P48967 · MPIP3_MOUSE
- ProteinM-phase inducer phosphatase 3
- GeneCdc25c
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids447 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 350 | |||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | mitochondrial intermembrane space | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Molecular Function | protein kinase binding | |
Molecular Function | protein tyrosine phosphatase activity | |
Molecular Function | WW domain binding | |
Biological Process | cell division | |
Biological Process | G2/M transition of mitotic cell cycle | |
Biological Process | positive regulation of G2/M transition of mitotic cell cycle | |
Biological Process | positive regulation of G2/MI transition of meiotic cell cycle | |
Biological Process | spermatogenesis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameM-phase inducer phosphatase 3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP48967
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000198648 | 2-447 | M-phase inducer phosphatase 3 | |||
Sequence: STGPIPPASEEGSFVSAPSFRSKQRKILHLLLERNTSFTIRSDFPESPKDKLHDSANLSILSGGTPKCCLDLSNLSSGEMSASPLTTSADLEDNGSLDSSGPLDRQLTGKDFHQDLMKGIPVQLLCSTPNAMNHGHRKKIAKRSTSAHKENINTSLKALEWEAPRTPRFRKMPGGPLTSPLCELEMKHLGSPITTVPKLSQNVKLEDQERISEDPMECSLGDQDAKGLSLRKMVPLCDMNAIQMEEEESGSELLIGDFSKVCVLPTVPGKHPDLKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLHSQKELHEFFLRKPVVPLDIQKRVIIVFLCEFSSERGPRMCRSLREKDRALNQYPALYYPELYILKGGYRDFFPEYMELCDPQSYCPMLHQDHQAELLSWRSQSKAQEGERQLQGQIALLVKGASPQ | ||||||
Modified residue | 20 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 38 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 56 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 60 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 63 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 66 | Phosphothreonine; by CDK1 | ||||
Sequence: T | ||||||
Modified residue | 128 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 129 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 192 | Phosphoserine; by CDK1 | ||||
Sequence: S | ||||||
Modified residue | 213 | Phosphoserine; by PLK3 | ||||
Sequence: S | ||||||
Modified residue | 220 | Phosphoserine; by PLK3 | ||||
Sequence: S | ||||||
Modified residue | 445 | Phosphoserine | ||||
Sequence: S |
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).
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
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 81-104 | Polar residues | ||||
Sequence: MSASPLTTSADLEDNGSLDSSGPL | ||||||
Region | 81-109 | Disordered | ||||
Sequence: MSASPLTTSADLEDNGSLDSSGPLDRQLT | ||||||
Domain | 294-401 | Rhodanese | ||||
Sequence: VIERFYIIDCRYPYEYLGGHILGALNLHSQKELHEFFLRKPVVPLDIQKRVIIVFLCEFSSERGPRMCRSLREKDRALNQYPALYYPELYILKGGYRDFFPEYMELCD |
Sequence similarities
Belongs to the MPI phosphatase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length447
- Mass (Da)50,046
- Last updated2002-05-27 v2
- Checksum513E51BAB3D1A39E
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A494BAB9 | A0A494BAB9_MOUSE | Cdc25c | 183 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 81-104 | Polar residues | ||||
Sequence: MSASPLTTSADLEDNGSLDSSGPL | ||||||
Sequence conflict | 153-165 | in Ref. 2; AAA37409 | ||||
Sequence: INTSLKALEWEAP → AAFLLLSLQLNDAGPSCADKHQFKGIGMGGT | ||||||
Sequence conflict | 336 | in Ref. 1; AAA74912 | ||||
Sequence: V → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |