Phosphotyrosine
Protein Tyrosine Phosphatases
Tyrosine
Phosphorylation
src Homology Domains
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.
Protein-Tyrosine Kinases
Vanadates
Shc Signaling Adaptor Proteins
Amino Acid Sequence
Molecular Sequence Data
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.
Signal Transduction
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.
Adaptor Proteins, Signal Transducing
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
Protein Tyrosine Phosphatase, Non-Receptor Type 6
Protein Tyrosine Phosphatase, Non-Receptor Type 11
Oncogene Protein pp60(v-src)
A tyrosine-specific protein kinase encoded by the v-src oncogene of ROUS SARCOMA VIRUS. The transforming activity of pp60(v-src) depends on both the lack of a critical carboxy-terminal tyrosine phosphorylation site at position 527, and the attachment of pp60(v-src) to the plasma membrane which is accomplished by myristylation of its N-terminal glycine.
GRB2 Adaptor Protein
A signal transducing adaptor protein that links extracellular signals to the MAP KINASE SIGNALING SYSTEM. Grb2 associates with activated EPIDERMAL GROWTH FACTOR RECEPTOR and PLATELET-DERIVED GROWTH FACTOR RECEPTORS via its SH2 DOMAIN. It also binds to and translocates the SON OF SEVENLESS PROTEINS through its SH3 DOMAINS to activate PROTO-ONCOGENE PROTEIN P21(RAS).
Binding Sites
Proto-Oncogene Proteins pp60(c-src)
Membrane-associated tyrosine-specific kinases encoded by the c-src genes. They have an important role in cellular growth control. Truncation of carboxy-terminal residues in pp60(c-src) leads to PP60(V-SRC) which has the ability to transform cells. This kinase pp60 c-src should not be confused with csk, also known as c-src kinase.
Protein Binding
src-Family Kinases
A PROTEIN-TYROSINE KINASE family that was originally identified by homology to the Rous sarcoma virus ONCOGENE PROTEIN PP60(V-SRC). They interact with a variety of cell-surface receptors and participate in intracellular signal transduction pathways. Oncogenic forms of src-family kinases can occur through altered regulation or expression of the endogenous protein and by virally encoded src (v-src) genes.
Receptor, Insulin
A cell surface receptor for INSULIN. It comprises a tetramer of two alpha and two beta subunits which are derived from cleavage of a single precursor protein. The receptor contains an intrinsic TYROSINE KINASE domain that is located within the beta subunit. Activation of the receptor by INSULIN results in numerous metabolic changes including increased uptake of GLUCOSE into the liver, muscle, and ADIPOSE TISSUE.
Enzyme Activation
Proteins
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.
SH2 Domain-Containing Protein Tyrosine Phosphatases
Intracellular Signaling Peptides and Proteins
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.
Protein Tyrosine Phosphatase, Non-Receptor Type 1
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.
Adaptor Proteins, Vesicular Transport
A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found.
3T3 Cells
Cell lines whose original growing procedure consisted being transferred (T) every 3 days and plated at 300,000 cells per plate (J Cell Biol 17:299-313, 1963). Lines have been developed using several different strains of mice. Tissues are usually fibroblasts derived from mouse embryos but other types and sources have been developed as well. The 3T3 lines are valuable in vitro host systems for oncogenic virus transformation studies, since 3T3 cells possess a high sensitivity to CONTACT INHIBITION.
Recombinant Fusion Proteins
Receptor, Epidermal Growth Factor
A cell surface receptor involved in regulation of cell growth and differentiation. It is specific for EPIDERMAL GROWTH FACTOR and EGF-related peptides including TRANSFORMING GROWTH FACTOR ALPHA; AMPHIREGULIN; and HEPARIN-BINDING EGF-LIKE GROWTH FACTOR. The binding of ligand to the receptor causes activation of its intrinsic tyrosine kinase activity and rapid internalization of the receptor-ligand complex into the cell.
Receptors, Platelet-Derived Growth Factor
Specific receptors on cell membranes that react with PLATELET-DERIVED GROWTH FACTOR, its analogs, or antagonists. The alpha PDGF receptor (RECEPTOR, PLATELET-DERIVED GROWTH FACTOR ALPHA) and the beta PDGF receptor (RECEPTOR, PLATELET-DERIVED GROWTH FACTOR BETA) are the two principle types of PDGF receptors. Activation of the protein-tyrosine kinase activity of the receptors occurs by ligand-induced dimerization or heterodimerization of PDGF receptor types.
Precipitin Tests
Proto-Oncogene Proteins
Substrate Specificity
Phosphoprotein Phosphatases
Focal Adhesion Protein-Tyrosine Kinases
Paxillin
Paxillin is a signal transducing adaptor protein that localizes to FOCAL ADHESIONS via its four LIM domains. It undergoes PHOSPHORYLATION in response to integrin-mediated CELL ADHESION, and interacts with a variety of proteins including VINCULIN; FOCAL ADHESION KINASE; PROTO-ONCOGENE PROTEIN PP60(C-SRC); and PROTO-ONCOGENE PROTEIN C-CRK.
Receptor Protein-Tyrosine Kinases
Insulin Receptor Substrate Proteins
A structurally-related group of signaling proteins that are phosphorylated by the INSULIN RECEPTOR PROTEIN-TYROSINE KINASE. The proteins share in common an N-terminal PHOSPHOLIPID-binding domain, a phosphotyrosine-binding domain that interacts with the phosphorylated INSULIN RECEPTOR, and a C-terminal TYROSINE-rich domain. Upon tyrosine phosphorylation insulin receptor substrate proteins interact with specific SH2 DOMAIN-containing proteins that are involved in insulin receptor signaling.
Sequence Homology, Amino Acid
Focal Adhesion Kinase 1
A non-receptor protein tyrosine kinase that is localized to FOCAL ADHESIONS and is a central component of integrin-mediated SIGNAL TRANSDUCTION PATHWAYS. Focal adhesion kinase 1 interacts with PAXILLIN and undergoes PHOSPHORYLATION in response to adhesion of cell surface integrins to the EXTRACELLULAR MATRIX. Phosphorylated p125FAK protein binds to a variety of SH2 DOMAIN and SH3 DOMAIN containing proteins and helps regulate CELL ADHESION and CELL MIGRATION.
Protein Kinases
Genes, src
Retrovirus-associated DNA sequences (src) originally isolated from the Rous sarcoma virus (RSV). The proto-oncogene src (c-src) codes for a protein that is a member of the tyrosine kinase family and was the first proto-oncogene identified in the human genome. The human c-src gene is located at 20q12-13 on the long arm of chromosome 20.
Epidermal Growth Factor
A 6-kDa polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. Epidermal growth factor exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and EPITHELIAL CELLS. It is synthesized as a transmembrane protein which can be cleaved to release a soluble active form.
Protein Structure, Tertiary
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.
Phosphothreonine
Phospholipase C gamma
Platelet-Derived Growth Factor
Phosphatidylinositol 3-Kinases
Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.
