Mitotic G2-G2/M phases (Homo sapiens)

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ArcPathVisio Brace Ellipse EndoplasmicReticulum GolgiApparatus HexagonPathVisio MimDegradation Mitochondria Octagon PentagonPathVisio Rectangle RoundedRectangle SarcoplasmicReticulum TriangleEquilateralEast TrianglePathVisio none cytosolnucleoplasmGolgi membraneCCNACDK1CCNA:CDK1ATPADPCCNA:p-T14-CDK1PKMYT1CCNA:p-T14-CDK1ATPCCNA:p-T14,T161-CDK1ADPCAKATPADPCCNA:p-T14,Y15,T161-CDK1WEE1H2OCCNA:p-T161-CDK1PiCDC25CCNBCCNB:CDK1ATPADPCCNB:p-T14-CDK1cytoplasmic CyclinB1:Cdc2 complexesnuclear CyclinB1:Cdc2 complexesATPCCNB1:p-T14-CDK1CCNB1:p-T14,T161-CDK1ADPCCNB1:p-T14,Y15,T161-CDK1CyclinB1:phospho-Cdc2(Thr161, Thr 14, Tyr15)XPO1CDC25BCDC25BH2OCCNB1:p-T161-CDK1PiCdc25ATPPhospho-CyclinB1(CRS):phospho-Cdc2(Thr 161)ADPCRS kinasephospho-cyclinB1(CRS):phosph-Cdc2(Thr 161)phospho-CyclinB1(CRS):phospho-Cdc2 (Thr 161)Cdc25H2OCCNB1:p-T161-CDK1nuclear CyclinB1:Cdc2 substratesATPADPphosphorylatednuclear CyclinB1:Cdc2 substratesactive nuclearCyclin B1:Cdc2complexesH2OCyclinB2:phospho-Cdc2(Thr14, Thr 161)PiCCNB2:p-T161-CDK1G2/M transitionproteinATPphospho-G2/Mtransition proteinADPp-S53-WEE1PLK1CDC25Cp-S198-CDC25CPKMYT1p-PKMYT1CDK11p58centrosomeCentrosomescontainingrecruited CDK11p58PLK1Centrosomeassociated Plk1NUMA1ATPADPp-NUMA1NuMA homodimercentrosome-nucleatedmicrotubulescentrosome-associated NuMANuMA-boundmicrotubulesgamma-tubulincomplexMature centrosomesenriched ingamma-TURCcomplexesATPCCNA:p-T160-CDK2:E2F1/E2F3CCNA:p-T160-CDK2:p-E2F1/p-E2F3ADPphospho-G2/Mtransition proteinCCNA1:p-T161-CDK1CCNA2:p-T161-CDK1Cyclin A1:Cdk2phosphorylated G2/Mtransition proteinADPCyclin A2:Cdk2phosphorylated G2/Mtransition proteinADPG2/M transitionproteinsATPG2/M transitionproteinsATPCEP250cNAP-1 depletedcentrosomeATPADPcentrosomecontainingphosphorylated NlpNlp-depletedcentrosomep-NINLCDC25CE2F1/E2F3CCNA:p-T160-CDK2ATPADPCentrosome:AURKAAJUBACentrosome:AURKA:AJUBAATPCentrosome:p-T288-AURKAp-S-AJUBAADPCentrosome:p-T288-AURKA:p-S252-BORA:PLK1ATPp-S252-BORA:p-T210-PLK1ADPATPp-S252,S497,T501-BORAp-T210-PLK1ADPSCF-beta-TrCp1,2p-S252,S497,T501-BORA:SCF-beta-TrCp1/2UbUb-p-S252,S497,T501-BORAOPTN:RAB8A:GTPATPRAB8A:GTPp-S177-OPTNADPBORAp-S177-OPTNp-T210-PLK1PhosphorylatedMyosin PhosphataseH2OPLK1PiATPADPp-S252-BORACCNB:p-T161-CDK1FOXM1p-T611-FOXM1p-CDK1/2:CCNA/p-T161-CDK1:CCNBATPADPp-T611-FOXM1:p-T210-PLK1ATPp-T611,S730,S739-FOXM1ADPH2OPP2A-PPP2R2APiCDC25A GeneEP300p-T611,S730,S739-FOXM1:EP300:CDC25A GeneCDC25AMYBL2PLK1 GeneMuvB complexp-T611,S730,S739-FOXM1:MuvB:MYBL2:PLK1 GeneCCNB1 Genep-T611,S730,S739-FOXM1:MuvB:MYBL2:CCNB1 GeneCCNB1CCNB2 Genep-T611,S730,S739-FOXM1:MuvB:MYBL2:CCNB2 GeneCCNB2CENPF Genep-T611,S730,S739-FOXM1:CENPF GeneCENPFCDK1p-T14-CDK1p-T14-CDK1p-T14,T161-CDK1CDK7CCNHMNAT1p-T14,Y15,T161-CDK1p-T161-CDK1CCNB1CCNB2CDK1p-T14-CDK1CCNB1CCNB2p-T14-CDK1CCNB1p-T14,Y15,T161-CDK1p-T161-CDK1p-4S-CCNB1CCNB1p-T14-CDK1p-T14,Y15,T161-CDK1p-4S-CCNB1p-T161-CDK1CCNB1p-T14-CDK1CCNB1p-T14,T161-CDK1CCNB1p-T14,Y15,T161-CDK1CCNB1p-T14,Y15,T161-CDK1CCNB1p-T161-CDK1p-4S-CCNB1p-T161-CDK1p-T161-CDK1p-4S-CCNB1p-T161-CDK1p-4S-CCNB1CCNB1p-T161-CDK1CCNB2p-T14,T161-CDK1CCNB2p-T161-CDK1NEDD1TUBG1CKAP5CLASP1HSP90AA1DYNC1I2PLK1PPP2R1ANEK2TUBA1ATUBA4ATUBB4BTUBB4ACSNK1DCSNK1EPAFAH1B1PRKAR2BPRKACANDE1CDK1MAPRE1YWHAECETN2PCNTSFI1AKAP9CDK5RAP2DYNC1H1CNTRLPCM1CEP250CENPJDCTN1-2PLK4ODF2TUBBDCTN3ACTR1ADCTN2YWHAGALMS1CEP192CEP290CEP164CEP152AZI1OFD1CCP110CEP135CEP78CEP76SDCCAG8CEP72CEP70CEP57CEP63FGFR1OPCEP41HAUS2SSNA1NINLDYNLL1NEDD1TUBG1CKAP5CLASP1HSP90AA1DYNC1I2PLK1PPP2R1ANEK2TUBA1ATUBA4ATUBB4BTUBB4ACSNK1DCSNK1EPAFAH1B1PRKAR2BPRKACANDE1CDK1MAPRE1YWHAECETN2PCNTSFI1AKAP9CDK5RAP2DYNC1H1CNTRLPCM1CEP250CENPJDCTN1-2PLK4ODF2TUBBDCTN3ACTR1ADCTN2YWHAGALMS1CEP192CEP290CEP164CEP152AZI1OFD1CCP110CEP135CEP78CEP76SDCCAG8CEP72CEP70CEP57CEP63FGFR1OPCEP41HAUS2SSNA1NINLDYNLL1PLK1NEDD1TUBG1CKAP5CLASP1HSP90AA1DYNC1I2PPP2R1ANEK2TUBA1ATUBA4ATUBB4BTUBB4ACSNK1DCSNK1EPAFAH1B1PRKAR2BPRKACANDE1CDK1MAPRE1YWHAECETN2PCNTSFI1AKAP9CDK5RAP2DYNC1H1CNTRLPCM1CEP250CENPJDCTN1-2PLK4ODF2TUBBDCTN3ACTR1ADCTN2YWHAGALMS1CEP192CEP290CEP164CEP152AZI1OFD1CCP110CEP135CEP78CEP76SDCCAG8CEP72CEP70CEP57CEP63FGFR1OPCEP41HAUS2SSNA1NINLDYNLL1p-NUMA1TUBGCP4TUBGCP5TUBGCP6NEDD1TUBG1TUBG2TUBGCP2TUBGCP3p-NUMA1TUBGCP4TUBGCP5TUBGCP6NEDD1TUBG1TUBG2TUBGCP2TUBGCP3TUBGCP4TUBGCP5TUBGCP6NEDD1TUBG1TUBG2TUBGCP2TUBGCP3p-NUMA1TUBGCP4TUBGCP5TUBGCP6NEDD1TUBG1TUBG2TUBGCP2TUBGCP3NEDD1TUBG1CKAP5CLASP1HSP90AA1DYNC1I2PLK1PPP2R1ANEK2TUBA1ATUBA4ATUBB4BTUBB4ACSNK1DCSNK1EPAFAH1B1PRKAR2BPRKACANDE1CDK1MAPRE1YWHAECETN2PCNTSFI1AKAP9CDK5RAP2DYNC1H1CNTRLPCM1CEP250CENPJDCTN1-2PLK4ODF2TUBBDCTN3ACTR1ADCTN2YWHAGALMS1CEP192CEP290CEP164CEP152AZI1OFD1CCP110CEP135CEP78CEP76SDCCAG8CEP72CEP70CEP57CEP63FGFR1OPCEP41HAUS2SSNA1NINLDYNLL1TUBGCP4TUBGCP5TUBGCP6TUBG2TUBGCP2TUBGCP3E2F1E2F3p-T160-CDK2p-T160-CDK2p-E2F1p-E2F3CCNA1p-T161-CDK1CCNA2p-T161-CDK1NEDD1TUBG1CKAP5CLASP1HSP90AA1DYNC1I2PLK1PPP2R1ANEK2TUBA1ATUBA4ATUBB4BTUBB4ACSNK1DCSNK1EPAFAH1B1PRKAR2BPRKACANDE1CDK1MAPRE1YWHAECETN2PCNTSFI1AKAP9CDK5RAP2DYNC1H1CNTRLPCM1CENPJDCTN1-2PLK4ODF2TUBBDCTN3ACTR1ADCTN2YWHAGALMS1CEP192CEP290CEP164CEP152AZI1OFD1CCP110CEP135CEP78CEP76SDCCAG8CEP72CEP70CEP57CEP63FGFR1OPCEP41HAUS2SSNA1NINLDYNLL1NEDD1TUBG1CKAP5CLASP1HSP90AA1DYNC1I2PLK1PPP2R1ANEK2TUBA1ATUBA4ATUBB4BTUBB4ACSNK1DCSNK1EPAFAH1B1PRKAR2BPRKACANDE1CDK1MAPRE1YWHAECETN2PCNTSFI1AKAP9CDK5RAP2DYNC1H1CNTRLPCM1CEP250CENPJDCTN1-2PLK4ODF2TUBBDCTN3ACTR1ADCTN2YWHAGALMS1CEP192CEP290CEP164CEP152AZI1OFD1CCP110CEP135CEP78CEP76SDCCAG8CEP72CEP70CEP57CEP63FGFR1OPCEP41HAUS2SSNA1p-NINLDYNLL1NEDD1TUBG1CKAP5CLASP1HSP90AA1DYNC1I2PLK1PPP2R1ANEK2TUBA1ATUBA4ATUBB4BTUBB4ACSNK1DCSNK1EPAFAH1B1PRKAR2BPRKACANDE1CDK1MAPRE1YWHAECETN2PCNTSFI1AKAP9CDK5RAP2DYNC1H1CNTRLPCM1CEP250CENPJDCTN1-2PLK4ODF2TUBBDCTN3ACTR1ADCTN2YWHAGALMS1CEP192CEP290CEP164CEP152AZI1OFD1CCP110CEP135CEP78CEP76SDCCAG8CEP72CEP70CEP57CEP63FGFR1OPCEP41HAUS2SSNA1DYNLL1p-T160-CDK2AURKANEDD1TUBG1CKAP5CLASP1HSP90AA1DYNC1I2PLK1PPP2R1ANEK2TUBA1ATUBA4ATUBB4BTUBB4ACSNK1DCSNK1EPAFAH1B1PRKAR2BPRKACANDE1CDK1MAPRE1YWHAECETN2PCNTSFI1AKAP9CDK5RAP2DYNC1H1CNTRLPCM1CEP250CENPJDCTN1-2PLK4ODF2TUBBDCTN3ACTR1ADCTN2YWHAGALMS1CEP192CEP290CEP164CEP152AZI1OFD1CCP110CEP135CEP78CEP76SDCCAG8CEP72CEP70CEP57CEP63FGFR1OPCEP41HAUS2SSNA1NINLDYNLL1AJUBAAURKANEDD1TUBG1CKAP5CLASP1HSP90AA1DYNC1I2PLK1PPP2R1ANEK2TUBA1ATUBA4ATUBB4BTUBB4ACSNK1DCSNK1EPAFAH1B1PRKAR2BPRKACANDE1CDK1MAPRE1YWHAECETN2PCNTSFI1AKAP9CDK5RAP2DYNC1H1CNTRLPCM1CEP250CENPJDCTN1-2PLK4ODF2TUBBDCTN3ACTR1ADCTN2YWHAGALMS1CEP192CEP290CEP164CEP152AZI1OFD1CCP110CEP135CEP78CEP76SDCCAG8CEP72CEP70CEP57CEP63FGFR1OPCEP41HAUS2SSNA1NINLDYNLL1NEDD1TUBG1CKAP5CLASP1HSP90AA1DYNC1I2PLK1PPP2R1ANEK2TUBA1ATUBA4ATUBB4BTUBB4ACSNK1DCSNK1EPAFAH1B1PRKAR2BPRKACANDE1CDK1MAPRE1YWHAECETN2PCNTSFI1AKAP9CDK5RAP2DYNC1H1CNTRLPCM1CEP250CENPJDCTN1-2PLK4ODF2TUBBDCTN3ACTR1ADCTN2YWHAGALMS1CEP192CEP290CEP164CEP152AZI1OFD1CCP110CEP135CEP78CEP76SDCCAG8CEP72CEP70CEP57CEP63FGFR1OPCEP41HAUS2SSNA1NINLDYNLL1p-T288-AURKAPLK1p-S252-BORANEDD1TUBG1CKAP5CLASP1HSP90AA1DYNC1I2PPP2R1ANEK2TUBA1ATUBA4ATUBB4BTUBB4ACSNK1DCSNK1EPAFAH1B1PRKAR2BPRKACANDE1CDK1MAPRE1YWHAECETN2PCNTSFI1AKAP9CDK5RAP2DYNC1H1CNTRLPCM1CEP250CENPJDCTN1-2PLK4ODF2TUBBDCTN3ACTR1ADCTN2YWHAGALMS1CEP192CEP290CEP164CEP152AZI1OFD1CCP110CEP135CEP78CEP76SDCCAG8CEP72CEP70CEP57CEP63FGFR1OPCEP41HAUS2SSNA1NINLDYNLL1p-T288-AURKAp-T210-PLK1p-S252-BORASKP1CUL1BTRCFBXW11SKP1CUL1BTRCFBXW11p-S252,S497,T501-BORAp-S252,S497,T501-BORARPS27A(1-76)UBA52(1-76)UBB(1-76)UBB(77-152)UBB(153-228)UBC(1-76)UBC(77-152)UBC(153-228)UBC(229-304)UBC(305-380)UBC(381-456)UBC(457-532)UBC(533-608)UBC(609-684)OPTNRAB8AGTPRAB8AGTPPPP1R12B-4p-S473-PPP1R12APPP1CBp-T161-CDK1p-T160-CDK2CCNB1CCNB2p-T611-FOXM1p-T210-PLK1PPP2R2Ap-T611,S730,S739-FOXM1CDC25A GeneEP300LIN37LIN52LIN54LIN9RBBP4p-T611,S730,S739-FOXM1LIN37LIN52LIN54LIN9RBBP4MYBL2PLK1 Genep-T611,S730,S739-FOXM1LIN37LIN52LIN54LIN9RBBP4MYBL2CCNB1 Genep-T611,S730,S739-FOXM1LIN37LIN52LIN54LIN9RBBP4MYBL2CCNB2 Genep-T611,S730,S739-FOXM1CENPF GeneName: Mitotic G2-G2/M phasesOrganism: Homo sapiens


