BioPAX pathway converted from "SUMOylation of DNA damage response and repair proteins" in the Reactome database.SUMOylation of DNA damage response and repair proteinsSUMOylation of DNA damage response and repair proteinsThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>SUMOylation of BLM with SUMO2,3SUMOylation of BLM with SUMO2,3This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 105384411nucleoplasmGO0005654UniProt:Q9VGI8BlmReactomehttp://www.reactome.orgDrosophila melanogasterNCBI Taxonomy7227UniProtQ9VGI8Chain Coordinates1EQUAL1417EQUALConverted from EntitySet in ReactomeReactome DB_ID: 105357484UBE2I:SUMO2,UBE2I:SUMO3 [nucleoplasm]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityReactome DB_ID: 105356518UniProt:Q7KNM2lwrUniProtQ7KNM21EQUAL158EQUALReactome DB_ID: 105384471sumoylated lysine (polySUMO2,3 [nucleoplasm]) at 317 (in Homo sapiens)317EQUALsumoylated lysinesumoylated lysine (polySUMO2,3 [nucleoplasm]) at 331 (in Homo sapiens)331EQUALsumoylated lysine (polySUMO2,3 [nucleoplasm]) at 344 (in Homo sapiens)344EQUALsumoylated lysine (polySUMO2,3 [nucleoplasm]) at 347 (in Homo sapiens)347EQUAL1EQUAL1417EQUALPHYSIOL-LEFT-TO-RIGHTACTIVATIONConverted from EntitySet in ReactomeReactome DB_ID: 10535748GO0019789GO molecular functionReactome Database ID Release 7510538168Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10538168Reactome Database ID Release 7510538449Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10538449ReactomeR-DME-45689141Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-4568914.1BLM is SUMOylated at lysine-317, lysine-331, lysine-344, and lysine-347 with SUMO2,3 (Eladad et al. 2005, Zhu et al. 2008, Ouyang et al. 2009, Ouyang et al. 2013, Hendriks et al. 2014). SUMOylation causes BLM to localize to PML bodies (Eladad et al. 2005). SUMOylated BLM recruits RAD51, which directly binds SUMO, and facilitates the substitution of RAD51 for RPA at stalled replication forks (Ouyang et al. 2009, 2013).19956565Pubmed2009SUMO modification regulates BLM and RAD51 interaction at damaged replication forksOuyang, Karen JWoo, Leslie LZhu, JianmeiHuo, DezhengMatunis, Michael JEllis, Nathan APLoS Biol. 7:e100025218708356Pubmed2008Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modificationZhu, JianmeiZhu, ShanshanGuzzo, Catherine MEllis, Nathan ASung, Ki SaChoi, Cheol YongMatunis, Michael JJ. Biol. Chem. 283:29405-1524027577Pubmed2013BLM SUMOylation regulates ssDNA accumulation at stalled replication forksOuyang, Karen JYagle, Mary KMatunis, Michael JEllis, Nathan AFront Genet 4:16715829507Pubmed2005Intra-nuclear trafficking of the BLM helicase to DNA damage-induced foci is regulated by SUMO modificationEladad, SoniaYe, Tian-ZhangHu, PengLeversha, MargaretBeresten, SergeyMatunis, Michael JEllis, Nathan AHum. Mol. Genet. 14:1351-6525218447Pubmed2014Uncovering global SUMOylation signaling networks in a site-specific mannerHendriks, Ivo AD'Souza, Rochelle C JYang, BingVerlaan-de Vries, MattyMann, MatthiasVertegaal, Alfred C ONat. Struct. Mol. Biol. 21:927-36inferred by electronic annotationIEAGOIEACBX4 (Pc2) SUMOylates CETN2 with SUMO2,3CBX4 (Pc2) SUMOylates CETN2 with SUMO2,3This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Converted from EntitySet in ReactomeReactome DB_ID: 105384611Homologues of CETN2 [nucleoplasm]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityCG15158 [nucleoplasm]Dmel\CG17493 [nucleoplasm]UniProtQ8T415UniProtM9PGG8Converted from EntitySet in ReactomeReactome DB_ID: 