Mitotic Prometaphase (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="Mitotic Prometaphase" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">The dissolution of the nuclear membrane marks the beginning of the prometaphase. Kinetochores are created when proteins attach to the centromeres. Microtubules then attach at the kinetochores, and the chromosomes begin to move to the metaphase plate. View original pathway at:[http://www.reactome.org/PathwayBrowser/#DIAGRAM=68877 Reactome].</Comment> <Comment Source="Reactome-Converter">Pathway is converted from Reactome ID: 68877</Comment> <Comment Source="Reactome-version">Reactome version: 64</Comment> <Attribute Key="reactome_id" Value="68877" /> <Graphics BoardWidth="1860.0" BoardHeight="3336.0" /> <DataNode TextLabel="PPP2R5D " GraphId="a023b" Type="Protein" GroupRef="bbc66"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-375305" /> <Attribute Key="copies_num" Value="98" /> <Graphics CenterX="100.0" CenterY="1336.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q14738" /> </DataNode> <DataNode TextLabel="APITD1 " GraphId="a030e" Type="Protein" GroupRef="db06e"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-1638796" /> <Attribute Key="copies_num" Value="722" /> 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TextLabel="NDEL1 " GraphId="a0b40" Type="Protein" GroupRef="bbc66"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-375305" /> <Attribute Key="copies_num" Value="2" /> <Graphics CenterX="100.0" CenterY="1136.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9GZM8" /> </DataNode> <DataNode TextLabel="ODF2 " GraphId="a0eb5" Type="Protein" GroupRef="b8b9c"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-380440" /> <Attribute Key="copies_num" Value="8" /> <Graphics CenterX="1640.0" CenterY="1596.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q5BJF6" /> </DataNode> <DataNode TextLabel="MLF1IP " GraphId="a0eed" Type="Protein" GroupRef="db06e"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-1638796" /> <Attribute 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</DataNode> <DataNode TextLabel="CENPK " GraphId="f7351" Type="Protein" GroupRef="b9cf1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2468282" /> <Attribute Key="copies_num" Value="767" /> <Graphics CenterX="660.0" CenterY="2176.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9BS16" /> </DataNode> <DataNode TextLabel="DCTN2 " GraphId="f744c" Type="Protein" GroupRef="f43eb"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-380495" /> <Attribute Key="copies_num" Value="21" /> <Graphics CenterX="1500.0" CenterY="1736.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q13561" /> </DataNode> <DataNode TextLabel="NDC80 " GraphId="f7469" Type="Protein" GroupRef="e2114"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2484819" /> <Attribute Key="copies_num" Value="809" /> <Graphics CenterX="940.0" CenterY="2116.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O14777" /> </DataNode> <DataNode TextLabel="CEP135 " GraphId="f74b1" Type="Protein" GroupRef="f43eb"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-380495" /> <Attribute Key="copies_num" Value="21" /> <Graphics CenterX="1500.0" CenterY="1936.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q66GS9" /> </DataNode> <DataNode TextLabel="CDCA8 " GraphId="f7ab6" Type="Protein" GroupRef="b9cf1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2468282" /> <Attribute Key="copies_num" Value="788" /> <Graphics CenterX="660.0" CenterY="2596.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q53HL2" /> </DataNode> <DataNode TextLabel="WAPAL " GraphId="f7d32" Type="Protein" GroupRef="db06e"> <Attribute Key="cellular_location" Value="chromosome, centromeric region" /> <Attribute Key="complex_id" Value="R-HSA-1638796" /> <Attribute Key="copies_num" Value="1176" /> <Graphics CenterX="380.0" CenterY="3296.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q7Z5K2" /> </DataNode> <DataNode TextLabel="ZWILCH " GraphId="f7e48" Type="Protein" GroupRef="c3a14"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2500242" /> <Attribute Key="copies_num" Value="868" /> <Graphics CenterX="1080.0" CenterY="2716.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9H900" /> </DataNode> <DataNode TextLabel="Sister Chromosomal Arm " GraphId="f7ef4" GroupRef="d582d"> <Attribute Key="cellular_location" Value="chromosome" /> <Attribute Key="complex_id" Value="R-HSA-1638802" /> <Attribute Key="copies_num" Value="2" /> <Graphics CenterX="380.0" CenterY="936.0" Width="100.0" Height="40.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Reactome" ID="R-ALL-1638790" /> </DataNode> <DataNode TextLabel="PPP2R1A " GraphId="f8658" Type="Protein" GroupRef="c3a14"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2500242" /> <Attribute Key="copies_num" Value="531" /> <Graphics CenterX="1080.0" CenterY="1636.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P30153" /> </DataNode> <DataNode TextLabel="MAD1L1 " GraphId="f8756" Type="Protein" GroupRef="c3a14"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2500242" /> <Attribute Key="copies_num" Value="872" /> <Graphics CenterX="1080.0" CenterY="2796.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9Y6D9" /> </DataNode> <DataNode TextLabel="CENPO " GraphId="f876c" Type="Protein" GroupRef="b9cf1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2468282" /> <Attribute Key="copies_num" Value="760" /> <Graphics CenterX="660.0" CenterY="2036.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9BU64" /> </DataNode> <DataNode TextLabel="SKA2 " GraphId="f8795" Type="Protein" GroupRef="db06e"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-1638796" /> <Attribute Key="copies_num" Value="23" /> <Graphics CenterX="380.0" CenterY="1736.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q8WVK7" /> </DataNode> <DataNode TextLabel="CEP290 " GraphId="f8885" Type="Protein" GroupRef="b8b9c"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-380440" /> <Attribute Key="copies_num" Value="8" /> <Graphics CenterX="1640.0" CenterY="1756.