4.8 Article

UniProt: the Universal Protein Knowledgebase in 2023

Journal

NUCLEIC ACIDS RESEARCH
Volume 51, Issue D1, Pages D523-D531

Publisher

OXFORD UNIV PRESS
DOI: 10.1093/nar/gkac1052

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The UniProt Knowledgebase aims to provide comprehensive, high-quality, and freely accessible protein sequences annotated with functional information. The database has expanded its data processing pipeline and website to accommodate the increasing information content, with over 227 million sequences and plans to include a reference proteome for each taxonomic group. Detailed annotations are extracted from the literature to update or create reviewed entries, while unreviewed entries are supplemented with annotations from automated systems. The new website, https://www.uniprot.org/, offers enhanced user experience and easy access to data, including AlphaFold structures and improved protein subcellular localization visualizations.
The aim of the UniProt Knowledgebase is to provide users with a comprehensive, high-quality and freely accessible set of protein sequences annotated with functional information. In this publication we describe enhancements made to our data processing pipeline and to our website to adapt to an ever-increasing information content. The number of sequences in UniProtKB has risen to over 227 million and we are working towards including a reference proteome for each taxonomic group. We continue to extract detailed annotations from the literature to update or create reviewed entries, while unreviewed entries are supplemented with annotations provided by automated systems using a variety of machine-learning techniques. In addition, the scientific community continues their contributions of publications and annotations to UniProt entries of their interest. Finally, we describe our new website (https://www.uniprot.org/), designed to enhance our users' experience and make our data easily accessible to the research community. This interface includes access to AlphaFold structures for more than 85% of all entries as well as improved visualisations for subcellular localisation of proteins.

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