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.
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 experimentally derived information about the human proteome including protein–protein interactions (PPIs), post-translational modifications (PTMs) and tissue expression. HPRD is an integrated knowledgebase for genomic and proteomic investigators. The database also includes (i) PhosphoMotif Finder that contains known kinase/phosphatase substrate and binding motifs, (ii) links to a signaling pathway resource called NetPath, (iii) a distributed annotation system, called Human Proteinpedia for enhanced community participation and allows the use of BLAST for querying mRNA/protein data.
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.
Deals with information related to post translational modifications (PTMs) in plants. Plant PTM Viewer offers a repository of information curated from more than 120 scientific publications proposing a framework for protein visualization as well as tools for further investigation. It also provides a search engine enabling to find ambiguous or specific amino acid motifs that are modified by one or more PTMs.
Allows users to search and find motifs with any sequence data set. scan-x is made to take output of motif-x and scan protein sequence files for the occurrences of these motifs in other proteins or proteomes. It uses fixed residues as a pattern to search within protein sequence files, and matches sequences that contain some patterns. The web interface offers users to realize a research from several dataset.
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.