MPIP2_HUMAN - dbPTM
MPIP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPIP2_HUMAN
UniProt AC P30305
Protein Name M-phase inducer phosphatase 2
Gene Name CDC25B
Organism Homo sapiens (Human).
Sequence Length 580
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole .
Protein Description Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Directly dephosphorylates CDK1 and stimulates its kinase activity. The three isoforms seem to have a different level of activity..
Protein Sequence MEVPQPEPAPGSALSPAGVCGGAQRPGHLPGLLLGSHGLLGSPVRAAASSPVTTLTQTMHDLAGLGSETPKSQVGTLLFRSRSRLTHLSLSRRASESSLSSESSESSDAGLCMDSPSPMDPHMAEQTFEQAIQAASRIIRNEQFAIRRFQSMPVRLLGHSPVLRNITNSQAPDGRRKSEAGSGAASSSGEDKENDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPDRKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKRVILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHEAFKDELKTFRLKTRSWAGERSRRELCSRLQDQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
12PhosphorylationQPEPAPGSALSPAGV
CCCCCCCCCCCCCCC
25.6123898821
15PhosphorylationPAPGSALSPAGVCGG
CCCCCCCCCCCCCCC
16.6628348404
36PhosphorylationLPGLLLGSHGLLGSP
CCCCCCCCCCCCCCC
17.8523898821
42PhosphorylationGSHGLLGSPVRAAAS
CCCCCCCCCHHHHHC
21.8617001009
49PhosphorylationSPVRAAASSPVTTLT
CCHHHHHCCCCCHHH
30.3722199227
49 (in isoform 2)Phosphorylation-30.3722210691
49 (in isoform 4)Phosphorylation-30.3722210691
50PhosphorylationPVRAAASSPVTTLTQ
CHHHHHCCCCCHHHH
20.7525850435
53PhosphorylationAAASSPVTTLTQTMH
HHHCCCCCHHHHHHH
21.3325850435
54PhosphorylationAASSPVTTLTQTMHD
HHCCCCCHHHHHHHH
28.2122199227
56PhosphorylationSSPVTTLTQTMHDLA
CCCCCHHHHHHHHHC
21.6522199227
58PhosphorylationPVTTLTQTMHDLAGL
CCCHHHHHHHHHCCC
15.9622199227
67PhosphorylationHDLAGLGSETPKSQV
HHHCCCCCCCCHHHH
43.2527080861
67 (in isoform 2)Phosphorylation-43.2522210691
67 (in isoform 4)Phosphorylation-43.2522210691
69PhosphorylationLAGLGSETPKSQVGT
HCCCCCCCCHHHHHH
37.4022199227
69 (in isoform 2)Phosphorylation-37.4022210691
69 (in isoform 4)Phosphorylation-37.4022210691
71UbiquitinationGLGSETPKSQVGTLL
CCCCCCCHHHHHHHH
62.02-
81PhosphorylationVGTLLFRSRSRLTHL
HHHHHHCCCCCCHHH
27.5523898821
86PhosphorylationFRSRSRLTHLSLSRR
HCCCCCCHHHHHHHH
21.4723927012
89PhosphorylationRSRLTHLSLSRRASE
CCCCHHHHHHHHHCC
19.3923927012
91PhosphorylationRLTHLSLSRRASESS
CCHHHHHHHHHCCCC
19.1523927012
97PhosphorylationLSRRASESSLSSESS
HHHHHCCCCCCCCCC
33.80-
115PhosphorylationDAGLCMDSPSPMDPH
CCCCCCCCCCCCCHH
10.61-
117PhosphorylationGLCMDSPSPMDPHMA
CCCCCCCCCCCHHHH
36.49-
127PhosphorylationDPHMAEQTFEQAIQA
CHHHHHHHHHHHHHH
22.2021640712
151PhosphorylationFAIRRFQSMPVRLLG
HHHHHHHHCCCHHHC
23.4930266825
