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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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/. |
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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. Database URL: http://lifecenter.sgst.cn/SysPTM/.</description><identifier>ISSN: 1758-0463</identifier><identifier>ISSN: 0162-4105</identifier><identifier>EISSN: 1758-0463</identifier><identifier>DOI: 10.1093/database/bau025</identifier><identifier>PMID: 24705204</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>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</subject><ispartof>Database (Weston), 2014, Vol.2014 (p.bau025-bau025), p.bau025-bau025</ispartof><rights>The Author(s) 2014. Published by Oxford University Press. 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c426t-5c44273c5bbd02496384670c2ada8c9c27300d232cb08e603fca751411a444cf3</citedby><cites>FETCH-LOGICAL-c426t-5c44273c5bbd02496384670c2ada8c9c27300d232cb08e603fca751411a444cf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3975108/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3975108/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,4009,27902,27903,27904,53770,53772</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24705204$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Jing</creatorcontrib><creatorcontrib>Jia, Jia</creatorcontrib><creatorcontrib>Li, Hong</creatorcontrib><creatorcontrib>Yu, Jian</creatorcontrib><creatorcontrib>Sun, Han</creatorcontrib><creatorcontrib>He, Ying</creatorcontrib><creatorcontrib>Lv, Daqing</creatorcontrib><creatorcontrib>Yang, Xiaojuan</creatorcontrib><creatorcontrib>Glocker, Michael O</creatorcontrib><creatorcontrib>Ma, Liangxiao</creatorcontrib><creatorcontrib>Yang, Jiabei</creatorcontrib><creatorcontrib>Li, Ling</creatorcontrib><creatorcontrib>Li, Wei</creatorcontrib><creatorcontrib>Zhang, Guoqing</creatorcontrib><creatorcontrib>Liu, Qian</creatorcontrib><creatorcontrib>Li, Yixue</creatorcontrib><creatorcontrib>Xie, Lu</creatorcontrib><title>SysPTM 2.0: an updated systematic resource for post-translational modification</title><title>Database (Weston)</title><addtitle>Database (Oxford)</addtitle><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/.</description><subject>Animals</subject><subject>Database Update</subject><subject>Databases, Protein</subject><subject>enzymes</subject><subject>histones</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Internet</subject><subject>post-translational modification</subject><subject>Protein Processing, Post-Translational</subject><subject>signal transduction</subject><subject>Software</subject><subject>tandem mass spectrometry</subject><subject>User-Computer Interface</subject><subject>Web Browser</subject><subject>world wide web</subject><issn>1758-0463</issn><issn>0162-4105</issn><issn>1758-0463</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUlPwzAQhS0EoqVw5oZ85JJ2vCRxOCChik0qi0Q5W47jQFASFztB6r_H0EXlxMljvTef3ughdEpgTCBjk0J1KlfeTHLVA4330JCksYiAJ2x_Zx6gI-8_AJJUCH6IBpSnEFPgQ_T4svTP8wdMx3CBVYv7RUCaAvul70yjukpjZ7ztnTa4tA4vrO-izqnW10G0rapxY4uqrPTv9xgdlKr25mT9jtDrzfV8ehfNnm7vp1ezSHOadFGsOacp03GeF0B5ljDBkxQ0VYUSOtNBAygoozoHYRJgpVZpTDghinOuSzZClyvuos8bU2jThky1XLiqUW4prarkX6Wt3uWb_ZIsCxwQAXC-Bjj72Rvfyaby2tS1ao3tvSSCAMQi4-n_1hAsXEMFCdbJyqqd9d6ZcpuIgPwpTG4Kk6vCwsbZ7iFb_6Yh9g2Wi5Rw</recordid><startdate>2014</startdate><enddate>2014</enddate><creator>Li, Jing</creator><creator>Jia, Jia</creator><creator>Li, Hong</creator><creator>Yu, Jian</creator><creator>Sun, Han</creator><creator>He, Ying</creator><creator>Lv, Daqing</creator><creator>Yang, Xiaojuan</creator><creator>Glocker, Michael O</creator><creator>Ma, Liangxiao</creator><creator>Yang, Jiabei</creator><creator>Li, Ling</creator><creator>Li, Wei</creator><creator>Zhang, Guoqing</creator><creator>Liu, Qian</creator><creator>Li, Yixue</creator><creator>Xie, Lu</creator><general>Oxford University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>2014</creationdate><title>SysPTM 2.0: an updated systematic resource for post-translational modification</title><author>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</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c426t-5c44273c5bbd02496384670c2ada8c9c27300d232cb08e603fca751411a444cf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Animals</topic><topic>Database Update</topic><topic>Databases, Protein</topic><topic>enzymes</topic><topic>histones</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Internet</topic><topic>post-translational modification</topic><topic>Protein Processing, Post-Translational</topic><topic>signal transduction</topic><topic>Software</topic><topic>tandem mass spectrometry</topic><topic>User-Computer Interface</topic><topic>Web Browser</topic><topic>world wide web</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Jing</creatorcontrib><creatorcontrib>Jia, Jia</creatorcontrib><creatorcontrib>Li, Hong</creatorcontrib><creatorcontrib>Yu, Jian</creatorcontrib><creatorcontrib>Sun, Han</creatorcontrib><creatorcontrib>He, Ying</creatorcontrib><creatorcontrib>Lv, Daqing</creatorcontrib><creatorcontrib>Yang, Xiaojuan</creatorcontrib><creatorcontrib>Glocker, Michael O</creatorcontrib><creatorcontrib>Ma, Liangxiao</creatorcontrib><creatorcontrib>Yang, Jiabei</creatorcontrib><creatorcontrib>Li, Ling</creatorcontrib><creatorcontrib>Li, Wei</creatorcontrib><creatorcontrib>Zhang, Guoqing</creatorcontrib><creatorcontrib>Liu, Qian</creatorcontrib><creatorcontrib>Li, Yixue</creatorcontrib><creatorcontrib>Xie, Lu</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Database (Weston)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Jing</au><au>Jia, Jia</au><au>Li, Hong</au><au>Yu, Jian</au><au>Sun, Han</au><au>He, Ying</au><au>Lv, Daqing</au><au>Yang, Xiaojuan</au><au>Glocker, Michael O</au><au>Ma, Liangxiao</au><au>Yang, Jiabei</au><au>Li, Ling</au><au>Li, Wei</au><au>Zhang, Guoqing</au><au>Liu, Qian</au><au>Li, Yixue</au><au>Xie, Lu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SysPTM 2.0: an updated systematic resource for post-translational modification</atitle><jtitle>Database (Weston)</jtitle><addtitle>Database (Oxford)</addtitle><date>2014</date><risdate>2014</risdate><volume>2014</volume><issue>p.bau025-bau025</issue><spage>bau025</spage><epage>bau025</epage><pages>bau025-bau025</pages><issn>1758-0463</issn><issn>0162-4105</issn><eissn>1758-0463</eissn><abstract>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/.</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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