PTMD 2.0: an updated database of disease-associated post-translational modifications

Various post-translational modifications (PTMs) participate in nearly all aspects of biological processes by regulating protein functions, and aberrant states of PTMs are frequently associated with human diseases. Here, we present a comprehensive database of PTMs associated with diseases (PTMD 2.0), including 342 624 PTM-disease associations (PDAs) in 15 105 proteins for 93 types of PTMs and 2083 diseases. Based on the distinct PTM states in diseases, we classified all PDAs into six categories: upregulation (U) or downregulation (D) of PTM levels, absence (A) or presence (P) of PTMs, and creation (C) or disruption (N) of PTM sites. We provided detailed annotations for each PDA and carefully annotated disease-associated proteins by integrating the knowledge from 101 additional resources that covered 13 aspects, including disease-associated information, variation and mutation, protein-protein interaction, protein functional annotation, DNA and RNA element, protein structure, chemical-target relationship, mRNA expression, protein expression/proteomics, subcellular localization, biological pathway annotation, functional domain annotation and physicochemical property. With a data volume of ∼8 GB, we anticipate that PTMD 2.0 will serve as a fundamental resource for further analysing the relationships between PTMs and diseases. The online service of PTMD 2.0 is freely available at https://ptmd.biocuckoo.cn/.

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Publication Details

Journal
Nucleic Acids Research
Published
2024-09-26
DOI
https://doi.org/10.1093/nar/gkae850
Citations
17
Primary Topic
RNA modifications and cancer
Type
article
Field-Weighted Citation Impact
3.97

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article

PTMD 2.0: an updated database of disease-associated post-translational modifications

Miaomiao Chen, Di Peng, Xinhe Huang, Dachao Tang et al.
17 citations
Nucleic Acids Research
RNA modifications and cancer
3.97
article

PTMD 2.0: an updated database of disease-associated post-translational modifications

Miaomiao Chen, Di Peng, Xinhe Huang, Dachao Tang, Yujie Gou, Zihao Feng, Yu Xue, Han Cheng, Dan Liu, Jianzhen Peng
article en
17 citations

Abstract

Various post-translational modifications (PTMs) participate in nearly all aspects of biological processes by regulating protein functions, and aberrant states of PTMs are frequently associated with human diseases. Here, we present a comprehensive database of PTMs associated with diseases (PTMD 2.0), including 342 624 PTM-disease associations (PDAs) in 15 105 proteins for 93 types of PTMs and 2083 diseases. Based on the distinct PTM states in diseases, we classified all PDAs into six categories: upregulation (U) or downregulation (D) of PTM levels, absence (A) or presence (P) of PTMs, and creation (C) or disruption (N) of PTM sites. We provided detailed annotations for each PDA and carefully annotated disease-associated proteins by integrating the knowledge from 101 additional resources that covered 13 aspects, including disease-associated information, variation and mutation, protein-protein interaction, protein functional annotation, DNA and RNA element, protein structure, chemical-target relationship, mRNA expression, protein expression/proteomics, subcellular localization, biological pathway annotation, functional domain annotation and physicochemical property. With a data volume of ∼8 GB, we anticipate that PTMD 2.0 will serve as a fundamental resource for further analysing the relationships between PTMs and diseases. The online service of PTMD 2.0 is freely available at https://ptmd.biocuckoo.cn/.

Nucleic Acids ResearchVol. 53(D1)
Institute of Art (PL), Huazhong University of Science and Technology (CN), Nanjing University (CN)
National Natural Science Foundation of China, National Key Research and Development Program of China
Partnerships for the goals
Openalex Percentile: Top 5%
RNA modifications and cancer
3.97
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