DICP OpenIR
Subject Area物理化学
Global Screening of CK2 Kinase Substrates by an Integrated Phosphoproteomics Workflow
Bian, Yangyang1,2; Ye, Mingliang1; Wang, Chunli1,2; Cheng, Kai1,2; Song, Chunxia1,2; Dong, Mingming1,2; Pan, Yanbo1,2; Qin, Hongqiang1,2; Zou, Hanfa1; Ye ML(叶明亮); Zou HF(邹汉法)
Source PublicationSCIENTIFIC REPORTS
2013-12-10
ISSN2045-2322
DOI10.1038/srep03460
Volume3Pages:03460
Indexed BySCI
Cooperation Status
SubtypeArticle
Department18
Funding Project1809
Contribution Rank待补充
WOS HeadingsScience & Technology
Funding Organization1,1 ; 1,1 ; 1,1 ; 1,1
WOS SubjectMultidisciplinary Sciences
WOS Research AreaScience & Technology - Other Topics
WOS KeywordPROTEIN-PHOSPHORYLATION ; COMPREHENSIVE RESOURCE ; IDENTIFICATION ; SPLICEOSOME ; COMPLEXES ; REVEALS ; ATLAS ; MOUSE ; ASSAY
AbstractDue to its constitutive activity and ubiquitous distribution, CK2 is the most pleiotropic kinase among the individual members of the protein kinase superfamily. Identification of CK2 substrates is vital to decipher its role in biological processes. However, only a limited number of CK2 substrates were identified so far. In this study, we developed an integrated phosphoproteomics workflow to identify the CK2 substrates in large scale. First, in vitro kinase reactions with immobilized proteomes were combined with quantitative phosphoproteomics to identify in vitro CK2 phosphorylation sites, which leaded to identification of 988 sites from 581 protein substrates. To reduce false positives, we proposed an approach by comparing these in vitro sites with the public databases that collect in vivo phosphorylation sites. After the removal of the sites that were excluded in the databases, 605 high confident CK2 sites corresponding to 356 proteins were retained. The CK2 substrates identified in this study were based on the discovery mode, in which an unbiased overview of CK2 substrates was provided. Our result revealed that CK2 substrates were significantly enriched in the spliceosomal proteins, indicating CK2 might regulate the functions of spliceosome.
Language英语
Funding Organization1,1 ; 1,1 ; 1,1 ; 1,1
URL查看原文
WOS IDWOS:000328125600003
Citation statistics
Cited Times:31[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/119581
Collection中国科学院大连化学物理研究所
Corresponding AuthorYe ML(叶明亮); Zou HF(邹汉法)
Affiliation1.Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&A Ctr, Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
Recommended Citation
GB/T 7714
Bian, Yangyang,Ye, Mingliang,Wang, Chunli,et al. Global Screening of CK2 Kinase Substrates by an Integrated Phosphoproteomics Workflow[J]. SCIENTIFIC REPORTS,2013,3:03460.
APA Bian, Yangyang.,Ye, Mingliang.,Wang, Chunli.,Cheng, Kai.,Song, Chunxia.,...&邹汉法.(2013).Global Screening of CK2 Kinase Substrates by an Integrated Phosphoproteomics Workflow.SCIENTIFIC REPORTS,3,03460.
MLA Bian, Yangyang,et al."Global Screening of CK2 Kinase Substrates by an Integrated Phosphoproteomics Workflow".SCIENTIFIC REPORTS 3(2013):03460.
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