Abstract
Sites of ubiquitin modification have been identified by mass spectrometry based on the increase in molecular mass of a tryptic peptide carrying two additional glycine residues from the ubiquitin moiety. However, such peptides with GG shifts have been difficult to discover. We identify 870 unique sites of ubiquitin attachment on 438 different proteins of the yeast Saccharomyces cerevisiae.
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Affinity Labels / metabolism
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Binding Sites
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Cysteine / metabolism
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Histidine / metabolism
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Mass Spectrometry / methods
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Peptides / isolation & purification
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Peptides / metabolism*
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / metabolism
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Ubiquitin / metabolism*
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Ubiquitin-Conjugating Enzymes / metabolism
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Ubiquitination
Substances
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Affinity Labels
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Peptides
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Saccharomyces cerevisiae Proteins
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Ubiquitin
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Histidine
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Ubiquitin-Conjugating Enzymes
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Cysteine