Phosphoprotein phosphatases. Medical search

A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)

An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. EC 3.1.3.17.

A phosphoprotein phosphatase subtype that is comprised of a catalytic subunit and two different regulatory subunits. At least two genes encode isoforms of the protein phosphatase catalytic subunit, while several isoforms of regulatory subunits exist due to the presence of multiple genes and the alternative splicing of their mRNAs. Protein phosphatase 2 acts on a broad variety of cellular proteins and may play a role as a regulator of intracellular signaling processes.

A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.

A eukayrotic protein serine-threonine phosphatase subtype that dephosphorylates a wide variety of cellular proteins. The enzyme is comprised of a catalytic subunit and regulatory subunit. Several isoforms of the protein phosphatase catalytic subunit exist due to the presence of multiple genes and the alternative splicing of their mRNAs. A large number of proteins have been shown to act as regulatory subunits for this enzyme. Many of the regulatory subunits have additional cellular functions.

A specific inhibitor of phosphoserine/threonine protein phosphatase 1 and 2a. It is also a potent tumor promoter. (Thromb Res 1992;67(4):345-54 & Cancer Res 1993;53(2):239-41)

The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.

A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.

A compound that, along with its isomer, Cleland's reagent (DITHIOTHREITOL), is used for the protection of sulfhydryl groups against oxidation to disulfides and for the reduction of disulfides to sulfhydryl groups.

Compounds of the general formula R-O-R arranged in a ring or crown formation.

A trace element with atomic symbol Mn, atomic number 25, and atomic weight 54.94. It is concentrated in cell mitochondria, mostly in the pituitary gland, liver, pancreas, kidney, and bone, influences the synthesis of mucopolysaccharides, stimulates hepatic synthesis of cholesterol and fatty acids, and is a cofactor in many enzymes, including arginase and alkaline phosphatase in the liver. (From AMA Drug Evaluations Annual 1992, p2035)

An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.

An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis.

A trihydroxy bile salt that is used as a digestive aid in dietary supplements. It is used in culture media and in conjunction with PAPAIN and PANCREATIN.

The rate dynamics in chemical or physical systems.

The sum of the weight of all the atoms in a molecule.

A class of glucosyltransferases that catalyzes the degradation of storage polysaccharides, such as glucose polymers, by phosphorolysis in animals (GLYCOGEN PHOSPHORYLASE) and in plants (STARCH PHOSPHORYLASE).

A toxic compound, isolated from the Spanish fly or blistering beetle (Lytta (Cantharis) vesicatoria) and other insects. It is a potent and specific inhibitor of protein phosphatases 1 (PP1) and 2A (PP2A). This compound can produce severe skin inflammation, and is extremely toxic if ingested orally.

Proteins which bind calmodulin. They are found in many tissues and have a variety of functions including F-actin cross-linking properties, inhibition of cyclic nucleotide phosphodiesterase and calcium and magnesium ATPases.

Five-membered heterocyclic ring structures containing an oxygen in the 1-position and a nitrogen in the 3-position, in distinction from ISOXAZOLES where they are at the 1,2 positions.

Unstable isotopes of phosphorus that decay or disintegrate emitting radiation. P atoms with atomic weights 28-34 except 31 are radioactive phosphorus isotopes.

A source of inorganic fluoride which is used topically to prevent dental caries.

Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.

A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

A phosphoprotein that was initially identified as a major target of DOPAMINE activated ADENYLYL CYCLASE in the CORPUS STRIATUM. It regulates the activities of PROTEIN PHOSPHATASE-1 and PROTEIN KINASE A, and it is a key mediator of the biochemical, electrophysiological, transcriptional, and behavioral effects of DOPAMINE.

The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.

A CALCIUM and CALMODULIN-dependent serine/threonine protein phosphatase that is composed of the calcineurin A catalytic subunit and the calcineurin B regulatory subunit. Calcineurin has been shown to dephosphorylate a number of phosphoproteins including HISTONES; MYOSIN LIGHT CHAIN; and the regulatory subunits of CAMP-DEPENDENT PROTEIN KINASES. It is involved in the regulation of signal transduction and is the target of an important class of immunophilin-immunosuppressive drug complexes.

An enzyme that catalyzes the conversion of ATP and PHOSPHORYLASE B to ADP and PHOSPHORYLASE A.

Contractile tissue that produces movement in animals.

A phenothiazine with actions similar to CHLORPROMAZINE. It is used as an antipsychotic and an antiemetic.

The chemical and physical integrity of a pharmaceutical product.

An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.

An enzyme that catalyzes the conversion of D-glucose 6-phosphate and water to D-glucose and orthophosphate. EC 3.1.3.9.

Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.

A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.

Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.

Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each.

The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.

Presence of warmth or heat or a temperature notably higher than an accustomed norm.

Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.

A subtype of non-receptor protein tyrosine phosphatases that contain two SRC HOMOLOGY DOMAINS. Mutations in the gene for protein tyrosine phosphatase, non-receptor type 11 are associated with NOONAN SYNDROME.

A sub-class of protein tyrosine phosphatases that contain an additional phosphatase activity which cleaves phosphate ester bonds on SERINE or THREONINE residues that are located on the same protein.

A subclass of dual specificity phosphatases that play a role in the progression of the CELL CYCLE. They dephosphorylate and activate CYCLIN-DEPENDENT KINASES.

A subtype of non-receptor protein tyrosine phosphatases that includes two distinctive targeting motifs; an N-terminal motif specific for the INSULIN RECEPTOR, and a C-terminal motif specific for the SH3 domain containing proteins. This subtype includes a hydrophobic domain which localizes it to the ENDOPLASMIC RETICULUM.

A Src-homology domain-containing protein tyrosine phosphatase found in the CYTOSOL of hematopoietic cells. It plays a role in signal transduction by dephosphorylating signaling proteins that are activated or inactivated by PROTEIN-TYROSINE KINASES.

A phosphoprotein phosphatase that is specific for MYOSIN LIGHT CHAINS. It is composed of three subunits, which include a catalytic subunit, a myosin binding subunit, and a third subunit of unknown function.

The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.

The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.

The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.

A subcategory of protein tyrosine phosphatases that occur in the CYTOPLASM. Many of the proteins in this category play a role in intracellular signal transduction.

Established cell cultures that have the potential to propagate indefinitely.

A subclass of receptor-like protein tryosine phosphatases that contain multiple extracellular immunoglobulin G-like domains and fibronectin type III-like domains. An additional memprin-A5-mu domain is found on some members of this subclass.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

A phosphomonoesterase involved in the synthesis of triacylglycerols. It catalyzes the hydrolysis of phosphatidates with the formation of diacylglycerols and orthophosphate. EC 3.1.3.4.

A dual specificity phosphatase subtype that plays a role in intracellular signal transduction by inactivating MITOGEN-ACTIVATED PROTEIN KINASES. It has specificity for P38 MITOGEN-ACTIVATED PROTEIN KINASES and JNK MITOGEN-ACTIVATED PROTEIN KINASES.

The phosphoric acid ester of serine.

The phosphoric acid ester of threonine. Used as an identifier in the analysis of peptides, proteins, and enzymes.

Inorganic salts of phosphoric acid.

A family of synaptic vesicle-associated proteins involved in the short-term regulation of NEUROTRANSMITTER release. Synapsin I, the predominant member of this family, links SYNAPTIC VESICLES to ACTIN FILAMENTS in the presynaptic nerve terminal. These interactions are modulated by the reversible PHOSPHORYLATION of synapsin I through various signal transduction pathways. The protein is also a substrate for cAMP- and CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASES. It is believed that these functional properties are also shared by synapsin II.

A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.

Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.

A subclass of receptor-like protein tryosine phosphatases that contain a single cytosolic protein tyrosine phosphate domain and multiple extracellular fibronectin III-like domains.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.

The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.

Oxyvanadium ions in various states of oxidation. They act primarily as ion transport inhibitors due to their inhibition of Na(+)-, K(+)-, and Ca(+)-ATPase transport systems. They also have insulin-like action, positive inotropic action on cardiac ventricular muscle, and other metabolic effects.

A subclass of receptor-like protein tryosine phosphatases that contain short highly glycosylated extracellular domains and two active cytosolic protein tyrosine phosphatase domains.

Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.

A subcategory of phosphohydrolases that are specific for MITOGEN-ACTIVATED PROTEIN KINASES. They play a role in the inactivation of the MAP KINASE SIGNALING SYSTEM.

Proteins found in any species of virus.

A ubiquitous phosphoprotein that serves as an intracellular substrate for a variety of SIGNAL TRANSDUCTION PATHWAYS. PHOSPHORYLATION of stathmin occurs during CELL CYCLE progression, and stathmin functions as a microtubule-destabilizing protein that promotes MICROTUBULE depolymerization during INTERPHASE and late MITOSIS. Stathmin is expressed at very high levels in a variety of human CANCERS.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.

A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.

A subcategory of protein tyrosine phosphatases that contain SH2 type SRC HOMOLOGY DOMAINS. Many of the proteins in this class are recruited to specific cellular targets such as a cell surface receptor complexes via their SH2 domain.

