4月14日，国际知名学术刊物《分子与细胞蛋白质组学》（Molecular and Cellular Proteomics）在线发表了中科院系统生物学重点实验室的一项研究成果，该工作开发了一个系统的蛋白质翻译后修饰数据在线分析平台-SysPTM。
蛋白质翻译后修饰，是调节蛋白质生物学功能的关键步骤之一。更重要的是，在一个生物系统中，往往有多种修饰同时协同发挥作用。近年来，高灵敏度、高准确性和高通量的质谱分析实现了对蛋白质翻译后修饰的大规模鉴定，大大扩展了实验确认的蛋白质翻译后修饰种类和数量。
中科院系统生物学重点实验室博士生李虹和邢晓斌在李亦学研究员和曾嵘研究员，以及谢鹭副研究员的共同指导下，开发了一个系统的蛋白质翻译后修饰研究数据平台。该平台首先将分散在公共数据库和文献中的实验鉴定的多种蛋白质翻译后修饰信息整合，建立了一个目前最完整的蛋白质翻译后修饰数据库，包括了近50种修饰类型，33421个蛋白质上的117349个修饰位点。在此数据基础上，SysPTM又开发了四个在线工具（PTMBlast，PTMPathway，PTMPhylog，PTMCluster），用户可以在线分析和比较各种翻译后修饰的功能和保守性等性质。该数据库为深入分析蛋白质翻译后修饰奠定了基础，在线工具也为解析高通量蛋白质修饰数据提供了有力支持。
该项工作得到国家科技部、国家自然科学基金、中国科学院的经费支持。（生物谷Bioon.com）
生物谷推荐原始出处：
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.
