Mitotic G2-G2/M phases (Homo sapiens)

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81124352, 16, 20, 36239274, 12, 1918, 32, 3321, 2928131341021, 2914, 313342265152511162647915, 17, 3018, 33E2F1/E2F3 Cyclin BCdc2 complex nucleoplasmCyclin Aphospho-Cdk2NuMA-bound microtubules centrosome containing phosphorylated Nlp gamma-TuSC RAB8AGTP centrosome-nucleated microtubules Cyclin Aphospho-Cdc2Cyclin Aphospho-Cdk2centrosome-nucleated microtubules Cyclin Aphospho-Cdc2Golgi membranephospho-Cyclin B1nuclear Cyclin B1phospho-Cdc2 gamma-TuSC p-T161-CDK1CCNB1 Cyclin B1phospho-Cdc2gamma-tubulin complex gamma-tubulin complex Cyclin Aphospho-Cdc2nuclear Cyclin B1Cdc2 complexes gamma-TuSC NuMA homodimer RAB8AGTP Cyclin B1phospho-Cdc2Centrosome associated Plk1 phospho-cyclin B1nuclear Cyclin B1phospho-Cdc2 Cyclin B2phospho-Cdc2gamma-tubulin complex gamma-TuSC Cyclin B1phospho-Cdc2phospho-Cdc2Cyclin Aphospho-Cdk2centrosome Cyclin ACdc2 Mature centrosomes enriched in gamma-TURC complexes gamma-tubulin complex cNAP-1 depleted centrosome OPTNRAB8AGTP CAK Cyclin Aphospho-Cdk2Centrosomes containing recruited CDK11p58 phospho-Cyclin B1phospho-Cdc2Nlp-depleted centrosome phospho-cyclin B1centrosome-nucleated microtubules Phosphorylated Myosin Phosphatase Cyclin Aphospho-Cdk2gamma-tubulin complex Cyclin B2phospho-Cdc2cytosolcentrosome Cyclin A2phospho-Cdc2NuMA homodimer Cyclin B gamma-TuSC Cyclin Bphospho-Cdc2Phospho-Cyclin B1 Cyclin A1phospho-Cdc2cytoplasmic Cyclin B1Cdc2 complexes Cyclin B Cyclin B1phospho-Cdc2centrosome-associated NuMA phospho-E2F1/E2F3 Cyclin B1phospho-Cdc2centrosome Cyclin Aphospho-Cdc2Cyclin B1phospho-Cdc2 NuMA homodimer Cyclin B1phospho-Cdc2 centrosome ATPCEP41 DCTN1-2 ALMS1 PLK1 CCP110 HAUS2 CLASP1 OFD1 CDK5RAP2 CSNK1D active nuclear Cyclin B1Cdc2 complexesDYNC1I2 PCM1 SFI1 AZI1 ALMS1 Cyclin AATPADPCSNK1E cNAP-1 depleted centrosomePLK4 Cyclin B2phospho-Cdc2CDK1 SFI1 TUBB4A CEP76 DYNC1I2 CEP78 OPTN TUBB YWHAGp-NUMA1 DCTN1-2 p-T14,T161-CDK1 CCNB1 CEP192 CKAP5 GTP DYNC1I2 H2ODCTN3ADPCEP78 p-T210-PLK1TUBGCP6 ODF2 p-NUMA1 TUBGCP2 NEK2 CDK1 CEP41 CDC25CDYNC1I2 CEP57 NEDD1 CEP290 ATPCNTRL TUBA1A CEP70 CEP192 CEP70 TUBB4A CEP76 TUBA4A MNAT1 NINL MAPRE1 HAUS2 p-S177-OPTNCEP250 NEK2 Cyclin Aphospho-Cdk2TUBGCP5 phospho-G2/M transition proteinPLK1 CEP57 DYNC1H1 TUBGCP3 MAPRE1 AZI1 OFD1 CDK1 Cyclin B1phospho-Cdc2CCNB1 PRKACA NINL p-T161-CDK1 TUBB PAFAH1B1ALMS1 gamma-tubulin complexp-T160-CDK2 p-T161-CDK1 ATPCEP290 PCM1 CEP164 TUBB ADPPRKAR2B DCTN1-2 DCTN2 CCNB1 p-NINLAKAP9 CEP152 YWHAGCEP76 CEP135 nuclear Cyclin B1Cdc2 complexesCDK1 PCNT CDK5RAP2 G2/M transition proteinsTUBGCP2 CSNK1D E2F1 p-4S-CCNB1 TUBB4B CEP57 p-NINL GTP CENPJ CCNB1 p-T14,T161-CDK1 PLK4 p-S177-OPTNCEP63 PRKAR2B NEDD1 CSNK1D DYNC1H1 CDK5RAP2 ADPPAFAH1B1CSNK1D SSNA1 CEP135 ALMS1 CDK5RAP2 PKMYT1p-S198-CDC25CCKAP5 TUBA1A TUBB4B DYNC1H1 CLASP1 TUBGCP2 CEP41 ADPCEP152 PLK4 AKAP9 CEP70 PRKACA CETN2 CEP78 CEP250 NDE1 ADPPCNT CSNK1E p-T14-CDK1 p-E2F3 CEP63 PLK4 Cyclin Aphospho-Cdc2PAFAH1B1CEP192 centrosome containing phosphorylated NlpPPP2R1AHAUS2 CDK11p58E2F3 AKAP9 CEP70 NDE1 p-4S-CCNB1 FGFR1OPYWHAGHAUS2 CSNK1E CSNK1E CENPJ PLK4 Cdc25phospho-G2/M transition proteinSSNA1 Phosphorylated Myosin Phosphatasep-T14,T161-CDK1 NEK2 SSNA1 FGFR1OPAZI1 TUBGCP5 CLASP1 CEP152 OFD1 TUBG1 TUBGCP2 PLK1 TUBGCP4 PRKAR2B CCNH CENPJ SFI1 PLK1 AZI1 ACTR1A Nlp-depleted centrosomeYWHAE TUBGCP6 CCNB1 H2OPCNT CCNB1 CEP41 p-T14,Y15,T161-CDK1 ADPCEP72 Cyclin A1Cdk2 phosphorylated G2/M transition proteinTUBGCP5 p-T14-CDK1 CEP192 p-T161-CDK1 DYNLL1 YWHAGCCNA1 NEDD1 ODF2 TUBGCP4 CCNB2 FGFR1OPCEP70 PCM1 YWHAE NEK2 CEP41 Cyclin Aphospho-Cdk2CEP41 G2/M transition proteinsODF2 p-T210-PLK1Cdc25TUBGCP3 CEP63 TUBGCP3 SFI1 DCTN1-2 CENPJ HSP90AA1 PRKAR2B DYNLL1 CEP72 TUBA4A Cyclin A2phospho-Cdc2TUBGCP4 CENPJ Cyclin A1phospho-Cdc2p-T161-CDK1 PCNT YWHAE