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O15078" /> </DataNode> <DataNode TextLabel="ERCC6L " GraphId="f88c1" Type="Protein" GroupRef="c3a14"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2500242" /> <Attribute Key="copies_num" Value="873" /> <Graphics CenterX="1080.0" CenterY="2816.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q2NKX8" /> </DataNode> <DataNode TextLabel="NUP37 " GraphId="f891c" Type="Protein" GroupRef="bbc66"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-375305" /> <Attribute Key="copies_num" Value="316" /> <Graphics CenterX="100.0" CenterY="2236.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q8NFH4" /> </DataNode> <DataNode TextLabel="DYNC1LI2 " GraphId="f8977" Type="Protein" GroupRef="db06e"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-1638796" /> <Attribute Key="copies_num" Value="784" /> <Graphics CenterX="380.0" CenterY="3216.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O43237" /> </DataNode> <DataNode TextLabel="CDC20 " GraphId="f8985" Type="Protein" GroupRef="bbc66"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-375305" /> <Attribute Key="copies_num" Value="317" /> <Graphics CenterX="100.0" CenterY="2436.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q12834" /> </DataNode> <DataNode TextLabel="SEC13 " GraphId="f8a11" Type="Protein" GroupRef="c3a14"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2500242" /> <Attribute Key="copies_num" Value="856" /> <Graphics CenterX="1080.0" CenterY="2516.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P55735" /> </DataNode> <DataNode TextLabel="SMC1A " GraphId="f8a2c" Type="Protein" GroupRef="db06e"> <Attribute Key="cellular_location" Value="chromosome, centromeric region" /> <Attribute Key="complex_id" Value="R-HSA-1638796" /> <Attribute Key="copies_num" Value="2" /> <Graphics CenterX="380.0" CenterY="1196.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q14683" /> </DataNode> <DataNode TextLabel="DYNC1LI1 " GraphId="f8bdc" Type="Protein" GroupRef="e2114"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2484819" /> <Attribute Key="copies_num" Value="859" /> <Graphics CenterX="940.0" CenterY="2796.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9Y6G9" /> </DataNode> <DataNode TextLabel="S Phase" GraphId="f8cb0" Type="Pathway"> <Comment Source="Reactome">DNA synthesis occurs in the S phase, or the synthesis phase, of the cell cycle. The cell duplicates its hereditary material, and two copies of the chromosome are formed. As DNA replication continues, the E type cyclins shared by the G1 and S phases, are destroyed and the levels of the mitotic cyclins rise.</Comment> <Attribute Key="org.pathvisio.DoubleLineProperty" Value="Double" /> <Graphics CenterX="510.0" CenterY="83.5" Width="96.0" Height="47.0" ZOrder="32768" FontSize="10" Valign="Middle" LineThickness="0.0" Color="14961e" /> <Xref Database="Reactome" ID="R-HSA-69242" /> </DataNode> <DataNode TextLabel="MZT1 " GraphId="f8ed6" Type="Protein" GroupRef="b8b9c"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-380440" /> <Attribute Key="copies_num" Value="23" /> <Graphics CenterX="1640.0" CenterY="2416.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q08AG7" /> </DataNode> <DataNode TextLabel="BUB3 " GraphId="f8ef9" Type="Protein" GroupRef="c3a14"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2500242" /> <Attribute Key="copies_num" Value="863" /> <Graphics CenterX="1080.0" CenterY="2656.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O43684" /> </DataNode> <DataNode TextLabel="B9D2 " GraphId="f8f28" Type="Protein" GroupRef="a540c"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-375303" /> <Attribute Key="copies_num" Value="325" /> <Graphics CenterX="240.0" CenterY="1656.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9BPU9" /> </DataNode> <DataNode TextLabel="CENPA " GraphId="f90fb" Type="Protein" GroupRef="c3a14"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2500242" /> <Attribute Key="copies_num" Value="6" /> <Graphics CenterX="1080.0" CenterY="1136.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P49450" /> </DataNode> <DataNode TextLabel="PCM1 " GraphId="f9190" Type="Protein" GroupRef="b8b9c"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-380440" /> <Attribute Key="copies_num" Value="8" /> <Graphics CenterX="1640.0" CenterY="1496.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q15154" /> </DataNode> <DataNode TextLabel="NUP85 " GraphId="f93cc" Type="Protein" GroupRef="e2114"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2484819" /> <Attribute Key="copies_num" Value="816" /> <Graphics CenterX="940.0" CenterY="2256.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9BW27" /> </DataNode> <DataNode TextLabel="DYNC1H1 " GraphId="f9454" Type="Protein" GroupRef="e2114"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2484819" /> <Attribute Key="copies_num" Value="841" /> <Graphics CenterX="940.0" CenterY="2676.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q14204" /> </DataNode> <DataNode TextLabel="PCM1 " GraphId="f9502" Type="Protein" GroupRef="e9567"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-380503" /> <Attribute Key="copies_num" Value="9" /> <Graphics CenterX="1360.0" CenterY="1676.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q15154" /> </DataNode> <DataNode TextLabel="ZWILCH " GraphId="f9748" Type="Protein" GroupRef="a540c"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-375303" /> <Attribute Key="copies_num" Value="326" /> <Graphics CenterX="240.0" CenterY="2516.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9H900" /> </DataNode> <DataNode TextLabel="SPC25 " GraphId="f9aae" Type="Protein" GroupRef="a540c"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-375303" /> <Attribute Key="copies_num" Value="325" /> <Graphics CenterX="240.0" CenterY="2156.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9HBM1" /> </DataNode> <DataNode TextLabel="PPP2R1A " GraphId="f9c56" Type="Protein" GroupRef="b8b9c"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-380440" /> <Attribute Key="copies_num" Value="8" /> <Graphics CenterX="1640.0" CenterY="1056.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P30153" /> </DataNode> <DataNode TextLabel="CLASP1 " GraphId="f9d62" Type="Protein" GroupRef="f43eb"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-380495" /> <Attribute Key="copies_num" Value="21" /> <Graphics CenterX="1500.0" CenterY="1036.