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Protein Page:
Cdc25B (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Cdc25B a member of the MPI phosphatase family. Activates the cyclin dependent kinase CDC2 by removing two phosphate groups and it is required for entry into mitosis. Shuttles between the nucleus and the cytoplasm due to nuclear localization and nuclear export signals. The protein is nuclear in the M and G1 phases of the cell cycle and moves to the cytoplasm during S and G2. CDC25B has oncogenic properties, although its role in tumor formation has not been determined. At least four transcript variants for this gene exist. Three splice variant isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Protein phosphatase, dual-specificity; Motility/polarity/chemotaxis; EC 3.1.3.48; Nuclear receptor co-regulator
Cellular Component: nucleoplasm; spindle pole; centrosome; intracellular; cytosol
Molecular Function: protein tyrosine phosphatase activity; protein kinase binding
Biological Process: mitosis; cell division; positive regulation of protein kinase activity; positive regulation of cell proliferation; mitotic cell cycle; positive regulation of mitotic cell cycle; G2/M transition of mitotic cell cycle; protein amino acid phosphorylation; oocyte maturation; female meiosis I
Reference #:  P30305 (UniProtKB)
Alt. Names/Synonyms: CDC25B; CDC25HU2; cell division cycle 25 homolog B (S. pombe); cell division cycle 25B; Dual specificity phosphatase Cdc25B; M-phase inducer phosphatase 2; MPIP2
Gene Symbols: CDC25B
Molecular weight: 64,987 Da
Basal Isoelectric point: 6  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Cdc25B
Protein Structure Not Found.


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Sites Implicated In
cell cycle regulation: S323‑p, S353‑p
enzymatic activity, induced: S321‑p
enzymatic activity, inhibited: S230‑p
intracellular localization: S321‑p
molecular association, regulation: S321‑p, S323‑p, S375‑p
phosphorylation: S321‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

► Hide Isoforms 		 
0 1 S15 PAPGSALSPAGVCGG
0 1 S42-p GSHGLLGsPVRAAAS
1 0 S50-p PVRAAASsPVttLtQ
1 0 T53-p AAASsPVttLtQtMH
1 0 T54-p AASsPVttLtQtMHD
1 0 T56-p SsPVttLtQtMHDLA
1 0 T58-p PVttLtQtMHDLAGL
0 2 S89-p RSRLTHLsLSRRASE
0 1 S91 RLTHLsLSRRASEsS
0 1 S97-p LSRRASEsSLSSESS
2 0 S115 DAGLCMDSPSPMDPH
2 0 S117 GLCMDSPSPMDPHMA
1 0 T127-p DPHMAEQtFEQAIQA
3 22 S151-p FAIRRFQsMPVRLLG