PRKACA DCTN1-2 Cyclin Aphospho-Cdc2HAUS2 OFD1 CETN2 ACTR1A RAB8AGTPCEP152 NINL phospho-cyclin B1CEP135 PLK1 SSNA1 CETN2 TUBA1A AKAP9 CDK5RAP2 CETN2 PLK4 Cyclin B1phospho-Cdc2p-T14-CDK1 p-T14-CDK1 TUBB4A YWHAGRAB8A CRS kinaseCyclin A2Cdk2 phosphorylated G2/M transition proteinCyclin B2phospho-Cdc2CCNA2 ADPCCP110 TUBA4A SFI1 ADPADPCLASP1 CEP164 CEP76 ADPCAKNDE1 CEP164 CSNK1D CEP70 FGFR1OPTUBG2 CEP57 CETN2 ALMS1 CCP110 CEP78 PLK4 DCTN2 CDK1 CDK5RAP2 DCTN2 ATPp-T161-CDK1 CCNB1 PAFAH1B1Phospho-Cyclin B1 DYNLL1 TUBGCP4 TUBA4A TUBGCP6 HSP90AA1 TUBA4A TUBGCP4 CEP76 H2Op-T161-CDK1 TUBG1 XPO1ACTR1A CCP110 CNTRL PAFAH1B1p-4S-CCNB1 p-T161-CDK1 SFI1 NEDD1 TUBB4B AKAP9 Cyclin Bphospho-Cdc2PLK1 DCTN3CEP72 CCNB2 ATPMAPRE1 Cyclin BPRKAR2B ODF2 PLK1p-T14,Y15,T161-CDK1 SSNA1 CEP192 p-T14,Y15,T161-CDK1 TUBB DCTN2 CEP63 CEP192 DYNC1I2 NEDD1 TUBG2 CENPJ Cdc25CEP290 p-T160-CDK2 CDK1 PRKACA Centrosome associated Plk1CEP57 TUBG1 p-NUMA1 phosphorylated nuclear Cyclin B1Cdc2 substratesPiTUBB CNTRL SSNA1 ODF2 DYNC1H1 cytoplasmic Cyclin B1Cdc2 complexesADPALMS1 CKAP5 ATPPCNT CEP164 HSP90AA1 ODF2 ATPPPP2R1ACCP110 ATPMature centrosomes enriched in gamma-TURC complexesFGFR1OPCEP78 SDCCAG8 TUBG2 PPP1CB ATPCEP164 TUBGCP6 ALMS1 CDK5RAP2 CDK1 TUBG1 PLK1Cyclin Aphospho-Cdc2CCP110 NEDD1 OFD1 PiCEP290 HSP90AA1 p-T14,Y15,T161-CDK1 TUBGCP6 DYNC1H1 CEP76 PRKACA p-T161-CDK1 MAPRE1 PKMYT1p-T14-CDK1 PiTUBG1 PPP2R1ADCTN3NDE1 CKAP5 p-T161-CDK1 PPP2R1Ap-T161-CDK1 CEP135 CEP63 TUBA1A p-PKMYT1TUBB4B TUBB4A OPTNRAB8AGTPDYNLL1 CEP250 centrosomeSDCCAG8 CEP250 Cyclin Aphospho-Cdc2ODF2 YWHAGPCM1 MAPRE1 H2OYWHAE HSP90AA1 CEP57 Cyclin B1phospho-Cdc2CEP290 TUBGCP5 centrosome-associated NuMAPRKAR2B CSNK1D p-S473-PPP1R12A MAPRE1 CDC25CADPWEE1HAUS2 TUBB HAUS2 Cyclin BCdc2 complexCETN2 NEK2 NuMA homodimerTUBA1A CEP290 TUBA4A TUBB4B AZI1 TUBB4A ATPAKAP9 CEP250NEDD1 DYNC1I2 DCTN2 DCTN3NEK2 NUMA1NEDD1 CDK1YWHAGCEP76 SDCCAG8 CEP78 CDK1 OFD1 PPP2R1ACEP164 CKAP5 SDCCAG8 ACTR1A CCNB1 ATPNEK2 CEP250 CDK7 TUBB H2OYWHAE NDE1 PAFAH1B1CDC25BCyclin ACdc2PRKACA AKAP9 CEP135 p-S53-WEE1ACTR1A PCM1 p-4S-CCNB1 DCTN2 NEDD1 SDCCAG8 G2/M transition proteinCEP135 CEP152 HSP90AA1 p-NUMA1Centrosomes containing recruited CDK11p58CEP72 PCNT NEDD1 TUBB4A ATPPPP2R1ATUBG2 p-T161-CDK1 TUBG1 CDK1 PCNT DCTN1-2 p-T161-CDK1CCNB1CEP192 YWHAE NINL PCM1 CEP135 CEP72 CNTRL SDCCAG8 CSNK1E PRKAR2B NuMA-bound microtubulesDCTN1-2 CETN2 p-T160-CDK2 TUBGCP5 SDCCAG8 NDE1 CSNK1E CLASP1 PPP1R12B-4 CLASP1 RAB8A PCM1 CEP57 NINL p-4S-CCNB1 phospho-Cyclin B1TUBG1 CEP78 p-E2F1 DYNLL1 CNTRL nuclear Cyclin B1phospho-Cdc2 TUBG1 nuclear Cyclin B1Cdc2 substratesCCNB1 Cyclin B1phospho-Cdc2 YWHAE CSNK1D CEP41 PAFAH1B1DYNC1H1 CNTRL PRKACA CEP250 ADPTUBG1 phospho-Cdc2TUBG1 p-T14,Y15,T161-CDK1 DCTN2 CENPJ TUBA1A PLK1CCNB2 CEP152 TUBB4B E2F1/E2F3CEP164 CKAP5 TUBG1 MAPRE1 CEP72 TUBGCP3 CKAP5 PLK1 DYNC1H1 CCP110 DYNC1I2 TUBG2 DCTN3DCTN3CEP63 CLASP1 centrosome-nucleated microtubulesPPP2R1AFGFR1OPPiACTR1A TUBA1A CEP63 ATPFGFR1OPDCTN3TUBA4A CEP290 TUBGCP2 HSP90AA1 CCNB1 AZI1 NEDD1 CSNK1E CCNB2 TUBB4B OFD1 CEP70 CEP72 ADPCEP152 CNTRL NDE1 p-T14-CDK1 DYNLL1 ATPAZI1 SFI1 CDC25BSSNA1 TUBGCP3 Cyclin Aphospho-Cdk2TUBB4A DYNLL1 ACTR1A


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  1. Bublik DR, Scolz M, Triolo G, Monte M, Schneider C.; ''Human GTSE-1 regulates p21(CIP1/WAF1) stability conferring resistance to paclitaxel treatment.''; PubMed Europe PMC Scholia
  2. Chiyoda T, Sugiyama N, Shimizu T, Naoe H, Kobayashi Y, Ishizawa J, Arima Y, Tsuda H, Ito M, Kaibuchi K, Aoki D, Ishihama Y, Saya H, Kuninaka S.; ''LATS1/WARTS phosphorylates MYPT1 to counteract PLK1 and regulate mammalian mitotic progression.''; PubMed Europe PMC Scholia
  3. Chan EH, Santamaria A, Silljé HH, Nigg EA.; ''Plk1 regulates mitotic Aurora A function through betaTrCP-dependent degradation of hBora.''; PubMed Europe PMC Scholia
