SUMOylation of DNA damage response and repair proteins (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="SUMOylation of DNA damage response and repair proteins" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">Several factors that participate in DNA damage response and repair are SUMOylated (reviewed in Dou et al. 2011, Bekker-Jensen and Mailand 2011, Ulrich 2012, Psakhye and Jentsch 2012, Bologna and Ferrari 2013, Flotho and Melchior 2013, Jackson and Durocher 2013). SUMOylation can alter enzymatic activity and protein stability or it can serve to recruit additional factors. For example, SUMOylation of Thymine DNA glycosylase (TDG) causes TDG to lose affinity for its product, an abasic site opposite a G residue, and thus increases turnover of the enzyme. During repair of double-strand breaks SUMO1, SUMO2, SUMO3, and the SUMO E3 ligases PIAS1 and PIAS4 accumulate at double-strand breaks where BRCA1, HERC1, RNF168, MDC1, and TP53BP1 are SUMOylated. SUMOylation of BRCA1 may increase its ubiquitin ligase activity while SUMOylation of MDC1 and HERC2 appears to play a role in recruitment of proteins such as RNF4 and RNF8 to double strand breaks. Similarly SUMOylation of RPA1 (RPA70) recruits RAD51 in the homologous recombination pathway. 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Type="Protein" GroupRef="d3889"> <BiopaxRef>fa1</BiopaxRef> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-3108231" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1511.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q8N3U4" /> </DataNode> <DataNode TextLabel="UBE2I-G97-SUMO1 " GraphId="f9ffd" Type="Protein" GroupRef="a49a3"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-2993783" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="940.0" CenterY="1391.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P63165" /> </DataNode> <DataNode TextLabel="SUMO1-HERC2 " GraphId="fab41" Type="Protein" GroupRef="bb48a"> <BiopaxRef>f77</BiopaxRef> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-4551752" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1151.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O95714" /> </DataNode> <DataNode TextLabel="UBE2I" GraphId="fafbd" Type="Protein"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Graphics CenterX="1390.5" CenterY="741.0" Width="53.0" Height="28.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P63279" /> </DataNode> <DataNode TextLabel="PHC3 " GraphId="fb0d1" Type="Protein" GroupRef="c2b35"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-389114" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1671.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q8NDX5" /> </DataNode> <DataNode TextLabel="SUMO1-C93-UBE2I " GraphId="fc172" Type="Protein" GroupRef="f78da"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-2993783" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1211.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P63279" /> </DataNode> <DataNode TextLabel="UBE2I-G93-SUMO2 " GraphId="fc2d0" Type="Protein" GroupRef="b6735"> <BiopaxRef>e0d</BiopaxRef> <BiopaxRef>f67</BiopaxRef> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-3899312" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="800.0" CenterY="1711.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P61956" /> </DataNode> <DataNode TextLabel="NUP155 " GraphId="fc6fe" Type="Protein" GroupRef="f7963"> <Attribute Key="cellular_location" Value="nuclear envelope" /> <Attribute Key="complex_id" Value="R-HSA-157689" /> <Attribute Key="copies_num" Value="286" /> <Graphics CenterX="660.0" CenterY="1551.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O75694" /> </DataNode> <DataNode TextLabel="UBE2I-G92-SUMO3 " GraphId="fd5bc" Type="Protein" GroupRef="b557e"> <BiopaxRef>f67</BiopaxRef> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-2993782" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="800.0" CenterY="1231.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P55854" /> </DataNode> <DataNode TextLabel="SUMO2:UBE2I" GraphId="fd937" Type="Complex"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Graphics CenterX="531.5" CenterY="870.5" Width="129.0" Height="31.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-2993778" /> </DataNode> <DataNode TextLabel="XPC" GraphId="fde01" Type="Protein"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Graphics CenterX="1209.5" CenterY="847.0" Width="65.0" Height="28.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q01831" /> </DataNode> <DataNode TextLabel="UBE2I,HDAC7" GraphId="fe026" Type="Complex"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Graphics CenterX="430.0" CenterY="682.5" Width="100.0" Height="27.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-3000385" /> </DataNode> <DataNode TextLabel="UBE2I:SUMO2,UBE2I:SUMO3" GraphId="fe2e1" Type="Complex"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Graphics CenterX="119.0" CenterY="344.0" Width="100.0" Height="44.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-3899312" /> </DataNode> <DataNode TextLabel="SUMO3-K65,K160,K490-PML" GraphId="fea4a" Type="Protein"> <Comment Source="Reactome">Fu et al. (2005) report that only lysine-160 is conjugated to SUMO3. Gong and Yeh (2006) report that lysine-65, lysine-160, and lysine-490 are conjugated to SUMO3.