151 (in isoform 3)Phosphorylation-23.4925850435
160PhosphorylationPVRLLGHSPVLRNIT
CCHHHCCCHHHHHCC
18.2030266825
167PhosphorylationSPVLRNITNSQAPDG
CHHHHHCCCCCCCCC
32.1621640712
169PhosphorylationVLRNITNSQAPDGRR
HHHHCCCCCCCCCCC
21.0422817900
177UbiquitinationQAPDGRRKSEAGSGA
CCCCCCCCCCCCCCC
51.81-
178PhosphorylationAPDGRRKSEAGSGAA
CCCCCCCCCCCCCCC
30.7625849741
182PhosphorylationRRKSEAGSGAASSSG
CCCCCCCCCCCCCCC
32.1029214152
186PhosphorylationEAGSGAASSSGEDKE
CCCCCCCCCCCCCCC
25.2212527891
187PhosphorylationAGSGAASSSGEDKEN
CCCCCCCCCCCCCCC
37.3212527891
188PhosphorylationGSGAASSSGEDKEND
CCCCCCCCCCCCCCC
43.64-
190 (in isoform 2)Ubiquitination-68.78-
192UbiquitinationASSSGEDKENDGFVF
CCCCCCCCCCCCEEE
54.86-
200UbiquitinationENDGFVFKMPWKPTH
CCCCEEEEECCCCCC
38.46-
201 (in isoform 3)Ubiquitination-3.0421890473
204UbiquitinationFVFKMPWKPTHPSST
EEEEECCCCCCCCHH
33.88-
209PhosphorylationPWKPTHPSSTHALAE
CCCCCCCCHHHHHHH
40.0221640712
228 (in isoform 2)Ubiquitination-22.1321890473
229PhosphorylationEAFAQRPSSAPDLMC
HHHHHCCCCCCCCEE
41.1223927012
230PhosphorylationAFAQRPSSAPDLMCL
HHHHCCCCCCCCEEE
46.6423927012
238PhosphorylationAPDLMCLSPDRKMEV
CCCCEEECCCCCCCH
21.5923401153
242SumoylationMCLSPDRKMEVEELS
EEECCCCCCCHHHHC
46.95-
242SumoylationMCLSPDRKMEVEELS
EEECCCCCCCHHHHC
46.95-
242UbiquitinationMCLSPDRKMEVEELS
EEECCCCCCCHHHHC
46.9521906983
242 (in isoform 1)Ubiquitination-46.9521890473
249PhosphorylationKMEVEELSPLALGRF
CCCHHHHCHHHCCEE
22.5829255136
258 (in isoform 3)Ubiquitination-6.4721890473
262 (in isoform 3)Ubiquitination-59.8221890473
263 (in isoform 4)Ubiquitination-49.6121890473
265PhosphorylationLTPAEGDTEEDDGFV
CCCCCCCCCCCCCCC
52.7321640712
266 (in isoform 3)Ubiquitination-65.2621890473
285 (in isoform 2)Ubiquitination-8.2721890473
289 (in isoform 2)Ubiquitination-3.7921890473
291PhosphorylationAVPPGMESLISAPLV
CCCCCHHHHHCCCHH
23.3121640712
293 (in isoform 2)Ubiquitination-4.6121890473
299UbiquitinationLISAPLVKTLEKEEE
HHCCCHHHHCCHHHH
55.89-
299 (in isoform 1)Ubiquitination-55.8921890473
303UbiquitinationPLVKTLEKEEEKDLV
CHHHHCCHHHHHHHH
73.8121906983
303 (in isoform 1)Ubiquitination-73.8121890473
307UbiquitinationTLEKEEEKDLVMYSK
HCCHHHHHHHHHHHH
60.6921906983
307 (in isoform 1)Ubiquitination-60.6921890473
312PhosphorylationEEKDLVMYSKCQRLF
HHHHHHHHHHHHHHH
9.48-
313PhosphorylationEKDLVMYSKCQRLFR
HHHHHHHHHHHHHHC
14.6224719451
320 (in isoform 4)Ubiquitination-52.8521890473
321PhosphorylationKCQRLFRSPSMPCSV
HHHHHHCCCCCCHHH
17.6223927012
323PhosphorylationQRLFRSPSMPCSVIR
HHHHCCCCCCHHHHH
36.2823927012
324 (in isoform 4)Ubiquitination-4.3821890473
327PhosphorylationRSPSMPCSVIRPILK
