S Phase (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="S Phase" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">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. View original pathway at [http://www.reactome.org/PathwayBrowser/#DIAGRAM=69242 Reactome].</Comment> <Comment Source="Reactome-Converter">Pathway is converted from Reactome ID: 69242</Comment> <Comment Source="Reactome-version">Reactome version: 75</Comment> <Attribute Key="reactome_id" Value="69242"/> <Graphics BoardWidth="2376.0" BoardHeight="2468.0"/> <DataNode TextLabel="SKP2 " GraphId="a07db" Type="Protein" GroupRef="e396d"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-187547"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="240.0" CenterY="1888.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q13309"/> </DataNode> <DataNode TextLabel="CCND1 " GraphId="a0878" Type="Protein" GroupRef="fe9b9"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-8848441"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="1500.0" CenterY="1568.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P24385"/> </DataNode> <DataNode TextLabel="Mitotic Prometaphase" GraphId="a0b25" Type="Pathway"> <Comment Source="Reactome">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. </Comment> <Attribute Key="org.pathvisio.DoubleLineProperty" Value="Double"/> <Graphics CenterX="1333.0" CenterY="1274.5" Width="178.0" Height="49.0" ZOrder="32768" FontSize="10" Valign="Middle" LineThickness="0.0" Color="14961e"/> <Xref Database="Reactome" ID="R-HSA-68877"/> </DataNode> <DataNode TextLabel="ESCO2 " GraphId="a0bce" Type="Protein" GroupRef="a496e"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-2468046"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="1080.0" CenterY="1568.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q56NI9"/> </DataNode> <DataNode TextLabel="E2F4 " GraphId="a1106" Type="Protein" GroupRef="af41c"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-8964470"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="1500.0" CenterY="1928.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q16254"/> </DataNode> <DataNode TextLabel="PSME4 " GraphId="a161b" Type="Protein" GroupRef="af457"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-68819"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="800.0" CenterY="2368.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q14997"/> </DataNode> <DataNode TextLabel="p-T187-CDKN1B " GraphId="a19b3" Type="Protein" GroupRef="ba1da"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-187568"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="380.0" CenterY="1868.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P46527"/> </DataNode> <DataNode TextLabel="CCNE1 " GraphId="a1b22" Type="Protein" GroupRef="fe9b9"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-8848441"/> <Attribute Key="copies_num" Value="9"/> <Graphics CenterX="1500.0" CenterY="1588.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P24864"/> </DataNode> <DataNode TextLabel="PSMC3 " GraphId="a1d7b" Type="Protein" GroupRef="f1686"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-177750"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="520.0" CenterY="1948.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P17980"/> </DataNode> <DataNode TextLabel="CCNA" GraphId="a1e20" Type="Complex"> <Attribute Key="cellular_location" Value="cytosol"/> <Graphics CenterX="392.0" CenterY="39.0" Width="68.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-170089"/> </DataNode> <DataNode TextLabel="RAD21 " GraphId="a1f31" Type="Protein" GroupRef="acbb6"> <Attribute Key="cellular_location" Value="chromosome, centromeric region"/> <Attribute Key="complex_id" Value="R-HSA-1638799"/> <Attribute Key="copies_num" Value="2"/> <Graphics CenterX="1080.0" CenterY="1908.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O60216"/> </DataNode> <DataNode TextLabel="ADP" GraphId="a2577" Type="Metabolite"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Graphics CenterX="495.0" CenterY="736.0" Width="46.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:456216"/> </DataNode> <DataNode TextLabel="Sister Centromere" GraphId="a270c"> <Attribute Key="cellular_location" Value="chromosome"/> <Graphics 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<DataNode TextLabel="RBBP4 " GraphId="c2e2c" Type="Protein" GroupRef="af41c"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-8964470"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="1500.0" CenterY="2088.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q09028"/> </DataNode> <DataNode TextLabel="CCNE1 " GraphId="c2fd3" Type="Protein" GroupRef="fc8a6"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-8848491"/> <Attribute Key="copies_num" Value="84"/> <Graphics CenterX="1640.0" CenterY="1788.