An amino acid that occurs in endogenous proteins. Tyrosine phosphorylation and dephosphorylation plays a role in cellular signal transduction and possibly in cell growth control and carcinogenesis.

Proteins prepared by recombinant DNA technology.

Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.

A dual specificity phosphatase subtype that plays a role in intracellular signal transduction by inactivating MITOGEN-ACTIVATED PROTEIN KINASES. It has specificity for EXTRACELLULAR SIGNAL-REGULATED MAP KINASES and is primarily localized to the CYTOSOL.

A subtype of non-receptor protein tyrosine phosphatase that is closely-related to PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 1. Alternative splicing of the mRNA for this phosphatase results in the production at two gene products, one of which includes a C-terminal nuclear localization domain that may be involved in the transport of the protein to the CELL NUCLEUS. Although initially referred to as T-cell protein tyrosine phosphatase the expression of this subtype occurs widely.

Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.

An egg yolk phosphoglycoprotein which contains about 90% of the yolk protein phosphorus. It is synthesized in the liver of the hen and transferred to the developing oocyte, where it is bound to lipoproteins within the yolk granules.

Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.

Electrophoresis in which a second perpendicular electrophoretic transport is performed on the separate components resulting from the first electrophoresis. This technique is usually performed on polyacrylamide gels.

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.

Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.

Cyclic heptapeptides found in MICROCYSTIS and other CYANOBACTERIA. Hepatotoxic and carcinogenic effects have been noted. They are sometimes called cyanotoxins, which should not be confused with chemicals containing a cyano group (CN) which are toxic.

A negatively-charged extracellular matrix protein that plays a role in the regulation of BONE metabolism and a variety of other biological functions. Cell signaling by osteopontin may occur through a cell adhesion sequence that recognizes INTEGRIN ALPHA-V BETA-3.

A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.

RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.

Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.

The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.

Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)

Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis.

Proteins found in the microtubules.

A lipid phosphatase that acts on phosphatidylinositol-3,4,5-trisphosphate to regulate various SIGNAL TRANSDUCTION PATHWAYS. It modulates CELL GROWTH PROCESSES; CELL MIGRATION; and APOPTOSIS. Mutations in PTEN are associated with COWDEN DISEASE and PROTEUS SYNDROME as well as NEOPLASTIC CELL TRANSFORMATION.

An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.

An enzyme that catalyzes the conversion of phosphorylated, inactive glycogen synthase D to active dephosphoglycogen synthase I. EC 3.1.3.42.

Transport proteins that carry specific substances in the blood or across cell membranes.

Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.

Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)

The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.

A group of enzymes that are dependent on CYCLIC AMP and catalyze the phosphorylation of SERINE or THREONINE residues on proteins. Included under this category are two cyclic-AMP-dependent protein kinase subtypes, each of which is defined by its subunit composition.

Glycoproteins which contain sialic acid as one of their carbohydrates. They are often found on or in the cell or tissue membranes and participate in a variety of biological activities.

A subclass of receptor-like protein tryosine phosphatases that contain an extracellular fibronectin III-like domain along with a carbonic anhydrase-like domain.

(Pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyzes the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. EC 3.1.3.43.

A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of a N-terminal catalytic domain and a large C-terminal domain that is enriched in PROLINE, GLUTAMIC ACID, SERINE, and THREONINE residues (PEST sequences). The phosphatase subtype is ubiquitously expressed and implicated in the regulation of a variety of biological processes such as CELL MOVEMENT; CYTOKINESIS; focal adhesion disassembly; and LYMPHOCYTE ACTIVATION.

Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.

CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)

Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.

A ubiquitous casein kinase that is comprised of two distinct catalytic subunits and dimeric regulatory subunit. Casein kinase II has been shown to phosphorylate a large number of substrates, many of which are proteins involved in the regulation of gene expression.

The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.

A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes

An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.

A subcategory of protein tyrosine phosphatases that are bound to the cell membrane. They contain cytoplasmic tyrosine phosphatase domains and extracellular protein domains that may play a role in cell-cell interactions by interacting with EXTRACELLULAR MATRIX components. They are considered receptor-like proteins in that they appear to lack specific ligands.

Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.

The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.

Regions of AMINO ACID SEQUENCE similarity in the SRC-FAMILY TYROSINE KINASES that fold into specific functional tertiary structures. The SH1 domain is a CATALYTIC DOMAIN. SH2 and SH3 domains are protein interaction domains. SH2 usually binds PHOSPHOTYROSINE-containing proteins and SH3 interacts with CYTOSKELETAL PROTEINS.

A type of CELL NUCLEUS division by means of which the two daughter nuclei normally receive identical complements of the number of CHROMOSOMES of the somatic cells of the species.

A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.

A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of an amino-terminal FERM domain, an intervening region containing five different PDZ domains, and a carboxyl-terminal phosphatase domain. In addition to playing a role as a regulator of the FAS RECEPTOR activity this subtype interacts via its PDZ and FERM domains with a variety of INTRACELLULAR SIGNALING PROTEINS and CYTOSKELETAL PROTEINS.

The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

A specialized CONNECTIVE TISSUE that is the main constituent of the SKELETON. The principle cellular component of bone is comprised of OSTEOBLASTS; OSTEOCYTES; and OSTEOCLASTS, while FIBRILLAR COLLAGENS and hydroxyapatite crystals form the BONE MATRIX.

Elements of limited time intervals, contributing to particular results or situations.

A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of an amino-terminal FERM domain, an intervening region containing one or more PDZ domains, and a carboxyl-terminal phosphatase domain. Expression of this phosphatase subtype has been observed in BONE MARROW; fetal LIVER; LYMPH NODES; and T LYMPHOCYTES.

Proteins conjugated with nucleic acids.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.

The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)

Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.

A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.

The type species of LYSSAVIRUS causing rabies in humans and other animals. Transmission is mostly by animal bites through saliva. The virus is neurotropic multiplying in neurons and myotubes of vertebrates.

Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.

Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.

Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.

A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.

An enzyme that catalyzes the hydrolysis of nitrophenyl phosphates to nitrophenols. At acid pH it is probably ACID PHOSPHATASE (EC 3.1.3.2); at alkaline pH it is probably ALKALINE PHOSPHATASE (EC 3.1.3.1). EC 3.1.3.41.

Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.

Inducible NO synthase: role in cellular signalling. (1/5093)

The discovery of endothelium-derived relaxing factor and its identification as nitric oxide (NO) was one of the most exciting discoveries of biomedical research in the 1980s. Besides its potent vasodilatory effects, NO was found under certain circumstances to be responsible for the killing of microorganisms and tumour cells by activated macrophages and to act as a novel, unconventional type of neurotransmitter. In 1992, Science picked NO as the 'Molecule of the Year', and over the past years NO has become established as a universal intercellular messenger that acutely affects important signalling pathways and, on a more long-term scale, modulates gene expression in target cells. These actions will form the focus of the present review. (+info)

Activation of Src in human breast tumor cell lines: elevated levels of phosphotyrosine phosphatase activity that preferentially recognizes the Src carboxy terminal negative regulatory tyrosine 530. (2/5093)

Elevated levels of Src kinase activity have been reported in a number of human cancers, including colon and breast cancer. We have analysed four human breast tumor cell lines that exhibit high levels of Src kinase activity, and have determined that these cell lines also exhibit a high level of a phosphotyrosine phosphatase activity that recognizes the Src carboxy-terminal P-Tyr530 negative regulatory site. Total Src kinase activity in these cell lines is elevated as much as 30-fold over activity in normal control cells and specific activity is elevated as much as 5.6-fold. When the breast tumor cells were grown in the presence of the tyrosine phosphatase inhibitor vanadate, Src kinase activity was reduced in all four breast tumor cell lines, suggesting that Src was being activated by a phosphatase which could recognize the Tyr530 negative regulatory site. In fractionated cell extracts from the breast tumor cells, we found elevated levels of a membrane associated tyrosine phosphatase activity that preferentially dephosphorylated a Src family carboxy-terminal phosphopeptide containing the regulatory tyrosine 530 site. Src was hypophosphorylated in vivo at tyrosine 530 in at least two of the tumor cell lines, further suggesting that Src was being activated by a phosphatase in these cells. In preliminary immunoprecipitation and antibody depletion experiments, we were unable to correlate the major portion of this phosphatase activity with several known phosphatases. (+info)

The MAP kinase ERK2 inhibits the cyclic AMP-specific phosphodiesterase HSPDE4D3 by phosphorylating it at Ser579. (3/5093)

The extracellular receptor stimulated kinase ERK2 (p42(MAPK))-phosphorylated human cAMP-specific phosphodiesterase PDE4D3 at Ser579 and profoundly reduced ( approximately 75%) its activity. These effects could be reversed by the action of protein phosphatase PP1. The inhibitory state of PDE4D3, engendered by ERK2 phosphorylation, was mimicked by the Ser579-->Asp mutant form of PDE4D3. In COS1 cells transfected to express PDE4D3, challenge with epidermal growth factor (EGF) caused the phosphorylation and inhibition of PDE4D3. This effect was blocked by the MEK inhibitor PD98059 and was not apparent using the Ser579-->Ala mutant form of PDE4D3. Challenge of HEK293 and F442A cells with EGF led to the PD98059-ablatable inhibition of endogenous PDE4D3 and PDE4D5 activities. EGF challenge of COS1 cells transfected to express PDE4D3 increased cAMP levels through a process ablated by PD98059. The activity of the Ser579-->Asp mutant form of PDE4D3 was increased by PKA phosphorylation. The transient form of the EGF-induced inhibition of PDE4D3 is thus suggested to be due to feedback regulation by PKA causing the ablation of the ERK2-induced inhibition of PDE4D3. We identify a novel means of cross-talk between the cAMP and ERK signalling pathways whereby cell stimuli that lead to ERK2 activation may modulate cAMP signalling. (+info)