CCCCCCHHHHHHHHH
18.0830576142
328 (in isoform 4)Ubiquitination-5.6921890473
334UbiquitinationSVIRPILKRLERPQD
HHHHHHHHHCCCCCC
56.51-
344PhosphorylationERPQDRDTPVQNKRR
CCCCCCCCCCCCCCC
26.6730576142
349UbiquitinationRDTPVQNKRRRSVTP
CCCCCCCCCCCCCCC
30.14-
353PhosphorylationVQNKRRRSVTPPEEQ
CCCCCCCCCCCHHHH
28.6525159151
355PhosphorylationNKRRRSVTPPEEQQE
CCCCCCCCCHHHHHH
34.0830278072
357 (in isoform 3)Ubiquitination-48.6821890473
367SumoylationQQEAEEPKARVLRSK
HHHHHCHHHHHHHHH
52.70-
367SumoylationQQEAEEPKARVLRSK
HHHHHCHHHHHHHHH
52.70-
367UbiquitinationQQEAEEPKARVLRSK
HHHHHCHHHHHHHHH
52.70-
367 (in isoform 3)Ubiquitination-52.7021890473
372 (in isoform 3)Ubiquitination-38.9021890473
373PhosphorylationPKARVLRSKSLCHDE
HHHHHHHHHHHCHHH
23.5723927012
374UbiquitinationKARVLRSKSLCHDEI
HHHHHHHHHHCHHHH
40.80-
375PhosphorylationARVLRSKSLCHDEIE
HHHHHHHHHCHHHHH
37.1629255136
384 (in isoform 2)Ubiquitination-3.4921890473
387PhosphorylationEIENLLDSDHRELIG
HHHHHHCCCHHHHHC
34.9723927012
394 (in isoform 2)Ubiquitination-40.1921890473
396PhosphorylationHRELIGDYSKAFLLQ
HHHHHCHHHHEEEEE
13.5721406692
397PhosphorylationRELIGDYSKAFLLQT
HHHHCHHHHEEEEEE
23.4221406692
398UbiquitinationELIGDYSKAFLLQTV
HHHCHHHHEEEEEEC
36.6121906983
398 (in isoform 1)Ubiquitination-36.6121890473
399 (in isoform 2)Ubiquitination-8.3821890473
404PhosphorylationSKAFLLQTVDGKHQD
HHEEEEEECCCCCCC
22.1221640712
408UbiquitinationLLQTVDGKHQDLKYI
EEEECCCCCCCCCCC
33.3621906983
408 (in isoform 1)Ubiquitination-33.3621890473
411 (in isoform 3)Ubiquitination-44.8621890473
413UbiquitinationDGKHQDLKYISPETM
CCCCCCCCCCCHHHH
49.1521906983
413 (in isoform 1)Ubiquitination-49.1521890473
414PhosphorylationGKHQDLKYISPETMV
CCCCCCCCCCHHHHH
17.5829496907
416PhosphorylationHQDLKYISPETMVAL
CCCCCCCCHHHHHHH
17.3722210691
419PhosphorylationLKYISPETMVALLTG
CCCCCHHHHHHHHHC
21.9624114839
419 (in isoform 4)Ubiquitination-21.9621890473
425PhosphorylationETMVALLTGKFSNIV
HHHHHHHHCCCCCCC
38.8922210691
427UbiquitinationMVALLTGKFSNIVDK
HHHHHHCCCCCCCCE
40.14-
429PhosphorylationALLTGKFSNIVDKFV
HHHHCCCCCCCCEEE
29.1822210691
429 (in isoform 4)Ubiquitination-29.1821890473
434UbiquitinationKFSNIVDKFVIVDCR
CCCCCCCEEEEEECC
30.54-
434 (in isoform 4)Ubiquitination-30.5421890473
438 (in isoform 2)Ubiquitination-4.8321890473
452UbiquitinationEYEGGHIKTAVNLPL
EECCCEEEEEEECCC
25.4321906983
452 (in isoform 1)Ubiquitination-25.4321890473
465PhosphorylationPLERDAESFLLKSPI
CCCCCHHHHHHCCCC
23.9426552605
469UbiquitinationDAESFLLKSPIAPCS
CHHHHHHCCCCCCCC
57.23-
470PhosphorylationAESFLLKSPIAPCSL
HHHHHHCCCCCCCCC
22.8525159151
473 (in isoform 4)Ubiquitination-11.4821890473
