SUMOylation of transcription cofactors (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="SUMOylation of transcription cofactors" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">SUMO1,2, and 3 are predominantly located in the nucleus and targets of SUMOylation are predominantly nuclear. Transcription cofactors are nuclear proteins that generally do not bind DNA themselves but interact with DNA-bound factors and influence transcription. SUMOylation of transcription cofactors usually inhibits the activity of the cofactor (reviewed in Girdwood et al. 2004, Gill 2005, Lyst and Stancheva 2007, Garcia-Dominguez and Reyes 2009). In the cases of coactivators such as PPARGC1A (PGC-1alpha) this results in decreased transcription; in the cases of corepressors such as MBD1 this results in increased transcription. View original pathway at [http://www.reactome.org/PathwayBrowser/#DIAGRAM=3899300 Reactome].</Comment> <Comment Source="Reactome-Converter">Pathway is converted from Reactome ID: 3899300</Comment> <Comment Source="Reactome-version">Reactome version: 73</Comment> <Comment Source="Reactome Author">Reactome Author: May, Bruce</Comment> <BiopaxRef>de3</BiopaxRef> <BiopaxRef>cc8</BiopaxRef> <BiopaxRef>d40</BiopaxRef> <BiopaxRef>bd7</BiopaxRef> <Attribute Key="reactome_id" Value="3899300" /> <Graphics BoardWidth="1454.0" BoardHeight="2061.0" /> <DataNode TextLabel="CBX4, UHRF2" GraphId="a0250" Type="Complex"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Graphics CenterX="184.5" CenterY="964.0" Width="115.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a" /> <Xref Database="Reactome" ID="R-HSA-3296158" /> </DataNode> <DataNode TextLabel="MKL1" GraphId="a0983" Type="Protein"> <Attribute Key="cellular_location" 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TextLabel="UBE2I-G97-SUMO1 " GraphId="b0589" Type="Protein" GroupRef="fb1d6"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-2993783" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="660.0" CenterY="1911.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P63165" /> </DataNode> <DataNode TextLabel="PIAS3 " GraphId="b0b68" Type="Protein" GroupRef="acde8"> <Attribute Key="cellular_location" Value="nucleoplasm" /> <Attribute Key="complex_id" Value="R-HSA-4086016" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1391.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9Y6X2" /> </DataNode> <DataNode TextLabel="SUMO1-K32-HIPK2 " GraphId="b0f98" Type="Protein" GroupRef="d5c90"> <Comment Source="Reactome">Hoffmann et al. 2005 (205) and Gresko et al. 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Value="R-HSA-2993783" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="660.0" CenterY="1451.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P63279" /> </DataNode> <Interaction GraphId="a0154"> <Comment Source="Reactome">As inferred from mouse homologs, CREBBP (CBP) is SUMOylated at lysine-998, lysine-1033, and lysine-1056 with SUMO1. SUMOylation recruits DAXX and HDAC2 to repress transcription.</Comment> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="705.0" Y="109.0" /> <Point X="706.0" Y="152.0" /> <Anchor Position="0.0" Shape="None" GraphId="aa7b8" /> <Anchor Position="0.99" Shape="None" GraphId="c0804" /> <Anchor Position="0.5" Shape="None" GraphId="d25dc" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3927959" /> </Interaction> <Interaction GraphId="a0255"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="613.0" Y="987.0" GraphRef="bbd9a" RelX="0.0" RelY="0.5299999999999727" /> <Point X="643.0" Y="1036.0" GraphRef="e7307" RelX="1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3782535" /> </Interaction> <Interaction GraphId="a0ce3"> <Comment Source="Reactome">NCOA1 (SRC1) is SUMOylated at lysine-732 and lysine-774 with SUMO1 (Chauchereau et al. 2003). SUMOylation enhances interaction between NCOA1 and the progesterone receptor and causes NCOA1 to be retained in the nucleus.