  4. Strausfeld U, Labbé JC, Fesquet D, Cavadore JC, Picard A, Sadhu K, Russell P, Dorée M.; ''Dephosphorylation and activation of a p34cdc2/cyclin B complex in vitro by human CDC25 protein.''; PubMed Europe PMC Scholia
  5. Kruiswijk F, Labuschagne CF, Vousden KH.; ''p53 in survival, death and metabolic health: a lifeguard with a licence to kill.''; PubMed Europe PMC Scholia
  6. Källström H, Lindqvist A, Pospisil V, Lundgren A, Rosenthal CK.; ''Cdc25A localisation and shuttling: characterisation of sequences mediating nuclear export and import.''; PubMed Europe PMC Scholia
  7. Bonnet J, Mayonove P, Morris MC.; ''Differential phosphorylation of Cdc25C phosphatase in mitosis.''; PubMed Europe PMC Scholia
  8. Seki A, Coppinger JA, Du H, Jang CY, Yates JR, Fang G.; ''Plk1- and beta-TrCP-dependent degradation of Bora controls mitotic progression.''; PubMed Europe PMC Scholia
  9. Parker LL, Piwnica-Worms H.; ''Inactivation of the p34cdc2-cyclin B complex by the human WEE1 tyrosine kinase.''; PubMed Europe PMC Scholia
  10. Macůrek L, Lindqvist A, Lim D, Lampson MA, Klompmaker R, Freire R, Clouin C, Taylor SS, Yaffe MB, Medema RH.; ''Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery.''; PubMed Europe PMC Scholia
  11. Strausfeld U, Fernandez A, Capony JP, Girard F, Lautredou N, Derancourt J, Labbe JC, Lamb NJ.; ''Activation of p34cdc2 protein kinase by microinjection of human cdc25C into mammalian cells. Requirement for prior phosphorylation of cdc25C by p34cdc2 on sites phosphorylated at mitosis.''; PubMed Europe PMC Scholia
  12. Hirota T, Kunitoku N, Sasayama T, Marumoto T, Zhang D, Nitta M, Hatakeyama K, Saya H.; ''Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells.''; PubMed Europe PMC Scholia
  13. Seki A, Coppinger JA, Jang CY, Yates JR, Fang G.; ''Bora and the kinase Aurora a cooperatively activate the kinase Plk1 and control mitotic entry.''; PubMed Europe PMC Scholia
  14. Bruinsma W, Raaijmakers JA, Medema RH.; ''Switching Polo-like kinase-1 on and off in time and space.''; PubMed Europe PMC Scholia
  15. Alvarez-Fernández M, Halim VA, Aprelia M, Laoukili J, Mohammed S, Medema RH.; ''Protein phosphatase 2A (B55α) prevents premature activation of forkhead transcription factor FoxM1 by antagonizing cyclin A/cyclin-dependent kinase-mediated phosphorylation.''; PubMed Europe PMC Scholia
  16. McGowan CH, Russell P.; ''Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15.''; PubMed Europe PMC Scholia
  17. Xu M, Sheppard KA, Peng CY, Yee AS, Piwnica-Worms H.; ''Cyclin A/CDK2 binds directly to E2F-1 and inhibits the DNA-binding activity of E2F-1/DP-1 by phosphorylation.''; PubMed Europe PMC Scholia
  18. Jang YJ, Ma S, Terada Y, Erikson RL.; ''Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase.''; PubMed Europe PMC Scholia
  19. Xing Y, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi Y.; ''Structural mechanism of demethylation and inactivation of protein phosphatase 2A.''; PubMed Europe PMC Scholia
  20. Kumagai A, Dunphy WG.; ''Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts.''; PubMed Europe PMC Scholia
  21. Krek W, Ewen ME, Shirodkar S, Arany Z, Kaelin WG, Livingston DM.; ''Negative regulation of the growth-promoting transcription factor E2F-1 by a stably bound cyclin A-dependent protein kinase.''; PubMed Europe PMC Scholia
  22. Laoukili J, Alvarez M, Meijer LA, Stahl M, Mohammed S, Kleij L, Heck AJ, Medema RH.; ''Activation of FoxM1 during G2 requires cyclin A/Cdk-dependent relief of autorepression by the FoxM1 N-terminal domain.''; PubMed Europe PMC Scholia
  23. Yu D, Jing T, Liu B, Yao J, Tan M, McDonnell TJ, Hung MC.; ''Overexpression of ErbB2 blocks Taxol-induced apoptosis by upregulation of p21Cip1, which inhibits p34Cdc2 kinase.''; PubMed Europe PMC Scholia
