Determination of the substrate specificity of protein-tyrosine phosphatase TULA-2 and identification of Syk as a TULA-2 substrate

Journal of Biological Chemistry

Volumn 285, Issue 41, 2010, Pages 31268-31276

  Chen, Xianwen ^a   Ren, Lige ^a   Kim, Soochong ^c   Carpino, Nicholas ^b   Daniel, James L ^c   Kunapuli, Satya P ^c   Tsygankov, Alexander Y ^c   Pei, Dehua ^a  

^a OHIO STATE UNIVERSITY   (United States)

^b STONY BROOK UNIVERSITY   (United States)

^c TEMPLE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; AROMATIC COMPOUNDS; AROMATIZATION; HYDROPHOBICITY; PEPTIDES; PHOSPHATASES; PHOSPHORYLATION; PLATELETS;

ACIDIC RESIDUES; AROMATIC RESIDUES; CLASS I; CLASS II; FOCAL ADHESION KINASE; HYDROPHILIC RESIDUES; HYDROPHOBIC RESIDUES; KINETIC ANALYSIS; KNOCK OUTS; LIBRARY SCREENING; N-TERMINALS; PEPTIDE LIBRARY; PROTEIN-TYROSINE PHOSPHATASE; SUBSTRATE SPECIFICITY; TERMINAL SIDES;

SUBSTRATES;

FOCAL ADHESION KINASE; PEPTIDE LIBRARY; PHOSPHATASE; PROLINE; PROTEIN KINASE SYK; PROTEIN TYROSINE PHOSPHATASE; TULA 1 PROTEIN; TULA 2 PROTEIN; TYROSINE; UNCLASSIFIED DRUG; CD36 ANTIGEN; LYMPHOCYTE ANTIGEN RECEPTOR; PROTEIN TYROSINE KINASE; SIGNAL PEPTIDE; STS-1 PROTEIN, MOUSE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELLULAR DISTRIBUTION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME PHOSPHORYLATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; GENE SILENCING; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; THROMBOCYTE; ANIMAL; CHEMISTRY; ENZYMOLOGY; GENETICS; KINETICS; KNOCKOUT MOUSE; METABOLISM; PEPTIDE LIBRARY; PHYSIOLOGY; THROMBOCYTE ACTIVATION;

ANIMALS; ANTIGENS, CD36; BLOOD PLATELETS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; KINETICS; MICE; MICE, KNOCKOUT; PEPTIDE LIBRARY; PLATELET ACTIVATION; PROTEIN TYROSINE PHOSPHATASES; PROTEIN-TYROSINE KINASES; RECEPTORS, ANTIGEN, T-CELL; SUBSTRATE SPECIFICITY;

EID: 77957758524     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.114181     Document Type: Article

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