Cited by 6,148Genomics and Phylogenetic StudiesEnzyme Structure and FunctionBioinformatics and Genomic Networks

Pfam: the protein families database

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Finn, Robert D., Bateman, Alex, Clements, Jody, Coggill, Penelope, Eberhardt, Ruth Y., Eddy, Sean R., Heger, Andreas, Hetherington, Kirstie +5 more·2014·Nucleic Acids Research

Abstract

Pfam, available via servers in the UK (http://pfam.sanger.ac.uk/) and the USA (http://pfam.janelia.org/), is a widely used database of protein families, containing 14 831 manually curated entries in the current release, version 27.0. Since the last update article 2 years ago, we have generated 1182 new families and maintained sequence coverage of the UniProt Knowledgebase (UniProtKB) at nearly 80%, despite a 50% increase in the size of the underlying sequence database. Since our 2012 article describing Pfam, we have also undertaken a comprehensive review of the features that are provided by Pfam over and above the basic family data. For each feature, we determined the relevance, computational burden, usage statistics and the functionality of the feature in a website context. As a consequence of this review, we have removed some features, enhanced others and developed new ones to meet the changing demands of computational biology. Here, we describe the changes to Pfam content. Notably, we now provide family alignments based on four different representative proteome sequence data sets and a new interactive DNA search interface. We also discuss the mapping between Pfam and known 3D structures.

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  • Because schizophrenia is under strong selection, ultra-rare variants of large effect are expected to be frequently de novo or of very recent origin and to contribute to risk in only a fraction of diagnosed patients.

    “Because schizophrenia as a trait is under strong selection39–41, we expect that URVs of large effect to be frequently de novo or of very recent origin and contribute to risk in only a fraction of diagnosed patients.”

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Authors
Finn, R. D., Bateman, A., Clements, J., Coggill, P., Eberhardt, R. Y., Eddy, S. R., Heger, A., Hetherington, K., Holm, L., Mistry, J., Sonnhammer, E. L. L., Tate, J., & Punta, M.
Affiliations
European Bioinformatics Institute (GB)
Corresponding author
Finn, Robert D.
Venue
Nucleic Acids Research
Published
2013-11-27
Volume
42
Issue
D1
Pages
D222-D230
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
OpenAlex
W2147526198
Cited by
6,148
References
44
Citations by year
2026: 177 · 2025: 290 · 2024: 436 · 2023: 417 · 2022: 482 · 2021: 598 · 2020: 472 · 2019: 471 · 2018: 465 · 2017: 537 · 2016: 797 · 2015: 753 · 2014: 235 · 2013: 5 · 2012: 1
FWCI
267.20
Type
journal article
Language
en
Open access
Locations
  • Nucleic Acids Research (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Työväentutkimus Vuosikirja (submittedVersion)
  • Zenodo (CERN European Organization for Nuclear Research)
Funders
  • Howard Hughes Medical Institute
  • Wellcome Trust (WT077044/Z/05/Z)
  • European Bioinformatics Institute
  • European Molecular Biology Laboratory
  • Biotechnology and Biological Sciences Research Council (BB/L024136/1, BB/F010435/1)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
Keywords
Pfam, protein families, protein family databases, sequence alignment
MeSH terms
Protein Conformation, Proteins, Sequence Alignment, Sequence Analysis, DNA, Internet, Sequence Analysis, Protein, Proteome, Databases, Protein, Intrinsically Disordered Proteins

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