Method of identifying protein phosphorylation modification sites on the basis of tandem mass spectrometry

Abstract

The invention provides a method of identifying protein phosphorylation modification sites on the basis of tandem mass spectrometry. According to the method, application result data is searched by tandem mass spectrometry MGF-formatted (mascot generic file-formatted) data and mascot and pFind databases; programming is performed by a Perl language program; identified protein phosphorylation modification sites are re-located fast; and the re-located protein phosphorylation modification sites are calculated by a new scoring algorithm. The method is more creditable and also allows for fast automatic batch exporting of mass spectrograms related to the protein phosphorylation modification sites. The method has the advantages that operation is simple, locating information of the modification sites is highly creditable and the extracted mass spectrograms are high in resolution. The method is well applicable to the field of proteomics study.

Description

technical field [0001] The invention relates to the field of biological information, in particular to a method for identifying protein phosphorylation modification sites based on tandem mass spectrometry. Background technique [0002] Protein phosphorylation is the most common and important post-translational modification of proteins in the biological world. In cells, approximately one-third of proteins are thought to be phosphorylated. The reversible process of protein phosphorylation and dephosphorylation is a key link in the expression regulation of prokaryotic and eukaryotic cells, almost regulating cell proliferation, development, differentiation signal transduction, apoptosis, neural activity, muscle contraction and tumor Reversible protein phosphorylation is the most important signal transfer method known so far. Therefore, the analysis of protein phosphorylation and the identification of phosphorylation sites have become the concerns of many biochemists and proteom...

AI Technical Summary

Problems solved by technology

Currently, software for protein phosphorylation site modification site evaluation includes PTMScore, Ascore, and PhosphoRS in MaxQuant, but these software have relatively high limitations and are only applicable to data generated by specific mass spectrometry instruments and specific database search programs, such as PTMScore and PhosphoRS in MaxQuant are only used for a series of mass spectrometers from Thermo, and Ascore is only compatible with the search results of the Sequest database; in addition, based on the PTMScore algorithm in MaxQuant, some modification site positioning methods have also been developed, such as literature Ming-kun Yang, Zhi -xian Qiao, Wan-yi Zhang, Qian Xiong, Jia Zhang, Tao Li, Feng Ge and Jin-dong Zhao, “Global Phosphoproteomic Analysis Reveals Diverse Functions of Serine / Threonine / Tyrosine Phosphorylation in the Model Cyanobacterium Synechococcus sp.Strain PCC7002” ,J.Proteome.Res,2013,12(4),1909-1923. The PTMScore algorithm used in the evaluation of the phosphorylation site, but this method is only compatible with Bruker mass spectrometry data

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