476PhosphorylationKSPIAPCSLDKRVIL
CCCCCCCCCCCCEEE
38.2523312004
479UbiquitinationIAPCSLDKRVILIFH
CCCCCCCCCEEEEEE
54.58-
482 (in isoform 3)Ubiquitination-2.5721890473
509 (in isoform 2)Ubiquitination-41.9621890473
513PhosphorylationRAVNDYPSLYYPEMY
HHHCCCCHHHCCCEE
23.8321640712
523UbiquitinationYPEMYILKGGYKEFF
CCCEEEECCCHHHHC
40.512190698
523 (in isoform 1)Ubiquitination-40.5121890473
527UbiquitinationYILKGGYKEFFPQHP
EEECCCHHHHCCCCC
51.85-
544 (in isoform 4)Ubiquitination-23.0021890473
551UbiquitinationPMNHEAFKDELKTFR
CCCHHHHHHHHHHHC
58.29-
555UbiquitinationEAFKDELKTFRLKTR
HHHHHHHHHHCHHCC
43.50-
556PhosphorylationAFKDELKTFRLKTRS
HHHHHHHHHCHHCCC
26.98-
561PhosphorylationLKTFRLKTRSWAGER
HHHHCHHCCCCCCHH
34.2318237113
563PhosphorylationTFRLKTRSWAGERSR
HHCHHCCCCCCHHHH
26.8923898821

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
50SPhosphorylationKinasePLK1P53350
PSP
50SPhosphorylationKinaseCDK1P06493
PSP
58TPhosphorylationKinasePLK1P53350
PSP
101SPhosphorylationKinaseMAPK8P45983
GPS
103SPhosphorylationKinaseMAPK8P45983
GPS
127TPhosphorylationKinasePLK1P53350
PSP
146SPhosphorylationKinaseCDK1P06493
PSP
160SPhosphorylationKinaseCDK1P06493
PhosphoELM
167TPhosphorylationKinasePLK1P53350
PSP
169SPhosphorylationKinaseMELKQ14680
Uniprot
169SPhosphorylationKinaseMAPKAPK2P49137
PSP
186SPhosphorylationKinaseCK2_GROUP-PhosphoELM
186SPhosphorylationKinaseCK2-FAMILY-GPS
186SPhosphorylationKinaseCSNK2A1P68400
GPS
187SPhosphorylationKinaseCK2_GROUP-PhosphoELM
187SPhosphorylationKinaseCK2-FAMILY-GPS
187SPhosphorylationKinaseCSNK2A1P68400
GPS
209SPhosphorylationKinasePLK1P53350
PSP
230SPhosphorylationKinaseCHEK1O14757
GPS
249SPhosphorylationKinaseP38-SUBFAMILY-GPS
249SPhosphorylationKinaseMAPK11Q15759
GPS
253SPhosphorylationKinaseAURKAO14965
GPS
265TPhosphorylationKinasePLK1P53350
PSP
291SPhosphorylationKinasePLK1P53350
PSP
307SPhosphorylationKinaseCDK1P06493
PSP
321SPhosphorylationKinaseCDK1P06493
PSP
323SPhosphorylationKinaseMELKQ14680
Uniprot
323SPhosphorylationKinaseMAPK14Q16539
Uniprot
323SPhosphorylationKinaseMAPK2P49137
PhosphoELM
353SPhosphorylationKinaseAKT-FAMILY-GPS
353SPhosphorylationKinaseAURAO14965
PSP
353SPhosphorylationKinasePLK1P53350
PSP
353SPhosphorylationKinaseMAPKAPK2P49137
PSP
353SPhosphorylationKinaseRPS6KA1Q15418
GPS
355TPhosphorylationKinaseRPS6KA1Q15418
GPS
375SPhosphorylationKinaseBRSK1Q8TDC3-2
GPS
375SPhosphorylationKinaseBRSK1Q8TDC3
Uniprot
375SPhosphorylationKinasePLK1P53350
PSP
375SPhosphorylationKinaseMAPK14Q16539
Uniprot
375SPhosphorylationKinaseMAPKAPK2P49137
PSP
397SPhosphorylationKinasePLK1P53350
PSP
404TPhosphorylationKinasePLK1P53350