Proto-Oncogene Proteins c-fyn
Cells, Cultured
Proto-Oncogene Proteins c-cbl
Peptides
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Transfection
Receptor, EphA8
Vanadium
Mutagenesis, Site-Directed
Peptide Mapping
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.
Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
This enzyme is a lymphoid-specific src family tyrosine kinase that is critical for T-cell development and activation. Lck is associated with the cytoplasmic domains of CD4, CD8 and the beta-chain of the IL-2 receptor, and is thought to be involved in the earliest steps of TCR-mediated T-cell activation.
Electrophoresis, Polyacrylamide Gel
Oncogene Protein v-crk
Immunoblotting
Isoenzymes
Enzyme Inhibitors
COS Cells
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).)
Protein Tyrosine Phosphatases, Non-Receptor
Sarcoma Viruses, Feline
Species of GAMMARETROVIRUS isolated from fibrosarcoma in cats. The viruses are actually recombinant feline leukemia viruses (FeLV) where part of the genome has been replaced by cellular oncogenes. It is unique to individuals and not transmitted naturally to other cats. FeSVs are replication defective and require FeLV to reproduce.
Glutathione Transferase
Tumor Cells, Cultured
Avian Sarcoma Viruses
Phosphorus Radioisotopes
Mutation
Type C Phospholipases
A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS.
Base Sequence
Amino Acid Motifs
Vinculin
Cloning, Molecular
Proto-Oncogene Proteins c-abl
Non-receptor tyrosine kinases encoded by the C-ABL GENES. They are distributed in both the cytoplasm and the nucleus. c-Abl plays a role in normal HEMATOPOIESIS especially of the myeloid lineage. Oncogenic transformation of c-abl arises when specific N-terminal amino acids are deleted, releasing the kinase from negative regulation.
Retroviridae Proteins, Oncogenic
Cell Transformation, Viral
Protein Tyrosine Phosphatase, Non-Receptor Type 12
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.
Cytoskeletal Proteins
Receptor, trkA
A protein-tyrosine kinase receptor that is specific for NERVE GROWTH FACTOR; NEUROTROPHIN 3; neurotrophin 4, neurotrophin 5. It plays a crucial role in pain sensation and thermoregulation in humans. Gene mutations that cause loss of receptor function are associated with CONGENITAL INSENSITIVITY TO PAIN WITH ANHIDROSIS, while gene rearrangements that activate the protein-tyrosine kinase function are associated with tumorigenesis.
Cell Division
Genistein
An isoflavonoid derived from soy products. It inhibits PROTEIN-TYROSINE KINASE and topoisomerase-II (DNA TOPOISOMERASES, TYPE II); activity and is used as an antineoplastic and antitumor agent. Experimentally, it has been shown to induce G2 PHASE arrest in human and murine cell lines and inhibits PROTEIN-TYROSINE KINASE.
Son of Sevenless Proteins
Anion Exchange Protein 1, Erythrocyte
A major integral transmembrane protein of the ERYTHROCYTE MEMBRANE. It is the anion exchanger responsible for electroneutral transporting in CHLORIDE IONS in exchange of BICARBONATE IONS allowing CO2 uptake and transport from tissues to lungs by the red blood cells. Genetic mutations that result in a loss of the protein function have been associated with type 4 HEREDITARY SPHEROCYTOSIS.
Cell Transformation, Neoplastic
Cell Adhesion Molecules
Sperm Capacitation
The structural and functional changes by which SPERMATOZOA become capable of oocyte FERTILIZATION. It normally requires exposing the sperm to the female genital tract for a period of time to bring about increased SPERM MOTILITY and the ACROSOME REACTION before fertilization in the FALLOPIAN TUBES can take place.
Insulin
A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).
Peptide Fragments
Blotting, Western
Protein Tyrosine Phosphatase, Non-Receptor Type 13
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.
Models, Molecular
Ligands
A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)
Oncogene Protein v-cbl
Antigens, CD45
High-molecular weight glycoproteins uniquely expressed on the surface of LEUKOCYTES and their hemopoietic progenitors. They contain a cytoplasmic protein tyrosine phosphatase activity which plays a role in intracellular signaling from the CELL SURFACE RECEPTORS. The CD45 antigens occur as multiple isoforms that result from alternative mRNA splicing and differential usage of three exons.
Amino Acids
Oncogene Proteins v-abl
ras GTPase-Activating Proteins
Cell Membrane
Organophosphorus Compounds
Acid Phosphatase
Immunosorbent Techniques
Membrane Proteins
Receptor, EphA3
An eph family receptor that is found primarily in adult BRAIN and variety of tissues in the developing embryo tissues. During embryonic development high levels of EphA3 receptor expression is seen in the nervous system and coincides with neuronal cell migration, suggesting a role for this protein in axonal pathfinding.
Antibodies, Phospho-Specific
Receptors, Cell Surface
Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.
Calcium-Calmodulin-Dependent Protein Kinases
A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)
Oncogene Proteins v-raf
Phosphoric Monoester Hydrolases
ZAP-70 Protein-Tyrosine Kinase
Yersinia
Benzoquinones
Fibroblasts
Cytoskeleton
Mitogen-Activated Protein Kinases
A superfamily of PROTEIN-SERINE-THREONINE KINASES that are activated by diverse stimuli via protein kinase cascades. They are the final components of the cascades, activated by phosphorylation by MITOGEN-ACTIVATED PROTEIN KINASE KINASES, which in turn are activated by mitogen-activated protein kinase kinase kinases (MAP KINASE KINASE KINASES).
DNA, Complementary
Oncogene Proteins
Cell Line, Transformed
Quinones
Proto-Oncogene Proteins c-crk
Proto-Oncogene Proteins c-bcr
Phosphotransferases (Alcohol Group Acceptor)
Mitogen-Activated Protein Kinase 1
Immunoprecipitation
Crystallography, X-Ray
Structure-Activity Relationship
Jurkat Cells
Protein Tyrosine Phosphatase, Non-Receptor Type 3
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.
STAT3 Transcription Factor
Tetradecanoylphorbol Acetate
Chick Embryo
Phosphotransferases
Cytoplasm
Sequence Alignment
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.
Antigens, CD
Differentiation antigens residing on mammalian leukocytes. CD stands for cluster of differentiation, which refers to groups of monoclonal antibodies that show similar reactivity with certain subpopulations of antigens of a particular lineage or differentiation stage. The subpopulations of antigens are also known by the same CD designation.
Calcium
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.
Proto-Oncogene Proteins c-yes
Organophosphates
Carbon-containing phosphoric acid derivatives. Included under this heading are compounds that have CARBON atoms bound to one or more OXYGEN atoms of the P(=O)(O)3 structure. Note that several specific classes of endogenous phosphorus-containing compounds such as NUCLEOTIDES; PHOSPHOLIPIDS; and PHOSPHOPROTEINS are listed elsewhere.
