Proteomics

Dataset Information

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N-acetyltransferase A - Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans


ABSTRACT: Not available

INSTRUMENT(S): Q-Tof Premier, instrument model, Agilent instrument model

ORGANISM(S): Homo Sapiens (human) Saccharomyces Cerevisiae (baker's Yeast)

TISSUE(S): Yeast

DISEASE(S): Cervix Carcinoma

SUBMITTER: Petra Van Damme  

PROVIDER: PRD000075 | Pride | 2009-07-28

REPOSITORIES: Pride

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Publications

Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans.

Arnesen Thomas T   Van Damme Petra P   Polevoda Bogdan B   Helsens Kenny K   Evjenth Rune R   Colaert Niklaas N   Varhaug Jan Erik JE   Vandekerckhove Joël J   Lillehaug Johan R JR   Sherman Fred F   Gevaert Kris K  

Proceedings of the National Academy of Sciences of the United States of America 20090506 20


N(alpha)-terminal acetylation is one of the most common protein modifications in eukaryotes. The COmbined FRActional DIagonal Chromatography (COFRADIC) proteomics technology that can be specifically used to isolate N-terminal peptides was used to determine the N-terminal acetylation status of 742 human and 379 yeast protein N termini, representing the largest eukaryotic dataset of N-terminal acetylation. The major N-terminal acetyltransferase (NAT), NatA, acts on subclasses of proteins with Ser-  ...[more]

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