Mitotic G2-G2/M phases (Homo sapiens)

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7, 32471718, 432722414, 13, 31, 5010, 45718, 43282610, 23, 2435, 4920, 323355152046929208422, 29, 403, 15, 2712, 45273814, 37, 4436627, 32257, 3237, 44165116217514826114819, 30, 46939114634cytosolnucleoplasmGolgi membraneNEDD1 TUBG1 YWHAE DCTN3 PRKAR2B TUBB LIN9 CEP192 LIN54 SKP1 p-NUMA1RAB8A:GTPCCNACEP135 CEP250TUBA4A AZI1 CEP135 DYNC1H1 p-S252-BORAPLK4 TUBG1 CLASP1 centrosomecontainingphosphorylated NlpODF2 Pip-T210-PLK1 p-T14-CDK1 Centrosome:p-T288-AURKAp-T14,Y15,T161-CDK1 CNTRL CEP63 CEP164 AZI1 CDK5RAP2 EP300ATPACTR1A NDE1 p-T611,S730,S739-FOXM1 SSNA1 DYNC1I2 CKAP5 CCNB1 CSNK1D CEP72 ATPCENPF Gene ADPCCNH MAPRE1 AKAP9 TUBA4A CCP110 p-4S-CCNB1 PPP2R1A ALMS1 PAFAH1B1 DCTN3 MAPRE1 CCNB1 G2/M transitionproteinFGFR1OP LIN37 p-T14,Y15,T161-CDK1 DYNC1I2 CSNK1D p-NUMA1 FBXW11 DCTN2 CEP63 ODF2 HAUS2 CEP290 PRKACA DCTN1-2 DYNLL1 CDK1CEP164 CCNB2 p-T161-CDK1 YWHAE RPS27A(1-76) CNTRL AKAP9 PLK4 CEP164 CDC25CATPDYNC1H1 CENPJ p-T611,S730,S739-FOXM1:MuvB:MYBL2:CCNB2 Genep-T14-CDK1 NDE1 CEP290 MAPRE1 ADPCEP57 YWHAG ALMS1 YWHAG UBB(153-228) ATPSDCCAG8 p-S252-BORA CNTRL CCNA:CDK1NEK2 ADPMAPRE1 ODF2 CEP78 centrosomeCEP72 PKMYT1CSNK1E PRKAR2B p-T611,S730,S739-FOXM1 CCNB1 GeneDYNC1H1 CEP72 p-T611-FOXM1 CCNB2 CLASP1 DYNC1I2 YWHAE SSNA1 DYNC1H1 G2/M transitionproteinsSDCCAG8 NEDD1 TUBB4A CEP135 TUBB4B PP2A-PPP2R2APPP1R12B-4 FGFR1OP AZI1 TUBA1A TUBB4B PRKACA NINL DYNC1I2 CEP135 AKAP9 PAFAH1B1 MAPRE1 PPP2R1A CEP152 DYNC1H1 TUBA4A LIN52 PRKACA ATPTUBGCP4 CCNB1:p-T161-CDK1CEP152 PCNT ATPCEP78 CKAP5 TUBA4A SDCCAG8 p-T14,Y15,T161-CDK1 BTRC p-T14-CDK1 CEP135 PLK4 YWHAE PKMYT1PCM1 ADPNEDD1 phospho-G2/Mtransition proteinOFD1 CDK1 AKAP9 NUMA1NDE1 p-T611-FOXM1:p-T210-PLK1p-T14,T161-CDK1 Mature centrosomesenriched ingamma-TURCcomplexesTUBB4A CEP290 CEP57 CEP57 DYNC1H1 CCNB1 p-S252,S497,T501-BORA PCNT ODF2 TUBB CLASP1 TUBB p-T161-CDK1 H2OTUBGCP5 CCNB1 centrosome-associated NuMACEP63 CENPJ p-T14-CDK1 TUBG1 Cdc25CCNB2CNTRL CEP63 PLK1 CEP192 CEP72 CEP57 TUBG1 CEP70 PRKAR2B ADPDYNLL1 Centrosome:AURKACEP152 NEK2 PLK1 p-T160-CDK2 HAUS2 MAPRE1 p-T611,S730,S739-FOXM1 PPP2R1A HSP90AA1 AKAP9 UBA52(1-76) PCM1 PRKAR2B HAUS2 p-T611-FOXM1H2OPCM1 CEP63 CCNA:p-T160-CDK2NEDD1 UBC(533-608) SSNA1 