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q7Z460" /> </DataNode> <DataNode TextLabel="NSL1 " GraphId="f9e64" Type="Protein" GroupRef="a540c"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-375303" /> <Attribute Key="copies_num" Value="325" /> <Graphics CenterX="240.0" CenterY="2056.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q96IY1" /> </DataNode> <DataNode TextLabel="PDS5B " GraphId="f9f48" Type="Protein" GroupRef="b9cf1"> <Attribute Key="cellular_location" Value="chromosome, centromeric region" /> <Attribute Key="complex_id" Value="R-HSA-2468282" /> <Attribute Key="copies_num" Value="2" /> <Graphics CenterX="660.0" CenterY="1056.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9NTI5" /> </DataNode> <DataNode TextLabel="PDS5A " GraphId="fa178" Type="Protein" GroupRef="b65d1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2545249" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="1220.0" CenterY="1476.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q29RF7" /> </DataNode> <DataNode TextLabel="Mitotic Metaphase&#xA;and Anaphase" GraphId="fa264" Type="Pathway"> <Comment Source="Reactome">Metaphase is marked by the formation of the metaphase plate. The metaphase plate is formed when the spindle fibers align the chromosomes along the middle of the cell. Such an organization helps to ensure that later, when the chromosomes are separated, each new nucleus that is formed receives one copy of each chromosome. This pathway has not yet been annotated in Reactome.&lt;br&gt;&lt;br&gt;The metaphase to anaphase transition during mitosis is triggered by the destruction of mitotic cyclins.&lt;br&gt;&lt;br&gt;In anaphase, the paired chromosomes separate at the centromeres, and move to the opposite sides of the cell. The movement of the chromosomes is facilitated by a combination of kinetochore movement along the spindle microtubules and through the physical interaction of polar microtubules.</Comment> <Attribute Key="org.pathvisio.DoubleLineProperty" Value="Double" /> <Graphics CenterX="1101.5" CenterY="790.5" Width="267.0" Height="43.0" ZOrder="32768" FontSize="10" Valign="Middle" LineThickness="0.0" Color="14961e" /> <Xref Database="Reactome" ID="R-HSA-2555396" /> </DataNode> <DataNode TextLabel="TUBGCP5 " GraphId="fa298" Type="Protein" GroupRef="b8b9c"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-380440" /> <Attribute Key="copies_num" Value="8" /> <Graphics CenterX="1640.0" CenterY="2316.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q96RT8" /> </DataNode> <DataNode TextLabel="MAD2L1 " GraphId="fa4ce" Type="Protein" GroupRef="b9cf1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2468282" /> <Attribute Key="copies_num" Value="789" /> <Graphics CenterX="660.0" CenterY="2616.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q13257" /> </DataNode> <DataNode TextLabel="NUF2 " GraphId="fa966" Type="Protein" GroupRef="bbc66"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-375305" /> <Attribute Key="copies_num" Value="316" /> <Graphics CenterX="100.0" CenterY="2076.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9BZD4" /> </DataNode> <DataNode TextLabel="ODF2 " GraphId="faaa8" Type="Protein" GroupRef="e9567"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-380503" /> <Attribute Key="copies_num" Value="9" /> <Graphics CenterX="1360.0" CenterY="1776.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q5BJF6" /> </DataNode> <DataNode TextLabel="DYNLL2 " GraphId="fab76" Type="Protein" GroupRef="db06e"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-1638796" /> <Attribute Key="copies_num" Value="781" /> <Graphics CenterX="380.0" CenterY="3196.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q96FJ2" /> </DataNode> <DataNode TextLabel="APITD1 " GraphId="fafbc" Type="Protein" GroupRef="b9cf1"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2468282" /> <Attribute Key="copies_num" Value="758" /> <Graphics CenterX="660.0" CenterY="1996.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q8N2Z9" /> </DataNode> <DataNode TextLabel="STAG1 " GraphId="fafd1" Type="Protein" GroupRef="b9cf1"> 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Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-2468282" /> <Attribute Key="copies_num" Value="774" /> <Graphics CenterX="660.0" CenterY="2316.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q9BZD4" /> </DataNode> <DataNode TextLabel="PPP2R5C " GraphId="ffdd1" Type="Protein" GroupRef="bbc66"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-375305" /> <Attribute Key="copies_num" Value="130" /> <Graphics CenterX="100.0" CenterY="1356.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="Q13362" /> </DataNode> <DataNode TextLabel="DCTN3 " GraphId="fff1e" Type="Protein" GroupRef="f43eb"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-380495" /> <Attribute Key="copies_num" Value="21" /> <Graphics CenterX="1500.0" CenterY="1696.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="O75935" /> </DataNode> <Interaction GraphId="a0d99"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="931.0" Y="148.0" GraphRef="cf795" RelX="-1.0" RelY="0.0" /> <Point X="735.0" Y="143.0" GraphRef="bc5f9" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2484822" /> </Interaction> <Interaction GraphId="a4027"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1167.0" Y="353.0" GraphRef="a8958" RelX="-1.0" RelY="0.0" /> <Point X="1133.0" Y="355.0" GraphRef="fde8b" RelX="0.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2529020" /> </Interaction> <Interaction GraphId="a787f"> <Comment Source="Reactome">Protein levels of condensin subunits are constant during the cell cycle. Four subunits, SMC4, NCAPD2, NCAPG and NCAPH, are phosphorylated in interphase cells (Takemoto et al. 2004) by CK2 i.e. casein kinase II (Takemoto et al. 2006). Except for the phosphorylation of NCAPH subunit on serine residue S570, CK2 phosphorylation sites in condensin I subunits have not been identified. Phosphorylation by CK2 inhibits condensin I-mediated introduction of positive supercoils into DNA and chromatin condensation. Mitotic activation of condensin I involves removal of phosphate groups added by CK2 (Takemoto et al. 2006), but the responsible phosphatase has not been identified.