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Entry version 139 (11 Dec 2019)
Sequence version 1 (01 Feb 1997)
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Protein

CTP pyrophosphohydrolase

Gene

nudG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Hydrolase with a preference for pyrimidine substrates. Has high activity with 5-methyl-dCTP, and much lower activity with CTP, dCTP, 5-hydroxy-dCTP, 2-hydroxy-dATP and 8-hydroxy-dGTP.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+2 Publications, Mn2+2 PublicationsNote: Divalent metal ions. Mg2+ or Mn2+.2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.028 mM for 5-methyl-dCTP2 Publications
  2. KM=0.027 mM for 2-hydroxy-dATP2 Publications
  3. KM=0.41 mM for 8-hydroxy-dGTP2 Publications
  4. KM=0.99 mM for dCTP2 Publications

    pH dependencei

    Optimum pH is 8.5-9.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei72SubstrateCurated1
    Binding sitei118SubstrateCurated1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase
    LigandMagnesium, Manganese

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:G6954-MONOMER
    ECOL316407:JW1748-MONOMER
    MetaCyc:G6954-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.6.1.65 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P77788

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    CTP pyrophosphohydrolase (EC:3.6.1.654 Publications)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:nudG
    Synonyms:ynjG
    Ordered Locus Names:b1759, JW1748
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi33E → A or Q: Increases enzyme activity with 2-hydroxy-ATP. Decreases enzyme activity with dCTP, 5-methyl-dCTP and 8-hydroxy-ATP. 1 Publication1
    Mutagenesisi33E → D: Decreases enzyme activity with 2-hydroxy-ATP, dCTP, 5-dmethyl-CTP and 8-hydroxy-ATP. 1 Publication1
    Mutagenesisi36G → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi37G → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi38K → A or R: Strongly reduces enzyme activity with dCTP, and to a lesser degree with 5-methyl-dCTP. 1 Publication1
    Mutagenesisi43E → A: Abolishes enzyme activity with dCTP and reduces enzyme activity with 5-methyl-dCTP. 1 Publication1
    Mutagenesisi51R → A: Abolishes enzyme activity with dCTP. Nearly abolishes enzyme activity with 5-methyl-dCTP. 1 Publication1
    Mutagenesisi52E → A, D or Q: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi53L → A: Reduces enzyme activity. 1 Publication1
    Mutagenesisi55E → A: Abolishes enzyme activity with dCTP and reduces enzyme activity with 5-methyl-dCTP. 1 Publication1
    Mutagenesisi55E → D or Q: Abolishes enzyme activity with dCTP and reduces enzyme activity with 5-methyl-dCTP. 1 Publication1
    Mutagenesisi56E → A, D or Q: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi72R → A: Strongly decreases the activity with 2-hydroxy-ATP. 1 Publication1
    Mutagenesisi77R → A: No effect. 1 Publication1
    Mutagenesisi118D → A or N: Abolishes enzyme activity with 2-hydroxy-ATP. No effect on activity with dCTP, 5-methyl-dCTP and 8-hydroxy-ATP. 1 Publication1
    Mutagenesisi118D → A: Abolishes enzyme activity with dCTP and 2-hydroxy-ATP and decreases activity with 5-methyl-dCTP. Increases activity with 8-hydroxy-ATP. 1 Publication1
    Mutagenesisi118D → E: Increases the activity with 2-hydroxy-ATP. Strongly decreases activity with 8-hydroxy-ATP. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000569901 – 135CTP pyrophosphohydrolaseAdd BLAST135

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P77788

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P77788

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.

    1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    P038132EBI-545184,EBI-545190

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4260320, 120 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-10376N

    Protein interaction database and analysis system

    More...
    IntActi
    P77788, 3 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b1759

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1135
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P77788

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 127Nudix hydrolasePROSITE-ProRule annotationAdd BLAST126

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni34 – 39Substrate bindingCurated6

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi37 – 58Nudix boxAdd BLAST22

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the Nudix hydrolase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105M6F Bacteria
    COG0494 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000261967

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P77788

    KEGG Orthology (KO)

    More...
    KOi
    K08320

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P77788

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR020476 Nudix_hydrolase
    IPR015797 NUDIX_hydrolase-like_dom_sf
    IPR020084 NUDIX_hydrolase_CS
    IPR000086 NUDIX_hydrolase_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00293 NUDIX, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00502 NUDIXFAMILY

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55811 SSF55811, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51462 NUDIX, 1 hit
    PS00893 NUDIX_BOX, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P77788-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKMIEVVAAI IERDGKILLA QRPAQSDQAG LWEFAGGKVE PDESQRQALV
    60 70 80 90 100
    RELREELGIE ATVGEYVASH QREVSGRIIH LHAWHVPDFH GTLQAHEHQA
    110 120 130
    LVWCSPEEAL QYPLAPADIP LLEAFMALRA ARPAD
    Length:135
    Mass (Da):15,046
    Last modified:February 1, 1997 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD85D8B3A6532CA82
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    U00096 Genomic DNA Translation: AAC74829.1
    AP009048 Genomic DNA Translation: BAA15549.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    G64935

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_416273.1, NC_000913.3
    WP_000781888.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC74829; AAC74829; b1759
    BAA15549; BAA15549; BAA15549

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946277

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW1748
    eco:b1759

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.496

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA Translation: AAC74829.1
    AP009048 Genomic DNA Translation: BAA15549.1
    PIRiG64935
    RefSeqiNP_416273.1, NC_000913.3
    WP_000781888.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2RRKNMR-A1-135[»]
    SMRiP77788
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4260320, 120 interactors
    DIPiDIP-10376N
    IntActiP77788, 3 interactors
    STRINGi511145.b1759

    Proteomic databases

    PaxDbiP77788
    PRIDEiP77788

    Genome annotation databases

    EnsemblBacteriaiAAC74829; AAC74829; b1759
    BAA15549; BAA15549; BAA15549
    GeneIDi946277
    KEGGiecj:JW1748
    eco:b1759
    PATRICifig|1411691.4.peg.496

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB3765

    Phylogenomic databases

    eggNOGiENOG4105M6F Bacteria
    COG0494 LUCA
    HOGENOMiHOG000261967
    InParanoidiP77788
    KOiK08320
    PhylomeDBiP77788

    Enzyme and pathway databases

    BioCyciEcoCyc:G6954-MONOMER
    ECOL316407:JW1748-MONOMER
    MetaCyc:G6954-MONOMER
    BRENDAi3.6.1.65 2026
    SABIO-RKiP77788

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P77788

    Family and domain databases

    InterProiView protein in InterPro
    IPR020476 Nudix_hydrolase
    IPR015797 NUDIX_hydrolase-like_dom_sf
    IPR020084 NUDIX_hydrolase_CS
    IPR000086 NUDIX_hydrolase_dom
    PfamiView protein in Pfam
    PF00293 NUDIX, 1 hit
    PRINTSiPR00502 NUDIXFAMILY
    SUPFAMiSSF55811 SSF55811, 1 hit
    PROSITEiView protein in PROSITE
    PS51462 NUDIX, 1 hit
    PS00893 NUDIX_BOX, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNUDG_ECOLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P77788
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: February 1, 1997
    Last modified: December 11, 2019
    This is version 139 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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