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Bibliography

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  55. Hutchins JR, Toyoda Y, Hegemann B, Poser I, Hériché JK, Sykora MM, Augsburg M, Hudecz O, Buschhorn BA, Bulkescher J, Conrad C, Comartin D, Schleiffer A, Sarov M, Pozniakovsky A, Slabicki MM, Schloissnig S, Steinmacher I, Leuschner M, Ssykor A, Lawo S, Pelletier L, Stark H, Nasmyth K, Ellenberg J, Durbin R, Buchholz F, Mechtler K, Hyman AA, Peters JM.; ''Systematic analysis of human protein complexes identifies chromosome segregation proteins.''; PubMed Europe PMC Scholia
  56. Timofeev O, Cizmecioglu O, Hu E, Orlik T, Hoffmann I.; ''Human Cdc25A phosphatase has a non-redundant function in G2 phase by activating Cyclin A-dependent kinases.''; PubMed Europe PMC Scholia
  57. Monte M, Benetti R, Buscemi G, Sandy P, Del Sal G, Schneider C.; ''The cell cycle-regulated protein human GTSE-1 controls DNA damage-induced apoptosis by affecting p53 function.''; PubMed Europe PMC Scholia
  58. Takahashi M, Yamagiwa A, Nishimura T, Mukai H, Ono Y.; ''Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex.''; PubMed Europe PMC Scholia
  59. Casenghi M, Meraldi P, Weinhart U, Duncan PI, Körner R, Nigg EA.; ''Polo-like kinase 1 regulates Nlp, a centrosome protein involved in microtubule nucleation.''; PubMed Europe PMC Scholia
  60. Dynlacht BD, Flores O, Lees JA, Harlow E.; ''Differential regulation of E2F transactivation by cyclin/cdk2 complexes.''; PubMed Europe PMC Scholia
  61. O'Farrell PH.; ''Triggering the all-or-nothing switch into mitosis.''; PubMed Europe PMC Scholia
  62. Galaktionov K, Beach D.; ''Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins.''; PubMed Europe PMC Scholia
  63. Kachaner D, Filipe J, Laplantine E, Bauch A, Bennett KL, Superti-Furga G, Israël A, Weil R.; ''Plk1-dependent phosphorylation of optineurin provides a negative feedback mechanism for mitotic progression.''; PubMed Europe PMC Scholia
  64. Pines J, Hunter T.; ''Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport.''; PubMed Europe PMC Scholia
  65. Graves PR, Lovly CM, Uy GL, Piwnica-Worms H.; ''Localization of human Cdc25C is regulated both by nuclear export and 14-3-3 protein binding.''; PubMed Europe PMC Scholia
  66. Coon TA, Glasser JR, Mallampalli RK, Chen BB.; ''Novel E3 ligase component FBXL7 ubiquitinates and degrades Aurora A, causing mitotic arrest.''; PubMed Europe PMC Scholia
  67. Sullivan C, Liu Y, Shen J, Curtis A, Newman C, Hock JM, Li X.; ''Novel interactions between FOXM1 and CDC25A regulate the cell cycle.''; PubMed Europe PMC Scholia
  68. Laoukili J, Kooistra MR, Brás A, Kauw J, Kerkhoven RM, Morrison A, Clevers H, Medema RH.; ''FoxM1 is required for execution of the mitotic programme and chromosome stability.''; PubMed Europe PMC Scholia
  69. Bayliss R, Sardon T, Vernos I, Conti E.; ''Structural basis of Aurora-A activation by TPX2 at the mitotic spindle.''; PubMed Europe PMC Scholia
  70. Goda T, Ishii T, Nakajo N, Sagata N, Kobayashi H.; ''The RRASK motif in Xenopus cyclin B2 is required for the substrate recognition of Cdc25C by the cyclin B-Cdc2 complex.''; PubMed Europe PMC Scholia
  71. Chen X, Müller GA, Quaas M, Fischer M, Han N, Stutchbury B, Sharrocks AD, Engeland K.; ''The forkhead transcription factor FOXM1 controls cell cycle-dependent gene expression through an atypical chromatin binding mechanism.''; PubMed Europe PMC Scholia
  72. Jascur T, Brickner H, Salles-Passador I, Barbier V, El Khissiin A, Smith B, Fotedar R, Fotedar A.; ''Regulation of p21(WAF1/CIP1) stability by WISp39, a Hsp90 binding TPR protein.''; PubMed Europe PMC Scholia
  73. Monte M, Benetti R, Collavin L, Marchionni L, Del Sal G, Schneider C.; ''hGTSE-1 expression stimulates cytoplasmic localization of p53.''; PubMed Europe PMC Scholia
  74. Draviam VM, Orrechia S, Lowe M, Pardi R, Pines J.; ''The localization of human cyclins B1 and B2 determines CDK1 substrate specificity and neither enzyme requires MEK to disassemble the Golgi apparatus.''; PubMed Europe PMC Scholia
  75. Desai D, Wessling HC, Fisher RP, Morgan DO.; ''Effects of phosphorylation by CAK on cyclin binding by CDC2 and CDK2.''; PubMed Europe PMC Scholia
  76. Timofeev O, Cizmecioglu O, Settele F, Kempf T, Hoffmann I.; ''Cdc25 phosphatases are required for timely assembly of CDK1-cyclin B at the G2/M transition.''; PubMed Europe PMC Scholia
  77. Bellanger S, de Gramont A, Sobczak-Thépot J.; ''Cyclin B2 suppresses mitotic failure and DNA re-replication in human somatic cells knocked down for both cyclins B1 and B2.''; PubMed Europe PMC Scholia
  78. Watanabe N, Arai H, Nishihara Y, Taniguchi M, Watanabe N, Hunter T, Osada H.; ''M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFbeta-TrCP.''; PubMed Europe PMC Scholia
  79. Major ML, Lepe R, Costa RH.; ''Forkhead box M1B transcriptional activity requires binding of Cdk-cyclin complexes for phosphorylation-dependent recruitment of p300/CBP coactivators.''; PubMed Europe PMC Scholia
  80. Toyoshima-Morimoto F, Taniguchi E, Nishida E.; ''Plk1 promotes nuclear translocation of human Cdc25C during prophase.''; PubMed Europe PMC Scholia
  81. Yang J, Bardes ES, Moore JD, Brennan J, Powers MA, Kornbluth S.; ''Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1.''; PubMed Europe PMC Scholia
  82. Liu XS, Li H, Song B, Liu X.; ''Polo-like kinase 1 phosphorylation of G2 and S-phase-expressed 1 protein is essential for p53 inactivation during G2 checkpoint recovery.''; PubMed Europe PMC Scholia
  83. Takizawa CG, Morgan DO.; ''Control of mitosis by changes in the subcellular location of cyclin-B1-Cdk1 and Cdc25C.''; PubMed Europe PMC Scholia
  84. Groen AC, Cameron LA, Coughlin M, Miyamoto DT, Mitchison TJ, Ohi R.; ''XRHAMM functions in ran-dependent microtubule nucleation and pole formation during anastral spindle assembly.''; PubMed Europe PMC Scholia
  85. Wei SJ, Williams JG, Dang H, Darden TA, Betz BL, Humble MM, Chang FM, Trempus CS, Johnson K, Cannon RE, Tennant RW.; ''Identification of a specific motif of the DSS1 protein required for proteasome interaction and p53 protein degradation.''; PubMed Europe PMC Scholia
  86. Hagting A, Jackman M, Simpson K, Pines J.; ''Translocation of cyclin B1 to the nucleus at prophase requires a phosphorylation-dependent nuclear import signal.''; PubMed Europe PMC Scholia
  87. Golsteyn RM, Mundt KE, Fry AM, Nigg EA.; ''Cell cycle regulation of the activity and subcellular localization of Plk1, a human protein kinase implicated in mitotic spindle function.''; PubMed Europe PMC Scholia
  88. Liu F, Stanton JJ, Wu Z, Piwnica-Worms H.; ''The human Myt1 kinase preferentially phosphorylates Cdc2 on threonine 14 and localizes to the endoplasmic reticulum and Golgi complex.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
114706
Reactome
view16:18, 25 January 2021ReactomeTeamReactome version 75
113151view11:21, 2 November 2020ReactomeTeamReactome version 74
112379view15:31, 9 October 2020ReactomeTeamReactome version 73
101750view12:30, 5 November 2018DeSlOntology Term : 'G2/M transition pathway' added !
101749view12:29, 5 November 2018DeSlOntology Term : 'G2 phase pathway' added !
101282view11:17, 1 November 2018ReactomeTeamreactome version 66
100819view20:47, 31 October 2018ReactomeTeamreactome version 65
100360view19:22, 31 October 2018ReactomeTeamreactome version 64
99905view16:06, 31 October 2018ReactomeTeamreactome version 63
99461view14:38, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
94019view13:51, 16 August 2017ReactomeTeamreactome version 61
93638view11:29, 9 August 2017ReactomeTeamreactome version 61
86753view09:25, 11 July 2016ReactomeTeamreactome version 56
83378view11:04, 18 November 2015ReactomeTeamVersion54
81553view13:05, 21 August 2015ReactomeTeamVersion53
77022view08:32, 17 July 2014ReactomeTeamFixed remaining interactions
76727view12:09, 16 July 2014ReactomeTeamFixed remaining interactions
75762view11:26, 10 June 2014ReactomeTeamReactome 48 Update
75112view14:06, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74759view08:50, 30 April 2014ReactomeTeamReactome46
44913view10:36, 6 October 2011MartijnVanIerselOntology Term : 'cell cycle pathway, mitotic' added !
42077view21:55, 4 March 2011MaintBotAutomatic update
39885view05:54, 21 January 2011MaintBotNew pathway