</Comment> <BiopaxRef>be7</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="945.0" Y="521.0" /> <Point X="946.0" Y="571.0" /> <Anchor Position="0.0" Shape="None" GraphId="d74da" /> <Anchor Position="0.99" Shape="None" GraphId="b9105" /> <Anchor Position="0.5" Shape="None" GraphId="a7a72" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4085296" /> </Interaction> <Interaction GraphId="a15a5"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="335.0" Y="60.0" GraphRef="c71d9" RelX="-0.014925373134328358" RelY="0.9259259259259259" /> <Point X="339.0" Y="101.0" GraphRef="bf72a" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3108209" /> </Interaction> <Interaction GraphId="a2503"> <Comment Source="Reactome">PIAS1, PIAS4 SUMOylate CASP8AP2 (FLASH) at lysine-1813 with SUMO1 (Alm-Kristiansen et al. 2009, Alm-Kristiansen et al. 2011). SUMOylation enhances the transcriptional coactivation activity of CASP8AP2. As inferred from mouse homologs, SUMOylation also appears to trigger proteasomal degradation of CASP8AP2 (Vennemann and Hofmann 2013).</Comment> <BiopaxRef>ff2</BiopaxRef> <BiopaxRef>aac</BiopaxRef> <BiopaxRef>fc2</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="115.0" Y="83.0" /> <Point X="115.0" Y="133.0" /> <Anchor Position="0.0" Shape="None" GraphId="e1714" /> <Anchor Position="0.99" Shape="None" GraphId="e4b6a" /> <Anchor Position="0.5" Shape="None" GraphId="d92ce" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-5228521" /> </Interaction> <Interaction GraphId="a260a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="946.0" Y="571.0" GraphRef="b9105" RelX="0.009999999999990905" RelY="0.5" /> <Point X="1001.0" Y="616.0" GraphRef="b269a" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4085296" /> </Interaction> <Interaction GraphId="a2d4f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="368.0" Y="47.0" GraphRef="c71d9" RelX="0.9701492537313433" RelY="-0.037037037037037035" /> <Point X="375.0" Y="98.0" GraphRef="fcd0e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3108203" /> </Interaction> <Interaction GraphId="a3753"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="377.0" Y="151.0" GraphRef="daae5" RelX="0.01999999999998181" RelY="0.5300000000000011" /> <Point X="397.0" Y="189.0" GraphRef="f366e" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3108203" /> </Interaction> <Interaction GraphId="a4c91"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="288.0" Y="108.0" GraphRef="e2f8d" RelX="0.9826086956521739" RelY="-0.037037037037037035" /> <Point X="337.0" Y="128.0" GraphRef="d2913" RelX="-1.5" RelY="2.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3108209" /> </Interaction> <Interaction GraphId="a6728"> <Comment Source="Reactome">NPM1 (Nucleophosmin, B23) is SUMOylated at lysine-263 with SUMO1 (Liu et al. 2007). SUMOylation enhances binding of NPM1 to Rb and enhances nuclear residency of NPM1.</Comment> <BiopaxRef>d29</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="482.0" Y="718.0" /> <Point X="483.0" Y="768.0" /> <Anchor Position="0.0" Shape="None" GraphId="d6055" /> <Anchor Position="0.99" Shape="None" GraphId="c0fc3" /> <Anchor Position="0.5" Shape="None" GraphId="ac857" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4086088" /> </Interaction> <Interaction GraphId="a728f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="582.0" Y="342.0" GraphRef="d214f" RelX="0.0" RelY="0.5" /> <Point X="568.0" Y="377.0" GraphRef="c67d1" RelX="0.9819819819819819" RelY="-0.03225806451612903" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4085347" /> </Interaction> <Interaction GraphId="a7f76"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="676.0" Y="351.0" GraphRef="fe707" RelX="0.009999999999990905" RelY="0.6299999999999955" /> <Point X="663.0" Y="380.0" GraphRef="ccd8b" RelX="1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4085372" /> </Interaction> <Interaction GraphId="a80d3"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="669.0" Y="566.0" GraphRef="cb128" RelX="0.009999999999990905" RelY="0.5" /> <Point X="687.0" Y="606.0" GraphRef="a13b0" RelX="1.0" RelY="-0.034482758620689655" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4086083" /> </Interaction> <Interaction GraphId="a8118"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="413.0" Y="318.0" GraphRef="fec4e" RelX="-1.0" RelY="-0.03225806451612903" /> <Point X="279.0" Y="304.0" GraphRef="b2fc1" RelX="-1.0" RelY="2.