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P24864"/> </DataNode> <DataNode TextLabel="CDCA5 " GraphId="c3153" Type="Protein" GroupRef="acbb6"> <Attribute Key="cellular_location" Value="chromosome, centromeric region"/> <Attribute Key="complex_id" Value="R-HSA-1638799"/> <Attribute Key="copies_num" Value="2"/> <Graphics CenterX="1080.0" CenterY="2008.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q96FF9"/> </DataNode> <DataNode TextLabel="CDKN1B" GraphId="c347f" Type="Protein"> <Attribute Key="cellular_location" Value="cytosol"/> <Graphics CenterX="953.5" CenterY="139.0" Width="61.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P46527"/> </DataNode> <DataNode TextLabel="CCNA:p-T160-CDK2" GraphId="c3758" Type="Complex"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Graphics CenterX="739.5" CenterY="372.5" Width="137.0" Height="21.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-187952"/> </DataNode> <DataNode TextLabel="E2F1:TFDP1,TFDP2:CDC25A gene" GraphId="c37fe" Type="Complex"> <BiopaxRef>ea6</BiopaxRef> <BiopaxRef>de8</BiopaxRef> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Graphics CenterX="279.0" CenterY="248.0" Width="126.0" Height="36.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-8961960"/> </DataNode> <DataNode TextLabel="UBC(77-152) " GraphId="c3b36" Type="Protein" GroupRef="bdbd1"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-177997"/> <Attribute Key="copies_num" Value="15"/> <Graphics CenterX="940.0" CenterY="1908.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P0CG48"/> </DataNode> <DataNode TextLabel="CCNA:CDK2" GraphId="c3f2c" Type="Complex"> <Attribute Key="cellular_location" Value="cytosol"/> <Graphics CenterX="444.5" CenterY="143.5" Width="93.0" Height="21.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-187501"/> </DataNode> <DataNode TextLabel="p-Y342-PTK6" GraphId="c4179" Type="Protein"> <Attribute Key="cellular_location" Value="cytosol"/> <Graphics CenterX="1036.5" CenterY="41.5" Width="93.0" Height="29.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q13882"/> </DataNode> <DataNode TextLabel="UBC(77-152) " GraphId="c48d0" Type="Protein" GroupRef="ed78f"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-68524"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="380.0" CenterY="1668.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P0CG48"/> </DataNode> <DataNode TextLabel="RPS27A(1-76) " GraphId="c4ab9" Type="Protein" GroupRef="bdbd1"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-177997"/> <Attribute Key="copies_num" Value="3"/> <Graphics CenterX="940.0" CenterY="1788.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P62979"/> </DataNode> <DataNode TextLabel="UBC(305-380) " GraphId="c4bbc" Type="Protein" GroupRef="bdbd1"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-177997"/> <Attribute Key="copies_num" Value="21"/> <Graphics CenterX="940.0" CenterY="1968.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P0CG48"/> </DataNode> <DataNode TextLabel="hyperphosphorylated RB1 " GraphId="c4cd5" Type="Protein" GroupRef="c2f55"> <Comment Source="Reactome">The pRB C-terminus contains a cluster of seven candidate in vivo cdk phosphorylation sites (residues 795, 807, 811, 821, and 826) and is phosphorylated in vitro by cyclin A, cyclin E, and cyclin D-associated kinases.</Comment> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-187920"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="1640.0" CenterY="1668.0" Width="100.0" Height="40.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P06400"/> </DataNode> <DataNode TextLabel="p-S795-RB1 " GraphId="c56fe" Type="Protein" GroupRef="c15c0"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-187963"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="1640.0" CenterY="1568.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P06400"/> </DataNode> <DataNode TextLabel="PSMB8 " GraphId="c57c0" Type="Protein" GroupRef="f1686"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-177750"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="520.0" CenterY="1868.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P28062"/> </DataNode> <DataNode TextLabel="CDKN1A " GraphId="c618b" Type="Protein" GroupRef="ca50e"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-182558"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="1788.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P38936"/> </DataNode> <DataNode TextLabel="Cyclin&#10;E/A:p-T160-CDK2:p-S130-CDKN1A,p-T187-CDKN1B" GraphId="c61cd" Type="Complex"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Graphics CenterX="592.0" CenterY="675.0" Width="160.0" Height="48.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-187522"/> </DataNode> <DataNode TextLabel="UBA52(1-76) " GraphId="c62f0" Type="Protein" GroupRef="ba1da"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" 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Database="Uniprot-TrEMBL" ID="Q8TAA3"/> </DataNode> <DataNode TextLabel="Sister Chromosomal&#10;Arm" GraphId="c69fc"> <Attribute Key="cellular_location" Value="chromosome"/> <Graphics CenterX="1164.5" CenterY="952.0" Width="87.0" Height="46.