PSP
465SPhosphorylationKinasePLK1P53350
PSP
513SPhosphorylationKinasePLK1P53350
PSP
563SPhosphorylationKinaseCHEK1O14757
GPS
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:21807946
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:21807946

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
169SPhosphorylation

15908796
323SPhosphorylation

11333986
353SPhosphorylation

15128871
375SPhosphorylation

11333986

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MPIP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KRT85_HUMANKRT85physical
17353931
PHB2_HUMANPHB2physical
17353931
K1H1_HUMANKRT31physical
17353931
KRT35_HUMANKRT35physical
17353931
ESR1_HUMANESR1physical
11689696
KAT2B_HUMANKAT2Bphysical
11689696
CHK1_HUMANCHEK1physical
9278511
MK14_HUMANMAPK14physical
11333986
1433F_HUMANYWHAHphysical
10713667
1433Z_HUMANYWHAZphysical
10713667
1433B_HUMANYWHABphysical
10713667
1433B_HUMANYWHABphysical
7644510
1433E_HUMANYWHAEphysical
7644510
ANDR_HUMANARphysical
12569365
FOXM1_HUMANFOXM1physical
15024056
FBW1A_HUMANBTRCphysical
15845771
CDK1_HUMANCDK1physical
11516829
CDK5_HUMANCDK5physical
11516829
CDC5L_HUMANCDC5Lphysical
26496610
CENPB_HUMANCENPBphysical
26496610
IF4B_HUMANEIF4Bphysical
26496610
1433B_HUMANYWHABphysical
26496610
1433G_HUMANYWHAGphysical
26496610
1433F_HUMANYWHAHphysical
26496610
1433Z_HUMANYWHAZphysical
26496610
FBW1A_HUMANBTRCphysical
26496610
1433T_HUMANYWHAQphysical
26496610
WDR6_HUMANWDR6physical
26496610
FBW1B_HUMANFBXW11physical
26496610
FBW1A_HUMANBTRCphysical
27880917
FBW1B_HUMANFBXW11physical
27880917
PPM1F_HUMANPPM1Fphysical
27880917
1433E_HUMANYWHAEphysical
27880917
MPIP2_HUMANCDC25Bphysical
27432908
FBW1B_HUMANFBXW11physical
27432908
CC28A_HUMANCCDC28Aphysical
27432908
1433F_HUMANYWHAHphysical
27432908
ANM1_HUMANPRMT1physical
27432908
CCNB1_HUMANCCNB1physical
27432908
CDC20_HUMANCDC20physical
27432908
1433G_HUMANYWHAGphysical
27432908
MISSL_HUMANMAPK1IP1Lphysical
27432908
CALU_HUMANCALUphysical
27432908
STK39_HUMANSTK39physical
27432908
1433B_HUMANYWHABphysical
27432908
RCN1_HUMANRCN1physical
27432908
1433Z_HUMANYWHAZphysical
27432908
SKP1_HUMANSKP1physical
27432908
PSME3_HUMANPSME3physical
27432908
1433E_HUMANYWHAEphysical
27432908
CUL1_HUMANCUL1physical
27432908
CDK3_HUMANCDK3physical
27432908
FBW1B_HUMANFBXW11physical
28514442
1433Z_HUMANYWHAZphysical
28514442
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
DEN1A_HUMANDENND1Aphysical
27173435
SRGP2_HUMANSRGAP2physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
ZN638_HUMANZNF638physical
27173435
SRS12_HUMANSRSF12physical
