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DataSet Summary

  • HostingRepository: jPOST
  • AnnounceDate: 2017-12-07
  • AnnouncementXML: Submission_2018-02-08_01:57:15.xml
  • DigitalObjectIdentifier:
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Unsupported dataset by repository
  • PrimarySubmitter: Miao-Hsia Lin
  • Title: Widespread protein histidine phosphorylation in bacteria
  • Description: For decades, extreme difficulties in analyzing histidine phosphorylation have limited the study of phosphohistidine signaling. Here we report a method revealing widespread and abundant protein histidine phosphorylation in E. coli. Our new approach generated the largest E. coli phosphoproteome dataset to date, of which a remarkable high percentage (~10%) are phosphohistidine sites. This resource enables a major step forward towards a better understanding of the biological function of histidine phosphorylation.
  • SpeciesList: scientific name: Escherichia coli; NCBI TaxID: 562;
  • ModificationList: iodoacetamide derivatized residue; (2S,3R)-3-hydroxyaspartic acid; L-aspartic 4-phosphoric anhydride
  • Instrument: Q Exactive

Dataset History

VersionDatetimeStatusChangeLog Entry
02017-12-05 05:55:14ID requested
12017-12-07 01:15:53announced
22018-02-08 01:57:16announcedUpdated PubMed.

Publication List

  1. Potel CM, Lin MH, Heck AJR, Lemeer S, Widespread bacterial protein histidine phosphorylation revealed by mass spectrometry-based proteomics. Nat Methods, 15(3):187-190(2018) [pubmed]

Keyword List

  1. submitter keyword: histidine phosphorylation, E. coli, phosphoproteome

Contact List

    Albert J.R. Heck
    • lab head:
    Miao-Hsia Lin
    • contact affiliation: Institute of Chemistry, Academia Sinica
    • dataset submitter:

Full Dataset Link List

  1. jPOST dataset URI
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