  24. Mailand N, Podtelejnikov AV, Groth A, Mann M, Bartek J, Lukas J.; ''Regulation of G(2)/M events by Cdc25A through phosphorylation-dependent modulation of its stability.''; PubMed Europe PMC Scholia
  25. Voges D, Zwickl P, Baumeister W.; ''The 26S proteasome: a molecular machine designed for controlled proteolysis.''; PubMed Europe PMC Scholia
  26. Sakchaisri K, Asano S, Yu LR, Shulewitz MJ, Park CJ, Park JE, Cho YW, Veenstra TD, Thorner J, Lee KS.; ''Coupling morphogenesis to mitotic entry.''; PubMed Europe PMC Scholia
  27. Liu D, Liao C, Wolgemuth DJ.; ''A role for cyclin A1 in the activation of MPF and G2-M transition during meiosis of male germ cells in mice.''; PubMed Europe PMC Scholia
  28. Scolz M, Widlund PO, Piazza S, Bublik DR, Reber S, Peche LY, Ciani Y, Hubner N, Isokane M, Monte M, Ellenberg J, Hyman AA, Schneider C, Bird AW.; ''GTSE1 is a microtubule plus-end tracking protein that regulates EB1-dependent cell migration.''; PubMed Europe PMC Scholia
  29. Mailand N, Falck J, Lukas C, Syljuâsen RG, Welcker M, Bartek J, Lukas J.; ''Rapid destruction of human Cdc25A in response to DNA damage.''; PubMed Europe PMC Scholia
  30. Teixidó-Travesa N, Villén J, Lacasa C, Bertran MT, Archinti M, Gygi SP, Caelles C, Roig J, Lüders J.; ''The gammaTuRC revisited: a comparative analysis of interphase and mitotic human gammaTuRC redefines the set of core components and identifies the novel subunit GCP8.''; PubMed Europe PMC Scholia
  31. Hagting A, Karlsson C, Clute P, Jackman M, Pines J.; ''MPF localization is controlled by nuclear export.''; PubMed Europe PMC Scholia
  32. Nakajima H, Toyoshima-Morimoto F, Taniguchi E, Nishida E.; ''Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate.''; PubMed Europe PMC Scholia
  33. Fu Z, Malureanu L, Huang J, Wang W, Li H, van Deursen JM, Tindall DJ, Chen J.; ''Plk1-dependent phosphorylation of FoxM1 regulates a transcriptional programme required for mitotic progression.''; PubMed Europe PMC Scholia
  34. Lindqvist A, Källström H, Karlsson Rosenthal C.; ''Characterisation of Cdc25B localisation and nuclear export during the cell cycle and in response to stress.''; PubMed Europe PMC Scholia
  35. Scrofani J, Sardon T, Meunier S, Vernos I.; ''Microtubule nucleation in mitosis by a RanGTP-dependent protein complex.''; PubMed Europe PMC Scholia
  36. Takizawa CG, Weis K, Morgan DO.; ''Ran-independent nuclear import of cyclin B1-Cdc2 by importin beta.''; PubMed Europe PMC Scholia
  37. Xu X, Wang X, Xiao Z, Li Y, Wang Y.; ''Two TPX2-dependent switches control the activity of Aurora A.''; PubMed Europe PMC Scholia
  38. Honda R, Ohba Y, Nagata A, Okayama H, Yasuda H.; ''Dephosphorylation of human p34cdc2 kinase on both Thr-14 and Tyr-15 by human cdc25B phosphatase.''; PubMed Europe PMC Scholia
  39. Maxwell CA, Keats JJ, Belch AR, Pilarski LM, Reiman T.; ''Receptor for hyaluronan-mediated motility correlates with centrosome abnormalities in multiple myeloma and maintains mitotic integrity.''; PubMed Europe PMC Scholia
  40. Mayor T, Stierhof YD, Tanaka K, Fry AM, Nigg EA.; ''The centrosomal protein C-Nap1 is required for cell cycle-regulated centrosome cohesion.''; PubMed Europe PMC Scholia
  41. Yamashiro S, Yamakita Y, Totsukawa G, Goto H, Kaibuchi K, Ito M, Hartshorne DJ, Matsumura F.; ''Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1.''; PubMed Europe PMC Scholia
  42. Vousden KH, Prives C.; ''Blinded by the Light: The Growing Complexity of p53.''; PubMed Europe PMC Scholia
  43. Sadasivam S, Duan S, DeCaprio JA.; ''The MuvB complex sequentially recruits B-Myb and FoxM1 to promote mitotic gene expression.''; PubMed Europe PMC Scholia
  44. Jackman M, Firth M, Pines J.; ''Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus.''; PubMed Europe PMC Scholia
  45. Dodson CA, Bayliss R.; ''Activation of Aurora-A kinase by protein partner binding and phosphorylation are independent and synergistic.''; PubMed Europe PMC Scholia
