Article

iProteinDB: an integrative database of <i>Drosophila</i> post-translational modifications

2018-08-07

Abstract excerpt

Post-translational modification (PTM) serves as a regulatory mechanism for protein function, influencing stability, protein interactions, activity and localization, and is critical in many signaling pathways. The best characterized PTM is phosphorylation, whereby a phosphate is added to an acceptor residue, commonly serine, threonine and tyrosine. As proteins are often phosphorylated at multiple sites, identifying...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: d59d2a51-5f0d-5723-806d-e043ac794f50
DOI: 10.1101/386268

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

iProteinDB: an integrative database of <i>Drosophila</i> post-translational modificationsDOI 10.1101/386268Read

EPSD 2.0: An Updated Database of Protein Phosphorylation Sites across Eukaryotic SpeciesSemantic proximity Read

Transitions in the proteome and phospho-proteome during <i>Xenopus laevis</i> developmentSemantic proximity Read

<i>In-silico</i> definition of the <i>Drosophila melanogaster</i> matrisomeSemantic proximity Read

Computational analysis of phosphoproteomics: progresses and perspectives.Semantic proximity Read

The functional landscape of the human phosphoproteomeSemantic proximity Read

dbPTM: an information repository of protein post-translational modification.Semantic proximity Read

Evolution of protein phosphorylation across 18 fungal species.Semantic proximity Read

PhosphoSitePlus, 2014: mutations, PTMs and recalibrations.Semantic proximity Read

PhosphoBlast, a computational tool for comparing phosphoprotein signatures among large datasets.Semantic proximity Read

Phosphorylation in the <i>Plasmodium falciparum</i> proteome: A meta-analysis of publicly available data setsSemantic proximity Read

iEKPD 2.0: an update with rich annotations for eukaryotic protein kinases, protein phosphatases and proteins containing phosphoprotein-binding domainsSemantic proximity Read

PhosphOrtholog: a web-based tool for cross-species mapping of orthologous protein post-translational modificationsSemantic proximity Read