4.8 Article

iEKPD 2.0: an update with rich annotations for eukaryotic protein kinases, protein phosphatases and proteins containing phosphoprotein-binding domains

期刊

NUCLEIC ACIDS RESEARCH
卷 47, 期 D1, 页码 D344-D350

出版社

OXFORD UNIV PRESS
DOI: 10.1093/nar/gky1063

关键词

-

资金

  1. Special Project on Precision Medicine under the National Key RD Program [2017YFC0906600]
  2. Natural Science Foundation of China [31671360, 31801095, 81701567]
  3. Fundamental Research Funds for the Central Universities [2017KFXKJC001]
  4. National Program for Support of Top-Notch Young Professionals
  5. Changjiang Scholars Program of China
  6. China Postdoctoral Science Foundation [2018M632870]
  7. program for HUST Academic Frontier Youth Team

向作者/读者索取更多资源

Here, we described the updated database iEKPD 2.0 (http://iekpd.biocuckoo.org) for eukaryotic protein kinases (PKs), protein phosphatases (PPs) and proteins containing phosphoprotein-binding domains (PPBDs), which are key molecules responsible for phosphorylation-dependent signalling networks and participate in the regulation of almost all biological processes and pathways. In total, iEKPD 2.0 contained 197 348 phosphorylation regulators, including 109 912 PKs, 23 294 PPs and 68 748 PPBD-containing proteins in 164 eukaryotic species. In particular, we provided rich annotations for the regulators of eight model organisms, especially humans, by compiling and integrating the knowledge from 100 widely used public databases that cover 13 aspects, including cancer mutations, genetic variations, disease-associated information, mRNA expression, DNA & RNA elements, DNA methylation, molecular interactions, drug-target relations, protein 3D structures, post-translational modifications, protein expressions/proteomics, subcellular localizations and protein functional annotations. Compared with our previously developed EKPD 1.0 (approximate to 0.5 GB), iEKPD 2.0 contains approximate to 99.8 GB of data with an approximate to 200-fold increase in data volume. We anticipate that iEKPD 2.0 represents a more useful resource for further study of phosphorylation regulators.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.8
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据