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CPLM 4.0: an updated database with rich annotations for protein lysine modifications

Here, we reported the compendium of protein lysine modifications (CPLM 4.0, http://cplm.biocuckoo.cn/), a data resource for various post-translational modifications (PTMs) specifically occurred at the side-chain amino group of lysine residues in proteins. From the literature and public databases, we...

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Detalles Bibliográficos
Autores principales: Zhang, Weizhi, Tan, Xiaodan, Lin, Shaofeng, Gou, Yujie, Han, Cheng, Zhang, Chi, Ning, Wanshan, Wang, Chenwei, Xue, Yu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8728254/
https://www.ncbi.nlm.nih.gov/pubmed/34581824
http://dx.doi.org/10.1093/nar/gkab849
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author Zhang, Weizhi
Tan, Xiaodan
Lin, Shaofeng
Gou, Yujie
Han, Cheng
Zhang, Chi
Ning, Wanshan
Wang, Chenwei
Xue, Yu
author_facet Zhang, Weizhi
Tan, Xiaodan
Lin, Shaofeng
Gou, Yujie
Han, Cheng
Zhang, Chi
Ning, Wanshan
Wang, Chenwei
Xue, Yu
author_sort Zhang, Weizhi
collection PubMed
description Here, we reported the compendium of protein lysine modifications (CPLM 4.0, http://cplm.biocuckoo.cn/), a data resource for various post-translational modifications (PTMs) specifically occurred at the side-chain amino group of lysine residues in proteins. From the literature and public databases, we collected 450 378 protein lysine modification (PLM) events, and combined them with the existing data of our previously developed protein lysine modification database (PLMD 3.0). In total, CPLM 4.0 contained 592 606 experimentally identified modification events on 463 156 unique lysine residues of 105 673 proteins for up to 29 types of PLMs across 219 species. Furthermore, we carefully annotated the data using the knowledge from 102 additional resources that covered 13 aspects, including variation and mutation, disease-associated information, protein-protein interaction, protein functional annotation, DNA & RNA element, protein structure, chemical-target relation, mRNA expression, protein expression/proteomics, subcellular localization, biological pathway annotation, functional domain annotation, and physicochemical property. Compared to PLMD 3.0 and other existing resources, CPLM 4.0 achieved a >2-fold increase in collection of PLM events, with a data volume of ∼45GB. We anticipate that CPLM 4.0 can serve as a more useful database for further study of PLMs.
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spelling pubmed-87282542022-01-05 CPLM 4.0: an updated database with rich annotations for protein lysine modifications Zhang, Weizhi Tan, Xiaodan Lin, Shaofeng Gou, Yujie Han, Cheng Zhang, Chi Ning, Wanshan Wang, Chenwei Xue, Yu Nucleic Acids Res Database Issue Here, we reported the compendium of protein lysine modifications (CPLM 4.0, http://cplm.biocuckoo.cn/), a data resource for various post-translational modifications (PTMs) specifically occurred at the side-chain amino group of lysine residues in proteins. From the literature and public databases, we collected 450 378 protein lysine modification (PLM) events, and combined them with the existing data of our previously developed protein lysine modification database (PLMD 3.0). In total, CPLM 4.0 contained 592 606 experimentally identified modification events on 463 156 unique lysine residues of 105 673 proteins for up to 29 types of PLMs across 219 species. Furthermore, we carefully annotated the data using the knowledge from 102 additional resources that covered 13 aspects, including variation and mutation, disease-associated information, protein-protein interaction, protein functional annotation, DNA & RNA element, protein structure, chemical-target relation, mRNA expression, protein expression/proteomics, subcellular localization, biological pathway annotation, functional domain annotation, and physicochemical property. Compared to PLMD 3.0 and other existing resources, CPLM 4.0 achieved a >2-fold increase in collection of PLM events, with a data volume of ∼45GB. We anticipate that CPLM 4.0 can serve as a more useful database for further study of PLMs. Oxford University Press 2021-09-28 /pmc/articles/PMC8728254/ /pubmed/34581824 http://dx.doi.org/10.1093/nar/gkab849 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Database Issue
Zhang, Weizhi
Tan, Xiaodan
Lin, Shaofeng
Gou, Yujie
Han, Cheng
Zhang, Chi
Ning, Wanshan
Wang, Chenwei
Xue, Yu
CPLM 4.0: an updated database with rich annotations for protein lysine modifications
title CPLM 4.0: an updated database with rich annotations for protein lysine modifications
title_full CPLM 4.0: an updated database with rich annotations for protein lysine modifications
title_fullStr CPLM 4.0: an updated database with rich annotations for protein lysine modifications
title_full_unstemmed CPLM 4.0: an updated database with rich annotations for protein lysine modifications
title_short CPLM 4.0: an updated database with rich annotations for protein lysine modifications
title_sort cplm 4.0: an updated database with rich annotations for protein lysine modifications
topic Database Issue
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8728254/
https://www.ncbi.nlm.nih.gov/pubmed/34581824
http://dx.doi.org/10.1093/nar/gkab849
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