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Dual-Specificity PhosphatasesDual Specificity Phosphatase 3Dual Specificity Phosphatase 6Dual Specificity Phosphatase 1Mitogen-Activated Protein Kinase Phosphatasescdc25 PhosphatasesProtein Tyrosine PhosphatasesPhosphoprotein PhosphatasesProtein Phosphatase 1Phosphoric Monoester HydrolasesProtein Tyrosine Phosphatases, Non-ReceptorSubstrate SpecificityCell Cycle ProteinsPhosphorylationCDC2 Protein KinaseDual Specificity Phosphatase 2Lafora DiseaseAcid PhosphataseProtein Phosphatase 2Molecular Sequence Datacdc42 GTP-Binding ProteinAmino Acid SequenceMAP Kinase Signaling SystemJNK Mitogen-Activated Protein KinasesImmediate-Early ProteinsEnzyme ActivationMitogen-Activated Protein KinasesMitosisGene Expression Regulation, EnzymologicMitogen-Activated Protein Kinase Kinasesp38 Mitogen-Activated Protein KinasesCOS CellsCdc20 ProteinsSequence Homology, Amino AcidMitogen-Activated Protein Kinase 1Signal TransductionBase SequenceProtein BindingProtein-Serine-Threonine KinasesMitogen-Activated Protein Kinase 3SeparaseGlucose-6-PhosphataseBinding SitesDNA, ComplementaryCell LineCyclin BAnaphaseEnzyme InhibitorsExtracellular Signal-Regulated MAP KinasesCdh1 ProteinsHeLa CellsSaccharomyces cerevisiae ProteinsSensitivity and SpecificityRNA, MessengerProtein KinasesCell NucleolusSaccharomyces cerevisiaeCell CycleFungal ProteinsMutationG2 PhaseCell Line, TumorProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 1KineticsOkadaic AcidProtein Tyrosine Phosphatase, Non-Receptor Type 6Schizosaccharomyces pombe ProteinsMyosin-Light-Chain PhosphataseProtein Structure, TertiaryPhosphorylase PhosphataseCyclin-Dependent Kinase 2Protein-Tyrosine KinasesRecombinant Fusion ProteinsRecombinant ProteinsCloning, MolecularChromosome SegregationCDC28 Protein Kinase, S cerevisiaeReceptor-Like Protein Tyrosine Phosphatases, Class 2Cyclin-Dependent KinasesEthers, CyclicAntibody SpecificityNuclear ProteinsPhosphatidate PhosphataseTyrosineCatalytic DomainMutagenesis, Site-Directedcdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCDC2-CDC28 KinasesReceptor-Like Protein Tyrosine Phosphatases, Class 3Cells, CulturedTransfectionReceptor-Like Protein Tyrosine Phosphatases, Class 4Sequence AlignmentIsoenzymesSerineDNA PrimersAmino Acid MotifsBlotting, WesternModels, Molecular
Protein tyrosine phoInhibitorsEnzymesProteinsPotent and selectiveSubfamilySubstrateCatalytic domainSubcellular localizationKinasesDephosphorylation3.48Ygr203wPhosphorylationDistinctYeastEnzymeExpressionFamilyRoleDomainsTestTyrosine-phosphataseProteinCdc25AMitoticProgressionKINASESActivityCellHighLarge
Protein tyrosine pho1
Inhibitors3
  • A large number of potent small-molecule Cdc25 Inhibitors have been identified that bind to the active site and belong to various chemical classes, including natural products, lipophilic acids, quinonoids, electrophiles, sulfonylated aminothiazoles and phosphate bioisosteres. (wikipedia.org)
  • Although some progress has been made in developing potent and selective inhibitors for Cdc25 family of proteins, there is scope for development of novel therapeutic strategies to target them. (wikipedia.org)
  • MA242 is a Dual Inhibitors of MDM2 and NFAT1 for Pancreatic Cancer Therapy. (csnpharm.com)
Enzymes3
  • The Cdc25 enzymes Cdc25A-C are known to control the transitions from G1 to S phase and G2 to M phase. (wikipedia.org)
  • Cdc25 enzymes are well conserved through evolution, and have been isolated from fungi such as yeasts as well as all metazoans examined to date, including humans. (wikipedia.org)
  • Apart from a CX3R motif, which is present at the active site of all known tyrosine phosphatases, Cdc25 does not share any obvious sequence similarity with any of those enzymes. (embl.de)
Proteins2
  • By removing inhibitory phosphate residues from target cyclin-dependent kinases (Cdks), Cdc25 proteins control entry into and progression through various phases of the cell cycle, including mitosis and S ("Synthesis") phase. (wikipedia.org)
  • The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. (embl.de)
Potent and selective1
  • NSC 95397 is a potent and selective irreversible inhibitor of Cdc25 dual specificity phosphatases (K i values are 32, 96 and 40 nM for inhibition of Cdc25A, -B and -C respectively). (tocris.com)
Subfamily2
