HP1 alpha binds Histone H3K9(me)3

Stable Identifier
Reaction [binding]
Homo sapiens
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Chromobox (CBX) genes encode members of the Heterochromatin Protein (HP) family. HP1 was discovered in Drosophila as a dominant suppressor of position-effect variegation and a major component of heterochromatin. The HP1 family is evolutionarily conserved, with members in fungi, plants and animals. Most animal species have several HP1 isoforms; humans have HP alpha, beta and gamme encoded by the genes CBX5, CBX1 and CBX3 respectively.
The HP1 amino-terminal chromodomain binds methylated lysine-9 of histone H3, causing transcriptional repression (Lachner et al. 2001). A crystal structure of human HP1 alpha in complex with H3K9(me)3 peptide is available (Amaya et al. 2008). The highly-conserved carboxy-terminal chromoshadow domain enables dimerization and also serves as a docking site for proteins involved in a wide variety of nuclear functions, from transcription to nuclear architecture.

Literature References
PubMed ID Title Journal Year
  Human chromobox homolog 5 (CBX5) in complex with H3K9(me)3 peptide

Amaya, MF, Ravichandran, M, Loppnau, P, Kozieradzki, I, Edwards, AM, Arrowsmith, CH, Weigelt, J, Bountra, C, Bochkarev, A, Min, J, Ouyang, H

11242053 Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins

Lachner, M, O'Carroll, D, Rea, S, Mechtler, K, Jenuwein, T

Nature 2001
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Orthologous Events