1 3 S160-p PVRLLGHsPVLRNIt
1 0 T167-p sPVLRNItNsQAPDG
3 2 S169-p VLRNItNsQAPDGRR
0 1 S178-p APDGRRKsEAGsGAA
0 1 S182-p RRKsEAGsGAAssSG
1 0 S186-p EAGsGAAssSGEDKE
1 2 S187-p AGsGAAssSGEDKEN
1 0 S209-p PWKPTHPsSTHALAE
4 0 S230-p AFAQRPSsAPDLMCL
0 1 S238-p APDLMCLsPDRkMEV
0 1 K242-u MCLsPDRkMEVEELs
2 7 S249-p kMEVEELsPLALGRF
1 0 T265-p LTPAEGDtEEDDGFV
1 0 S291-p AVPPGMEsLISAPLV
0 1 K303-u PLVKTLEkEEEkDLV
0 1 K307-u TLEkEEEkDLVMySK
0 1 Y312-p EEkDLVMySKCQRLF
2 2 S321-p KCQRLFRsPsMPCSV
11 23 S323-p QRLFRsPsMPCSVIR
6 12 S353-p VQNKRRRsVtPPEEQ
0 6 T355-p NKRRRsVtPPEEQQE
4 9 S375-p ARVLRSKsLCHDEIE
1 0 S397-p RELIGDYskAFLLQt
0 2 K398-u ELIGDYskAFLLQtV
1 0 T404-p skAFLLQtVDGkHQD
0 1 K408-u LLQtVDGkHQDLkYI
0 1 K413-u DGkHQDLkYISPETM
0 1 K452-u EYEGGHIkTAVNLPL
1 0 S465-p PLERDAEsFLLKSPI
1 0 S513-p RAVNDYPsLYYPEMY
0 1 K523-u YPEMYILkGGYKEFF
0 2 T556-p AFKDELKtFRLKTRs
1 1 S563-p tFRLKTRsWAGERSR
  Cdc25B iso2  
S15 PAPGSALSPAGVCGG
S42 GSHGLLGSPVRAAAS
S50 PVRAAASSPVTTLTQ
T53 AAASSPVTTLTQTMH
T54 AASSPVTTLTQTMHD
T56 SSPVTTLTQTMHDLA
T58 PVTTLTQTMHDLAGL
S75 RSRLTHLSLSRRASE
S77 RLTHLSLSRRASESS
S83 LSRRASESSLSSESS
S101-p DAGLCMDsPsPMDPH
S103-p GLCMDsPsPMDPHMA
T113 DPHMAEQTFEQAIQA
S137 FAIRRFQSMPVRLLG
S146-p PVRLLGHsPVLRNIT
T153 sPVLRNITNSQAPDG
S155 VLRNITNSQAPDGRR
S164 APDGRRKSEAGSGAA
S168 RRKSEAGSGAASSSG
S172 EAGSGAASSSGEDKE
S173 AGSGAASSSGEDKEN
S195 PWKPTHPSSTHALAE
S216 AFAQRPSSAPDLMCL
S224 APDLMCLSPDRKMEV
K228 MCLSPDRKMEVEELS
S235 KMEVEELSPLALGRF
T251 LTPAEGDTEEDDGFV
S277 AVPPGMESLISAPLV
K289 PLVKTLEKEEEKDLV
K293 TLEKEEEKDLVMYSK
Y298 EEKDLVMYSKCQRLF
S307-p KCQRLFRsPsMPCSV
S309-p QRLFRsPsMPCSVIR
S339 VQNKRRRSVTPPEEQ
T341 NKRRRSVTPPEEQQE
S361 ARVLRSKSLCHDEIE
S383 RELIGDYSKAFLLQT
K384 ELIGDYSKAFLLQTV
T390 SKAFLLQTVDGKHQD
K394 LLQTVDGKHQDLKYI
K399 DGKHQDLKYISPETM
K438 EYEGGHIKTAVNLPL
S451 PLERDAESFLLKSPI
S499 RAVNDYPSLYYPEMY
K509 YPEMYILKGGYKEFF
T542 AFKDELKTFRLKTRS
S549 TFRLKTRSWAGERSR
  Cdc25B iso3  
S15 PAPGSALSPAGVCGG
S42 GSHGLLGSPVRAAAS
S50 PVRAAASSPVTTLTQ
T53 AAASSPVTTLTQTMH
T54 AASSPVTTLTQTMHD
T56 SSPVTTLTQTMHDLA
T58 PVTTLTQTMHDLAGL
S89 RSRLTHLSLSRRASE
S91 RLTHLSLSRRASESS
S97 LSRRASESSLSSESS
S115 DAGLCMDSPSPMDPH
S117 GLCMDSPSPMDPHMA
T127 DPHMAEQTFEQAIQA
S151-p FAIRRFQsMPDGFVF
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S168 PWKPTHPSSTHALAE
S189 AFAQRPSSAPDLMCL
S197 APDLMCLSPDRKMEV
K201 MCLSPDRKMEVEELS
S208 KMEVEELSPLALGRF
T224 LTPAEGDTEEDDGFV
S250 AVPPGMESLISAPLV
K262 PLVKTLEKEEEKDLV