External references

DataNodes

View all...
Name  ↓Type  ↓Database reference  ↓Comment  ↓
ACTR1A ProteinP61163 (Uniprot-TrEMBL)
ADPMetaboliteCHEBI:16761 (ChEBI)
AJUBA ProteinQ96IF1 (Uniprot-TrEMBL)
AJUBAProteinQ96IF1 (Uniprot-TrEMBL)
AKAP9 ProteinQ99996 (Uniprot-TrEMBL)
ALMS1 ProteinQ8TCU4 (Uniprot-TrEMBL)
ATPMetaboliteCHEBI:15422 (ChEBI)
AURKA ProteinO14965 (Uniprot-TrEMBL)
AZI1 ProteinQ9UPN4 (Uniprot-TrEMBL)
BORAProteinQ6PGQ7 (Uniprot-TrEMBL)
BTRC ProteinQ9Y297 (Uniprot-TrEMBL)
CAKComplexR-HSA-69221 (Reactome)
CCNA1 ProteinP78396 (Uniprot-TrEMBL)
CCNA1:p-T161-CDK1ComplexR-HSA-68892 (Reactome)
CCNA2 ProteinP20248 (Uniprot-TrEMBL)
CCNA2:p-T161-CDK1ComplexR-HSA-68906 (Reactome)
CCNA:CDK1ComplexR-HSA-170091 (Reactome)
CCNA:p-T14,T161-CDK1ComplexR-HSA-170092 (Reactome)
CCNA:p-T14,Y15,T161-CDK1ComplexR-HSA-170147 (Reactome)
CCNA:p-T14-CDK1ComplexR-HSA-170085 (Reactome)
CCNA:p-T14-CDK1ComplexR-HSA-170090 (Reactome)
CCNA:p-T160-CDK2:E2F1/E2F3ComplexR-HSA-187932 (Reactome)
CCNA:p-T160-CDK2:p-E2F1/p-E2F3ComplexR-HSA-187944 (Reactome)
CCNA:p-T160-CDK2ComplexR-HSA-187952 (Reactome)
CCNA:p-T161-CDK1ComplexR-HSA-170146 (Reactome)
CCNAProteinR-HSA-170089 (Reactome)
CCNB1 Gene ProteinENSG00000134057 (ENSEMBL)
CCNB1 GeneENSG00000134057 (ENSEMBL)
CCNB1 ProteinP14635 (Uniprot-TrEMBL)
CCNB1:p-T14,T161-CDK1ComplexR-HSA-170073 (Reactome)
CCNB1:p-T14,Y15,T161-CDK1ComplexR-HSA-170065 (Reactome)
CCNB1:p-T14-CDK1ComplexR-HSA-170056 (Reactome)
CCNB1:p-T161-CDK1ComplexR-HSA-157456 (Reactome)
CCNB1:p-T161-CDK1ComplexR-HSA-170160 (Reactome)
CCNB1ProteinP14635 (Uniprot-TrEMBL)
CCNB2 Gene ProteinENSG00000157456 (ENSEMBL)
CCNB2 GeneENSG00000157456 (ENSEMBL)
CCNB2 ProteinO95067 (Uniprot-TrEMBL)
CCNB2:p-T161-CDK1ComplexR-HSA-68898 (Reactome)
CCNB2ProteinO95067 (Uniprot-TrEMBL)
CCNB:CDK1ComplexR-HSA-170077 (Reactome)
CCNB:p-T14-CDK1ComplexR-HSA-170069 (Reactome)
CCNB:p-T161-CDK1R-HSA-2311324 (Reactome)
CCNBProteinR-HSA-157461 (Reactome)
CCNH ProteinP51946 (Uniprot-TrEMBL)
CCP110 ProteinO43303 (Uniprot-TrEMBL)
CDC25A Gene ProteinENSG00000164045 (ENSEMBL)
CDC25A GeneENSG00000164045 (ENSEMBL)
CDC25AProteinP30304 (Uniprot-TrEMBL)
CDC25BProteinP30305 (Uniprot-TrEMBL)
CDC25CProteinP30307 (Uniprot-TrEMBL)
CDC25R-HSA-69261 (Reactome)
CDK1 ProteinP06493 (Uniprot-TrEMBL)
CDK11p58ProteinR-HSA-380452 (Reactome)
CDK1ProteinP06493 (Uniprot-TrEMBL)
CDK5RAP2 ProteinQ96SN8 (Uniprot-TrEMBL)
CDK7 ProteinP50613 (Uniprot-TrEMBL)
CENPF Gene ProteinENSG00000117724 (ENSEMBL)
CENPF GeneENSG00000117724 (ENSEMBL)
CENPFProteinP49454 (Uniprot-TrEMBL)
CENPJ ProteinQ9HC77 (Uniprot-TrEMBL)
CEP135 ProteinQ66GS9 (Uniprot-TrEMBL)
CEP152 ProteinO94986 (Uniprot-TrEMBL)
CEP164 ProteinQ9UPV0 (Uniprot-TrEMBL)
CEP192 ProteinQ8TEP8 (Uniprot-TrEMBL)
CEP250 ProteinQ9BV73 (Uniprot-TrEMBL)
CEP250ProteinQ9BV73 (Uniprot-TrEMBL)
CEP290 ProteinO15078 (Uniprot-TrEMBL)
CEP41 ProteinQ9BYV8 (Uniprot-TrEMBL)
CEP57 ProteinQ86XR8 (Uniprot-TrEMBL)
CEP63 ProteinQ96MT8 (Uniprot-TrEMBL)
CEP70 ProteinQ8NHQ1 (Uniprot-TrEMBL)
CEP72 ProteinQ9P209 (Uniprot-TrEMBL)
CEP76 ProteinQ8TAP6 (Uniprot-TrEMBL)
CEP78 ProteinQ5JTW2 (Uniprot-TrEMBL)
CETN2 ProteinP41208 (Uniprot-TrEMBL)
CKAP5 ProteinQ14008 (Uniprot-TrEMBL)
CLASP1 ProteinQ7Z460 (Uniprot-TrEMBL)
CNTRL ProteinQ7Z7A1 (Uniprot-TrEMBL)
CRS kinaseR-HSA-170106 (Reactome)
CSNK1D ProteinP48730 (Uniprot-TrEMBL)
CSNK1E ProteinP49674 (Uniprot-TrEMBL)
CUL1 ProteinQ13616 (Uniprot-TrEMBL)
Cdc25ProteinR-HSA-170108 (Reactome)
Cdc25ProteinR-HSA-186979 (Reactome)
Centrosome associated Plk1ComplexR-HSA-380288 (Reactome)
Centrosome:AURKA:AJUBAComplexR-HSA-2574836 (Reactome)
Centrosome:AURKAComplexR-HSA-2574827 (Reactome)
Centrosome:p-T288-AURKA:p-S252-BORA:PLK1ComplexR-HSA-3000313 (Reactome)
Centrosome:p-T288-AURKAComplexR-HSA-3000302 (Reactome)
Centrosomes