E2F1/E2F3ALMS1 CEP78 PPP2R1A ADPADPDYNLL1 CNTRL ATPNINL CEP135 CCP110 E2F1 CEP290 SFI1 CLASP1 ODF2 CEP78 CEP57 CENPJ ATPPRKACA PRKACA NEK2 CCP110 CCP110 NINL CETN2 FOXM1MYBL2 DCTN2 CCNB1 CETN2 HSP90AA1 DYNLL1 p-NINL CETN2 CDK5RAP2 TUBB4B CSNK1E OFD1 CEP135 CEP63 HAUS2 CEP41 CEP192 TUBB4A ODF2 NDE1 PRKACA ADPPLK4 OPTN:RAB8A:GTPDCTN1-2 DCTN2 CEP192 p-S473-PPP1R12A Phospho-CyclinB1(CRS):phospho-Cdc2(Thr 161)TUBGCP5 OFD1 ACTR1A p-T161-CDK1 TUBG1 CyclinB1:phospho-Cdc2(Thr161, Thr 14, Tyr15)SFI1 DYNC1I2 DCTN2 CEP41 CCNB2 ADPTUBB4A OFD1 PiCEP290 PPP2R1A MAPRE1 HAUS2 Ub-p-S252,S497,T501-BORAMAPRE1 DCTN1-2 TUBG1 UBC(229-304) CEP72 AZI1 NEDD1 p-S53-WEE1p-S177-OPTNCNTRL YWHAG DYNLL1 HAUS2 TUBA4A CSNK1D CEP70 NINL NEK2 UBC(381-456) TUBG2 RAB8A CEP250 ACTR1A CEP250 CSNK1D PLK1 CCNB2 OPTN LIN9 p-S252-BORA:p-T210-PLK1CENPJ HSP90AA1 p-E2F3 CDK5RAP2 TUBA4A DCTN2 FGFR1OP UBC(77-152) CSNK1E UBC(153-228) CEP76 PCNT CRS kinaseAURKA CEP70 Cyclin A2:Cdk2phosphorylated G2/Mtransition proteinSDCCAG8 MAPRE1 DYNC1H1 CCNA1 DCTN1-2 SSNA1 FGFR1OP TUBGCP6 ODF2 MAPRE1 CEP76 YWHAE TUBB4A CCNB1 ALMS1 CEP70 YWHAG CCNB2 Gene CEP152 NEK2 CEP76 ODF2 DCTN3 TUBG2 p-PKMYT1SSNA1 CEP41 ADPYWHAE LIN52 CCNA:p-T160-CDK2:E2F1/E2F3CEP76 TUBB4A p-T288-AURKA ADPp-4S-CCNB1 CEP164 CEP63 DCTN2 PCNT HAUS2 CSNK1E NEDD1 H2OATPSDCCAG8 CEP63 CSNK1D CDK1 p-NUMA1 OFD1 OFD1 CEP250 SDCCAG8 Centrosome:AURKA:AJUBATUBA4A TUBGCP2 CEP63 FGFR1OP SSNA1 CCNB1:p-T14,T161-CDK1p-T161-CDK1 PCM1 DCTN1-2 CEP164 TUBGCP2 ATPSFI1 HAUS2 FGFR1OP ATPCEP78 DYNLL1 PLK1 NDE1 PPP2R2A PLK1CCNB1:p-T14-CDK1CETN2 E2F3 FGFR1OP DYNC1H1 CyclinB2:phospho-Cdc2(Thr14, Thr 161)TUBB4A SFI1 ACTR1A PCNT PAFAH1B1 SSNA1 PRKACA CNTRL DCTN3 CCNA2 LIN54 ADPCLASP1 PLK4 TUBB4A CSNK1D GTP CEP72 TUBA1A CEP41 SDCCAG8 PLK4 TUBB CEP41 CEP152 CCNA:p-T161-CDK1DYNC1I2 PAFAH1B1 TUBB4A ODF2 p-T161-CDK1 SFI1 BTRC TUBGCP4 DCTN3 CUL1 LIN54 RAB8A DCTN2 CAKCSNK1D PPP2R1A NuMA-boundmicrotubulesPCM1 NEDD1 CCP110 TUBB PiCEP72 ATPPRKAR2B CEP78 CENPJ CEP78 SSNA1 active nuclearCyclin B1:Cdc2complexesCEP76 TUBB4B phosphorylatednuclear CyclinB1:Cdc2 substratesCCP110 TUBG1 CCNB2 PLK1 CEP192 TUBGCP5 DCTN1-2 NDE1 CCNB2 GeneMAPRE1 PRKAR2B CCNB1 Gene CDC25Aphospho-G2/Mtransition proteinCCNBPAFAH1B1 LIN52 Cdc25CDK1 p-T160-CDK2 CCNA:p-T14-CDK1AZI1 NINL