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Protein Page:
Cdc25C (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Cdc25C 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: Motility/polarity/chemotaxis; Protein phosphatase, dual-specificity; EC 3.1.3.48
Cellular Component: nucleoplasm; perinuclear region of cytoplasm; nucleus; cytosol
Molecular Function: protein binding; WW domain binding; protein tyrosine phosphatase activity; protein kinase binding
Biological Process: cell proliferation; mitosis; viral reproduction; regulation of cell cycle; regulation of mitosis; spermatogenesis; regulation of cyclin-dependent protein kinase activity; mitotic cell cycle; G2/M transition of mitotic cell cycle; DNA replication
Reference #:  P30307 (UniProtKB)
Alt. Names/Synonyms: CDC25; CDC25C; cell division cycle 25 homolog C (S. pombe); cell division cycle 25C; Dual specificity phosphatase Cdc25C; M-phase inducer phosphatase 3; mitosis inducer CDC25; MPIP3; phosphotyrosine phosphatase
Gene Symbols: CDC25C
Molecular weight: 53,365 Da
Basal Isoelectric point: 6.34  Predict pI for various phosphorylation states
CST Pathways:  G2/M DNA Damage Checkpoint  |  GPCR Signaling to MAPKs  |  Growth And Differentiation Control by MAPKs
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Cdc25C

Protein Structure Not Found.


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Sites Implicated In
cell adhesion, altered: T48‑p, T67‑p, S122‑p, T130‑p, S168‑p, S214‑p
cell cycle regulation: T48‑p, T67‑p, S122‑p, T130‑p, S168‑p, S214‑p, S216‑p
enzymatic activity, induced: S214‑p
enzymatic activity, inhibited: S168‑p, S216‑p
intracellular localization: S191‑p, S198‑p, S216‑p, T236‑p, S263‑p
molecular association, regulation: T48‑p, T67‑p, S214‑p, S216‑p, T236‑p
protein degradation: T48‑p, T67‑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-p STREEGSsGSGPsFR
0 1 S20-p GSsGSGPsFRSNQRK
0 6 S38-p LLLERDTsFTVCPDV
5 11 T48-p VCPDVPRtPVGKFLG
0 1 S57-p VGKFLGDsANLsILs
0 3 S61-p LGDsANLsILsGGtP
0 3 S64-p sANLsILsGGtPKRC
4 4 T67-p LsILsGGtPKRCLDL
1 5 S122-p DQHLMKCsPAQLLCS
4 7 T130-p PAQLLCStPNGLDRG
0 2 - gap
0 1 S148-p RDAMCSSsANkENDN
1 2 K151-u MCSSsANkENDNGNL
0 2 Y165-p LVDSEMKyLGsPITT
4 64 S168-p SEMKyLGsPITTVPK
1 1 S191-p EDQAEEIsDELMEFs
3 1 S198-p sDELMEFsLKDQEAK
0 2 Y212-p KVSRSGLyRsPsMPE
4 11 S214-p SRSGLyRsPsMPENL
47 43 S216-p SGLyRsPsMPENLNR
1 0 T236-p VEKFKDNtIPDKVKK
1 0 S247-p KVKKKYFsGQGKLRK
1 5 S263-p LCLKKTVsLCDITIT
0 3 S449-p TELLRCRsQSKVQEG
0 1 S472-p ALLVKDMsP______
9527 : Phospho-cdc25C (Thr48) Antibody
12028 : Phospho-cdc25C (Thr48) (D2H3) Rabbit mAb
9529 : Phospho-cdc25C (Ser198) Antibody
4901 : Phospho-cdc25C (Ser216) (63F9) Rabbit mAb
9528 : Phospho-cdc25C (Ser216) Antibody
  Cdc25C iso3  
S15 STREEGSSGSGPSFR
S20 GSSGSGPSFRSNQRK
S38 LLLERDTSFTVCPDV
T48 VCPDVPRTPVGKFLG
S57 VGKFLGDSANLsILS
S61-p LGDSANLsILSGsPG
S64 SANLsILSGsPGFFR
S66-p NLsILSGsPGFFRTS
- gap
T87 DAQLLCSTPNGLDRG
- gap
S105 RDAMCSSSANKENDN
K108 MCSSSANKENDNGNL
Y122 LVDSEMKYLGSPITT
S125 SEMKYLGSPITTVPK
S148 EDQAEEISDELMEFS
S155 SDELMEFSLKDQEAK
Y169 KVSRSGLYRsPsMPE
S171-p SRSGLYRsPsMPENL
S173-p SGLYRsPsMPENLNR
T193 VEKFKDNTIPDKVKK
S204 KVKKKYFSGQGKLRK
S220 LCLKKTVSLCDITIT
S406 TELLRCRSQSKVQEG
S429 ALLVKDMSP______
  mouse

 
F15 PASEEGSFVSAPSFR
S20 GSFVSAPSFRSKQRK
S38-p LLLERNTsFTIRSDF
S48 IRSDFPESPKDKLHD
S56 PKDKLHDSANLSILS
S60 LHDSANLSILSGGTP
S63 SANLSILSGGTPKCC
T66 LSILSGGTPKCCLDL
- gap
T129 PVQLLCSTPNAMNHG
K143-u GHRKKIAkRSTSAHk
S147 KIAkRSTSAHkENIN
K150-u kRSTSAHkENINTSL
- gap
S192 LEMKHLGSPITTVPK
S213-p LEDQERIsEDPMECs
S220-p sEDPMECsLGDQDAK
- gap
- gap
- gap
- gap
G222 DPMECsLGDQDAKGL
P236 LSLRKMVPLCDMNAI
S422 AELLSWRSQSKAQEG
S445 ALLVKGASPQ_____
  frog

 
T15 SSEAPPKTNTGLNFR
N20 PKTNTGLNFRTNCRM
S38 LLREKDCSVTFSPEQ
T48-p FSPEQPLtPVTDLAV
F57 VTDLAVGFSNLSTFS
S61 AVGFSNLSTFSGEtP
S64 FSNLSTFSGEtPKRC
T67-p LSTFSGEtPKRCLDL
S129 CPRGNMNSVLPRLLC
T138-p LPRLLCStPSFKKTS
- gap
T185 VDSQFSPTPENKVDI
K189 FSPTPENKVDISLDE
- gap
S205-p CEMNILGsPISADPP
S259 SSMAILLSGPLLNQD
- gap
Y283 SLNRSRLYRsPsMPE
S285-p NRSRLYRsPsMPEKL
S287-p SRLYRsPsMPEKLDR
E307 PVRPLDSETPVRVKR
Q323 RSTSSSLQPQEENFQ
S343 TSLKKTLSLCDVDIS
T529 EELLKFRTKCKTSVG
- gap
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