</Comment> <BiopaxRef>ef6</BiopaxRef> <BiopaxRef>e72</BiopaxRef> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Graphics CenterX="587.5" CenterY="789.0" Width="119.0" Height="36.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P29590" /> </DataNode> <DataNode TextLabel="SUMO1:SP100" GraphId="feb2f" Type="Complex"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Graphics CenterX="294.0" CenterY="1009.5" Width="112.0" Height="27.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-3730791" /> </DataNode> <DataNode TextLabel="3SUMO1:WRN" GraphId="ffe21" Type="Complex"> <BiopaxRef>f64</BiopaxRef> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Graphics CenterX="1267.0" CenterY="747.5" Width="122.0" Height="31.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-4568903" /> </DataNode> <DataNode TextLabel="SUMO3-C93-UBE2I " GraphId="fff2f" Type="Protein" GroupRef="b6d19"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-3899312" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1491.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P63279" /> </DataNode> <Interaction GraphId="a262f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="563.0" Y="53.0" GraphRef="da7f5" RelX="-1.0" RelY="0.0" /> <Point X="573.0" Y="85.0" GraphRef="c0152" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2997709" /> </Interaction> <Interaction GraphId="a2827"> <Comment Source="Reactome">TDG is SUMOylated at lysine-330 with SUMO1 by UBE2I (Hardeland et al. 2002, Baba et al. 2005, Steinacher et al. 2005, Knipscheer et al. 2008, Smet-Nocca et al. 2011). Conjugation of SUMO1 to TDG induces dissociation of TDG from its product, an abasic site, and increases turnover of TDG with G:U substrate but abolishes activity with G:T substrate (Hardeland et al. 2002).</Comment> <BiopaxRef>fb6</BiopaxRef> <BiopaxRef>f6b</BiopaxRef> <BiopaxRef>ab1</BiopaxRef> <BiopaxRef>be6</BiopaxRef> <BiopaxRef>b18</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="997.0" Y="616.0" /> <Point X="998.0" Y="699.0" /> <Anchor Position="0.0" Shape="None" GraphId="b0fa4" /> <Anchor Position="0.99" Shape="None" GraphId="e5792" /> <Anchor Position="0.5" Shape="None" GraphId="ed5c6" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551648" /> </Interaction> <Interaction GraphId="a29a9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1399.0" Y="176.0" GraphRef="db38b" RelX="-0.01999999999998181" RelY="0.6899999999999977" /> <Point X="1404.0" Y="225.0" GraphRef="eead6" RelX="0.9831932773109243" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551724" /> </Interaction> <Interaction GraphId="a2b59"> <Comment Source="Reactome">RANBP2 of the nuclear pore complex SUMOylates PML with SUMO1 at lysine-65, lysine-160, and lysine-490 (Sternsdorf et al. 1997, Kamitani et al. 1998, Duprez et al. 1999). SUMOylated PML is observed during interphase but not during mitosis (Everett et al. 1999). RANBP2 contains both a binding site for SUMO1 and a binding site for UBE2I (Tatham et al. 2005). The binding site for SUMO1 may play a role in SUMOylation of PML with SUMO1. Knockdown of RANBP2 reduces the number of PML bodies (Saitoh et al. 2006).</Comment> <BiopaxRef>eb2</BiopaxRef> <BiopaxRef>a4c</BiopaxRef> <BiopaxRef>a51</BiopaxRef> <BiopaxRef>eea</BiopaxRef> <BiopaxRef>f41</BiopaxRef> <BiopaxRef>eb9</BiopaxRef> <BiopaxRef>b2b</BiopaxRef> <BiopaxRef>dd5</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="296.0" Y="648.0" /> <Point X="297.0" Y="709.0" /> <Anchor Position="0.0" Shape="None" GraphId="ba3be" /> <Anchor Position="0.99" Shape="None" GraphId="d1d83" /> <Anchor Position="0.5" Shape="None" GraphId="ac250" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-5228508" /> </Interaction> <Interaction GraphId="a310e"> <Comment Source="Reactome">RANBP2 SUMOylates SP100 with SUMO1 at lysine-297 (Pichler et al. 2002, Tatham et al. 2005). RANBP2 has a binding site for SUMO1 and a binding site for UBE2I (UBC9) which may recruit the SUMO1:UBE2I (SUMO1:UBC9) complex (Tatham et al. 2005). RANBP2 is located on the cytoplasmic filaments of the nuclear pore so that SUMOylation may occur during nuclear import of SP100 (Pichler et al. 2002)</Comment> <BiopaxRef>eb9</BiopaxRef> <BiopaxRef>f0c</BiopaxRef> <BiopaxRef>ab1</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="345.0" Y="911.0" /> <Point X="345.0" Y="973.0" /> <Anchor Position="0.0" Shape="None" GraphId="f0c7b" /> <Anchor Position="0.99" Shape="None" GraphId="f41c6" /> <Anchor Position="0.5" Shape="None" GraphId="ba3cb" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000399" /> </Interaction> <Interaction GraphId="a343f"> <Comment Source="Reactome">TDG is SUMOylated at lysine-330 with SUMO2,3 by UBE2I and perhaps another E3 ligase (Hardeland et al. 2002, Baba et al. 2006, Hendriks et al. 2014, Tammsalu et al. 2014). SUMOylation increases turnover of TDG with G:U substrate and abolishes activity with G:T substrate (Hardeland et al. 2002).