The Saccharomyces cerevisiae poly(A)-binding protein is subject to multiple post-translational modifications, including the methylation of glutamic acid

Biochemical and Biophysical Research Communications

Volumn 443, Issue 2, 2014, Pages 543-548

  Low, Jason K K ^a   Hart Smith, Gene ^a   Erce, Melissa A ^a   Wilkins, Marc R ^a  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

Author keywords

Glutamate methylation; Methylation; Methyltransferase; Poly(A) binding protein; Post translational modification; Saccharomyces cerevisiae

Indexed keywords

AMINO ACID; GLUTAMIC ACID; LYSINE; POLYADENYLIC ACID BINDING PROTEIN; PROTEIN METHYLTRANSFERASE; SERINE;

ACETYLATION; ARTICLE; CONTROLLED STUDY; HUMAN; MOUSE; NONHUMAN; ORTHOLOGY; PRIORITY JOURNAL; PROTEIN METHYLATION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; SACCHAROMYCES CEREVISIAE; SALMONELLA TYPHIMURIUM; YEAST;

EUKARYOTA; SACCHAROMYCES CEREVISIAE; SALMONELLA TYPHIMURIUM;

GLUTAMATE METHYLATION; METHYLATION; METHYLTRANSFERASE; POLY(A) BINDING PROTEIN; POST-TRANSLATIONAL MODIFICATION; SACCHAROMYCES CEREVISIAE;

AMINO ACID SEQUENCE; ANIMALS; CONSERVED SEQUENCE; GLUTAMIC ACID; HUMANS; METHYLATION; MICE; MOLECULAR SEQUENCE DATA; POLY(A)-BINDING PROTEINS; PROTEIN PROCESSING, POST-TRANSLATIONAL; SACCHAROMYCES CEREVISIAE PROTEINS; SPECIES SPECIFICITY;

EID: 84892442404     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.12.009     Document Type: Article

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