K266 TLEKEEEKDLVMYSK
Y271 EEKDLVMYSKCQRLF
S280 KCQRLFRSPSMPCSV
S282 QRLFRSPSMPCSVIR
S312 VQNKRRRSVTPPEEQ
T314 NKRRRSVTPPEEQQE
S334 ARVLRSKSLCHDEIE
S356 RELIGDYSKAFLLQT
K357 ELIGDYSKAFLLQTV
T363 SKAFLLQTVDGKHQD
K367 LLQTVDGKHQDLKYI
K372 DGKHQDLKYISPETM
K411 EYEGGHIKTAVNLPL
S424 PLERDAESFLLKSPI
S472 RAVNDYPSLYYPEMY
K482 YPEMYILKGGYKEFF
T515 AFKDELKTFRLKTRS
S522 TFRLKTRSWAGERSR
  mouse

 
S15-p SAPGSALsPARVLGG
S42 ESDGFLGSPEPTASS
S50 PEPTASSSPVTTLTQ
T53 TASSSPVTTLTQTMH
T54 ASSSPVTTLTQTMHN
T56 SSPVTTLTQTMHNLA
T58 PVTTLTQTMHNLAGL
S87 QNRLADLSLsRRTSE
S89-p RLADLSLsRRTSECS
C95 LsRRTSECSLSSESS
S113 DAGLCMDSPSPVDPQ
S115 GLCMDSPSPVDPQMA
T125 DPQMAERTFEQAIQA
S149-p FTIKRFRsLPVRLLE
S158-p PVRLLEHsPVLQSIT
T165 sPVLQSITNSRALDS
S167 VLQSITNSRALDSWR
T176 ALDSWRKTEAGYRAA
R181 RKTEAGYRAAANsPG
A184 EAGYRAAANsPGEDK
S186-p GYRAAANsPGEDKEN
S208 PQELPHSSSAQALAE
S229-p AFTQRPSsAPDLMCL
T237 APDLMCLTTEWKMEV
K241 MCLTTEWKMEVEELs
S248-p KMEVEELsPVAQSSS
S263 LTPVERASEEDDGFV
N289 KVPAGMENLISAPLV
K301 PLVKKLDKEEEQDLI
Q305 KLDKEEEQDLIMFSK
F310 EEQDLIMFSKCQRLF
S319 KCQRLFRSPsMPCSV
S321-p QRLFRSPsMPCSVIR
S351-p VQSKRRKsVtPLEEQ
T353-p SKRRKsVtPLEEQQL
S372-p ARVFRSKsLCHEIEN
S393 RGLIGDYSKAFLLQT
K394 GLIGDYSKAFLLQTV
T400 SKAFLLQTVDGKHQD
K404 LLQTVDGKHQDLKYI
K409 DGKHQDLKYISPETM
K448 EYEGGHIKNAVNLPL
T461 PLERDAETFLLQRPI
S509 RAANDYPSLYYPEMY
K519 YPEMYILKGGYKEFF
N552 AFRDELRNFRLKTRS
S559 NFRLKTRSWAGERSR
  rat

 
S15 SAPGSALSTARVLGG
S42 GSDGLLGSPERAASS
S50 PERAASSSPVTTLTQ
T53 AASSSPVTTLTQTMY
T54 ASSSPVTTLTQTMYN
T56 SSPVTTLTQTMYNLA
T58 PVTTLTQTMYNLAGL
S87 QNRLTDLSLSRRTSE
S89 RLTDLSLSRRTSECS
C95 LSRRTSECSLSSESS
S113 DAGLCMDSPSPMDPQ
S115 GLCMDSPSPMDPQTA
T125 DPQTAERTFEQAIQA
V148 QFTIKASVFASEAAG
S157 ASEAAGHSPVLQNIT
T164 SPVLQNITNSQALDS
S166 VLQNITNSQALDSWE
D175 ALDSWEKDEAGYRAA
Y179 WEKDEAGYRAASSPG
S183 EAGYRAASSPGEDKE
S184 AGYRAASSPGEDKEN
S206 PQKLPHSSSARALAE
S227 AFTQRPSSAPDLMCL
T235 APDLMCLTTDGKMDV
K239 MCLTTDGKMDVEEAS
S246 KMDVEEASPVAQSSS
C261 LTPVERACEEDDGFV
N287 MVPAGMENLISAPLV
K299 PLVKKLDKEEEQDLI
Q303 KLDKEEEQDLIMFSK
F308 EEQDLIMFSKCQRLF
S317 KCQRLFRSPSMPCSV
S319 QRLFRSPSMPCSVIR
S349 VLSKRRKSGTPLEEQ
T351 SKRRKSGTPLEEQQL
S370 ARVFRSKSLCHEIES
S391 RGLIGDYSKAFLLQT
K392 GLIGDYSKAFLLQTV
T398 SKAFLLQTVDGKHQD
K402 LLQTVDGKHQDLKYI
K407 DGKHQDLKYISPETM
K446 EYEGGHIKNAVNLPL
T459 PLEPDAETFLLKHPI
S507 RAANDYPSLYYPEMY
K517 YPEMYILKGGYKEFF
N550 AFRDELRNFRLKTRS
S557 NFRLKTRSWAGERST
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