Tyrphostins
Point Mutation
Talin
Carrier Proteins
Ephrin-A5
Cytosol
Protein Conformation
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Receptor-Like Protein Tyrosine Phosphatases, Class 4
Receptors, Antigen, T-Cell
Molecules on the surface of T-lymphocytes that recognize and combine with antigens. The receptors are non-covalently associated with a complex of several polypeptides collectively called CD3 antigens (ANTIGENS, CD3). Recognition of foreign antigen and the major histocompatibility complex is accomplished by a single heterodimeric antigen-receptor structure, composed of either alpha-beta (RECEPTORS, ANTIGEN, T-CELL, ALPHA-BETA) or gamma-delta (RECEPTORS, ANTIGEN, T-CELL, GAMMA-DELTA) chains.
Antibodies
Retroviridae Proteins
Protein Processing, Post-Translational
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.
Receptor Aggregation
Isoflavones
Fusion Proteins, bcr-abl
Translation products of a fusion gene derived from CHROMOSOMAL TRANSLOCATION of C-ABL GENES to the genetic locus of the breakpoint cluster region gene on chromosome 22. Several different variants of the bcr-abl fusion proteins occur depending upon the precise location of the chromosomal breakpoint. These variants can be associated with distinct subtypes of leukemias such as PRECURSOR CELL LYMPHOBLASTIC LEUKEMIA-LYMPHOMA; LEUKEMIA, MYELOGENOUS, CHRONIC, BCR-ABL POSITIVE; and NEUTROPHILIC LEUKEMIA, CHRONIC.
Actins
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
Oncogene Proteins v-erbB
Diamide
Serine
Two-Hybrid System Techniques
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
Mass Spectrometry
Octoxynol
Focal Adhesions
An anchoring junction of the cell to a non-cellular substrate. It is composed of a specialized area of the plasma membrane where bundles of the ACTIN CYTOSKELETON terminate and attach to the transmembrane linkers, INTEGRINS, which in turn attach through their extracellular domains to EXTRACELLULAR MATRIX PROTEINS.
Proto-Oncogene Proteins c-ret
Receptor protein-tyrosine kinases involved in the signaling of GLIAL CELL-LINE DERIVED NEUROTROPHIC FACTOR ligands. They contain an extracellular cadherin domain and form a receptor complexes with GDNF RECEPTORS. Mutations in ret protein are responsible for HIRSCHSPRUNG DISEASE and MULTIPLE ENDOCRINE NEOPLASIA TYPE 2.
DNA-Binding Proteins
Models, Biological
Microscopy, Fluorescence
Cattle
Catalysis
PC12 Cells
Protein Kinase C
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.
Trypsin
STAT5 Transcription Factor
A signal transducer and activator of transcription that mediates cellular responses to a variety of CYTOKINES. Stat5 activation is associated with transcription of CELL CYCLE regulators such as CYCLIN KINASE INHIBITOR P21 and anti-apoptotic genes such as BCL-2 GENES. Stat5 is constitutively activated in many patients with acute MYELOID LEUKEMIA.
Protein-Serine-Threonine Kinases
Chromatography, Affinity
Amyloid beta-Protein Precursor
Subcellular Fractions
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)
Cricetinae
Caseins
Janus Kinase 2
A Janus kinase subtype that is involved in signaling from GROWTH HORMONE RECEPTORS; PROLACTIN RECEPTORS; and a variety of CYTOKINE RECEPTORS such as ERYTHROPOIETIN RECEPTORS and INTERLEUKIN RECEPTORS. Dysregulation of Janus kinase 2 due to GENETIC TRANSLOCATIONS have been associated with a variety of MYELOPROLIFERATIVE DISORDERS.
Cell Movement
Role of alphavbeta3 integrin in the activation of vascular endothelial growth factor receptor-2. (1/3233)
Interaction between integrin alphavbeta3 and extracellular matrix is crucial for endothelial cells sprouting from capillaries and for angiogenesis. Furthermore, integrin-mediated outside-in signals co-operate with growth factor receptors to promote cell proliferation and motility. To determine a potential regulation of angiogenic inducer receptors by the integrin system, we investigated the interaction between alphavbeta3 integrin and tyrosine kinase vascular endothelial growth factor receptor-2 (VEGFR-2) in human endothelial cells. We report that tyrosine-phosphorylated VEGFR-2 co-immunoprecipitated with beta3 integrin subunit, but not with beta1 or beta5, from cells stimulated with VEGF-A165. VEGFR-2 phosphorylation and mitogenicity induced by VEGF-A165 were enhanced in cells plated on the alphavbeta3 ligand, vitronectin, compared with cells plated on the alpha5beta1 ligand, fibronectin or the alpha2beta1 ligand, collagen. BV4 anti-beta3 integrin mAb, which does not interfere with endothelial cell adhesion to vitronectin, reduced (i) the tyrosine phosphorylation of VEGFR-2; (ii) the activation of downstream transductor phosphoinositide 3-OH kinase; and (iii) biological effects triggered by VEGF-A165. These results indicate a new role for alphavbeta3 integrin in the activation of an in vitro angiogenic program in endothelial cells. Besides being the most important survival system for nascent vessels by regulating cell adhesion to matrix, alphavbeta3 integrin participates in the full activation of VEGFR-2 triggered by VEGF-A, which is an important angiogenic inducer in tumors, inflammation and tissue regeneration. (+info)Involvement of tyrosine phosphorylation in HMG-CoA reductase inhibitor-induced cell death in L6 myoblasts. (2/3233)
Our previous studies have shown that the HMG-CoA reductase (HCR) inhibitor (HCRI), simvastatin, causes myopathy in rabbits and kills L6 myoblasts. The present study was designed to elucidate the molecular mechanism of HCRI-induced cell death. We have demonstrated that simvastatin induces the tyrosine phosphorylation of several cellular proteins within 10 min. These phosphorylations were followed by apoptosis, as evidenced by the occurrence of internucleosomal DNA fragmentation and by morphological changes detected with Nomarski optics. Simvastatin-induced cell death was prevented by tyrosine kinase inhibitors. The MTT assay revealed that the addition of mevalonic acid into the culture medium partially inhibited simvastatin-induced cell death. Thus, these results suggested that protein tyrosine phosphorylation might play an important role in the intracellular signal transduction pathway mediating the HCRI-induced death of myoblasts. (+info)Phosphotyrosine binding domains of Shc and insulin receptor substrate 1 recognize the NPXpY motif in a thermodynamically distinct manner. (3/3233)
Phosphotyrosine binding (PTB) domains of the adaptor protein Shc and insulin receptor substrate (IRS-1) interact with a distinct set of activated and tyrosine-phosphorylated cytokine and growth factor receptors and play important roles in mediating mitogenic signal transduction. By using the technique of isothermal titration calorimetry, we have studied the thermodynamics of binding of the Shc and IRS-1 PTB domains to tyrosine-phosphorylated NPXY-containing peptides derived from known receptor binding sites. The results showed that relative contributions of enthalpy and entropy to the free energy of binding are dependent on specific phosphopeptides. Binding of the Shc PTB domain to tyrosine-phosphorylated peptides from TrkA, epidermal growth factor, ErbB3, and insulin receptors is achieved via an overall entropy-driven reaction. On the other hand, recognition of the phosphopeptides of insulin and interleukin-4 receptors by the IRS-1 PTB domain is predominantly an enthalpy-driven process. Mutagenesis and amino acid substitution experiments showed that in addition to the tyrosine-phosphorylated NPXY motif, the PTB domains of Shc and IRS-1 prefer a large hydrophobic residue at pY-5 and a small hydrophobic residue at pY-1, respectively (where pY is phosphotyrosine). These results agree with the calculated solvent accessibility of these two key peptide residues in the PTB domain/peptide structures and support the notion that the PTB domains of Shc and IRS-1 employ functionally distinct mechanisms to recognize tyrosine-phosphorylated receptors. (+info)In situ detection of activated Bruton's tyrosine kinase in the Ig signaling complex by phosphopeptide-specific monoclonal antibodies. (4/3233)