  46. Taniguchi E, Toyoshima-Morimoto F, Nishida E.; ''Nuclear translocation of plk1 mediated by its bipartite nuclear localization signal.''; PubMed Europe PMC Scholia
  47. Shi P, Zhu S, Lin Y, Liu Y, Liu Y, Chen Z, Shi Y, Qian Y.; ''Persistent stimulation with interleukin-17 desensitizes cells through SCFβ-TrCP-mediated degradation of Act1.''; PubMed Europe PMC Scholia
  48. Sen I, Veprintsev D, Akhmanova A, Steinmetz MO.; ''End binding proteins are obligatory dimers.''; PubMed Europe PMC Scholia
  49. Johnson EO, Chang KH, de Pablo Y, Ghosh S, Mehta R, Badve S, Shah K.; ''PHLDA1 is a crucial negative regulator and effector of Aurora A kinase in breast cancer.''; PubMed Europe PMC Scholia
  50. Petretti C, Savoian M, Montembault E, Glover DM, Prigent C, Giet R.; ''The PITSLRE/CDK11p58 protein kinase promotes centrosome maturation and bipolar spindle formation.''; PubMed Europe PMC Scholia
  51. De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J.; ''Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue.''; PubMed Europe PMC Scholia
  52. Wang G, Jiang Q, Zhang C.; ''The role of mitotic kinases in coupling the centrosome cycle with the assembly of the mitotic spindle.''; PubMed Europe PMC Scholia
  53. Liu Y, Lear T, Zhao Y, Zhao J, Zou C, Chen BB, Mallampalli RK.; ''F-box protein Fbxl18 mediates polyubiquitylation and proteasomal degradation of the pro-apoptotic SCF subunit Fbxl7.''; PubMed Europe PMC Scholia
  54. Hutterer A, Berdnik D, Wirtz-Peitz F, Zigman M, Schleiffer A, Knoblich JA.; ''Mitotic activation of the kinase Aurora-A requires its binding partner Bora.''; PubMed Europe PMC Scholia
  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
114706view16:18, 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...
NameTypeDatabase referenceComment
ACTR1A ProteinP61163 (Uniprot-TrEMBL)
ADPMetaboliteCHEBI:16761 (ChEBI)
AKAP9 ProteinQ99996 (Uniprot-TrEMBL)
ALMS1 ProteinQ8TCU4 (Uniprot-TrEMBL)
ATPMetaboliteCHEBI:15422 (ChEBI)
AZI1 ProteinQ9UPN4 (Uniprot-TrEMBL)
CAKComplexREACT_5717 (Reactome)
CCNA1 ProteinP78396 (Uniprot-TrEMBL)
CCNA2 ProteinP20248 (Uniprot-TrEMBL)
CCNB1 ProteinP14635 (Uniprot-TrEMBL)
CCNB2 ProteinO95067 (Uniprot-TrEMBL)
CCNH ProteinP51946 (Uniprot-TrEMBL)
CCP110 ProteinO43303 (Uniprot-TrEMBL)
CDC25BProteinP30305 (Uniprot-TrEMBL)
CDC25CProteinP30307 (Uniprot-TrEMBL)
CDK1 ProteinP06493 (Uniprot-TrEMBL)
CDK11p58ProteinREACT_16059 (Reactome)
CDK1ProteinP06493 (Uniprot-TrEMBL)
CDK5RAP2 ProteinQ96SN8 (Uniprot-TrEMBL)
CDK7 ProteinP50613 (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 kinaseREACT_6373 (Reactome)
CSNK1D ProteinP48730 (Uniprot-TrEMBL)
CSNK1E ProteinP49674 (Uniprot-TrEMBL)
Cdc25REACT_3533 (Reactome)
Cdc25ProteinREACT_6588 (Reactome)
Cdc25ProteinREACT_9309 (Reactome)
Centrosome associated Plk1ComplexREACT_18209 (Reactome)
Centrosomes containing recruited CDK11p58ComplexREACT_17657 (Reactome)
Cyclin A Cdc2ComplexREACT_6461 (Reactome)
Cyclin A phospho-Cdc2ComplexREACT_6613 (Reactome)
Cyclin A phospho-Cdc2ComplexREACT_6620 (Reactome)
Cyclin A phospho-Cdc2ComplexREACT_6644 (Reactome)
Cyclin A phospho-Cdc2ComplexREACT_6673 (Reactome)
Cyclin A phospho-Cdk2ComplexREACT_9177 (Reactome)
Cyclin A phospho-Cdk2ComplexREACT_9267 (Reactome)
Cyclin A phospho-Cdk2ComplexREACT_9292 (Reactome)
Cyclin A1 Cdk2 phosphorylated G2/M transition proteinREACT_23084 (Reactome)
Cyclin A1 phospho-Cdc2ComplexREACT_4408 (Reactome)
Cyclin A2 Cdk2 phosphorylated G2/M transition proteinREACT_22726 (Reactome)
Cyclin A2 phospho-Cdc2ComplexREACT_4651 (Reactome)
Cyclin AProteinREACT_6541 (Reactome)
Cyclin B Cdc2 complexComplexREACT_6447 (Reactome)
Cyclin B phospho-Cdc2ComplexREACT_6524 (Reactome)
Cyclin B1 phospho-Cdc2 ComplexREACT_6474 (Reactome)
Cyclin B1 phospho-Cdc2ComplexREACT_3166 (Reactome)
