Consensus substrate sequence for protein-tyrosine phosphatase receptor type Z

Journal of Biological Chemistry

Volumn 286, Issue 43, 2011, Pages 37137-37146

  Fujikawa, Akihiro ^a   Fukada, Masahide ^a   Makioka, Yoshikazu ^c   Suzuki, Ryoko ^a   Chow, Jeremy Pak Hong ^a,b   Matsumoto, Masahito ^a   Noda, Masaharu ^a,b  

^a NATIONAL INSTITUTE FOR BASIC BIOLOGY   (Japan)

^b GRADUATE UNIVERSITY FOR ADVANCED STUDIES   (Japan)

^c TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC RESIDUES; CATALYTIC DOMAINS; CATALYTIC EFFICIENCIES; CELL-BASED ASSAYS; CELLULAR CONTEXTS; CONSENSUS MOTIF; DEPHOSPHORYLATES; DEPHOSPHORYLATIONS; FLUORESCENT PEPTIDES; GTPASE-ACTIVATING PROTEIN; GUANYLATE KINASE; IN-VITRO; MOLECULAR BASIS; MOTIF SEQUENCE; MULTIPLE SUBSTRATES; PAXILLIN; PHOSPHORYLATION SITES; PHOSPHOTYROSINE; PRIMARY SEQUENCES; PROTEIN-TYROSINE PHOSPHATASE; SIDE-CHAINS; STRUCTURAL DETERMINANTS; SUBSTRATE MOTIFS; SUBSTRATE RECOGNITION;

AMINO ACIDS; PHOSPHATASES; PHOSPHORYLATION; PROTEINS;

SUBSTRATES;

ASPARTIC ACID; G PROTEIN COUPLED RECEPTOR KINASE INTERACTOR 1; GLYCINE; GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE ASSOCIATED GUANYLATE CYCLASE KINASE; PAXILLIN; PROTEIN MAGI1; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE Z; RECEPTOR LIKE PROTEIN TYROSINE PHOSPHATASE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CELL ASSAY; CONTROLLED STUDY; ENZYME SUBSTRATE; FLUORESCENCE ANALYSIS; HUMAN; HUMAN CELL; IN VITRO STUDY; MOLECULAR RECOGNITION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEPHOSPHORYLATION; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; RESIDUE ANALYSIS; SEQUENCE ANALYSIS;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID MOTIFS; ANIMALS; CELL ADHESION MOLECULES, NEURONAL; CELL CYCLE PROTEINS; HEK293 CELLS; HUMANS; PAXILLIN; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; RATS; RECEPTOR-LIKE PROTEIN TYROSINE PHOSPHATASES, CLASS 5; SUBSTRATE SPECIFICITY;

EID: 80054802080     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.270140     Document Type: Article

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