AI Chat Paper
Note: Please note that the following content is generated by AMiner AI. SciOpen does not take any responsibility related to this content.
{{lang === 'zh_CN' ? '文章概述' : 'Summary'}}
{{lang === 'en_US' ? '中' : 'Eng'}}
Chat more with AI
PDF (4.1 MB)
Collect
Submit Manuscript AI Chat Paper
Show Outline
Outline
Show full outline
Hide outline
Outline
Show full outline
Hide outline
Protocol | Open Access

A protocol of using PTMiner for quality control and localization of protein modifications identified by open or closed search of tandem mass spectra

Zhiyuan Cheng1,4Ge Song2,3Yan Fu1,4( )
Academy of Mathematics and Systems Science, Chinese Academy of Sciences, Beijing 100190, China
Graduate School of Peking Union Medical College, Beijing 100730, China
National Institute of Biological Sciences, Beijing, Beijing 102206, China
School of Mathematical Sciences, University of Chinese Academy of Sciences, Beijing 100049, China
Show Author Information

Graphical Abstract

Abstract

In recent years, an open search of tandem mass spectra has greatly promoted the detection of post-translational modifications (PTMs) in shotgun proteomics. However, post-processing of the results from open searches remains an unsatisfactorily resolved problem, which hinders the open search mode from wide practical use. PTMiner is a software tool based on dedicated statistical algorithms for reliable filtering, localization and annotation of the modifications (mass shifts) detected by open search. Furthermore, PTMiner also supports quality control and re-localization of modifications identified by the traditional closed search. In this protocol, we describe how to use PTMiner for the two search modes. Currently, the search engines supported by PTMiner include pFind, MSFragger, MaxQuant, Comet, MS-GF + and SEQUEST.

References

 

Aebersold R, Mann M (2016) Mass-spectrometric exploration of proteome structure and function. Nature 537(7620): 347−355

 
An Z, Gong F, Fu Y (2018) Unrestrictive protein modification localization and quality control for open search of mass spectra. ChemRxiv. 10.26434/chemrxiv. 5797995. v1
 

An ZW, Zhai LH, Ying WT, Qian XH, Gong FZ, Tan MJ, Fu Y (2019) PTMiner: localization and quality control of protein modifications detected in an open search and its application to comprehensive post-translational modification characterization in human proteome. Mol Cell Proteomics 18(2): 391−405

 

Chambers MC, Maclean B, Burke R, Amodei D, Ruderman DL, Neumann S, Gatto L, Fischer B, Pratt B, Egertson J, Hoff K, Kessner D, Tasman N, Shulman N, Frewen B, Baker TA, Brusniak MY, Paulse C, Creasy D, Flashner L, Kani K, Moulding C, Seymour SL, Nuwaysir LM, Lefebvre B, Kuhlmann F, Roark J, Rainer P, Detlev S, Hemenway T, Huhmer A, Langridge J, Connolly B, Chadick T, Holly K, Eckels J, Deutsch EW, Moritz RL, Katz JE, Agus DB, MacCoss M, Tabb DL, Mallick P (2012) A cross-platform toolkit for mass spectrometry and proteomics. Nat Biotechnol 30(10): 918−920

 

Chi H, Liu C, Yang H, Zeng W-F, Wu L, Zhou W-J, Wang R-M, Niu X-N, Ding Y-H, Zhang Y (2018) Comprehensive identification of peptides in tandem mass spectra using an efficient open search engine. Nat Biotechnol 36(11): 1059−1061

 

Fu Y (2016) Data analysis strategies for protein modification identification. Methods Mol Biol 1362: 265−275

 

Fu Y, Qian X (2014) Transferred subgroup false discovery rate for rare post-translational modifications detected by mass spectrometry. Mol Cell Proteomics 13(5): 1359−1368

 
He K, Fu Y, Zeng W-F, Luo L, Chi H, Liu C, Qing L-Y, Sun R-X, He S-M (2015) A theoretical foundation of the target-decoy search strategy for false discovery rate control in proteomics. arXiv. 10.48550/arXiv. 1501.00537
 

Kong AT, Leprevost FV, Avtonomov DM, Mellacheruvu D, Nesvizhskii AI (2017) MSFragger: ultrafast and comprehensive peptide identification in mass spectrometry–based proteomics. Nat Methods 14(5): 513−520

 

Pevzner PA, Dancik V, Tang CL (2000) Mutation-tolerant protein identification by mass spectrometry. J Comput Biol 7(6): 777−787

 

Yates JR, Eng JK, Mccormack AL, Schieltz D (1995) Method to correlate tandem mass-spectra of modified peptides to amino-acid-sequences in the protein database. Anal Chem 67(8): 1426−1436

Biophysics Reports
Pages 269-281
Cite this article:
Cheng Z, Song G, Fu Y. A protocol of using PTMiner for quality control and localization of protein modifications identified by open or closed search of tandem mass spectra. Biophysics Reports, 2022, 8(5-6): 269-281. https://doi.org/10.52601/bpr.2022.220024

253

Views

6

Downloads

0

Crossref

0

Scopus

0

CSCD

Altmetrics

Received: 23 September 2022
Accepted: 07 November 2022
Published: 04 April 2023
© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

Return