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P48966 (MPIP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 90. 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 2
EC=3.1.3.48
Alternative name(s):
Dual specificity phosphatase Cdc25B
Gene names
Name:Cdc25b
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Directly dephosphorylates CDK1 and stimulates its kinase activity By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulation

Stimulated by B-type cyclins.

Subunit structure

Interacts with MAPK14 and 14-3-3 proteins By similarity.

Subcellular location

Cytoplasm › cytoskeleton › centrosome By similarity. Cytoplasm › cytoskeleton › spindle pole By similarity.

Post-translational modification

Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which inhibits the activity of this protein. Phosphorylation at Ser-349 by AURKA might locally participate in the control of the onset of mitosis. Phosphorylation by MELK at Ser-166 promotes localization to the centrosome and the spindle poles during mitosis. Phosphorylation at Ser-319 and Ser-370 by MAPK14 is required for binding to 14-3-3 proteins By similarity.

Sequence similarities

Belongs to the MPI phosphatase family.

Contains 1 rhodanese domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574M-phase inducer phosphatase 2
PRO_0000198646

Regions

Domain425 – 532108Rhodanese

Sites

Active site4811 By similarity

Amino acid modifications

Modified residue1661Phosphoserine; by MELK By similarity
Modified residue2461Phosphoserine By similarity
Modified residue3191Phosphoserine; by MAPKAPK2 and MELK; alternate By similarity
Modified residue3191Phosphoserine; by MELK and MAPK14; alternate By similarity
Modified residue3491Phosphoserine; by AURKA By similarity
Modified residue3701Phosphoserine; by BRSK1 and MAPK14 By similarity

Sequences

Sequence LengthMass (Da)Tools
P48966 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9367CE203B15FAAD

FASTA57464,287
        10         20         30         40         50         60 
MEVPPQKSAP GSALSTARVL GGIQRPRHLS GFGFGSDGLL GSPERAASSS PVTTLTQTMY 

        70         80         90        100        110        120 
NLAGLGSETP KTQVGSLSFQ NRLTDLSLSR RTSECSLSSE SSESSDAGLC MDSPSPMDPQ 

       130        140        150        160        170        180 
TAERTFEQAI QAASRVIQKM QFTIKASVFA SEAAGHSPVL QNITNSQALD SWEKDEAGYR 

       190        200        210        220        230        240 
AASSPGEDKE NDGYIFKMPQ KLPHSSSARA LAEWASRREA FTQRPSSAPD LMCLTTDGKM 

       250        260        270        280        290        300 
DVEEASPVAQ SSSLTPVERA CEEDDGFVDI LESDLKDDDM VPAGMENLIS APLVKKLDKE 

       310        320        330        340        350        360 
EEQDLIMFSK CQRLFRSPSM PCSVIRPILK RLERPHDRDV PVLSKRRKSG TPLEEQQLEE 

       370        380        390        400        410        420 
PKARVFRSKS LCHEIESILD SDHRGLIGDY SKAFLLQTVD GKHQDLKYIS PETMVALLTG 

       430        440        450        460        470        480 
KFSNIVEKFV IVDCRYPYEY EGGHIKNAVN LPLEPDAETF LLKHPITPCN LDKRIILIFH 

       490        500        510        520        530        540 
CEFSSERGPR MCRFIRERDR AANDYPSLYY PEMYILKGGY KEFFPQHPNF CEPQDYRPMN 

       550        560        570 
HAAFRDELRN FRLKTRSWAG ERSTTQLCSR LQDQ

« Hide

References

[1]"Cdc25A is a novel phosphatase functioning early in the cell cycle."
Jinno S., Suto K., Nagata A., Igarashi M., Kanaoka Y., Nojima H., Okayama H.
EMBO J. 13:1549-1556(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: NRK49F.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D16237 mRNA. Translation: BAA03762.1.
IPIIPI00568754.
RefSeqNP_598256.1. NM_133572.1.
UniGeneRn.11312.

3D structure databases

ProteinModelPortalP48966.
SMRP48966. Positions 381-558.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000028864.

PTM databases

PhosphoSiteP48966.

Proteomic databases

PaxDbP48966.
PRIDEP48966.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID171103.
KEGGrno:171103.

Organism-specific databases

CTD994.
RGD621500. Cdc25b.

Phylogenomic databases

eggNOGCOG5105.
HOGENOMHOG000082672.
HOVERGENHBG052501.
KOK05866.

Gene expression databases

ArrayExpressP48966.
GenevestigatorP48966.
GermOnlineENSRNOG00000021248. Rattus norvegicus.

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...

Other

NextBio621786.

Entry information

Entry nameMPIP2_RAT
AccessionPrimary (citable) accession number: P48966
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 90 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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