SysPTM


24705204	SysPTM 2.0: an updated systematic resource for post-translational modification. [PMID: 24705204] Li J, Jia J, Li H, Yu J, Sun H, He Y, Lv D, Yang X, Glocker MO, Ma L, Yang J, Li L, Li W, Zhang G, Liu Q, Li Y, Xie L. 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/. Database (Oxford). 2014:2014() \| 28 Citations (from Europe PMC, 2025-03-22)
19366988	SysPTM: a systematic resource for proteomic research on post-translational modifications. [PMID: 19366988] Li H, Xing X, Ding G, Li Q, Wang C, Xie L, Zeng R, Li Y. Abstract 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 data base, 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 117,349 experimentally determined PTM sites on 33,421 proteins involving nearly 50 PTM types, curated from public resources including five data bases and four web servers 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 data base. 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 role 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 online at www.sysbio.ac.cn/SysPTM. Mol Cell Proteomics. 2009:8(8) \| 79 Citations (from Europe PMC, 2025-03-22)

SysPTM 2.0: an updated systematic resource for post-translational modification. [PMID: 24705204]

Li J, Jia J, Li H, Yu J, Sun H, He Y, Lv D, Yang X, Glocker MO, Ma L, Yang J, Li L, Li W, Zhang G, Liu Q, Li Y, Xie L.

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/.

Database (Oxford). 2014:2014() | 28 Citations (from Europe PMC, 2025-03-22)

SysPTM: a systematic resource for proteomic research on post-translational modifications. [PMID: 19366988]

Li H, Xing X, Ding G, Li Q, Wang C, Xie L, Zeng R, Li Y.

Abstract

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 data base, 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 117,349 experimentally determined PTM sites on 33,421 proteins involving nearly 50 PTM types, curated from public resources including five data bases and four web servers 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 data base. 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 role 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 online at www.sysbio.ac.cn/SysPTM.

Mol Cell Proteomics. 2009:8(8) | 79 Citations (from Europe PMC, 2025-03-22)

URL:	http://lifecenter.sgst.cn/SysPTM
Full name:
Description:	SysPTM is installed with comprehensive PTM (post-translational modification) data and a suite of web tools for annotation of PTMs.
Year founded:	2009
Last update:	2014
Version:	2.0
Accessibility:	Unaccessible
Country/Region:	China

Data type:	Protein
Data object:	Animal
Database category:	Modification
Major species:	Homo sapiens
Keywords:	tandem mass spectrometry PTMBlast PTMPathway PTMPhylog PTMCluster post-translational modification (PTM)

University/Institution:	Huazhong University of Science and Technology
Address:	Key Laboratory of Biomedical Photonics of Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, P. R. China
City:	Wuhan
Province/State:	Hubei
Country/Region:	China
Contact name (PI/Team):	Yixue Li
Contact email (PI/Helpdesk):	yxli@sibs.ac.cn

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