TY - JOUR
T1 - YPIBP
T2 - A repository for phosphoinositide-binding proteins in yeast
AU - Rathod, Jagat
AU - Yen, Han Chen
AU - Liang, Biqing
AU - Tseng, Yan Yuan
AU - Chen, Chien Sheng
AU - Wu, Wei Sheng
N1 - Funding Information:
This work was supported by the Ministry of Science and Technology of Taiwan under Grant No. [MOST 108-2320-B-006-038-MY3] to CSC, [108-2116-M-006-009 and 109-2811-M-006-524] to BL, and [107-2221-E-006-225-MY3 and 108-2628-E-006-004-MY3] to WSW. YYT was supported by NCI RO1 CA204962. CSC also acknowledges funding support in part from the Center of Allergy and Mucosal Immunity, and the Headquarters of University Advancement at National Cheng Kung University, which is sponsored by the Ministry of Education in Taiwan.
Publisher Copyright:
© 2021 The Author(s)
PY - 2021/1
Y1 - 2021/1
N2 - Phosphoinositides (PIs) are a family of eight lipids consisting of phosphatidylinositol (PtdIns) and its seven phosphorylated forms. PIs have important regulatory functions in the cell including lipid signaling, protein transport, and membrane trafficking. Yeast has been recognized as a eukaryotic model system to study lipid-protein interactions. Hundreds of yeast PI-binding proteins have been identified, but this research knowledge remains scattered. Besides, the complete PI-binding spectrum and potential PI-binding domains have not been interlinked. No comprehensive databases are available to support the lipid-protein interaction research on phosphoinositides. Here we constructed the first knowledgebase of Yeast Phosphoinositide-Binding Proteins (YPIBP), a repository consisting of 679 PI-binding proteins collected from high-throughput proteome-array and lipid-array studies, QuickGO, and a rigorous literature mining. The YPIBP also contains protein domain information in categories of lipid-binding domains, lipid-related domains and other domains. The YPIBP provides search and browse modes along with two enrichment analyses (PI-binding enrichment analysis and domain enrichment analysis). An interactive visualization is given to summarize the PI-domain-protein interactome. Finally, three case studies were given to demonstrate the utility of YPIBP. The YPIBP knowledgebase consolidates the present knowledge and provides new insights of the PI-binding proteins by bringing comprehensive and in-depth interaction network of the PI-binding proteins. YPIBP is available at http://cosbi7.ee.ncku.edu.tw/YPIBP/.
AB - Phosphoinositides (PIs) are a family of eight lipids consisting of phosphatidylinositol (PtdIns) and its seven phosphorylated forms. PIs have important regulatory functions in the cell including lipid signaling, protein transport, and membrane trafficking. Yeast has been recognized as a eukaryotic model system to study lipid-protein interactions. Hundreds of yeast PI-binding proteins have been identified, but this research knowledge remains scattered. Besides, the complete PI-binding spectrum and potential PI-binding domains have not been interlinked. No comprehensive databases are available to support the lipid-protein interaction research on phosphoinositides. Here we constructed the first knowledgebase of Yeast Phosphoinositide-Binding Proteins (YPIBP), a repository consisting of 679 PI-binding proteins collected from high-throughput proteome-array and lipid-array studies, QuickGO, and a rigorous literature mining. The YPIBP also contains protein domain information in categories of lipid-binding domains, lipid-related domains and other domains. The YPIBP provides search and browse modes along with two enrichment analyses (PI-binding enrichment analysis and domain enrichment analysis). An interactive visualization is given to summarize the PI-domain-protein interactome. Finally, three case studies were given to demonstrate the utility of YPIBP. The YPIBP knowledgebase consolidates the present knowledge and provides new insights of the PI-binding proteins by bringing comprehensive and in-depth interaction network of the PI-binding proteins. YPIBP is available at http://cosbi7.ee.ncku.edu.tw/YPIBP/.
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U2 - 10.1016/j.csbj.2021.06.035
DO - 10.1016/j.csbj.2021.06.035
M3 - Article
AN - SCOPUS:85116952211
SN - 2001-0370
VL - 19
SP - 3692
EP - 3707
JO - Computational and Structural Biotechnology Journal
JF - Computational and Structural Biotechnology Journal
ER -