): 147–54. doi:10.1016/j.gde.2004.02.009. PMID15196461.
Yang CS, Weiner H (2002). "Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol". Arch. Biochem. Biophys. 400 (1): 105–10. doi:10.1006/abbi.2002.2778. PMID11913976.
Cai Y, Jin J, Tomomori-Sato C, et al. (2003). "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex". J. Biol. Chem. 278 (44): 42733–6. doi:10.1074/jbc.C300389200. PMID12963728.
Xin H, Yoon HG, Singh PB, et al. (2004). "Components of a pathway maintaining histone modification and heterochromatin protein 1 binding at the pericentric heterochromatin in Mammalian cells". J. Biol. Chem. 279 (10): 9539–46. doi:10.1074/jbc.M311587200. PMID14665632.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Liu Z, Fisher RA (2004). "RGS6 interacts with DMAP1 and DNMT1 and inhibits DMAP1 transcriptional repressor activity". J. Biol. Chem. 279 (14): 14120–8. doi:10.1074/jbc.M309547200. PMID14734556.
Muromoto R, Sugiyama K, Takachi A, et al. (2004). "Physical and functional interactions between Daxx and DNA methyltransferase 1-associated protein, DMAP1". J. Immunol. 172 (5): 2985–93. doi:10.4049/jimmunol.172.5.2985. PMID14978102.
Muromoto R, Sugiyama K, Yamamoto T, et al. (2004). "Physical and functional interactions between Daxx and TSG101". Biochem. Biophys. Res. Commun. 316 (3): 827–33. doi:10.1016/j.bbrc.2004.02.126. PMID15033475.
Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID15345747.
Cai Y, Jin J, Florens L, et al. (2005). "The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes". J. Biol. Chem. 280 (14): 13665–70. doi:10.1074/jbc.M500001200. PMID15647280.
