Proteomics

Dataset Information

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Lysine propionylation is a prevalent post-translational modification in Thermus thermophilus


ABSTRACT: Immunoaffinity purification with anti-propionyllysine antibody and nanoLC-MS/MS analysis

INSTRUMENT(S): Bruker Daltonics micrOTOF series, micrOTOF-Q II

ORGANISM(S): Thermus Thermophilus (strain Hb8 / Atcc 27634 / Dsm 579)

TISSUE(S): Myeloid Cell Line

SUBMITTER: Kwang Kim  

LAB HEAD: Seiki Kuramitsu

PROVIDER: PXD000544 | Pride | 2019-11-28

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
LS_A1_4727.baf Other
LS_A1_4727.dat Other
LS_A2_4731.baf Other
LS_A2_4731.dat Other
LS_A3_4815.baf Other
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Publications

Lysine propionylation is a prevalent post-translational modification in Thermus thermophilus.

Okanishi Hiroki H   Kim Kwang K   Masui Ryoji R   Kuramitsu Seiki S  

Molecular & cellular proteomics : MCP 20140617 9


Recent studies of protein post-translational modifications revealed that various types of lysine acylation occur in eukaryotic and bacterial proteins. Lysine propionylation, a newly discovered type of acylation, occurs in several proteins, including some histones. In this study, we identified 361 propionylation sites in 183 mid-exponential phase and late stationary phase proteins from Thermus thermophilus HB8, an extremely thermophilic eubacterium. Functional classification of the propionylprote  ...[more]

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