Mitotic G2-G2/M phases (Homo sapiens)

From WikiPathways

Revision as of 11:04, 18 November 2015 by ReactomeTeam (Talk | contribs)
Jump to: navigation, search
23234221028, 4429392132, 41453523, 279, 11241, 28132, 414303220, 33, 4474726, 42, 4340, 419, 115, 19, 37, 381621425, 36404948244615776, 23, 272, 418, 12, 1845124240143133134491217, 32, 5051nucleoplasmGolgi membranecytosolDCTN1-2 centrosome-nucleatedmicrotubulesYWHAG p-T611,S730,S739-FOXM1:EP300:CDC25A GeneCCNB2SDCCAG8 YWHAG CEP76 ADPNINL GTP AKAP9 AKAP9 SKP1 CDC25A Gene NEDD1 CEP76 CCNB1:p-T161-CDK1PPP2R1A Centrosome:p-T288-AURKAOFD1 gamma-tubulincomplexNDE1 MAPRE1 PRKAR2B SDCCAG8 UBC(229-304) UBA52(1-76) CCNA:p-T14,Y15,T161-CDK1CSNK1E CAKCEP152 PLK1 CCNA2 NINL NEDD1 UBC(381-456) PCNT CEP72 PLK4 p-T611-FOXM1 TUBB4A MAPRE1 AKAP9 CDK1 CENPJ TUBB4A MNAT1 PiCCNB1:p-T14,T161-CDK1DCTN2 TUBGCP6 CDK5RAP2 LIN52 cNAP-1 depletedcentrosomeCCNB2 CEP250 E2F1/E2F3CEP192 CCNA2 DCTN3 ADPCDC25BNEK2 p-T210-PLK1 CCNB2 Gene CCNA1 phospho-CyclinB1(CRS):phospho-Cdc2 (Thr 161)YWHAG FGFR1OP CEP78 CEP70 PRKACA CEP72 TUBA1A G2/M transitionproteinsPLK1 Gene TUBB p-NUMA1 CSNK1D SSNA1 CCNA:p-T14-CDK1CCNA:p-T14,T161-CDK1ACTR1A CEP57 TUBG2 p-T161-CDK1 CCNA1 NEDD1 PAFAH1B1 PAFAH1B1 CEP290 microtubule p-T611-FOXM1:p-T210-PLK1ADPTUBB HSP90AA1 ACTR1A p-T14-CDK1 PRKAR2B TUBG1 YWHAG TUBGCP2 Centrosomeassociated Plk1HAUS2 CEP78 CLASP1 NDE1 CEP164 p-T611,S730,S739-FOXM1:MuvB:MYBL2:PLK1 GeneODF2 WEE1AZI1 CEP70 TUBA1A p-T161-CDK1 CLASP1 ATPDCTN1-2 DCTN1-2 UBC(533-608) PiAZI1 CLASP1 RPS27A(1-76) p-T14,Y15,T161-CDK1 CDK1 YWHAE microtubule YWHAE p-E2F1 CEP135 CKAP5 PRKACA PCM1 TUBA4A CDK5RAP2 UBC(77-152) NDE1 PPP2R1A DCTN1-2 centrosome-associated NuMAactive nuclearCyclin B1:Cdc2complexesPRKACA SFI1 NEK2 ALMS1 DCTN2 CEP164 TUBG2 p-T160-CDK2 p-T611,S730,S739-FOXM1:CENPF GeneCEP152 PLK4 CCNB:p-T161-CDK1CCNA:p-T160-CDK2:E2F1/E2F3CCNAHAUS2 LIN54 CCNB2 SSNA1 CEP78 p-T611,S730,S739-FOXM1 CDK1 TUBB4B YWHAE TUBGCP4 TUBB4B ATPCEP135 MuvB complexAURKA FGFR1OP CCP110 CEP63 p-S252,S497,T501-BORA:SCF-beta-TrCp1/2PAFAH1B1 TUBB CEP250CyclinB2:phospho-Cdc2(Thr14, Thr 161)CEP152 CETN2 E2F1 p-S252,S497,T501-BORA p-T14,Y15,T161-CDK1 NuMA homodimerTUBGCP6 DYNLL1 PPP2R1A DYNC1I2 CEP70 CCNA:p-T161-CDK1CEP70 ALMS1 p-T161-CDK1 