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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

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Related Experiment Video

Updated: Jun 24, 2026

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
08:12

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

SysPTM: a systematic resource for proteomic research on post-translational modifications.

Hong Li1, Xiaobin Xing, Guohui Ding

  • 1Key Lab of Systems Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.

Molecular & Cellular Proteomics : MCP
|April 16, 2009
PubMed
Summary

SysPTM is a new database for analyzing protein post-translational modification (PTM) data. It offers a curated knowledge base and four data mining tools to explore PTMs in a biological context.

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Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
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Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

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Related Experiment Videos

Last Updated: Jun 24, 2026

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
08:12

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Area of Science:

  • Proteomics
  • Bioinformatics
  • Systems Biology

Background:

  • The rapid growth of proteomic studies necessitates a centralized resource for analyzing protein post-translational modification (PTM) data.
  • Existing resources may lack comprehensive PTM data or integrated analytical tools.

Purpose of the Study:

  • To develop and present SysPTM, a curated, web-accessible database and analytical platform for proteomic PTM research.
  • To provide a systematic approach for investigating the roles of single-type and multi-type modifications within their biological context.

Main Methods:

  • Curated a knowledge base of multi-type PTM data from public resources and literature.
  • Integrated protein annotations (Pfam, KEGG, GO, orthologs).
  • Developed four data mining tools: PTMBlast, PTMPathway, PTMPhylog, and PTMCluster.

Main Results:

  • SysPTM contains 117,349 PTM sites on 33,421 proteins across nearly 50 PTM types.
  • The database integrates diverse protein annotations for comprehensive analysis.
  • Four specialized tools facilitate PTM data comparison, pathway mapping, conservation analysis, and cluster identification.

Conclusions:

  • SysPTM serves as a valuable resource for modificomics research by enabling systematic investigation of PTMs.
  • The platform facilitates understanding PTMs within a broader biological framework.
  • SysPTM is freely accessible online, promoting collaborative research.