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PTMint database of experimentally verified PTM regulation on protein–protein interaction
MOTIVATION: Post-translational modification (PTM) is an important biochemical process. which includes six most well-studied types: phosphorylation, acetylation, methylation, sumoylation, ubiquitylation and glycosylation. PTM is involved in various cell signaling pathways and biological processes. Ab...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9848059/ https://www.ncbi.nlm.nih.gov/pubmed/36548389 http://dx.doi.org/10.1093/bioinformatics/btac823 |
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author | Hong, Xiaokun Li, Ningshan Lv, Jiyang Zhang, Yan Li, Jing Zhang, Jian Chen, Hai-Feng |
author_facet | Hong, Xiaokun Li, Ningshan Lv, Jiyang Zhang, Yan Li, Jing Zhang, Jian Chen, Hai-Feng |
author_sort | Hong, Xiaokun |
collection | PubMed |
description | MOTIVATION: Post-translational modification (PTM) is an important biochemical process. which includes six most well-studied types: phosphorylation, acetylation, methylation, sumoylation, ubiquitylation and glycosylation. PTM is involved in various cell signaling pathways and biological processes. Abnormal PTM status is closely associated with severe diseases (such as cancer and neurologic diseases) by regulating protein functions, such as protein–protein interactions (PPIs). A set of databases was constructed separately for PTM sites and PPI; however, the resource of regulation for PTM on PPI is still unsolved. RESULTS: Here, we firstly constructed a public accessible database of PTMint (PTMs that are associated with PPIs) (https://ptmint.sjtu.edu.cn/) that contains manually curated complete experimental evidence of the PTM regulation on PPIs in multiple organisms, including Homo sapiens, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Saccharomyces cerevisiae and Schizosaccharomyces pombe. Currently, the first version of PTMint encompassed 2477 non-redundant PTM sites in 1169 proteins affecting 2371 protein–protein pairs involving 357 diseases. Various annotations were systematically integrated, such as protein sequence, structure properties and protein complex analysis. PTMint database can help to insight into disease mechanism, disease diagnosis and drug discovery associated with PTM and PPI. AVAILABILITY AND IMPLEMENTATION: PTMint is freely available at: https://ptmint.sjtu.edu.cn/. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online. |
format | Online Article Text |
id | pubmed-9848059 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-98480592023-01-20 PTMint database of experimentally verified PTM regulation on protein–protein interaction Hong, Xiaokun Li, Ningshan Lv, Jiyang Zhang, Yan Li, Jing Zhang, Jian Chen, Hai-Feng Bioinformatics Original Paper MOTIVATION: Post-translational modification (PTM) is an important biochemical process. which includes six most well-studied types: phosphorylation, acetylation, methylation, sumoylation, ubiquitylation and glycosylation. PTM is involved in various cell signaling pathways and biological processes. Abnormal PTM status is closely associated with severe diseases (such as cancer and neurologic diseases) by regulating protein functions, such as protein–protein interactions (PPIs). A set of databases was constructed separately for PTM sites and PPI; however, the resource of regulation for PTM on PPI is still unsolved. RESULTS: Here, we firstly constructed a public accessible database of PTMint (PTMs that are associated with PPIs) (https://ptmint.sjtu.edu.cn/) that contains manually curated complete experimental evidence of the PTM regulation on PPIs in multiple organisms, including Homo sapiens, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Saccharomyces cerevisiae and Schizosaccharomyces pombe. Currently, the first version of PTMint encompassed 2477 non-redundant PTM sites in 1169 proteins affecting 2371 protein–protein pairs involving 357 diseases. Various annotations were systematically integrated, such as protein sequence, structure properties and protein complex analysis. PTMint database can help to insight into disease mechanism, disease diagnosis and drug discovery associated with PTM and PPI. AVAILABILITY AND IMPLEMENTATION: PTMint is freely available at: https://ptmint.sjtu.edu.cn/. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online. Oxford University Press 2022-12-22 /pmc/articles/PMC9848059/ /pubmed/36548389 http://dx.doi.org/10.1093/bioinformatics/btac823 Text en © The Author(s) 2022. Published by Oxford University Press. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Paper Hong, Xiaokun Li, Ningshan Lv, Jiyang Zhang, Yan Li, Jing Zhang, Jian Chen, Hai-Feng PTMint database of experimentally verified PTM regulation on protein–protein interaction |
title | PTMint database of experimentally verified PTM regulation on protein–protein interaction |
title_full | PTMint database of experimentally verified PTM regulation on protein–protein interaction |
title_fullStr | PTMint database of experimentally verified PTM regulation on protein–protein interaction |
title_full_unstemmed | PTMint database of experimentally verified PTM regulation on protein–protein interaction |
title_short | PTMint database of experimentally verified PTM regulation on protein–protein interaction |
title_sort | ptmint database of experimentally verified ptm regulation on protein–protein interaction |
topic | Original Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9848059/ https://www.ncbi.nlm.nih.gov/pubmed/36548389 http://dx.doi.org/10.1093/bioinformatics/btac823 |
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