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UniProt: the Universal Protein Knowledgebase in 2023
Open accessAbstract
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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“The impact of the predicted structures is further enhanced by their seamless integration into several core data resources, including PDBe-KB (17), UniProt (6), Ensembl (16), InterPro (15), Genecards (24) and MobiDB (25), among others.”
From AlphaFold Protein Structure Database in 2024: providing structure coverage for over 214 million protein sequences (2024) · cites this paper as [6]
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“of the 51 human PX domain-containing proteins, 26 possess a serine or threonine at positions corresponding to SNX17 S38 or SNX3 S72 (38, 42)”
From Phosphorylation of SNX17 impedes activation of Retriever-mediated sorting (2025) · cites this paper as [42]
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Database resources of the National Center for Biotechnology Information: update
Wheeler, D. L. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkh073 · Cited by 10,695
Varadi, M., Anyango, S., Deshpande, M., Nair, S., Natassia, C., Yordanova, G., Yuan, D., Stroe, O., Wood, G., Laydon, A., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1061 · Cited by 7,850 · cited 1×
“Over 85% of UniProt entries now contain a predicted protein structure, provided by AlphaFold, an artificial intelligence system developed by DeepMind that makes predictions of protein structures from their amino-acid sequences (1).”
BackgroundUniProt: the universal protein knowledgebase in 2021
The UniProt Consortium, Bateman, A., Martin, M.-J., Orchard, S., Magrane, M., Agivetova, R., Ahmad, S., Alpi, E., Bowler-Barnett, E. H., Britto, R., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1100 · Cited by 6,372
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Sayers, E. W., Bolton, E. E., Brister, J. R., Canese, K., Chan, J., Comeau, D. C., Connor, R., Funk, K., Kelly, C., Kim, S., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1112 · Cited by 2,812
Paysan‐Lafosse, T., Blum, M., Chuguransky, S., Grego, T., Pinto, B. L., Salazar, G. A., Bileschi, M. L., Bork, P., Bridge, A. J., Colwell, L. J., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac993 · Cited by 2,457
Self-citationCunningham, F., Allen, J. E., Allen, J., Alvarez-Jarreta, J., Amode, M. R., Armean, I. M., Austine-Orimoloye, O., Azov, A. G., Barnes, I., Bennett, R., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1049 · Cited by 1,923
Burley, S. K., Bhikadiya, C., Bi, C., Bittrich, S., Chen, L., Crichlow, G. V., Christie, C. H., Dalenberg, K., Di Costanzo, L., Duarte, J. M., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1038 · Cited by 1,581
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Hastings, J., Owen, G., Dekker, A., Ennis, M., Kale, N., Muthukrishnan, V., Turner, S., Swainston, N., Mendes, P., & Steinbeck, C. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1031 · Cited by 1,083
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BioLiP: a semi-manually curated database for biologically relevant ligand–protein interactions
Yang, J., Roy, A., & Zhang, Y. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks966 · Cited by 749
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Self-citationBasu, S., Zhao, B., Biró, B., Faraggi, E., Gsponer, J. A., Hu, G., Kloczkowski, A., Malhis, N., Mirdita, M., Söding, J., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad985 · Cited by 15