</Comment> <BiopaxRef>fb6</BiopaxRef> <BiopaxRef>d87</BiopaxRef> <BiopaxRef>f85</BiopaxRef> <BiopaxRef>c2a</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="924.0" Y="631.0" /> <Point X="927.0" Y="699.0" /> <Anchor Position="0.0" Shape="None" GraphId="e16e4" /> <Anchor Position="0.99" Shape="None" GraphId="ae172" /> <Anchor Position="0.5" Shape="None" GraphId="bd4b0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551738" /> </Interaction> <Interaction GraphId="a36af"> <Comment Source="Reactome">MDC1 is SUMOylated at lysine-1840 with SUMO2,3 (Luo et al. 2012, Hendriks et al. 2014, Tammsalu et al. 2014). SUMOylation is required for degradation of MDC1. SUMOylation of MDC1 is required for recruitment of RNF4 (Yin et al. 2012), which is believed to ubiquitinylate MDC1, resulting in degradation of MDC1.</Comment> <BiopaxRef>a95</BiopaxRef> <BiopaxRef>d87</BiopaxRef> <BiopaxRef>f85</BiopaxRef> <BiopaxRef>ac4</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="180.0" Y="395.0" /> <Point X="170.0" Y="453.0" /> <Anchor Position="0.0" Shape="None" GraphId="cc1ba" /> <Anchor Position="0.99" Shape="None" GraphId="e5117" /> <Anchor Position="0.5" Shape="None" GraphId="d0440" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570553" /> </Interaction> <Interaction GraphId="a5042"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="177.0" Y="64.0" GraphRef="c231e" RelX="-1.0" RelY="0.0" /> <Point X="144.0" Y="105.0" GraphRef="a7aa6" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568914" /> </Interaction> <Interaction GraphId="a52ea"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="984.0" Y="583.0" GraphRef="b1b80" RelX="1.0" RelY="-0.034482758620689655" /> <Point X="997.0" Y="616.0" GraphRef="b0fa4" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551648" /> </Interaction> <Interaction GraphId="a543a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="280.0" Y="343.0" GraphRef="b420a" RelX="-1.0" RelY="-0.03225806451612903" /> <Point X="287.0" Y="411.0" GraphRef="d9ca6" RelX="3.0" RelY="-2.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570554" /> </Interaction> <Interaction GraphId="a659d"> <Comment Source="Reactome">PIAS1,4 SUMOylate BRCA1 with SUMO2,3 (Galanty et al. 2009, Morris et al. 2009, Vialter et al. 2011, Hendriks et al. 2014). More SUMO2,3-BRCA1 than SUMO1-BRCA1 is observed in vivo (Morris et al. 2009, Galanty et al. 2009). SUMOylation with SUMO2,3 increases in response to oxidative stress (Vialter et al. 2011). SUMOylation of BRCA1 increases its ubiquitin ligase activity (Morris et al. 2009).</Comment> <BiopaxRef>f3e</BiopaxRef> <BiopaxRef>ca1</BiopaxRef> <BiopaxRef>e73</BiopaxRef> <BiopaxRef>d87</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="422.0" Y="88.0" /> <Point X="423.0" Y="156.0" /> <Anchor Position="0.0" Shape="None" GraphId="ef076" /> <Anchor Position="0.99" Shape="None" GraphId="e034a" /> <Anchor Position="0.5" Shape="None" GraphId="b4014" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2997616" /> </Interaction> <Interaction GraphId="a7a51"> <Comment Source="Reactome">UBE2I (UBC9) alone and in association with HDAC7 can SUMOylate PML with SUMO1 at lysine-65, lysine-160, and lysine-490 (Sternsdorf et al. 1997, Kamitani et al. 1998, Duprez et al. 1999, Knipscheer et al. 2008). SUMOylated PML is observed during interphase but not during mitosis (Everett et al. 1999). Knockdown of HDAC7 reduces the number of PML bodies (Gao et al. 2008).</Comment> <BiopaxRef>eb2</BiopaxRef> <BiopaxRef>a4c</BiopaxRef> <BiopaxRef>a51</BiopaxRef> <BiopaxRef>eea</BiopaxRef> <BiopaxRef>f41</BiopaxRef> <BiopaxRef>b42</BiopaxRef> <BiopaxRef>dd5</BiopaxRef> <BiopaxRef>ab1</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="517.0" Y="643.0" /> <Point X="517.0" Y="720.0" /> <Anchor Position="0.0" Shape="None" GraphId="d929a" /> <Anchor Position="0.99" Shape="None" GraphId="d4a4a" /> <Anchor Position="0.5" Shape="None" GraphId="ac1b1" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000383" /> </Interaction> <Interaction GraphId="a7b86"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="133.0" Y="68.0" GraphRef="e3864" RelX="0.9710144927536232" RelY="0.0" /> <Point X="144.0" Y="105.0" GraphRef="a7aa6" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568914" /> </Interaction> <Interaction GraphId="aa9c7"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="170.0" Y="453.0" GraphRef="e5117" RelX="-0.09999999999999432" RelY="0.5799999999999841" /> <Point X="225.0" Y="488.0" GraphRef="f62e5" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570553" /> </Interaction> <Interaction GraphId="ab1af"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1389.0" Y="453.0" GraphRef="fed41" RelX="0.0" RelY="0.5900000000000318" /> <Point X="1389.0" Y="491.0" GraphRef="f1083" RelX="-1.0" RelY="-0.03225806451612903" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551604" /> </Interaction> <Interaction GraphId="ab9e4"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="533.0" Y="454.0" GraphRef="d323c" RelX="0.0" RelY="0.7200000000000273" /> <Point X="549.0" Y="496.0" GraphRef="f9910" RelX="0.984" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568863" /> </Interaction> <Interaction GraphId="abcea"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="399.0" Y="67.0" GraphRef="bdecc" RelX="0.9805825242718447" RelY="-0.023255813953488372" /> <Point X="422.0" Y="88.0" GraphRef="ef076" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2997616" /> </Interaction> <Interaction GraphId="acd23"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1350.0" Y="427.0" GraphRef="eede8" RelX="1.0" RelY="0.0" /> <Point X="1389.0" Y="425.0" GraphRef="a864f" RelX="0.0" RelY="1.