Cyclin B1 phospho-Cdc2ComplexREACT_6566 (Reactome)
Cyclin B1 phospho-Cdc2ComplexREACT_6704 (Reactome)
Cyclin B2 phospho-Cdc2ComplexREACT_4066 (Reactome)
Cyclin B2 phospho-Cdc2ComplexREACT_6445 (Reactome)
Cyclin BProteinREACT_6593 (Reactome)
DCTN1-2 ProteinQ14203-2 (Uniprot-TrEMBL)
DCTN2 ProteinQ13561 (Uniprot-TrEMBL)
DCTN3ProteinO75935 (Uniprot-TrEMBL)
DYNC1H1 ProteinQ14204 (Uniprot-TrEMBL)
DYNC1I2 ProteinQ13409 (Uniprot-TrEMBL)
DYNLL1 ProteinP63167 (Uniprot-TrEMBL)
E2F1 ProteinQ01094 (Uniprot-TrEMBL)
E2F1/E2F3REACT_9082 (Reactome)
E2F3 ProteinO00716 (Uniprot-TrEMBL)
FGFR1OPProteinO95684 (Uniprot-TrEMBL)
G2/M transition proteinREACT_2998 (Reactome)
G2/M transition proteinsREACT_22572 (Reactome)
G2/M transition proteinsREACT_23060 (Reactome)
GTP MetaboliteCHEBI:15996 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HAUS2 ProteinQ9NVX0 (Uniprot-TrEMBL)
HSP90AA1 ProteinP07900 (Uniprot-TrEMBL)
MAPRE1 ProteinQ15691 (Uniprot-TrEMBL)
MNAT1 ProteinP51948 (Uniprot-TrEMBL)
Mature centrosomes enriched in gamma-TURC complexesComplexREACT_15605 (Reactome)
NDE1 ProteinQ9NXR1 (Uniprot-TrEMBL)
NEDD1 ProteinQ8NHV4 (Uniprot-TrEMBL)
NEK2 ProteinP51955 (Uniprot-TrEMBL)
NINL ProteinQ9Y2I6 (Uniprot-TrEMBL)
NUMA1ProteinQ14980 (Uniprot-TrEMBL)
Nlp-depleted centrosomeComplexREACT_18075 (Reactome)
NuMA homodimerComplexREACT_15940 (Reactome)
NuMA-bound microtubulesComplexREACT_18043 (Reactome)
ODF2 ProteinQ5BJF6 (Uniprot-TrEMBL)
OFD1 ProteinO75665 (Uniprot-TrEMBL)
OPTN

RAB8A

GTP		ComplexREACT_161318 (Reactome)
OPTN ProteinQ96CV9 (Uniprot-TrEMBL)
PAFAH1B1ProteinP43034 (Uniprot-TrEMBL)
PCM1 ProteinQ15154 (Uniprot-TrEMBL)
PCNT ProteinO95613 (Uniprot-TrEMBL)
PKMYT1ProteinQ99640 (Uniprot-TrEMBL)
PLK1 ProteinP53350 (Uniprot-TrEMBL)
PLK1ProteinP53350 (Uniprot-TrEMBL)
PLK4 ProteinO00444 (Uniprot-TrEMBL)
PPP1CB ProteinP62140 (Uniprot-TrEMBL)
PPP1R12B-4 ProteinO60237-4 (Uniprot-TrEMBL)
PPP2R1AProteinP30153 (Uniprot-TrEMBL)
PRKACA ProteinP17612 (Uniprot-TrEMBL)
PRKAR2B ProteinP31323 (Uniprot-TrEMBL)
Phospho-Cyclin B1 ComplexREACT_6578 (Reactome)
Phosphorylated Myosin PhosphataseComplexREACT_160462 (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 GTPComplexREACT_160437 (Reactome)
RAB8A ProteinP61006 (Uniprot-TrEMBL)
SDCCAG8 ProteinQ86SQ7 (Uniprot-TrEMBL)
SFI1 ProteinA8K8P3 (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)
WEE1ProteinP30291 (Uniprot-TrEMBL)
XPO1ProteinO14980 (Uniprot-TrEMBL)
YWHAE ProteinP62258 (Uniprot-TrEMBL)
YWHAGProteinP61981 (Uniprot-TrEMBL)
active nuclear Cyclin B1 Cdc2 complexesREACT_6519 (Reactome)
cNAP-1 depleted centrosomeComplexREACT_17186 (Reactome)
centrosome containing phosphorylated NlpComplexREACT_17093 (Reactome)
centrosome-associated NuMAComplexREACT_15920 (Reactome)
centrosome-nucleated microtubulesComplexREACT_16122 (Reactome)
centrosomeComplexREACT_15979 (Reactome)
cytoplasmic Cyclin B1 Cdc2 complexesComplexREACT_6372 (Reactome)
gamma-tubulin complexComplexREACT_15704 (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 complexesComplexREACT_6641 (Reactome)
nuclear Cyclin B1 Cdc2 substratesREACT_6526 (Reactome)
nuclear Cyclin B1 phospho-Cdc2 ComplexREACT_6390 (Reactome)
p-4S-CCNB1 ProteinP14635 (Uniprot-TrEMBL)
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-S177-OPTNProteinQ96CV9 (Uniprot-TrEMBL)
p-S198-CDC25CProteinP30307 (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 CCNB1ComplexREACT_6540 (Reactome)
p-T161-CDK1 ProteinP06493 (Uniprot-TrEMBL)
p-T210-PLK1ProteinP53350 (Uniprot-TrEMBL)
phospho-Cdc2ComplexREACT_6681 (Reactome)
phospho-Cyclin B1ComplexREACT_6646 (Reactome)
phospho-G2/M transition proteinREACT_3843 (Reactome)
phospho-G2/M transition proteinREACT_4658 (Reactome)
phospho-cyclin B1ComplexREACT_6436 (Reactome)
phosphorylated nuclear Cyclin B1 Cdc2 substratesREACT_8297 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
