Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database
By George A. Khoury, Richard C. Baliban, Christodoulos A. Floudas. Scientific Reports, 2011
915 citations recorded by the source corpus.
Post-translational modifications (PTMs) broadly contribute to the recent explosion of proteomic data and possess a complexity surpassing that of protein design. PTMs are the chemical modification of a protein after its translation, and have wide effects broadening its range of functionality. Based on previous estimates, it is widely believed that more than half of proteins are glycoproteins. Whereas mutations can only occur once per position, different forms of post-translational modifications may occur in tandem. With the number and abundances of modifications constantly being discovered, there is no method to readily assess their relative levels. Here we report the relative abundances of each PTM found experimentally and putatively, from high-quality, manually curated, proteome-wide data, and show that at best, less than one-fifth of proteins are glycosylated. We make available to the academic community a continuously updated resource (http://selene.princeton.edu/PTMCuration) containing the statistics so scientists can assess “how many” of each PTM exists.
Subfields: Molecular Biology, Spectroscopy
View Paper: https://www.semanticscholar.org/paper/93c26f2bf00c00653fc814221b5a03e985c38a0b
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In Molecular Biology
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In Spectroscopy
Citations in the corpus
- Post-translational modifications in proteins: resources, tools and prediction methods (2021, background): “There are more than 400 different types of PTMs (27) affecting many aspects of protein functions.”
- Post-Translational Modifications That Drive Prostate Cancer Progression (2021, background): “As such, targeting PTMs offers the opportunity to interfere with crucial events in cancer biology as depicted on Figure 2.”
- Systematic exploration of ubiquitin sequence, E1 activation efficiency, and experimental fitness in yeast (2014, background): “…we propose that E1 can discriminately activate ubiquitin protein molecules that are capable of binding to other partners from the pool of ubiquitin protein in cells that will include molecules with synthetic errors 60 and/or chemical damage (e.g. deamination of glutamine to glutamate) 61 (Fig.”
- The Roles of Post-translational Modifications in the Context of Protein Interaction Networks (2015, background): “Several databases have been established to store the obtained information, such as UniProt [8], dbPTM [9], PTMCuration [10], PTMcode [11] and many others.”
- 15 years of PhosphoSitePlus®: integrating post-translationally modified sites, disease variants and isoforms (2018, background): “While there are over 400 known PTMs (3), the major classes of modifications that are curated into PSP include those that are most widely studied in the regulation of intracellular signaling: phosphorylation of serine, threonine and tyrosine; ubiquitylation and ubiquitin-like modifications of lysine;”