DYNLL1 p-T161-CDK1 SDCCAG8 ATPUBC(1-76) SSNA1 ATPACTR1A NEK2 OFD1 CCNA2 PLK4 CCNB:p-T14-CDK1PPP2R1B p-E2F3 NEK2 TUBG1 DCTN2 LIN9 CCNA:p-T160-CDK2TUBA1A DYNC1I2 NUMA1PLK1 PLK4 CEP152 AZI1 CSNK1D YWHAE ATPCENPJ HAUS2 PCM1 MAPRE1 YWHAG p-S177-OPTNPLK4 CDK1 CEP192 CEP63 ADPCEP192 TUBA1A CCP110 PAFAH1B1 PRKACA AKAP9 p-S252-BORA TUBA4A PRKAR2B Cyclin A2:Cdk2phosphorylated G2/Mtransition proteinRBBP4 TUBB4B PCNT UBB(153-228) PAFAH1B1 CSNK1E CEP70 TUBB4A TUBG1 HSP90AA1 DYNC1H1 TUBG1 TUBGCP5 MAPRE1 CEP76 PLK1 DYNC1I2 PLK1p-T14-CDK1 PLK4 CEP290 Cdc25NEDD1 ATPDCTN3 CETN2 ACTR1A CCNA:p-CDK1/2 NEDD1 CDK1 DCTN2 FGFR1OP TUBB4A CSNK1D CEP192 CEP290 PCM1 PCM1 Nlp-depletedcentrosomep-S252-BORA PLK1 TUBA4A TUBA1A LIN37 SSNA1 CEP250 PKMYT1ODF2 ODF2 CCNB1:p-T161-CDK1CEP76 ATPCDC25CPLK1CEP41 CCNB1 MAPRE1 NEK2 Centrosomescontainingrecruited CDK11p58p-T161-CDK1 CEP72 CCNA2 CCNA1 CEP41 CEP41 PRKACA p-S252,S497,T501-BORA MAPRE1 ACTR1A NEK2 CDK1HAUS2 SSNA1 OFD1 MAPRE1 CEP72 CCNA1 CEP135 MYBL2CEP164 EP300p-T288-AURKA DYNC1I2 ATPPRKAR2B CCNB1 FBXW11 CEP57 DCTN1-2 PLK1 GeneADPNDE1 PAFAH1B1 DYNC1H1 PCM1 HSP90AA1 TUBB4B AKAP9 p-S252-BORA:p-T210-PLK1ATPp-T210-PLK1FGFR1OP NEDD1 CEP135 ODF2 CENPJ CNTRL CENPJ CCNB1 p-S252,S497,T501-BORAp-S177-OPTNPRKAR2B CEP76 YWHAE PLK4 CEP192 AKAP9 LIN52 FGFR1OP CSNK1D NINL TUBGCP2 DYNLL1 TUBA4A CEP192 CCNB1 PRKAR2B PAFAH1B1 CEP152 NEK2 CCNB2 CEP72 ACTR1A CEP41 TUBB4B TUBA1A YWHAE TUBGCP4 p-T611,S730,S739-FOXM1 TUBGCP3 CKAP5 DCTN2 PCM1 PKMYT1HAUS2 HSP90AA1 HAUS2 PPP2R1A G2/M transitionproteinsPLK4 CLASP1 CEP41 CEP72 CEP152 Phospho-CyclinB1(CRS):phospho-Cdc2(Thr 161)TUBA4A NEK2 CEP164 p-T14,T161-CDK1 PhosphorylatedMyosin PhosphataseCDK5RAP2 TUBG1 p-NUMA1 CSNK1D PCNT CDK7 ATPPPP2R1A Cyclin A1:Cdk2phosphorylated G2/Mtransition proteinTUBGCP4 TUBA1A CENPJ DYNC1H1 ADPMAPRE1 CKAP5 PRKACA CEP250 DCTN2 LIN52 DYNC1H1 Centrosome:AURKA:AJUBACLASP1 TUBGCP3 HSP90AA1 CSNK1E DCTN3 AZI1 PPP2R1A NDE1 TUBB4B CCNA1 CEP152 SDCCAG8 p-T288-AURKA ADPCCP110 ALMS1 TUBB4B PPP2R1A TUBG1 PCNT MYBL2 PCNT ACTR1A UBC(153-228) CCNB1SFI1 ATPp-T160-CDK2 CNTRL CEP192 NEK2 TUBG1 CCNB1:p-T14,Y15,T161-CDK1p-T161-CDK1 EP300 CEP164 CEP57 DCTN2 ADPTUBB TUBB4A DCTN1-2 SDCCAG8 CEP57 ALMS1 PPP1R12B-4 CDK1 CNTRL SDCCAG8 CNTRL nuclear CyclinB1:Cdc2 substratesBTRC