BioPAX pathway converted from "DNA polymerase epsilon binds at the origin" in the Reactome database.DNA polymerase epsilon binds at the originDNA polymerase epsilon binds at the originThis 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: 97077321nucleoplasmGO0005654DNA polymerase epsilon [nucleoplasm]DNA polymerase epsilonReactome DB_ID: 97077181UniProt:Q9WVF7PoleReactomehttp://www.reactome.orgMus musculusNCBI Taxonomy10090UniProtQ9WVF7Chain Coordinates1EQUAL2286EQUALReactome DB_ID: 97077221UniProt:O54956Pole2UniProtO549561EQUAL527EQUALReactome DB_ID: 97077301UniProt:Q9CQ36Pole4UniProtQ9CQ362EQUAL117EQUALReactome DB_ID: 97077261UniProt:Q9JKP7Pole3UniProtQ9JKP72EQUAL147EQUALReactome Database ID Release 759707732Database 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=9707732ReactomeR-MMU-684831Reactome 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-MMU-68483.1Reactome DB_ID: 684191origin of replication [nucleoplasm]origin of replicationARSautonomously replicating sequenceoriginReactome DB_ID: 97077341DNA polymerase epsilon:origin complex [nucleoplasm]DNA polymerase epsilon:origin complexReactome DB_ID: 97077321Reactome DB_ID: 684191Reactome Database ID Release 759707734Database 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=9707734ReactomeR-MMU-684851Reactome 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-MMU-68485.1Reactome Database ID Release 759707868Database 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=9707868ReactomeR-MMU-689601Reactome 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-MMU-68960.1At the beginning of this reaction, 1 molecule of 'origin of replication', and 1 molecule of 'DNA polymerase epsilon' are present. At the end of this reaction, 1 molecule of 'DNA polymerase epsilon:origin complex' is present.<br><br> <br>12045100Pubmed2002DNA replication in eukaryotic cells.Bell, SPDutta, AAnnu Rev Biochem 71:333-74inferred by electronic annotationIEAGOIEAACTIVATIONReactome Database ID Release 759707788Database 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=9707788Reactome DB_ID: 9707785CDK:DDK:MCM10:active pre-replicative complex:CDC45:RPA1-4 [nucleoplasm]CDK:DDK:MCM10:active pre-replicative complex:CDC45:RPA1-4Reactome DB_ID: 97077501RPA1-4 [nucleoplasm]RPA1-4Reactome DB_ID: 97077471Ghost homologue of RPA4 [nucleoplasm]Ghost homologue of RPA4Reactome DB_ID: 9124661UniProt:Q9CQ71 Rpa3Rpa3Rpa3FUNCTION As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER), probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA.SUBUNIT Component of the canonical replication protein A complex (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3. Also component of the aRPA, the alternative replication protein A complex, a trimeric complex similar to the replication protein A complex/RPA but where RPA1 and RPA3 are associated with RPA4 instead of RPA2 (By similarity).PTM Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination.SIMILARITY Belongs to the replication factor A protein 3 family.UniProtQ9CQ711EQUAL121EQUALReactome DB_ID: 9124331UniProt:Q62193 Rpa2Rpa2Rpa34Rpa2FUNCTION As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.SUBUNIT Component of the replication protein A complex (RPA/RP-A), a heterotrimeric complex composed of RPA1, RPA2 and RPA3. Interacts with PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it ubiquitinates the replication protein A complex (RPA) (By similarity). Interacts with SERTAD3. Interacts with TIPIN (PubMed:17141802). Interacts with TIMELESS (PubMed:17141802). Interacts with PPP4R2; the interaction is direct, DNA damage-dependent and mediates the recruitment of the PP4 catalytic subunit PPP4C (By similarity). Interacts (hyperphosphorylated) with RAD51 (By similarity). Interacts with SMARCAL1; the interaction is direct and mediates the recruitment to the RPA complex of SMARCAL1 (By similarity). Interacts with RAD52 and XPA; those interactions are direct and associate RAD52 and XPA to the RPA complex (By similarity). Interacts with FBH1 (By similarity). Interacts with ETAA1; the interaction is direct and promotes ETAA1 recruitment at stalled replication forks (By similarity). Interacts with DDI2 (By similarity).PTM Differentially phosphorylated throughout the cell cycle, becoming phosphorylated at the G1-S transition and dephosphorylated in late mitosis. Mainly phosphorylated at Ser-23 and Ser-29, by cyclin A-CDK2 and cyclin B-CDK1, respectively during DNA replication and mitosis. Dephosphorylation may require the serine/threonine-protein phosphatase 4. Phosphorylation at Ser-23 and Ser-29 is a prerequisite for further phosphorylation. Becomes hyperphosphorylated on additional residues including Ser-4, Ser-8, Thr-21 and Ser-33 in response to DNA damage. Hyperphosphorylation is mediated by ATM, ATR and PRKDC. Primarily recruited to DNA repair nuclear foci as a hypophosphorylated form it undergoes subsequent hyperphosphorylation, catalyzed by ATR. Hyperphosphorylation is required for RAD51 recruitment to chromatin and efficient DNA repair. Phosphorylation at Thr-21 depends upon RFWD3 presence.PTM DNA damage-induced 'Lys-63'-linked polyubiquitination by PRPF19 mediates ATRIP recruitment to the RPA complex at sites of DNA damage and activation of ATR. Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination.SIMILARITY Belongs to the replication factor A protein 2 family.UniProtQ621931EQUAL270EQUALReactome DB_ID: 97077441UniProt:Q8VEE4 Rpa1Rpa1Rpa1FUNCTION As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.SUBUNIT Component of the canonical replication protein A complex (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3. The DNA-binding activity may reside exclusively on the RPA1 subunit. Interacts with PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it ubiquitinates the replication protein A complex (RPA). Interacts with RIPK1. Interacts with the polymerase alpha subunit POLA1/p180; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp. Interacts with RAD51 and SENP6 to regulate DNA repair. Interacts with HELB; this interaction promotes HELB recruitment to chromatin following DNA damage. Interacts with PRIMPOL; leading to recruit PRIMPOL on chromatin and stimulate its DNA primase activity. Interacts with XPA; the interaction is direct and associates XPA with the RPA complex. Interacts with ETAA1; the interaction is direct and promotes ETAA1 recruitment at stalled replication forks. Interacts with RPA1; this interaction associates HROB with the RPA complex (PubMed:31467087).PTM DNA damage-induced 'Lys-63'-linked polyubiquitination by PRPF19 mediates ATRIP recruitment to the RPA complex at sites of DNA damage and activation of ATR. Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination.PTM Sumoylated on lysine residues Lys-458 and Lys-586, with Lys-458 being the major site. Sumoylation promotes recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. Desumoylated by SENP6 (By similarity).SIMILARITY Belongs to the replication factor A protein 1 family.UniProtQ8VEE42EQUAL616EQUALReactome Database ID Release 759707750Database 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=9707750ReactomeR-MMU-685671Reactome 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-MMU-68567.1Reactome DB_ID: 97077831CDK:DDK:MCM10:active pre-replicative complex:CDC45 [nucleoplasm]CDK:DDK:MCM10:active pre-replicative complex:CDC45Reactome DB_ID: 97077811CDK:DDK:MCM10:active pre-replicative complex [nucleoplasm]CDK:DDK:MCM10:active pre-replicative complexReactome DB_ID: 97077711DDK [nucleoplasm]DDKReactome DB_ID: 97077651UniProt:Q9Z0H0Cdc7UniProtQ9Z0H01EQUAL574EQUALReactome DB_ID: 97077691UniProt:Q9QZ41Dbf4UniProtQ9QZ411EQUAL674EQUALReactome Database ID Release 759707771Database 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=9707771ReactomeR-MMU-683881Reactome 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-MMU-68388.1Reactome DB_ID: 97077791MCM10:active pre-replicative complex [nucleoplasm]MCM10:active pre-replicative complexReactome DB_ID: 97077751UniProt:Q0VBD2Mcm10UniProtQ0VBD21EQUAL875EQUALReactome DB_ID: 97077771active pre-replicative complex [nucleoplasm]active pre-replicative complexReactome DB_ID: 97076901MCM2-7 [nucleoplasm]MCM2-7Reactome DB_ID: 97076761UniProt:P49718Mcm5UniProtP497181EQUAL734EQUALReactome DB_ID: 97076841UniProt:Q61881Mcm7UniProtQ618812EQUAL719EQUALReactome DB_ID: 97076681UniProt:P25206Mcm3UniProtP252062EQUAL808EQUALReactome DB_ID: 97076881UniProt:P97310Mcm2UniProtP973102EQUAL904EQUALReactome DB_ID: 97076801UniProt:P97311Mcm6UniProtP973111EQUAL821EQUALReactome DB_ID: 97076721UniProt:P49717Mcm4UniProtP497172EQUAL863EQUALReactome Database ID Release 759707690Database 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=9707690ReactomeR-MMU-685581Reactome 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-MMU-68558.1Reactome DB_ID: 97074881CDC6:ORC:origin complex [nucleoplasm]CDC6:ORC:origin complexReactome DB_ID: 97074861ORC:origin of replication [nucleoplasm]ORC:origin of replicationReactome DB_ID: 97074161UniProt:Q9JK30Orc3UniProtQ9JK301EQUAL711EQUALReactome DB_ID: 97074301UniProt:Q9WUV0Orc5UniProtQ9WUV01EQUAL435EQUALReactome DB_ID: 97074841Orc2 associated with MCM8 [nucleoplasm]Orc2 associated with MCM8Reactome DB_ID: 97074821UniProt:Q9CWV1Mcm8UniProtQ9CWV11EQUAL840EQUALReactome