ScanProsite: detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins
Open accessAbstract
ScanProsite--http://www.expasy.org/tools/scanprosite/--is a new and improved version of the web-based tool for detecting PROSITE signature matches in protein sequences. For a number of PROSITE profiles, the tool now makes use of ProRules--context-dependent annotation templates--to detect functional and structural intra-domain residues. The detection of those features enhances the power of function prediction based on profiles. Both user-defined sequences and sequences from the UniProt Knowledgebase can be matched against custom patterns, or against PROSITE signatures. To improve response times, matches of sequences from UniProtKB against PROSITE signatures are now retrieved from a pre-computed match database. Several output modes are available including simple text views and a rich mode providing an interactive match and feature viewer with a graphical representation of results.
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A ScanProsite search of the human proteome for the p23 tail-helix-like motif FXXMMN identified NCoA3/SRC-3 among the top 10 hits.
“Using ScanProsite28 to search the human proteome for a p23tail-helix -like motif (“FXXMMN”), remarkably, Nuclear Coactivator 3 (NCoA3/SRC-3), a canonical co-activator protein for SHRs, was among the top 10 hits.”
From Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism (2022) · cites this paper as [28]
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- Authors
- de Castro, E., Sigrist, C. J. A., Gattiker, A., Bulliard, V., Langendijk-Genevaux, P. S., Gasteiger, E., Bairoch, A., & Hulo, N.
- Affiliations
- SIB Swiss Institute of Bioinformatics (CH)
- National Institute of Technology and Evaluation (JP)
- University of Geneva (CH)
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2006-07-01
- Volume
- 34
- Issue
- Web Server
- Pages
- W362-W365
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2125079066
- Cited by
- 1,686
- References
- 12
- Citations by year
- 2026: 57 · 2025: 73 · 2024: 126 · 2023: 127 · 2022: 130 · 2021: 130 · 2020: 135 · 2019: 108 · 2018: 95 · 2017: 86 · 2016: 101 · 2015: 99 · 2014: 87 · 2013: 45 · 2012: 58
- FWCI
- 15.34
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- other-oa
- Locations
- Nucleic Acids Research (publishedVersion, other-oa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (publishedVersion, other-oa)
- reroDoc Digital Library (submittedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Funders
- National Science Foundation
- Australian Government
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (103922)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- protein function prediction, protein structure prediction, domain annotation, web-based annotation tool, UniProtKB
- MeSH terms
- Amino Acids, Proteins, Software, User-Computer Interface, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Internet, Sequence Analysis, Protein, Databases, Protein
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