P48967 · MPIP3_MOUSE

  • Protein
    M-phase inducer phosphatase 3
  • Gene
    Cdc25c
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

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

Catalytic activity

Features

Showing features for active site.

144750100150200250300350400
TypeIDPosition(s)Description
Active site350

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentmitochondrial intermembrane space
Cellular Componentnucleus
Cellular Componentperinuclear region of cytoplasm
Molecular Functionprotein kinase binding
Molecular Functionprotein tyrosine phosphatase activity
Molecular FunctionWW domain binding
Biological Processcell division
Biological ProcessG2/M transition of mitotic cell cycle
Biological Processpositive regulation of G2/M transition of mitotic cell cycle
Biological Processpositive regulation of G2/MI transition of meiotic cell cycle
Biological Processspermatogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    M-phase inducer phosphatase 3
  • EC number
  • Alternative names
    • Dual specificity phosphatase Cdc25C

Gene names

    • Name
      Cdc25c
    • Synonyms
      Cdc25m1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P48967
  • Secondary accessions
    • Q99KG6

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
ChainPRO_00001986482-447M-phase inducer phosphatase 3
Modified residue20Phosphoserine
Modified residue38Phosphoserine
Modified residue56Phosphoserine
Modified residue60Phosphoserine
Modified residue63Phosphoserine
Modified residue66Phosphothreonine; by CDK1
Modified residue128Phosphoserine
Modified residue129Phosphothreonine
Modified residue192Phosphoserine; by CDK1
Modified residue213Phosphoserine; by PLK3
Modified residue220Phosphoserine; by PLK3
Modified residue445Phosphoserine

Post-translational modification

Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity (By similarity).
Phosphorylated by CHEK1 and MAPKAPK2. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase activity. Phosphorylation by PLK3 at Ser-213 promotes nuclear translocation. Ser-220 is a minor phosphorylation site (By similarity).
Phosphorylation by CDK1 occurs at G2 and G2-M transition and leads to increased activity (By similarity).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Spleen and thymus.

Gene expression databases

Interaction

Subunit

Interacts with MAPK14 and 14-3-3 proteins. When phosphorylated on Ser-128 and/or Thr-129, interacts with PLK1. Interacts with MARK3/C-TAK1.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias81-104Polar residues
Region81-109Disordered
Domain294-401Rhodanese

Sequence similarities

Belongs to the MPI phosphatase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    447
  • Mass (Da)
    50,046
  • Last updated
    2002-05-27 v2
  • Checksum
    513E51BAB3D1A39E
MSTGPIPPASEEGSFVSAPSFRSKQRKILHLLLERNTSFTIRSDFPESPKDKLHDSANLSILSGGTPKCCLDLSNLSSGEMSASPLTTSADLEDNGSLDSSGPLDRQLTGKDFHQDLMKGIPVQLLCSTPNAMNHGHRKKIAKRSTSAHKENINTSLKALEWEAPRTPRFRKMPGGPLTSPLCELEMKHLGSPITTVPKLSQNVKLEDQERISEDPMECSLGDQDAKGLSLRKMVPLCDMNAIQMEEEESGSELLIGDFSKVCVLPTVPGKHPDLKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLHSQKELHEFFLRKPVVPLDIQKRVIIVFLCEFSSERGPRMCRSLREKDRALNQYPALYYPELYILKGGYRDFFPEYMELCDPQSYCPMLHQDHQAELLSWRSQSKAQEGERQLQGQIALLVKGASPQ

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A494BAB9A0A494BAB9_MOUSECdc25c183

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias81-104Polar residues
Sequence conflict153-165in Ref. 2; AAA37409
Sequence conflict336in Ref. 1; AAA74912

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U15562
EMBL· GenBank· DDBJ
AAA74912.1
EMBL· GenBank· DDBJ
mRNA
L16926
EMBL· GenBank· DDBJ
AAA37409.1
EMBL· GenBank· DDBJ
mRNA
BC004669
EMBL· GenBank· DDBJ
AAH04669.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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