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    <!-- http://purl.obolibrary.org/obo/HINO_0007116 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0007116">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Dephosphorylation of STAT1 by SHP2</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/HINO_0007117 -->

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    <!-- http://purl.obolibrary.org/obo/HINO_0007118 -->

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    <!-- http://purl.obolibrary.org/obo/HINO_0007119 -->

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    <!-- http://purl.obolibrary.org/obo/HINO_0007120 -->

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    <!-- http://purl.obolibrary.org/obo/HINO_0022257 -->

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        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Regulation of IFNA signaling</rdfs:label>
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        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Authored: Garapati, P V, 2010-07-07</rdfs:comment>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Edited: Garapati, P V, 2010-07-07</rdfs:comment>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">GENE ONTOLOGYGO:0060338</rdfs:seeAlso>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed10526574</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed16311601</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed16710296</ns3:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome Database ID Release 43912694</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_25216</rdfs:seeAlso>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reviewed: Abdul-Sater, AA, Schindler, C, 2010-08-17</rdfs:comment>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">There are several proteins and mechanisms involved in controlling the extent of ligand stimulation of IFNA/B signaling. These mechanisms can effect every step of the IFNA/B cascade. Dephosphorylation of JAK and STAT by SHP protein phosphatases, inhibition of STAT function in the nucleus by protein inhibitors of activated STATs (PIAS) proteins, inhibition of tyrosine kinase activity of JAKs by SOCS as well as inhibition of JAK and IFNAR2 interaction by UBP43 are few of the negative regulation mechanisms in controling type I IFN signaling.</rdfs:comment>
    </Class>
    


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