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Branella, G. M., Lee, J. Y., Okáľová, J., Parwani, K. K., Alexander, J. S., Arthuzo, R. F., Fedanov, A., Yu, B., McCarty, D., Brown, H. C., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1294555 · Cited by 15
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Olzhabayeva, A. O., Baimanov, Z. N., Умбетова, Ш., Shegenbayev, A. T., & Daldabayeva, G. T. (2023) · Bulletin of Korkyt Ata Kyzylorda University · doi:10.52081/bkaku.2023.v66.i3.108 · Cited by 15
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Gaidhani, P. M., Chakraborty, S., Ramesh, K., Chellam, P. V., & van Hullebusch, E. D. (2024) · Chemosphere · doi:10.1016/j.chemosphere.2024.141155 · Cited by 13
A Massive Proteogenomic Screen Identifies Thousands of Novel Peptides From the Human “Dark” Proteome
Cao, X., Sun, S., & Xing, J. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100719 · Cited by 17
Horizontal gene transfer after faecal microbiota transplantation in adolescents with obesity
Behling, A. H., Wilson, B. C., Ho, D., Cutfield, W. S., Vatanen, T., & O'Sullivan, J. M. (2024) · Microbiome · doi:10.1186/s40168-024-01748-6 · Cited by 14
DERNA Enables Pareto Optimal RNA Design
Gu, X., Qi, Y., & El-Kebir, M. (2024) · Journal of Computational Biology · doi:10.1089/cmb.2023.0283 · Cited by 14
MSF-PFP: A Novel Multisource Feature Fusion Model for Protein Function Prediction
Li, X., Qian, Y., Hu, Y., Chen, J., Yue, H., & Deng, L. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c01794 · Cited by 14
Janssen, A. W. F., Holleboom, W. J., Rijkers, D., Louisse, J., Hoekstra, S. A., Schild, S., Vrolijk, M. F., Hoogenboom, L. A. P., & Beekmann, K. (2024) · Frontiers in Toxicology · doi:10.3389/ftox.2024.1347965 · Cited by 14
The WIP6 transcription factor TOO MANY LATERALS specifies vein type in C4 and C3 grass leaves
Vlad, D., Zaidem, M., Perico, C., Sedelnikova, O. V., Bhattacharya, S., & Langdale, J. A. (2024) · Current Biology · doi:10.1016/j.cub.2024.03.007 · Cited by 16
Emergence of an Orphan Nitrogenase Protein Following Atmospheric Oxygenation
Cuevas-Zuviría, B., Garcia, A. K., Rivier, A. J., Rucker, H. R., Carruthers, B. M., & Kaçar, B. (2024) · Molecular Biology and Evolution · doi:10.1093/molbev/msae067 · Cited by 14
GraphKM: machine and deep learning for KM prediction of wildtype and mutant enzymes
He, X. D., & Yan, M. (2024) · BMC Bioinformatics · doi:10.1186/s12859-024-05746-1 · Cited by 14
Sultana, T., Mou, S. I., Chatterjee, D., Faruk, M. O., & Hosen, M. I. (2024) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2024.101703 · Cited by 16
Click, Compute, Create: A Review of Web‐based Tools for Enzyme Engineering
Tripp, A., Braun, M., Wieser, F., Oberdorfer, G., & Lechner, H. (2024) · ChemBioChem · doi:10.1002/cbic.202400092 · Cited by 17
Deciphering the Diversity in Bacterial Transporters That Salvage Queuosine Precursors
Quaiyum, S., Yuan, Y., Kuipers, P. J., Martinelli, M., Jaroch, M., & de Crécy‐Lagard, V. (2024) · Epigenomes · doi:10.3390/epigenomes8020016 · Cited by 13
Cystine-knot peptide inhibitors of HTRA1 bind to a cryptic pocket within the active site region
Li, Y., Wei, Y., Ultsch, M. H., Li, W., Tang, W., Tombling, B. J., Gao, X., Dimitrova, Y. N., Gampe, C. M., Fuhrmann, J., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-48655-w · Cited by 14
Ferrari, R. R., Ricardo, P. C., Dias, F. C., Araujo, N. D. S., Soares, D. O., Zhou, Q., Zhu, C., Coutinho, L. L., Arias, M. C., & Batista, T. M. (2024) · BMC Genomics · doi:10.1186/s12864-024-10502-z · Cited by 15