</Comment> <BiopaxRef>d78</BiopaxRef> <BiopaxRef>bd8</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1134.0" Y="414.0" /> <Point X="1132.0" Y="296.0" /> <Anchor Position="0.0" Shape="None" GraphId="d22fa" /> <Anchor Position="0.99" Shape="None" GraphId="ea0a4" /> <Anchor Position="0.5" Shape="None" GraphId="fde8b" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2529020" /> </Interaction> <Interaction GraphId="ab1e0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="991.0" Y="127.0" GraphRef="c704b" RelX="0.20000000000004547" RelY="0.3499999999999943" /> <Point X="996.0" Y="130.0" GraphRef="cf795" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-375302" /> </Interaction> <Interaction GraphId="ab617"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="736.0" Y="296.0" GraphRef="e54cf" RelX="0.0" RelY="1.0" /> <Point X="732.0" Y="341.0" GraphRef="b119d" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2468287" /> </Interaction> <Interaction GraphId="ab69d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="993.0" Y="65.0" GraphRef="f70e1" RelX="0.0" RelY="1.0" /> <Point X="971.0" Y="92.0" GraphRef="dbf6f" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-375302" /> </Interaction> <Interaction GraphId="ac593"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="333.0" Y="718.0" GraphRef="f0bf2" RelX="-1.0" RelY="-0.02857142857142857" /> <Point X="303.0" Y="716.0" GraphRef="a03f5" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2545253" /> </Interaction> <Interaction GraphId="ad5b8"> <Comment Source="Reactome">Cohesin complexes dissociate from chromosomal arms in prometaphase, leading to sister chromatid resolution. Sister chromatid resolution involves separation of sister chromosomal arms while cohesion at sister centromeres persists (Losada et al. 1998, Hauf et al. 2001, Hauf et al. 2005). Cohesin and CDCA5 (Sororin) simultaneously dissociate from chromosomal arms in prometaphase (Nishiyama et al. 2010, Zhang et al. 2011). This process, triggered by CDK1-mediated phosphorylation of CDCA5 (Dreier et al. 2011, Zhang et al. 2011) and PLK1-mediated phosphorylation of the STAG2 cohesin subunit (Hauf et al. 2005), is controlled by WAPAL (Gandhi et al. 2006, Kueng et al. 2006, Shintomi and Hirano 2009). WAPAL controls cohesion of sister chromatids likely through competing with CDCA5 for binding to cohesin-associated PDS5 (PDS5A and PDS5B) (Nishiyama et al. 2010). While the interaction of WAPAL with PDS5 depends on CDCA5 (Nishiyama et al. 2010), WAPAL maintains its association with cohesin through interaction with cohesin subunits (Kueng et al. 2006, Shintomi and Hirano 2009).</Comment> <BiopaxRef>b8e</BiopaxRef> <BiopaxRef>d37</BiopaxRef> <BiopaxRef>f0d</BiopaxRef> <BiopaxRef>a58</BiopaxRef> <BiopaxRef>fab</BiopaxRef> <BiopaxRef>b97</BiopaxRef> <BiopaxRef>a13</BiopaxRef> <BiopaxRef>a0c</BiopaxRef> <BiopaxRef>d05</BiopaxRef> <BiopaxRef>ae5</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="511.0" Y="683.0" /> <Point X="513.0" Y="727.0" /> <Anchor Position="0.0" Shape="None" GraphId="d0bc4" /> <Anchor Position="0.99" Shape="None" GraphId="a115f" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2467794" /> </Interaction> <Interaction GraphId="ad941"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="970.0" Y="377.0" GraphRef="db123" RelX="0.0" RelY="0.37999999999999545" /> <Point X="929.0" Y="378.0" GraphRef="b50b1" RelX="1.0" RelY="-0.043478260869565216" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2529015" /> </Interaction> <Interaction GraphId="af1c0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="457.0" Y="356.0" GraphRef="d0ac3" RelX="1.0" RelY="-0.037037037037037035" /> <Point X="508.0" Y="354.0" GraphRef="ea95b" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2468293" /> </Interaction> <Interaction GraphId="b00fc"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1013.0" Y="416.0" GraphRef="b953c" RelX="1.0" RelY="0.0" /> <Point X="1134.0" Y="414.0" GraphRef="d22fa" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2529020" /> </Interaction> <Interaction GraphId="b140c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="944.0" Y="81.0" GraphRef="aff03" RelX="0.9775280898876404" RelY="-0.047619047619047616" /> <Point X="971.0" Y="92.0" GraphRef="dbf6f" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-375302" /> </Interaction> <Interaction GraphId="b205a"> <Comment Source="Reactome">Phosphorylation of CDCA5 (Sororin) coincides with dissociation of CDCA5 from chromosomal arms in prometaphase. Several serine and threonine residues in CDCA5 are phosphorylated by CDK1 in prometaphase, but only the three sites that perfectly match the CDK1 consensus phosphorylation sequence are shown here - serines S21 and S75 and threonine T159 (Drier et al. 2011, Zhang et al. 2011).</Comment> <BiopaxRef>a13</BiopaxRef> <BiopaxRef>a0c</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="508.0" Y="354.0" /> <Point X="508.0" Y="399.0" /> <Anchor Position="0.0" Shape="None" GraphId="ea95b" /> <Anchor Position="0.99" Shape="None" GraphId="ce78f" /> <Anchor Position="0.5" Shape="None" GraphId="a2b43" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2468293" /> </Interaction> <Interaction GraphId="b223a"> <Comment Source="Reactome">Inhibitory phosphate groups that were added to condensin I subunits by CK2 during interphase have to be removed for full mitotic activation of condensin I (Takemoto et al. 2006). The responsible phosphatase has not been identified.