CSNK1E DYNLL1 CDK1 CSNK1D CEP78 LIN54 CEP70 TUBA1A PLK1 DCTN1-2 CENPFCEP250 DYNC1H1 CEP78 CCNB1 YWHAG DYNC1H1 YWHAG CEP70 CENPF GeneCDK5RAP2 ODF2 FOXM1CUL1 NEDD1 TUBGCP4 DCTN1-2 CCP110 TUBGCP2 CDK1 AJUBA NINL CyclinB1:phospho-Cdc2(Thr161, Thr 14, Tyr15)CSNK1E CDC25BATPCKAP5 CEP78 RBBP4 NEDD1 YWHAE p-T14,T161-CDK1 TUBB4A CNTRL CCNB1 Centrosome:AURKANDE1 ATPPCNT FGFR1OP ALMS1 CCP110 CEP164 ADPTUBB CENPJ CCNB:p-T161-CDK1 OPTN H2OCCNA1 PLK4 ATPp-T14,Y15,T161-CDK1 ACTR1A NDE1 ADPTUBB4B p-4S-CCNB1 GTP CEP63 DYNC1H1 SFI1 TUBGCP6 CSNK1E HAUS2 DYNC1H1 microtubule CEP192 DYNLL1 PPP2CB p-NUMA1 DYNC1I2 CCNB2 CEP72 TUBB Cdc25p-PKMYT1AZI1 PCM1 PLK4 TUBB SFI1 TUBA1A p-S198-CDC25CCENPJ NEDD1 NINL CEP192 CNTRL NEK2 p-T161-CDK1 OFD1 LIN37 nuclear CyclinB1:Cdc2 complexesCENPJ PLK4 SKP1 HAUS2 PRKAR2B CEP63 H2OTUBGCP5 CCP110 XPO1FGFR1OP ODF2 H2OPRKAR2B RAB8A:GTPDYNC1I2 NINL CEP164 ADPp-T14-CDK1 CETN2 YWHAE CCNB2:p-T161-CDK1CEP63 DCTN1-2 p-4S-CCNB1 CEP76 UBC(609-684) CEP192 PPP2R1A p-T14,T161-CDK1 PCNT CSNK1D CSNK1E CSNK1E DCTN2 CEP57 HSP90AA1 CCNA1 p-4S-CCNB1 Ub-p-S252,S497,T501-BORACEP76 FGFR1OP PCNT p-T611,S730,S739-FOXM1 ODF2 CEP290 PCM1 HAUS2 AKAP9 ATPTUBB4B NDE1 NDE1 CEP76 CEP250 TUBA4A MYBL2 FGFR1OP MYBL2 CEP41 TUBG1 CENPJ ODF2 UBC(457-532) YWHAG BTRC ATPCSNK1E DYNC1H1 PRKACA ADPCEP72 CDK5RAP2 AKAP9 AKAP9 DCTN3 CLASP1 CSNK1D CDK5RAP2 DCTN1-2 TUBB4A p-S473-PPP1R12A DYNLL1 E2F3 TUBG1 H2OFGFR1OP centrosomecontainingphosphorylated NlpLIN9 CEP250 CLASP1 TUBGCP2 CEP78 CEP135 CDC25PAFAH1B1 CEP164 p-T161-CDK1 DYNLL1 CEP57 p-S53-WEE1OFD1 CCNB1 CKAP5 CCNA2 p-T161-CDK1 DCTN3 p-T14,Y15,T161-CDK1 LIN9 CCNB:CDK1p-T611,S730,S739-FOXM1:MuvB:MYBL2:CCNB2 GenePRKAR2B CNTRL p-T210-PLK1TUBG1 FGFR1OP CCNB1 Centrosome:p-T288-AURKA:p-S252-BORA:PLK1SSNA1 SFI1 p-T210-PLK1 CETN2 CSNK1D CEP76 CNTRL TUBG2 LIN9 PiUBC(305-380) ACTR1A CEP78 YWHAG PRKAR2B DCTN3 CEP135 PPP2R1A UbATPTUBA4A ALMS1 CENPJ CCNA2 CEP250 OFD1 CEP78 CDK5RAP2 CCP110 CSNK1E AZI1 OFD1 CEP57 PCM1 NINL SSNA1 RBBP4 CCNH AZI1 TUBA4A TUBA1A DYNC1I2 CEP57 SSNA1 CEP135 CEP164 CEP135 CEP41 PAFAH1B1 ALMS1 PLK1 ATPADPCDK11A ALMS1 DCTN3 CEP135 ADPCCNB1:p-T14-CDK1PCNT RAB8A CEP135 PiCEP76 cytoplasmic CyclinB1:Cdc2 complexesCLASP1 CCNA1:p-T161-CDK1G2/M transitionproteinCCNA1 CEP72 CETN2 p-4S-CCNB1 