Tan, J., Xu, Y., Deng, Q., Li, Y., Yin, Y., Liang, X., & Luo, Y. (2024) · Industrial Crops and Products · doi:10.1016/j.indcrop.2024.118960 · Cited by 14
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Radzlin, N., Ali, M. S. M., Goh, K. M., Yaakop, A. S., Zakaria, I. I., & Kahar, U. M. (2024) · AMB Express · doi:10.1186/s13568-024-01722-3 · Cited by 14
Longarela, N. R., Paredes-Ramos, M., & Vilariño, J. M. L. (2024) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2024.2367571 · Cited by 14
Redlich, R., Kowalczyk, A., Tene, M., Sestili, H. H., Foley, K., Saputra, E., Clark, N., Chikina, M., Meyer, W. K., & Pfenning, A. R. (2024) · Molecular Biology and Evolution · doi:10.1093/molbev/msae210 · Cited by 14
Molecular mechanism of condensin I activation by KIF4A
Cutts, E. E., Tetiker, D., Kim, E., & Aragon, L. (2025) · The EMBO Journal · doi:10.1038/s44318-024-00340-w · Cited by 18
Johnson, Z., Anderson, D., Cheung, M. S., & Bohutskyi, P. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1569559 · Cited by 12
CC + : A searchable database of validated coiled coils in PDB structures and AlphaFold2 models
Kumar, P., Petrenas, R., Dawson, W. M., Schweke, H., Levy, E. D., & Woolfson, D. N. (2023) · Protein Science · doi:10.1002/pro.4789 · Cited by 11
“, 20x7 tables for the occurrence of each amino acid at the 7 positions of the heptad repeats, which can be normalized internally or using amino-acid frequencies from Uniprot/Swissprot.(33) In addition, the adjacent drop-down menu and ‘Save’ button allow users to download a flat csv files for the ‘Summary and CC Sequen…”
MethodRamasamy, P., Zuallaert, J., Martens, L., & Vranken, W. F. (2026) · Protein Science · doi:10.1002/pro.70376 · Cited by 15
A conserved mechanism for the retrieval of polyubiquitinated proteins from cilia
Lange, S. M., Bennett, J. A., Eisert, R. J., & Brown, A. (2025) · Cell · doi:10.1016/j.cell.2025.07.043 · Cited by 11
Metadata
- Authors
- The UniProt Consortium, Bateman, A., Martin, M.-J., Orchard, S., Magrane, M., Ahmad, S., Alpi, E., Bowler-Barnett, E. H., Britto, R., Bye-A-Jee, H., Cukura, A., Denny, P., Dogan, T., Ebenezer, T., Fan, J., Garmiri, P., da Costa Gonzales, L. J., Hatton-Ellis, E., Hussein, A., Ignatchenko, A., Insana, G., Ishtiaq, R., Joshi, V., Jyothi, D., Kandasaamy, S., Lock, A., Luciani, A., Lugaric, M., Luo, J., Lussi, Y., MacDougall, A., Madeira, F., Mahmoudy, M., Mishra, A., Moulang, K., Nightingale, A., Pundir, S., Qi, G., Raj, S., Raposo, P., Rice, D. L., Saidi, R., Santos, R., Speretta, E., Stephenson, J., Totoo, P., Turner, E., Tyagi, N., Vasudev, P., Warner, K., Watkins, X., Zaru, R., Zellner, H., Bridge, A. J., Aimo, L., Argoud-Puy, G., Auchincloss, A. H., Axelsen, K. B., Bansal, P., Baratin, D., Batista Neto, T. M., Blatter, M.-C., Bolleman, J. T., Boutet, E., Breuza, L., Gil, B. C., Casals-Casas, C., Echioukh, K. C., Coudert, E., Cuche, B., de Castro, E., Estreicher, A., Famiglietti, M. L., Feuermann, M., Gasteiger, E., Gaudet, P., Gehant, S., Gerritsen, V., Gos, A., Gruaz, N., Hulo, C., Hyka-Nouspikel, N., Jungo, F., Kerhornou, A., Le Mercier, P., Lieberherr, D., Masson, P., Morgat, A., Muthukrishnan, V., Paesano, S., Pedruzzi, I., Pilbout, S., Pourcel, L., Poux, S., Pozzato, M., Pruess, M., Redaschi, N., Rivoire, C., Sigrist, C. J. A., Sonesson, K., Sundaram, S., Wu, C. H., Arighi, C. N., Arminski, L., Chen, C., Chen, Y., Huang, H., Laiho, K., McGarvey, P., Natale, D. A., Ross, K., Vinayaka, C. R., Wang, Q., Wang, Y., & Zhang, J.