</Comment> <BiopaxRef>d78</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="970.0" Y="339.0" /> <Point X="970.0" Y="377.0" /> <Anchor Position="0.0" Shape="None" GraphId="e7a47" /> <Anchor Position="0.99" Shape="None" GraphId="db123" /> <Anchor Position="0.5" Shape="None" GraphId="bce9e" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2529015" /> </Interaction> <Interaction GraphId="b37f5"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="513.0" Y="727.0" GraphRef="a115f" RelX="0.01999999999998181" RelY="0.44000000000005457" /> <Point X="424.0" Y="774.0" GraphRef="b8040" RelX="1.0" RelY="-0.037037037037037035" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2467794" /> </Interaction> <Interaction GraphId="b3c81"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="215.0" Y="244.0" GraphRef="dd084" RelX="0.020000000000010232" RelY="0.539999999999992" /> <Point X="216.0" Y="247.0" GraphRef="b1304" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-380508" /> </Interaction> <Interaction GraphId="b4914"> <Comment Source="Reactome">CDK1 (CDC2) in complex with CCNB (cyclin B) phosphorylates condensin I subunits NCAPD2, NCAPG and NCAPH in mitosis (Kimura et al. 2001, Takemoto et al. 2006), but other mitotic kinases may also be involved. CDK1 phosphorylation sites in NCAPH have not been established. NCAPD2 threonine residues T1339, T1384 and T1389 are inferred to be phosphorylated by CDK1 based on homologues sites in Xenopus laevis Ncapd2 (Kimura et al. 1998). NCAPG threonine residues T308 and T332 are phosphorylated by CDK1 in vitro and functionally important. The functional importance of threonine T931, also phosphorylated by CDK1 in vitro, has not been demonstrated (Murphy et al. 2008). Phosphorylation by CDK1 is required for mitotic activation of condensin I and promotes chromosomal binding, introduction of positive supercoils into DNA, and chromatin condensation (Kimura et al. 1998, Kimura et al. 2001, Takemoto et al. 2006). </Comment> <BiopaxRef>ad0</BiopaxRef> <BiopaxRef>d78</BiopaxRef> <BiopaxRef>b7c</BiopaxRef> <BiopaxRef>c54</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="972.0" Y="451.0" /> <Point X="973.0" Y="494.0" /> <Anchor Position="0.0" Shape="None" GraphId="b41e5" /> <Anchor Position="0.99" Shape="None" GraphId="c0952" /> <Anchor Position="0.5" Shape="None" GraphId="b0604" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2514854" /> </Interaction> <Interaction GraphId="b4dfc"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="669.0" Y="374.0" GraphRef="bc6d6" RelX="0.9797979797979798" RelY="0.0" /> <Point X="972.0" Y="470.0" GraphRef="b0604" RelX="-0.5" RelY="-2.5" 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RelY="0.4300000000000068" /> <Point X="974.0" Y="518.0" GraphRef="b3338" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2514854" /> </Interaction> <Interaction GraphId="c8d4c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="779.0" Y="344.0" GraphRef="a7b5b" RelX="-1.0" RelY="0.0" /> <Point X="732.0" Y="341.0" GraphRef="b119d" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2468287" /> </Interaction> <Interaction GraphId="cc67d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="513.0" Y="727.0" GraphRef="a115f" RelX="0.01999999999998181" RelY="0.44000000000005457" /> <Point X="514.0" Y="788.0" GraphRef="d5409" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2467794" /> </Interaction> <Interaction GraphId="cc6ec"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="973.0" Y="494.0" GraphRef="c0952" RelX="0.009999999999990905" RelY="0.4300000000000068" /> <Point X="1014.0" Y="497.0" GraphRef="da60d" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2514854" /> </Interaction> <Interaction GraphId="cce2c"> <Comment Source="Reactome">After the nuclear envelope breakdown, phosphorylated NuMA rapidly moves to the centrosomal region (Compton and Luo 1995, Hsu and Yeh 1996, Kotak et al. 2013).</Comment> <BiopaxRef>b92</BiopaxRef> <BiopaxRef>c34</BiopaxRef> <BiopaxRef>d34</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="213.0" Y="190.0" /> <Point X="215.0" Y="244.0" /> <Anchor Position="0.0" Shape="None" GraphId="a4a87" /> <Anchor Position="0.99" Shape="None" GraphId="dd084" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-380508" /> </Interaction> <Interaction GraphId="ccf5f"> <Comment Source="Reactome">The kinetochore assembly on centromeres of replicated chromosomes is completed by mitotic prometaphase. Some kinetochore components are associated with centromeres throughout the cell cycle while others associate with centromeres during mitosis. The sequential kinetochore assembly and kinetochore dynamics is not shown here. For a review of this process, please refer to Cheeseman and Desai 2008.</Comment> <BiopaxRef>cb1</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="735.0" Y="143.0" /> <Point X="736.0" Y="201.0" /> <Anchor Position="0.0" Shape="None" GraphId="bc5f9" /> <Anchor Position="0.99" Shape="None" GraphId="b9d20" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2484822" /> </Interaction> <Interaction GraphId="ce98a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="731.0" Y="396.0" GraphRef="fe957" RelX="-0.009999999999990905" RelY="0.5500000000000114" /> <Point X="734.0" Y="438.0" GraphRef="d407d" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2468287" /> </Interaction> <Interaction GraphId="d0e59"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="787.0" Y="695.0" GraphRef="fb9ff" RelX="-1.0" RelY="-0.043478260869565216" /> <Point X="733.0" Y="697.0" GraphRef="c625e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1638821" /> </Interaction> <Interaction GraphId="d2282"> <Comment Source="Reactome">Prior to anaphase onset, sister-chromatids are held together by cohesin complexes distributed along chromosomal arms and at centromeres. In prometaphase, PLK1, likely recruited to cohesin complexes by binding to CDK1-phosphorylated CDCA5 (Sororin) (Zhang et al. 2011), phosphorylates cohesin subunits STAG2 (SA2) and RAD21 (Hauf et al. 2005). PLK1-mediated phosphorylation of cohesin subunits at centromeres is counteracted by the phosphatase activity of PP2A complex (containing the regulatory subunit B56 i.e. PPP2R5), which is recruited to the kinetochore by shugoshin proteins, SGOL1 and SGOL2 (Kitajima et al. 2006). Therefore, while cohesin complexes dissociate from chromosomal arms in prometaphase (Hauf et al. 2001), they remain bound to centromeres until anaphase onset (Hauf et al. 2001, Hauf et al. 2005, Kitajima et al. 2006). When separase is activated after its inhibitor securin is degraded by APC/C at the onset of anaphase, RAD21 is cleaved by separase. Phosphorylation of RAD21 by PLK1 facilitates subsequent cleavage of RAD21 by separase (Hauf et al. 2005). There are several potential PLK1 phosphorylation sites in STAG2 and RAD21, but the exact positions of in vivo phosphorylation of STAG2 and RAD21 by PLK1 have not been explicitly established (Hauf et al. 2005).