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551604" /> </Interaction> <Interaction GraphId="ace6c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="424.0" Y="884.0" GraphRef="cc9fe" RelX="0.0" RelY="1.0" /> <Point X="451.0" Y="921.0" GraphRef="a617e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000348" /> </Interaction> <Interaction GraphId="ad0a1"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1284.0" Y="603.0" GraphRef="f1dbf" RelX="0.9649122807017544" RelY="-0.037037037037037035" /> <Point X="1320.0" Y="641.0" GraphRef="e8a36" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568846" /> </Interaction> <Interaction GraphId="ad87a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="110.0" Y="803.0" GraphRef="e762a" RelX="0.9813084112149533" RelY="-0.022222222222222223" /> <Point X="451.0" Y="936.0" GraphRef="c680a" RelX="-0.5" RelY="-10.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000348" /> </Interaction> <Interaction GraphId="aed0a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="280.0" Y="343.0" GraphRef="b420a" RelX="-1.0" RelY="-0.03225806451612903" /> <Point X="283.0" Y="386.0" GraphRef="fd0c6" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570554" /> </Interaction> <Interaction GraphId="af271"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="385.0" Y="575.0" GraphRef="f2709" RelX="-1.0" RelY="-0.04" /> <Point X="296.0" Y="648.0" GraphRef="ba3be" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-5228508" /> </Interaction> <Interaction GraphId="affec"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1321.0" Y="708.0" GraphRef="f8d17" RelX="0.009999999999990905" RelY="0.6699999999999591" /> <Point X="1328.0" Y="747.0" GraphRef="ffe21" RelX="1.0" RelY="-0.03225806451612903" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568846" /> </Interaction> <Interaction GraphId="b0984"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="452.0" Y="971.0" GraphRef="f6126" RelX="0.009999999999990905" RelY="0.5" /> <Point X="432.0" Y="1009.0" GraphRef="ce9c8" RelX="0.9622641509433962" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000348" /> </Interaction> <Interaction GraphId="b18c3"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="863.0" Y="197.0" GraphRef="c6f73" RelX="0.0" RelY="0.9099999999999966" /> <Point X="885.0" Y="237.0" GraphRef="eaecd" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570463" /> </Interaction> <Interaction GraphId="b195b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1256.0" Y="957.0" GraphRef="ae208" RelX="0.03999999999996362" RelY="0.7200000000000273" /> <Point X="1273.0" Y="989.0" GraphRef="e6fb5" RelX="0.9823008849557522" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570528" /> </Interaction> <Interaction GraphId="b2292"> <Comment Source="Reactome">MDC1 is SUMOylated at lysine-1840 with SUMO1. SUMOyation of MDC1 is required for its degradation, which is thought to be directed by ubiquitinylation by RNF4 (Luo et al. 2012).</Comment> <BiopaxRef>a95</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="283.0" Y="386.0" /> <Point X="285.0" Y="441.0" /> <Anchor Position="0.0" Shape="None" GraphId="fd0c6" /> <Anchor Position="0.99" Shape="None" GraphId="a5b5b" /> <Anchor Position="0.5" Shape="None" GraphId="d9ca6" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570554" /> </Interaction> <Interaction GraphId="b267d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="524.0" Y="47.0" GraphRef="db11c" RelX="0.9672131147540983" RelY="0.0" /> <Point X="573.0" Y="85.0" GraphRef="c0152" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2997709" /> </Interaction> <Interaction GraphId="b296c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="110.0" Y="803.0" GraphRef="e762a" RelX="0.9813084112149533" RelY="-0.022222222222222223" /> <Point X="344.0" Y="943.0" GraphRef="ba3cb" RelX="-1.0" RelY="1.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000399" /> </Interaction> <Interaction GraphId="b2cc5"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="534.0" Y="351.0" GraphRef="dc5b3" RelX="0.9710144927536232" RelY="0.0" /> <Point X="533.0" Y="382.0" GraphRef="d6dcf" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568863" /> </Interaction> <Interaction GraphId="b30d2"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1256.0" Y="957.0" GraphRef="ae208" RelX="0.03999999999996362" RelY="0.7200000000000273" /> <Point X="1310.0" Y="989.0" GraphRef="d98ae" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570528" /> </Interaction> <Interaction GraphId="b45ec"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="177.0" Y="64.0" GraphRef="c231e" RelX="-1.0" RelY="0.0" /> <Point X="147.0" Y="146.0" GraphRef="c0393" RelX="0.5" RelY="4.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568914" /> </Interaction> <Interaction GraphId="b4778"> <Comment Source="Reactome">RANBP2 of the nuclear pore complex SUMOylates PML with SUMO2 at lysine-65, lysine-160, and lysine-490 (Kamitani et al. 1998, Tatham et al. 2005). RANBP2 contains both a binding site for SUMO1 and a binding site for UBE2I (Tatham et al. 2005). The binding site for UBE2I participates in SUMOylation of PML with SUMO2. SUMO2 colocalizes significantly with PML bodies (Vertegaal et al. 2004).