• M-phase inducer phosphatase 1 also known as dual specificity phosphatase Cdc25A is a protein that in humans is encoded by the cell division cycle 25 homolog A (CDC25A) gene. (wikipedia.org)
  • The catalytic domain of this dual-specificity phosphatase has recently been mapped to the 180 most C-terminal amino acids. (embl.de)
  • They represent a subgroup of the tyrosine phosphatase family (as opposed to the serine/threonine phosphatase family). (wikipedia.org)
  • The cdc25 gene product is a tyrosine phosphatase that acts as an initiator of M-phase in eukaryotic cell cycles by activating p34 cdc2 . (biologists.com)
  • 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)
  • A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain. (embl.de)
  • Cdc25 phosphatase catalytic domain. (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)
  • All mammals examined to date have three homologues of the ancestral Cdc25 gene (found e.g. in the fungus species S. pombe), designated Cdc25A, Cdc25B, and Cdc25C. (wikipedia.org)
  • Three CDC25B phosphatases can be found in higher eukaryotes, CDC25A, CDC25C[13] and CDC25B. (pkc-inhibitor.com)
  • Second, CDC25B activates the mitotic kinase CDK1/cyclin B complicated in the cytoplasm to stimulate cell routine development [16]. (pkc-inhibitor.com)
  • The CP-673451 supplier specificity and sensitivity of CDC25B-Abs for recognition of ESCC were 56.7% and 91.0%, respectively, when CDC25-Abs-positive examples were thought as people that have an A450 higher than the cut-off worth of 0.725. (pkc-inhibitor.com)
  • The surface positioning of subfamily-specific conserved residues allows us to predict the sites of interaction with Cdk2, a physiological target of Cdc25a. (embl.de)
  • CDC25A is considered an oncogene, as it can cooperate with oncogenic RAS to transform rodent fibroblasts, and it is overexpressed in tumours from a variety of tissues, including breast and head & neck tumours. (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)
  • By counteracting the activities of kinases, phosphatases play an important role in the control of a wide variety of cellular functions including cell cycle checkpoints, responsiveness to growth factors, contact inhibition, and cellular motility. (rndsystems.com)
  • This entry represents the PTPase domain found in several tyrosine-specific protein phosphatases (PTPases). (embl.de)
  • A number of successful drugs have been developed that target protein phosphatases. (rndsystems.com)
  • CDC25A is a member of the CDC25 family of dual-specificity phosphatases. (wikipedia.org)
  • Until very recently, the Cdc25 family was the only subfamily of tyrosine phosphates for which no three-dimensional structural data were available. (embl.de)
  • 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)
  • Disturbances in phosphatase activity are implicated in a wide variety of disease states such as colon cancer, obesity, and immunodeficiencies. (rndsystems.com)
  • The inactive domains of tandem phosphatases can be divided into two classes. (embl.de)
  • non-catalytic domains of eukaryotic dual-specificity MAPK-phosphatases. (embl.de)
  • non-catalytic domains of yeast PTP-type MAPK-phosphatases. (embl.de)