</Comment> <BiopaxRef>fab</BiopaxRef> <BiopaxRef>b97</BiopaxRef> <BiopaxRef>f67</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="733.0" Y="516.0" /> <Point X="733.0" Y="576.0" /> <Anchor Position="0.0" Shape="None" GraphId="c6d95" /> <Anchor Position="0.99" Shape="None" GraphId="a517b" /> <Anchor Position="0.5" Shape="None" GraphId="ec1bd" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1638803" /> </Interaction> <Interaction GraphId="d32e8"> <Comment Source="Reactome">While condensin II complex (consisting of subunits SMC2, SMC4, NCAPD3, NCAPG2 and NCAPH2), responsible for condensation of chromosomes in prophase (Hirota et al. 2004, Abe et al. 2011), is nuclear, condensin I is cytosolic and gains access to chromosomes only after the nuclear envelope breakdown at the start of prometaphase (Ono et al. 2004). Condensin I, activated by CDK1 phosphorylation (Kimura et al. 1998, Kimura et al. 2001, Takemoto et al. 2006, Murphy et al. 2008), promotes further condensation of chromosomes in prometaphase and metaphase, visible as longitudinal chromosome shortening (Hirota et al. 2004). Besides CDK1-mediated phosphorylation, association of condensin I with chromosomes may be regulated by AURKB (Lipp et al. 2007). In budding yeast, condensin phosphorylation by Cdc2 (CDK1 ortholog) is followed by Cdc5-mediated phosphorylation (Cdc5 is PLK1 ortholog), which is important for the sustained mitotic activity of condensin complex (St-Pierre et al. 2009). Phosphorylation by PLK1 is also important for the activation of human condensin II complex (Abe et al. 2011).</Comment> <BiopaxRef>e89</BiopaxRef> <BiopaxRef>ad0</BiopaxRef> <BiopaxRef>b7c</BiopaxRef> <BiopaxRef>dca</BiopaxRef> <BiopaxRef>d78</BiopaxRef> <BiopaxRef>f85</BiopaxRef> <BiopaxRef>d07</BiopaxRef> <BiopaxRef>c54</BiopaxRef> <BiopaxRef>db0</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="971.0" Y="635.0" /> <Point X="970.0" Y="683.0" /> <Anchor Position="0.0" Shape="None" GraphId="feaf6" /> <Anchor Position="0.99" Shape="None" GraphId="c14da" /> <Anchor Position="0.5" Shape="None" GraphId="c88d9" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2520883" /> </Interaction> <Interaction GraphId="d64ca"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="856.0" Y="81.0" GraphRef="aff03" RelX="-1.0" RelY="-0.047619047619047616" /> <Point X="270.0" Y="321.0" GraphRef="af799" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-380316" /> </Interaction> <Interaction GraphId="da623"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="733.0" Y="679.0" GraphRef="ff1a8" RelX="-0.0053475935828877" RelY="1.0" /> <Point X="734.0" Y="716.0" GraphRef="f2db7" RelX="0.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1638821" /> </Interaction> <Interaction GraphId="dacbd"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="973.0" Y="632.0" GraphRef="d96a2" RelX="-0.010309278350515464" RelY="1.0" /> <Point X="971.0" Y="635.0" GraphRef="feaf6" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2520883" /> </Interaction> <Interaction GraphId="db134"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="970.0" Y="377.0" GraphRef="db123" RelX="0.0" RelY="0.37999999999999545" /> <Point X="972.0" Y="405.0" GraphRef="b953c" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2529015" /> </Interaction> <Interaction GraphId="dc9dd"> <Comment Source="Reactome">HDAC8 deacetylates cohesin in prometaphase, after cohesin dissociates from chromosomal arms (Deardorff et al. 2012).</Comment> <BiopaxRef>e0f</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="303.0" Y="716.0" /> <Point X="259.0" Y="716.0" /> <Anchor Position="0.0" Shape="None" GraphId="a03f5" /> <Anchor Position="0.99" Shape="None" GraphId="b2ddf" /> <Anchor Position="0.5" Shape="None" GraphId="f4e5e" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2545253" /> </Interaction> <Interaction GraphId="df8fa"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="735.0" Y="112.0" GraphRef="ed243" RelX="-0.007874015748031496" RelY="1.0" /> <Point X="735.0" Y="143.0" GraphRef="bc5f9" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2484822" /> </Interaction> <Interaction GraphId="e0c15"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1174.0" Y="415.0" GraphRef="c2480" RelX="-1.0" RelY="0.0" /> <Point X="1134.0" Y="414.0" GraphRef="d22fa" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2529020" /> </Interaction> <Interaction GraphId="e1df1"> <Comment Source="Reactome">The human kinetochore, is a complex proteinaceous structure that assembles on centromeric DNA and mediates the association of mitotic chromosomes with spindle microtubules in prometaphase. The molecular composition of the human kinetochore is reviewed in detail in Cheeseman et al., 2008. This complex structure is composed of numerous protein complexes and networks including: the constitutive centromere-associated network (CCAN) containing several sub-networks such as (CENP-H, I, K), (CENP-50/U, O, P, Q, R), the KMN network (containing KNL1, the Mis12 complex, and the Ndc80 complex), the chromosomal passenger complex, the mitotic checkpoint complex, the nucleoporin 107-160 complex and the RZZ complex. &lt;br&gt;At prometaphase, following breakdown of the nuclear envelope, the kinetochores of condensed chromosomes begin to interact with spindle microtubules. In humans, 15-20 microtubules are bound to each kinetochore (McEwen et al., 2001), and the attachment of 15 microtubules to the kinetochore is shown in this reaction. Recently, it was found that the core kinetochore-microtubule attachment site is within the KMN network and is likely to be formed by two closely apposed low-affinity microtubule-binding sites, one in the Ndc80 complex and a second in KNL1 (Cheeseman et al., 2006). </Comment> <BiopaxRef>b20</BiopaxRef> <BiopaxRef>c76</BiopaxRef> <BiopaxRef>c72</BiopaxRef> <BiopaxRef>d71</BiopaxRef> <BiopaxRef>cb1</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="971.0" Y="92.0" /> <Point X="991.0" Y="127.0" /> <Anchor Position="0.0" Shape="None" GraphId="dbf6f" /> <Anchor Position="0.99" Shape="None" GraphId="c704b" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-375302" /> </Interaction> <Interaction GraphId="e5311"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="571.0" Y="374.0" GraphRef="bc6d6" RelX="-1.0" RelY="0.0" /> <Point X="508.0" Y="375.0" GraphRef="a2b43" RelX="0.0" RelY="-1.