Bruton's tyrosine kinase (Btk) is a critical transducer of signals originating from the B cell antigen receptor (BCR). Dosage, sequential phosphorylation, and protein interactions are interdependent mechanisms influencing Btk function. Phosphopeptide-specific mAbs recognizing two distinct phosphotyrosine modifications were used to quantify Btk activation by immunofluorescent techniques during B cell stimulation. In a population of cultured B cells stimulated by BCR crosslinking and analyzed by flow cytometry, transient phosphorylation of the regulatory Btk tyrosine residues (551Y and 223Y) was detected. The kinetics of phosphorylation of the residues were temporally distinct. Tyrosine 551, a transactivating substrate site for Src-family kinases, was maximally phosphorylated within approximately 30 seconds of stimulation as monitored by flow cytometry. Tyrosine 223, an autophosphorylation site within the SH3 domain, was maximally phosphorylated at approximately 5 minutes. Btk returned to a low tyrosine phosphorylation level within 30 minutes, despite persistent elevation of global tyrosine phosphorylation. Colocalization of activated Btk molecules with the crosslinked BCR signaling complex was observed to coincide with the period of maximal Btk tyrosine phosphorylation when stimulated B cells were analyzed with confocal microscopy. The results of these in situ temporal and spatial analyses imply that Btk signaling occurs in the region of the Ig receptor signaling complex, suggesting a similar location for downstream targets of its activity. (+info)Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. (5/3233)
Protein tyrosine phosphatase-1B (PTP-1B) has been implicated in the negative regulation of insulin signaling. Disruption of the mouse homolog of the gene encoding PTP-1B yielded healthy mice that, in the fed state, had blood glucose concentrations that were slightly lower and concentrations of circulating insulin that were one-half those of their PTP-1B+/+ littermates. The enhanced insulin sensitivity of the PTP-1B-/- mice was also evident in glucose and insulin tolerance tests. The PTP-1B-/- mice showed increased phosphorylation of the insulin receptor in liver and muscle tissue after insulin injection in comparison to PTP-1B+/+ mice. On a high-fat diet, the PTP-1B-/- and PTP-1B+/- mice were resistant to weight gain and remained insulin sensitive, whereas the PTP-1B+/+ mice rapidly gained weight and became insulin resistant. These results demonstrate that PTP-1B has a major role in modulating both insulin sensitivity and fuel metabolism, thereby establishing it as a potential therapeutic target in the treatment of type 2 diabetes and obesity. (+info)Interferon-alpha activates multiple STAT proteins and upregulates proliferation-associated IL-2Ralpha, c-myc, and pim-1 genes in human T cells. (6/3233)
Interferon-alpha (IFN-alpha) is a pleiotropic cytokine that has antiviral, antiproliferative, and immunoregulatory functions. There is increasing evidence that IFN-alpha has an important role in T-cell biology. We have analyzed the expression of IL-2Ralpha, c-myc, and pim-1 genes in anti-CD3-activated human T lymphocytes. The induction of these genes is associated with interleukin-2 (IL-2)-induced T-cell proliferation. Treatment of T lymphocytes with IFN-alpha, IL-2, IL-12, and IL-15 upregulated IL-2Ralpha, c-myc, and pim-1 gene expression. IFN-alpha also sensitized T cells to IL-2-induced proliferation, further suggesting that IFN-alpha may be involved in the regulation of T-cell mitogenesis. When we analyzed the nature of STAT proteins capable of binding to IL-2Ralpha, pim-1, and IRF-1 GAS elements after cytokine stimulation, we observed IFN-alpha-induced binding of STAT1, STAT3, and STAT4, but not STAT5 to all of these elements. Yet, IFN-alpha was able to activate binding of STAT5 to the high-affinity IFP53 GAS site. IFN-alpha enhanced tyrosine phosphorylation of STAT1, STAT3, STAT4, STAT5a, and STAT5b. IL-12 induced STAT4 and IL-2 and IL-15 induced STAT5 binding to the GAS elements. Taken together, our results suggest that IFN-alpha, IL-2, IL-12, and IL-15 have overlapping activities on human T cells. These findings thus emphasize the importance of IFN-alpha as a T-cell regulatory cytokine. (+info)Involvement of wiskott-aldrich syndrome protein in B-cell cytoplasmic tyrosine kinase pathway. (7/3233)
Bruton's tyrosine kinase (Btk) has been shown to play a role in normal B-lymphocyte development. Defective expression of Btk leads to human and murine immunodeficiencies. However, the exact role of Btk in the cytoplasmic signal transduction in B cells is still unclear. This study represents a search for the substrate for Btk in vivo. We identified one of the major phosphoproteins associated with Btk in the preB cell line NALM6 as the Wiskott-Aldrich syndrome protein (WASP), the gene product responsible for Wiskott-Aldrich syndrome, which is another hereditary immunodeficiency with distinct abnormalities in hematopoietic cells. We demonstrated that WASP was transiently tyrosine-phosphorylated after B-cell antigen receptor cross-linking on B cells, suggesting that WASP is located downstream of cytoplasmic tyrosine kinases. An in vivo reconstitution system demonstrated that WASP is physically associated with Btk and can serve as the substrate for Btk. A protein binding assay suggested that the tyrosine-phosphorylation of WASP alters the association between WASP and a cellular protein. Furthermore, identification of the phosphorylation site of WASP in reconstituted cells allowed us to evaluate the catalytic specificity of Btk, the exact nature of which is still unknown. (+info)Expression of the erythropoietin receptor by trophoblast cellsin the human placenta. (8/3233)
Nonclassical sites of erythropoietin (EPO) and erythropoietin receptor (EPO-R) expression have been described that suggest new physiological roles for this hormone unrelated to erythropoiesis. The recent finding of EPO expression by trophoblast cells in the human placenta prompted us to consider whether these cells also express EPO-R. With use of immunocytochemistry, EPO-R was identified in villous and extravillous cytotrophoblast cells, as well as in the syncytiotrophoblast at all gestational ages. EPO-R was also expressed by cells within the villous core, including endothelial cells of fetoplacental blood vessels. Placental tissues and isolated and immunopurified trophoblast cells, as well as trophoblast-derived choriocarcinoma Jar cells, expressed immunoreactive EPO-R on Western blot. EPO-R mRNA was also detected in the same placental tissues and trophoblast cells by nested-primer reverse transcription-polymerase chain reaction. Finally, EPO-R was functional insofar as the receptor was phosphorylated on tyrosine residues in response to exogenous EPO treatment of cultured trophoblast or Jar cells. Thus, the present findings support the hypothesis that trophoblast cells of the human placenta express EPO-R. In view of these results, taken together with previous work demonstrating EPO expression by the same cells, an autocrine role for this hormone in the survival, proliferation, or differentiation of placental trophoblast cells is proposed. (+info)
RCSB PDB - 1SPR: BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED...
