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P48968 (MPIP3_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
M-phase inducer phosphatase 3
EC=3.1.3.48
Alternative name(s):
Dual specificity phosphatase Cdc25C
Gene names
Name:CDC25C
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. Directly dephosphorylates CDK1 and activates its kinase activity. When phosphorylated, highly effective in activating G2 cells into prophase By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with MAPK14 and 14-3-3 proteins By similarity. When phosphorylated at Ser-126 and/or Thr-127, interacts with PLK1 By similarity.

Subcellular location

Nucleus By similarity.

Post-translational modification

Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-219 promotes nuclear translocation. Ser-226 is a minor phosphorylation site By similarity. Phosphorylation by CDK1 occurs at G2 and G2-M transition and leads to increased activity By similarity.

Sequence similarities

Belongs to the MPI phosphatase family.

Contains 1 rhodanese domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentNucleus
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological_processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-tyrosine dephosphorylation

Inferred from electronic annotation. Source: GOC

   Cellular_componentnucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420M-phase inducer phosphatase 3
PRO_0000198649

Regions

Domain266 – 373108Rhodanese

Sites

Active site3221 By similarity

Amino acid modifications

Modified residue381Phosphoserine By similarity
Modified residue541Phosphoserine By similarity
Modified residue581Phosphoserine By similarity
Modified residue611Phosphoserine By similarity
Modified residue641Phosphothreonine; by CDK1 By similarity
Modified residue1261Phosphoserine By similarity
Modified residue1271Phosphothreonine; by CDK1 By similarity
Modified residue1981Phosphoserine; by CDK1 By similarity
Modified residue2191Phosphoserine; by PLK3 By similarity
Modified residue2261Phosphoserine; by PLK3 By similarity
Modified residue4181Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P48968 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: D7564B0AF2124783

FASTA42047,327
        10         20         30         40         50         60 
MSTGPFPSSR REESSVSAPS FRFSQRKMLN LLLERNTSFT QDFPRSPGDK LLDSTNLSIL 

        70         80         90        100        110        120 
SGGTPKRCLD LSNLSNGEMS ASPLITSADF DDTGSLDSSG PQDVQLTEKN HHQDPMKGIP 

       130        140        150        160        170        180 
VQLLCSTPNA LDHSHRKKDA VRGLSANKEN INTNLKTLQW ESPRIPRFQN TPGDPLASPL 

       190        200        210        220        230        240 
PLLGNGVSMD TEVRSLGSPI TAVPKLSKNL NLEDQEEISE EPMEFSLEDH DTKECVLPTV 

       250        260        270        280        290        300 
SGKHQDLKYI TPDTVAALLS GKFQGLIEKF YIIDCRYPYE YLGGHILGAI NLCSQKELHE 

       310        320        330        340        350        360 
FFLKKPIVPL DIQKRVIIVF LCEFSSERGP RMCRSLRRKD RALNQYPALY YPELYILKGG 

       370        380        390        400        410        420 
YRDFFPEYTE LCEPQGYCPM HHQDHQAELL MWRNQSKAQE GERQLSEQIA LLMKKGVSLP

« Hide

References

[1]"Chromosome condensation caused by loss of RCC1 function requires the cdc25C protein that is located in the cytoplasm."
Seki T., Yamashita K., Nishitani H., Takagi T., Russell P., Nishimoto T.
Mol. Biol. Cell 3:1373-1388(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D10878 mRNA. Translation: BAA01646.1.

3D structure databases

ProteinModelPortalP48968.
SMRP48968. Positions 232-386.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG052501.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PANTHERPTHR10828. PTHR10828. 1 hit.
PfamPF06617. M-inducer_phosp. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSPR00716. MPIPHPHTASE.
SMARTSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. Rhodanese-like. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMPIP3_MESAU
AccessionPrimary (citable) accession number: P48968
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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