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2468293" /> </Interaction> <Interaction GraphId="e65dc"> <Comment Source="Reactome">PLK1-mediated phosphorylation of the STAG2 subunit of centromeric cohesin (Hauf et al. 2005) is counteracted by the kinetochore PP2A phosphatase, containing the 56 kDa regulatory B subunit (PP2A-B56 i.e. PP2A-PPP2R5). PP2A-B56 is recruited to the centromeric cohesin complex by shugoshin proteins (SGOL1 and SGOL2) (Kitajima et al. 2006), which are also kinetochore constituents (Cheeseman and Desai 2008). SGOL1 localization to centromeres is sustained by the interaction with histone H2A possessing the phosphorylation of T120 which is introduced by the protein kinase BUB1, and heterochromatin protein HP1 (Kitajima et al. 2005, Kawashima et al. 2010, Yamagishi et al. 2008). Shugoshin- and PP2A-B56-regulated dephosphorylation of centromeric STAG2 ensures that the cohesin complex remains bound to centromeres throughout prometaphase and metaphase, thereby preventing premature separation of sister chromatids (Salic et al. 2004, Kitajima et al. 2004, Kitajima et al. 2005, Kitajima et al. 2006).</Comment> <BiopaxRef>f67</BiopaxRef> <BiopaxRef>e5d</BiopaxRef> <BiopaxRef>d84</BiopaxRef> <BiopaxRef>a16</BiopaxRef> <BiopaxRef>b97</BiopaxRef> <BiopaxRef>cb1</BiopaxRef> <BiopaxRef>f21</BiopaxRef> <BiopaxRef>f0a</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="733.0" Y="697.0" /> <Point X="734.0" Y="735.0" /> <Anchor Position="0.0" Shape="None" GraphId="c625e" /> <Anchor Position="0.99" Shape="None" GraphId="f25bb" /> <Anchor Position="0.5" Shape="None" GraphId="f2db7" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1638821" /> </Interaction> <Interaction GraphId="ea4df"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="259.0" Y="716.0" GraphRef="b2ddf" RelX="-0.4399999999999977" RelY="0.0" /> <Point X="208.0" Y="716.0" GraphRef="b6fb0" RelX="1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2545253" /> </Interaction> <Interaction GraphId="eac8d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="513.0" Y="727.0" GraphRef="a115f" RelX="0.01999999999998181" RelY="0.44000000000005457" /> <Point X="433.0" Y="718.0" GraphRef="f0bf2" RelX="1.0" RelY="-0.02857142857142857" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2467794" /> </Interaction> <Interaction GraphId="ebea6"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1002.0" Y="445.0" GraphRef="b8c1b" RelX="-1.0" RelY="-0.043478260869565216" /> <Point X="972.0" Y="451.0" GraphRef="b41e5" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2514854" /> </Interaction> <Interaction GraphId="ecd7d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="178.0" Y="149.0" GraphRef="a607a" RelX="1.0" RelY="-0.0196078431372549" /> <Point X="213.0" Y="190.0" GraphRef="a4a87" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-380508" /> </Interaction> <Interaction GraphId="edf7f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="259.0" Y="716.0" GraphRef="b2ddf" RelX="-0.4399999999999977" RelY="0.0" /> <Point X="253.0" Y="671.0" GraphRef="e26f6" RelX="0.9672131147540983" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2545253" /> </Interaction> <Interaction GraphId="ef3b8"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="511.0" Y="490.0" GraphRef="c4bd7" RelX="0.0" RelY="0.9591836734693877" /> <Point X="509.0" Y="521.0" GraphRef="f859e" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2466068" /> </Interaction> <Interaction GraphId="f0d50"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="972.0" Y="427.0" GraphRef="b953c" RelX="0.0" RelY="1.0" /> <Point X="972.0" Y="451.0" GraphRef="b41e5" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2514854" /> </Interaction> <Interaction GraphId="f1790"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="508.0" Y="399.0" GraphRef="ce78f" RelX="0.0" RelY="0.44999999999998863" /> <Point X="511.0" Y="442.0" GraphRef="c4bd7" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2468293" /> </Interaction> <Interaction GraphId="f194b"> <Comment Source="Reactome">NuMA can interact with microtubules by direct binding to tubulin. Binding occurs through amino acids 1868-1967 of human NuMA (tail IIA) and appears to play a role in the organization of the spindle poles by stably crosslinking microtubule fibers (Haren and Merdes 2002). While the exact mechanism of microtubule bundling is not known, NuMA has been shown to form large fibrous networks (Saredi et al. 1996, Gueth-Hallonet et al.1998, Harborth et al.1999) apparently as a result of dimerization of the NuMA rod domains followed by association of multiple NuMA dimers through their tail domains.</Comment> <BiopaxRef>eb3</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="270.0" Y="321.0" /> <Point X="245.0" Y="386.0" /> <Anchor Position="0.0" Shape="None" GraphId="af799" /> <Anchor Position="0.99" Shape="None" GraphId="a80a6" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-380316" /> </Interaction> <Interaction GraphId="f2698"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="508.0" Y="399.0" GraphRef="ce78f" RelX="0.0" RelY="0.44999999999998863" /> <Point X="457.0" Y="407.0" GraphRef="e765c" RelX="1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2468293" /> </Interaction> <Interaction GraphId="f281f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="974.0" Y="564.0" GraphRef="b3338" RelX="0.0" RelY="0.9574468085106383" /> <Point X="971.0" Y="656.0" GraphRef="c88d9" RelX="0.5" RelY="-3.