PROSITE
PID1 Gene - GeneCards | PCLI1 Protein | PCLI1 Antibody
[email protected]:
Bridging the gap between protein-tyrosine phosphorylation networks, metabolism and physiology in...
Signal-Seeker™ Phosphotyrosine Enrichment Kit (immunoprecipitation format) - Cytoskeleton, Inc.
Structure Cluster
- 1K2M: Solution Structure of the FHA2 Domain of Rad53 Complexed with a Phosphotyrosyl Peptide...
Actin Colocalizes with Tir and Phosphotyrosine (PY) Sta | Open-i
Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions....
Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.
Analysis of tyro sine phosphorylation-dependent interactions between stimulatory effector proteins and the B cell co-receptor...
Detecting Tyrosine-Phosphorylated Proteins by Western Blot Analysis - Current Protocols in Immunology - Sawasdikosol - Wiley...
1ptv - Proteopedia, life in 3D
Patent US4543439 - Production and use of monoclonal antibodies to phosphotyrosine-containing ... - Google Patents
Alexa Fluor® 647 Anti-Phosphotyrosine antibody [EPR16871] (ab205480) | Abcam
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unphosphorylated Dok1 (Ser-450) Peptide - ECM Biosciences
The role of His66 and His72 in the reaction mechanism of bovine liver low-M(r) phosphotyrosine protein phosphatase. | IRIS...
Cross-linking of ICAM-1 on T cells induces transient tyrosine phosphorylation and inactivation of cdc2 kinase. | The Journal of...
Exploitation of host cell signaling machinery: Activation of macrophage phosphotyrosine phosphatases as a novel mechanism of...
A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is...
Results for cd00047
Studies on the role of the SH2 domain-containing phosphotyrosine phosphatase, PTP2C, in insulin signaling. :: Dartmouth...
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Tyrosine Phosphorylation as a Widespread Regulatory Mechanism in Prokaryotes | Journal of Bacteriology
Cloning, purification, and properties of a phosphotyrosine pro...
Scientific Protocols -
Detection of phosphorylation on large proteins by western blotting using Phos-tag containing gel
PhosphoDetect™ Anti-Phosphotyrosine Mouse mAb (PY20) | 525295
Tyrosine phosphorylation of Syk after stimulation of NK | Open-i
ErbB4 phosphorylation | Scientist Solutions
ACK Inhibition | ACK Inhibitor Review
Association of the tyrosine phosphorylated epidermal growth factor receptor with a 55-kD tyrosine phosphorylated protein at the...
Mitogenic signalling pathway of tumour necrosis factor involves the rapid tyrosine phosphorylation of 41,000-Mr and 43,000-Mr...
Identification and characterization of the autophosphorylation sites of phosphoinositide 3-kinase isoforms beta and gamma -...
Supplementary MaterialsSupplementary Document. phosphorylated at tyrosine 97 in the postischemic mind | The Critical Role of...
Identification of tyrosine-phosphorylated proteins associated with metastasis and functional analysis of FER in human...
Identification of tyrosine-phosphorylated proteins associated with metastasis and functional analysis of FER in human...
Phosphoinositide 3-kinase-dependent phosphorylation of the dual adaptor for phosphotyrosine and 3-phosphoinositides by the Src...
Direct visualization of the phosphorylated epidermal growth factor receptor during its internalization in A-431 cells. | JCB
Tyrosine phosphorylation profiling in FGF-2 stimulated human embryonic stem cells | [email protected]
Systemic analysis of tyrosine phosphorylated proteins in angiopoietin-1 induced signaling pathway of endothelial cells<...
Comparisons of tyrosine phosphorylated proteins in cells expressing lung cancer-specific alleles of EGFR and KRAS - CORE
Phosphoproteomics identified Endofin, DCBLD2, and KIAA0582 as novel tyrosine phosphorylation targets of EGF signaling and...
BeatingCancerCenter - The Di Bella Method - The activation of the phosphotyrosine phosphatase eta (r-PTP eta) is responsible...
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High-Throughput Phosphotyrosine Profiling Using SH2 Domains by Kazuya Machida, Christopher M. Thompson et al.
anti-STAT1 anticorps (pTyr701) | Produit ABIN539531
anti-Calcineurin B anticorps (pTyr106) (HRP) | Produit ABIN1712443
Tyrosine
Tyrosine 500 mg
Best Time To Take Tyrosine 2020
Anti-Nitro tyrosine抗体[HM.11] (ab7048)参考文献
Abdominal Exercise Machine Electric Muscle Stimulator ABS EMS Trainer Fitness Burn Fat Weight Loss Body Slimming Massage -...
Phosphotyrosine-binding domain
In molecular biology, Phosphotyrosine-binding domains are protein domains which bind to phosphotyrosine. The phosphotyrosine- ... The phosphotyrosine-binding domain of insulin receptor substrate-1 is not related to the phosphotyrosine-binding domain of ... Two arginines in this domain are responsible for hydrogen bonding phosphotyrosine residues on an Ac-LYASSNPApY-NH2 peptide in ... Insulin receptor substrate-1 proteins contain both a pleckstrin homology domain and a phosphotyrosine binding (PTB) domain. The ...
Phosphotyrosine interaction domain containing 1
"Entrez Gene: Phosphotyrosine interaction domain containing 1". Retrieved 2018-06-01. Wang B, Zhang M, Ni YH, Liu F, Fan HQ, Fei ... Phosphotyrosine interaction domain containing 1 is a protein that in humans is encoded by the PID1 gene. GRCh38: Ensembl ... a novel gene containing a phosphotyrosine-binding (PTB) domain that stimulates 3T3-L1 preadipocytes proliferation". Gene. 379: ...
Parvularia atlantis
"Earliest Holozoan expansion of phosphotyrosine signaling". Molecular Biology and Evolution. 31 (3): 517-528. doi:10.1093/molbev ...