- ORCID
- Bateman, Alex
- Martin, Maria-Jesus
- Orchard, Sandra
- Magrane, Michele
- Ahmad, Shadab
- Alpi, Emanuele
- Bowler-Barnett, Emily H
- Britto, Ramona
- Denny, Paul
- Ebenezer, ThankGod
- Fan, Jun
- Garmiri, Penelope
- Hatton-Ellis, Emma
- Hussein, Abdulrahman
- Ignatchenko, Alexandr
- Insana, Giuseppe
- Ishtiaq, Rizwan
- Joshi, Vishal
- Jyothi, Dushyanth
- Kandasaamy, Swaathi
- Lock, Antonia
- Luo, Jie
- Lussi, Yvonne
- Nightingale, Andrew
- Pundir, Sangya
- Qi, Guoying
- Raj, Shriya
- Raposo, Pedro
- Rice, Daniel L
- Saidi, Rabie
- Santos, Rafael
- Speretta, Elena
- Stephenson, James
- Totoo, Prabhat
- Tyagi, Nidhi
- Warner, Kate
- Watkins, Xavier
- Zaru, Rossana
- Bridge, Alan J
- Aimo, Lucila
- Auchincloss, Andrea H
- Axelsen, Kristian B
- Bansal, Parit
- Baratin, Delphine
- Blatter, Marie-Claude
- Bolleman, Jerven T
- Boutet, Emmanuel
- Breuza, Lionel
- Gil, Blanca Cabrera
- Coudert, Elisabeth
- Cuche, Beatrice
- de Castro, Edouard
- Estreicher, Anne
- Famiglietti, Maria L
- Feuermann, Marc
- Gasteiger, Elisabeth
- Gaudet, Pascale
- Gos, Arnaud
- Hulo, Chantal
- Jungo, Florence
- Kerhornou, Arnaud
- Lieberherr, Damien
- Masson, Patrick
- Morgat, Anne
- Muthukrishnan, Venkatesh
- Pedruzzi, Ivo
- Pourcel, Lucille
- Poux, Sylvain
- Pozzato, Monica
- Redaschi, Nicole
- Rivoire, Catherine
- Sigrist, Christian J A
- Sundaram, Shyamala
- Wu, Cathy H
- Arighi, Cecilia N
- Chen, Chuming
- Huang, Hongzhan
- McGarvey, Peter
- Natale, Darren A
- Ross, Karen
- Wang, Qinghua
- Wang, Yuqi
- Zhang, Jian
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2022-11-21
- Volume
- 51
- Issue
- D1
- Pages
- D523-D531
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC9825514
- OpenAlex
- W4309506674
- Cited by
- 7,210
- References
- 41
- Citations by year
- 2026: 1511 · 2025: 2294 · 2024: 2343 · 2023: 887 · 2022: 78
- FWCI
- 464.54
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Nucleic Acids Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Human Genome Research Institute (OD/DPCPSI/ODSS)
- National Institute of Allergy and Infectious Diseases
- National Institute on Aging
- National Institute of General Medical Sciences
- National Institute of Diabetes and Digestive and Kidney Diseases
- National Eye Institute
- National Cancer Institute
- National Heart, Lung, and Blood Institute
- National Institutes of Health (U24HG007822)
- NHGRI NIH (HG002273)
- Biotechnology and Biological Sciences Research Council (BB/T010541/1, BB/S01781X/1)
- Open Targets
- SERI
- European Molecular Biology Laboratory
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
- Keywords
- protein sequence annotation, reference proteomes, machine learning annotation, AlphaFold protein structure, subcellular localization, data pipelines
- MeSH terms
- Machine Learning, Amino Acid Sequence, Proteome, Databases, Protein, Knowledge Bases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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