</Comment> <BiopaxRef>a4c</BiopaxRef> <BiopaxRef>eb9</BiopaxRef> <BiopaxRef>cd9</BiopaxRef> <BiopaxRef>f85</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="272.0" Y="632.0" /> <Point X="273.0" Y="719.0" /> <Anchor Position="0.0" Shape="None" GraphId="f1ae6" /> <Anchor Position="0.99" Shape="None" GraphId="de05f" /> <Anchor Position="0.5" Shape="None" GraphId="b8a28" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000411" /> </Interaction> <Interaction GraphId="b4a9a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="954.0" Y="597.0" GraphRef="b1b80" RelX="0.0" RelY="0.9310344827586207" /> <Point X="924.0" Y="631.0" GraphRef="e16e4" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551738" /> </Interaction> <Interaction GraphId="b4e0a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1142.0" Y="201.0" GraphRef="ace7a" RelX="0.049999999999954525" RelY="0.7300000000000182" /> <Point X="1145.0" Y="248.0" GraphRef="b76c3" RelX="0.9862068965517241" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3108212" /> </Interaction> <Interaction GraphId="b5472"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1103.0" Y="164.0" GraphRef="b7508" RelX="0.9875776397515528" RelY="0.0" /> <Point X="1139.0" Y="164.0" GraphRef="aa340" RelX="-0.5" RelY="-0.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3108212" /> </Interaction> <Interaction GraphId="b5668"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="273.0" Y="719.0" GraphRef="de05f" RelX="0.009999999999990905" RelY="0.8700000000000045" /> <Point X="441.0" Y="814.0" GraphRef="b4405" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000411" /> </Interaction> <Interaction GraphId="b5949"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="789.0" Y="460.0" GraphRef="c4e3a" RelX="0.009999999999990905" RelY="0.8199999999999932" /> <Point X="819.0" Y="498.0" GraphRef="da244" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551661" /> </Interaction> <Interaction GraphId="b6b5b"> <Comment Source="Reactome">PIAS4 SUMOylates PARP1 at lysine-203 and lysine-486 with SUMO1 (Martin et al. 2009, Matafora et al. 2009, Messner et al. 2009, Zilio et al. 2013, Impens et al. 2014). SUMOylation abrogates acetylation of PARP1 by p300 (Messner et al. 2009). PARP1 reciprocally poly(ADP-ribose)ylates PIAS4 (Martin et al. 2009). PARP1 is SUMOylated in response to heat shock and SUMOylation is required for full activation of the HSP70.1 promoter (Martin et al 2009).</Comment> <BiopaxRef>db6</BiopaxRef> <BiopaxRef>c3a</BiopaxRef> <BiopaxRef>d4b</BiopaxRef> <BiopaxRef>b21</BiopaxRef> <BiopaxRef>ce1</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1389.0" Y="394.0" /> <Point X="1389.0" Y="453.0" /> <Anchor Position="0.0" Shape="None" GraphId="ccdfd" /> <Anchor Position="0.99" Shape="None" GraphId="fed41" /> <Anchor Position="0.5" Shape="None" GraphId="a864f" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551604" /> </Interaction> <Interaction GraphId="b75c6"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="913.0" Y="963.0" GraphRef="e891b" RelX="0.0" RelY="0.6900000000000546" /> <Point X="917.0" Y="994.0" GraphRef="b7a64" RelX="1.0" RelY="-0.034482758620689655" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568848" /> </Interaction> <Interaction GraphId="b883a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="464.0" Y="47.0" GraphRef="db11c" RelX="-1.0" RelY="0.0" /> <Point X="422.0" Y="88.0" GraphRef="ef076" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2997616" /> </Interaction> <Interaction GraphId="b95d3"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="345.0" Y="973.0" GraphRef="f41c6" RelX="0.0" RelY="0.6200000000000045" /> <Point X="350.0" Y="1009.0" GraphRef="feb2f" RelX="1.0" RelY="-0.037037037037037035" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000399" /> </Interaction> <Interaction GraphId="b9d8e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="545.0" Y="722.0" GraphRef="dc4b2" RelX="-0.029999999999972715" RelY="0.7000000000000455" /> <Point X="493.0" Y="814.0" GraphRef="b4405" RelX="0.9622641509433962" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000433" /> </Interaction> <Interaction GraphId="b9f6b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="863.0" Y="197.0" GraphRef="c6f73" RelX="0.0" RelY="0.9099999999999966" /> <Point X="860.0" Y="242.0" GraphRef="d5f78" RelX="1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570463" /> </Interaction> <Interaction GraphId="b9fd9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="517.0" Y="720.0" GraphRef="d4a4a" RelX="0.0" RelY="0.7699999999999818" /> <Point X="397.0" Y="810.0" GraphRef="aaf97" RelX="0.9801980198019802" RelY="-0.037037037037037035" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000383" /> </Interaction> <Interaction GraphId="baf72"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1321.0" Y="708.0" GraphRef="f8d17" RelX="0.009999999999990905" RelY="0.6699999999999591" /> <Point X="1364.0" Y="741.0" GraphRef="fafbd" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568846" /> </Interaction> <Interaction GraphId="bb84b"> <Comment Source="Reactome">PIAS4 SUMOylates PARP1 at lysine-203 and lysine-486 with SUMO2,3 in response to heat shock (Martin et al. 2009, Lamoliatte et al. 2013, Hendriks et al. 2014, Tammsalu et al. 2014). PARP1 reciprocally poly(ADP-ribose)ylates PIAS4 (Martin et al. 2009). SUMOylation of PARP1 is required for full activation of the HSP70.1 promoter (Martin et al. 2009).