ArticleDatabase : the journal of biological databases and curation2014
SysPTM 2.0: an updated systematic resource for post-translational modification.
Article in Database : the journal of biological databases and curation, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- EPSD 2.0: An Updated Database of Protein Phosphorylation Sites Across Eukaryotic Species.Genomics, proteomics & bioinformatics · 2025Article
- Analysis and review of techniques and tools based on machine learning and deep learning for prediction of lysine malonylation sites in protein sequences.Database : the journal of biological databases and curation · 2024Review
- A Review of Machine Learning and Algorithmic Methods for Protein Phosphorylation Site Prediction.Genomics, proteomics & bioinformatics · 2023Review
- Characterization of Proteoform Post-Translational Modifications by Top-Down and Bottom-Up Mass Spectrometry in Conjunction with Annotations.Journal of proteome research · 2023Article
- qPTM: an updated database for PTM dynamics in human, mouse, rat and yeast.Nucleic acids research · 2023Article
- Databases and prospects of dynamic gene regulation in eukaryotes: A mini review.Computational and structural biotechnology journal · 2023Review
- PIM1 promotes hepatic conversion by suppressing reprogramming-induced ferroptosis and cell cycle arrest.Nature communications · 2022Article
- qPTMplants: an integrative database of quantitative post-translational modifications in plants.Nucleic acids research · 2022Article
- Enhancing the Discovery of Functional Post-Translational Modification Sites with Machine Learning Models - Development, Validation, and Interpretation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Integrated omics in Drosophila uncover a circadian kinome.Nature communications · 2020Article
- PRISMOID: a comprehensive 3D structure database for post-translational modifications and mutations with functional impact.Briefings in bioinformatics · 2020Article
- qPhos: a database of protein phosphorylation dynamics in humans.Nucleic acids research · 2019Article
- Sequence analysis of the ATP synthase of subunits (Mitochondrial DNA. Part B, Resources · 2018Article
- Semantic Analysis of Posttranslational Modification of Proteins Accumulated in Thyroid Cancer Cells Exposed to Simulated Microgravity.International journal of molecular sciences · 2018Article
- NTyroSite: Computational Identification of Protein Nitrotyrosine Sites Using Sequence Evolutionary Features.Molecules (Basel, Switzerland) · 2018Article
- Genetic Analysis of Rare Human Variants of Regulators of G Protein Signaling Proteins and Their Role in Human Physiology and Disease.Pharmacological reviews · 2018Review
- Methods and approaches to disease mechanisms using systems kinomics.Synthetic and systems biotechnology · 2018Review
- dbDEPC 3.0: the database of differentially expressed proteins in human cancer with multi-level annotation and drug indication.Database : the journal of biological databases and curation · 2018Article
- In silico re-identification of properties of drug target proteins.BMC bioinformatics · 2017Article
- Phosphoproteome-based kinase activity profiling reveals the critical role of MAP2K2 and PLK1 in neuronal autophagy.Autophagy · 2017Article
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Authors and funding
17 authors.
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Abstract
Post-translational modifications (PTMs) of proteins play essential roles in almost all cellular processes, and are closely related to physiological activity and disease development of living organisms. The development of tandem mass spectrometry (MS/MS) has resulted in a rapid increase of PTMs identified on proteins from different species. The collection and systematic ordering of PTM data should provide invaluable information for understanding cellular processes and signaling pathways regulated by PTMs. For this original purpose we developed SysPTM, a systematic resource installed with comprehensive PTM data and a suite of web tools for annotation of PTMs in 2009. Four years later, there has been a significant advance with the generation of PTM data and, consequently, more sophisticated analysis requirements have to be met. Here we submit an updated version of SysPTM 2.0 (http://lifecenter.sgst.cn/SysPTM/), with almost doubled data content, enhanced web-based analysis tools of PTMBlast, PTMPathway, PTMPhylog, PTMCluster. Moreover, a new session SysPTM-H is constructed to graphically represent the combinatorial histone PTMs and dynamic regulation of histone modifying enzymes, and a new tool PTMGO is added for functional annotation and enrichment analysis. SysPTM 2.0 not only facilitates resourceful annotation of PTM sites but allows systematic investigation of PTM functions by the user. Database URL: http://lifecenter.sgst.cn/SysPTM/.
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