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

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    <!-- http://purl.obolibrary.org/obo/HINO_0004101 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0004101">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Beta-catenin/gamma catenin</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/HINO_0010602 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0010602">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Classic Cadherin</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/HINO_0010753 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0010753">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Interaction of cadherin with Beta/gamma catenin, alpha catenin and p120 catenin</rdfs:label>
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        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Authored: Matthews, L, 2009-05-15 19:26:33</rdfs:comment>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Edited: Matthews, L, 2009-08-26</rdfs:comment>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed16025097</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed16325583</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed17005550</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed17158740</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed18093941</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed7806582</ns3:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome Database ID Release 43419002</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_19131</rdfs:seeAlso>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reviewed: Ebnet, K, 2009-08-26</rdfs:comment>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">The cytoplasmic tails of classical cadherins form a multiprotein complex with alpha-catenin, beta/gamma-catenins and p120 catenin (p120ctn) (Gumbiner, 2005). Beta-catenin and p120ctn directly interact with the cadherin molecule through highly conserved regions in the membrane-distal and membrane-proximal domains, respectively, of the cadherin. The interactions with beta-catenin and p120ctn regulate cadherin localization at cell-cell contacts as well as its adhesive activity (Halbleib and Nelson, 2006). The association of beta-catenin and alpha-catenin probably serves to link the cadherin-catenin complex to the F-actin cytoskeleton through the protein ELPIN (Abe and Takeichi, 2008). Independently of its association with the cadherin-catenin complex, alpha-catenin also regulates the bundling and growth of actin filaments at sites of cell-cell contact formation (Drees et al., 2005; Weis and Nelson, 2006).</rdfs:comment>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/HINO_0021417 -->

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

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    <!-- http://purl.obolibrary.org/obo/UniProt_O60716 -->

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    <!-- http://purl.obolibrary.org/obo/UniProt_P35221 -->

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