LNX1
Dho SE, Jacob S, Wolting CD, French MB, Rohrschneider LR, McGlade CJ (Apr 1998). "The mammalian numb phosphotyrosine-binding ...
Mehdi Mollapour
Mayer, Matthias P. (2010). "Phosphotyrosine Confers Client Specificity to Hsp90". Molecular Cell. 37 (3): 295-296. doi:10.1016/ ...
NUMB (gene)
Identification of cytoplasmic and membrane-associated variants of the phosphotyrosine binding domain". J. Biol. Chem. 274 (46 ... 1998). "The mammalian numb phosphotyrosine-binding domain. Characterization of binding specificity and identification of a ... 2003). "Integrin β cytoplasmic domain interactions with phosphotyrosine-binding domains: A structural prototype for diversity ... was found to selectively tag the membrane Notch1 receptor for ubiquitination through the interaction of its Phosphotyrosine- ...
Tyrosine
Phosphotyrosine can be detected through specific antibodies. Tyrosine residues may also be modified by the addition of a ... In its phosphorylated form, tyrosine is called phosphotyrosine. Tyrosine phosphorylation is considered to be one of the key ... Tyrosine sulfation is catalyzed by tyrosylprotein sulfotransferase (TPST). Like the phosphotyrosine antibodies mentioned above ...
TMEM128
Grossmann A, Benlasfer N, Birth P, Hegele A, Wachsmuth F, Apelt L, Stelzl U (March 2015). "Phospho-tyrosine dependent protein- ...
Coiled-coil domain containing 74a
Grossmann A, Benlasfer N, Birth P, Hegele A, Wachsmuth F, Apelt L, Stelzl U (March 2015). "Phospho-tyrosine dependent protein- ... Grossmann A, Benlasfer N, Birth P, Hegele A, Wachsmuth F, Apelt L, Stelzl U (March 2015). "Phospho-tyrosine dependent protein- ...
Giulio Superti-Furga
2002; 108:247-259, doi:10.1016/S0092-8674(02)00623-2. Hantschel, O. et al.: A Myristoyl / Phosphotyrosine Switch Regulates c- ...
Adapter molecule crk
9614078 Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Mol. Syst. Biol. 1 ... Mayer BJ, Hanafusa H (1990). "Association of the v-crk oncogene product with phosphotyrosine-containing proteins and protein ... recruiting cytoplasmic proteins in the vicinity of tyrosine kinase through SH2-phosphotyrosine interaction. The N-terminal SH2 ...
Lewis C. Cantley
Christofk HR, Vander Heiden MG, Wu N, Asara JM, Cantley LC (March 2008). "Pyruvate kinase M2 is a phosphotyrosine-binding ... and that the SH2 domain of p85 specifically recognized phosphotyrosines on growth factor receptors or adaptor proteins via the ...
HER2
Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Molecular Systems Biology ...
QSER1
Eight are phosphoserines, one phosphotyrosine, and three phosphothreonines. Three of these sites have been shown to be ...
STAT5A
Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Mol. Syst. Biol. 1 (1): E1 ...
SH3BGRL
Schulze WX, Deng L, Mann M (2006). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Mol. Syst. Biol. 1 (1): ...
CBLB (gene)
Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Mol. Syst. Biol. 1: E1-E13 ...
Epidermal growth factor receptor
Sakaguchi K, Okabayashi Y, Kido Y, Kimura S, Matsumura Y, Inushima K, Kasuga M (April 1998). "Shc phosphotyrosine-binding ... Keilhack H, Tenev T, Nyakatura E, Godovac-Zimmermann J, Nielsen L, Seedorf K, Böhmer FD (September 1998). "Phosphotyrosine 1173 ... Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Molecular Systems Biology ... and signaling by several other proteins that associate with the phosphorylated tyrosines through their own phosphotyrosine- ...
GRB2
Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Molecular Systems Biology ... "Involvement of SH2-containing phosphotyrosine phosphatase Syp in erythropoietin receptor signal transduction pathways". The ...
PKM2
Christofk HR, Vander Heiden MG, Wu N, Asara JM, Cantley LC (March 2008). "Pyruvate kinase M2 is a phosphotyrosine-binding ...
PTPN11
"Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human ... Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Mol. Syst. Biol. 1 (1): E1 ... This PTP contains two tandem Src homology-2 domains, which function as phospho-tyrosine binding domains and mediate the ... "The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp". J. Biol. Chem. 268 (16): ...
ErbB
Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Mol. Syst. Biol. 1 ( ...
ERBB4
Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Molecular Systems Biology ...
PTPN5
Nguyen TH, Liu J, Lombroso PJ (Jul 2002). "Striatal enriched phosphatase 61 dephosphorylates Fyn at phosphotyrosine 420". The ... Nguyen TH, Liu J, Lombroso PJ (Jul 2002). "Striatal enriched phosphatase 61 dephosphorylates Fyn at phosphotyrosine 420". The ...
N-acetyl-D-glucosamine kinase
Maguire PB, Wynne KJ, Harney DF, O'Donoghue NM, Stephens G, Fitzgerald DJ (Jun 2002). "Identification of the phosphotyrosine ...
Src family kinase
August 2008). "Global impact of oncogenic Src on a phosphotyrosine proteome". Journal of Proteome Research. 7 (8): 3447-60. doi ...
Integrin beta 3
"The phosphotyrosine binding-like domain of talin activates integrins". J. Biol. Chem. 277 (24): 21749-58. doi:10.1074/jbc. ...
TLN1
Calderwood DA, Yan B, de Pereda JM, Alvarez BG, Fujioka Y, Liddington RC, Ginsberg MH (Jun 2002). "The phosphotyrosine binding- ...
TLN2
Calderwood DA, Yan B, de Pereda JM, Alvarez BG, Fujioka Y, Liddington RC, Ginsberg MH (Jun 2002). "The phosphotyrosine binding- ...
Talin (protein)
Calderwood DA, Yan B, de Pereda JM, Alvarez BG, Fujioka Y, Liddington RC, Ginsberg MH (June 2002). "The phosphotyrosine binding ...
Phosphotyrosine MAP2K1 ELISA Kit | Sigma-Aldrich
Human Metabolome Database: Showing metabocard for O-Phosphotyrosine (HMDB0006049)
O-Phosphotyrosine. Description. O-Phosphotyrosine is a phosphorylated amino acid that occurs in a number of proteins. Tyrosine ... 3D MOL for HMDB0006049 (O-Phosphotyrosine). HMDB0006049 RDKit 3D O-Phosphotyrosine 29 29 0 0 0 0 0 0 0 0999 V2000 -4.2204 ... 3D-SDF for HMDB0006049 (O-Phosphotyrosine). HMDB0006049 RDKit 3D O-Phosphotyrosine 29 29 0 0 0 0 0 0 0 0999 V2000 -4.2204 ... O-Phosphotyrosine,4TMS,isomer #1. C[Si](C)(C)N[[email protected]@H](CC1=CC=C(OP(=O)(O[Si](C)(C)C)O[Si](C)(C)C)C=C1)C(=O)O[Si](C)(C)C. 2371.9. ...