</Comment> <BiopaxRef>c3a</BiopaxRef> <BiopaxRef>d87</BiopaxRef> <BiopaxRef>a05</BiopaxRef> <BiopaxRef>f85</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1265.0" Y="407.0" /> <Point X="1265.0" Y="455.0" /> <Anchor Position="0.0" Shape="None" GraphId="a3d99" /> <Anchor Position="0.99" Shape="None" GraphId="a4952" /> <Anchor Position="0.5" Shape="None" GraphId="d7e09" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551768" /> </Interaction> <Interaction GraphId="bbe7f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="998.0" Y="699.0" GraphRef="e5792" RelX="0.009999999999990905" RelY="0.8300000000000409" /> <Point X="1016.0" Y="752.0" GraphRef="d739c" RelX="-1.0" RelY="-0.03225806451612903" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551648" /> </Interaction> <Interaction GraphId="bd5b0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="170.0" Y="453.0" GraphRef="e5117" RelX="-0.09999999999999432" RelY="0.5799999999999841" /> <Point X="131.0" Y="480.0" GraphRef="a8b85" RelX="-0.006369426751592357" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570553" /> </Interaction> <Interaction GraphId="bd6db"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="423.0" Y="156.0" GraphRef="e034a" RelX="0.009999999999990905" RelY="0.6800000000000068" /> <Point X="408.0" Y="215.0" GraphRef="c7d88" RelX="-0.008264462809917356" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2997616" /> </Interaction> <Interaction GraphId="bfe2f"> <Comment Source="Reactome">PIAS4 SUMOylates RNF168 at an unknown lysine residue (Danielsen et al. 2012). Both RNF168 and HERC2 are SUMOylated at double-strand breaks in DNA. SUMOylation of RNF168 is required for its retention at double-strand breaks.</Comment> <BiopaxRef>f77</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="788.0" Y="378.0" /> <Point X="789.0" Y="460.0" /> <Anchor Position="0.0" Shape="None" GraphId="a6098" /> <Anchor Position="0.99" Shape="None" GraphId="c4e3a" /> <Anchor Position="0.5" Shape="None" GraphId="eae21" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551661" /> </Interaction> <Interaction GraphId="bff05"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1047.0" Y="454.0" GraphRef="cc105" RelX="0.009999999999990905" RelY="0.5799999999999841" /> <Point X="1083.0" Y="492.0" GraphRef="a9aa4" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551616" /> </Interaction> <Interaction GraphId="c00df"> <Comment Source="Reactome">RAD52 is SUMOylated at lysine-411, lysine-412, and lysine-414 with SUMO1. SUMOylation is important for localization of RAD52 to the nucleus.</Comment> <BiopaxRef>d55</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="533.0" Y="382.0" /> <Point X="533.0" Y="454.0" /> <Anchor Position="0.0" Shape="None" GraphId="d6dcf" /> <Anchor Position="0.99" Shape="None" GraphId="d323c" /> <Anchor Position="0.5" Shape="None" GraphId="a8a50" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568863" /> </Interaction> <Interaction GraphId="c0f40"> <Comment Source="Reactome">XPC is SUMOylated at lysine-655 with SUMO1 (Wang et al. 2005, 2007). SUMOylation occurs after UV irradiation and may target XPC for destruction (Wang et al. 2007).</Comment> <BiopaxRef>dda</BiopaxRef> <BiopaxRef>a81</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1252.0" Y="885.0" /> <Point X="1256.0" Y="957.0" /> <Anchor Position="0.0" Shape="None" GraphId="b2855" /> <Anchor Position="0.99" Shape="None" GraphId="ae208" /> <Anchor Position="0.5" Shape="None" GraphId="c4e80" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570528" /> </Interaction> <Interaction GraphId="c11ed"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="927.0" Y="699.0" GraphRef="ae172" RelX="0.029999999999972715" RelY="0.6800000000000637" /> <Point X="967.0" Y="744.0" GraphRef="ab03f" RelX="-0.018867924528301886" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551738" /> </Interaction> <Interaction GraphId="c14af"> <Graphics ConnectorType="Segmented" ZOrder="12288" 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/> <Point X="1166.0" Y="246.0" GraphRef="bde93" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3108212" /> </Interaction> <Interaction GraphId="cd5fa"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="433.0" Y="575.0" GraphRef="f2709" RelX="0.9591836734693877" RelY="-0.04" /> <Point X="517.0" Y="643.0" GraphRef="d929a" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000383" /> </Interaction> <Interaction GraphId="cdba0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="864.0" Y="928.0" GraphRef="f15a0" RelX="1.0" RelY="-0.047619047619047616" /> <Point X="911.0" Y="926.0" GraphRef="ea134" RelX="-2.0" RelY="-2.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568848" /> </Interaction> <Interaction GraphId="cdfbd"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="345.0" Y="973.0" GraphRef="f41c6" RelX="0.0" RelY="0.6200000000000045" /> <Point X="380.0" Y="1009.0" GraphRef="ce9c8" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000399" /> </Interaction> <Interaction GraphId="cf4a0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="828.0" Y="145.0" GraphRef="a1cc7" RelX="0.9826086956521739" RelY="-0.037037037037037035" /> <Point X="863.0" Y="146.0" GraphRef="d6b9f" RelX="0.0" RelY="-5.