H2OPLK1 GeneALMS1 HSP90AA1 TUBA1A DCTN3 CEP41 PLK4 TUBA1A TUBA4A TUBGCP6 CEP152 p-T611,S730,S739-FOXM1:CENPF GeneNEDD1 CEP135 SFI1 PCM1 TUBA1A p-S198-CDC25CTUBB PCM1 CKAP5 PAFAH1B1 TUBB4A NEK2 CCP110 PLK4 p-T160-CDK2 CEP78 CEP290 NDE1 TUBB4B CEP41 ACTR1A SKP1 phospho-CyclinB1(CRS):phospho-Cdc2 (Thr 161)PAFAH1B1 p-CDK1/2:CCNA/p-T161-CDK1:CCNBCEP164 CEP57 TUBGCP3 RBBP4 TUBB CUL1 p-T161-CDK1 YWHAG ADPMYBL2 Centrosome:p-T288-AURKA:p-S252-BORA:PLK1LIN37 CEP57 ODF2 DYNC1H1 GTP ADPAURKA p-S252,S497,T501-BORAPCNT DCTN2 p-E2F1 p-T14,T161-CDK1 p-4S-CCNB1 AKAP9 CDC25A Gene p-T161-CDK1 CEP76 CCNB1 TUBGCP2 SDCCAG8 ATPp-S-AJUBAp-T161-CDK1 PCM1 CEP70 CCNB:p-T14-CDK1PPP2R1A ADPBORATUBGCP6 ALMS1 NEDD1 PRKAR2B p-S252,S497,T501-BORA:SCF-beta-TrCp1/2TUBB p-T14-CDK1 ATPMuvB complexCEP57 p-S252-BORA CLASP1 DYNC1H1 DYNC1I2 HAUS2 CENPJ CENPJ YWHAG HSP90AA1 CDK1 p-T611,S730,S739-FOXM1:EP300:CDC25A GeneCETN2 p-T14,Y15,T161-CDK1 p-T160-CDK2 UBC(305-380) CEP57 CKAP5 NEDD1 CEP192 TUBB CLASP1 TUBA1A PPP2R1A PRKACA CEP72 AJUBAPLK1 PAFAH1B1 DYNLL1 LIN9 ACTR1A CDK1 DCTN2 NDE1 UBB(1-76) OFD1 CEP152 CDK1 CEP250 PLK4 XPO1ADPPRKACA CCNB1:p-T161-CDK1AZI1 DCTN2 CEP250 CEP250 TUBB4B CEP164 YWHAE PLK1 NDE1 phospho-cyclinB1(CRS):phosph-Cdc2(Thr 161)CDC25BFGFR1OP TUBA4A LIN37 CEP135 ACTR1A H2OOFD1 UBC(1-76) TUBG1 UBC(457-532) CCNA:p-T14-CDK1NINL ATPDCTN1-2 FBXW11 YWHAG CETN2 CDC25A GeneSFI1 CCNA2:p-T161-CDK1TUBG1 CCNA1:p-T161-CDK1AKAP9 MNAT1 FGFR1OP ATPp-T611,S730,S739-FOXM1:MuvB:MYBL2:CCNB1 GeneCEP41 PRKACA p-S177-OPTNCSNK1D p-T14-CDK1 CCNA:p-T160-CDK2:p-E2F1/p-E2F3PCNT TUBGCP5 NuMA homodimerCNTRL p-T288-AURKA CNTRL TUBB PLK1PLK1 TUBGCP6 ALMS1 p-T161-CDK1 CDK1 CEP70 FGFR1OP CEP164 CENPJ PLK4 PCNT AKAP9 CCNA:p-T14,T161-CDK1PCM1 UBB(77-152) CDK7 CCNA:p-T14,Y15,T161-CDK1Nlp-depletedcentrosomeCETN2 CEP57 CCNB1UBC(609-684) ACTR1A CDK1 TUBB4B TUBGCP4 p-T611,S730,S739-FOXM1 p-T161-CDK1 NEK2 LIN52 CETN2 p-T14,Y15,T161-CDK1 p-S252,S497,T501-BORA p-T161-CDK1 CEP192 PPP1CB DCTN1-2 CDK5RAP2 cytoplasmic CyclinB1:Cdc2 complexesCDK5RAP2 CLASP1 HSP90AA1 CDK5RAP2 p-NINLSFI1 CEP72 LIN9 CEP57 ACTR1A ALMS1 CLASP1 ACTR1A cNAP-1 depletedcentrosomeAKAP9 CEP78 H2OCEP76 PRKAR2B TUBGCP3 SFI1 TUBGCP4 HAUS2 CCNB:p-T161-CDK1nuclear CyclinB1:Cdc2 substratesDCTN3 AJUBA DYNC1H1 HSP90AA1 CEP250 NDE1 CEP76 