Lysine acetylation site databases | Post-translational modification data analysis
As a reversible post-translational modification (PTM) discovered decades ago, protein lysine acetylation was known for its regulation of transcription through the modification of histones. Recent studies discovered that lysine acetylation targets broad substrates and especially plays an essential role in cellular metabolic regulation.
Offers a collection of post-translational modifications (PTMs). dbPTM contains a dataset of experimentally verified PTMs supported by the literature and gives an access to databases and tools associated with PTM analysis. It integrates the emerging S-nitrosylation, S-glutathionylation and succinylation, from approximately 500 research articles which were extracted by text mining.
Allows the retrieval of phosphorylation, acetylation, and N-glycosylation data of any protein of interest. PHOSIDA lists posttranslational modification sites associated with particular projects and proteomes or, alternatively, displays posttranslational modifications found for any protein or protein group of interest. In addition, structural and evolutionary information on each modified protein and posttranslational modification site is integrated. Importantly, Phosida links extensive peptide information to the sites, such as several peptides implicating the same site and temporal profiles of each site in response to stimulus (e.g., EGF stimulation).
Provides access to data about protein lysine modification. PLMD allows users to search through an interface containing more than 280 000 modifications events in more than 53 000 proteins across 176 eukaryotes and prokaryotes for up to 20 types of protein lysine modifications (PLMs). Its configuration permits to explore contents using several filters such as modification types, species numbers, or protein numbers.
A database for histone acetyltransferases, histone deacetylases, histone methyltransferases, histone demethylases and acetyl- or methyl-binding proteins, which catalyze, remove and recognize histone acetylation and methylation sites as ‘writers’, ‘erasers’ and ‘readers’, and synergistically determine the ‘histone code’. WERAM database contains more than 20 thousand nonredundant histone regulators from 148 eukaryotes.
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