105357481Reactome DB_ID: 1053565121EQUAL158EQUALConverted from EntitySet in ReactomeReactome DB_ID: 105384691Homologues of SUMO2,3-CETN2 [nucleoplasm]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityDmel\CG17493 [nucleoplasm]CG15158 [nucleoplasm]PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 10535989PRC1 complex [nucleoplasm]PRC1 complexConverted from EntitySet in ReactomeReactome DB_ID: 105359461BMI1,PCGF2 [nucleoplasm]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntitySu(z)2 [nucleoplasm]Psc [nucleoplasm]Psc [nucleoplasm]UniProtP25172UniProtP35820Reactome DB_ID: 105359871UniProt:P26017PcUniProtP260171EQUAL389EQUALReactome DB_ID: 105359801UniProt:Q9VB08SceUniProtQ9VB081EQUAL406EQUALConverted from EntitySet in ReactomeReactome DB_ID: 105359751PHC1,PHC2,PHC3 [nucleoplasm]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntitySamuel [nucleoplasm]ph-p [nucleoplasm]ph-d [nucleoplasm]Samuel [nucleoplasm]ph-d [nucleoplasm]ph-d [nucleoplasm]ph-p [nucleoplasm]UniProtQ9VKL0UniProtP39769UniProtQ9W523Reactome DB_ID: 105359301UniProt:Q9VHA0ScmUniProtQ9VHA01EQUAL660EQUALReactome Database ID Release 7510535989Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10535989ReactomeR-DME-3891141Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-389114.1Reactome Database ID Release 7510535990Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10535990Reactome Database ID Release 7510538471Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10538471ReactomeR-DME-45704631Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-4570463.1CBX4 (Pc2) in the PRC1 complex SUMOylates CETN2 at an unknown residue with SUMO2,3 (Klein and Nigg 2009). SUMOylation of CETN2 enhances its nuclear localization. Interaction with XPC is also required for nuclear localization of CETN2.19706679Pubmed2009SUMO-dependent regulation of centrin-2Klein, Ulf RNigg, EAJ. Cell. Sci. 122:3312-21inferred by electronic annotationIEAGOIEASUMOylation of MDC1 with SUMO2,3SUMOylation of MDC1 with SUMO2,3This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 105385021UniProt:Q9VUB7PtipUniProtQ9VUB71EQUAL2089EQUALConverted from EntitySet in ReactomeReactome DB_ID: 105357481Reactome DB_ID: 105385051sumoylated lysine (polySUMO2,3 [nucleoplasm]) at 1840 (in Homo sapiens)1840EQUAL1EQUAL2089EQUALReactome DB_ID: 1053565121EQUAL158EQUALPHYSIOL-LEFT-TO-RIGHTACTIVATIONConverted from EntitySet in ReactomeReactome DB_ID: 10535748Reactome Database ID Release 7510538507Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10538507ReactomeR-DME-45705531Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-4570553.1MDC1 is SUMOylated at lysine-1840 with SUMO2,3 (Luo et al. 2012, Hendriks et al. 2014, Tammsalu et al. 2014). SUMOylation is required for degradation of MDC1. SUMOylation of MDC1 is required for recruitment of RNF4 (Yin et al. 2012), which is believed to ubiquitinylate MDC1, resulting in degradation of MDC1.24782567Pubmed2014Proteome-wide identification of SUMO2 modification sitesTammsalu, TriinMatic, IvanJaffray, Ellis GIbrahim, Adel F MTatham, Michael HHay, Ronald TSci Signal 7:rs222635276Pubmed2012Sumoylation of MDC1 is important for proper DNA damage responseLuo, KuntianZhang, HaoxingWang, LieweiYuan, JianLou, ZEMBO J. 31:3008-1922661230Pubmed2012SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damageYin, YiliSeifert, AnneChua, Joy ShijiaMaure, Jean-FrançoisGolebiowski, FilipHay, Ronald TGenes Dev. 26:1196-208inferred by electronic annotationIEAGOIEAPIAS4 SUMOylates PARP1 with