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3900194" /> </Interaction> <Interaction GraphId="a831c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1207.0" Y="572.0" GraphRef="f1825" RelX="0.01999999999998181" RelY="0.5099999999999909" /> <Point X="1253.0" Y="617.0" GraphRef="e40dc" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3900070" /> </Interaction> <Interaction GraphId="a8455"> <Comment Source="Reactome">TOPORS SUMOylates SIN3A at an unknown lysine residue with SUMO1 (Pungaliya et al. 2007).</Comment> <BiopaxRef>b7e</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1202.0" Y="945.0" /> <Point X="1203.0" Y="997.0" /> <Anchor Position="0.0" Shape="None" GraphId="d6768" /> <Anchor Position="0.99" Shape="None" GraphId="d3382" /> <Anchor Position="0.5" Shape="None" GraphId="ea831" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4085994" /> </Interaction> <Interaction GraphId="a8874"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="566.0" Y="681.0" GraphRef="a9c26" RelX="1.0" RelY="-0.03225806451612903" /> <Point X="601.0" Y="713.0" GraphRef="f1c50" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4086059" /> </Interaction> <Interaction GraphId="a9efc"> <Comment Source="Reactome">DAXX is SUMOylated at lysine-630 and lysine-631 with SUMO1 (Jang et al. 2002, Lalioti et al. 2002, Lin et al. 2006). SUMOylation of DAXX does not prevent it from localizing to PML oncogenic domains.</Comment> <BiopaxRef>fa7</BiopaxRef> <BiopaxRef>de8</BiopaxRef> <BiopaxRef>d96</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="979.0" Y="99.0" /> <Point X="980.0" Y="156.0" /> <Anchor Position="0.0" Shape="None" GraphId="d3b2b" /> <Anchor Position="0.99" Shape="None" GraphId="befa1" /> <Anchor Position="0.5" Shape="None" GraphId="ba0ed" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4085992" /> </Interaction> <Interaction GraphId="aa9c7"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="167.0" Y="334.0" GraphRef="f6719" RelX="0.0" RelY="0.4800000000000182" /> <Point X="195.0" Y="372.0" GraphRef="d4d28" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3900177" /> </Interaction> <Interaction GraphId="abdfc"> <Comment Source="Reactome">The PHD domain of TRIM28 (KAP1) acts as a SUMO E3 ligase to SUMOylate the bromodomain of TRIM28 with SUMO1 (Ivanov et al. 2007, Lee et al. 2007, Li et al. 2007, Mascle et al. 2007, Zeng et al. 2008, Impens et al. 2014). SUMOylation enhances repression of p21 transcription by the TRIM28:ZNF350 (KAP1:ZBRK1) complex. 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RelX="-0.009999999999990905" RelY="0.4900000000000091" /> <Point X="341.0" Y="175.0" GraphRef="eb7f6" RelX="-0.009523809523809525" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3108209" /> </Interaction> <Interaction GraphId="b9f33"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="970.0" Y="250.0" GraphRef="c90ff" RelX="0.9692307692307692" RelY="-0.034482758620689655" /> <Point X="979.0" Y="293.0" GraphRef="c47d2" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3899291" /> </Interaction> <Interaction GraphId="ba685"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="369.0" Y="460.0" GraphRef="ccf49" RelX="-1.0" RelY="-0.037037037037037035" /> <Point X="363.0" Y="495.0" GraphRef="b0f57" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4086036" /> </Interaction> <Interaction GraphId="baa32"> <Comment Source="Reactome">CBX4 (Pc2) and UHRF2 are able to SUMOylate ZNF131 on lysine-601 (lysine-567 in the isoform in Oh and Chung 2012, Oh and Chung 2013) . SUMOylation of ZNF131 increases the inhibition of ERalpha signaling by ZNF131 through suppression of ERalpha homodimerization.