containing

recruited CDK11p58		ComplexR-HSA-380453 (Reactome)
Cyclin

B1:phospho-Cdc2(Thr 161, Thr 14, Tyr

15)		ComplexR-HSA-170068 (Reactome)
Cyclin

B2:phospho-Cdc2(Thr

14, Thr 161)		ComplexR-HSA-170152 (Reactome)
Cyclin A1:Cdk2

phosphorylated G2/M

transition protein		R-HSA-617372 (Reactome)
Cyclin A2:Cdk2

phosphorylated G2/M

transition protein		R-HSA-617371 (Reactome)
DCTN1-2 ProteinQ14203-2 (Uniprot-TrEMBL)
DCTN2 ProteinQ13561 (Uniprot-TrEMBL)
DCTN3 ProteinO75935 (Uniprot-TrEMBL)
DYNC1H1 ProteinQ14204 (Uniprot-TrEMBL)
DYNC1I2 ProteinQ13409 (Uniprot-TrEMBL)
DYNLL1 ProteinP63167 (Uniprot-TrEMBL)
E2F1 ProteinQ01094 (Uniprot-TrEMBL)
E2F1/E2F3R-HSA-187942 (Reactome)
E2F3 ProteinO00716 (Uniprot-TrEMBL)
EP300 ProteinQ09472 (Uniprot-TrEMBL)
EP300ProteinQ09472 (Uniprot-TrEMBL)
FBXW11 ProteinQ9UKB1 (Uniprot-TrEMBL)
FGFR1OP ProteinO95684 (Uniprot-TrEMBL)
FOXM1ProteinQ08050 (Uniprot-TrEMBL)
G2/M transition proteinR-HSA-157449 (Reactome)
G2/M transition proteinsR-HSA-617370 (Reactome)
G2/M transition proteinsR-HSA-617374 (Reactome)
GTP MetaboliteCHEBI:15996 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HAUS2 ProteinQ9NVX0 (Uniprot-TrEMBL)
HSP90AA1 ProteinP07900 (Uniprot-TrEMBL)
LIN37 ProteinQ96GY3 (Uniprot-TrEMBL)
LIN52 ProteinQ52LA3 (Uniprot-TrEMBL)
LIN54 ProteinQ6MZP7 (Uniprot-TrEMBL)
LIN9 ProteinQ5TKA1 (Uniprot-TrEMBL)
MAPRE1 ProteinQ15691 (Uniprot-TrEMBL)
MNAT1 ProteinP51948 (Uniprot-TrEMBL)
MYBL2 ProteinP10244 (Uniprot-TrEMBL)
MYBL2ProteinP10244 (Uniprot-TrEMBL)
Mature centrosomes

enriched in gamma-TURC

complexes		ComplexR-HSA-380440 (Reactome)
MuvB complexComplexR-HSA-1362248 (Reactome)
NDE1 ProteinQ9NXR1 (Uniprot-TrEMBL)
NEDD1 ProteinQ8NHV4 (Uniprot-TrEMBL)
NEK2 ProteinP51955 (Uniprot-TrEMBL)
NINL ProteinQ9Y2I6 (Uniprot-TrEMBL)
NUMA1ProteinQ14980 (Uniprot-TrEMBL)
Nlp-depleted centrosomeComplexR-HSA-380705 (Reactome)
NuMA homodimerComplexR-HSA-380486 (Reactome)
NuMA-bound microtubulesComplexR-HSA-380495 (Reactome)
ODF2 ProteinQ5BJF6 (Uniprot-TrEMBL)
OFD1 ProteinO75665 (Uniprot-TrEMBL)
OPTN ProteinQ96CV9 (Uniprot-TrEMBL)
OPTN:RAB8A:GTPComplexR-HSA-2562537 (Reactome)
PAFAH1B1 ProteinP43034 (Uniprot-TrEMBL)
PCM1 ProteinQ15154 (Uniprot-TrEMBL)
PCNT ProteinO95613 (Uniprot-TrEMBL)
PKMYT1ProteinQ99640 (Uniprot-TrEMBL)
PLK1 Gene ProteinENSG00000166851 (ENSEMBL)
PLK1 GeneENSG00000166851 (ENSEMBL)
PLK1 ProteinP53350 (Uniprot-TrEMBL)
PLK1ProteinP53350 (Uniprot-TrEMBL)
PLK4 ProteinO00444 (Uniprot-TrEMBL)
PP2A-PPP2R2AComplexR-HSA-4088142 (Reactome)
PPP1CB ProteinP62140 (Uniprot-TrEMBL)
PPP1R12B-4 ProteinO60237-4 (Uniprot-TrEMBL)
PPP2R1A ProteinP30153 (Uniprot-TrEMBL)
PPP2R2A ProteinP63151 (Uniprot-TrEMBL)
PRKACA ProteinP17612 (Uniprot-TrEMBL)
PRKAR2B ProteinP31323 (Uniprot-TrEMBL)
Phospho-Cyclin

B1

(CRS):phospho-Cdc2(Thr 161)		ComplexR-HSA-170121 (Reactome)
Phosphorylated Myosin PhosphataseComplexR-HSA-3002804 (Reactome) All known myosin phosphatases consist of PP1 beta and both a large and a small myosin phosphatase targetting (Mypt) subunit. The large Mypt targets PP1 beta to myosin and determines the substrate specifity of the phosphatase. The Large Mypt subunit is encoded by one of three human genes, PPP1R12A (MYPT1), PPP1R12B (MYPT2) and PPP1R12C. Only MYPT1 is represented here. The small subunit is an alternative transcript of MYPT2. The function of the small Mypt subunit remains unclear, but because it is known to interact directly with myosin and the large Mypt it is thought to have an unspecified regulatory role.
PiMetaboliteCHEBI:18367 (ChEBI)
RAB8A ProteinP61006 (Uniprot-TrEMBL)
RAB8A:GTPComplexR-HSA-2562539 (Reactome)
RBBP4 ProteinQ09028 (Uniprot-TrEMBL)
RPS27A(1-76) ProteinP62979 (Uniprot-TrEMBL)
SCF-beta-TrCp1,2ComplexR-HSA-1168601 (Reactome)
SDCCAG8 ProteinQ86SQ7 (Uniprot-TrEMBL)
SFI1 ProteinA8K8P3 (Uniprot-TrEMBL)
SKP1 ProteinP63208 (Uniprot-TrEMBL)
SSNA1 ProteinO43805 (Uniprot-TrEMBL)
TUBA1A ProteinQ71U36 (Uniprot-TrEMBL)
TUBA4A ProteinP68366 (Uniprot-TrEMBL)
TUBB ProteinP07437 (Uniprot-TrEMBL)
TUBB4A ProteinP04350 (Uniprot-TrEMBL)
TUBB4B ProteinP68371 (Uniprot-TrEMBL)
TUBG1 ProteinP23258 (Uniprot-TrEMBL)
TUBG2 ProteinQ9NRH3 (Uniprot-TrEMBL)
TUBGCP2 ProteinQ9BSJ2 (Uniprot-TrEMBL)
TUBGCP3 ProteinQ96CW5 (Uniprot-TrEMBL)
TUBGCP4 ProteinQ9UGJ1 (Uniprot-TrEMBL)
TUBGCP5 ProteinQ96RT8 (Uniprot-TrEMBL)
TUBGCP6 ProteinQ96RT7 (Uniprot-TrEMBL)
UBA52(1-76) ProteinP62987 (Uniprot-TrEMBL)
UBB(1-76) ProteinP0CG47 (Uniprot-TrEMBL)
UBB(153-228) ProteinP0CG47 (Uniprot-TrEMBL)
UBB(77-152) ProteinP0CG47 (Uniprot-TrEMBL)
UBC(1-76) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(153-228) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(229-304) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(305-380) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(381-456) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(457-532) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(533-608) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(609-684) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(77-152) ProteinP0CG48 (Uniprot-TrEMBL)
Ub-p-S252,S497,T501-BORAComplexR-HSA-3000337 (Reactome)
UbProteinR-HSA-113595 (Reactome)
WEE1ProteinP30291 (Uniprot-TrEMBL)
XPO1ProteinO14980 (Uniprot-TrEMBL)
YWHAE ProteinP62258 (Uniprot-TrEMBL)
YWHAG ProteinP61981 (Uniprot-TrEMBL)
active nuclear

Cyclin B1:Cdc2

complexes		R-HSA-170168 (Reactome)
cNAP-1 depleted centrosomeComplexR-HSA-380698 (Reactome)
centrosome

containing

phosphorylated Nlp		ComplexR-HSA-380704 (Reactome)
centrosome-associated NuMAComplexR-HSA-380503 (Reactome)
centrosome-nucleated microtubulesComplexR-HSA-379273 (Reactome)
centrosomeComplexR-HSA-380268 (Reactome)
cytoplasmic Cyclin B1:Cdc2 complexesComplexR-HSA-170079 (Reactome)
gamma-tubulin complexComplexR-HSA-379277 (Reactome) A current model of the arrangement of subunits within the  TuRC postulates that 6-7 TuSC subcomplexes are held together by  the other Grip proteins, which together form the cap subunits(Reviewed in Wiese and Zheng, 2006).
nuclear Cyclin B1:Cdc2 complexesComplexR-HSA-170051 (Reactome)
nuclear Cyclin B1:Cdc2 substratesR-NUL-170150 (Reactome)
p-4S-CCNB1 ProteinP14635 (Uniprot-TrEMBL)
p-CDK1/2:CCNA/p-T161-CDK1:CCNBComplexR-HSA-4088061 (Reactome)
p-E2F1 ProteinQ01094 (Uniprot-TrEMBL)
p-E2F3 ProteinO00716 (Uniprot-TrEMBL)
p-NINL ProteinQ9Y2I6 (Uniprot-TrEMBL)
p-NINLProteinQ9Y2I6 (Uniprot-TrEMBL)
p-NUMA1 ProteinQ14980 (Uniprot-TrEMBL)
p-NUMA1ProteinQ14980 (Uniprot-TrEMBL)
p-PKMYT1ProteinQ99640 (Uniprot-TrEMBL)
p-S-AJUBAProteinQ96IF1 (Uniprot-TrEMBL)
p-S177-OPTNProteinQ96CV9 (Uniprot-TrEMBL)
p-S198-CDC25CProteinP30307 (Uniprot-TrEMBL)
p-S252,S497,T501-BORA ProteinQ6PGQ7 (Uniprot-TrEMBL)
p-S252,S497,T501-BORA:SCF-beta-TrCp1/2ComplexR-HSA-3000340 (Reactome)
p-S252,S497,T501-BORAProteinQ6PGQ7 (Uniprot-TrEMBL)
p-S252-BORA ProteinQ6PGQ7 (Uniprot-TrEMBL)
p-S252-BORA:p-T210-PLK1ComplexR-HSA-3000305 (Reactome)
p-S252-BORAProteinQ6PGQ7 (Uniprot-TrEMBL)
p-S473-PPP1R12A ProteinO14974 (Uniprot-TrEMBL)
p-S53-WEE1ProteinP30291 (Uniprot-TrEMBL)
p-T14,T161-CDK1 ProteinP06493 (Uniprot-TrEMBL)
p-T14,Y15,T161-CDK1 ProteinP06493 (Uniprot-TrEMBL)
p-T14-CDK1 ProteinP06493 (Uniprot-TrEMBL)
p-T160-CDK2 ProteinP24941 (Uniprot-TrEMBL)
p-T161-CDK1 ProteinP06493 (Uniprot-TrEMBL)
p-T210-PLK1 ProteinP53350 (Uniprot-TrEMBL)
p-T210-PLK1ProteinP53350 (Uniprot-TrEMBL)
p-T288-AURKA ProteinO14965 (Uniprot-TrEMBL)
p-T611,S730,S739-FOXM1 ProteinQ08050 (Uniprot-TrEMBL)
p-T611,S730,S739-FOXM1:CENPF GeneComplexR-HSA-4088442 (Reactome)
p-T611,S730,S739-FOXM1:EP300:CDC25A GeneComplexR-HSA-4088158 (Reactome)
p-T611,S730,S739-FOXM1:MuvB:MYBL2:CCNB1 GeneComplexR-HSA-4088308 (Reactome)
p-T611,S730,S739-FOXM1:MuvB:MYBL2:CCNB2 GeneComplexR-HSA-4088297 (Reactome)
p-T611,S730,S739-FOXM1:MuvB:MYBL2:PLK1 GeneComplexR-HSA-4088300 (Reactome)
p-T611,S730,S739-FOXM1ProteinQ08050 (Uniprot-TrEMBL)
p-T611-FOXM1 ProteinQ08050 (Uniprot-TrEMBL)
p-T611-FOXM1:p-T210-PLK1ComplexR-HSA-4088136 (Reactome)
p-T611-FOXM1ProteinQ08050 (Uniprot-TrEMBL)
phospho-Cyclin B1(CRS):phospho-Cdc2 (Thr 161)ComplexR-HSA-170127 (Reactome)
phospho-G2/M transition proteinR-HSA-157604 (Reactome)
phospho-G2/M transition proteinR-HSA-69753 (Reactome)
phospho-cyclin B1(CRS):phosph-Cdc2(Thr 161)ComplexR-HSA-170047 (Reactome)
phosphorylated

nuclear Cyclin

B1:Cdc2 substrates		R-NUL-182620 (Reactome)