SUMO2,3PIAS4 SUMOylates PARP1 with SUMO2,3This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 105335461UniProt:P35875ParpUniProtP358752EQUAL1014EQUALConverted from EntitySet in ReactomeReactome DB_ID: 105357482Reactome DB_ID: 105384291sumoylated lysine (polySUMO2,3 [nucleoplasm]) at 203 (in Homo sapiens)203EQUALsumoylated lysine (polySUMO2,3 [nucleoplasm]) at 486 (in Homo sapiens)486EQUAL2EQUAL1014EQUALReactome DB_ID: 1053565141EQUAL158EQUALPHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 10538059UniProt:A1Z7P5Su(var)2-10UniProtA1Z7P52EQUAL510EQUALReactome Database ID Release 7510538408Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10538408Reactome Database ID Release 7510538431Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10538431ReactomeR-DME-45517681Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-4551768.1PIAS4 SUMOylates PARP1 at lysine-203 and lysine-486 with SUMO2,3 in response to heat shock (Martin et al. 2009, Lamoliatte et al. 2013, Hendriks et al. 2014, Tammsalu et al. 2014). PARP1 reciprocally poly(ADP-ribose)ylates PIAS4 (Martin et al. 2009). SUMOylation of PARP1 is required for full activation of the HSP70.1 promoter (Martin et al. 2009).23750026Pubmed2013Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ionsLamoliatte, FredericBonneil, EricDurette, ChantalCaron-Lizotte, OlivierWildemann, DirkZerweck, JohannesWenshuk, HolgerThibault, PierreMol. Cell Proteomics 12:2536-5019779455Pubmed2009PARP-1 transcriptional activity is regulated by sumoylation upon heat shockMartin, NadineSchwamborn, KlausSchreiber, ValérieWerner, AndreasGuillier, ChristelleZhang, Xiang-DongBischof, OliverSeeler, Jacob-SDejean, AnneEMBO J. 28:3534-48inferred by electronic annotationIEAGOIEARANBP2 SUMOylates PML with SUMO2RANBP2 SUMOylates PML with SUMO2Conjugation of SUMO2 to PMLThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Converted from EntitySet in ReactomeReactome DB_ID: 105358411Homologues of PML [nucleoplasm]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityDmel\CG8419 [nucleoplasm]mei-P26 [nucleoplasm]UniProtQ9VLR7UniProtM9PH32Reactome DB_ID: 105357386SUMO2:UBE2I [nucleoplasm]SUMO2:UBE2IReactome DB_ID: 105357331Inter-chain Crosslink via S-(glycyl)-L-cysteine (Cys-Gly) at 93 and 93 (in Homo sapiens)93EQUALS-(glycyl)-L-cysteine (Cys-Gly)ChEBI24411modification1EQUAL158EQUALReactome DB_ID: 105357361UniProt:O97102smt3UniProtO97102Inter-chain Crosslink via S-(glycyl)-L-cysteine (Cys-Gly) at 93 and 93 (in Homo sapiens)93EQUALChEBI23511modification1EQUAL93EQUALReactome Database ID Release 7510535738Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10535738ReactomeR-DME-29937781Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-2993778.1Converted from EntitySet in ReactomeReactome DB_ID: 105358531Homologues of SUMO2-K65,K160,K490-PML [nucleoplasm]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntitymei-P26 [nucleoplasm]Dmel\CG8419 [nucleoplasm]Reactome DB_ID: 1053565161EQUAL158EQUALPHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 10496750nuclear envelopeGO0005635Nuclear Pore Complex (NPC) [nuclear envelope]Nuclear Pore Complex (NPC)Reactome DB_ID: 1049664832cytosolGO0005829UniProt:Q9GYU8mboUniProtQ9GYU81EQUAL741EQUALReactome DB_ID: 1049668532UniProt:Q9VCG4Ndc1UniProtQ9VCG41EQUAL674EQUALReactome DB_ID: 1049666316UniProt:Q7K2X8Nup44AUniProtQ7K2X81EQUAL360EQUALReactome DB_ID: 1049661216UniProt:A1Z6H7Gp210UniProtA1Z6H727EQUAL1887EQUALReactome DB_ID: 104966228UniProt:Q9VXE6Nup153UniProtQ9VXE62EQUAL1475EQUALReactome