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570463" /> </Interaction> <Interaction GraphId="cf50b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1030.0" Y="349.0" GraphRef="b7801" RelX="1.0" RelY="0.0" /> <Point X="1046.0" Y="396.0" GraphRef="fc3ed" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551616" /> </Interaction> <Interaction GraphId="cfb35"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="385.0" Y="575.0" GraphRef="f2709" RelX="-1.0" RelY="-0.04" /> <Point X="272.0" Y="632.0" GraphRef="f1ae6" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000411" /> </Interaction> <Interaction GraphId="d09b2"> <Comment Source="Reactome">PIAS1,4 SUMOylate BRCA1 with SUMO1 at lysine-109 (Morris et al. 2009, Xu et al. 2009). SUMOylation occurs in response to genotoxic stress and double-strand breaks to which PIAS1 and PIAS4 are recruited (Galanty et al. 2009). SUMOylation enhances the ability of BRCA1 to bind and modulate ESR1 (ERalpha) transcriptional activity (Xu et al. 2009). More SUMO2:BRCA1 than SUMO1:BRCA1 is observed in vivo (Morris et al. 2009, Galanty et al. 2009).</Comment> <BiopaxRef>ca1</BiopaxRef> <BiopaxRef>d6d</BiopaxRef> <BiopaxRef>f3e</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="573.0" Y="85.0" /> <Point X="573.0" Y="158.0" /> <Anchor Position="0.0" Shape="None" GraphId="c0152" /> <Anchor Position="0.99" Shape="None" GraphId="a0654" /> <Anchor Position="0.5" Shape="None" GraphId="e3c47" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2997709" /> </Interaction> <Interaction GraphId="d28ce"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1285.0" Y="674.0" GraphRef="a17d7" RelX="1.0" RelY="0.0" /> <Point X="1321.0" Y="673.0" GraphRef="e10d0" RelX="0.5" RelY="-1.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568846" /> </Interaction> <Interaction GraphId="d2953"> <Comment Source="Reactome">CDKN2A (p14-ARF) SUMOylates WRN at lysine-356, lysine-496, and lysine-898 with SUMO1 (Woods et al. 2004). SUMOylation of WRN causes it to be released from the nucleolus.</Comment> <BiopaxRef>f64</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1320.0" Y="641.0" /> <Point X="1321.0" Y="708.0" /> <Anchor Position="0.0" Shape="None" GraphId="e8a36" /> <Anchor Position="0.99" Shape="None" GraphId="f8d17" /> <Anchor Position="0.5" Shape="None" GraphId="e10d0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568846" /> </Interaction> <Interaction GraphId="d4f13"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="922.0" Y="851.0" GraphRef="aadba" RelX="-1.0" RelY="-0.034482758620689655" /> <Point X="913.0" Y="894.0" GraphRef="f4511" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568848" /> </Interaction> <Interaction GraphId="d5856"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1110.0" Y="70.0" GraphRef="e5f59" RelX="1.0" RelY="-0.02702702702702703" /> <Point X="1137.0" Y="128.0" GraphRef="ca33e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3108212" /> </Interaction> <Interaction GraphId="d5bd4"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="548.0" Y="348.0" GraphRef="ba1f5" RelX="-1.0" RelY="0.0" /> <Point X="533.0" Y="382.0" GraphRef="d6dcf" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568863" /> </Interaction> <Interaction GraphId="d5edc"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1271.0" Y="848.0" GraphRef="be1ec" RelX="-1.0" RelY="0.0" /> <Point X="1252.0" Y="885.0" GraphRef="b2855" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570528" /> </Interaction> <Interaction GraphId="d6109"> <Comment Source="Reactome">CBX4 (Pc2) in the PRC1 complex SUMOylates CETN2 at an unknown residue with SUMO2,3 (Klein and Nigg 2009). SUMOylation of CETN2 enhances its nuclear localization. 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HERC2 binds SUMO1 and is then SUMOylated. SUMOylation of HERC2 promotes binding to RNF8 at double-strand breaks in DNA.</Comment> <BiopaxRef>f77</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1401.0" Y="107.0" /> <Point X="1399.0" Y="176.0" /> <Anchor Position="0.0" Shape="None" GraphId="ef81a" /> <Anchor Position="0.99" Shape="None" GraphId="db38b" /> <Anchor Position="0.5" Shape="None" GraphId="a69ab" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551724" /> </Interaction> <Interaction GraphId="d9ceb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="110.0" Y="803.0" GraphRef="e762a" RelX="0.9813084112149533" RelY="-0.022222222222222223" /> <Point X="296.0" Y="685.0" GraphRef="ac250" RelX="-0.5" RelY="6.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-5228508" /> </Interaction> <Interaction GraphId="da9ed"> <Comment Source="Reactome">RANBP2 of the nuclear pore complex SUMOylates SP100 with SUMO2 at lysine-297 (Tatham et al. 2005, Hendriks et al. 2014). 