SysPTM 2.0: an updated systematic resource for post-translational modification

Post-translational modifications (PTMs) of proteins play essential roles in almost all cellular processes, and are closely related to physiological activity and disease development of living organisms. The development of tandem mass spectrometry (MS/MS) has resulted in a rapid increase of PTMs ident...

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Veröffentlicht in:Database (Weston) 2014, Vol.2014 (p.bau025-bau025), p.bau025-bau025
Hauptverfasser: Li, Jing, Jia, Jia, Li, Hong, Yu, Jian, Sun, Han, He, Ying, Lv, Daqing, Yang, Xiaojuan, Glocker, Michael O, Ma, Liangxiao, Yang, Jiabei, Li, Ling, Li, Wei, Zhang, Guoqing, Liu, Qian, Li, Yixue, Xie, Lu
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container_end_page bau025
container_issue p.bau025-bau025
container_start_page bau025
container_title Database (Weston)
container_volume 2014
creator Li, Jing
Jia, Jia
Li, Hong
Yu, Jian
Sun, Han
He, Ying
Lv, Daqing
Yang, Xiaojuan
Glocker, Michael O
Ma, Liangxiao
Yang, Jiabei
Li, Ling
Li, Wei
Zhang, Guoqing
Liu, Qian
Li, Yixue
Xie, Lu
description Post-translational modifications (PTMs) of proteins play essential roles in almost all cellular processes, and are closely related to physiological activity and disease development of living organisms. The development of tandem mass spectrometry (MS/MS) has resulted in a rapid increase of PTMs identified on proteins from different species. The collection and systematic ordering of PTM data should provide invaluable information for understanding cellular processes and signaling pathways regulated by PTMs. For this original purpose we developed SysPTM, a systematic resource installed with comprehensive PTM data and a suite of web tools for annotation of PTMs in 2009. Four years later, there has been a significant advance with the generation of PTM data and, consequently, more sophisticated analysis requirements have to be met. Here we submit an updated version of SysPTM 2.0 (http://lifecenter.sgst.cn/SysPTM/), with almost doubled data content, enhanced web-based analysis tools of PTMBlast, PTMPathway, PTMPhylog, PTMCluster. Moreover, a new session SysPTM-H is constructed to graphically represent the combinatorial histone PTMs and dynamic regulation of histone modifying enzymes, and a new tool PTMGO is added for functional annotation and enrichment analysis. SysPTM 2.0 not only facilitates resourceful annotation of PTM sites but allows systematic investigation of PTM functions by the user. Database URL: http://lifecenter.sgst.cn/SysPTM/.
doi_str_mv 10.1093/database/bau025
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The development of tandem mass spectrometry (MS/MS) has resulted in a rapid increase of PTMs identified on proteins from different species. The collection and systematic ordering of PTM data should provide invaluable information for understanding cellular processes and signaling pathways regulated by PTMs. For this original purpose we developed SysPTM, a systematic resource installed with comprehensive PTM data and a suite of web tools for annotation of PTMs in 2009. Four years later, there has been a significant advance with the generation of PTM data and, consequently, more sophisticated analysis requirements have to be met. Here we submit an updated version of SysPTM 2.0 (http://lifecenter.sgst.cn/SysPTM/), with almost doubled data content, enhanced web-based analysis tools of PTMBlast, PTMPathway, PTMPhylog, PTMCluster. Moreover, a new session SysPTM-H is constructed to graphically represent the combinatorial histone PTMs and dynamic regulation of histone modifying enzymes, and a new tool PTMGO is added for functional annotation and enrichment analysis. SysPTM 2.0 not only facilitates resourceful annotation of PTM sites but allows systematic investigation of PTM functions by the user. 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Moreover, a new session SysPTM-H is constructed to graphically represent the combinatorial histone PTMs and dynamic regulation of histone modifying enzymes, and a new tool PTMGO is added for functional annotation and enrichment analysis. SysPTM 2.0 not only facilitates resourceful annotation of PTM sites but allows systematic investigation of PTM functions by the user. 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Moreover, a new session SysPTM-H is constructed to graphically represent the combinatorial histone PTMs and dynamic regulation of histone modifying enzymes, and a new tool PTMGO is added for functional annotation and enrichment analysis. SysPTM 2.0 not only facilitates resourceful annotation of PTM sites but allows systematic investigation of PTM functions by the user. Database URL: http://lifecenter.sgst.cn/SysPTM/.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>24705204</pmid><doi>10.1093/database/bau025</doi><oa>free_for_read</oa></addata></record>
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subjects Animals
Database Update
Databases, Protein
enzymes
histones
Histones - metabolism
Humans
Internet
post-translational modification
Protein Processing, Post-Translational
signal transduction
Software
tandem mass spectrometry
User-Computer Interface
Web Browser
world wide web
title SysPTM 2.0: an updated systematic resource for post-translational modification
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