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Reactome" ID="R-ALL-1638790"/> </DataNode> <DataNode TextLabel="PSMA6 " GraphId="c6cfb" Type="Protein" GroupRef="af457"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-68819"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="800.0" CenterY="1668.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P60900"/> </DataNode> <DataNode TextLabel="CDKN1A " GraphId="c75db" Type="Protein" GroupRef="e66b3"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-182504"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="1640.0" 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Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-68819"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="800.0" CenterY="2148.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O43242"/> </DataNode> <DataNode TextLabel="CUL1:SKP1:SKP2" GraphId="ca0ef" Type="Complex"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Graphics CenterX="820.5" CenterY="725.0" Width="83.0" Height="36.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-187541"/> </DataNode> <DataNode TextLabel="PSMD5 " GraphId="ca4fd" Type="Protein" GroupRef="af457"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-68819"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="800.0" CenterY="2188.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q16401"/> </DataNode> <DataNode TextLabel="PSMB6 " GraphId="ca515" Type="Protein" GroupRef="f1686"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-177750"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="520.0" CenterY="1828.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P28072"/> </DataNode> <DataNode TextLabel="UBC(305-380) " GraphId="caac3" Type="Protein" GroupRef="ed78f"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-68524"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="380.0" CenterY="1728.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P0CG48"/> </DataNode> <DataNode TextLabel="ATP" GraphId="cc6ab" Type="Metabolite"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Graphics CenterX="362.0" CenterY="722.0" Width="40.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:30616"/> </DataNode> <DataNode TextLabel="UBC(609-684) " GraphId="cca97" Type="Protein" GroupRef="c6514"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-113595"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="660.0" CenterY="2188.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P0CG48"/> </DataNode> <DataNode TextLabel="PSMA5 " GraphId="ccce9" Type="Protein" GroupRef="af457"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-68819"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="800.0" CenterY="1648.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P28066"/> </DataNode> <DataNode 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Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-113595"/> </DataNode> <DataNode TextLabel="PSMD10 " GraphId="cd2df" Type="Protein" GroupRef="af457"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-68819"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="800.0" CenterY="2048.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O75832"/> </DataNode> <DataNode TextLabel="ATP" GraphId="cd4bc" Type="Metabolite"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Graphics CenterX="1047.0" CenterY="632.0" Width="42.0" Height="28.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:30616"/> </DataNode> <DataNode TextLabel="CUL1 " GraphId="cdbce" Type="Protein" GroupRef="e93e2"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" 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</DataNode> <DataNode TextLabel="PSMB4 " GraphId="ce59d" Type="Protein" GroupRef="f1686"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" Value="R-HSA-177750"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="520.0" CenterY="1788.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P28070"/> </DataNode> <DataNode TextLabel="CCNA1 " GraphId="ce9e4" Type="Protein" GroupRef="c0a53"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-170089"/> <Attribute Key="copies_num" Value="7"/> <Graphics CenterX="100.0" CenterY="1508.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P78396"/> </DataNode> <DataNode TextLabel="p-Y15-CDK2 " GraphId="cea3e" Type="Protein" GroupRef="a111e"> <Attribute Key="cellular_location" Value="nucleoplasm"/> <Attribute Key="complex_id" 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Several factors contribute to the recruitment of CDCA5 to chromatin-associated cohesin: DNA replication (i.e. presence of two sister chromatids), association of cohesin complex with PDS5, and acetylation of the SMC3 cohesin subunit by ESCO1/ESCO2 acetyltransferases. Experiments in which a recombinant tagged mouse CDCA5 was expressed in human HeLa cell line showed that CDCA5 starts to accumulate on chromatin in S-phase and dissociates from chromosomal arms in prophase (Nishiyama et al. 2010). &lt;br&gt;&lt;br&gt; CDCA5 is essential for the establishment of chromosomal cohesion only in the presence of WAPAL, suggesting that the key role of CDCA5 (Sororin) is to antagonize WAPAL. Both CDCA5 and WAPAL contain an FGF (phenylalanine-glycine-phenylalanine) motif that is essential for PDS5 binding and is also essential for CDCA5 function in cohesion establishment. Indeed, CDCA5 is able to displace WAPAL from PDS5:WAPAL heterodimers in vitro. 