DB_ID: 104966388Ghost homologue of RANBP2 [cytosol]Ghost homologue of RANBP2Reactome DB_ID: 1049665348UniProt:Q9W2E7Rae1UniProtQ9W2E71EQUAL368EQUALReactome DB_ID: 1049661716UniProt:Q9I7N3Dmel\CG18789UniProtQ9I7N31EQUAL423EQUALReactome DB_ID: 1049662416Ghost homologue of NUP188 [nuclear envelope]Ghost homologue of NUP188Reactome DB_ID: 1049664332UniProt:Q7K0D8Nup50UniProtQ7K0D81EQUAL468EQUALReactome DB_ID: 1049674832Nup93 complex [nuclear envelope]Nup93 complexReactome DB_ID: 104967461UniProt:Q8IQV9Nup205UniProtQ8IQV92EQUAL2012EQUALReactome DB_ID: 104967311UniProt:Q9V463Nup154UniProtQ9V4631EQUAL1391EQUALReactome DB_ID: 104967361UniProt:Q9VFE7Nup93-2UniProtQ9VFE71EQUAL819EQUALReactome DB_ID: 104967411UniProt:Q9VWS2Nup35UniProtQ9VWS21EQUAL326EQUALReactome Database ID Release 7510496748Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10496748ReactomeR-DME-96341831Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-9634183.1Converted from EntitySet in ReactomeReactome DB_ID: 104966368Homologues of NUP214 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityDmel\CG14712 [cytosol]Nup214 [cytosol]UniProtQ9VGL0UniProtQ9W1X4Reactome DB_ID: 104966688UniProt:Q9VCH5Nup98-96UniProtQ9VCH51EQUAL863EQUALReactome DB_ID: 1049660232Nup62 Complex [nuclear envelope]Nup62 ComplexReactome DB_ID: 104966001UniProt:Q9VDV3Nup58UniProtQ9VDV31EQUAL599EQUALReactome DB_ID: 104965901UniProt:Q7JXF5Nup62UniProtQ7JXF51EQUAL522EQUALReactome DB_ID: 104965951UniProt:Q9V6B9Nup54UniProtQ9V6B91EQUAL507EQUALReactome Database ID Release 7510496602Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10496602ReactomeR-DME-1577121Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-157712.1Reactome DB_ID: 104966078UniProt:Q9W351AladinUniProtQ9W3511EQUAL546EQUALReactome DB_ID: 1049665816UniProt:A1Z8P9MtorUniProtA1Z8P92EQUAL2363EQUALConverted from EntitySet in ReactomeReactome DB_ID: 1049668016POM121 [nuclear envelope]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityNup214 [nuclear envelope]Dmel\CG14712 [nuclear envelope]Nup214 [nuclear envelope]Reactome DB_ID: 1049672632Nup107-160 complex [cytosol]Nup107-160 complexReactome DB_ID: 104966951UniProt:Q9VCW3Nup133UniProtQ9VCW31EQUAL1156EQUALReactome DB_ID: 1049670711EQUAL880EQUALReactome DB_ID: 104967121UniProt:Q9VBU8Nup37UniProtQ9VBU81EQUAL326EQUALReactome DB_ID: 104967221UniProt:Q9V3J4Sec13UniProtQ9V3J42EQUAL322EQUALReactome DB_ID: 104967171UniProt:Q9VE85Nup43UniProtQ9VE851EQUAL380EQUALReactome DB_ID: 104967001UniProt:Q9VKJ3Nup160UniProtQ9VKJ31EQUAL1436EQUALReactome DB_ID: 104967051UniProt:A1YK02Nup75UniProtA1YK021EQUAL656EQUALReactome DB_ID: 104966901UniProt:Q9V466Nup107UniProtQ9V4661EQUAL925EQUALReactome DB_ID: 1049672411EQUAL360EQUALReactome Database ID Release 7510496726Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10496726ReactomeR-DME-3778831Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-377883.1Reactome Database ID Release 7510496750Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10496750ReactomeR-DME-1576891Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-157689.1Reactome Database ID Release 7510535854Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10535854Reactome Database ID Release 7510535856Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10535856ReactomeR-DME-30004111Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-3000411.1RANBP2 of the nuclear pore complex SUMOylates PML with SUMO2 at lysine-65, lysine-160, and lysine-490 (Kamitani et al. 1998, Tatham et