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2520883" /> </Interaction> <Interaction GraphId="f36cb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1132.0" Y="296.0" GraphRef="ea0a4" RelX="-0.01999999999998181" RelY="-1.1800000000000068" /> <Point X="1023.0" Y="297.0" GraphRef="a29f9" RelX="1.0" RelY="-0.02040816326530612" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2529020" /> </Interaction> <Interaction GraphId="f39a0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="970.0" Y="683.0" GraphRef="c14da" RelX="-0.009999999999990905" RelY="0.4800000000000182" /> <Point X="970.0" Y="686.0" GraphRef="e45d0" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2520883" /> </Interaction> <Interaction GraphId="f3ae2"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="279.0" Y="646.0" GraphRef="cc5ff" RelX="-0.0196078431372549" RelY="1.0" /> <Point X="278.0" Y="717.0" GraphRef="f4e5e" RelX="-3.0" RelY="1.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2545253" /> </Interaction> <Interaction GraphId="f4e29"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="669.0" Y="374.0" GraphRef="bc6d6" RelX="0.9797979797979798" RelY="0.0" /> <Point X="731.0" Y="374.0" GraphRef="f1ea2" RelX="-0.5" RelY="5.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2468287" /> </Interaction> <Interaction GraphId="f58a0"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="507.0" Y="330.0" GraphRef="f1852" RelX="-0.008695652173913044" RelY="0.974025974025974" /> <Point X="508.0" Y="354.0" GraphRef="ea95b" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2468293" /> </Interaction> <Interaction GraphId="f891d"> <Comment Source="Reactome">Prior to anaphase onset, sister-chromatids are held together by cohesin complexes. PLK1-dependent phosphorylation of the cohesin subunit STAG2 (SA2) (Hauf et al. 2005) promotes dissociation of cohesins from chromosomal arms in prometaphase (Hauf et al. 2001). Besides phosphorylating STAG2, PLK1 also phosphorylates RAD21 cohesin subunit, but the phosphorylation of RAD21 is not required for the dissociation of cohesin from chromosomal arms in early mitosis (Hauf et al. 2005). There are several potential PLK1 phosphorylation sites in STAG2 and RAD21, but the exact positions of in vivo phosphorylation of STAG2 and RAD21 by PLK1 have not been explicitly established (Hauf et al. 2005). It is likely that the phosphorylation of cohesin-bound CDCA5 (Sororin) by CDK1 creates a docking site for PLK1 at threonine T159 of CDCA5, thus enabling PLK1 to phosphorylate cohesin subunits (Zhang et al. 2011).</Comment> <BiopaxRef>fab</BiopaxRef> <BiopaxRef>b97</BiopaxRef> <BiopaxRef>a13</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="509.0" Y="521.0" /> <Point X="510.0" Y="580.0" /> <Anchor Position="0.0" Shape="None" GraphId="f859e" /> <Anchor Position="0.99" Shape="None" GraphId="a5754" /> <Anchor Position="0.5" Shape="None" GraphId="f2c5b" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2466068" /> </Interaction> <Interaction GraphId="f9697"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="630.0" Y="548.0" GraphRef="c2c20" RelX="1.0" RelY="0.0" /> <Point X="732.0" Y="549.0" GraphRef="ec1bd" RelX="-1.0" RelY="3.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1638803" /> </Interaction> <Interaction GraphId="f988f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1022.0" Y="360.0" GraphRef="ec50c" RelX="-1.0" RelY="0.0" /> <Point X="970.0" Y="361.0" GraphRef="bce9e" RelX="0.0" RelY="3.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2529015" /> </Interaction> <Interaction GraphId="f9ffb"> <Comment Source="Reactome">Phosphorylation of CDCA5 (Sororin) coincides with dissociation of CDCA5 from chromosomal arms in prometaphase, but phosphorylated CDCA5 persists on centromeres throughout prophase and metaphase. Several serine and threonine residues in CDCA5 are phosphorylated by CDK1 in prometaphase, but only the three sites that perfectly match the CDK1 consensus phosphorylation sequence are shown here - serines S21 and S75 and threonine T159 (Drier et al. 2011, Zhang et al. 2011).</Comment> <BiopaxRef>a13</BiopaxRef> <BiopaxRef>a0c</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="732.0" Y="341.0" /> <Point X="731.0" Y="396.0" /> <Anchor Position="0.0" Shape="None" GraphId="b119d" /> <Anchor Position="0.99" Shape="None" GraphId="fe957" /> <Anchor Position="0.5" Shape="None" GraphId="f1ea2" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-2468287" /> </Interaction> <Interaction GraphId="fa4f7"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="734.0" Y="490.0" GraphRef="d407d" RelX="0.0" RelY="1.0" /> <Point X="733.0" Y="516.0" GraphRef="c6d95" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" 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rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Kotak S, Busso C, Gönczy 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="d84"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">15723797</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">Human Bub1 defines the persistent cohesion site along the mitotic chromosome by affecting Shugoshin localization.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Kitajima TS, Hauf S, Ohsugi M, Yamamoto T, Watanabe Y.</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="f0d"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">17112726</bp:ID> 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</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="f67"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">16541025</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">Shugoshin collaborates with protein phosphatase 2A to protect cohesin.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Kitajima TS, Sakuno T, Ishiguro K, Iemura S, Natsume T, Kawashima SA, Watanabe Y.</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="cb1"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">18097444</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE 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xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="f0a"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">18716626</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">Heterochromatin links to centromeric protection by recruiting shugoshin.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Yamagishi Y, Sakuno T, Shimura M, Watanabe Y.</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="d78"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">17066080</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">Negative regulation of condensin I by 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