Annotated Interactions

View all...
Source  ↓Target  ↓Type  ↓Database reference  ↓Comment  ↓
ADPArrowR-HSA-156678 (Reactome)
ADPArrowR-HSA-170055 (Reactome)
ADPArrowR-HSA-170070 (Reactome)
ADPArrowR-HSA-170076 (Reactome)
ADPArrowR-HSA-170087 (Reactome)
ADPArrowR-HSA-170116 (Reactome)
ADPArrowR-HSA-170126 (Reactome)
ADPArrowR-HSA-170156 (Reactome)
ADPArrowR-HSA-170157 (Reactome)
ADPArrowR-HSA-187959 (Reactome)
ADPArrowR-HSA-2562526 (Reactome)
ADPArrowR-HSA-2574840 (Reactome)
ADPArrowR-HSA-3000310 (Reactome)
ADPArrowR-HSA-3000327 (Reactome)
ADPArrowR-HSA-380272 (Reactome)
ADPArrowR-HSA-380278 (Reactome)
ADPArrowR-HSA-4086410 (Reactome)
ADPArrowR-HSA-4088024 (Reactome)
ADPArrowR-HSA-4088134 (Reactome)
ADPArrowR-HSA-69754 (Reactome)
ADPArrowR-HSA-69756 (Reactome)
ADPArrowR-HSA-69759 (Reactome)
AJUBAR-HSA-2574845 (Reactome)
ATPR-HSA-156678 (Reactome)
ATPR-HSA-170055 (Reactome)
ATPR-HSA-170070 (Reactome)
ATPR-HSA-170076 (Reactome)
ATPR-HSA-170087 (Reactome)
ATPR-HSA-170116 (Reactome)
ATPR-HSA-170126 (Reactome)
ATPR-HSA-170156 (Reactome)
ATPR-HSA-170157 (Reactome)
ATPR-HSA-187959 (Reactome)
ATPR-HSA-2562526 (Reactome)
ATPR-HSA-2574840 (Reactome)
ATPR-HSA-3000310 (Reactome)
ATPR-HSA-3000327 (Reactome)
ATPR-HSA-380272 (Reactome)
ATPR-HSA-380278 (Reactome)
ATPR-HSA-4086410 (Reactome)
ATPR-HSA-4088024 (Reactome)
ATPR-HSA-4088134 (Reactome)
ATPR-HSA-69754 (Reactome)
ATPR-HSA-69756 (Reactome)
ATPR-HSA-69759 (Reactome)
BORAR-HSA-4086410 (Reactome)
CAKmim-catalysisR-HSA-170076 (Reactome)
CAKmim-catalysisR-HSA-170087 (Reactome)
CCNA1:p-T161-CDK1mim-catalysisR-HSA-69754 (Reactome)
CCNA2:p-T161-CDK1mim-catalysisR-HSA-69756 (Reactome)
CCNA:CDK1ArrowR-HSA-170084 (Reactome)
CCNA:CDK1R-HSA-170116 (Reactome)
CCNA:p-T14,T161-CDK1ArrowR-HSA-170087 (Reactome)
CCNA:p-T14,T161-CDK1R-HSA-170156 (Reactome)
CCNA:p-T14,Y15,T161-CDK1ArrowR-HSA-170156 (Reactome)
CCNA:p-T14,Y15,T161-CDK1R-HSA-170158 (Reactome)
CCNA:p-T14-CDK1ArrowR-HSA-170088 (Reactome)
CCNA:p-T14-CDK1ArrowR-HSA-170116 (Reactome)
CCNA:p-T14-CDK1R-HSA-170087 (Reactome)
CCNA:p-T14-CDK1R-HSA-170088 (Reactome)
CCNA:p-T160-CDK2:E2F1/E2F3ArrowR-HSA-187937 (Reactome)
CCNA:p-T160-CDK2:E2F1/E2F3R-HSA-187959 (Reactome)
CCNA:p-T160-CDK2:E2F1/E2F3mim-catalysisR-HSA-187959 (Reactome)
CCNA:p-T160-CDK2:p-E2F1/p-E2F3ArrowR-HSA-187959 (Reactome)
CCNA:p-T160-CDK2R-HSA-187937 (Reactome)
CCNA:p-T161-CDK1ArrowR-HSA-170158 (Reactome)
CCNAR-HSA-170084 (Reactome)
CCNB1 GeneR-HSA-4088298 (Reactome)
CCNB1 GeneR-HSA-4088307 (Reactome)
CCNB1:p-T14,T161-CDK1ArrowR-HSA-170076 (Reactome)
CCNB1:p-T14,T161-CDK1R-HSA-170070 (Reactome)
CCNB1:p-T14,Y15,T161-CDK1ArrowR-HSA-170070 (Reactome)
CCNB1:p-T14,Y15,T161-CDK1R-HSA-170072 (Reactome)
CCNB1:p-T14,Y15,T161-CDK1R-HSA-170153 (Reactome)
CCNB1:p-T14-CDK1R-HSA-170076 (Reactome)
CCNB1:p-T161-CDK1ArrowR-HSA-170153 (Reactome)
CCNB1:p-T161-CDK1ArrowR-HSA-170161 (Reactome)
CCNB1:p-T161-CDK1R-HSA-170126 (Reactome)
CCNB1:p-T161-CDK1mim-catalysisR-HSA-380278 (Reactome)
CCNB1ArrowR-HSA-4088298 (Reactome)
CCNB2 GeneR-HSA-4088299 (Reactome)
CCNB2 GeneR-HSA-4088309 (Reactome)
CCNB2:p-T161-CDK1ArrowR-HSA-170162 (Reactome)
CCNB2:p-T161-CDK1mim-catalysisR-HSA-69759 (Reactome)
CCNB2ArrowR-HSA-4088299 (Reactome)
CCNB:CDK1ArrowR-HSA-170057 (Reactome)
CCNB:CDK1R-HSA-170055 (Reactome)
CCNB:p-T14-CDK1ArrowR-HSA-170055 (Reactome)
CCNB:p-T161-CDK1mim-catalysisR-HSA-4086410 (Reactome)
CCNBR-HSA-170057 (Reactome)
CDC25A GeneR-HSA-4088152 (Reactome)
CDC25A GeneR-HSA-4088162 (Reactome)
CDC25AArrowR-HSA-4088152 (Reactome)
CDC25BArrowR-HSA-170120 (Reactome)
CDC25BR-HSA-170120 (Reactome)
CDC25CArrowR-HSA-170149 (Reactome)
CDC25CR-HSA-156678 (Reactome)
CDC25CR-HSA-170149 (Reactome)
CDC25mim-catalysisR-HSA-170153 (Reactome)
CDC25mim-catalysisR-HSA-170158 (Reactome)
CDK11p58ArrowR-HSA-380311 (Reactome)
CDK11p58R-HSA-380455 (Reactome)
CDK1R-HSA-170057 (Reactome)
CDK1R-HSA-170084 (Reactome)
CENPF GeneR-HSA-4088439 (Reactome)
CENPF GeneR-HSA-4088441 (Reactome)
CENPFArrowR-HSA-4088441 (Reactome)
CEP250ArrowR-HSA-380294 (Reactome)
CRS kinasemim-catalysisR-HSA-170126 (Reactome)
Cdc25ArrowR-HSA-170159 (Reactome)
Cdc25R-HSA-170159 (Reactome)
Cdc25mim-catalysisR-HSA-170161 (Reactome)
Cdc25mim-catalysisR-HSA-170162 (Reactome)
Centrosome associated Plk1ArrowR-HSA-380311 (Reactome)
Centrosome:AURKA:AJUBAArrowR-HSA-2574845 (Reactome)
Centrosome:AURKA:AJUBAR-HSA-2574840 (Reactome)
Centrosome:AURKA:AJUBAmim-catalysisR-HSA-2574840 (Reactome)
Centrosome:AURKAR-HSA-2574845 (Reactome)
Centrosome:p-T288-AURKA:p-S252-BORA:PLK1ArrowR-HSA-3000319 (Reactome)
Centrosome:p-T288-AURKA:p-S252-BORA:PLK1R-HSA-3000310 (Reactome)
Centrosome:p-T288-AURKA:p-S252-BORA:PLK1mim-catalysisR-HSA-3000310 (Reactome)
Centrosome:p-T288-AURKAArrowR-HSA-2574840 (Reactome)
Centrosome:p-T288-AURKAArrowR-HSA-3000310 (Reactome)
Centrosome:p-T288-AURKAR-HSA-3000319 (Reactome)
Centrosomes

containing

recruited CDK11p58		ArrowR-HSA-380455 (Reactome)
Cyclin

B1:phospho-Cdc2(Thr 161, Thr 14, Tyr

15)		ArrowR-HSA-170072 (Reactome)
Cyclin

B1:phospho-Cdc2(Thr 161, Thr 14, Tyr

15)		R-HSA-170161 (Reactome)
Cyclin

B2:phospho-Cdc2(Thr

14, Thr 161)		R-HSA-170162 (Reactome)
Cyclin A1:Cdk2

phosphorylated G2/M

transition protein		ArrowR-HSA-69754 (Reactome)
Cyclin A2:Cdk2

phosphorylated G2/M

transition protein		ArrowR-HSA-69756 (Reactome)
E2F1/E2F3R-HSA-187937 (Reactome)
EP300R-HSA-4088162 (Reactome)
FOXM1ArrowR-HSA-4088141 (Reactome)
FOXM1R-HSA-4088024 (Reactome)
G2/M transition proteinR-HSA-69759 (Reactome)
G2/M transition proteinsR-HSA-69754 (Reactome)
G2/M transition proteinsR-HSA-69756 (Reactome)
H2OR-HSA-170153 (Reactome)
H2OR-HSA-170158 (Reactome)
H2OR-HSA-170161 (Reactome)
H2OR-HSA-170162 (Reactome)
H2OR-HSA-3002811 (Reactome)
H2OR-HSA-4088141 (Reactome)
MYBL2R-HSA-4088306 (Reactome)
MYBL2R-HSA-4088307 (Reactome)
MYBL2R-HSA-4088309 (Reactome)
Mature centrosomes

enriched in gamma-TURC

complexes		ArrowR-HSA-380283 (Reactome)
MuvB complexR-HSA-4088306 (Reactome)
MuvB complexR-HSA-4088307 (Reactome)
MuvB complexR-HSA-4088309 (Reactome)
NUMA1R-HSA-380278 (Reactome)
Nlp-depleted centrosomeArrowR-HSA-380303 (Reactome)
NuMA homodimerR-HSA-380316 (Reactome)
NuMA homodimerR-HSA-380508 (Reactome)
NuMA-bound microtubulesArrowR-HSA-380316 (Reactome)
OPTN:RAB8A:GTPR-HSA-2562526 (Reactome)
PKMYT1R-HSA-162657 (Reactome)
PKMYT1mim-catalysisR-HSA-170055 (Reactome)
PKMYT1mim-catalysisR-HSA-170116 (Reactome)
PLK1 GeneR-HSA-4088305 (Reactome)
PLK1 GeneR-HSA-4088306 (Reactome)
PLK1ArrowR-HSA-3002811 (Reactome)
PLK1ArrowR-HSA-4088305 (Reactome)
PLK1R-HSA-3000319 (Reactome)
PLK1R-HSA-380311 (Reactome)
PLK1mim-catalysisR-HSA-156678 (Reactome)
PLK1mim-catalysisR-HSA-156699 (Reactome)
PLK1mim-catalysisR-HSA-162657 (Reactome)
PLK1mim-catalysisR-HSA-380272 (Reactome)
PP2A-PPP2R2Amim-catalysisR-HSA-4088141 (Reactome)
Phospho-Cyclin