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In addition to CDKN1A and CDKN1B, the active CCNA:p-T160-CDK2 complex also phosphorylates FZR1 (Cdh1) and RB1. All this creates auto-amplification loops that render Cdk2 increasingly more active. 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Cks1 binds to Skp2 in the leucine-rich repeat (LRR) domain and C-terminal tail (Hao et al., 2005). The phosphorylated Thr187 side chain of p27 associates with a phosphate binding site on Cks1, and the side chain containing Glu185 is positioned in the interface between Skp2 and Cks1 where it interacts with both (Hao et al., 2005).</Comment> <BiopaxRef>f84</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="768.0" Y="760.0"/> <Point X="768.0" Y="819.0"/> <Anchor Position="0.0" Shape="None" GraphId="a0003"/> <Anchor Position="0.99" Shape="None" GraphId="c3402"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-187545"/> </Interaction> <Interaction GraphId="da68a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="306.0" Y="505.0" GraphRef="dadaf" RelX="0.9661016949152542" RelY="0.0"/> <Point X="340.0" Y="430.0" GraphRef="f0cd1" RelX="11.0" RelY="0.0" ArrowHead="Arrow"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-174164"/> </Interaction> <Interaction GraphId="dacfd"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1345.0" Y="91.0" GraphRef="d08d9" RelX="0.7799999999999727" RelY="0.04000000000000625"/> <Point X="1370.0" Y="120.0" GraphRef="e0147" RelX="-1.0" RelY="0.0" ArrowHead="Arrow"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-8848436"/> </Interaction> <Interaction GraphId="db35e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="2125.0" Y="282.0" GraphRef="cd100" RelX="-1.0" RelY="0.0"/> <Point X="2029.0" Y="358.0" GraphRef="f4342" RelX="0.0" RelY="0.0"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-75824"/> </Interaction> <Interaction GraphId="dc058"> <Comment Source="Reactome">During G1, the activity of cyclin-dependent kinases (CDKs) is controlled by the CDK inhibitors (CKIs) CDKN1A (p21) and CDKN1B (p27), thereby preventing premature entry into S phase (Guardavaccaro and Pagano, 2006). </Comment> <BiopaxRef>a5c</BiopaxRef> <BiopaxRef>a9e</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="512.0" Y="459.0"/> <Point X="513.0" Y="530.0"/> <Anchor Position="0.0" Shape="None" GraphId="cc680"/> <Anchor Position="0.99" Shape="None" GraphId="f9e56"/> <Anchor Position="0.5" Shape="None" GraphId="cdf21"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-187934"/> </Interaction> <Interaction GraphId="dc274"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="750.0" Y="80.0" GraphRef="b9930" RelX="0.0" RelY="1.0"/> <Point X="726.0" Y="119.0" GraphRef="d9ab8" RelX="0.0" RelY="0.0"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-198613"/> </Interaction> <Interaction GraphId="dc3b7"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="562.0" Y="418.0" GraphRef="b8d42" RelX="0.9813084112149533" RelY="-0.04"/> <Point X="617.0" Y="415.0" GraphRef="d8121" RelX="0.0" RelY="0.0"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-187949"/> </Interaction> <Interaction GraphId="dc506"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1291.0" Y="947.0" GraphRef="b67c8" RelX="-1.0" RelY="0.0"/> <Point X="1243.0" Y="977.0" GraphRef="da2f8" RelX="0.0" RelY="0.0"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-2468041"/> </Interaction> <Interaction GraphId="de222"> <Comment Source="Reactome">Recognition of p27 by SCF(Skp2) and the subsequent ubiquitination of p27 is dependent upon Cyclin E/A:Cdk2-mediated phosphorylation of p27 at Thr 187 (Montagnoli et al., 1999). p21 is also phosphorylated at a specific site (Ser130) by Cyclin E/A:Cdk2, stimulating its ubiquitination. Unlike p27, however, p21 ubiquitination can take place in the absence of phosphorylation, although with less efficiency (Bornstein et al.,2003).</Comment> <BiopaxRef>a5c</BiopaxRef> <BiopaxRef>f84</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="406.0" Y="542.0"/> <Point X="329.0" Y="543.0"/> <Anchor Position="0.0" Shape="None" GraphId="a36a9"/> <Anchor Position="0.99" Shape="None" GraphId="edd54"/> <Anchor Position="0.5" Shape="None" GraphId="a7e78"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-187916"/> </Interaction> <Interaction GraphId="df63e"> <Comment Source="Reactome">The interaction between the Skp2 subunit of the SCF(Skp2) complex and p27 is dependent upon Cdk2:Cyclin A/E mediated phosphorylation of p27 at Thr 187 (Carrano et al, 1999; Tsvetkov et al, 1999). There is evidence that Cyclin A/B:Cdk1 can also bind and phosphorylate p27 on Thr 187 (Nakayama et al., 2004). 