The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
15 years of PhosphoSitePlus®: integrating post-translationally modified sites, disease variants and isoforms
Open accessAbstract
For 15 years the mission of PhosphoSitePlus® (PSP, https://www.phosphosite.org) has been to provide comprehensive information and tools for the study of mammalian post-translational modifications (PTMs). The number of unique PTMs in PSP is now more than 450 000 from over 22 000 articles and thousands of MS datasets. The most important areas of growth in PSP are in disease and isoform informatics. Germline mutations associated with inherited diseases and somatic cancer mutations have been added to the database and can now be viewed along with PTMs and associated quantitative information on novel 'lollipop' plots. These plots enable researchers to interactively visualize the overlap between disease variants and PTMs, and to identify mutations that may alter phenotypes by rewiring signaling networks. We are expanding the sequence space to include over 30 000 human and mouse isoforms to enable researchers to explore the important but understudied biology of isoforms. This represents a necessary expansion of sequence space to accommodate the growing precision and depth of coverage enabled by ongoing advances in mass spectrometry. Isoforms are aligned using a new algorithm. Exploring the worlds of PTMs and disease mutations in the entire isoform space will hopefully lead to new biomarkers, therapeutic targets, and insights into isoform biology.
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Cites
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“Proteins associated with inherited diseases have been retrieved from ClinVar (16), which lists 3265 proteins with missense mutations that are ‘pathogenic’ or ‘pathogenic/likely pathogenic’ in their July 2018 release.”
BackgroundPhosphoSitePlus, 2014: mutations, PTMs and recalibrations
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Self-citationOncogenic Signaling Pathways in The Cancer Genome Atlas
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Cited by
Post-translational modifications in proteins: resources, tools and prediction methods
Ramazi, S., & Zahiri, J. (2021) · Database · doi:10.1093/database/baab012 · Cited by 772
An atlas of substrate specificities for the human serine/threonine kinome
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Self-citationThe functional landscape of the human phosphoproteome
Ochoa, D., Jarnuczak, A. F., Viéitez, C., Gehre, M., Soucheray, M., Mateus, A., Kleefeldt, A. A., Hill, A., Garcia-Alonso, L., Stein, F., et al. (2020) · Nature Biotechnology · doi:10.1038/s41587-019-0344-3 · Cited by 491
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The intrinsic substrate specificity of the human tyrosine kinome
Yaron-Barir, T. M., Joughin, B. A., Huntsman, E. M., Kerelsky, A., Cizin, D. M., Cohen, B. M., Regev, A., Song, J., Vasan, N., Lin, T.-Y., et al. (2024) · Nature · doi:10.1038/s41586-024-07407-y · Cited by 189
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Metadata
- Authors
- Hornbeck, P. V., Kornhauser, J. M., Latham, V., Murray, B., Nandhikonda, V., Nord, A., Skrzypek, E., Wheeler, T., Zhang, B., & Gnad, F.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2018-11-16
- Volume
- 47
- Issue
- D1
- Pages
- D433-D441
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2901496107
- Cited by
- 346
- References
- 35
- FWCI
- 9.35
- Type
- journal article
- Language
- en
- Open access
- gold
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- Hornbeck, P. V., Kornhauser, J. M., Latham, V., Murray, B., Nandhikonda, V., Nord, A., Skrzypek, E., Wheeler, T., Zhang, B., & Gnad, F. (2019). 15 years of PhosphoSitePlus®: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Research. https://doi.org/10.1093/nar/gky1159
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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