</Comment> <BiopaxRef>f5e</BiopaxRef> <BiopaxRef>ed6</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="274.0" Y="934.0" /> <Point X="273.0" Y="989.0" /> <Anchor Position="0.0" Shape="None" GraphId="ab632" /> <Anchor Position="0.99" Shape="None" GraphId="f9377" /> <Anchor Position="0.5" Shape="None" GraphId="b1de6" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3296126" /> </Interaction> <Interaction GraphId="baa7a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="150.0" Y="46.0" GraphRef="c3e46" RelX="-1.0" RelY="0.0" /> <Point X="115.0" Y="83.0" GraphRef="e1714" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-5228521" /> </Interaction> <Interaction GraphId="bafcd"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="977.0" Y="249.0" GraphRef="cf123" RelX="-1.0" RelY="-0.034482758620689655" /> <Point X="979.0" Y="293.0" GraphRef="c47d2" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3899291" /> </Interaction> <Interaction GraphId="bbc0d"> <Comment Source="Reactome">PIAS2-1 (PIASxalpha) SUMOylates PARK7 (DJ-1) at lysine-130 with SUMO1 (Takahashi et al. 2001, Shinbo et al. 2006). SUMOylation causes PARK7 to be retained in the nucleus where it represses transcription activation by P53 (TP53). A non-SUMOylatable mutant of PARK7 is located in the cytoplasm and fails to repress TP53 (p53) transcriptional activity (Fan et al. 2008).</Comment> <BiopaxRef>dc9</BiopaxRef> <BiopaxRef>edc</BiopaxRef> <BiopaxRef>b49</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1203.0" Y="725.0" /> <Point X="1203.0" Y="775.0" /> <Anchor Position="0.0" Shape="None" GraphId="fb27b" /> <Anchor Position="0.99" Shape="None" GraphId="ddece" /> <Anchor Position="0.5" Shape="None" GraphId="dcec9" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4085331" /> </Interaction> <Interaction GraphId="bbc22"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1189.0" Y="690.0" GraphRef="ee8cb" RelX="-1.0" RelY="-0.037037037037037035" /> <Point X="1203.0" Y="725.0" GraphRef="fb27b" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4085331" /> </Interaction> <Interaction GraphId="bc3ff"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="899.0" Y="896.0" GraphRef="ac517" RelX="0.9797979797979798" RelY="-0.034482758620689655" /> <Point X="917.0" Y="932.0" GraphRef="ba1a9" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3903017" /> </Interaction> <Interaction GraphId="bc7b6"> <Comment Source="Reactome">PIAS1 SUMOylates SAFB at lysine-231 and lysine-294 with SUMO1 (Garee et al. 2011). SUMOylation of SAFB is required for co-repressor activity of SAFB at promoters regulated by the estrogen receptor (ER). In contrast, SUMOylated SAFB increases transcription of genes encoding ribosomal proteins (Liu 2015).</Comment> <BiopaxRef>dac</BiopaxRef> <BiopaxRef>bdc</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="582.0" Y="292.0" /> <Point X="582.0" Y="342.0" /> <Anchor Position="0.0" Shape="None" GraphId="fad8b" /> <Anchor Position="0.99" Shape="None" GraphId="d214f" /> <Anchor Position="0.5" Shape="None" GraphId="bd98d" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4085347" /> </Interaction> <Interaction GraphId="bc9f6"> <Comment Source="Reactome">MKL1 is SUMOylated with SUMO1 at lysine-499, lysine-576, and lysine-624 (Nakagawa and Kuzumaki 2005) SUMOylation represses transcriptional activity of MKL1. MKL1 is a coactivator of SRF.</Comment> <BiopaxRef>d34</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1205.0" Y="521.0" /> <Point X="1207.0" Y="572.0" /> <Anchor Position="0.0" Shape="None" GraphId="bc317" /> <Anchor Position="0.99" Shape="None" GraphId="f1825" /> <Anchor Position="0.5" Shape="None" GraphId="afa94" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3900070" /> </Interaction> <Interaction GraphId="bfb3b"> <Comment Source="Reactome">HIPK2 is SUMOylated at lysine-32 with SUMO1. (Lysine-25 is cited by Hofmann et al. 2005 and Gresko et al. 2005, however the sequence motif listed in Hoffmann et al. 2005 corresponds to lysine-32 of the UniProt reference protein. An alternative isoform having lysine-25 is listed as accession AAG35710 in GenBank.) SUMOylation of HIPK2 disrupts interaction of HIPK2 with GROUCHO corepressor, inhibits JNK activation, and inhibits p53-independent antiproliferative function.