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ESCO1 and ESCO2 share sequence homology in the C-terminal region, consisting of a H2C2 zinc finger motif and an acetyltransferase domain (Hou and Zou 2005). Both ESCO1 and ESCO2 acetylate the cohesin subunit SMC3 on two lysine residues, K105 and K106 (Zhang et al. 2008), an important step in the establishment of sister-chromatid cohesion during the S-phase of the cell cycle. Divergent N-termini of ESCO1 and ESCO2, necessary for chromatin binding, suggest that ESCO1 and ESCO2 may perform distinct functions in sister chromatid cohesion (Hou and Zou 2005). Several studies suggest that ESCO2 may be predominantly involved in acetylation of the SMC3 subunit of centromeric cohesin. A conditional targeting of Esco2 locus in mice leads to pre-implantational loss of homozygous Esco2 -/- embryos at the eight-cell stage. Prometaphase chromosomes isolated from two-cell stage Esco2 knockout embryos show marked cohesion defect at centromeres (Whelan et al. 2012). ESCO2 protein appears in the S-phase (Hou and Zou 2005, Whelan et al. 2012) and in mouse embryonic fibroblasts Esco2 predominantly localizes to pericentric heterochromatin (Whelan et al. 2012). Mutations in the ESCO2 gene (Vega et al. 2005) that impair ESCO2 acetyltransferase activity (Gordillo et al. 2008) are the cause of the Roberts syndrome, an autosomal recessive disorder characterized by craniofacial and limb abnormalities, and intellectual disability. 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rdf:datatype="http://www.w3.org/2001/XMLSchema#string">9372967</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">A dominant-negative cyclin D1 mutant prevents nuclear import of cyclin-dependent kinase 4 (CDK4) and its phosphorylation by CDK-activating kinase.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Diehl JA, Sherr CJ.</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="ec6"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">21111234</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">Sororin mediates sister chromatid cohesion by antagonizing Wapl.</bp:TITLE> <bp:AUTHORS 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<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="aea"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">22885700</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">HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Deardorff MA, Bando M, Nakato R, Watrin E, Itoh T, Minamino M, Saitoh K, Komata M, Katou Y, Clark D, Cole KE, De Baere E, Decroos C, Di Donato N, Ernst S, Francey LJ, Gyftodimou Y, Hirashima K, Hullings M, Ishikawa Y, Jaulin C, Kaur M, Kiyono T, Lombardi PM, Magnaghi-Jaulin L, Mortier GR, Nozaki N, Petersen MB, Seimiya H, Siu VM, Suzuki Y, Takagaki K, Wilde JJ, Willems PJ, Prigent C, Gillessen-Kaesbach G, Christianson DW, Kaiser FJ, Jackson LG, Hirota T, Krantz 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rdf:datatype="http://www.w3.org/2001/XMLSchema#string">1312467</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">Cyclin A is required at two points in the human cell cycle.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pagano M, Pepperkok R, Verde F, Ansorge W, Draetta G.</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="e8a"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">10375532</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">p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Tsvetkov LM, Yeh KH, Lee SJ, Sun H, Zhang 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="c2a"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">22101327</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">Cohesin acetyltransferase Esco2 is a cell viability factor and is required for cohesion in pericentric heterochromatin.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Whelan G, Kreidl E, Kreidl E, Wutz G, Egner A, Peters JM, Eichele G.</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="f84"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">11231585</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 cell-cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Ganoth D, Bornstein G, Ko TK, Larsen B, Tyers M, Pagano M, Hershko 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="e6c"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">15199159</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">Noncatalytic requirement for cyclin A-cdk2 in p27 turnover.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Zhu XH, Nguyen H, Halicka HD, Traganos F, Koff 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="ea6"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">7623816</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">Cellular targets for activation by the E2F1 transcription factor include DNA synthesis- and G1/S-regulatory genes.