All-trans-retinoic acid inhibits Jun N-terminal kinase by increasing dual-specificity phosphatase activity. (4/5093)

Jun N-terminal kinases (JNKs) are serine-threonine kinases that play a critical role in the regulation of cell growth and differentiation. We previously observed that JNK activity is suppressed by all-trans-retinoic acid (t-RA), a ligand for retinoic acid nuclear receptors (RARs), in normal human bronchial epithelial cells, which are growth inhibited by t-RA. In this study, we investigated the mechanism by which t-RA inhibits JNK and the possibility that this signaling event is blocked in non-small cell lung cancer (NSCLC) cells. Virtually all NSCLC cell lines are resistant to the growth-inhibitory effects of t-RA, and a subset of them have a transcriptional defect specific to retinoid nuclear receptors. We found that in NSCLC cells expressing functional retinoid receptors, serum-induced JNK phosphorylation and activity were inhibited by t-RA in a bimodal pattern, transiently within 30 min and in a sustained fashion beginning at 12 h. Retinoid receptor transcriptional activation was required for the late, but not the early, suppression of JNK activity. t-RA inhibited serum-induced JNK activity by blocking mitogen-activated protein (MAP) kinase kinase 4-induced signaling events. This effect of t-RA was phosphatase dependent and involved an increase in the expression of the dual-specificity MAP kinase phosphatase 1 (MKP-1). t-RA did not activate MKP-1 expression or inhibit JNK activity in a NSCLC cell line with retinoid receptors that are refractory to ligand-induced transcriptional activation. These findings provide the first evidence that t-RA suppresses JNK activity by inhibiting JNK phosphorylation. Retinoid receptor transcriptional activation was necessary for the sustained inhibition of JNK activity by t-RA, and this signaling event was disrupted in NSCLC cells with retinoid receptors that are refractory to ligand-induced transcriptional activation. (+info)

The yeast ser/thr phosphatases sit4 and ppz1 play opposite roles in regulation of the cell cycle. (5/5093)

Yeast cells overexpressing the Ser/Thr protein phosphatase Ppz1 display a slow-growth phenotype. These cells recover slowly from alpha-factor or nutrient depletion-induced G1 arrest, showing a considerable delay in bud emergence as well as in the expression of the G1 cyclins Cln2 and Clb5. Therefore, an excess of the Ppz1 phosphatase interferes with the normal transition from G1 to S phase. The growth defect is rescued by overexpression of the HAL3/SIS2 gene, encoding a negative regulator of Ppz1. High-copy-number expression of HAL3/SIS2 has been reported to improve cell growth and to increase expression of G1 cyclins in sit4 phosphatase mutants. We show here that the described effects of HAL3/SIS2 on sit4 mutants are fully mediated by the Ppz1 phosphatase. The growth defect caused by overexpression of PPZ1 is intensified in strains with low G1 cyclin levels (such as bck2Delta or cln3Delta mutants), whereas mutation of PPZ1 rescues the synthetic lethal phenotype of sit4 cln3 mutants. These results reveal a role for Ppz1 as a regulatory component of the yeast cell cycle, reinforce the notion that Hal3/Sis2 serves as a negative modulator of the biological functions of Ppz1, and indicate that the Sit4 and Ppz1 Ser/Thr phosphatases play opposite roles in control of the G1/S transition. (+info)

Purification and identification of a novel subunit of protein serine/threonine phosphatase 4. (6/5093)

The catalytic subunit of protein serine/threonine phosphatase 4 (PP4C) has greater than 65% amino acid identity to the catalytic subunit of protein phosphatase 2A (PP2AC). Despite this high homology, PP4 does not appear to associate with known PP2A regulatory subunits. As a first step toward characterization of PP4 holoenzymes and identification of putative PP4 regulatory subunits, PP4 was purified from bovine testis soluble extracts. PP4 existed in two complexes of approximately 270-300 and 400-450 kDa as determined by gel filtration chromatography. The smaller PP4 complex was purified by sequential phenyl-Sepharose, Source 15Q, DEAE2, and Superdex 200 gel filtration chromatographies. The final product contained two major proteins: the PP4 catalytic subunit plus a protein that migrated as a doublet of 120-125 kDa on SDS-polyacrylamide gel electrophoresis. The associated protein, termed PP4R1, and PP4C also bound to microcystin-Sepharose. Mass spectrometry analysis of the purified complex revealed two major peaks, at 35 (PP4C) and 105 kDa (PP4R1). Amino acid sequence information of several peptides derived from the 105 kDa protein was utilized to isolate a human cDNA clone. Analysis of the predicted amino acid sequence revealed 13 nonidentical repeats similar to repeats found in the A subunit of PP2A (PP2AA). The PP4R1 cDNA clone engineered with an N-terminal Myc tag was expressed in COS M6 cells and PP4C co-immunoprecipitated with Myc-tagged PP4R1. These data indicate that one form of PP4 is similar to the core complex of PP2A in that it consists of a catalytic subunit and a "PP2AA-like" structural subunit. (+info)

Caffeine can override the S-M checkpoint in fission yeast. (7/5093)

The replication checkpoint (or 'S-M checkpoint') control prevents progression into mitosis when DNA replication is incomplete. Caffeine has been known for some time to have the capacity to override the S-M checkpoint in animal cells. We show here that caffeine also disrupts the S-M checkpoint in the fission yeast Schizosaccharomyces pombe. By contrast, no comparable effects of caffeine on the S. pombe DNA damage checkpoint were seen. S. pombe cells arrested in early S phase and then exposed to caffeine lost viability rapidly as they attempted to enter mitosis, which was accompanied by tyrosine dephosphorylation of Cdc2. Despite this, the caffeine-induced loss of viability was not blocked in a temperature-sensitive cdc2 mutant incubated at the restrictive temperature, although catastrophic mitosis was prevented under these conditions. This suggests that, in addition to S-M checkpoint control, a caffeine-sensitive function may be important for maintenance of cell viability during S phase arrest. The lethality of a combination of caffeine with the DNA replication inhibitor hydroxyurea was suppressed by overexpression of Cds1 or Chk1, protein kinases previously implicated in S-M checkpoint control and recovery from S phase arrest. In addition, the same combination of drugs was specifically tolerated in cells overexpressing either of two novel S. pombe genes isolated in a cDNA library screen. These findings should allow further molecular investigation of the regulation of S phase arrest, and may provide a useful system with which to identify novel drugs that specifically abrogate the checkpoint control. (+info)

Activation of myosin phosphatase targeting subunit by mitosis-specific phosphorylation. (8/5093)

It has been demonstrated previously that during mitosis the sites of myosin phosphorylation are switched between the inhibitory sites, Ser 1/2, and the activation sites, Ser 19/Thr 18 (Yamakita, Y., S. Yamashiro, and F. Matsumura. 1994. J. Cell Biol. 124:129- 137; Satterwhite, L.L., M.J. Lohka, K.L. Wilson, T.Y. Scherson, L.J. Cisek, J.L. Corden, and T.D. Pollard. 1992. J. Cell Biol. 118:595-605), suggesting a regulatory role of myosin phosphorylation in cell division. To explore the function of myosin phosphatase in cell division, the possibility that myosin phosphatase activity may be altered during cell division was examined. We have found that the myosin phosphatase targeting subunit (MYPT) undergoes mitosis-specific phosphorylation and that the phosphorylation is reversed during cytokinesis. MYPT phosphorylated either in vivo or in vitro in the mitosis-specific way showed higher binding to myosin II (two- to threefold) compared to MYPT from cells in interphase. Furthermore, the activity of myosin phosphatase was increased more than twice and it is suggested this reflected the increased affinity of myosin binding. These results indicate the presence of a unique positive regulatory mechanism for myosin phosphatase in cell division. The activation of myosin phosphatase during mitosis would enhance dephosphorylation of the myosin regulatory light chain, thereby leading to the disassembly of stress fibers during prophase. The mitosis-specific effect of phosphorylation is lost on exit from mitosis, and the resultant increase in myosin phosphorylation may act as a signal to activate cytokinesis. (+info)

Phosphoprotein levels are counterbalanced by phosphatases. Ultimately, transcriptional activation of certain target genes ...

https://en.wikipedia.org/wiki/Restriction_point

ISBN 978-1-4292-2936-4. Gong CX, Singh TJ, Grundke-Iqbal I, Iqbal K (September 1993). "Phosphoprotein phosphatase activities in ... Protein phosphatase 1 (PP1) belongs to a certain class of phosphatases known as protein serine/threonine phosphatases. This ... Regulation of HIV-1 transcription by Protein Phosphatase 1 (PP1). It has been recognized that protein phosphatase-1 (PP1) ... type of phosphatase includes metal-dependent protein phosphatases (PPMs) and aspartate-based phosphatases. PP1 has been found ...

