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iPTM-mLys: identifying multiple lysine PTM sites and their different types
Author(s) -
WangRen Qiu,
BiQian Sun,
Xuan Xiao,
Zhaochun Xu,
KuoChen Chou
Publication year - 2016
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/btw380
Subject(s) - succinylation , computer science , lysine , computational biology , random forest , set (abstract data type) , artificial intelligence , pseudo amino acid composition , machine learning , web server , protein sequencing , acetylation , biology , peptide sequence , amino acid , biochemistry , the internet , world wide web , programming language , dipeptide , gene
Post-translational modification, abbreviated as PTM, refers to the change of the amino acid side chains of a protein after its biosynthesis. Owing to its significance for in-depth understanding various biological processes and developing effective drugs, prediction of PTM sites in proteins have currently become a hot topic in bioinformatics. Although many computational methods were established to identify various single-label PTM types and their occurrence sites in proteins, no method has ever been developed for multi-label PTM types. As one of the most frequently observed PTMs, the K-PTM, namely, the modification occurring at lysine (K), can be usually accommodated with many different types, such as 'acetylation', 'crotonylation', 'methylation' and 'succinylation'. Now we are facing an interesting challenge: given an uncharacterized protein sequence containing many K residues, which ones can accommodate two or more types of PTM, which ones only one, and which ones none?

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