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DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2014-07-24
  • AnnouncementXML: Submission_2014-07-24_05:19:45.xml
  • DigitalObjectIdentifier: http://dx.doi.org/10.6019/PXD000783
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Supported dataset by repository
  • PrimarySubmitter: William Slade
  • Title: The Phophoproteome of Chlamydomonas reinhardtii
  • Description: Chlamydomonas reinhardtii is the most intensively-studied and well-developed model for investigation of a wide-range of microalgal processes ranging from basic development through understanding triacylglycerol production. While proteomic technologies permit interrogation of these processes at the protein level and efforts to date indicate phosphorylation-based regulation of proteins in C. reinhardtii is essential for its underlying biology, characterization of the C. reinhardtii phosphoproteome has been limited. Herein, we report the richest exploration of the C. reinhardtii proteome to date. Complementary enrichment strategies were used to detect 4,588 phosphoproteins distributed among every cellular component in C. reinhardtii. Additionally, we report 18,160 unique phosphopeptides at <1% false discovery rate, which comprise 15,862 unique phosphosites – 98% of which are novel. Given that an estimated 30% of proteins in a eukaryotic cell are subject to phosphorylation, we report the majority of the phosphoproteome (23%) of C. reinhardtii. Proteins in key biological pathways were phosphorylated, including photosynthesis, pigment production, carbon assimilation, glycolysis, and protein and carbohydrate metabolism, and it is noteworthy that hyperphosphorylation was observed in flagellar proteins. This rich dataset will significantly enhance understanding of a range of regulatory mechanisms controlling a variety of cellular process and will serve as a critical resource for the microalgal community.
  • SpeciesList: scientific name: Chlamydomonas reinhardtii CC3269; NCBI TaxID: 906914;
  • ModificationList: Oxidation; Phospho; Acetyl; Carbamidomethyl; Deamidated
  • Instrument: LTQ Orbitrap Velos; TripleTOF 5600

Dataset History

VersionDatetimeStatusChangeLog Entry
02014-02-28 15:50:28ID requested
12014-06-11 02:56:36announced
22014-06-24 04:10:33announcedUpdated publication reference for PubMed record(s): 24917610.
32014-07-24 05:19:46announcedUpdated project metadata.

Publication List

  1. Wang H, Gau B, Slade WO, Juergens M, Li P, Hicks LM, The global phosphoproteome of Chlamydomonas reinhardtii reveals complex organellar phosphorylation in the flagella and thylakoid membrane. Mol Cell Proteomics, 13(9):2337-53(2014) [pubmed]

Keyword List

  1. curator keyword: Biological
  2. submitter keyword: algae, chlamydomonas, phosphoproteomics, phosphopeptides

Contact List

    Leslie M. Hicks
    • contact affiliation: University of North Carolina at Chapel Hill, Dept. of Chemistry
    • contact email: lmhicks@unc.edu
    • lab head:
    William Slade
    • contact affiliation: University of North Carolina at Chapel Hill
    • contact email: wslade@email.unc.edu
    • dataset submitter:

Full Dataset Link List

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