https://en.wikipedia.org/wiki/Protein_phosphatase_1

Eto M, Karginov A, Brautigan DL (Jan 2000). "A novel phosphoprotein inhibitor of protein type-1 phosphatase holoenzymes". ... Protein phosphatase 1 regulatory subunit 14B is an enzyme that in humans is encoded by the PPP1R14B gene. GRCh38: Ensembl ... "Entrez Gene: PPP1R14B protein phosphatase 1, regulatory (inhibitor) subunit 14B". Dias Neto E, Correa RG, Verjovski-Almeida S, ... Tountas NA, Mandell JW, Everett AD, Brautigan DL (2005). "Juxtamembrane localization of the protein phosphatase-1 inhibitor ...

https://en.wikipedia.org/wiki/PPP1R14B

Sundarajan TA; Sarma PS (1959). "Substrate specificity of phosphoprotein phosphatase from spleen". Biochem. J. 71 (3): 537-544 ... This enzyme is also called creatine phosphatase. Parvin R, Smith RA (1969). "Phosphoramidates. V. Probable identity of rat ... liver microsomal glucose 6-phosphatase, phosphoramidase, and phosphoramidate-hexose phosphotransferase". Biochemistry. 8 (4): ...

https://en.wikipedia.org/wiki/Phosphoamidase

"PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. ... evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Molecular & Cellular Proteomics. 4 (11 ...

https://en.wikipedia.org/wiki/CCT3

"PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. ... Serine/threonine-protein phosphatase 4 regulatory subunit 3B is an enzyme that in humans is encoded by the SMEK2 gene. SMEK2 ... "A PP4-phosphatase complex dephosphorylates gamma-H2AX generated during DNA replication". Molecular Cell. 31 (1): 33-46. doi: ... evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity" (PDF). Molecular & Cellular Proteomics ...

https://en.wikipedia.org/wiki/SMEK2

https://en.wikipedia.org/wiki/CCT4

https://en.wikipedia.org/wiki/CCT5_(gene)

"PP4R4/KIAA1622 Forms a Novel Stable Cytosolic Complex with Phosphoprotein Phosphatase 4". J. Biol. Chem. 283 (43): 29273-84. ... evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Mol. Cell. Proteomics. 4 (11): 1725-40 ...

https://en.wikipedia.org/wiki/CCT6A

https://en.wikipedia.org/wiki/CCT2_(gene)

"PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. ... Serine/threonine-protein phosphatase 4 catalytic subunit is an enzyme that in humans is encoded by the PPP4C gene. PPP4C has ... Chen L, Dong W, Zou T, Ouyang L, He G, Liu Y, Qi Y (Aug 2008). "Protein phosphatase 4 negatively regulates LPS cascade by ... Hu MC, Tang-Oxley Q, Qiu WR, Wang YP, Mihindukulasuriya KA, Afshar R, Tan TH (Dec 1998). "Protein phosphatase X interacts with ...

https://en.wikipedia.org/wiki/PPP4C

1996). "Identification of the sites of interaction between lymphocyte phosphatase-associated phosphoprotein (LPAP) and CD45". J ... Protein tyrosine phosphatase receptor type C-associated protein is an enzyme that in humans is encoded by the PTPRCAP gene. The ... Vogel A, Strassburg CP, Manns MP (2003). "77 C/G mutation in the tyrosine phosphatase CD45 gene and autoimmune hepatitis: ... 1994). "LPAP, a novel 32-kDa phosphoprotein that interacts with CD45 in human lymphocytes". J. Biol. Chem. 269 (46): 29102-11. ...

https://en.wikipedia.org/wiki/PTPRCAP

Pandey AV, Mellon SH, Miller WL (2003). "Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17 ... 2007). "Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts". J. Biochem. 140 (5): 677-686. doi:10.1093/ ... 2003). "Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling". J. Biol. Chem. 278 (5): 2787-2791. doi ... Lipid phosphate phosphohydrolase 1 also known as phosphatidic acid phosphatase 2a is an enzyme that in humans is encoded by the ...

https://en.wikipedia.org/wiki/PPAP2A

This process is valuable in the extraction of proteins and specifically phosphoprotein and phosphopeptide phosphatases. Another ...

https://en.wikipedia.org/wiki/Liquid–liquid_extraction

"The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases". The Journal of ... Like kinases, phosphatases too play a role in regulating the phosphorylation of tau. For example, PP2A and PP2B are both ... Tau is a phosphoprotein with 79 potential Serine (Ser) and Threonine (Thr) phosphorylation sites on the longest tau isoform. ... Fujio K, Sato M, Uemura T, Sato T, Sato-Harada R, Harada A (July 2007). "14-3-3 proteins and protein phosphatases are not ...

https://en.wikipedia.org/wiki/Tau_protein

1991). "A functional complex is formed in human T lymphocytes between the protein tyrosine phosphatase CD45, the protein ... Acidic leucine-rich nuclear phosphoprotein 32 family member A is a protein that in humans is encoded by the ANP32A gene. It is ... Acidic leucine-rich nuclear phosphoprotein 32 family member A has been shown to interact with MAP1B, TAF1A and Protein SET. ... "Entrez Gene: ANP32A Acidic (leucine-rich) nuclear phosphoprotein 32 family, member A". Opal, Puneet; Garcia Jesus J; Propst ...

https://en.wikipedia.org/wiki/Acidic_leucine-rich_nuclear_phosphoprotein_32_family_member_A

https://en.wikipedia.org/wiki/CCT7

... ion exchange chromatography was used to identify phosphoprotein phosphatase I and II. Since the discovery of these ... Tau dephosphorylation is catalysed by protein phosphatase-2A and phosphatase-2B. Deficiency or modification of one or both ... By using a desphosphorylating phosphatase, re-ligation can be avoided. Alkaline phosphatases, which remove the phosphate group ... and substrate specificities of phosphoprotein phosphatase(s) from rabbit liver". The Journal of Biological Chemistry. 251 (16 ...

https://en.wikipedia.org/wiki/Dephosphorylation

https://en.wikipedia.org/wiki/T-complex_1

"PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. ... "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the ...

https://en.wikipedia.org/wiki/CCDC6

"PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. ... "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex ... Chung H, Nairn AC, Murata K, Brautigan DL (Aug 1999). "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic ... Chung H, Nairn AC, Murata K, Brautigan DL (Aug 1999). "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic ...

https://en.wikipedia.org/wiki/IGBP1

"PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. ... Serine/threonine-protein phosphatase 4 regulatory subunit 1 is an enzyme that in humans is encoded by the PPP4R1 gene. PPP4R1 ... "Entrez Gene: PPP4R1 protein phosphatase 4, regulatory subunit 1". Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom- ... "Cloning and characterization of a novel subunit of protein serine/threonine phosphatase 4 from mesangial cells". Journal of the ...

https://en.wikipedia.org/wiki/PPP4R1

"The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells ... "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells ... Wisniewski D, Strife A, Wojciechowicz D, Lambek C, Clarkson B (1994). "A 62-kilodalton tyrosine phosphoprotein constitutively ...

https://en.wikipedia.org/wiki/DOK1

June 2000). "Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase". FEBS ... July 2001). "Identification of human CPI-17, an inhibitory phosphoprotein for myosin phosphatase". Biochemical and Biophysical ... Protein phosphatase 1 regulatory subunit 14A also known as CPI-17 (C-kinase potentiated Protein phosphatase-1 Inhibitor Mr = 17 ... There are three homologues of CPI-17: Phosphatase Holoenzyme Inhibitor (PHI: PPP1R14B), Kinase Enhanced Phosphatase Inhibitor ( ...

https://en.wikipedia.org/wiki/PPP1R14A

This latter enzyme is itself activated by protein kinase A and deactivated by phosphoprotein phosphatase-1. Protein kinase A ...

https://en.wikipedia.org/wiki/Glycogenesis

2000). "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl ... "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells ...

https://en.wikipedia.org/wiki/DOK2

Protein phosphatase 1 regulatory subunit 1B (PPP1R1B), also known as dopamine- and cAMP-regulated neuronal phosphoprotein ( ... "Entrez Gene: PPP1R1B protein phosphatase 1, regulatory (inhibitor) subunit 1B (dopamine and cAMP regulated phosphoprotein, ... monophosphate-regulated neuronal phosphoprotein. II. Comparison of the kinetics of phosphorylation of DARPP-32 and phosphatase ... This gene is also known as DARPP-32, highlighting its role as a dopamine- and cyclic AMP-regulated phosphoprotein. As such ...

https://en.wikipedia.org/wiki/PPP1R1B

In eukaryotic cells, phosphatases catalyze the removal of phosphate groups from tyrosine, serine and threonine phosphoproteins ... Tolstykh, T (2000). "Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory ... The catalytic subunit of the major serine/threonine phosphatases, like Protein phosphatase 2 is covalently modified by the ... C-terminal protein methylation regulates the assembly of protein phosphatase. Methylation of the protein phosphatase 2A ...