al. 2005). RANBP2 contains both a binding site for SUMO1 and a binding site for UBE2I (Tatham et al. 2005). The binding site for UBE2I participates in SUMOylation of PML with SUMO2. SUMO2 colocalizes significantly with PML bodies (Vertegaal et al. 2004).15608651Pubmed2005Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selectionTatham, Michael HKim, SuhkmannJaffray, EllisSong, JingChen, YuanHay, Ronald TNat. Struct. Mol. Biol. 12:67-7415175327Pubmed2004A proteomic study of SUMO-2 target proteinsVertegaal, Alfred C OOgg, Stephen CJaffray, EllisRodriguez, Manuel SHay, Ronald TAndersen, JSMann, MatthiasLamond, Angus IJ. Biol. Chem. 279:33791-89452416Pubmed1998Covalent modification of PML by the sentrin family of ubiquitin-like proteinsKamitani, TNguyen, H PKito, KFukuda-Kamitani, TYeh, E TJ. Biol. Chem. 273:3117-20inferred by electronic annotationIEAGOIEASUMOylation of PML with SUMO3SUMOylation of PML with SUMO3Conjugation of SUMO3 to PMLThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Converted from EntitySet in ReactomeReactome DB_ID: 105358411Reactome DB_ID: 105357466SUMO3:UBE2I [nucleoplasm]SUMO3:UBE2IReactome DB_ID: 105357411Inter-chain Crosslink via S-(glycyl)-L-cysteine (Cys-Gly) at 93 and 92 (in Homo sapiens)93EQUAL1EQUAL158EQUALReactome DB_ID: 105357441Inter-chain Crosslink via S-(glycyl)-L-cysteine (Cys-Gly) at 92 and 93 (in Homo sapiens)92EQUAL1EQUAL92EQUALReactome Database ID Release 7510535746Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10535746ReactomeR-DME-29937821Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-2993782.1Reactome DB_ID: 1053565161EQUAL158EQUALConverted from EntitySet in ReactomeReactome DB_ID: 105358681Homologues of SUMO3-K65,K160,K490-PML [nucleoplasm]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityDmel\CG8419 [nucleoplasm]mei-P26 [nucleoplasm]PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 10535746Reactome Database ID Release 7510535869Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10535869Reactome Database ID Release 7510535871Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10535871ReactomeR-DME-30004331Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-3000433.1PML is observed to be SUMOylated with SUMO3 at lysine-65, lysine-160, and lysine-490 (Kamitani et al. 1998). SUMO3 is almost identical with SUMO2 therefore the same E3 ligase (RANBP2) that SUMOylate PML with SUMO2 may also be active with SUMO3, but this has not been proven. PML colocalizes with SUMO3 in nuclear bodies and disruption of SUMO3 expression reduces the number of nuclear bodies (Fu et al. 2005).15940266Pubmed2005Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3Fu, ChuanhaiAhmed, KashifDing, HushengDing, XiaLan, JianpingYang, ZhihongMiao, YongZhu, YuanyuanShi, YunyuZhu, JingdeHuang, HeYao, XOncogene 24:5401-1316608850Pubmed2006Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3Gong, LiminYeh, Edward T HJ. Biol. Chem. 281:15869-77inferred by electronic annotationIEAGOIEASUMOylation of TDG with SUMO2,3SUMOylation of TDG with SUMO2,3This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 104982291UniProt:Q9V4D8Thd1UniProtQ9V4D81EQUAL410EQUALConverted from EntitySet in ReactomeReactome DB_ID: 105357481Reactome DB_ID: 105384231sumoylated lysine (polySUMO2,3 [nucleoplasm]) at 330 (in Homo sapiens)330EQUAL1EQUAL410EQUALReactome DB_ID: 1053565121EQUAL158EQUALPHYSIOL-LEFT-TO-RIGHTACTIVATIONConverted from EntitySet in ReactomeReactome DB_ID: 10535748Reactome Database ID Release 