ADPArrowREACT_15386 (Reactome)
ADPArrowREACT_15543 (Reactome)
ADPArrowREACT_160293 (Reactome)
ADPArrowREACT_1627 (Reactome)
ADPArrowREACT_2119 (Reactome)
ADPArrowREACT_406 (Reactome)
ADPArrowREACT_6139 (Reactome)
ADPArrowREACT_6178 (Reactome)
ADPArrowREACT_6217 (Reactome)
ADPArrowREACT_6314 (Reactome)
ADPArrowREACT_6327 (Reactome)
ADPArrowREACT_6338 (Reactome)
ADPArrowREACT_6342 (Reactome)
ADPArrowREACT_6353 (Reactome)
ADPArrowREACT_852 (Reactome)
ADPArrowREACT_9023 (Reactome)
ATPREACT_15386 (Reactome)
ATPREACT_15543 (Reactome)
ATPREACT_160293 (Reactome)
ATPREACT_1627 (Reactome)
ATPREACT_2119 (Reactome)
ATPREACT_406 (Reactome)
ATPREACT_6139 (Reactome)
ATPREACT_6178 (Reactome)
ATPREACT_6217 (Reactome)
ATPREACT_6314 (Reactome)
ATPREACT_6327 (Reactome)
ATPREACT_6338 (Reactome)
ATPREACT_6342 (Reactome)
ATPREACT_6353 (Reactome)
ATPREACT_852 (Reactome)
ATPREACT_9023 (Reactome)
CAKmim-catalysisREACT_6139 (Reactome)
CAKmim-catalysisREACT_6314 (Reactome)
CDC25CREACT_2119 (Reactome)
CDK11p58ArrowREACT_15470 (Reactome)
CDK11p58REACT_15401 (Reactome)
CDK1REACT_6216 (Reactome)
CDK1REACT_6308 (Reactome)
CEP250ArrowREACT_15313 (Reactome)
CRS kinasemim-catalysisREACT_6353 (Reactome)
Cdc25mim-catalysisREACT_6175 (Reactome)
Cdc25mim-catalysisREACT_6255 (Reactome)
Cdc25mim-catalysisREACT_6257 (Reactome)
Cdc25mim-catalysisREACT_6294 (Reactome)
Cyclin A Cdc2REACT_6342 (Reactome)
Cyclin A phospho-Cdc2ArrowREACT_6139 (Reactome)
Cyclin A phospho-Cdc2ArrowREACT_6294 (Reactome)
Cyclin A phospho-Cdc2ArrowREACT_6327 (Reactome)
Cyclin A phospho-Cdc2REACT_6139 (Reactome)
Cyclin A phospho-Cdc2REACT_6294 (Reactome)
Cyclin A phospho-Cdc2REACT_6327 (Reactome)
Cyclin A phospho-Cdk2ArrowREACT_9023 (Reactome)
Cyclin A phospho-Cdk2REACT_9021 (Reactome)
Cyclin A phospho-Cdk2REACT_9023 (Reactome)
Cyclin A phospho-Cdk2mim-catalysisREACT_9023 (Reactome)
Cyclin A1 Cdk2 phosphorylated G2/M transition proteinArrowREACT_406 (Reactome)
Cyclin A1 phospho-Cdc2mim-catalysisREACT_406 (Reactome)
Cyclin A2 Cdk2 phosphorylated G2/M transition proteinArrowREACT_1627 (Reactome)
Cyclin A2 phospho-Cdc2mim-catalysisREACT_1627 (Reactome)
Cyclin AREACT_6308 (Reactome)
Cyclin B Cdc2 complexREACT_6217 (Reactome)
Cyclin B phospho-Cdc2ArrowREACT_6217 (Reactome)
Cyclin B1 phospho-Cdc2 ArrowREACT_6314 (Reactome)
Cyclin B1 phospho-Cdc2 REACT_6178 (Reactome)
Cyclin B1 phospho-Cdc2ArrowREACT_6178 (Reactome)
Cyclin B1 phospho-Cdc2ArrowREACT_6257 (Reactome)
Cyclin B1 phospho-Cdc2REACT_6255 (Reactome)
Cyclin B1 phospho-Cdc2REACT_6257 (Reactome)
Cyclin B1 phospho-Cdc2REACT_6353 (Reactome)
Cyclin B2 phospho-Cdc2ArrowREACT_6175 (Reactome)
Cyclin B2 phospho-Cdc2REACT_6175 (Reactome)
Cyclin B2 phospho-Cdc2mim-catalysisREACT_852 (Reactome)
Cyclin BREACT_6216 (Reactome)
E2F1/E2F3REACT_9021 (Reactome)
G2/M transition proteinREACT_852 (Reactome)
G2/M transition proteinsREACT_1627 (Reactome)
G2/M transition proteinsREACT_406 (Reactome)
H2OREACT_160137 (Reactome)
H2OREACT_6175 (Reactome)
H2OREACT_6255 (Reactome)
H2OREACT_6257 (Reactome)
H2OREACT_6294 (Reactome)
NUMA1REACT_15543 (Reactome)
Nlp-depleted centrosomeArrowREACT_15440 (Reactome)
NuMA homodimerREACT_15294 (Reactome)
NuMA homodimerREACT_15444 (Reactome)
OPTN

RAB8A

GTP		REACT_160293 (Reactome)
PKMYT1mim-catalysisREACT_6342 (Reactome)
PLK1ArrowREACT_160137 (Reactome)
PLK1REACT_15470 (Reactome)
PLK1mim-catalysisREACT_15386 (Reactome)
PLK1mim-catalysisREACT_1944 (Reactome)
PLK1mim-catalysisREACT_2119 (Reactome)
PLK1mim-catalysisREACT_414 (Reactome)
Phospho-Cyclin B1 ArrowREACT_6353 (Reactome)
Phosphorylated Myosin Phosphatasemim-catalysisREACT_160137 (Reactome)
PiArrowREACT_160137 (Reactome)
PiArrowREACT_6175 (Reactome)
PiArrowREACT_6255 (Reactome)
PiArrowREACT_6257 (Reactome)
PiArrowREACT_6294 (Reactome)
RAB8A GTPArrowREACT_160293 (Reactome)
REACT_15294 (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.