  • Until very recently, the Cdc25 family was the only subfamily of tyrosine phosphates for which no three-dimensional structural data were available. (embl.de)
  • The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. (nih.gov)
Substrate2
  • Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. (nih.gov)
  • Substrate specificity of AKR1B10 is definitely drastically affected by the mutation of the residue 299 from Cys to Ser. (tam-receptor.com)
Catalytic domain5
  • Cdc25 phosphatase catalytic domain. (embl.de)
  • A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain. (embl.de)
  • The catalytic domain of this dual-specificity phosphatase has recently been mapped to the 180 most C-terminal amino acids. (embl.de)
  • The relationship of Cdc25 to the structurally well-characterized rhodanese spans the entire catalytic domain and served as template for a structural model for human Cdc25a, which is fundamentally different from previously suggested models for Cdc25 catalytic domain organization. (embl.de)
  • A triple mutant of the PTPâ D2 domain (A455N/V457Y/E597D) was also constructed to reconstitute the residues of the PTPâ D1 catalytic domain that are important for phosphatase activity, resulting in only a slight increase in the phosphatase activity compared with the native D2 protein. (bvsalud.org)
Subcellular localization1
  • F-box protein specificity for g1 cyclins is dictated by subcellular localization. (umassmed.edu)
Kinases10
  • Cdc25 activates cyclin dependent kinases by removing phosphate from residues in the Cdk active site. (wikipedia.org)
  • Mammalian Cdc25 phosphatase is responsible for the dephosphorylation of Cdc2 and other cyclin-dependent kinases at Thr14 and Tyr15, thus activating the kinase and allowing cell cycle progression. (embl.de)
  • These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. (nih.gov)
  • Levels of cellular protein phosphorylation are modulated both by protein kinases and phosphatases. (rupress.org)
  • Although the importance of kinases in this process has long been recognized, an appreciation for the complex and fundamental role of phosphatases is more recent. (rupress.org)
  • Through extensive biochemical and genetic analysis, we now know that pathways are not simply switched on with kinases and off with phosphatases. (rupress.org)
  • Furthermore, kinases and phosphatases may work together to modulate the strength of a signal. (rupress.org)
  • Adding further complexity to this picture is the fact that both kinases and phosphatases can function in signaling networks where multiple kinases and phosphatases contribute to the outcome of a pathway. (rupress.org)
  • To fully understand this complex and essential regulatory process, the kinases and phosphatases mediating the changes in cellular phosphorylation must be identified and characterized. (rupress.org)
  • A variety of approaches, including biochemical purification, gene isolation by homology, and genetic screens, have been successfully used for the identification of putative protein kinases and phosphatases. (rupress.org)
Dephosphorylation1
  • Cdk activity can be reactivated after dephosphorylation by Cdc25. (wikipedia.org)
3.483
  • The Cdc25 family of protein dual specificity phosphatases (EC 3.1.3.48 ). (expasy.org)
  • The MKP1/PAC1 family of MAP-kinase phosphatases (EC 3.1.3.48 / EC 3.1.3.16 ). (expasy.org)
  • The Pyp1/Pyp2 family of MAP-kinase phosphatases (EC 3.1.3.48 ). (expasy.org)
Ygr203w1
  • Based on the results of this analysis, we also predict that the budding yeast arsenate resistance protein Acr2 and the ORF Ygr203w encode protein phosphatases with catalytic properties similar to that of the Cdc25 family. (embl.de)
Phosphorylation1
Distinct1
  • An exception is the nematode Caenorhabditis elegans, which has four distinct Cdc25 genes (Cdc-25.1 to Cdc-25.4). (wikipedia.org)
Yeast3
  • Cdc25 is a dual-specificity phosphatase first isolated from the yeast Schizosaccharomyces pombe as a cell cycle defective mutant. (wikipedia.org)
  • Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. (embl.de)
  • non-catalytic domains of yeast PTP-type MAPK-phosphatases. (embl.de)
Enzyme2
  • Yeasts have a single Cdc25 (as well as a distantly related enzyme known as Itsy-bitsy phosphatase 1, or Ibp1). (wikipedia.org)