7510538425Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10538425ReactomeR-DME-45517381Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-4551738.1TDG is SUMOylated at lysine-330 with SUMO2,3 by UBE2I and perhaps another E3 ligase (Hardeland et al. 2002, Baba et al. 2006, Hendriks et al. 2014, Tammsalu et al. 2014). SUMOylation increases turnover of TDG with G:U substrate and abolishes activity with G:T substrate (Hardeland et al. 2002).11889051Pubmed2002Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnoverHardeland, UlrikeSteinacher, RolandJiricny, JosefSchär, PrimoEMBO J. 21:1456-6416626738Pubmed2006Crystal structure of SUMO-3-modified thymine-DNA glycosylaseBaba, DaichiMaita, NobuoJee, Jun-GooUchimura, YasuhiroSaitoh, HisatoSugasawa, KaoruHanaoka, FumioTochio, HidehitoHiroaki, HidekazuShirakawa, MasahiroJ. Mol. Biol. 359:137-47inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510569235Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10569235ReactomeR-DME-31082141Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DME-3108214.1Several factors that participate in DNA damage response and repair are SUMOylated (reviewed in Dou et al. 2011, Bekker-Jensen and Mailand 2011, Ulrich 2012, Psakhye and Jentsch 2012, Bologna and Ferrari 2013, Flotho and Melchior 2013, Jackson and Durocher 2013). SUMOylation can alter enzymatic activity and protein stability or it can serve to recruit additional factors. For example, SUMOylation of Thymine DNA glycosylase (TDG) causes TDG to lose affinity for its product, an abasic site opposite a G residue, and thus increases turnover of the enzyme. During repair of double-strand breaks SUMO1, SUMO2, SUMO3, and the SUMO E3 ligases PIAS1 and PIAS4 accumulate at double-strand breaks where BRCA1, HERC1, RNF168, MDC1, and TP53BP1 are SUMOylated. SUMOylation of BRCA1 may increase its ubiquitin ligase activity while SUMOylation of MDC1 and HERC2 appears to play a role in recruitment of proteins such as RNF4 and RNF8 to double strand breaks. Similarly SUMOylation of RPA1 (RPA70) recruits RAD51 in the homologous recombination pathway.21664912Pubmed2011The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaksBekker-Jensen, SimonMailand, NielsFEBS Lett. 585:2914-923746258Pubmed2013Sumoylation: a regulatory protein modification in health and diseaseFlotho, AnnetteMelchior, FraukeAnnu. Rev. Biochem. 82:357-8521896653Pubmed2011Shared and unique properties of ubiquitin and SUMO interaction networks in DNA repairvan Wijk, Sjoerd J LMüller, StefanDikic, IvanGenes Dev. 25:1763-922018829Pubmed2012SUMO playing tag with ubiquitinPraefcke, Gerrit J KHofmann, KayDohmen, R JürgenTrends Biochem. Sci. 37:23-3122357966Pubmed2012Ubiquitin and SUMO in DNA repair at a glanceUlrich, Helle DJ. Cell. Sci. 125:249-5423416108Pubmed2013Regulation of DNA damage responses by ubiquitin and SUMOJackson, Stephen PDurocher, DanielMol. Cell 49:795-80721486569Pubmed2011SUMOylation and de-SUMOylation in response to DNA damageDou, HongHuang, ChaoVan Nguyen, ThangLu, Long-ShengYeh, Edward T HFEBS Lett. 585:2891-623781231Pubmed2013It takes two to tango: Ubiquitin and SUMO in the DNA damage responseBologna, SerenaFerrari, StefanoFront Genet 4:10624926426Pubmed2012Sumoylation and the DNA damage responseCremona, Catherine ASarangi, PrabhaZhao, XiaolanBiomolecules 2:376-8823122649Pubmed2012Protein group modification and synergy in the SUMO pathway as exemplified in DNA repairPsakhye, IvanJentsch, StefanCell 151:807-20inferred by electronic annotationIEAGOIEA