Ceramide kinase profiling by mass spectrometry reveals a conserved phosphorylation pattern downstream of the catalytic site

Journal of Proteome Research

Volumn 9, Issue 1, 2010, Pages 420-429

  Chen, Wei Qiang ^a   Graf, Christine ^d   Zimmel, David ^e   Rovina, Philipp ^f   Krapfenbauer, Kurt ^g   Jaritz, Markus ^h   Parker, Peter J ^b,c   Lubec, Gert ^a   Bornancin, Frédéric ⁱ  

^a MEDICAL UNIVERSITY OF VIENNA   (Austria)

^b IMPERIAL CANCER RESEARCH FUND   (United Kingdom)

^c KING'S COLLEGE LONDON   (United Kingdom)

^d AFFiRiS GmbH   (Austria)

^e CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

^f Roche Diagnostics GmbH   (Austria)

^g EPMA Headquarters   (Belgium)

^h RESEARCH INSTITUTE OF MOLECULAR PATHOLOGY   (Austria)

ⁱ NOVARTIS PHARMA AG   (Switzerland)

Author keywords

Activation loop; Ceramide; Glycine rich loop; Kinase; LC MS; Phosphorylation

Indexed keywords

ADENOSINE TRIPHOSPHATE; CERAMIDE; CERAMIDE 1 PHOSPHATE; CERAMIDE KINASE; MUTANT PROTEIN; SERINE; SPHINGOSINE KINASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME PHOSPHORYLATION; ENZYME REGULATION; MASS SPECTROMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROCESSING;

AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CERCOPITHECUS AETHIOPS; COS CELLS; HUMANS; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; PHOSPHOPROTEINS; PHOSPHORYLATION; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); POINT MUTATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SERINE;

HEXAPODA;

EID: 73649119922     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr900763z     Document Type: Article

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