2Department of Computer Science, Turkish-German University, Beykoz 34820 Istanbul, Türkiye DOI : 10.29228/jrp.286 One of the most important mechanisms that directly affect protein diversity and function is post-translational modification, which has grown exponentially and now encompasses a vast quantity of data. In order to better understand the nature of Post Translational modifications, in this study we elaborated those modifications and classified them into different perspectives
In order to base our investigations on high-confidence PTM occurrences, we confined our study to post-translational modifications that have been experimentally verified on humans, leaving out any annotated PTMs based solely on computation prediction. Utilizing chemical and functional details from external databases and literature, 170 distinct alterations from the neXtProt database were examined and identified. These modifications had a total occurrence of 187.220.
A careful examination of the data at hand led to the identification of 47 types that contained all 170 modifications. It was revealed that every amino acid underwent at least one type of modification, with cysteine serving as the target of the most diverse modifications—28 in all. Another finding was that most modifications function by converting the target amino acid, while small chemical groups are the most frequent functional groups.
The purpose of comprehensively classifying post-translational modifications is to provide an approach that may help understand the effects of these modifications on protein function. It's known that the physicochemical nature of these modifications exerts significant effects on function. However, there is a need to further deepen the current classifications
Keywords : Post-translational modifications; amino acid modifications; reversible /irreversible modifications; Data analysis of modifications