REACT_15313 (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).
REACT_15386 (Reactome) Phosphorylation of NlP by Plk1 regulates the interaction of Nlp with both centrosomes and ?-TuRCs (Casenghi et al., 2003).
REACT_15401 (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).
REACT_15440 (Reactome) Mitotic activation of Plk1 is required for efficient displacement of Nlp from the centrosome (Casenghi et al., 2003).
REACT_15444 (Reactome) The mechanism by which human NuMA is translocated to the centrosomes has not yet been determined.
REACT_15467 (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.
REACT_15470 (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).
REACT_15543 (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).
REACT_160137 (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).
REACT_160188 (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).
REACT_160281 (Reactome) Phosphorylation of OPTN (optineurin) on serine S177 by PLK1 promotes translocation of OPTN to the nucleus (Kachaner et al. 2012).
REACT_160293 (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).
REACT_1627 (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'.

REACT_1944 (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.
REACT_2119 (Reactome) It has been shown that Xenopus polo homolog,Plx1, directly phosphorylates and activates Cdc25C, which in turn dephosphoryates 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.
REACT_406 (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'.

REACT_414 (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.
REACT_6139 (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).
REACT_6156 (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).
REACT_6163 (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).
REACT_6175 (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'.

REACT_6178 (Reactome) Wee1, a nuclear kinase, phosphorylates cyclin B1:Cdc2 on tyrosine 15 inactivating the complex.
REACT_6183 (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).
REACT_6216 (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.
REACT_6217 (Reactome) Myt1, which localizes preferentially to the endoplasmic reticulum and Golgi complex, phosphorylates Cdc2 on threonine 14 ( Liu et al., 1997).
REACT_6255 (Reactome) Following its translocation to the nucleus, Cdc25 dephosphorylates and activates nuclear cyclin B1:Cdc2 complexes (Strausfeld et al., 1991).
REACT_6257 (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.
REACT_6276 (Reactome) Cyclin A:Cdc2 complexes translocate to the nucleus in G1 and may associate with condensing chromosomes in prophase (Pines and Hunter 1991).
REACT_6279 (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)
REACT_6294 (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)
REACT_6308 (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.
REACT_6314 (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).
REACT_6327 (Reactome) The human Wee1 kinase phosphorylates Cdc2 on tyrosine 15 inactivating the cyclin:CDK complex (Watanabe et al., 1995).
REACT_6338 (Reactome) A description of the mitotic proteins targeted by the mitotic cyclin:CDK complexes will be covered in a later release.
REACT_6342 (Reactome) Myt1, which localizes preferentially to the endoplasmic reticulum and Golgi complex, phosphorylates Cdc2 on threonine 14 ( Liu et al., 1997).
REACT_6343 (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).
REACT_6345 (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).
REACT_6353 (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).
REACT_852 (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).


REACT_9021 (Reactome) In G2, the cyclin A:Cdk2 complex associates with E2F1 and E2F3.
REACT_9023 (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).
WEE1mim-catalysisREACT_6178 (Reactome)
WEE1mim-catalysisREACT_6327 (Reactome)
XPO1ArrowREACT_6183 (Reactome)
active nuclear Cyclin B1 Cdc2 complexesmim-catalysisREACT_6338 (Reactome)
cNAP-1 depleted centrosomeArrowREACT_15313 (Reactome)
centrosome containing phosphorylated NlpArrowREACT_15386 (Reactome)
centrosome-nucleated microtubulesREACT_15294 (Reactome)
centrosome-nucleated microtubulesREACT_15444 (Reactome)
centrosomeREACT_15386 (Reactome)
centrosomeREACT_15401 (Reactome)
centrosomeREACT_15467 (Reactome)
centrosomeREACT_15470 (Reactome)
gamma-tubulin complexREACT_15467 (Reactome)
nuclear Cyclin B1 Cdc2 substratesREACT_6338 (Reactome)
nuclear Cyclin B1 phospho-Cdc2 REACT_6314 (Reactome)
p-NINLArrowREACT_15440 (Reactome)
p-NUMA1ArrowREACT_15543 (Reactome)
p-S177-OPTNArrowREACT_160137 (Reactome)
p-S177-OPTNArrowREACT_160293 (Reactome)
p-S198-CDC25CArrowREACT_2119 (Reactome)
p-T161-CDK1 CCNB1ArrowREACT_6255 (Reactome)
p-T161-CDK1 CCNB1mim-catalysisREACT_15543 (Reactome)
p-T210-PLK1REACT_160137 (Reactome)
p-T210-PLK1mim-catalysisREACT_160293 (Reactome)
phospho-Cdc2ArrowREACT_6342 (Reactome)
phospho-G2/M transition proteinArrowREACT_1627 (Reactome)
phospho-G2/M transition proteinArrowREACT_852 (Reactome)
phosphorylated nuclear Cyclin B1 Cdc2 substratesArrowREACT_6338 (Reactome)
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