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2015 ProteomeScout: A repository and analysis resource for post-translational modifications and proteins Matthew K. Matlock Washington University School of Medicine in St. Louis
Alex S. Holehouse Washington University School of Medicine in St. Louis
Kristen M. Naegle Washington University in St Louis
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Recommended Citation Matlock, Matthew K.; Holehouse, Alex S.; and Naegle, Kristen M., ,"ProteomeScout: A repository and analysis resource for post- translational modifications and proteins." Nucleic Acids Research.43,. D521-D530. (2015). https://digitalcommons.wustl.edu/open_access_pubs/3715
This Open Access Publication is brought to you for free and open access by Digital Commons@Becker. It has been accepted for inclusion in Open Access Publications by an authorized administrator of Digital Commons@Becker. For more information, please contact [email protected]. Published online 20 November 2014 Nucleic Acids Research, 2015, Vol. 43, Database issue D521–D530 doi: 10.1093/nar/gku1154 ProteomeScout: a repository and analysis resource for post-translational modifications and proteins Matthew K. Matlock, Alex S. Holehouse and Kristen M. Naegle*
Department of Biomedical Engineering and the Center for Biological Systems Engineering, Washington University, St Louis, MO 63130, USA
Received August 15, 2014; Revised October 28, 2014; Accepted October 29, 2014 Downloaded from
ABSTRACT databases––it is the only database that encompasses PTM compendia and allows for the community deposition of ProteomeScout (https://proteomescout.wustl.edu)is PTM experiments, and it is the only web service that has a resource for the study of proteins and their post- built-in subset selection and enrichment for exploring and translational modifications (PTMs) consisting of a analyzing PTM experiments. ProteomeScout is also unique http://nar.oxfordjournals.org/ database of PTMs, a repository for experimental data, in the world of protein resources––it is a resource that en- an analysis suite for PTM experiments, and a tool tails a flexible, track-based viewer of protein annotations. for visualizing the relationships between complex The purposeful design of these features was inspired by protein annotations. The PTM database is a com- the historical progression of resources for other types of pendium of public PTM data, coupled with user- molecules, including: the UCSC Genome Browser (1)and uploaded experimental data. ProteomeScout pro- the Gene Expression Omnibus (GEO) (2). The rapid expan- vides analysis tools for experimental datasets, in- sion in the identification of protein PTMs, enabled by high- throughput experimental techniques (3), has led to explo- at Washington University, Law School Library on February 25, 2015 cluding summary views and subset selection, which sive growth in the number of specialized PTM databases, can identify relationships within subsets of data by although none of which reflect the full capabilities of the testing for statistically significant enrichment of pro- UCSC Genome Browser or the GEO. A sampling of PTM- tein annotations. Protein annotations are incorpo- specific databases includes Phosida (4), PhosphoSitePlus rated in the ProteomeScout database from external (5), phospho.ELM (6), PTMScout (7), dbPTM (8), PTM- resources and include terms such as Gene Ontology SD (9), PTMCode (10) and O-GLYCBASE (11). The names annotations, domains, secondary structure and non- of these databases reflect the progression of PTM research, synonymous polymorphisms. These annotations are and despite initially being focused on phosphorylation, available in the database download, in the analysis many of them now encompass multiple modification types. tools and in the protein viewer. The protein viewer Growth in PTM identification is just one part of the rapid allows for the simultaneous visualization of anno- expansion in PTM-centric research; the other part involves the quantitative profiling of PTM changes across condi- tations in an interactive web graphic, which can tions. New experimental capabilities have enabled a number be exported in Scalable Vector Graphics (SVG) for- of studies, including high-throughput profiling of tyrosine mat. Finally, quantitative data measurements asso- phosphorylation changes in response to receptor tyrosine ciated with public experiments are also easily view- kinase activation (12,13), methylation response to methyl- able within protein records, allowing researchers to transferase inhibition (14) and ubiquitination response to see how PTMs change across different contexts. proteasome inhibition (15). These datasets contain rich in- ProteomeScout should prove useful for protein re- formation about the regulation of proteins. However, sup- searchers and should benefit the proteomics com- plementary data standards in this research field have made munity by providing a stable repository for PTM ex- it difficult for researchers to garner the power of this infor- periments. mation. The status quo for PTM data involves publication of iso- lated, static supplementary tables. This means that there is INTRODUCTION no single standard format, no central repository and, due to ProteomeScout is a database of protein post-translational the volatility of protein databases (16), there is no persistent modifications, protein annotations and a web resource for mapping of identified PTMs to protein database records. analysis of PTMs and proteins. ProteomeScout is unique Protein identifiers become out-of-date relatively quickly, in the world of post-translational modification (PTM) and in the most extreme cases, disappear altogether––as
*To whom correspondence should be addressed. Tel: (314) 935-7665; Fax: (314) 9357448; Email: [email protected]