ArticleNature communications2021
Spatially interacting phosphorylation sites and mutations in cancer.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The trial behind it
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Who cites it
12 citing papers in PubMed.
- Article
- Mutation impact on mRNA versus protein expression across human cancers.GigaScience · 2025Article
- NAK-associated protein 1/NAP1 activates TBK1 to ensure accurate mitosis and cytokinesis.The Journal of cell biology · 2024Article
- Integrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation.Molecular cancer research : MCR · 2024Article
- Plasminogen missense variants and their involvement in cardiovascular and inflammatory disease.Frontiers in cardiovascular medicine · 2024Review
- VIPpred: a novel model for predicting variant impact on phosphorylation events driving carcinogenesis.Briefings in bioinformatics · 2023Article
- Identification of ZBTB9 as a potential therapeutic target against dysregulation of tumor cells proliferation and a novel biomarker in Liver Hepatocellular Carcinoma.Journal of translational medicine · 2022Article
- Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches.Antioxidants (Basel, Switzerland) · 2022Review
- Monodisperse TiMikrochimica acta · 2022Article
- Cancer proteogenomics: current impact and future prospects.Nature reviews. Cancer · 2022Review
- Proteomic Analyses Identify Therapeutic Targets in Hepatocellular Carcinoma.Frontiers in oncology · 2022Article
- Review
Corrections and comments
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Authors and funding
20 authors.
Funding
Abstract
Advances in mass-spectrometry have generated increasingly large-scale proteomics datasets containing tens of thousands of phosphorylation sites (phosphosites) that require prioritization. We develop a bioinformatics tool called HotPho and systematically discover 3D co-clustering of phosphosites and cancer mutations on protein structures. HotPho identifies 474 such hybrid clusters containing 1255 co-clustering phosphosites, including RET p.S904/Y928, the conserved HRAS/KRAS p.Y96, and IDH1 p.Y139/IDH2 p.Y179 that are adjacent to recurrent mutations on protein structures not found by linear proximity approaches. Hybrid clusters, enriched in histone and kinase domains, frequently include expression-associated mutations experimentally shown as activating and conferring genetic dependency. Approximately 300 co-clustering phosphosites are verified in patient samples of 5 cancer types or previously implicated in cancer, including CTNNB1 p.S29/Y30, EGFR p.S720, MAPK1 p.S142, and PTPN12 p.S275. In summary, systematic 3D clustering analysis highlights nearly 3,000 likely functional mutations and over 1000 cancer phosphosites for downstream investigation and evaluation of potential clinical relevance.
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