B1

(CRS):phospho-Cdc2(Thr 161)		ArrowR-HSA-170126 (Reactome)
Phosphorylated Myosin Phosphatasemim-catalysisR-HSA-3002811 (Reactome)
PiArrowR-HSA-170153 (Reactome)
PiArrowR-HSA-170158 (Reactome)
PiArrowR-HSA-170161 (Reactome)
PiArrowR-HSA-170162 (Reactome)
PiArrowR-HSA-3002811 (Reactome)
PiArrowR-HSA-4088141 (Reactome)
R-HSA-156678 (Reactome) It has been shown that Xenopus polo homolog, Plx1, directly phosphorylates and activates Cdc25C, which in turn dephosphorylates and activates Cdc2. This step is critical for the onset of mitosis. Since Plx1-dependent Cdc25C phosphorylation occurs in the absence of Cdc2 activity, it is likely that Plx1 is a triggering kinase, which leads to the activation of Cdc2 and therefore the normal onset of mitosis. In addition to catalytically activating CDC25C, PLK1-mediated phosphorylation also results in the nuclear accumulation of CDC25C (Toyoshima-Morimoto et al. 2002).
R-HSA-156699 (Reactome) *Plk1 is shown to phosphorylate Wee1A, an event that is likely critical for recognition and ubiquitination of Wee1A by SCF and therefore for the subsequent degradation of Wee1A . **Plk1 phosphorylates Wee1A at S53, creating the second phosphodegron, PD53. ** Evidence also exists in budding yeast that the budding yeast polo homolog Cdc5 directly phosphorylates and down-regulate the budding yeast Wee1 ortholog Swe1. Thus, polo kinase-dependent phosphorylation and degradation of Wee1A (or Swe1) is likely conserved throughout evolution and is critical for normal mitotic entry.
R-HSA-162657 (Reactome) At mitotic entry Plk1 phosphorylates and inhibits Myt1 activity. Cyclin B1-bound Cdc2, which is the target of Myt1, functions in a feedback loop and phosphorylates and further inhibits Myt1.
R-HSA-170044 (Reactome) During interphase, cyclin B1:Cdc2 shuttles continuously in and out of the nucleus. Cyclin B1:Cdc2 is transported into the nucleus by an unusual mechanism that requires importin b but not importin a or Ran. Dissociation of the cyclin-B1:Cdc2:importin complex in the nucleus requires ATP and involves other yet unidentified nuclear factors (Takizawa et al.,1991).
R-HSA-170055 (Reactome) Myt1, which localizes preferentially to the endoplasmic reticulum and Golgi complex, phosphorylates Cdc2 on threonine 14 ( Liu et al., 1997).
R-HSA-170057 (Reactome) Cyclin dependent kinases are themselves catalytically inactive due to the fact that their active site is blocked by a portion of the Cdk molecule itself. Binding to their corresponding cyclin partner results in conformational change that partially exposes the active site.
R-HSA-170070 (Reactome) Wee1, a nuclear kinase, phosphorylates cyclin B1:Cdc2 on tyrosine 15 inactivating the complex.
R-HSA-170072 (Reactome) During interphase, cyclin B1 shuttles continuously in and out of the nucleus. The cyclin B cytoplasmic retention sequence (CRS), which is responsible for its interphase cytoplasmic localization, functions as a nuclear export sequence (Yang et al., 1998).
R-HSA-170076 (Reactome) Full activity of most CDKs is dependent on CAK mediated phosphorylation at a conserved residue (Thr 161 in Cdc2). This modification is thought to improve substrate binding. Cyclin B:Cdc2 complexes have considerably low activity in the absence of CAK mediated phosphorylation (Desai et al 1995).
R-HSA-170084 (Reactome) Cyclin A is synthesized and associates with Cdc2 in G1. Cyclin dependent kinases are themselves catalytically inactive due to the fact that their active sites are blocked by a portion of the CDK molecule itself. Binding to their corresponding cyclin partner results in a conformational change that partially exposes the active site.
R-HSA-170087 (Reactome) Full activity of most CDKs is dependent on CAK mediated phosphorylation at a conserved residue (Thr 161 in Cdc2). This modification is thought to improve substrate binding. High affinity binding of Cyclin A within the Cyclin A:Cdc2 complex requires this phosphorylation (Desai et al 1995).
R-HSA-170088 (Reactome) Cyclin A:Cdc2 complexes translocate to the nucleus in G1 and may associate with condensing chromosomes in prophase (Pines and Hunter 1991).
R-HSA-170116 (Reactome) Myt1, which localizes preferentially to the endoplasmic reticulum and Golgi complex, phosphorylates Cdc2 on threonine 14 ( Liu et al., 1997).
R-HSA-170120 (Reactome) Cdc25B shuttles between the nucleus and the cytoplasm. Translocation out of the nucleus involves a nuclear export sequence in the N-terminus of Cdc25B (Lindqvist et al., 2004).
R-HSA-170126 (Reactome) At the onset of mitosis, cyclin B is phosphorylated in the CRS sequence which creates a nuclear import signal in the amino terminus. The kinase(s) responsible for this phosphorylation are not yet known (Hagting et al., 1999).
R-HSA-170131 (Reactome) The rapid translocation of cyclin B1:Cdc2 from the cytoplasm to the nucleus at the onset of mitosis is a result of an increase in the rate of import and, likely, a decreased rate of export. The increased rate of nuclear import is dependent upon phosphorylation of the CRS which creates a nuclear import signal in the amino terminus of cyclin B1 (Hagting et al, 1999).
R-HSA-170149 (Reactome) During interphase, phopshorylated Cdc25C is associated with 14-3-3 proteins preventing nuclear import. At the onset of mitosis, dephosphorylation of Cdc25C and dissociation of 14-3-3 increases the rate of import (see Takizawa and Morgan, 2000)
R-HSA-170153 (Reactome) Following its translocation to the nucleus, Cdc25 dephosphorylates and activates nuclear cyclin B1:Cdc2 complexes (Strausfeld et al., 1991).
R-HSA-170156 (Reactome) The human Wee1 kinase phosphorylates Cdc2 on tyrosine 15 inactivating the cyclin:CDK complex (Watanabe et al., 1995).
R-HSA-170157 (Reactome) A description of the mitotic proteins targeted by the mitotic cyclin:CDK complexes will be covered in a later release.
R-HSA-170158 (Reactome) Activation of the mitotic cyclin:Cdc2 complexes at mitosis requires the removal of the inhibitory phosphate groups on Cdc2. This dephosphorylation is achieved by the activity of the Cdc25 family of phosphatases. The Cdc25 members, Cdc25A, Cdc25B, and Cdc25C are kept inactive during interphase and are activated at the G2/M transition (see Wolfe and Gould 2004)
R-HSA-170159 (Reactome) The localization of the Cdc25A, B and C proteins is dynamic involving the shuttling of these proteins between the nucleus and the cytoplasm. Sequences in these proteins mediate both nuclear export and import (Kallstrom et al., 2005; Lindqvist et al., 2004; Graves et al, 2001; Takizawa and Morgan, 2000).
R-HSA-170161 (Reactome) Activation of the mitotic cyclin:Cdc2 complexes at mitosis requires the removal of the inhibitory phosphate groups on Cdc2. This dephosphorylation is achieved by the activity of the Cdc25 family of phosphatases. The Cdc25 members, Cdc25A, Cdc25B, and Cdc25C are kept inactive during interphase and are activated at the G2/M transition. Cyclin B1:Cdc2 itself appears to participate in the full activation of Cdc25 in a process that involves an amplication loop (see Wolfe and Gould, 2004). The initial activation of the cyclin B1-Cdc2 complex occurs in the cytoplasm in prophase (Jackman et al., 2003). Cdc25B, which is present at highest concentrations in the cytoplasm at this time, is thought to trigger the activation of cyclin B1-Cdc2 (Lindqvist et al. 2004; Honda et al., 1993). Active cyclin B:Cdc2 then phosphorylates and activates Cdc25C and stabilizes Cdc25A (Strausfeld et al., 1994; Hoffman et al.,1993; Mailand et al, 2002). This creates positive feedback loops that allows Cdc25A and Cdc25C to dephosphorylate and further activate Cdc2.
R-HSA-170162 (Reactome) At the beginning of this reaction, 1 molecule of 'Cyclin B2:phospho-Cdc2(Thr 14, Thr 161)', and 1 molecule of 'H2O' are present. At the end of this reaction, 1 molecule of 'Cyclin B2:phospho-Cdc2(Thr 161)', and 1 molecule of 'Orthophosphate' are present.

This reaction takes place in the 'cytosol' and is mediated by the 'phosphoprotein phosphatase activity' of 'Cdc25'.