CDK5RAP2 TUBA1A CDK5RAP2 AZI1 PLK1 DCTN1-2 PPP2R1A CEP76 CEP70 TUBG1 ATPCDC25CNDE1 HSP90AA1 CDK1 TUBGCP3 DYNC1I2 p-T210-PLK1CEP290 TUBB PCM1 ODF2 ACTR1A SDCCAG8 NEK2 CEP290 CEP76 PRKACA NINL SSNA1 CDC25YWHAG CKAP5 CCNB2:p-T161-CDK1NEK2 p-T161-CDK1 CETN2 DYNLL1 CEP78 TUBG2 CKAP5 CDK1 SSNA1 CDC25BNEDD1 p-T14,T161-CDK1 CDK5RAP2 OFD1 OFD1 TUBG1 ATPTUBGCP3 ALMS1 CEP250 TUBA1A DYNC1I2 PPP2R1A TUBA1A CEP41 DYNLL1 p-T210-PLK1ADPDCTN3 CEP164 CSNK1E CNTRL p-T611,S730,S739-FOXM1CSNK1E TUBB4B FGFR1OP YWHAG CNTRL CEP250 NEDD1 MYBL2SDCCAG8 SSNA1 CKAP5 DCTN1-2 PAFAH1B1 TUBG1 PAFAH1B1 CEP70 AZI1 ADPDYNLL1 HAUS2 WEE1PRKAR2B DYNC1I2 CKAP5 CCNB:CDK1YWHAE TUBGCP6 ATPCDK11p58TUBG1 PLK4 RBBP4 AZI1 CEP135 CEP192 NEDD1 CDK1 PCNT DYNC1I2 SFI1 AKAP9 TUBB4A CEP135 CDK1 CDK1 PLK1CSNK1D CENPJ centrosome-nucleatedmicrotubulesCENPFCENPJ CSNK1E YWHAG CCP110 CETN2 CEP192 ADPCCNB1 CEP78 CSNK1E PRKAR2B CCNB1 CEP192 CEP70 TUBG2 DYNLL1 CEP76 CEP290 PPP2R1A CSNK1E CEP70 HSP90AA1 CEP72 NINL CEP152 NEK2 CENPJ CEP152 CEP192 YWHAE CEP152 CSNK1D CEP70 EP300 CETN2 LIN37 TUBB4B LIN54 PLK1 Gene CCP110 CEP63 NEDD1 CSNK1D TUBGCP2 PCNT PCNT AZI1 CEP164 Cyclin A1:Cdk2phosphorylated G2/Mtransition proteinTUBGCP5 NEDD1 ADPCEP250 PiSCF-beta-TrCp1,2TUBB4B OFD1 CEP152 p-4S-CCNB1 CEP290 G2/M transitionproteinsp-4S-CCNB1 CCNB1 YWHAE CEP164 p-T611,S730,S739-FOXM1 gamma-tubulincomplexCentrosomeassociated Plk1CEP63 CLASP1 TUBG1 PRKAR2B HSP90AA1 YWHAE TUBA1A HSP90AA1 TUBG2 NINL CKAP5 p-T611,S730,S739-FOXM1:MuvB:MYBL2:PLK1 GeneDCTN3 UbCCP110 DCTN1-2 CKAP5 CCP110 AZI1 DCTN2 CDK5RAP2 PCM1 RBBP4 YWHAG ATPPiCDK5RAP2 PLK1 CLASP1 p-NUMA1 CEP290 PAFAH1B1 CSNK1E TUBA4A NEK2 CKAP5 p-T210-PLK1 DCTN3 TUBGCP4 TUBGCP3 DCTN3 ATPPhosphorylatedMyosin PhosphataseTUBA1A CCNB1:p-T14,Y15,T161-CDK1MYBL2 CSNK1E SFI1 TUBA4A ALMS1 ADPTUBB4B RBBP4 CEP41 CEP41 TUBG1 CENPF Genenuclear CyclinB1:Cdc2 complexesTUBGCP2 CCNB1 AKAP9 PLK1 SDCCAG8 ALMS1 CEP72 Centrosomescontainingrecruited CDK11p585120327, 327527


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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)
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...
SourceTargetTypeDatabase referenceComment
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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