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Chromobox homolog 3

HP1gamma, M32, CBX3
At the nuclear envelope, the nuclear lamina and heterochromatin are adjacent to the inner nuclear membrane. The protein encoded by this gene binds DNA and is a component of heterochromatin. This protein also can bind lamin B receptor, an integral membrane protein found in the inner nuclear membrane. The dual binding functions of the encoded protein may explain the association of heterochromatin with the inner nuclear membrane. This protein binds histone H3 tails methylated at Lys-9 sites. This protein is also recruited to sites of ultraviolet-induced DNA damage and double-strand breaks. Two transcript variants encoding the same protein but differing in the 5' UTR, have been found for this gene.[provided by RefSeq, Mar 2011] (from NCBI)
Papers on HP1gamma
Structural basis of the chromodomain of Cbx3 bound to methylated peptides from histone h1 and G9a.
Zang et al., Hefei, China. In Plos One, 2011
The Cbx3 chromodomain binds with comparable affinities to all of the methylated H3K9, H1K26 and G9aK185 peptides.
HP1γ links histone methylation marks to meiotic synapsis in mice.
Koseki et al., Yokohama, Japan. In Development, 2011
the role of the HP1gamma/G9a axis is to retain centromeric regions of unpaired homologous chromosomes in close alignment and facilitate progression of their pairing in early meiotic prophase
Epigenetic displacement of HP1 from heterochromatin by HIV-1 Vpr causes premature sister chromatid separation.
Ishizaka et al., Tokyo, Japan. In J Cell Biol, 2011
HIV-1 Vpr displaces heterochromatin protein 1-alpha and heterochromatin protein 1-gamma from chromatin, resulting in premature chromatid separation.
A role for heterochromatin protein 1γ at human telomeres.
Smith et al., New York City, United States. In Genes Dev, 2011
HP1gamma localizes to telomeres in S phase, where it is required to establish/maintain cohesion
Recruitment of the cohesin loading factor NIPBL to DNA double-strand breaks depends on MDC1, RNF168 and HP1γ in human cells.
Yamashita et al., Nagasaki, Japan. In Biochem Biophys Res Commun, 2011
this study reveals that human NIPBL is a novel protein recruited to DSB sites, and the recruitment is controlled by MDC1, RNF168 and HP1gamma.
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