Human Phosphotyrosine STAT6 ELISA PEL-STAT6-Y-1 ELISA | tebu-b...
RBC membrane damage and decreased band 3 phospho-tyrosine phosphatase activity are markers of COPD progression
CD15 monoclonal antibodies react with a phosphotyrosine-containing protein on the surface of human neutrophils<...
Skubitz, K. M. ; Mendiola, J. R. ; Collett, M. S. / CD15 monoclonal antibodies react with a phosphotyrosine-containing protein ... CD15 monoclonal antibodies react with a phosphotyrosine-containing protein on the surface of human neutrophils. / Skubitz, K. M ... Skubitz, K. M., Mendiola, J. R., & Collett, M. S. (1988). CD15 monoclonal antibodies react with a phosphotyrosine-containing ... CD15 monoclonal antibodies react with a phosphotyrosine-containing protein on the surface of human neutrophils. Journal of ...
Negative regulation of TCR signaling by linker for activation of X cells via phosphotyrosine-dependent and -independent...
"The Tyrosine Kinase BceF and the Phosphotyrosine Phosphatase BceD of B" by Ana S. Ferreira, Ines N. Silva et al.
... investigate the pathogenicity and potential mechanisms of virulence dependent on the tyrosine kinase BceF and phosphotyrosine ... The Tyrosine Kinase BceF and the Phosphotyrosine Phosphatase BceD of Burkholderia contaminans Are Required for Efficient ... The Tyrosine Kinase BceF and the Phosphotyrosine Phosphatase BceD of Burkholderia contaminans are required for efficient ... investigate the pathogenicity and potential mechanisms of virulence dependent on the tyrosine kinase BceF and phosphotyrosine ...
Anti-Phosphotyrosine [PY20] | Absolute Antibody
Phosphotyrosine (p-Tyr) antibody. Clone PY20. Engineered into new species and isotypes to improve your experiments. ... Immunogen: Phosphotyrosine conjugated to Keyhole limpet hemocyanin (KLH). Specificity: PY20 recognizes phospho-tyrosine and ... Monoclonal antibodies to phosphotyrosine. J Immunol Methods. PMID:2452204 Note on publication: Describes generation of anti- ... An excellent comparison of anti-phosphotyrosine antibodies can be found here .. Antibody first published in: Glenney et al. ...
Anti-Phosphotyrosine IgG Polyclonal Antibody | Eagle Biosciences
The Anti-Phosphotyrosine IgG Polyclonal Antibody is specific for phosphotyrosine and is not species specific; for research use ... Anti-Phosphotyrosine IgG Polyclonal Antibody. THe Anti-Phosphotyrosine IgG Polyclonal Antibody is For Research Use Only ... Anti-Phosphotyrosine IgG Polyclonal Antibody quantity. Add to cart. SKU: PHT00-A250 Categories: All Products, Antibodies / ... Anti-Phosphotyrosine IgG Polyclonal Antibody. $160.00. This Eagle Biosciences goat polyclonal antibody is specific for ...
phosphotyrosine phosphatase - Lab Artificial Skins and Bones
S-EPMC177630 - Cloning, purification, and properties of a phosphotyrosine protein phosphatase from Streptomyces coelicolor A3(2...
The purified fusion enzyme catalyzed the removal of phosphate from p-nitrophenylphosphate (PNPP), phosphotyrosine (PY), and a ... acidic phosphotyrosine protein phosphatases (PTPases). After expression of S. coelicolor ptpA in Escherichia coli with a pT7-7- ... commercial phosphopeptide containing a single phosphotyrosine residue but did not cleave phosphoserine or phosphothreonine. The ... the enzyme appears to prefer phosphotyrosine and/or peptides containing phosphotyrosine in comparison to serine and threonine. ...
JH Schatz | Schnell Lab
Phosphotyrosine couples peptide binding and SHP2 activation via a dynamic allosteric network | Carlomagno Group
Crystallisation of a low molecular weight phosphotyrosine protein phosphatase from bovine liver. | FEBS Lett;343(2): 107-8,...
Crystallisation of a low molecular weight phosphotyrosine protein phosphatase from bovine Crystallisation of a low molecular ... Single crystals of a low molecular weight phosphotyrosine protein phosphatase from bovine liver have been grown. The crystals ... weight phosphotyrosine protein phosphatase from bovine liver. Su, X D; Agango, E G; Taddei, N; Bucciantini, M; Stefani, M; ...
Insulin Differentially Regulates Protein Phosphotyrosine Phosphatase Activity in Rat Hepatoma Cells<...
Meyerovitch J, Backer JM, Kahn CR, Shoelson SE, Csermely P. Insulin Differentially Regulates Protein Phosphotyrosine ... We have studied the effect of insulin stimulation on phosphotyrosine phosphatase (PTPase) activity in the well-differentiated ... Insulin Differentially Regulates Protein Phosphotyrosine Phosphatase Activity in Rat Hepatoma Cells. In: Biochemistry. 1992 ; ... abstract = "We have studied the effect of insulin stimulation on phosphotyrosine phosphatase (PTPase) activity in the well- ...
Bradykinin-induced inhibition of cell proliferation and tyrosine kinase activity in rat mesangial cells
... phosphotyrosine kinase activity and bradykinin receptor activation in rat mesangial cells was investigated. We demonstrated ... We next found that BK induced a dose-dependent inhibition of phospho-tyrosine kinase activity. Treatments with pertussis-toxin ... The relationship between cell proliferation, protein tyrosine phosphorylation, phosphotyrosine kinase activity and bradykinin ... kinase C inhibitors and chelation of free cytosolic calcium did not change the bradykinin-induced inhibition of phosphotyrosine ...
SHE Src homology 2 domain containing E [Homo sapiens (human)] - Gene - NCBI
SQSTM1 gene: MedlinePlus Genetics
An oncogenic epidermal growth factor receptor signals via a p21-activated kinase-caldesmon-myosin phosphotyrosine complex<...
An oncogenic epidermal growth factor receptor signals via a p21-activated kinase-caldesmon-myosin phosphotyrosine complex. In: ... An oncogenic epidermal growth factor receptor signals via a p21-activated kinase-caldesmon-myosin phosphotyrosine complex. ... An oncogenic epidermal growth factor receptor signals via a p21-activated kinase-caldesmon-myosin phosphotyrosine complex. / ... An oncogenic epidermal growth factor receptor signals via a p21-activated kinase-caldesmon-myosin phosphotyrosine complex. ...
Cell growth, global phosphotyrosine elevation, and c-Met phosphorylation through Src family kinases in colorectal cancer cells....
Cell growth, global phosphotyrosine elevation, and c-Met phosphorylation through Src family kinases in colorectal cancer cells. ... Cell growth, global phosphotyrosine elevation, and c-Met phosphorylation through Src family kinases in colorectal cancer cells. ... Cell Line, Tumor, Cell Proliferation, Colorectal Neoplasms, Humans, Phosphotyrosine, Proto-Oncogene Proteins c-met, src-Family ...
