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利用植物 PTM 查看器探索翻译后修饰。

Exploring Posttranslational Modifications with the Plant PTM Viewer.

机构信息

Department of Plant Biotechnology and Bioinformatics, Ghent University, Ghent, Belgium.

VIB-Center for Plant Systems Biology, Ghent, Belgium.

出版信息

Methods Mol Biol. 2022;2447:285-296. doi: 10.1007/978-1-0716-2079-3_23.

DOI:10.1007/978-1-0716-2079-3_23
PMID:35583790
Abstract

An increasing numbed and diversity of protein posttranslational modifications are mapped by proteomics. Knowledge of modified protein sites can be of direct relevance to steer downstream functional studies, but such information can be difficult to distill from the numerous individual studies that often report modified sites in supplementary data files. In this chapter, we provide basic instructions and use cases to browse and collect plant protein modifications from over 100 studies in a user-friendly manner with the Plant PTM Viewer. The Plant PTM Viewer ( https://www.psb.ugent.be/PlantPTMViewer ) is a central resource compiling currently 24 modifications types for ten thousands of plant proteins. Next to viewing modifications for a protein of interest, we demonstrate how evolutionary conserved modifications can be retrieved using PTM Blast. In addition, modifications themselves located in a motif or sequence context of interest can be retrieved by PTM search. Altogether, these operations can be performed, are intuitive, and open for non-bioinformatic experts.

摘要

蛋白质翻译后修饰的数量和种类不断增加,通过蛋白质组学可以对其进行映射。对修饰蛋白位点的了解可以直接指导下游功能研究,但这些信息很难从经常在补充数据文件中报告修饰位点的众多单独研究中提取出来。在本章中,我们将提供基本说明和用例,以便使用 Plant PTM Viewer 以用户友好的方式从 100 多项研究中浏览和收集植物蛋白修饰。Plant PTM Viewer(https://www.psb.ugent.be/PlantPTMViewer)是一个集中资源,为成千上万的植物蛋白编译了目前 24 种修饰类型。除了查看感兴趣的蛋白质的修饰外,我们还展示了如何使用 PTM Blast 检索进化保守修饰。此外,还可以通过 PTM 搜索检索位于感兴趣的模体或序列上下文内的修饰。总之,这些操作直观且易于操作,即使是非生物信息学专家也可以使用。

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Exploring Posttranslational Modifications with the Plant PTM Viewer.利用植物 PTM 查看器探索翻译后修饰。
Methods Mol Biol. 2022;2447:285-296. doi: 10.1007/978-1-0716-2079-3_23.
2
The Plant PTM Viewer, a central resource for exploring plant protein modifications.植物 PTM 浏览器,探索植物蛋白修饰的核心资源。
Plant J. 2019 Aug;99(4):752-762. doi: 10.1111/tpj.14345. Epub 2019 May 13.
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本文引用的文献

1
Identification of Sulfenylated Cysteines in Proteins Using a Disulfide-Linked Peptide Reporter.使用二硫键连接的肽报告分子鉴定蛋白质中的亚磺酰化半胱氨酸
Front Plant Sci. 2020 Jul 2;11:777. doi: 10.3389/fpls.2020.00777. eCollection 2020.
2
Mass-spectrometry-based draft of the Arabidopsis proteome.基于质谱的拟南芥蛋白质组草图。
Nature. 2020 Mar;579(7799):409-414. doi: 10.1038/s41586-020-2094-2. Epub 2020 Mar 11.
3
Mining for protein S-sulfenylation in uncovers redox-sensitive sites.在蛋白质 S-亚磺化修饰组学中挖掘出了氧化还原敏感位点。
Proc Natl Acad Sci U S A. 2019 Oct 15;116(42):21256-21261. doi: 10.1073/pnas.1906768116. Epub 2019 Oct 2.
4
The Plant PTM Viewer, a central resource for exploring plant protein modifications.植物 PTM 浏览器,探索植物蛋白修饰的核心资源。
Plant J. 2019 Aug;99(4):752-762. doi: 10.1111/tpj.14345. Epub 2019 May 13.
5
InterPro in 2019: improving coverage, classification and access to protein sequence annotations.InterPro 在 2019 年:提高蛋白质序列注释的覆盖范围、分类和访问。
Nucleic Acids Res. 2019 Jan 8;47(D1):D351-D360. doi: 10.1093/nar/gky1100.
6
Elucidating crosstalk mechanisms between phosphorylation and O-GlcNAcylation.阐明磷酸化和 O-连接的 N-乙酰葡萄糖胺糖基化之间的串扰机制。
Proc Natl Acad Sci U S A. 2017 Aug 29;114(35):E7255-E7261. doi: 10.1073/pnas.1620529114. Epub 2017 Aug 14.
7
Araport11: a complete reannotation of the Arabidopsis thaliana reference genome.Araport11:拟南芥参考基因组的完整重新注释。
Plant J. 2017 Feb;89(4):789-804. doi: 10.1111/tpj.13415. Epub 2017 Feb 10.
8
Extracellular peptidase hunting for improvement of protein production in plant cells and roots.寻找用于提高植物细胞和根系中蛋白质产量的细胞外肽酶。
Front Plant Sci. 2015 Feb 6;6:37. doi: 10.3389/fpls.2015.00037. eCollection 2015.
9
An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database.一种将肽的串联质谱数据与蛋白质数据库中氨基酸序列相关联的方法。
J Am Soc Mass Spectrom. 1994 Nov;5(11):976-89. doi: 10.1016/1044-0305(94)80016-2.
10
Family-wide characterization of matrix metalloproteinases from Arabidopsis thaliana reveals their distinct proteolytic activity and cleavage site specificity.对拟南芥基质金属蛋白酶的全家族特征分析揭示了它们独特的蛋白水解活性和裂解位点特异性。
Biochem J. 2014 Jan 15;457(2):335-46. doi: 10.1042/BJ20130196.