</Comment> <BiopaxRef>e3c</BiopaxRef> <BiopaxRef>af8</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1230.0" Y="299.0" /> <Point X="1230.0" Y="352.0" /> <Anchor Position="0.0" Shape="None" GraphId="b74c8" /> <Anchor Position="0.99" Shape="None" GraphId="e1942" /> <Anchor Position="0.5" Shape="None" GraphId="fde86" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4090284" /> </Interaction> <Interaction GraphId="c05bb"> <Comment Source="Reactome">DDX17 is SUMOylated at lysine-50 with SUMO1 or SUMO2 (Mooney et al. 2010, Fuller-Pace and Nicol 2012, Impens et al. 2014). SUMOylation reduces the transactivation activity of DDX17 with the estrogen receptor and with p53. SUMOylation also promotes association of DDX17 with HDAC1.</Comment> <BiopaxRef>b7c</BiopaxRef> <BiopaxRef>d46</BiopaxRef> <BiopaxRef>d36</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1242.0" Y="104.0" /> <Point X="1245.0" Y="148.0" /> <Anchor Position="0.0" Shape="None" GraphId="bd5de" /> <Anchor Position="0.99" Shape="None" GraphId="c8854" /> <Anchor Position="0.5" Shape="None" GraphId="beaf4" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3900047" /> </Interaction> <Interaction GraphId="c07db"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="212.0" Y="454.0" GraphRef="bb70a" RelX="-1.0" RelY="0.0" /> <Point X="195.0" Y="502.0" GraphRef="dade0" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4090288" /> </Interaction> <Interaction GraphId="c09a1"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="184.0" Y="459.0" GraphRef="ca795" RelX="1.0" RelY="-0.034482758620689655" /> <Point X="195.0" Y="502.0" GraphRef="dade0" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4090288" /> </Interaction> <Interaction GraphId="c1866"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="114.0" Y="42.0" GraphRef="d2c65" RelX="0.9753086419753086" RelY="-0.034482758620689655" /> <Point X="142.0" Y="93.0" GraphRef="b9952" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3927824" /> </Interaction> <Interaction GraphId="c3189"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="170.0" Y="250.0" GraphRef="e2441" RelX="0.9847328244274809" RelY="0.0" /> <Point X="167.0" Y="286.0" GraphRef="eec5b" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3900177" /> </Interaction> <Interaction GraphId="c340e"> <Comment Source="Reactome">CBX4 (Pc2) via its SUMO-interacting motifs recruits both CTBP1 and SUMO2,3:UBE2I (SUMO1:UBC9) to polycomb bodies where CTBP1 is SUMOylated with SUMO2,3 at lysine-428, as inferred from SUMOylation with SUMO1 (Merrill et al. 2010, Yang and Sharrocks 2010).</Comment> <BiopaxRef>e1d</BiopaxRef> <BiopaxRef>ebb</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="375.0" Y="98.0" /> <Point X="377.0" Y="151.0" /> <Anchor Position="0.0" Shape="None" GraphId="fcd0e" /> <Anchor Position="0.99" Shape="None" GraphId="daae5" /> <Anchor Position="0.5" Shape="None" GraphId="f8f66" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3108203" /> </Interaction> <Interaction GraphId="c5394"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="913.0" Y="787.0" GraphRef="c7ea8" RelX="0.01999999999998181" RelY="0.5599999999999454" /> <Point X="956.0" Y="824.0" GraphRef="a2c1d" RelX="-1.0" RelY="-0.034482758620689655" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4085318" /> </Interaction> <Interaction GraphId="c6a39"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="706.0" Y="152.0" GraphRef="c0804" RelX="0.009999999999990905" RelY="0.4300000000000068" /> <Point X="725.0" Y="183.0" GraphRef="b462b" RelX="0.984251968503937" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3927959" /> </Interaction> <Interaction GraphId="c90ad"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1185.0" Y="479.0" GraphRef="a40bf" RelX="-1.0" RelY="0.0" /> <Point X="1206.0" Y="550.0" GraphRef="afa94" RelX="0.0" RelY="3.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3900070" /> </Interaction> <Interaction GraphId="c99aa"> <Comment Source="Reactome">As inferred from mouse homologs, NCOR2 (SMRT) is sumoylated at lysine-668 with SUMO1. SUMOylation reduces repression of transcription by NCOR2.