5.9
CiteScore
5.9
Impact Factor
Volume 45 Issue 7
Jul.  2018
Turn off MathJax
Article Contents

PhoPepMass: A database and search tool assisting human phosphorylation peptide identification from mass spectrometry data

doi: 10.1016/j.jgg.2018.07.005
More Information
  • Protein phosphorylation, one of the most important protein post-translational modifications, is involved in various biological processes, and the identification of phosphorylation peptides (phosphopeptides) and their corresponding phosphorylation sites (phosphosites) will facilitate the understanding of the molecular mechanism and function of phosphorylation. Mass spectrometry (MS) provides a high-throughput technology that enables the identification of large numbers of phosphosites. PhoPepMass is designed to assist human phosphopeptide identification from MS data based on a specific database of phophopeptide masses and a multivariate hypergeometric matching algorithm. It contains 244,915 phosphosites from several public sources. Moreover, the accurate masses of peptides and fragments with phosphosites were calculated. It is the first database that provides a systematic resource for the query of phosphosites on peptides and their corresponding masses. This allows researchers to search certain proteins of which phosphosites have been reported, to browse detailed phosphopeptide and fragment information, to match masses from MS analyses with defined threshold to the corresponding phosphopeptide, and to compare proprietary phosphopeptide discovery results with results from previous studies. Additionally, a database search software is created and a “two-stage search strategy” is suggested to identify phosphopeptides from tandem mass spectra of proteomics data. We expect PhoPepMass to be a useful tool and a source of reference for proteomics researchers. PhoPepMass is available at https://www.scbit.org/phopepmass/index.html.
  • These authors contributed equally to this work.
  • loading
  • [1]
    Bern, M., Cai, Y., Goldberg, D. Anal. Chem., 79 (2007),pp. 1393-1400
    [2]
    Boeckmann, B., Bairoch, A., Apweiler, R. et al. The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003 Nucleic Acids Res., 31 (2003),pp. 365-370
    [3]
    Breitkreutz, A., Choi, H., Sharom, J.R. et al. A global protein kinase and phosphatase interaction network in yeast Science, 328 (2010),pp. 1043-1046
    [4]
    Chamrad, D.C., Korting, G., Stuhler, K. et al. Evaluation of algorithms for protein identification from sequence databases using mass spectrometry data Proteomics, 4 (2004),pp. 619-628
    [5]
    Cohen, P. The regulation of protein function by multisite phosphorylation--a 25 year update Trends Biochem. Sci., 25 (2000),pp. 596-601
    [6]
    Craig, R., Beavis, R.C. A method for reducing the time required to match protein sequences with tandem mass spectra Rapid Commun. Mass Spectrom., 17 (2003),pp. 2310-2316
    [7]
    Craig, R., Beavis, R.C. TANDEM: matching proteins with tandem mass spectra Bioinformatics, 20 (2004),pp. 1466-1467
    [8]
    Creasy, D.M., Cottrell, J.S. Error tolerant searching of uninterpreted tandem mass spectrometry data Proteomics, 2 (2002),pp. 1426-1434
    [9]
    Deutsch, E.W., Mendoza, L., Shteynberg, D. et al. Trans-Proteomic Pipeline, a standardized data processing pipeline for large-scale reproducible proteomics informatics Proteonomics Clin. Appl., 9 (2015),pp. 745-754
    [10]
    Diella, F., Gould, C.M., Chica, C. et al. Phospho.ELM: a database of phosphorylation sites--update 2008 Nucleic Acids Res., 36 (2008),pp. D240-D244
    [11]
    Eickner, T., Mikkat, S., Lorenz, P. et al. EJMS protocol: systematic studies on TiO2-based phosphopeptide enrichment procedures upon in-solution and in-gel digestions of proteins. Are there readily applicable protocols suitable for matrix-assisted laser desorption/ionization mass spectrometry-based phosphopeptide stability estimations? Eur. J. Mass Spectrom., 17 (2011),pp. 507-523
    [12]
    Eng, J.K., McCormack, A.L., Yates, J.R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database J. Am. Soc. Mass Spectrom., 5 (1994),pp. 976-989
    [13]
    Geer, L.Y., Markey, S.P., Kowalak, J.A. et al. Open mass spectrometry search algorithm J. Proteome Res., 3 (2004),pp. 958-964
    [14]
    Hornbeck, P.V., Kornhauser, J.M., Tkachev, S. et al. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse Nucleic Acids Res., 40 (2012),pp. D261-D270
    [15]
    Huang, K.Y., Su, M.G., Kao, H.J. et al. dbPTM 2016: 10-year anniversary of a resource for post-translational modification of proteins Nucleic Acids Res., 44 (2016),pp. D435-D446
    [16]
    Keshava Prasad, T.S., Goel, R., Kandasamy, K. et al. Human protein reference Database--2009 update Nucleic Acids Res., 37 (2009),pp. D767-D772
    [17]
    Li, J., Jia, J., Li, H. et al. SysPTM 2.0: an updated systematic resource for post-translational modification Database (Oxford), 2014 (2014)
    [18]
    McHugh, L., Arthur, J.W. Computational methods for protein identification from mass spectrometry data PLoS Comput. Biol., 4 (2008),p. e12
    [19]
    Paradela, A., Albar, J.P. Advances in the analysis of protein phosphorylation J. Proteome Res., 7 (2008),pp. 1809-1818
    [20]
    Perkins, D.N., Pappin, D.J., Creasy, D.M. et al. Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis, 20 (1999),pp. 3551-3567
    [21]
    Ren, L., Li, C., Shao, W. et al. TiO2 with Tandem Fractionation (TAFT): an approach for rapid, deep, reproducible, and high-throughput phosphoproteome analysis J. Proteome Res., 17 (2018),pp. 710-721
    [22]
    Riley, N.M., Coon, J.J. Phosphoproteomics in the age of rapid and deep proteome profiling Anal. Chem., 88 (2016),pp. 74-94
    [23]
    Salazar, C., Hofer, T. Multisite protein phosphorylation--from molecular mechanisms to kinetic models FEBS J., 276 (2009),pp. 3177-3198
    [24]
    Tabb, D.L., Fernando, C.G., Chambers, M.C. MyriMatch: highly accurate tandem mass spectral peptide identification by multivariate hypergeometric analysis J. Proteome Res., 6 (2007),pp. 654-661
    [25]
    Yefremova, Y., Al-Majdoub, M., Opuni, K.F. et al. J. Am. Soc. Mass Spectrom., 26 (2015),pp. 482-492
    [26]
    Zerbino, D.R., Achuthan, P., Akanni, W. et al. Ensembl 2018 Nucleic Acids Res., 46 (2018),pp. D754-d761
    [27]
    Zhang, M., Li, H., He, Y. et al. Construction and deciphering of human phosphorylation-mediated signaling transduction networks J. Proteome Res., 14 (2015),pp. 2745-2757
  • 加载中

Catalog

    通讯作者: 陈斌, bchen63@163.com
    • 1. 

      沈阳化工大学材料科学与工程学院 沈阳 110142

    1. 本站搜索
    2. 百度学术搜索
    3. 万方数据库搜索
    4. CNKI搜索

    Article Metrics

    Article views (87) PDF downloads (3) Cited by ()
    Proportional views
    Related

    /

    DownLoad:  Full-Size Img  PowerPoint
    Return
    Return