4月14日,，國(guó)際知名學(xué)術(shù)刊物《分子與細(xì)胞蛋白質(zhì)組學(xué)》（Molecular and Cellular Proteomics）在線發(fā)表了中科院系統(tǒng)生物學(xué)重點(diǎn)實(shí)驗(yàn)室的一項(xiàng)研究成果,，該工作開發(fā)了一個(gè)系統(tǒng)的蛋白質(zhì)翻譯后修飾數(shù)據(jù)在線分析平臺(tái)-SysPTM,。
蛋白質(zhì)翻譯后修飾，是調(diào)節(jié)蛋白質(zhì)生物學(xué)功能的關(guān)鍵步驟之一,。更重要的是，在一個(gè)生物系統(tǒng)中,，往往有多種修飾同時(shí)協(xié)同發(fā)揮作用,。近年來(lái),，高靈敏度,、高準(zhǔn)確性和高通量的質(zhì)譜分析實(shí)現(xiàn)了對(duì)蛋白質(zhì)翻譯后修飾的大規(guī)模鑒定,，大大擴(kuò)展了實(shí)驗(yàn)確認(rèn)的蛋白質(zhì)翻譯后修飾種類和數(shù)量。
中科院系統(tǒng)生物學(xué)重點(diǎn)實(shí)驗(yàn)室博士生李虹和邢曉斌在李亦學(xué)研究員和曾嶸研究員,，以及謝鷺副研究員的共同指導(dǎo)下,，開發(fā)了一個(gè)系統(tǒng)的蛋白質(zhì)翻譯后修飾研究數(shù)據(jù)平臺(tái),。該平臺(tái)首先將分散在公共數(shù)據(jù)庫(kù)和文獻(xiàn)中的實(shí)驗(yàn)鑒定的多種蛋白質(zhì)翻譯后修飾信息整合,，建立了一個(gè)目前最完整的蛋白質(zhì)翻譯后修飾數(shù)據(jù)庫(kù)，包括了近50種修飾類型,，33421個(gè)蛋白質(zhì)上的117349個(gè)修飾位點(diǎn)。在此數(shù)據(jù)基礎(chǔ)上,，SysPTM又開發(fā)了四個(gè)在線工具（PTMBlast,，PTMPathway，PTMPhylog,，PTMCluster）,，用戶可以在線分析和比較各種翻譯后修飾的功能和保守性等性質(zhì)。該數(shù)據(jù)庫(kù)為深入分析蛋白質(zhì)翻譯后修飾奠定了基礎(chǔ),，在線工具也為解析高通量蛋白質(zhì)修飾數(shù)據(jù)提供了有力支持,。
該項(xiàng)工作得到國(guó)家科技部,、國(guó)家自然科學(xué)基金、中國(guó)科學(xué)院的經(jīng)費(fèi)支持,。（生物谷Bioon.com）
生物谷推薦原始出處：
MCP Published on April 14, 2009
SysPTM: A Systematic Resource for Proteomic Research on Post-translational Modifications
Hong Li1,2,3? Xiaobin Xing1,2,3? Guohui Ding1, Qingrun Li1,3, Chuan Wang1, Lu Xie2*, Rong Zeng1*, Yixue Li1,2*
1. Key Lab of Systems Biology, Shanghai Institutes for Biological Sciences,Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, P.R.China
2. Shanghai Center for Bioinformation Technology, 100 Qinzhou Road, Shanghai 200235, P.R.China
3. Graduate School of the Chinese Academy of Sciences, 19 Yuquan Road, Beijing 100039, P.R.China
With the rapid expansion of protein post-translational modification (PTM) research based on large-scale proteomic work, there is an increasing demand for a suitable repository to analyze PTM data. Here we present a curated, web-accessible PTM database-SysPTM. SysPTM provides a systematic and sophisticated platform for proteomic PTM research, equipped not only with a knowledge base of manually curated multi-type modification data, but also with four fully developed, in-depth data mining tools. Currently, SysPTM contains data detailing 117349 experimentally determined PTM sites on 33421 proteins involving nearly 50 PTM types, curated from public resources including five databases and four webservers and more than one hundred peer-reviewed mass spectrometry papers. Protein annotations including Pfam domains, KEGG pathways, GO functional classification, and ortholog groups are integrated into the database. Four online tools have been developed and incorporated, including: PTMBlast, to compare a user’s PTM dataset with PTM data in SysPTM; PTMPathway, to map PTM proteins to KEGG pathways; PTMPhylog, to discover potentially conserved PTM sites; and PTMCluster, to find clusters of multi-site modifications. The workflow of SysPTM was demonstrated by analyzing an in-house phosphorylation dataset identified by MS/MS. It is shown that, in SysPTM, the roles of single-type and multi-type modifications can be systematically investigated in a full biological context. SysPTM could be an important contribution to modificomics research. SysPTM is freely available at:http://www.sysbio.ac.cn/SysPTM or http://lifecenter.sgst.cn/SysPTM.
