Protein ubiquitination is an evolutional conserved and functional diversity posttranslational modification which is achieved through the sequential action of E1 activating enzymes, E2 conjugating enzymes, and E3 ligases. Hundreds of ubiquitined proteins had been discovered by large scale mass spectrometry or traditional biochemistry methods in the past few decades. Summary of validated ubiquitination substrates and prediction of new substrates had also been done in yeast. However, systematic summary of human ubiquitination substrates with experimental evidence and the enzymatic cascade of each substrate is not available. Here, we introduce a web resources hUbiquitome which is a public resource for the retrieval of experimentally verified human ubiquination enzymes and substrates. It is the first comprehensive database of human ubiqutitination pathway proteins and ubiquitin binding-site sequences which is freely available to academia.
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Yipeng Du, Nanfang Xu, Ming Lu, Tingting Li. hUbiquitome: A database of experimentally verified ubiquitination cascades in human.
|hUbiquitome.v1.0.zip||All data in hUbiquitome in csv format||Oct. 2011|
Citation: Yipeng Du, Nanfang Xu, Ming Lu, Tingting Li. hUbiquitome: A database of experimentally verified ubiquitination cascades in human.