https://en.wikipedia.org/wiki/Protein_methylation

As a phosphoprotein phosphatase, insulin dephosphorylates the enzyme, thus activating the PFK-2 and inhibiting the FBPase-2 ...

https://en.wikipedia.org/wiki/Fructose_2,6-bisphosphate

"The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells ... Src homology 2 (SH2) domain containing inositol polyphosphate 5-phosphatase 1 (SHIP1) is an enzyme with phosphatase activity. ... "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells ... "Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-phosphatase SHIP with gp49B1, and chromosomal assignment of ...

https://en.wikipedia.org/wiki/INPP5D

Holsinger LJ, Ward K, Duffield B, Zachwieja J, Jallal B (2002). "The transmembrane receptor protein tyrosine phosphatase DEP1 ... "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130-5. Bibcode: ... "The receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinase ...

https://en.wikipedia.org/wiki/NOL1

The encoded protein is a tyrosine phosphatase and belongs to the Cdc25 phosphatase family. It directs dephosphorylation of ... "The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins". Genes Dev. UNITED ... M-phase inducer phosphatase 3 is an enzyme that in humans is encoded by the CDC25C gene. This gene is highly conserved during ... Nilsson I, Hoffmann I (2000). "Cell cycle regulation by the Cdc25 phosphatase family". Progress in Cell Cycle Research. 4: 107- ...

https://en.wikipedia.org/wiki/CDC25C

... protein-tyrosine-phosphatase - proteinoid - proteomics - protirelin - proto-oncogene - proto-oncogene proteins - proto-oncogene ... phosphoprotein - phosphorus - phosphorylation - phosphoserine - phosphothreonine - phosphotyrosine - photobiology - photolysis ...

https://en.wikipedia.org/wiki/Index_of_biochemistry_articles

... encoding enzyme M-phase phosphoprotein 6 MT1G: encoding protein Metallothionein-1G MT1X: encoding protein Metallothionein 1X ... encoding protein Pyruvate dehydrogenase phosphatase regulatory subunit PKDTS: Polycystic kidney disease, infantile severe, with ...

https://en.wikipedia.org/wiki/Chromosome_16

Ishino M, Ohba T, Sasaki H, Sasaki T (1995). "Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains a Src ... Liu F, Hill DE, Chernoff J (1996). "Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src ... Bradbury P, Mahmassani M, Zhong J, Turner K, Paul A, Verrills NM, O'Neill GM (2012). "PP2A phosphatase suppresses function of ... a novel mechanism of protein tyrosine phosphatase substrate recognition". Oncogene. 15 (8): 877-85. doi:10.1038/sj.onc.1201279 ...

https://en.wikipedia.org/wiki/NEDD9

"A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex ... "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130-5. Bibcode: ... "A mammalian homolog of yeast MOB1 is both a member and a putative substrate of striatin family-protein phosphatase 2A complexes ... nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A". J ...

https://en.wikipedia.org/wiki/STRN3

It has been shown that osteopontin and bone sialoprotein, bone matrix phosphoproteins, are highly efficient in vitro TRAP ... Tartrate-resistant acid phosphatase (TRAP or TRAPase), also called acid phosphatase 5, tartrate resistant (ACP5), is a ... Minkin C (May 1982). "Bone acid phosphatase: tartrate-resistant acid phosphatase as a marker of osteoclast function". Calcified ... tartrate-resistant+acid+phosphatase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (CS1 ...

https://en.wikipedia.org/wiki/Tartrate-resistant_acid_phosphatase

Protein phosphatase 2A (PP2A) is a trimeric serine-threonine phosphatase consisting of a catalytic C-subunit (PP2Ac), a ... a vast majority of all cellular serine/threonine phosphorylated proteins including large number of phosphoproteins involved in ...

https://en.wikipedia.org/wiki/KIAA1524

CEP55 is a mitotic phosphoprotein that plays a key role in cytokinesis, the final stage of cell division. Diploid Telophase - ... by phosphorylation of the myosin light chain and also inhibits myosin phosphatase by phosphorylation of the phosphatase- ... 5-bisphosphate 5-phosphatase OCRL. Understanding the mechanism by which the plasma membrane ultimately splits requires further ...

https://en.wikipedia.org/wiki/Cytokinesis

Ollendorff V, Donoghue DJ (Dec 1997). "The serine/threonine phosphatase PP5 interacts with CDC16 and CDC27, two ... "The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins". Genes & Development ... Ollendorff V, Donoghue DJ (Dec 1997). "The serine/threonine phosphatase PP5 interacts with CDC16 and CDC27, two ... "The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins". Genes & Development ...

https://en.wikipedia.org/wiki/CDC27

"Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130". J. Biol. ... "Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn ... "Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane ...

https://en.wikipedia.org/wiki/FYN

1999). "Structure and splice products of the human gene encoding sds22, a putative mitotic regulator of protein phosphatase-1 ... 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130-5. ...

https://en.wikipedia.org/wiki/PASK

Rudrabhatla, P.; Albers, W.; Pant, H. C. (2009-11-25). "Peptidyl-Prolyl Isomerase 1 Regulates Protein Phosphatase 2A-Mediated ... "A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and ... "The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins". Genes & Development ... "The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins". Genes & Development ...

https://en.wikipedia.org/wiki/PIN1

Lester LB, Scott JD (1997). "Anchoring and scaffold proteins for kinases and phosphatases". Recent Prog. Horm. Res. 52: 409-29 ... 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130-5. ...

https://en.wikipedia.org/wiki/AKAP8

"A novel nuclear phosphoprotein, GANP, is up-regulated in centrocytes of the germinal center and associated with MCM3, a protein ... "MCM3-binding GANP DNA-primase is associated with a novel phosphatase component G5PR". Genes Cells. 7 (8): 821-34. doi:10.1046/j ... "A novel nuclear phosphoprotein, GANP, is up-regulated in centrocytes of the germinal center and associated with MCM3, a protein ...

https://en.wikipedia.org/wiki/MCM3AP

Steen RL, Martins SB, Taskén K, Collas P (2000). "Recruitment of Protein Phosphatase 1 to the Nuclear Envelope by a-Kinase ... 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130-5. ... Lester LB, Scott JD (1997). "Anchoring and scaffold proteins for kinases and phosphatases". Recent Prog. Horm. Res. 52: 409-29 ... 2004). "Mitochondrial AKAP121 Binds and Targets Protein Tyrosine Phosphatase D1, a Novel Positive Regulator of src Signaling". ...

https://en.wikipedia.org/wiki/AKAP1

The requirement for phosphatase activation can be seen in budding yeast, which do not have redundant phosphatases for mitotic ... A shift in the whole-cell phosphoprotein profile is only the broadest of many regulatory mechanisms contributing to the onset ... exit and rely on the phosphatase cdc14. Blocking cdc14 activation in these cells results in the same phenotypic arrest as does ... of dephosphorylation permissive to telophase events requires both the inactivation of Cdks and the activation of phosphatases. ...

https://en.wikipedia.org/wiki/Telophase

Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell ... regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm". The ... "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex ... Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform is an enzyme that in humans is encoded by the ...

https://en.wikipedia.org/wiki/PPP2R5A

... there was a need for convenient substrates for protein kinases and protein phosphatases. Casein has been used as a substrate ... it was known from metabolic labeling studies using radioactive phosphate that phosphate groups attached to phosphoproteins ... and most attention was centered on kinases and phosphatases that could regulate the activity of important enzymes. Casein ...

https://en.wikipedia.org/wiki/Casein_kinase_1

"The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding ... "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130-12135. ... "The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding ...

https://en.wikipedia.org/wiki/PKN2

... between a methylene group of microcystin-LR and a cystine residue at the catalytic subunit of the phosphoprotein phosphatase ( ... In vitro studies showed that microcystin-LR is a potent inhibitor of protein phosphatase 1 (PP-1) and PP2A, but has no effect ... Microcystin-LR inhibits protein phosphatase type 1 and type 2A (PP1 and PP2A) activities in the cytoplasm of liver cells. This ... In this way the protein phosphatase is inhibited and more phosphorylated proteins in the liver cells are left, which is ...

https://en.wikipedia.org/wiki/Microcystin-LR

PEST-domain enriched tyrosine phosphatase (PEP), and protein tyrosine phosphatase-PEST. In contrast, Csk has an opposite role ... "Evidence that the transforming gene of avian sarcoma virus encodes a protein kinase associated with a phosphoprotein". Cell. 15 ... Lymphoid protein tyrosine phosphatase (lyp), is one of the suppressor of lck activity and mutations in this protein are ... These differences are due to differential regulation by SH2 domain-containing phosphatase-1 (Shp-1) and C-terminal Src kinase. ...

https://en.wikipedia.org/wiki/Lck

Inositol polyphosphate 1-phosphatase INPP4A: inositol polyphosphate-4-phosphatase type A ITM2C: Integral membrane protein 2C ... M-phase phosphoprotein 10 MSH2: mutS homolog 2, colon cancer, nonpolyposis type 1 (E. coli) MSH6: mutS homolog 6 (E. coli) ...