CEP78 CSNK1E CCP110 CLASP1 p-T611-FOXM1PPP2R1A CEP63 CEP41 TUBGCP5 CEP70 SDCCAG8 SDCCAG8 NEDD1 TUBB4A CCNB1 Gene TUBB SFI1 CEP192 CDK1 TUBB4B CCNB1 CDK11p58PAFAH1B1 ATPYWHAE AZI1 TUBG2 TUBG1 CEP152 H2OAZI1 CKAP5 PRKACA CEP78 SFI1 TUBG1 PAFAH1B1 PRKACA SCF-beta-TrCp1,2PiCEP152 LIN37 TUBGCP6 CEP152 OFD1 CETN2 CETN2 CEP41 CCNA2:p-T161-CDK1OFD1 SSNA1 centrosomeHSP90AA1 TUBGCP2 RBBP4 HSP90AA1 TUBG1 TUBG1 TUBB4B CDK1 CCNA:CDK1CEP41 p-T611,S730,S739-FOXM1 phospho-cyclinB1(CRS):phosph-Cdc2(Thr 161)CCNB1 CDK5RAP2 p-T611,S730,S739-FOXM1:MuvB:MYBL2:CCNB1 GeneCUL1 AZI1 PCNT NEDD1 CCNB2 GeneODF2 PRKACA CEP290 TUBA4A CCNBCEP290 p-T14,Y15,T161-CDK1 CEP164 ADPLIN54 DYNC1I2 CRS kinaseDCTN3 CKAP5 CEP70 ODF2 CETN2 CETN2 CDK5RAP2 TUBA4A CSNK1D CEP63 NINL CEP250 phospho-G2/Mtransition proteinUBB(77-152) DCTN1-2 ODF2 PPP2R1A CEP57 AZI1 CEP63 CEP72 RAB8A CKAP5 p-T611,S730,S739-FOXM1 PRKAR2B CDK1 CEP63 TUBGCP3 MAPRE1 ALMS1 DYNC1I2 ADPTUBB4A NDE1 NEDD1 CNTRL CEP57 CCNA2 DCTN3 CENPJ CCNA:p-T14-CDK1p-4S-CCNB1 CEP70 CEP72 p-CDK1/2:CCNA/p-T161-CDK1:CCNBHSP90AA1 TUBA4A LIN37 CLASP1 SDCCAG8 DCTN3 CENPF Gene YWHAG NEDD1 CEP76 LIN54 CEP290 DCTN2 AURKA TUBB ADPp-T161-CDK1 TUBG2 phospho-G2/Mtransition proteinCNTRL CDC25A GeneCCP110 ACTR1A CDC25CTUBA1A NuMA-boundmicrotubulesTUBGCP3 p-T161-CDK1 CKAP5 TUBGCP5 CEP290 CCNA2 HAUS2 HSP90AA1 CETN2 YWHAE CLASP1 CCNA1 CEP164 SFI1 YWHAG PLK1 PCM1 HSP90AA1 TUBB4A p-NINL NINL CEP135 PLK1 NEDD1 OFD1 p-S-AJUBADCTN3 CSNK1D OPTN:RAB8A:GTPCCP110 p-S252-BORAACTR1A p-T611,S730,S739-FOXM1PLK1PPP2R1A TUBB4A ADPDCTN2 CCNB1 GeneCEP57 CCNA:p-T160-CDK2:p-E2F1/p-E2F3CEP290 ATPLIN52 DYNLL1 CEP290 CEP250 DYNLL1 CCP110 SFI1 DYNC1H1 DYNLL1 TUBG1 p-T14-CDK1 CDC25ASSNA1 OFD1 CCNA1 FBXW11 CEP152 DYNC1I2 PPP2R2A CEP41 AKAP9 PLK1 CEP63 CDK5RAP2 phosphorylatednuclear CyclinB1:Cdc2 substratesPCNT ALMS1 TUBGCP3 MAPRE1 CEP70 MAPRE1 TUBGCP4 BORADYNLL1 SDCCAG8 PLK1 HAUS2 NDE1 NEDD1 AJUBAp-NINLSDCCAG8 ADPPPP1CB CEP63 UBB(1-76) ADPp-T160-CDK2 YWHAE CEP250 DCTN2 Mature centrosomesenriched ingamma-TURCcomplexesTUBGCP6 ALMS1 DYNC1H1 AKAP9 CDK1 PRKACA CDK11B PCM1 p-NUMA1SSNA1 p-T14-CDK1 CDK5RAP2 H2OPP2A-PPP2R2AATPCEP290 TUBB PLK1 SFI1 TUBGCP5 ADPNEK2 CDK1 CNTRL PPP2CA CCNA2 TUBB p-T14-CDK1 CCNA2 CETN2 CKAP5 CKAP5 DYNC1I2 SFI1 1441402322, 417


