Scientific article
OA Policy
English

The Sulfinator: predicting tyrosine sulfation sites in protein sequences

Published inBioinformatics, vol. 18, no. 5, p. 769-770
Collection
  • Open Access - Licence nationale Oxford University Press
Publication date2002
Abstract

Protein tyrosine sulfation is an important post-translational modification of proteins that go through the secretory pathway. No clear-cut acceptor motif can be defined that allows the prediction of tyrosine sulfation sites in polypeptide chains. The Sulfinator is a software tool that can be used to predict tyrosine sulfation sites in protein sequences with an overall accuracy of 98%. Four different Hidden Markov Models were constructed, each of them specialized to recognize sulfated tyrosine residues depending on their location within the sequence: near the N-terminus, near the C-terminus, in the center of a window with a size of at least 25 amino acids, as well as in windows containing several tyrosine residues.

Keywords
  • Amino Acid Sequence
  • Animals
  • Caenorhabditis elegans/genetics/metabolism
  • Database Management Systems
  • Databases, Protein
  • Drosophila/genetics/metabolism
  • Humans
  • Molecular Sequence Data
  • Proteins/genetics/metabolism
  • Sensitivity and Specificity
  • Sequence Alignment
  • Sequence Analysis, Protein/methods
  • Software
  • Sulfates/metabolism
  • Tyrosine/genetics/metabolism
Citation (ISO format)
MONIGATTI, Flavio et al. The Sulfinator: predicting tyrosine sulfation sites in protein sequences. In: Bioinformatics, 2002, vol. 18, n° 5, p. 769–770. doi: 10.1093/bioinformatics/18.5.769
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Article (Published version)
Identifiers
Journal ISSN1367-4803
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379downloads

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Update30/03/2023 10:27:53
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