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qPhos: a database of protein phosphorylation dynamics in humans

Temporal and spatial protein phosphorylation dynamically orchestrates a broad spectrum of biological processes and plays various physiological and pathological roles in diseases and cancers. Recent advancements in high-throughput proteomics techniques greatly promoted the profiling and quantificatio...

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Autores principales: Yu, Kai, Zhang, Qingfeng, Liu, Zekun, Zhao, Qi, Zhang, Xiaolong, Wang, Yan, Wang, Zi-Xian, Jin, Ying, Li, Xiaoxing, Liu, Ze-Xian, Xu, Rui-Hua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6323974/
https://www.ncbi.nlm.nih.gov/pubmed/30380102
http://dx.doi.org/10.1093/nar/gky1052
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author Yu, Kai
Zhang, Qingfeng
Liu, Zekun
Zhao, Qi
Zhang, Xiaolong
Wang, Yan
Wang, Zi-Xian
Jin, Ying
Li, Xiaoxing
Liu, Ze-Xian
Xu, Rui-Hua
author_facet Yu, Kai
Zhang, Qingfeng
Liu, Zekun
Zhao, Qi
Zhang, Xiaolong
Wang, Yan
Wang, Zi-Xian
Jin, Ying
Li, Xiaoxing
Liu, Ze-Xian
Xu, Rui-Hua
author_sort Yu, Kai
collection PubMed
description Temporal and spatial protein phosphorylation dynamically orchestrates a broad spectrum of biological processes and plays various physiological and pathological roles in diseases and cancers. Recent advancements in high-throughput proteomics techniques greatly promoted the profiling and quantification of phosphoproteome. However, although several comprehensive databases have reserved the phosphorylated proteins and sites, a resource for phosphorylation quantification still remains to be constructed. In this study, we developed the qPhos (http://qphos.cancerbio.info) database to integrate and host the data on phosphorylation dynamics. A total of 3 537 533 quantification events for 199 071 non-redundant phosphorylation sites on 18 402 proteins under 484 conditions were collected through exhaustive curation of published literature. The experimental details, including sample materials, conditions and methods, were recorded. Various annotations, such as protein sequence and structure properties, potential upstream kinases and their inhibitors, were systematically integrated and carefully organized to present details about the quantified phosphorylation sites. Various browse and search functions were implemented for the user-defined filtering of samples, conditions and proteins. Furthermore, the qKinAct service was developed to dissect the kinase activity profile from user-submitted quantitative phosphoproteome data through annotating the kinase activity-related phosphorylation sites. Taken together, the qPhos database provides a comprehensive resource for protein phosphorylation dynamics to facilitate related investigations.
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spelling pubmed-63239742019-01-10 qPhos: a database of protein phosphorylation dynamics in humans Yu, Kai Zhang, Qingfeng Liu, Zekun Zhao, Qi Zhang, Xiaolong Wang, Yan Wang, Zi-Xian Jin, Ying Li, Xiaoxing Liu, Ze-Xian Xu, Rui-Hua Nucleic Acids Res Database Issue Temporal and spatial protein phosphorylation dynamically orchestrates a broad spectrum of biological processes and plays various physiological and pathological roles in diseases and cancers. Recent advancements in high-throughput proteomics techniques greatly promoted the profiling and quantification of phosphoproteome. However, although several comprehensive databases have reserved the phosphorylated proteins and sites, a resource for phosphorylation quantification still remains to be constructed. In this study, we developed the qPhos (http://qphos.cancerbio.info) database to integrate and host the data on phosphorylation dynamics. A total of 3 537 533 quantification events for 199 071 non-redundant phosphorylation sites on 18 402 proteins under 484 conditions were collected through exhaustive curation of published literature. The experimental details, including sample materials, conditions and methods, were recorded. Various annotations, such as protein sequence and structure properties, potential upstream kinases and their inhibitors, were systematically integrated and carefully organized to present details about the quantified phosphorylation sites. Various browse and search functions were implemented for the user-defined filtering of samples, conditions and proteins. Furthermore, the qKinAct service was developed to dissect the kinase activity profile from user-submitted quantitative phosphoproteome data through annotating the kinase activity-related phosphorylation sites. Taken together, the qPhos database provides a comprehensive resource for protein phosphorylation dynamics to facilitate related investigations. Oxford University Press 2019-01-08 2018-10-31 /pmc/articles/PMC6323974/ /pubmed/30380102 http://dx.doi.org/10.1093/nar/gky1052 Text en © The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://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
Yu, Kai
Zhang, Qingfeng
Liu, Zekun
Zhao, Qi
Zhang, Xiaolong
Wang, Yan
Wang, Zi-Xian
Jin, Ying
Li, Xiaoxing
Liu, Ze-Xian
Xu, Rui-Hua
qPhos: a database of protein phosphorylation dynamics in humans
title qPhos: a database of protein phosphorylation dynamics in humans
title_full qPhos: a database of protein phosphorylation dynamics in humans
title_fullStr qPhos: a database of protein phosphorylation dynamics in humans
title_full_unstemmed qPhos: a database of protein phosphorylation dynamics in humans
title_short qPhos: a database of protein phosphorylation dynamics in humans
title_sort qphos: a database of protein phosphorylation dynamics in humans
topic Database Issue
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6323974/
https://www.ncbi.nlm.nih.gov/pubmed/30380102
http://dx.doi.org/10.1093/nar/gky1052
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