P48967 (MPIP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 116.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: M-phase inducer phosphatase 3 EC=3.1.3.48 Alternative name(s): Dual specificity phosphatase Cdc25C | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 447 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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. May be involved in regulating the proliferation of T-lymphocytes following cytokine stimulation. |
| 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-128 and/or Thr-129, interacts with PLK1 By similarity. |
| Subcellular location | |
| Tissue specificity | Spleen and thymus. |
| 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. |
| Sequence similarities | Belongs to the MPI phosphatase family. Contains 1 rhodanese domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell cycle Cell division Mitosis |
| Cellular component | Nucleus |
| Molecular function | Hydrolase Protein phosphatase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | M phase of mitotic cell cycle Inferred from electronic annotation. Source: InterPro cell divisionInferred from electronic annotation. Source: UniProtKB-KW mitosisInferred from electronic annotation. Source: UniProtKB-KW peptidyl-tyrosine dephosphorylationInferred from electronic annotation. Source: GOC |
| Cellular_component | cytoplasm Inferred from direct assay PubMed 12937170. Source: MGI nucleusInferred from direct assay PubMed 12937170. Source: MGI |
| Molecular_function | protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 447 | 447 | M-phase inducer phosphatase 3 | PRO_0000198648 | |||||
Regions | |||||||||
| Domain | 294 – 401 | 108 | Rhodanese | ||||||
Sites | |||||||||
| Active site | 350 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 38 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 56 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 60 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 63 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 66 | 1 | Phosphothreonine; by CDK1 By similarity | ||||||
| Modified residue | 128 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 129 | 1 | Phosphothreonine; by CDK1 By similarity | ||||||
| Modified residue | 192 | 1 | Phosphoserine; by CDK1 By similarity | ||||||
| Modified residue | 213 | 1 | Phosphoserine; by PLK3 By similarity | ||||||
| Modified residue | 220 | 1 | Phosphoserine; by PLK3 By similarity | ||||||
| Modified residue | 445 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 153 – 165 | 13 | INTSL…EWEAP → AAFLLLSLQLNDAGPSCADK HQFKGIGMGGT in AAA37409. Ref.2 | ||||||
| Sequence conflict | 336 | 1 | V → L in AAA74912. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The distinct and developmentally regulated patterns of expression of members of the mouse Cdc25 gene family suggest differential functions during gametogenesis." Wu S., Wolgemuth D.J. Dev. Biol. 170:195-206(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Cloning and characterization of a cdc25 phosphatase from mouse lymphocytes." Nargi J.L., Woodford-Thomas T.A. Immunogenetics 39:99-108(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U15562 mRNA. Translation: AAA74912.1. L16926 mRNA. Translation: AAA37409.1. BC004669 mRNA. Translation: AAH04669.1. |
| IPI | IPI00266454. |
| PIR | I49126. |
| RefSeq | NP_033990.2. NM_009860.2. |
| UniGene | Mm.286602. |
3D structure databases | |
| ProteinModelPortal | P48967. |
| SMR | P48967. Positions 255-421. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P48967. 1 interaction. |
PTM databases | |
| PhosphoSite | P48967. |
Proteomic databases | |
| PaxDb | P48967. |
| PRIDE | P48967. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000060710; ENSMUSP00000055427; ENSMUSG00000044201. |
| GeneID | 12532. |
| KEGG | mmu:12532. |
| UCSC | uc008elf.1. mouse. |
Organism-specific databases | |
| CTD | 995. |
| MGI | MGI:88350. Cdc25c. |
Phylogenomic databases | |
| eggNOG | COG5105. |
| HOGENOM | HOG000082672. |
| HOVERGEN | HBG052501. |
| InParanoid | P48967. |
| KO | K05867. |
| OMA | FRSNQRK. |
| OrthoDB | EOG47D9G1. |
Gene expression databases | |
| ArrayExpress | P48967. |
| Bgee | P48967. |
| CleanEx | MM_CDC25C. |
| Genevestigator | P48967. |
Family and domain databases | |
| Gene3D | 3.40.250.10. 1 hit. |
| InterPro | IPR000751. MPI_Phosphatase. IPR001763. Rhodanese-like_dom. [Graphical view] |
| PANTHER | PTHR10828. PTHR10828. 1 hit. |
| Pfam | PF06617. M-inducer_phosp. 1 hit. PF00581. Rhodanese. 1 hit. [Graphical view] |
| PRINTS | PR00716. MPIPHPHTASE. |
| SMART | SM00450. RHOD. 1 hit. [Graphical view] |
| SUPFAM | SSF52821. Rhodanese-like. 1 hit. |
| PROSITE | PS50206. RHODANESE_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 281566. |
| SOURCE | Search... |
Entry information
| Entry name | MPIP3_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P48967 Secondary accession number(s): Q99KG6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