https://en.wikipedia.org/wiki/Chromosome_2

Yang, Fenghua; Aiello, David L.; Pyle, W. Glen (2008-02-01). "Cardiac myofilament regulation by protein phosphatase type 1alpha ... These factors include ENA/VASP (enabled/vasodilator-stimulated phosphoprotein). CapZ is not regulated by calcium or calmodulin ...

https://en.wikipedia.org/wiki/CapZ

enables myosin phosphatase activity IEA Inferred from Electronic Annotation. more info. enables phosphoprotein phosphatase ... Inhibition of PHLPP1/2 phosphatases rescues pancreatic beta-cells in diabetes. Title: Inhibition of PHLPP1/2 phosphatases ... PH domain and leucine rich repeat protein phosphatase 2provided by MGI. Primary source. MGI:MGI:2444928 See related. Ensembl: ... PH domain leucine-rich repeat-containing protein phosphatase 2. Names. GTPase activating protein and VPS9 domains 1. NP_ ...

https://www.ncbi.nlm.nih.gov/gene/?term=244650

Symbols: PAPP5, PP5 , PAPP5/PP5 (PROTEIN PHOSPHATASE 5); phosphoprotein phosphatase/ protein b…. ... Serine/threonine-protein phosphatase 5 OS=Solanum lycopersicum GN=PP5 PE=1 SV=1. ...

https://www.sgn.cornell.edu/search/unigene.pl?unigene_id=583112

A Quantitative Chemical Proteomic Strategy for Profiling Phosphoprotein Phosphatases from Yeast to Humans.. * Armina Kettenbach ... Identification of the substrate recruitment mechanism of the muscle glycogen protein phosphatase 1 holoenzyme. » ...

https://kettenbachlab.org/publications/a-quantitative-chemical-proteomic-strategy-for-profiling-phosphoprotein-phosphatases-from-yeast-to-humans/

Phosphoprotein Phosphatase. Phosphoprotein Phosphatases. Protein-Tyrosine-Phosphatase. Protein Tyrosine Phosphatases. Rhodopsin ... SHP1 Protein Tyrosine Phosphatase. Protein Tyrosine Phosphatase, Non-Receptor Type 6. Thioredoxin Reductase (NADPH). ...

https://decs.bvs.br/I/rep_i2008.htm

Activity based profiling of Phosphoprotein phosphatases in cancer using mass spectrometry-based proteomics. ... Activity based profiling of Phosphoprotein phosphatases in cancer using mass spectrometry-based proteomics ... The majority of protein dephosphorylation is carried out by phosphoprotein phosphatases (PPPs). The PPPfamily consists of nine ... and alterations in phosphatase signaling networks that antagonize substrate phosphorylation ordirectly modulate kinase activity ...

https://imat.cancer.gov/about-imat/grants-awarded/2019/activity-based-profiling-phosphoprotein-phosphatases-cancer-using

phosphoprotein phosphatase CDC14 Feature Type. ORF , Verified EC Number. 3.1.3.48 Experimental Data Contains experimentally- ...

https://www.yeastgenome.org/locus/S000001924/protein

enables phosphoprotein phosphatase activity IDA Inferred from Direct Assay. more info. PubMed ... B56; Protein phosphatase 2A regulatory B subunit (B56 family). * NM_006243.4 → NP_006234.1 serine/threonine-protein phosphatase ... Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell ... serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform. Names. PR61alpha. protein phosphatase 2 ...

https://www.ncbi.nlm.nih.gov/gene/5525

phosphoprotein phosphatase activity Annotations: * A0A1L8HFW5 (TrEMBL, spp.: X.laevis.L). * Q6GQ14 (TrEMBL, spp.: X.laevis.L) ...

https://www.xenbase.org/entry/gene/showGoTerm.do?method=display&geneId=1011379&geneSymbol=

Protein phosphatases and associated proteins [BR:hsa01009]. Protein serine/threonine phosphatases. Phosphoprotein phosphatases ... 01009 Protein phosphatases and associated proteins [BR:hsa01009]. 56288 (PARD3). ...

https://www.kegg.jp/entry/hsa:56288

The signaling complex may also include anchoring of a phosphoprotein phosphatase (Westphal et al., 1999). Second, translocation ... Fourth, in addition to substrate and Ca2+, the localization of kinase relative to phosphatases (Strack et al., 1997b) and ... Textbook descriptions of protein kinases and phosphatases encourage a simplistic view with on-off-like shifts in ... A special feature of this form of autonomous activity is that it cannot be reversed by phosphatase activity. Interaction with ...

https://www.jneurosci.org/content/24/39/8399

... phosphoprotein NCP94; protein phosphatase 1, regulatory subunit 74; proto-oncogene c-Fer; tyrosine kinase 3; tyrosine-protein ...

https://www.discoverx.com/target-data-sheets/kinase/fer

Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with ... is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of ...

http://smart.embl.de/smart/do_annotation.pl?DOMAIN=RIIa&BLAST=DUMMY

c, Untreated and treated wild-type TPC1 with lambda phosphatase for 1 h at 25 °C. d, Schematic of TPC1 truncations (NΔ1; 2-11, ... b-e, Polyacrylamide gels of purified TPC1 (10 μg) stained with phosphoprotein-specific probe ProDiamond-Q, SyproRuby or ... The first two lanes are PrecisionPlus protein molecular weight standards and PeppermintStick phosphoprotein molecular weight ...

https://www.nature.com/articles/nature17194?error=cookies_not_supported&code=60835ecf-0b01-48d2-b2c2-f4ffa1ce486b

Phosphoprotein Phosphatases Medicine & Life Sciences 93% * Phosphoric Monoester Hydrolases Medicine & Life Sciences 81% ... Visualization of phosphatase activity in living cells with a FRET-based calcineurin activity sensor. In: Molecular BioSystems. ... Visualization of phosphatase activity in living cells with a FRET-based calcineurin activity sensor. / Newman, Robert H.; Zhang ... Newman RH, Zhang J. Visualization of phosphatase activity in living cells with a FRET-based calcineurin activity sensor. ...

https://jhu.pure.elsevier.com/en/publications/visualization-of-phosphatase-activity-in-living-cells-with-a-fret-4

Dual-specificity MAP kinase phosphatases in health and disease. Ole-Morten Seternes, Andrew M. Kidger, Stephen Keyse (Lead / ...

https://discovery.dundee.ac.uk/en/publications/dual-specificity-map-kinase-phosphatases-in-health-and-disease/projects/?status=FINISHED

Phosphoproteins * Ppargc1a protein, mouse * Trans-Activators * Transcription Factors * Glucose-6-Phosphatase * ...

https://pubmed.ncbi.nlm.nih.gov/16271533/

Phosphoprotein Phosphatases Medicine & Life Sciences 38% * Oncogene Proteins Medicine & Life Sciences 36% ... PCDH7 potentiated ERK signaling by facilitating interaction of protein phosphatase PP2A with its potent inhibitor, the SET ... PCDH7 potentiated ERK signaling by facilitating interaction of protein phosphatase PP2A with its potent inhibitor, the SET ... PCDH7 potentiated ERK signaling by facilitating interaction of protein phosphatase PP2A with its potent inhibitor, the SET ...

https://mayoclinic.pure.elsevier.com/en/publications/protocadherin-7-acts-through-set-and-pp2a-to-potentiate-mapk-sign

Phosphatase Inhibitor Cocktail. Ready-to-use broad-spectrum cocktail of inhibitors to preserve phosphoproteins in your samples. ...

https://www.activemotif.com/catalog/62/nuclear-cytoplasmic-extraction

... as well as the phosphorylating or dephosphorylating activity of a kinase or phosphatase. ... to determine the amount of substrate that is phosphorylated or dephosphorylated during the course of a kinase or phosphatase ... The invention relates to novel fluorescence-based assays for protein kinases and phosphatases which can be used in high ... Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle ...

https://patentscope.wipo.int/search/en/detail.jsf?docId=WO1999029894

Phosphoprotein Phosphatases 18% * Adenosine Triphosphate 18% * DNA 18% * Castration 17% * Antifungal Agents 17% ...

https://kyushu-u.pure.elsevier.com/en/persons/shigeru-muta/fingerprints/

It is an exon 4 splice variant of the tyrosine phosphatase CD45. The CD45RA isoform is expressed on resting/naïve T cells, ... CD45 non-covalently associates with lymphocyte phosphatase-associated phosphoprotein (LPAP) on T and B lymphocytes. CD45 has ... It is an exon 4 splice variant of the tyrosine phosphatase CD45. The CD45RA isoform is expressed on resting/naïve T cells, ...

https://www.biolegend.com/en-us/products/pe-dazzle-594-anti-human-cd45ra-22103

"The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases". The Journal of ... Like the kinases, the phosphatases also play a role in the regulation of tau phosphorylation. ... the degree of which in all six isoforms decreases with age due to activation of phosphatases. ...

https://www.labclinics.com/2022/07/25/tau-proteins-and-their-importance-in-mental-illness/?lang=en

Phospho-Proteins (464) Postsynaptic proteins (213) Presynaptic proteins (161) Prion (CD230) (24) Proteases (174) Protein ... Kinases/Phosphatase (447) Protein Modifiers (18) Purinergic Receptors (25) Scaffold Proteins (39) Secretases (11) Semaphorin ...