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</Graphics> <Xref Database="Reactome" ID="R-HSA-4551768" /> </Interaction> <Interaction GraphId="df178"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="789.0" Y="460.0" GraphRef="c4e3a" RelX="0.009999999999990905" RelY="0.8199999999999932" /> <Point X="800.0" Y="500.0" GraphRef="b7116" RelX="1.0" RelY="-0.034482758620689655" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551661" /> </Interaction> <Interaction GraphId="df88f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="528.0" Y="118.0" GraphRef="eb177" RelX="1.0" RelY="-0.037037037037037035" /> <Point X="571.0" Y="121.0" GraphRef="e3c47" RelX="-2.0" RelY="-0.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2997709" /> </Interaction> <Interaction GraphId="df966"> <Comment Source="Reactome">The NSMCE2 (NSE2, MMS21) subunit of the SMC5/6 complex SUMOylates the RAD21 and STAG2 subunits of cohesin with SUMO1 (Potts et al. 2006 supplementary data, reviewed in Stephan et al 2011). RAD21 (SCC1) is SUMOylated at several lysines (Wu et al. 2012). SUMOylation of RAD21 occurs during DNA damage repair and is necessary for sister chromatid recombination (Wu et al. 2012).</Comment> <BiopaxRef>d0d</BiopaxRef> <BiopaxRef>fa1</BiopaxRef> <BiopaxRef>a89</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1137.0" Y="128.0" /> <Point X="1142.0" Y="201.0" /> <Anchor Position="0.0" Shape="None" GraphId="ca33e" /> <Anchor Position="0.99" Shape="None" GraphId="ace7a" /> <Anchor Position="0.5" Shape="None" GraphId="aa340" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3108212" /> </Interaction> <Interaction GraphId="df9ca"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="901.0" Y="853.0" GraphRef="c8c3b" RelX="1.0" RelY="0.0" /> <Point X="913.0" Y="894.0" GraphRef="f4511" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4568848" /> </Interaction> <Interaction GraphId="dfb59"> <Graphics ConnectorType="Segmented" ZOrder="12288" 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ID="R-HSA-4568848" /> </Interaction> <Interaction GraphId="e7ce9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="285.0" Y="441.0" GraphRef="a5b5b" RelX="0.01999999999998181" RelY="0.5500000000000114" /> <Point X="251.0" Y="474.0" GraphRef="f62e5" RelX="-0.018867924528301886" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570554" /> </Interaction> <Interaction GraphId="ea4ce"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="311.0" Y="885.0" GraphRef="f7253" RelX="-0.007194244604316547" RelY="0.9310344827586207" /> <Point X="345.0" Y="911.0" GraphRef="f0c7b" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000399" /> </Interaction> <Interaction GraphId="eaa09"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="546.0" Y="587.0" GraphRef="cc757" RelX="-1.0" RelY="0.0" /> <Point X="548.0" Y="652.0" GraphRef="b7ae7" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3000433" /> </Interaction> <Interaction GraphId="eaafb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1389.0" Y="453.0" GraphRef="fed41" RelX="0.0" RelY="0.5900000000000318" /> <Point X="1361.0" Y="485.0" GraphRef="e52b1" RelX="0.9622641509433962" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4551604" /> </Interaction> <Interaction GraphId="eb05b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="265.0" Y="336.0" GraphRef="df403" RelX="0.9692307692307692" RelY="0.0" /> <Point X="283.0" Y="386.0" GraphRef="fd0c6" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4570554" /> </Interaction> <Interaction GraphId="eb901"> <Comment Source="Reactome">PML is observed to be SUMOylated with SUMO3 at lysine-65, lysine-160, and lysine-490 (Kamitani et al. 1998). SUMO3 is almost identical with SUMO2 therefore the same E3 ligase (RANBP2) that SUMOylate PML with SUMO2 may also be active with SUMO3, but this has not been proven. 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interplay between SUMO-dependent/independent activities of Ubc9 on E2-induced ERalpha activation/repression and degradation in breast cancer cells.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Xu J, Watkins T, Reddy A, Reddy ES, Rao VN.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="db6"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">19622798</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Sumoylation of poly(ADP-ribose) polymerase 1 inhibits its acetylation and restrains transcriptional coactivator function.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Messner S, Schuermann D, Altmeyer M, Kassner I, Schmidt D, Schär P, Müller S, Hottiger MO.</bp:AUTHORS> 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rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Gong L, Yeh ET.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="ca1"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">20016594</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Morris JR, Boutell C, Keppler M, Densham R, Weekes D, Alamshah A, Butler L, Galanty Y, Pangon L, Kiuchi T, Ng T, Solomon E.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="a05"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">23750026</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenshuk H, Thibault P.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="b67"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">12196509</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> 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</bp:openControlledVocabulary> </Biopax> </Pathway>

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