R-HSA-187937 (Reactome) In G2, the cyclin A:Cdk2 complex associates with E2F1 and E2F3.
R-HSA-187959 (Reactome) In G2 Cdk2, in association with cyclin A, phosphorylates E2F1 and E2F3 resulting in the inactivation and possibly degradation of these two transcription factors (Dynlacht et al., 1994; Krek et al., 1994).
R-HSA-2562526 (Reactome) Activated PLK1 phosphorylates OPTN (optineurin) on serine residue S177. Phosphorylation at S177 disrupts OPTN binding to Golgi-membrane localized RAB8A (Kachaner et al. 2012).
R-HSA-2562594 (Reactome) Phosphorylation of OPTN (optineurin) on serine S177 by PLK1 promotes translocation of OPTN to the nucleus (Kachaner et al. 2012).
R-HSA-2574840 (Reactome) AURKA (Aurora A kinase) activation through autophosphorylation of threonine T288 is facilitated by AJUBA binding. AJUBA is also phosphorylated by AURKA on an unidentified serine or threonine residue (Hirota et al. 2003).
R-HSA-2574845 (Reactome) AJUBA, a LIM domain-containing protein, binds centrosome-associated AURKA (Aurora A kinase) through interaction of LIM-2 and LIM-3 domains of AJUBA with the N-terminus of AURKA (Hirota et al. 2003).
R-HSA-3000310 (Reactome) AURKA (Aurora A kinase) phosphorylates PLK1 on threonine residue T210 that lies in the conserved aurora kinase consensus site (Seki et al. 2008). PLK1 needs to be phosphorylated on T210 to become catalytically active (Jang et al. 2002). BORA, but not other AURKA co-activators, facilitate PLK1 phosphorylation by AURKA (Macurek et al. 2008, Seki et al. 2008).
R-HSA-3000319 (Reactome) BORA is able to interact with both AURKA (Aurora A kinase) and PLK1. Binding of BORA to PLK1 increases the accessibility of PLK1 threonine residue T210 and also brings PLK1 in proximity to AURKA, enabling AURKA to phosphorylate T210 of PLK1 and thereby activate PLK1 (Seki et al. 2008). While BORA is required for mitotic activation of AURKA in Drosophila (Hutterer et al. 2006), it does not significantly activate AURKA in human cells (Seki et al. 2008). AURKA is able to phosphorylate BORA in vitro, but the functional significance of this modification has not been determined (Hutterer et al. 2006).
R-HSA-3000327 (Reactome) PLK1 phosphorylates BORA on serine residue S497 and threonine residue T501 that both lie in the DSGYNT degron recognized by beta-TrCP F-box proteins (Seki et al. 2008).
R-HSA-3000335 (Reactome) SCF-beta-TrCP ubiquitin ligases promote ubiquitination and degradation of BORA phosphorylated by PLK1, and this is required for timely mitotic progression (Seki et al. 2008).
R-HSA-3000339 (Reactome) The substrate recognition subunits beta-TrCP (BTRC) and beta-TrCP2 (FBXW11) of SCF-beta-TrPC1 and SCF-beta-TrPC2 ubiquitin ligases, respectively, bind the phosphorylated DSGYNT motif of BORA (Seki et al. 2008).
R-HSA-3002798 (Reactome) PLK1 is induced in S phase and can be find in both cytosol and nucleus in S and G2 phases of the cell cycle. PLK1 possesses a bipartite nuclear localization signal (NLS) that enables it to enter the nucleus (Taniguchi et al. 2002).
R-HSA-3002811 (Reactome) The myosin phosphatase complex can dephosphorylate PLK1 threonine residue T210 and inactivate PLK1 (Yamashiro et al. 2008). Myosin phosphatase is activated through phosphorylation of its PPP1R12A (MYPT1) subunit. Several kinases, including CDK1 (Yamashiro et al. 2008) and LATS1 (Chiyoda et al. 2012) have been implicated in myosin phosphatase activation, but the position and temporal order of key PPP1R12A phosphorylations need to be investigated further. Phosphorylated OPTN (optineurin) is able to bind PPP1R12A (MYPT1) and positively regulates PLK1 dephosphorylation by myosin phosphatase, posibly by facilitating PPP1R12A phosphorylation and myosin phosphatase activation (Kachaner et al. 2012).
R-HSA-380272 (Reactome) Phosphorylation of NlP by Plk1 regulates the interaction of Nlp with both centrosomes and ?-TuRCs (Casenghi et al., 2003).
R-HSA-380278 (Reactome) After the initiation of DNA condensation during mitosis, NuMA is phosphorylated by Cdc2 kinase and transported rapidly to the centrosomal region (Hsu and Yeh, 1996). Another phosphorylation event occurs when NuMA associates with the mitotic spindle (Gaglio et al., 1995; Hsu and Yeh, 1996). While p34cdc2/cyclin B-dependent phosphorylation appears to plays an essential role in the targeting of NuMA to the spindle apparatus (Compton and Luo, 1995)(Hsu and Yeh, 1996), there may be additional protein kinases that promote the release of NuMA from the nuclear compartment at nuclear envelope breakdown (Saredi et al., 1997).
R-HSA-380283 (Reactome) Microtubule nucleation at the centrosome is mediated by the gamma tubulin ring complex (gamma TuRC) (reviewed in Raynaud-Messina and Merdes, 2006; Wiese and Zheng, 2006). In humans, this large complex contains the tubulin superfamily member gamma-tubulin, five gamma complex proteins (GCP2-GPC6) and NEDD1/GCP-WD. A current model of the arrangement of subunits within the gamma-TuRC proposes that 6-7 TuSC subcomplexes are held together by the other Grip proteins (at an unknown stoichiometry), which together form the cap subunits. In many animal cells, the recruitment of gamma-tubulin complexes to the centrosome rapidly increases (3–5 fold ) before mitosis  to support the formation of new spindle microtubules (Khodjakov and Rieder 1999).  NEDD1/GCP-WD  plays  an essential role in recruitment of these complexes to the centrosomes (Haren et al., 2006;  Luders et al., 2006) and to the mitotic spindle (Luders et al., 2006). GCP-WD/NEDD1  associates directly with the  gamma-TuRC.  The carboxy-terminal half  binds to the gamma-TuRC whereas the amino-terminal half, corresponding to the WD-repeat domain,  is responsible for its attachment to the centrosome (Haren et al., 2006). Additional centrosomal proteins have also been implicated in the docking of gamma-TuRC to the centrosomes. CG-NAP/AKAP450  and kendrin  are  necessary for the initiation of microtubule nucleation and interact  with GCP2/GCP3 and GCP2, respectively (Takahashi et al., 2002).  Pericentrin  plays an important role in  microtubule organization in mitotic cells and anchors gamma- TuRC through domains that bind GCP2 and GCP3  (Zimmerman  et al. 2004). Ninein localizes to the centriole via its C-terminus and interacts with gamma-tubulin-containing complexes via its N-terminus.
R-HSA-380294 (Reactome) The centrosomal protein C-Nap1 is thought to play an important role in centrosome cohesion during interphase (Fry et al.,1998). At the onset of mitosis, when centrosomes separate to form the bipolar spindle, C-Nap1 dissociates (Mayor et al., 2000). Dissociation of C-Nap1 from mitotic centrosomes appears to be regulated by phosphorylation (Mayor et al. 2002).
R-HSA-380303 (Reactome) Mitotic activation of Plk1 is required for efficient displacement of Nlp from the centrosome (Casenghi et al., 2003).
R-HSA-380311 (Reactome) Plk1 is associated with the centrosomes early in mitosis (Golsteyn et al. 1995). Plk1 activity is necessary for the maturation of centrosomes at the G2/M transition and the establishment of a bipolar spindle (Lane and Nigg 1996). Specific inhibitors against Plk1 or silencing of Plk1 produce a monopolar mitotic apparatus (Sumara et al, 2004, van Vugt et al, 2004, McInnes et al, 2006, Peters et al, 2006, Lénárt et al, 2007).
R-HSA-380316 (Reactome) NuMA can interact with microtubules by direct binding to tubulin. Binding occurs through amino acids 1868-1967 of human NuMA (tail IIA) and appears to play a role in the organization of the spindle poles by stably crosslinking microtubule fibers (Haren and Merdes 2002). While the exact mechanism of microtubule bundling is not known, NuMA has been shown to form large fibrous networks (Saredi et al., 1996; Gueth-Hallonet et al., 1998; Harborth et al., 1999) apparently as a result of dimerization of the NuMA rod domains followed by association of multiple NuMA dimers through their tail domains.
R-HSA-380455 (Reactome) CDK11p58 is a kinase that is active during mitosis when it associates with centrosomes, and has a crucial role in centrosome maturation and bipolar spindle formation (Petretti et al., 2006). CDK11p58 facilitates microtubule nucleation and is required for the recruitment of Aurora and Plk1 to the centrosome (Petretti et al., 2006).
R-HSA-380508 (Reactome) The mechanism by which human NuMA is translocated to the centrosomes has not yet been determined.
R-HSA-4086410 (Reactome) CDK1 phosphorylates both human and Drosophila BORA protein (Hutterer et al. 2006) on an evolutionarily conserved serine residue - S252 in human BORA (Chan et al. 2008), providing a docking site for PLK1.
R-HSA-4088024 (Reactome) In the G2 phase of the cell cycle, cyclin A (CCNA) and B (CCNB)-dependent kinases CDK1 and CDK2 phosphorylate FOXM1 transcription factor, increasing its transcriptional activity. Threonine residue T611 (corresponds to T596 in FOXM1B isoform) was shown to be phosphorylated by both CCNA:CDK1/2 and CCNB:CDK1 complexes and its functional relevance is best establshed (Major et al. 2004, Laoukili et al. 2008, Fu et al. 2008). CCNA:CDK1/2 may also phosphorylate FOXM1 on T600 (Laoukili et al. 2008), while CCNB:CDK1 may phosphorylate it on S693 (S678 in FOXM1B isoform) (Fu et al. 2008). The phosphorylation of FOXM1 threonine residue T611 relieves the N-terminal domain-mediated autoinhibition of FOXM1 transcriptional activity (Laoukili et al. 2008), likely enabling interaction with transcriptional co-activators (Major et al. 2004), and creates a docking site for the Polo-box domain (PBD) of PLK1 (Fu et al. 2008).
R-HSA-4088130 (Reactome) PLK1 polo-box domain (PBD) binds a consensus sequence S-pS/pT-P/X in the transactivation domain (TAD) of FOXM1 after the threonine T611 (T596 in FOXM1B isoform) in this sequence is phosphorylated by cyclin-dependent kinase(s). PLK1 may also bind to another consensus site in the TAD of FOXM1, which involves CDK-phosphorylated serine S693 (S678 in FOXM1B isoform) (Fu et al. 2008).
R-HSA-4088134 (Reactome) PLK1 phosphorylates FOXM1 on serine residues S730 and S739 (S715 and S724 in FOXM1B isoform) in the C-terminal transactivation domain (TAD). PLK1-mediated phosphorylation of FOXM1 upregulates FOXM1 transcriptional activity and is crucial for FOXM1 function at G2/M transition (Fu et al. 2008).
R-HSA-4088141 (Reactome) FOXM1 can bind the regulatory subunit B55-alpha (PPP2R2A) of serine/threonine-protein phosphatase 2A (PP2A). PP2A dephosphorylates FOXM1, preventing its premature activation (Alvarez-Fernandez et al. 2011).
R-HSA-4088152 (Reactome) Binding of phosphorylated FOXM1 to CDC25A promoter stimulates CDC25A transcription (Sullivan et al. 2012).
R-HSA-4088162 (Reactome) Phosphorylated FOXM1 transcription factor binds the promoter of CDC25A gene and also recruits EP300 (p300) transcriptional coactivator to the promoter (Sullivan et al. 2012). While FOXM1 DNA binding may not depend on phosphorylation, the phosphorylation of the threonine residue T611 (T596 in FOXM1B isoform) is necessary for EP300 recruitment (Major et al. 2004).
R-HSA-4088298 (Reactome) FOXM1 bound to the MuvB complex (consisting of LIN9, LIN37, LIN52, LIN54 and RBBP4) and MYBL2 (B-MYB) stimulates CCNB1 (cyclin B1) transcription (Laoukili et al. 2005, Sadasivam et al. 2012).
R-HSA-4088299 (Reactome) FOXM1, bound to the MuvB complex (consisting of LIN9, LIN37, LIN52, LIN54 and RBBP4) and MYBL2 (B-MYB), stimulates CCNB2 (cyclin B2) transcription (Chen et al. 2013).
R-HSA-4088305 (Reactome) FOXM1 bound to the MuvB complex (consisting of LIN9, LIN37, LIN52, LIN54 and RBBP4) and MYBL2 (B-MYB) stimulates PLK1 transcription. This creates a positive feedback loop, where PLK1 phosphorylates and activates FOXM1 (Fu et al. 2008), while FOXM1 transcriptional activity results in increased PLK1 levels. MuvB and FOXM1 may persist on the PLK1 promoter throughout G2, while MYBL2 may gradually dissociate from the PLK1 promoter due to proteasome-mediated degradation initiated when MYBL2 is phosphorylated by CCNA (cyclin A)-associated CDKs (Sadasivam et al. 2012).
R-HSA-4088306 (Reactome) MuvB complex, consisting of LIN9, LIN37, LIN52, LIN54 and RBBP4, together with MYBL2 (B-MYB), recruits FOXM1 to CHR (cell cycle genes homology regions) motifs in the promoter of PLK1 gene (Sadasivam et al. 2012, Chen et al. 2013).
R-HSA-4088307 (Reactome) The MuvB complex (consisting of LIN9, LIN37, LIN52, LIN54 and RBBP4), together with MYBL2 (B-MYB), recruits FOXM1 to CHR motifs in the promoter of the CCNB1 (cyclin B1) gene (Sadasivam et al. 2012, Chen et al. 2013).
R-HSA-4088309 (Reactome) MuvB complex (consisting of LIN9, LIN37, LIN52, LIN54 and RBBP4), together with MYBL2 (B-MYB) recruits FOMX1 to the CCNB2 (cyclin B2) promoter (Chen et al. 2013).
R-HSA-4088439 (Reactome) FOXM1, possibly in cooperation with other transcription factors, binds the promoter of the CENPF gene (Laoukili et al. 2005).
R-HSA-4088441 (Reactome) FOXM1 stimulates the transcription of the kinetochore protein CENPF. FOXM1-depleted cells have reduced CENPF levels, leading to the misalignment of mitotic chromosomes (Laoukili et al. 2005).
R-HSA-69754 (Reactome) At the beginning of this reaction, 1 molecule of 'ATP', and 1 molecule of 'G2/M transition protein' are present. At the end of this reaction, 1 molecule of 'ADP', and 1 molecule of 'phospho-G2/M transition protein' are present.

