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Protein Page:
Cdc25A (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
Cdc25A a member of the MPI phosphatase family. Functions as a dosage-dependent inducer in mitotic control.. Required for progression from G1 to the S phase of the cell cycle. It activates the cyclin-dependent kinase CDC2 by removing two phosphate groups. CDC25A is specifically degraded in response to DNA damage, which prevents cells with chromosomal abnormalities from progressing through cell division. CDC25A is an oncogene, although its exact role in oncogenesis has not been demonstrated. Two splice variant isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: EC 3.1.3.48; Motility/polarity/chemotaxis; Protein phosphatase, dual-specificity
Cellular Component: nucleoplasm; cytosol
Molecular Function: protein binding; protein tyrosine phosphatase activity; protein kinase binding
Biological Process: mitosis; cell proliferation; response to radiation; regulation of cell cycle; mitotic cell cycle; regulation of cyclin-dependent protein kinase activity; G2/M transition of mitotic cell cycle; DNA replication; G1/S transition of mitotic cell cycle
Reference #:  P30304 (UniProtKB)
Alt. Names/Synonyms: CDC25A; CDC25A2; cell division cycle 25 homolog A (S. pombe); cell division cycle 25A; Dual specificity phosphatase Cdc25A; M-phase inducer phosphatase 1; MPIP1
Gene Symbols: CDC25A
Molecular weight: 59,087 Da
Basal Isoelectric point: 6.49  Predict pI for various phosphorylation states
CST Pathways:  G1/S Checkpoint  |  G2/M DNA Damage Checkpoint
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Cdc25A

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: T507‑p
cell cycle regulation: S18‑p, S76‑p, S82‑p, S88‑p, S116‑p, S513‑p, S519‑p
activity, inhibited: T507‑p
enzymatic activity, inhibited: T507‑p
molecular association, regulation: S76‑p, S79‑p, T80‑p, S82‑p, S178‑p, T507‑p
phosphorylation: S76‑p, S79‑p, T80‑p
protein degradation: S76‑p, S79‑p, T80‑p, S82‑p, S88‑p, S124‑p, S178‑p, S279‑p, S293‑p, S513‑p, S519‑p
protein stabilization: S18‑p, S116‑p
ubiquitination: S76‑p, S79‑p, T80‑p, S82‑p, S88‑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
 
3 1 S18-p RRLLFACsPPPASQP
11 1 S76-p SNLQRMGsSEstDsG
3 0 S79-p QRMGsSEstDsGFCL
2 0 T80-p RMGsSEstDsGFCLD
5 0 S82-p GsSEstDsGFCLDsP
3 0 S88-p DsGFCLDsPGPLDSK
0 1 S107-p NPMRRIHsLPQKLLG
2 1 S116-p PQKLLGCsPALKRSH
6 0 S124-p PALKRSHsDsLDHDI
0 1 S126-p LKRSHsDsLDHDIFQ
3 0 S178-p LFTQRQNsAPARMLS
1 0 S279-p VLKRPERsQEESPPG
2 0 S293-p GSTKRRKsMsGASPK
1 1 S295-p TKRRKsMsGASPKES
1 2 S321-p QSLSLASsPKGTIEN
0 1 K343-u DLIGDFSkGYLFHTV
4 1 T507-p KFRTKSRtWAGEKsK
1 1 S513-p RtWAGEKsKREMYsR
1 1 S519-p KsKREMYsRLKKL__
  Cdc25A iso2  
S18 RRLLFACSPPPASQP
S76 SNLQRMGSSESTDSG
S79 QRMGSSESTDSGFCL
T80 RMGSSESTDSGFCLD
S82 GSSESTDSGFCLDSP
S88 DSGFCLDSPGPLDSK
S107 NPMRRIHSLPQKLLG
S116 PQKLLGCSPALKRSH
S124 PALKRSHSDSLDHDI
S126 LKRSHSDSLDHDIFQ
- gap
S239 VLKRPERSQEESPPG
S253 GSTKRRKSMSGASPK
S255 TKRRKSMSGASPKES
S281 QSLSLASSPKGTIEN
K303 DLIGDFSKGYLFHTV
T467 KFRTKSRTWAGEKSK
S473 RTWAGEKSKREMYSR
S479 KSKREMYSRLKKL__
  mouse

 
S18 RRLFFACSPTPAPQP
S75-p SSLQRMGsSESTDSG
S78 QRMGsSESTDSGFCL
T79 RMGsSESTDSGFCLD
S81 GsSESTDSGFCLDSP
S87 DSGFCLDSPGPLDSK
S106 ISLTRINSLPQKLLG
S115 PQKLLGCSPALKRSH
S123-p PALKRSHsDSLDHDT
S125 LKRSHsDSLDHDTFH
S172 PFTHRQNSAPARMLS
S271 VLKRADRSHEEPPRG
S284 RGTKRRKSVPSPVKA
P286 TKRRKSVPSPVKAKA
S311 QSLSLMSSPKGTIEN
K333 DLIGDFSKGYLFNTV
T497 KFRTKSRTWAGEKSK
R503 under review
S509 KSKREMYSRLKKL__
  rat

 
S18 RRLLFTCSPTPAPQP
S76 SSLQRMGSSESTDSG
S79 QRMGSSESTDSGFCL
T80 RMGSSESTDSGFCLD
S82 GSSESTDSGFCLDSP
S88 DSGFCLDSPGPLDSK
C107 ISLRRINCLPQKLLG
S116 PQKLLGCSPALKRSH
S124 PALKRSHSDSLDHDI
S126 LKRSHSDSLDHDIFQ
S178 PFTHRQNSAPARMLS
S283 AVKRADRSHEESPRG
S296 RGTKRRKSSEASPVK
S297 GTKRRKSSEASPVKA
F322 QSLSLTSFPKGTIEN
K344 DLIGDFSKGYLFHTV
T508 KFRTKSRTWAGEKSK
S514 RTWAGEKSKREMYSR
S520 KSKREMYSRLKKL__
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