https://www.biolegend.com/de-de/search-results?GroupID=&PageNum=3&k1=mouse%20F4/80

... a phosphoprotein that inhibits PP2A (66). Active PP2A activates protein tyrosine phosphatase 1, which catalyzes BCR-ABL1 ... Protein phosphatase 2A. Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase that acts as a tumor suppressor by ...

https://aacrjournals.org/clincancerres/article/14/14/4392/72722/Therapeutic-Options-Against-BCR-ABL1-T315I

DOKLADY AN SSSR, BIOCHEMISTRY// 00/12/1981,VO261,NO004, PP 1006-1009 PHOSPHOPROTEIN PHOSPHATASE OF KIDNEY TISSUE AND REGULATION ...

https://www.cia.gov/readingroom/document/cia-rdp91-00403r000201060004-4

Of the 28 phosphoprotein targets measured using multiplex ELISA, the GWI model (CORT+DFP) had numerous targets with increased ... as well as endogenous proteases and phosphatases. From these datasets, the alterations of ACh in the brain do not appear to ... AChE-independent phosphoprotein signaling in an acute mouse model of Gulf War Illness. ... Therefore, interrogation of potential organophosphorylation targets and aberrant phosphoprotein responses of critical signaling ...

http://www2a.cdc.gov/nioshtic-2/BuildQyr.asp?s1=asthma+OR+%27allerg%2A%27+OR+%27immune%2A%27&f1=%2A&Startyear=&Adv=0&terms=1&EndYear=&Limit=10000&sort=&D1=10&PageNo=61&RecNo=603&View=f&

putative phosphoprotein phosphatase. 80. SEQF2168,AP012280.1. BAK86972.1 jb [NA] [AA] 681/226. 95456-94776. hypothetical ... putative acid phosphatase. 199. SEQF2168,AP012280.1. BAK87091.1 jb [NA] [AA] 918/305. 224005-223088. putative transcriptional ... D%2CD-heptose 1%2C7-bisphosphate phosphatase. 7. SEQF2168,AP012280.1. BAK86899.1 jb [NA] [AA] 1707/568. 8728-10434. ...

https://homd.org/genome/explorer?gid=SEQF2168&anno=ncbi

Complex protein phosphorylation networks emerge through the interplay of protein kinases, protein phosphatases, phosphorylation ... site-dependent binding proteins, and their phosphoprotein substrates. I modelled the interactions of protein kinases with ... as well as the effects of inhibition of protein-tyrosine phosphatases and protein synthesis. Taken together, along with over ...

https://www.grad.ubc.ca/researcher/15206-pelech

When phosphorylated at threonine 34 by protein kinase A (PKA), it is a potent inhibitor of protein phosphatase 1 (PP1). ... Dopamine and cAMP-regulated Phosphoprotein, Mr 32 kDa (DARPP-32), also known as PPP1R1B, is found almost exclusively in ...

https://www.rndsystems.com/target/darpp-32?species=Mouse&clonality=Polyclonal&brand=rnd&rnd_applications=Immunohistochemistry

Predicted to enable protein serine/threonine phosphatase activity. (nih.gov)
A group of enzymes removing the SERINE - or THREONINE -bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (bvsalud.org)
The cocktail is provided as a ready-to-use broad-spectrum solution of inhibitors targeting both serine/threonine phosphatases and protein tyrosine phosphatases (PTPs). (activemotif.jp)
The Phosphatase Inhibitor Cocktail is a broad-spectrum solution of phosphatase inhibitors specific for serine/threonine as well as protein tyrosine phosphatases (PTPs). (activemotif.jp)
Violin plots show distribution of expression levels for Serine/threonine-protein phosphatase with EF-hands (SMED30019620) in cells (dots) of each of the 12 neoblast clusters. (stowers.org)
A sub-class of protein tyrosine phosphatases that contain an additional phosphatase activity which cleaves phosphate ester bonds on SERINE or THREONINE residues that are located on the same protein. (jefferson.edu)

For instance, mutationor amplification of the targeted kinase, functional compensation by related kinases, reprograming of kinasesignaling, and alterations in phosphatase signaling networks that antagonize substrate phosphorylation ordirectly modulate kinase activity are common.Tremendous progress has been made in deciphering the cancer kinome and its response to anti-cancertreatment. (cancer.gov)
These studies were enabled by an array of innovative technologies, including a chemical proteomicsstrategy that utilizes kinase inhibitors immobilized on beads and mass spectrometry (MS).The majority of protein dephosphorylation is carried out by phosphoprotein phosphatases (PPPs). (cancer.gov)
When phosphorylated at threonine 34 by protein kinase A (PKA), it is a potent inhibitor of protein phosphatase 1 (PP1). (rndsystems.com)
Of note is that the profile of the reported phosphoproteome reflects the global status of proteins resulting from a balance between endogenous kinase and phosphatase activities. (biomedcentral.com)
We also provide co-expression network analysis to determine the functional context of kinase/phosphatase genes. (kinasebiotech.com)
Active Motif's Phosphatase Inhibitor Cocktail is designed to protect phosphoproteins from dephosphorylation during lysis and extraction procedures from mammalian cells or tissues and for immunoprecipitation and kinase assays. (activemotif.jp)
Metabolic stabilization of MAP kinase phosphatase-2 in senescence of human fibroblasts. (jefferson.edu)

Dual-Specificity Phosphatases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (jefferson.edu)
This graph shows the total number of publications written about "Dual-Specificity Phosphatases" by people in this website by year, and whether "Dual-Specificity Phosphatases" was a major or minor topic of these publications. (jefferson.edu)
Below are the most recent publications written about "Dual-Specificity Phosphatases" by people in Profiles. (jefferson.edu)

The product of this gene belongs to the phosphatase 2A regulatory subunit B family. (nih.gov)
PPP2R5A: A multirole protein phosphatase subunit in regulating cancer development. (nih.gov)
In the past decade, a vast body of research has provided converging evidence that the key mechanism of the mode of action of the PP1c subunit resides in the presence of interacting regulators that direct the proper functions of this phosphatase (i.e. localization, specificity and the level of activity) [ 21 - 23 ]. (biomedcentral.com)
A comparison of polymorphisms in the imp3 strain and the other 15 strains allowed us to identify a deletion of the last three amino acids, Y 313 F 314 L 315 , in a protein phosphatase 2A catalytic subunit (PP2A3) in the imp3 strain. (wustl.edu)
Here we show that human protein phosphatase 4 (PP4) dephosphorylates replication protein A (RPA) subunit RPA2, regulating its role in the DSB response. (uthscsa.edu)

Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. (embl.de)
One of the post-translational modifications is phosphorylation , the degree of which in all six isoforms decreases with age due to activation of phosphatases. (labclinics.com)
Like the kinases, the phosphatases also play a role in the regulation of tau phosphorylation. (labclinics.com)
Of the 28 phosphoprotein targets measured using multiplex ELISA, the GWI model (CORT+DFP) had numerous targets with increased phosphorylation over DFP alone (e.g. (cdc.gov)
Kinases and phosphatases are responsible for phosphorylation and dephosphorylation, respectively, and are themselves regulated by phosphorylation, thus forming a complex cellular signaling network. (kinasebiotech.com)
Therefore, combining large-scale, multi-tissue kinases/phosphatases expression analysis with phosphorylation site identification is essential to provide new insights into the crucial role of phosphorylation in cell signaling. (kinasebiotech.com)
Discovery and identification of phosphoproteins is a key step in understanding the regulatory role of phosphorylation. (kinasebiotech.com)
Double-stranded DNA breaks (DSBs) induce a phosphorylation-mediated signaling cascade, but the role of phosphatases in this pathway remains unclear. (uthscsa.edu)

Ready-to-use broad-spectrum cocktail of inhibitors to preserve phosphoproteins in your samples. (activemotif.com)
Since phosphatase levels may vary among cell and tissue types, it may be necessary to increase the concentration of inhibitors. (activemotif.jp)

Protein kinases and phosphatases are organized into complex intracellular signaling networks designed to coordinate their activities in both space and time. (elsevier.com)
In order to better understand the molecular mechanisms underlying the regulation of signal transduction networks, it is important to define the spatiotemporal dynamics of both protein kinases and phosphatases within their endogenous environment. (elsevier.com)
It is clear that the coordinated and reciprocal actions of kinases and phosphatases are fundamental in the regulation of development and growth of the malaria parasite. (biomedcentral.com)
Among the essential actors in the growth and division of the parasite are kinases and phosphatases. (biomedcentral.com)
Creative BioMart provides our customers with high-quality customized services to help them analyze the tissue-specific expression of their kinases and/or phosphatases of interest. (kinasebiotech.com)
Protein kinases and phosphatases display tissue specificity. (kinasebiotech.com)
Creative BioMart offers comprehensive analysis of tissue-specific expression for almost all kinds of kinases and phosphatases in different species. (kinasebiotech.com)
Predicting the function of kinases and phosphatases by detecting their tissue-specific gene expression levels is essential for exploring their role in diseases, which provides the basis for targeted therapies. (kinasebiotech.com)
Our scientists can help our customers reveal diverse functions of kinases/phosphatases using tissue-specific approaches and provide insights into their potential functional roles in health and disease. (kinasebiotech.com)
We can perform functional analysis of phosphoproteins and nonmodified proteins expressed in different tissues to generate molecular networks dynamically regulated by tissue-specific kinases and phosphatases. (kinasebiotech.com)

