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The Sulfinator: predicting tyrosine sulfation sites in protein sequences
Author(s) -
Flavio Monigatti,
Elisabeth Gasteiger,
Amos Bairoch,
E. Jung
Publication year - 2002
Publication title -
bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.599
H-Index - 390
eISSN - 1367-4811
pISSN - 1367-4803
DOI - 10.1093/bioinformatics/18.5.769
Subject(s) - sulfation , tyrosine , amino acid , biochemistry , computer science , computational biology , protein sequencing , chemistry , peptide sequence , biology , gene
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.

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