  • Rhodanese domains, either catalytic or inactive (i.e. where the active-site Cys is replaced by another residue), are also found associated with other protein domains such as MAPK-phosphatases or thiL, an Escherichia coli enzyme involved in thiamin and thiouridine biosynthesis. (expasy.org)
Expression1
  • Expression of Dual-Specificity Phosphatase 9 in Placenta and Its Relationship with Gestational Diabetes Mellitus. (nih.gov)
Family1
  • The Cdc25 family appears to have expanded in relation to the complexity of the cell-cycle and life-cycle of higher animals. (wikipedia.org)
Role2
  • DUSP9, a Dual-Specificity Phosphatase with a Key Role in Cell Biology and Human Diseases. (nih.gov)
  • Here, new crystal structures are presented of the isolated membrane-proximal D1 and distal D2 domains of protein tyrosine phosphatase epsilon (PTPâ ), a protein tyrosine phosphatase that has been shown to play a positive role in the survival of human breast cancer cells. (bvsalud.org)
Domains1
  • non-catalytic domains of eukaryotic dual-specificity MAPK-phosphatases. (embl.de)
Test1
Tyrosine-phosphatase4
  • Citation.Title 'A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. (bmrb.io)
  • Here, new crystal structures are presented of the isolated membrane-proximal D1 and distal D2 domains of protein tyrosine phosphatase epsilon (PTPâ ), a protein tyrosine phosphatase that has been shown to play a positive role in the survival of human breast cancer cells. (bvsalud.org)
  • Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. (nih.gov)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Protein Tyrosine Phosphatase Receptor Type J (PTPRJ) in Tissue homogenates, cell lysates and other biological fluids. (1elisakits.com)
Protein5
  • Dual-specificity phosphatases are considered a sub-class of protein tyrosine phosphatases. (wikipedia.org)
  • A triple mutant of the PTPâ D2 domain (A455N/V457Y/E597D) was also constructed to reconstitute the residues of the PTPâ D1 catalytic domain that are important for phosphatase activity, resulting in only a slight increase in the phosphatase activity compared with the native D2 protein. (bvsalud.org)
  • The protein-tyrosine/dual-specificity phosphatases and rhodanese domains constitute a sprawling superfamily of Rossmannoid domains that use a conserved active site with a cysteine to catalyze a range of phosphate-transfer, thiotransfer, selenotransfer and redox activities. (nih.gov)
  • Dual specificity protein phosphatase (PubMed:9788880). (nih.gov)
  • Dual function of CDC6: a yeast protein required for DNA replication also inhibits nuclear division. (vt.edu)
Cdc25A3
  • The Cdc25 enzymes Cdc25A-C are known to control the transitions from G1 to S phase and G2 to M phase. (wikipedia.org)
  • Arsenite slows S phase progression via inhibition of cdc25A dual specificity phosphatase gene transcription. (nih.gov)
  • Cdc25A dual specificity phosphatase controls entry into and progression through S phase by dephosphorylating sites of inhibitory phosphorylation on cyclin E-cdk2 (Thr14 and Tyr15). (nih.gov)
Mitotic1
  • Pds1p of budding yeast has dual roles: inhibition of anaphase initiation and regulation of mitotic exit. (vt.edu)
Progression1
  • A subclass of dual specificity phosphatases that play a role in the progression of the CELL CYCLE . (nih.gov)
KINASES1
  • Cdc25 activates cyclin dependent kinases by removing phosphate from residues in the Cdk active site. (wikipedia.org)
Activity2
  • Cdk activity can be reactivated after dephosphorylation by Cdc25. (wikipedia.org)
  • Together our outcomes portray Cks being a multifunctional phosphoadaptor that acts as a specificity aspect for Cdk activity. (conferencedequebec.org)
Cell1
  • The Cdc25 family appears to have expanded in relation to the complexity of the cell-cycle and life-cycle of higher animals. (wikipedia.org)
High1
  • BTSA1 is a BAX activator that binds to the N-terminal activation site with high affinity and specificity, induces conformational changes to BAX leading to BAX-mediated apoptosis. (csnpharm.cn)
Large1
  • A large number of potent small-molecule Cdc25 Inhibitors have been identified that bind to the active site and belong to various chemical classes, including natural products, lipophilic acids, quinonoids, electrophiles, sulfonylated aminothiazoles and phosphate bioisosteres. (wikipedia.org)