Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3-dehydroquinate dehydratase

Gene

aroQ

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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

Catalyzes a trans-dehydration via an enolate intermediate.By similarity

<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 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=1100 µM for 3-dehydroquinate (at pH 8 and 25 degrees Celsius)

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: chorismate biosynthesis

    This protein is involved in step 3 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.
    Proteins known to be involved in the 7 steps of the subpathway in this organism are:
    1. Phospho-2-dehydro-3-deoxyheptonate aldolase (SCO3210), Phospho-2-dehydro-3-deoxyheptonate aldolase (aroH)
    2. 3-dehydroquinate synthase (aroB)
    3. 3-dehydroquinate dehydratase (aroQ)
    4. no protein annotated in this organism
    5. Shikimate kinase (aroK)
    6. 3-phosphoshikimate 1-carboxyvinyltransferase 2 (aroA2), 3-phosphoshikimate 1-carboxyvinyltransferase 1 (aroA1)
    7. Chorismate synthase (aroC)
    This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei24Transition state stabilizer1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei29Proton acceptor1
    <p>This subsection of the ‘Function’ 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 sitei80Substrate1
    Binding sitei86Substrate1
    Binding sitei93Substrate1
    Active sitei107Proton donor1
    Binding sitei118Substrate1

    <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 functionLyase
    Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.2.1.10 5998

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P15474

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00053;UER00086

    <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:
    3-dehydroquinate dehydratase (EC:4.2.1.10)
    Short name:
    3-dehydroquinase
    Alternative name(s):
    Type II DHQase
    <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:aroQ
    Ordered Locus Names:SCO1961
    ORF Names:SCC54.21c
    <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>OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    <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 identifieri100226 [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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    <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
    • UP000001973 <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

    <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>Mutagenesisi24R → A: Reduces Kcat 30000-fold. Reduces KM for 3-dehydroquinate 6-fold. 1 Publication1
    Mutagenesisi24R → K: Reduces Kcat 2700-fold. Reduces KM for 3-dehydroquinate 4-fold. 1 Publication1
    Mutagenesisi24R → Q: Reduces Kcat 3100-fold. Reduces KM for 3-dehydroquinate 8-fold. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5276

    Drug and drug target database

    More...
    DrugBanki
    DB02786 2-Anhydro-3-Fluoro-Quinic Acid
    DB04347 3-Dehydroshikimate

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00001599302 – 1573-dehydroquinate dehydrataseAdd BLAST156

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P15474

    <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

    Homododecamer.3 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    100226.SCO1961

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P15474

    <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

    1157
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P15474

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

    More...
    SMRi
    P15474

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P15474

    <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

    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>Regioni108 – 109Substrate binding2

    <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 type-II 3-dehydroquinase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108Z38 Bacteria
    COG0757 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000217278

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P15474

    KEGG Orthology (KO)

    More...
    KOi
    K03786

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    CAGIVIN

    Database of Orthologous Groups

    More...
    OrthoDBi
    POG091H03XJ

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P15474

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00466 DHQase_II, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.9100, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00169 AroQ, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001874 DHquinase_II
    IPR018509 DHquinase_II_CS
    IPR036441 DHquinase_II_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR21272 PTHR21272, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01220 DHquinase_II, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF001399 DHquinase_II, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52304 SSF52304, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01088 aroQ, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01029 DEHYDROQUINASE_II, 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>.<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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P15474-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPRSLANAPI MILNGPNLNL LGQRQPEIYG SDTLADVEAL CVKAAAAHGG
    60 70 80 90 100
    TVDFRQSNHE GELVDWIHEA RLNHCGIVIN PAAYSHTSVA ILDALNTCDG
    110 120 130 140 150
    LPVVEVHISN IHQREPFRHH SYVSQRADGV VAGCGVQGYV FGVERIAALA

    GAGSARA
    Length:157
    Mass (Da):16,682
    Last modified:January 23, 2007 - v3
    <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:i61D9F95C7E2C67EB
    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
    AJ001493 Genomic DNA Translation: CAA04787.1
    AL939110 Genomic DNA Translation: CAB38151.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S08196
    T35990

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_626225.1, NC_003888.3
    WP_003976858.1, NC_003888.3

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAB38151; CAB38151; CAB38151

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    1097395

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sco:SCO1961

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|100226.15.peg.1987

    <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
    AJ001493 Genomic DNA Translation: CAA04787.1
    AL939110 Genomic DNA Translation: CAB38151.1
    PIRiS08196
    T35990
    RefSeqiNP_626225.1, NC_003888.3
    WP_003976858.1, NC_003888.3

    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
    1D0IX-ray1.80A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    1GTZX-ray1.60A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    1GU0X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    1GU1X-ray1.80A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    1V1JX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    2BT4X-ray1.70A/B/C/D/E/F/G/H/I/J/K/L1-157[»]
    2CJFX-ray1.95A/B/C/D/E/F/G/H/I/J/K/L1-157[»]
    ProteinModelPortaliP15474
    SMRiP15474
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi100226.SCO1961

    Chemistry databases

    BindingDBiP15474
    ChEMBLiCHEMBL5276
    DrugBankiDB02786 2-Anhydro-3-Fluoro-Quinic Acid
    DB04347 3-Dehydroshikimate

    Proteomic databases

    PRIDEiP15474

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB38151; CAB38151; CAB38151
    GeneIDi1097395
    KEGGisco:SCO1961
    PATRICifig|100226.15.peg.1987

    Phylogenomic databases

    eggNOGiENOG4108Z38 Bacteria
    COG0757 LUCA
    HOGENOMiHOG000217278
    InParanoidiP15474
    KOiK03786
    OMAiCAGIVIN
    OrthoDBiPOG091H03XJ
    PhylomeDBiP15474

    Enzyme and pathway databases

    UniPathwayi
    UPA00053;UER00086

    BRENDAi4.2.1.10 5998
    SABIO-RKiP15474

    Miscellaneous databases

    EvolutionaryTraceiP15474

    Protein Ontology

    More...
    PROi
    PR:P15474

    Family and domain databases

    CDDicd00466 DHQase_II, 1 hit
    Gene3Di3.40.50.9100, 1 hit
    HAMAPiMF_00169 AroQ, 1 hit
    InterProiView protein in InterPro
    IPR001874 DHquinase_II
    IPR018509 DHquinase_II_CS
    IPR036441 DHquinase_II_sf
    PANTHERiPTHR21272 PTHR21272, 1 hit
    PfamiView protein in Pfam
    PF01220 DHquinase_II, 1 hit
    PIRSFiPIRSF001399 DHquinase_II, 1 hit
    SUPFAMiSSF52304 SSF52304, 1 hit
    TIGRFAMsiTIGR01088 aroQ, 1 hit
    PROSITEiView protein in PROSITE
    PS01029 DEHYDROQUINASE_II, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiAROQ_STRCO
    <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: P15474
    Secondary accession number(s): O33608
    <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: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 143 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again