Emily Bowler-Barnett (Cambridge / GB), Jun Fan (Cambridge / GB), Kerry Ramsbottom (Liverpool / GB), Oscar Martin Camacho (Liverpool / GB), Ananth Prakash (Cambridge / GB), Sun Zhi (Cambridge / GB), Yasset Perez Riverol (Cambridge / GB), Eric Deutsch (Seattle, WA / US), Juan Vizcaino (Cambridge / GB), Andrew Jones (Liverpool / GB), Sandra Orchard (Cambridge / GB), Maria Martin (Cambridge / GB), UniProt Consortium (Cambridge / GB)
UniProtKB is a comprehensive, expert-led, publicly available database of protein sequence, function and disease variation information. Incorporation of data from a wide variety of resources, either imported from collaborative sources or added from the scientific literature by manual curation, provides a wealth of protein sequence, peptide modification, interaction, and protein function data.
Post-translational modifications (PTMs) increase proteome diversity and allow a protein to alter many aspects of its biological state, including its function, cellular localization, interaction partners, and stability. PTMs can be fluid throughout the life cycle of a protein and contribute to the proteomes" dynamic and robust response to stimuli and biological pressures. PTMs therefore play a key role in both endogenous cellular systems and disease signaling pathology.
Manual curation of the scientific literature facilitates the detailed capture of how proteins are modified within a cell and additionally how this might modify the function, cellular location, or interactions of that protein. The PTMeXchange project, in conjunction with the University of Liverpool, Peptide Atlas and PRIDE aims to re-analyse publicly available PTM-enriched proteomics datasets and control for accurate modification site localization, whilst abiding by FAIR data principles.
We present an update to the protein post-translational modification landscape in UniProtKB, including new visualization tools, and multi-query search functionality both on the website as well as the UniProt Proteins API which allows access and complex querying of the whole database.