Endothelial Scaffolding Protein ENH (Enigma Homolog Protein) Promotes PHLPP2 (Pleckstrin Homology Domain and Leucine-Rich Repeat Protein Phosphatase 2)-Mediated Dephosphorylation of AKT1 and eNOS (Endothelial NO Synthase) Promoting Vascular Remodeling. (nih.gov)
It is recommended to use 10 µl of the Phosphatase Inhibitor Cocktail solution to inhibit dephosphorylation of proteins for 1 ml of lysate. (activemotif.jp)

Dual specificity phosphatase 4 mediates cardiomyopathy caused by lamin A/C (LMNA) gene mutation. (jefferson.edu)

It is an exon 4 splice variant of the tyrosine phosphatase CD45. (biolegend.com)
PTP1B) is a non-receptor protein tyrosine phosphatase. (guidetopharmacology.org)
2013) Identification of a potent salicylic acid-based inhibitor of tyrosine phosphatase PTP1B. (guidetopharmacology.org)
2019) Identification and structure-function analyses of an allosteric inhibitor of the tyrosine phosphatase PTPN22. (guidetopharmacology.org)
2002) Protein tyrosine phosphatase 1B as a target for the treatment of impaired glucose tolerance and type II diabetes. (guidetopharmacology.org)

To fully evaluate the brain-region specific effects of DFP and CORT+DFP on AChE, ACh concentrations were measured in cortex (CTX), hippocampus (HIP) and striatum (STR) using HILIC UPLC-MS/MS. Mice were euthanized using focused microwave irradiation to ensure rapid inactivation of AChE, as well as endogenous proteases and phosphatases. (cdc.gov)

The Phosphatase Inhibitor Cocktail is provided as a ready-to-use 100X stock solution in DMSO. (activemotif.jp)
The Phosphatase Inhibitor Cocktail is guaranteed stable for 6 months when stored properly. (activemotif.jp)

Herein, we report the development of a genetically-encoded protein biosensor designed to specifically probe the activity of the Ca 2+ /calmodulin-dependent protein phosphatase, calcineurin. (elsevier.com)
Our reporter design utilizes a phosphatase activity-dependent molecular switch based on the N-terminal regulatory domain of the nuclear factor of activated T-cells as a specific substrate of calcineurin, sandwiched between cyan fluorescent protein and yellow fluorescent protein. (elsevier.com)
The successful design of a prototype phosphatase activity sensor lays a foundation for studying targeting and compartmentation of phosphatases. (elsevier.com)
Newman, RH & Zhang, J 2008, ' Visualization of phosphatase activity in living cells with a FRET-based calcineurin activity sensor ', Molecular BioSystems , vol. 4, no. 6, pp. 496-501. (elsevier.com)
Taken together, our data suggest that the PfI2 protein could play a role in the regulation of the P. falciparum cell cycle through its PfPP1 phosphatase regulatory activity. (biomedcentral.com)
The majority of regulators that inhibit the phosphatase activity interact with PP1c through an amino acid sequence present in the regulator and designated as the 'RVxF' motif. (biomedcentral.com)

To our surprise, we observed induction of significantly high sister chromatid exchanges (SCEs) at concentrations known to inhibit both protein phosphatase-1 (PP-1) and protein phosphatase -2A (PP-2A). (who.int)

PCDH7 potentiated ERK signaling by facilitating interaction of protein phosphatase PP2A with its potent inhibitor, the SET oncoprotein. (elsevier.com)

A Quantitative Chemical Proteomic Strategy for Profiling Phosphoprotein Phosphatases from Yeast to Humans. (kettenbachlab.org)
In the yeast Saccharomyces cerevisiae , the overexpression of Ser/Thr phosphatase Ppz1 drastically blocks cell proliferation, with a profound change in the transcriptomic and phosphoproteomic profiles. (mdpi.com)

Formation of stable attachments between kinetochores and microtubules depends on the B56-PP2A phosphatase. (nih.gov)

1990) Molecular cloning and chromosome mapping of the human gene encoding protein phosphotyrosyl phosphatase 1B. (guidetopharmacology.org)
Gene expression of bone morphogenetic protein 2 (BMP-2), runt-related transcription factor 2 (RUNX-2), and alkaline phosphatase (ALP) osteogenic markers were evaluated by real-time polymerase chain reaction (RT-qPCR). (bvsalud.org)

IMSEAR at SEARO: Protein phosphatase-1 inhibition induces high SCEs in normal whole blood cultures. (who.int)
Mann RK, Bamezai R. Protein phosphatase-1 inhibition induces high SCEs in normal whole blood cultures. (who.int)

Protein Phosphatase type 1 is a key enzyme playing diverse and essential roles in cell survival. (biomedcentral.com)

Creative BioMart provides comprehensive analysis of tissue-specific expression of phosphoproteins using Western blot, in situ hybridization, mass spectrometry, proteomics, and other technologies. (kinasebiotech.com)

Therefore, interrogation of potential organophosphorylation targets and aberrant phosphoprotein responses of critical signaling pathways in the STR were conducted. (cdc.gov)

Orthologous to human PHLPP2 (PH domain and leucine rich repeat protein phosphatase 2). (nih.gov)

Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. (nih.gov)

AChE-independent phosphoprotein signaling in an acute mouse model of Gulf War Illness. (cdc.gov)

It also helps maintain phosphoproteins and protect them from degradation better than traditional detergent based extraction buffers. (tebu-bio.com)

Anatomy14

Organisms7

Chemicals and Drugs102

Analytical, Diagnostic and Therapeutic Techniques and Equipment14

Phenomena and Processes23

Technology, Industry, Agriculture1

Information Science3

Health Care1

Inducible NO synthase: role in cellular signalling. (1/5093)

Activation of Src in human breast tumor cell lines: elevated levels of phosphotyrosine phosphatase activity that preferentially recognizes the Src carboxy terminal negative regulatory tyrosine 530. (2/5093)

The MAP kinase ERK2 inhibits the cyclic AMP-specific phosphodiesterase HSPDE4D3 by phosphorylating it at Ser579. (3/5093)

All-trans-retinoic acid inhibits Jun N-terminal kinase by increasing dual-specificity phosphatase activity. (4/5093)

The yeast ser/thr phosphatases sit4 and ppz1 play opposite roles in regulation of the cell cycle. (5/5093)

Purification and identification of a novel subunit of protein serine/threonine phosphatase 4. (6/5093)

Caffeine can override the S-M checkpoint in fission yeast. (7/5093)

Activation of myosin phosphatase targeting subunit by mitosis-specific phosphorylation. (8/5093)

Phosphoprotein Phosphatases

Phosphoproteins

Phosphorylase Phosphatase

Protein Phosphatase 2

Phosphoric Monoester Hydrolases

Protein Phosphatase 1

Okadaic Acid

Phosphorylation

Protein Kinases

Dithioerythritol

Ethers, Cyclic

Manganese

Acid Phosphatase

Protein Tyrosine Phosphatases

Sodium Cholate

Kinetics

Molecular Weight

Phosphorylases

Cantharidin

Calmodulin-Binding Proteins

Oxazoles

Phosphorus Radioisotopes

Sodium Fluoride

Enzyme Activation

Magnesium

Molecular Sequence Data

Amino Acid Sequence

Substrate Specificity

Dopamine and cAMP-Regulated Phosphoprotein 32

Mercaptoethanol

Rabbits

Cattle

Adenosine Triphosphate

Calcineurin

Phosphorylase Kinase

Muscles

Trifluoperazine

Drug Stability

Cyclic AMP

Electrophoresis, Polyacrylamide Gel

Macromolecular Substances

Glucose-6-Phosphatase

Hydroxymethylglutaryl CoA Reductases

Liver

Cytosol

Calmodulin

Enzyme Inhibitors

Histones

Hydrogen-Ion Concentration

Proteins

Hot Temperature

Rats, Inbred Strains

Protein Tyrosine Phosphatase, Non-Receptor Type 11

Dual-Specificity Phosphatases

cdc25 Phosphatases

Protein Tyrosine Phosphatase, Non-Receptor Type 1

Protein Tyrosine Phosphatase, Non-Receptor Type 6

Myosin-Light-Chain Phosphatase

Brain

Myocardium

Signal Transduction

Protein Tyrosine Phosphatases, Non-Receptor

Cell Line

Receptor-Like Protein Tyrosine Phosphatases, Class 2

Base Sequence

Microfilament Proteins

Protein Binding

Phosphatidate Phosphatase

Phosphopeptides

Dual Specificity Phosphatase 1

Phosphoserine

Phosphothreonine

Phosphates

Synapsins

Tyrosine

Isoenzymes

Receptor-Like Protein Tyrosine Phosphatases, Class 3

Sequence Homology, Amino Acid

Intracellular Signaling Peptides and Proteins

Cloning, Molecular