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Cdc25C (human)

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; nucleus; cytosol Molecular Function: protein binding; WW domain binding; protein tyrosine phosphatase activity; protein kinase binding Biological Process: mitosis; traversing start control point of mitotic cell cycle; regulation of cell cycle; cell proliferation; M phase of mitotic cell cycle; cell division; virus-host interaction; regulation of mitosis; mitotic cell cycle; regulation of cyclin-dependent protein kinase activity; G2/M transition of mitotic cell cycle; DNA replication; cell cycle checkpoint 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:  Cell Cycle: G2/M DNA Damage Checkpoint  |  GPCRs Signaling to MAPK/Erk  |  MAPK/Erk in Growth and Differentiation Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below Cdc25C 3BZI - E=126-134 (human) 3OP3 - A=270-462 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 3BZI 3OP3  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	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

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		T37-p	NLLLERDtsFTVCPD
0	5		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		S146-p	RKRDAMCsSsANkEN
0	1		S148-p	RDAMCsSsANkENDN
1	2		K151-u	MCsSsANkENDNGNL
0	2		Y165-p	LVDSEMKyLGsPItt
4	63		S168-p	SEMKyLGsPIttVPK
0	1		T171-p	KyLGsPIttVPKLDK
0	1		T172-p	yLGsPIttVPKLDKN
1	1		S191-p	EDQAEEIsDELMEFs
3	1		S198-p	sDELMEFsLKDQEAK
0	1		S207-p	KDQEAKVsRsGLyRs
0	1		S209-p	QEAKVsRsGLyRsPs
0	2		Y212-p	KVsRsGLyRsPsMPE
4	10		S214-p	sRsGLyRsPsMPENL
46	42		S216-p	sGLyRsPsMPENLNR
1	0		T236-p	VEKFKDNtIPDKVKK
0	1		C257	GKLRKGLCLKKTVsL
1	4		S263-p	LCLKKTVsLCDITIT
0	1		K317-u	VAALLSGkFQGLIEK
0	1		Y401-p	EDRSLNQyPALYYPE
0	1		Y416-p	LYILKGGyRDFFPEY
0	3		S449-p	TELLRCRsQSKVQEG
0	1		S472-p	ALLVKDMsP______

	Cdc25C iso3
S15	STREEGSSGSGPSFR
T37	NLLLERDTSFTVCPD
S38	LLLERDTSFTVCPDV
T48	VCPDVPRTPVGKFLG
S57	VGKFLGDSANLsILS
S61-p	LGDSANLsILSGsPG
S64	SANLsILSGsPGFFR
S66-p	NLsILSGsPGFFRTS
-	gap
T87	DAQLLCSTPNGLDRG
-	gap
S103	RKRDAMCSSSANKEN
S105	RDAMCSSSANKENDN
K108	MCSSSANKENDNGNL
Y122	LVDSEMKYLGSPITT
S125	SEMKYLGSPITTVPK
T128	KYLGSPITTVPKLDK
T129	YLGSPITTVPKLDKN
S148	EDQAEEISDELMEFS
S155	SDELMEFSLKDQEAK
S164-p	KDQEAKVsRsGLYRs
S166-p	QEAKVsRsGLYRsPs
Y169	KVsRsGLYRsPsMPE
S171-p	sRsGLYRsPsMPENL
S173-p	sGLYRsPsMPENLNR
T193	VEKFKDNTIPDKVKK
C214	GKLRKGLCLKKTVSL
S220	LCLKKTVSLCDITIT
K274	VAALLSGKFQGLIEK
Y358	EDRSLNQYPALYYPE
Y373	LYILKGGYRDFFPEY
S406	TELLRCRSQSKVQEG
S429	ALLVKDMSP______

	mouse
F15	PASEEGSFVSAPSFR
T37	HLLLERNTsFTIRSD
S38-p	LLLERNTsFTIRSDF
S48	IRSDFPESPKDKLHD
S56	PKDKLHDSANLSILS
S60	LHDSANLSILSGGTP
S63	SANLSILSGGTPKCC
T66	LSILSGGTPKCCLDL
-	gap
T129	PVQLLCSTPNAMNHG
K143-u	GHRKKIAkRSTSAHk
S145	RKKIAkRSTSAHkEN
S147	KIAkRSTSAHkENIN
K150-u	kRSTSAHkENINTSL
H189	LCELEMKHLGSPITT
S192	LEMKHLGSPITTVPK
T195	KHLGSPITTVPKLSQ
T196	HLGSPITTVPKLSQN
S213-p	LEDQERIsEDPMECs
S220-p	sEDPMECsLGDQDAK
-	gap
-	gap
-	gap
-	gap
-	gap
-	gap
S230-p	DQDAKGLsLRKMVPL
P236	LsLRKMVPLCDMNAI
K290	VAALLSGKFQSVIER
Y374	KDRALNQYPALYYPE
Y389	LYILKGGYRDFFPEY
S422	AELLSWRSQSKAQEG
S445	ALLVKGASPQ_____

	frog
T15	SSEAPPKTNTGLNFR
C37	NLLREKDCSVTFSPE
S38	LLREKDCSVTFSPEQ
T48-p	FSPEQPLtPVTDLAV
F57	VTDLAVGFSNLSTFS
S61	AVGFSNLSTFSGEtP
S64	FSNLSTFSGEtPKRC
T67-p	LSTFSGEtPKRCLDL
S129	CPRGNMNSVLPRLLC
T138-p	LPRLLCStPSFKKTS
-	gap
S183	EVVDSQFSPTPENKV
T185	VDSQFSPTPENKVDI
K189	FSPTPENKVDISLDE
-	gap
S205-p	CEMNILGsPISADPP
S208	NILGsPISADPPCLD
A209	ILGsPISADPPCLDG
S259	SSMAILLSGPLLNQD
-	gap
S270	LNQDIEVSNVNNISL
S280	NNISLNRSRLYRsPs
Y283	SLNRSRLYRsPsMPE
S285-p	NRSRLYRsPsMPEKL
S287-p	SRLYRsPsMPEKLDR
E307	PVRPLDSETPVRVKR
S337	QPQRRGTSLKKTLSL
S343	TSLKKTLSLCDVDIS
D397	LAALIHGDFSSLVEK
Y481	EDRARNEYPSLYYPE
Y496	LYLLKGGYKDFFPEY
T529	EELLKFRTKCKTSVG
-	gap

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