27173435
SYDE1_HUMANSYDE1physical
27173435
AGAP1_HUMANAGAP1physical
27173435
CDK16_HUMANCDK16physical
27173435
F110B_HUMANFAM110Bphysical
27173435
UBP21_HUMANUSP21physical
27173435
AN34A_HUMANANKRD34Aphysical
27173435
FA53C_HUMANFAM53Cphysical
27173435
F110A_HUMANFAM110Aphysical
27173435
TBC25_HUMANTBC1D25physical
27173435
MAST3_HUMANMAST3physical
27173435
HDAC4_HUMANHDAC4physical
27173435
RAB3I_HUMANRAB3IPphysical
27173435
TIAM1_HUMANTIAM1physical
27173435
NADK_HUMANNADKphysical
27173435
M3K21_HUMANKIAA1804physical
27173435
NF1_HUMANNF1physical
27173435
CBY1_HUMANCBY1physical
27173435
NGAP_HUMANRASAL2physical
27173435
MELK_HUMANMELKphysical
27173435
CING_HUMANCGNphysical
27173435
PKHA7_HUMANPLEKHA7physical
27173435
AFAD_HUMANMLLT4physical
27173435
DEP1B_HUMANDEPDC1Bphysical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
SH3B4_HUMANSH3BP4physical
27173435
CAMP2_HUMANCAMSAP2physical
27173435
PKHA5_HUMANPLEKHA5physical
27173435
NAV1_HUMANNAV1physical
27173435

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MPIP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates theG2/M transition and S phase progression in response to UVirradiation.";
Manke I.A., Nguyen A., Lim D., Stewart M.Q., Elia A.E., Yaffe M.B.;
Mol. Cell 17:37-48(2005).
Cited for: PHOSPHORYLATION AT SER-323 BY MAPKAPK2.
"CDC25B phosphorylated by pEg3 localizes to the centrosome and thespindle poles at mitosis.";
Mirey G., Chartrain I., Froment C., Quaranta M., Bouche J.P.,Monsarrat B., Tassan J.P., Ducommun B.;
Cell Cycle 4:806-811(2005).
Cited for: PHOSPHORYLATION AT SER-169, AND SUBCELLULAR LOCATION.
"Phosphorylation of CDC25B by Aurora-A at the centrosome contributesto the G2-M transition.";
Dutertre S., Cazales M., Quaranta M., Froment C., Trabut V.,Dozier C., Mirey G., Bouche J.P., Theis-Febvre N., Schmitt E.,Monsarrat B., Prigent C., Ducommun B.;
J. Cell Sci. 117:2523-2531(2004).
Cited for: SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-353 BY AURKA.
"Human pEg3 kinase associates with and phosphorylates CDC25Bphosphatase: a potential role for pEg3 in cell cycle regulation.";
Davezac N., Baldin V., Blot J., Ducommun B., Tassan J.P.;
Oncogene 21:7630-7641(2002).
Cited for: PHOSPHORYLATION AT SER-323.
"Initiation of a G2/M checkpoint after ultraviolet radiation requiresp38 kinase.";
Bulavin D.V., Higashimoto Y., Popoff I.J., Gaarde W.A., Basrur V.,Potapova O., Appella E., Fornace A.J. Jr.;
Nature 411:102-107(2001).
Cited for: PHOSPHORYLATION AT SER-323 AND SER-375, AND INTERACTION WITH MAPK14AND 14-3-3 PROTEINS.

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