دورية أكاديمية

YPIBP: A repository for phosphoinositide-binding proteins in yeast.

التفاصيل البيبلوغرافية
العنوان: YPIBP: A repository for phosphoinositide-binding proteins in yeast.
المؤلفون: Rathod J; Department of Earth Sciences, College of Sciences, National Cheng Kung University, Tainan 701, Taiwan., Yen HC; Department of Electrical Engineering, College of Electrical Engineering and Computer Science, National Cheng Kung University, Tainan 701, Taiwan., Liang B; Department of Earth Sciences, College of Sciences, National Cheng Kung University, Tainan 701, Taiwan., Tseng YY; Center for Molecular Medicine and Genetics, Wayne State University, School of Medicine, Detroit, MI 48201, USA., Chen CS; Department of Food Safety/Hygiene and Risk Management, College of Medicine, National Cheng Kung University, Tainan 701, Taiwan.; Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan 701, Taiwan., Wu WS; Department of Electrical Engineering, College of Electrical Engineering and Computer Science, National Cheng Kung University, Tainan 701, Taiwan.
المصدر: Computational and structural biotechnology journal [Comput Struct Biotechnol J] 2021 Jun 24; Vol. 19, pp. 3692-3707. Date of Electronic Publication: 2021 Jun 24 (Print Publication: 2021).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology Country of Publication: Netherlands NLM ID: 101585369 Publication Model: eCollection Cited Medium: Print ISSN: 2001-0370 (Print) Linking ISSN: 20010370 NLM ISO Abbreviation: Comput Struct Biotechnol J Subsets: PubMed not MEDLINE
أسماء مطبوعة: Publication: Amsterdam : Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology
Original Publication: Gothenburg, Sweden : Research Network of Computational and Structural Biotechnology
مستخلص: 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/.
Competing Interests: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(© 2021 The Author(s).)
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معلومات مُعتمدة: R01 CA204962 United States CA NCI NIH HHS
فهرسة مساهمة: Keywords: ANTH, AP180 N-terminal Homology; BAR, Bin-Amphiphysin-Rvs; CAFA, Critical Assessment of Functional Annotation; CRAL-TRIO, cellular retinaldehyde-binding protein (CRALBP) and TRIO guanine exchange factor; Cvt, Cytoplasm-to-vacuole targeting; ENTH, Epsin N-terminal Homology; FDR, False Discovery Rate; FYVE, Fab 1 (yeast orthologue of PIKfyve), YOTB, Vac 1 (vesicle transport protein), and EEA1; GO, Gene Ontology; ITC, Isothermal Titration Calorimetry; LBD, Lipid-Binding Domain; LMPD, LIPID MAPS Proteome Database; LMSD, LIPID MAPS Structure Database; LRD, Lipid-Related Domain; Lipid-binding domain; OMIM, Online Mendelian Inheritance in Man; OSBP, Oxysterol-Binding Protein; PH, Pleckstrin Homology; PI(3,4)P2, phosphatidylinositol-3,4-bisphosphate; PI(3,4,5)P3, phosphatidylinositol-3,4,5-trisphosphate; PI(3,5)P2, phosphatidylinositol-3,5-bisphosphate; PI(4,5)P2, phosphatidylinositol-4,5-bisphosphate; PI-binding protein; PI3P, phosphatidylinositol-3-phosphate; PI4P, phosphatidylinositol-4-phosphate; PI5P, phosphatidylinositol-5-phosphate; PIs, Phosphoinositides; PMID, PubMed ID; PX, Phox Homology; Phosphatidylinositol (PtdIns); Phosphoinositides (PIs); PtdIns, Phosphatidylinositol; QCM, Quartz Crystal Microbalance; S. cerevisiae; SNX, Sorting Nexin; SPR, Surface Plasmon Resonance; YPIBP, Yeast Phosphoinositide-Binding Proteins; Yeast
تواريخ الأحداث: Date Created: 20210721 Latest Revision: 20240505
رمز التحديث: 20240505
مُعرف محوري في PubMed: PMC8261538
DOI: 10.1016/j.csbj.2021.06.035
PMID: 34285772
قاعدة البيانات: MEDLINE
الوصف
تدمد:2001-0370
DOI:10.1016/j.csbj.2021.06.035