</Comment> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="178.0" Y="729.0" /> <Point X="178.0" Y="780.0" /> <Anchor Position="0.0" Shape="None" GraphId="f325c" /> <Anchor Position="0.99" Shape="None" GraphId="cf666" /> <Anchor Position="0.5" Shape="None" GraphId="f1d87" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3927886" /> </Interaction> <Interaction GraphId="c9c4e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1245.0" Y="148.0" GraphRef="c8854" RelX="0.029999999999972715" RelY="0.4399999999999977" /> <Point X="1284.0" Y="195.0" GraphRef="de96e" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3900047" /> </Interaction> <Interaction GraphId="c9e9c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1225.0" Y="62.0" GraphRef="a9ed5" RelX="-1.0" RelY="0.0" /> <Point X="1244.0" Y="129.0" GraphRef="beaf4" RelX="0.5" RelY="3.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3900047" /> </Interaction> <Interaction GraphId="cb6a6"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="178.0" Y="780.0" GraphRef="cf666" RelX="0.0" RelY="0.5099999999999909" /> <Point X="140.0" Y="808.0" GraphRef="bb3da" RelX="-0.007633587786259542" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3927886" /> </Interaction> <Interaction GraphId="cc8a0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="669.0" Y="566.0" GraphRef="cb128" RelX="0.009999999999990905" RelY="0.5" /> <Point X="698.0" Y="604.0" GraphRef="fd32c" RelX="-1.0" RelY="-0.037037037037037035" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4086083" /> </Interaction> <Interaction GraphId="cc8aa"> <Comment Source="Reactome">DDX5 is SUMOylated at lysine-53 with SUMO1 (Mooney et al. 2010, Matafora et al. 2009, Impens et al. 2014). 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SUMOylation of SAFB is required for co-repressor activity.</Comment> <BiopaxRef>dac</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="675.0" Y="288.0" /> <Point X="676.0" Y="351.0" /> <Anchor Position="0.0" Shape="None" GraphId="cb5c0" /> <Anchor Position="0.99" Shape="None" GraphId="fe707" /> <Anchor Position="0.5" Shape="None" GraphId="f19d2" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4085372" /> </Interaction> <Interaction GraphId="d0d14"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="115.0" Y="133.0" GraphRef="e4b6a" RelX="0.0" RelY="0.5" /> <Point X="101.0" Y="169.0" GraphRef="d6c84" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-5228521" /> </Interaction> <Interaction GraphId="d1032"> <Comment Source="Reactome">PIAS1 SUMOylates DDX5 at lysine-53 with SUMO2 (Jacobs et al. 2007, Hendriks et al. 2014, Impens et al. 2014). SUMOylation reduces the coactivation activity of DDX5 with p53 but enhances coactivation of the estrogen receptor. SUMOylation also increases stability of DDX5 and promotes interaction of DDX5 with HDAC1. DDX5 is a coactivator of p53 (TP53).</Comment> <BiopaxRef>f68</BiopaxRef> <BiopaxRef>d46</BiopaxRef> <BiopaxRef>bd8</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="279.0" Y="275.0" /> <Point X="281.0" Y="329.0" /> <Anchor Position="0.0" Shape="None" GraphId="edb36" /> <Anchor Position="0.99" Shape="None" GraphId="b5e63" /> <Anchor Position="0.5" Shape="None" GraphId="b2fc1" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-3900194" /> </Interaction> <Interaction GraphId="d128b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1162.0" Y="971.0" GraphRef="ec80c" RelX="0.9770114942528736" RelY="-0.034482758620689655" /> <Point X="1202.0" Y="972.0" GraphRef="ea831" RelX="-0.5" RelY="1.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-4085994" /> </Interaction> <Interaction GraphId="d18ac"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="913.0" 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Janknecht R.</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="e3c"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">15958389</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">Regulation of homeodomain-interacting protein kinase 2 (HIPK2) effector function through dynamic small ubiquitin-related modifier-1 (SUMO-1) modification.