RhoA Antibody (Mouse Monoclonal) - Cytoskeleton, Inc.
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Mitochondrial stress induced by continuous stimulation under hypoxia rapidly drives T cell exhaustion | Nature Immunology
6: Persistent mtROS increases elevation of phosphotyrosine signaling and NFAT localization.. a, Global phosphotyrosine staining ... 6b). Phosphotyrosine signaling is a major player in T cell biology downstream of many cell surface interactions, including TCR ... Phosphotyrosine antibody (P-Tyr-100) was obtained from Cell Signaling. SIINFEKL peptide was obtained from AnaSpec. IL-2 and IL- ... 8a). Phosphotyrosine cascades promote nuclear accumulation of NFAT1, and ROS induction alone (via actinomycin A) drove ...
SMART: ZnF C2H2 domain annotation
Neuroacanthocytosis Syndromes Differential Diagnoses
A Novel Classification of Lung Cancer into Molecular Subtypes | PLOS ONE
oxygen binding Antibodies | Invitrogen
...
Gene Ontology Classifications
Molecular weight phosphotyrosine protein1
- Crystallisation of a low molecular weight phosphotyrosine protein phosphatase from bovine liver. (bvsalud.org)
Proteins2
- O-Phosphotyrosine is a phosphorylated amino acid that occurs in a number of proteins. (hmdb.ca)
- Vadlamudi RK, Joung I, Strominger JL, Shin J. p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins. (medlineplus.gov)
Tyrosine4
- The Tyrosine Kinase BceF and the Phosphotyrosine Phosphatase BceD of B" by Ana S. Ferreira, Ines N. Silva et al. (tudublin.ie)
- The aim of this study was to investigate the pathogenicity and potential mechanisms of virulence dependent on the tyrosine kinase BceF and phosphotyrosine phosphatase BceD of the cystic fibrosis opportunistic pathogen Burkholderia contaminans IST408. (tudublin.ie)
- SHP2 is a ubiquitous protein tyrosine phosphatase, whose activity is regulated by phosphotyrosine (pY)-containing peptides generated in response to extracellular stimuli. (carlomagno-group.org)
- The relationship between cell proliferation, protein tyrosine phosphorylation, phosphotyrosine kinase activity and bradykinin receptor activation in rat mesangial cells was investigated. (nih.gov)
Protein6
- Phosphoamino acid analysis of the 170- to 190-kDa protein showed that it contained predominantly phosphotyrosine and a low level of phosphoserine. (umn.edu)
- Skubitz, KM , Mendiola, JR & Collett, MS 1988, ' CD15 monoclonal antibodies react with a phosphotyrosine-containing protein on the surface of human neutrophils ', Journal of Immunology , vol. 141, no. 12, pp. 4318-4323. (umn.edu)
- Cloning, purification, and properties of a phosphotyrosine protein phosphatase from Streptomyces coelicolor A3(2). (omicsdi.org)
- We describe the isolation and characterization of a gene (ptpA) from Streptomyces coelicolor A3(2) that codes for a protein with a deduced M(r) of 17,690 containing significant amino acid sequence identity with mammalian and prokaryotic small, acidic phosphotyrosine protein phosphatases (PTPases). (omicsdi.org)
- The major secreted isoenzyme of human prostatic acid phosphatase (PAcP) (EC 3.1.3.2), which catalyses p-nitrophenyl phosphate (PNPP) hydrolysis at acid pH values, was found to have phosphotyrosyl protein phosphatase activity since it dephosphorylated three different phosphotyrosine-containing protein substrates. (omicsdi.org)
- Treatments with pertussis-toxin, inhibition of phospholipase C and protein kinase C inhibitors and chelation of free cytosolic calcium did not change the bradykinin-induced inhibition of phosphotyrosine kinase. (nih.gov)
Residue3
- The purified fusion enzyme catalyzed the removal of phosphate from p-nitrophenylphosphate (PNPP), phosphotyrosine (PY), and a commercial phosphopeptide containing a single phosphotyrosine residue but did not cleave phosphoserine or phosphothreonine. (omicsdi.org)
- Predicted to enable phosphotyrosine residue binding activity. (nih.gov)
- Enables miRNA binding activity and phosphotyrosine residue binding activity. (jax.org)
Peptides1
- although, the enzyme appears to prefer phosphotyrosine and/or peptides containing phosphotyrosine in comparison to serine and threonine. (omicsdi.org)
Phosphorylation1
- Cell growth, global phosphotyrosine elevation, and c-Met phosphorylation through Src family kinases in colorectal cancer cells. (ox.ac.uk)
Cytosol1
- Phosphorylated STATs dimerize within the cytosol via their phosphotyrosines and Src-homology 2 (SH2) domains. (medscape.com)
Oncogenic1
- 11] "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. (tcdb.org)
Monoclonal2
- Recombinant monoclonal antibody to Phosphotyrosine. (absoluteantibody.com)
- Monoclonal antibodies to phosphotyrosine. (absoluteantibody.com)
Kinase1
- Phosphotyrosine interactome of the ErbB-receptor kinase family. (mpg.de)
Species1
- This Eagle Biosciences goat polyclonal antibody is specific for phosphotyrosine and is not species specific. (eaglebio.com)
Insulin1
- We have studied the effect of insulin stimulation on phosphotyrosine phosphatase (PTPase) activity in the well-differentiated rat hepatoma cell line Fao. (elsevier.com)
Phosphoserine1
- The apparent Km values for phosphorylated angiotensin II, anti-pp60src immunoglobulin G and casein were in the nM range for phosphotyrosine residues, which was about 50-fold lower than the Km for phosphoserine residues in casein. (omicsdi.org)
Amino1
- FRS2 contains both a consensus myristylation sequence, involved in its recruitment to the cell membrane and a putative phosphotyrosine binding (PTB)domain in its amino-terminus. (novusbio.com)
Receptor1
- Phosphotyrosine and the PTH/PTHrP receptor immunoreactivity was identified by Western blot analysis. (monash.edu)
Domain2
- Feng, M.-H., Philippopoulos, M., MacKerell, Jr., A.D. and Lim, C. !Structural Characterization of the Phosphotyrosine Binding Region of a !High-Affinity aSH2 Domain-Phosphopeptide Complex by Molecular Dynamics !Simulation and Chemical Shift Calculations. (uiuc.edu)
- We determined the crystal structure of the AICD in complex with the C-terminal phosphotyrosine-binding (PTB) domain of Fe65. (rcsb.org)
Cells1
- Negative regulation of TCR signaling by linker for activation of X cells via phosphotyrosine-dependent and -independent mechanisms. (duke.edu)
Sites1
- The TKD-EGFR displayed chronically elevated basal autophosphorylation at five known phosphotyrosine sites. (elsevier.com)