Provides information and resources to facilitate phosphorylation research. PhosphoSite is a curated database dedicated to aggregating information on physiological protein phosphorylation sites. Its goal is to identify and organize information about all in vivo phosphorylation sites in human and mouse proteomes. It contains over 330 000 non-redundant post-translational modifications (PTMs), including phospho, acetyl, ubiquityl and methyl groups.
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.
Allows users to look into human ubiquitin ligase-substrate interaction network. UbiBrowser tries to simplify access to information concerning human ubiquitin ligase (E3) or substrate protein. The interface of this database presents the potential E3-substrate interactions in two main views: network view and sequence view. This resource offers users to explore more than 20220 human proteins’ corresponding E3 ligases.
Facilitates the experimental detection of co-modified peptides for investigating post-translational modifications (PTMs) cross-talk. TCellXTalk is a comprehensive database of phosphorylation, ubiquitination and acetylation sites in human T cells, a prime cellular model to investigate signal transduction and the immune response. All data are derived exclusively from studies conducted in primary human T cells or Jurkat cells.
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.
Offers users an effective platform to efficiently study protein ubiquitylation networks among large-scale ubiquitylation data. The current version of UbiNet was designed specifically for humans to serve as not only a meaningful framework for E3-substrate regulatory networks but also a new scheme to discover potential E3 ligases for ubiquitylated substrates. To date, UbiNet has accumulated 43 948 experimentally verified ubiquitylation sites from 14 692 ubiquitylated proteins of humans.
A public resource for the retrieval of experimentally verified human ubiquitination enzymes and substrates. hUbiquitome is the first comprehensive database of human ubiquitination cascades. Currently, hUbiquitome has in its repertoire curated data comprising 1 E1 enzyme, 12 E2 enzymes, 138 E3 ligases or complexes, 279 different substrate proteins and 17 deubiquitination enzyme terms. The biological functions of substrates from different kinds of E3s were analyzed using the collected data.
Provides a scientific community with a comprehensive, freely and high-quality accessible resource of mammalian protein ubiquitination sites. The mUbiSiDa was designed to be a widely used tool for biologists and biomedical researchers with a user-friendly interface, and facilitate the further research of protein ubiquitination, biological networks and functional proteomics. It can also provide blast function to predict novel protein ubiquitination sites in other species by blast the query sequence in the deposit sequences.
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