This reaction takes place in the 'nucleoplasm' and is mediated by the 'cyclin-dependent protein kinase activity' of 'Cyclin A1:Cdc2'.

R-HSA-69756 (Reactome) At the beginning of this reaction, 1 molecule of 'ATP', and 1 molecule of 'G2/M transition protein' are present. At the end of this reaction, 1 molecule of 'ADP', and 1 molecule of 'phospho-G2/M transition protein' are present.

This reaction takes place in the 'nucleoplasm' and is mediated by the 'cyclin-dependent protein kinase activity' of 'Cyclin A2:Cdc2'.

R-HSA-69759 (Reactome) Substrate specificity of cyclin B:Cdk1 complexes is primarily conferred by their subcellular localization (Draviam et al., 2001).
Cyclin B1 is primarily cytoplasmic but shuttles continuously between the nucleus and the cytoplasm during interphase (Hagting et al. 1998 Down; Toyoshima et al. 1998 Down; Yang et al. 1998 Down). At the end of prophase, it abruptly translocates into the nucleus (Furuno et al. 1999 Down; Hagting et al. 1999 Down) and then associates with mitotic apparatus (Pines and Hunter 1991 Down; Hagting et al. 1998 Down; Clute and Pines 1999 Down). Cyclin B2 is primarily associated with the Golgi apparatus during interphase and mitosis (Jackman et al. 1995 Down; Brandeis et al. 1998 Down). Cyclin B1–CDK1 promotes chromosome condensation, reorganization microtubule reorgnization, and disassembly of the nuclear lamina and the Golgi apparatus. Cyclin B2–CDK1 functions in disassembly of the Golgi apparatus (Draviam et al., 2001).


RAB8A:GTPArrowR-HSA-2562526 (Reactome)
SCF-beta-TrCp1,2ArrowR-HSA-3000335 (Reactome)
SCF-beta-TrCp1,2R-HSA-3000339 (Reactome)
Ub-p-S252,S497,T501-BORAArrowR-HSA-3000335 (Reactome)
UbR-HSA-3000335 (Reactome)
WEE1R-HSA-156699 (Reactome)
WEE1mim-catalysisR-HSA-170070 (Reactome)
WEE1mim-catalysisR-HSA-170156 (Reactome)
XPO1ArrowR-HSA-170072 (Reactome)
active nuclear

Cyclin B1:Cdc2

complexes		mim-catalysisR-HSA-170157 (Reactome)
cNAP-1 depleted centrosomeArrowR-HSA-380294 (Reactome)
centrosome

containing

phosphorylated Nlp		ArrowR-HSA-380272 (Reactome)
centrosome

containing

phosphorylated Nlp		R-HSA-380303 (Reactome)
centrosome-associated NuMAArrowR-HSA-380508 (Reactome)
centrosome-nucleated microtubulesR-HSA-380316 (Reactome)
centrosome-nucleated microtubulesR-HSA-380508 (Reactome)
centrosomeR-HSA-380272 (Reactome)
centrosomeR-HSA-380283 (Reactome)
centrosomeR-HSA-380294 (Reactome)
centrosomeR-HSA-380311 (Reactome)
centrosomeR-HSA-380455 (Reactome)
cytoplasmic Cyclin B1:Cdc2 complexesR-HSA-170044 (Reactome)
gamma-tubulin complexR-HSA-380283 (Reactome)
nuclear Cyclin B1:Cdc2 complexesArrowR-HSA-170044 (Reactome)
nuclear Cyclin B1:Cdc2 substratesR-HSA-170157 (Reactome)
p-CDK1/2:CCNA/p-T161-CDK1:CCNBmim-catalysisR-HSA-4088024 (Reactome)
p-NINLArrowR-HSA-380303 (Reactome)
p-NUMA1ArrowR-HSA-380278 (Reactome)
p-PKMYT1ArrowR-HSA-162657 (Reactome)
p-S-AJUBAArrowR-HSA-2574840 (Reactome)
p-S177-OPTNArrowR-HSA-2562526 (Reactome)
p-S177-OPTNArrowR-HSA-2562594 (Reactome)
p-S177-OPTNArrowR-HSA-3002811 (Reactome)
p-S177-OPTNR-HSA-2562594 (Reactome)
p-S198-CDC25CArrowR-HSA-156678 (Reactome)
p-S252,S497,T501-BORA:SCF-beta-TrCp1/2ArrowR-HSA-3000339 (Reactome)
p-S252,S497,T501-BORA:SCF-beta-TrCp1/2R-HSA-3000335 (Reactome)
p-S252,S497,T501-BORA:SCF-beta-TrCp1/2mim-catalysisR-HSA-3000335 (Reactome)
p-S252,S497,T501-BORAArrowR-HSA-3000327 (Reactome)
p-S252,S497,T501-BORAR-HSA-3000339 (Reactome)
p-S252-BORA:p-T210-PLK1ArrowR-HSA-3000310 (Reactome)
p-S252-BORA:p-T210-PLK1R-HSA-3000327 (Reactome)
p-S252-BORA:p-T210-PLK1mim-catalysisR-HSA-3000327 (Reactome)
p-S252-BORAArrowR-HSA-4086410 (Reactome)
p-S252-BORAR-HSA-3000319 (Reactome)
p-S53-WEE1ArrowR-HSA-156699 (Reactome)
p-T210-PLK1ArrowR-HSA-3000327 (Reactome)
p-T210-PLK1ArrowR-HSA-3002798 (Reactome)
p-T210-PLK1ArrowR-HSA-4088134 (Reactome)
p-T210-PLK1R-HSA-3002798 (Reactome)
p-T210-PLK1R-HSA-3002811 (Reactome)
p-T210-PLK1R-HSA-4088130 (Reactome)
p-T210-PLK1mim-catalysisR-HSA-2562526 (Reactome)
p-T611,S730,S739-FOXM1:CENPF GeneArrowR-HSA-4088439 (Reactome)
p-T611,S730,S739-FOXM1:CENPF GeneArrowR-HSA-4088441 (Reactome)
p-T611,S730,S739-FOXM1:EP300:CDC25A GeneArrowR-HSA-4088152 (Reactome)
p-T611,S730,S739-FOXM1:EP300:CDC25A GeneArrowR-HSA-4088162 (Reactome)
p-T611,S730,S739-FOXM1:MuvB:MYBL2:CCNB1 GeneArrowR-HSA-4088298 (Reactome)
p-T611,S730,S739-FOXM1:MuvB:MYBL2:CCNB1 GeneArrowR-HSA-4088307 (Reactome)
p-T611,S730,S739-FOXM1:MuvB:MYBL2:CCNB2 GeneArrowR-HSA-4088299 (Reactome)
p-T611,S730,S739-FOXM1:MuvB:MYBL2:CCNB2 GeneArrowR-HSA-4088309 (Reactome)
p-T611,S730,S739-FOXM1:MuvB:MYBL2:PLK1 GeneArrowR-HSA-4088305 (Reactome)
p-T611,S730,S739-FOXM1:MuvB:MYBL2:PLK1 GeneArrowR-HSA-4088306 (Reactome)
p-T611,S730,S739-FOXM1ArrowR-HSA-4088134 (Reactome)
p-T611,S730,S739-FOXM1R-HSA-4088162 (Reactome)
p-T611,S730,S739-FOXM1R-HSA-4088306 (Reactome)
p-T611,S730,S739-FOXM1R-HSA-4088307 (Reactome)
p-T611,S730,S739-FOXM1R-HSA-4088309 (Reactome)
p-T611,S730,S739-FOXM1R-HSA-4088439 (Reactome)
p-T611-FOXM1:p-T210-PLK1ArrowR-HSA-4088130 (Reactome)
p-T611-FOXM1:p-T210-PLK1R-HSA-4088134 (Reactome)
p-T611-FOXM1:p-T210-PLK1mim-catalysisR-HSA-4088134 (Reactome)
p-T611-FOXM1ArrowR-HSA-4088024 (Reactome)
p-T611-FOXM1R-HSA-4088130 (Reactome)
p-T611-FOXM1R-HSA-4088141 (Reactome)
phospho-Cyclin B1(CRS):phospho-Cdc2 (Thr 161)ArrowR-HSA-170131 (Reactome)
phospho-G2/M transition proteinArrowR-HSA-69756 (Reactome)
phospho-G2/M transition proteinArrowR-HSA-69759 (Reactome)
phospho-cyclin B1(CRS):phosph-Cdc2(Thr 161)R-HSA-170131 (Reactome)
phosphorylated

nuclear Cyclin

B1:Cdc2 substrates		ArrowR-HSA-170157 (Reactome)
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