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Hofmann TG, Jaffray E, Stollberg N, Hay RT, Will H.</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="fc2"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">23673342</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">SUMO regulates proteasome-dependent degradation of FLASH/Casp8AP2.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Vennemann A, Hofmann TG.</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="aac"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">21338522</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">PIAS1 interacts with FLASH and enhances its co-activation of c-Myb.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Alm-Kristiansen AH, Lorenzo PI, Molværsmyr AK, Matre V, Ledsaak M, Sæther T, Gabrielsen OS.</bp:AUTHORS> </bp:PublicationXref> 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rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">A tissue-specific coactivator of steroid receptors, identified in a functional genetic screen.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Knutti D, Kaul A, Kralli A.</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="dac"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">21527249</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">Co-repressor activity of scaffold attachment factor B1 requires sumoylation.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Garee JP, Meyer R, Oesterreich S.</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="af8"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">15766567</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">Covalent modification of human homeodomain interacting protein kinase 2 by SUMO-1 at lysine 25 affects its stability.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Gresko E, Möller A, Roscic A, Schmitz ML.</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="ff2"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">19615980</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">SUMO modification regulates the transcriptional activity of FLASH.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Alm-Kristiansen AH, Norman IL, Matre V, Gabrielsen OS.</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="dd8"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">16757475</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">Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Uchimura Y, Ichimura T, Uwada J, Tachibana T, Sugahara S, Nakao M, Saitoh H.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" 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JJ.</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="bdc"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">25800734</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 chromatin scaffold protein SAFB1 localizes SUMO-1 to the promoters of ribosomal protein genes to facilitate transcription initiation and splicing.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Liu HW, Banerjee T, Guan X, Freitas MA, Parvin JD.</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="c9f"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">9556629</bp:ID> <bp:DB 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rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Uncovering global SUMOylation signaling networks in a site-specific manner.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Hendriks IA, D'Souza RC, Yang B, Verlaan-de Vries M, Mann M, Vertegaal AC.</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="f5e"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">22467880</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">Small ubiquitin-like modifier (SUMO) modification of zinc finger protein 131 potentiates its negative effect on estrogen signaling.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Oh Y, Chung KC.</bp:AUTHORS> </bp:PublicationXref> <bp:openControlledVocabulary 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