Six lysine residues on c-Myc are direct substrates for acetylation by p300

Biochemical and Biophysical Research Communications

Volumn 336, Issue 1, 2005, Pages 274-280

  Zhang, Kangling ^a   Faiola, Francesco ^b   Martinez, Ernest ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Acetylation; c Myc; Histone acetyltransferase; Mass spectrometry; p300

Indexed keywords

HISTONE ACETYLTRANSFERASE; LYSINE; MAX PROTEIN; MYC PROTEIN; PROTEIN; PROTEIN MIZ 1; PROTEIN P300; UNCLASSIFIED DRUG;

ACETYLATION; ARTICLE; ENZYME SUBSTRATE; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DNA BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION;

ACETYLATION; AMINO ACID SEQUENCE; DNA; DNA-BINDING PROTEINS; HUMANS; LYSINE; MOLECULAR SEQUENCE DATA; NUCLEAR PROTEINS; PROTEIN BINDING; PROTO-ONCOGENE PROTEINS C-MYC; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS;

MAMMALIA;

EID: 24344451246     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.075     Document Type: Article

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