DB_ID: 97074201UniProt:Q60862Orc2UniProtQ608621EQUAL577EQUALReactome Database ID Release 759707484Database 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=9707484ReactomeR-MMU-1769701Reactome 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-MMU-176970.1Reactome DB_ID: 97074461UniProt:Q9Z1N2Orc1UniProtQ9Z1N21EQUAL861EQUALReactome DB_ID: 97074381UniProt:O88708Orc4UniProtO887081EQUAL436EQUALReactome DB_ID: 97074541UniProt:Q9WUJ8Orc6UniProtQ9WUJ81EQUAL252EQUALReactome DB_ID: 684191Reactome Database ID Release 759707486Database 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=9707486ReactomeR-MMU-685401Reactome 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-MMU-68540.1Reactome DB_ID: 97074621UniProt:O89033Cdc6UniProtO890331EQUAL560EQUALReactome Database ID Release 759707488Database 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=9707488ReactomeR-MMU-685431Reactome 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-MMU-68543.1Reactome Database ID Release 759707777Database 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=9707777ReactomeR-MMU-1565621Reactome 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-MMU-156562.1Reactome Database ID Release 759707779Database 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=9707779ReactomeR-MMU-1565641Reactome 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-MMU-156564.1Reactome DB_ID: 97077611CDK [nucleoplasm]CDKReactome DB_ID: 97077561Ghost homologue of cyclin [nucleoplasm]Ghost homologue of cyclinReactome DB_ID: 97077591UniProt:P97377 Cdk2Cdk2Cdkn2Cdk2FUNCTION Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization. Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability (PubMed:23853094). Phosphorylates CDK2AP2 (By similarity). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (By similarity).ACTIVITY REGULATION Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-160 activates it. Stimulated by MYC. Inactivated by CDKN1A (p21) (By similarity).SUBUNIT Found in a complex with CABLES1, CCNA1 and CCNE1. Interacts with CABLES1 (PubMed:11585773). Interacts with UHRF2. Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts with the Speedy/Ringo proteins SPDYA and SPDYC. Interaction with SPDYA promotes kinase activation via a conformation change that alleviates obstruction of the substrate-binding cleft by the T-loop. Found in a complex with both SPDYA and CDKN1B/KIP1. Binds to RB1 and CDK7. Binding to CDKN1A (p21) leads to CDK2/cyclin E inactivation at the G1-S phase DNA damage checkpoint, thereby arresting cells at the G1-S transition during DNA repair. Associated with PTPN6 and beta-catenin/CTNNB1. Interacts with CACUL1. May interact with CEP63. Interacts with ANKRD17 (By similarity). Interacts with CEBPA (when phosphorylated) (PubMed:15107404). Forms a ternary complex with CCNA2 and CDKN1B; CDKN1B inhibits the kinase activity of CDK2 through conformational rearrangements. Interacts with cyclins A, B1, B3, D, or E. Interacts with CDK2AP2 (By similarity).PTM Phosphorylated at Thr-160 by CDK7 in a CAK complex. Phosphorylation at Thr-160 promotes kinase activity, whereas phosphorylation at Tyr-15 by WEE1 reduces slightly kinase activity. Phosphorylated on Thr-14 and Tyr-15 during S and G2 phases before being dephosphorylated by CDC25A.PTM Nitrosylated after treatment with nitric oxide (DETA-NO).DISRUPTION PHENOTYPE Reduced body size and impaired neural progenitor cell proliferation. Sterility due to defective meiosis; no effect on mitotic cells. Premature translocation of CDK1 from the cytoplasm to the nucleus compensating CDK2 loss. Prolonged and impaired DNA repair activity upon DNA damage by gamma-irradiation.SIMILARITY Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.UniProtP973771EQUAL298EQUALReactome Database ID Release 759707761Database 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=9707761ReactomeR-MMU-683801Reactome 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-MMU-68380.1Reactome Database ID Release 759707781Database 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=9707781ReactomeR-MMU-685611Reactome 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-MMU-68561.1Reactome DB_ID: 97077541UniProt:Q9Z1X9Cdc45UniProtQ9Z1X91EQUAL566EQUALReactome Database ID Release 759707783Database 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=9707783ReactomeR-MMU-685641Reactome 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-MMU-68564.1Reactome Database ID Release 759707785Database 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=9707785ReactomeR-MMU-685681Reactome 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-MMU-68568.1