ERK1/2 is dephosphorylated by a novel phosphatase - CacyBP/SIP

Biochemical and Biophysical Research Communications

Volumn 404, Issue 1, 2011, Pages 179-183

  Kilanczyk, Ewa ^a   Filipek, Slawomir ^b   Filipek, Anna ^a  

^a NENCKI INSTITUTE OF EXPERIMENTAL BIOLOGY   (Poland)

^b UNIVERSITY OF WARSAW   (Poland)

Author keywords

CacyBP SIP; ERK1 2 kinases; Phosphatase activity; Signaling pathway

Indexed keywords

CACYBP PROTEIN; LYSINE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; OKADAIC ACID; PHENYLALANINE; PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE; SIP PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CELL DIFFERENTIATION; CELL DIVISION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; IC 50; MUTANT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEPHOSPHORYLATION; PROTEIN FUNCTION;

AMINO ACID SEQUENCE; ANIMALS; CALCIUM-BINDING PROTEINS; CELL LINE, TUMOR; MICE; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOGEN-ACTIVATED PROTEIN KINASE 3; MOLECULAR SEQUENCE DATA; PHOSPHORIC MONOESTER HYDROLASES; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY;

EID: 78650904301     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.11.088     Document Type: Article

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