Description

View original pathway at:Reactome.

Try the New WikiPathways

View approved pathways at the new wikipathways.org.

Quality Tags

Ontology Terms

 

Bibliography

View all...
  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-CDK1/2 R-HSA-4088020 (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 GeneGeneProductENSG00000134057 (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 GeneGeneProductENSG00000157456 (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-CDK1 R-HSA-4088041 (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 GeneGeneProductENSG00000164045 (Ensembl)
CDC25AProteinP30304 (Uniprot-TrEMBL)
CDC25BProteinP30305 (Uniprot-TrEMBL)
CDC25CProteinP30307 (Uniprot-TrEMBL)
CDC25R-HSA-69261 (Reactome)
CDK1 ProteinP06493 (Uniprot-TrEMBL)
CDK11A ProteinQ9UQ88 (Uniprot-TrEMBL)
CDK11B ProteinP21127 (Uniprot-TrEMBL)
CDK11p58ProteinR-HSA-380452 (Reactome)
CDK1ProteinP06493 (Uniprot-TrEMBL)
CDK5RAP2 ProteinQ96SN8 (Uniprot-TrEMBL)
CDK7 ProteinP50613 (Uniprot-TrEMBL)
CENPF Gene ProteinENSG00000117724 (Ensembl)
CENPF GeneGeneProductENSG00000117724 (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 GeneGeneProductENSG00000166851 (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)
PPP2CA ProteinP67775 (Uniprot-TrEMBL)
PPP2CB ProteinP62714 (Uniprot-TrEMBL)
PPP2R1A ProteinP30153 (Uniprot-TrEMBL)
PPP2R1B ProteinP30154 (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).
microtubule R-HSA-190599 (Reactome)
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)
Personal tools