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">DeGregori J, Kowalik T, Nevins JR.</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="f53"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">11907280</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">Cyclin A- and cyclin E-Cdk complexes shuttle between the nucleus and the cytoplasm.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Jackman M, Kubota Y, den Elzen N, Hagting A, Pines J.</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="d55"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">15735756</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">Phosphorylation of cyclin D1 at Thr 286 during S phase leads to its proteasomal degradation and allows efficient DNA synthesis.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Guo Y, Yang K, Harwalkar J, Nye JM, Mason DR, Garrett MD, Hitomi M, Stacey DW.</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="c9b"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">16209941</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">Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Hao B, Zheng N, Schulman BA, Wu G, Miller JJ, Pagano M, Pavletich NP.</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="e78"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">16582612</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">Dual regulation of the anaphase promoting complex in human cells by cyclin A-Cdk2 and cyclin A-Cdk1 complexes.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Mitra J, Enders GH, Azizkhan-Clifford J, Lengel KL.</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="a5a"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">12244303</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">Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation in breast cancer.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Viglietto G, Motti ML, Bruni P, Melillo RM, D'Alessio A, Califano D, Vinci F, Chiappetta G, Tsichlis P, Bellacosa A, Fusco A, Santoro M.</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="de8"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">10454584</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">CDC25A phosphatase is a target of E2F and is required for efficient E2F-induced S phase.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Vigo E, Müller H, Prosperini E, Hateboer G, Cartwright P, Moroni MC, Helin K.</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="d33"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">24901984</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">Glycogen synthase kinase (GSK) 3β phosphorylates and protects nuclear myosin 1c from proteasome-mediated degradation to activate rDNA transcription in early G1 cells.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Sarshad AA, Corcoran M, Al-Muzzaini B, Borgonovo-Brandter L, Von Euler A, Lamont D, Visa N, Percipalle 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="b65"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">15958495</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">Two human orthologues of Eco1/Ctf7 acetyltransferases are both required for proper sister-chromatid cohesion.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Hou F, Zou 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="a21"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">25733683</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">Brk/Protein tyrosine kinase 6 phosphorylates p27KIP1, regulating the activity of cyclin D-cyclin-dependent kinase 4.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Patel P, Asbach B, Shteyn E, Gomez C, Coltoff A, Bhuyan S, Tyner AL, Wagner R, Blain SW.</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="bbb"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">10559916</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">SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Carrano AC, Eytan E, Hershko A, Pagano M.</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="d01"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">15837422</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">Sororin, a substrate of the anaphase-promoting complex, is required for sister chromatid cohesion in vertebrates.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Rankin S, Ayad NG, Kirschner MW.</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="e98"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">8700224</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">Cdc25 cell-cycle phosphatase as a target of c-myc.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Galaktionov K, Chen X, Beach D.</bp:AUTHORS> </bp:PublicationXref> <bp:openControlledVocabulary xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#"><bp:TERM>S phase pathway</bp:TERM><bp:ID>PW:0000089</bp:ID><bp:Ontology>Pathway Ontology</bp:Ontology></bp:openControlledVocabulary></Biopax> </Pathway>

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