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    <!-- http://purl.obolibrary.org/obo/RO_0002233 -->

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    <!-- http://purl.obolibrary.org/obo/RO_0002234 -->

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    <!-- 
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    <!-- http://purl.obolibrary.org/obo/HINO_0006439 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0006439">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">HP1alpha:Histone H3 methylated at K9</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/HINO_0015211 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0015211">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Histone H3 methylated at lysine-9</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/HINO_0020165 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0020165">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">HP1 alpha binds Histone H3K9(me)3</rdfs:label>
        <rdfs:subClassOf rdf:resource="http://purl.obolibrary.org/obo/INO_0000040"/>
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                <someValuesFrom rdf:resource="http://purl.obolibrary.org/obo/UniProt_P45973"/>
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                <someValuesFrom rdf:resource="http://purl.obolibrary.org/obo/HINO_0015211"/>
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        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Authored: Akkerman, JW, 2010-10-29</rdfs:comment>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">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. &lt;br&gt;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.&lt;br&gt;</rdfs:comment>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Edited: Jupe, S, 2010-11-12</rdfs:comment>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed11242053</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed17224041</ns3:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome Database ID Release 43994106</rdfs:seeAlso>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome, http://www.reactome.org</ns3:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">ReactomeREACT_25059</rdfs:seeAlso>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reviewed: Ouwehand, WH, 2010-11-12</rdfs:comment>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/INO_0000040 -->

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    <!-- http://purl.obolibrary.org/obo/UniProt_P45973 -->

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