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Entry version 111 (26 Feb 2020)
Sequence version 1 (20 Dec 2005)
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Protein

Thiamine-monophosphate kinase

Gene

thiL

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

Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. Cannot use thiamine as substrate. Is highly specific for ATP as phosphate donor.2 Publications

Miscellaneous

Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Is markedly activated by the monovalent cations K+, NH4+, and Rb+. Is significantly inhibited by ADP, AMP, p-chloromercuribenzoate, N-ethylmaleimide, pyrophosphate, and EDTA.1 Publication

<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=1.1 µM for thiamine-monophosphate1 Publication
  2. KM=270 µM for ATP1 Publication

    pH dependencei

    Optimum pH is about 8.0.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: thiamine diphosphate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes thiamine diphosphate from thiamine phosphate.
    Proteins known to be involved in this subpathway in this organism are:
    1. Thiamine-monophosphate kinase (thiL)
    This subpathway is part of the pathway thiamine diphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes thiamine diphosphate from thiamine phosphate, the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi30Magnesium 3By similarity1
    Metal bindingi30Magnesium 4; via carbonyl oxygenBy similarity1
    Metal bindingi45Magnesium 4By similarity1
    Metal bindingi46Magnesium 1; via carbonyl oxygenBy similarity1
    Metal bindingi47Magnesium 1By similarity1
    Metal bindingi47Magnesium 2By similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei54SubstrateBy similarity1
    Metal bindingi75Magnesium 2By similarity1
    Metal bindingi75Magnesium 3By similarity1
    Metal bindingi75Magnesium 4By similarity1
    Metal bindingi122Magnesium 1By similarity1
    Binding sitei146ATPBy similarity1
    Metal bindingi212Magnesium 3By similarity1
    Binding sitei214ATPBy similarity1
    Metal bindingi215Magnesium 5By similarity1
    Binding sitei263SubstrateBy similarity1
    Binding sitei319SubstrateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi121 – 122ATPBy similarity2

    <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

    • ATP binding Source: EcoCyc
    • magnesium ion binding Source: EcoCyc
    • metal ion binding Source: EcoCyc
    • thiamine-phosphate kinase activity Source: UniProtKB

    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 functionKinase, Transferase
    Biological processThiamine biosynthesis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:THI-P-KIN-MONOMER
    ECOL316407:JW0407-MONOMER
    MetaCyc:THI-P-KIN-MONOMER

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

    More...
    UniPathwayi
    UPA00060;UER00142

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Thiamine-monophosphate kinase (EC:2.7.4.16)
    Short name:
    TMP kinase
    Short name:
    Thiamine-phosphate kinase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:thiL
    Ordered Locus Names:b0417, JW0407
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 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_00000961941 – 325Thiamine-monophosphate kinaseAdd BLAST325

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0AGG0

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

    More...
    PaxDbi
    P0AGG0

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0AGG0

    <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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4259339, 26 interactors
    851709, 6 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-2140 IscS-ThiL complex

    Protein interaction database and analysis system

    More...
    IntActi
    P0AGG0, 15 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b0417

    <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

    3D structure databases

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

    More...
    SMRi
    P0AGG0

    Database of comparative protein structure models

    More...
    ModBasei
    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

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CG2 Bacteria
    COG0611 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_046964_3_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0AGG0

    KEGG Orthology (KO)

    More...
    KOi
    K00946

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0AGG0

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd02194 ThiL, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.1330.10, 1 hit
    3.90.650.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_02128 TMP_kinase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR010918 PurM-like_C_dom
    IPR036676 PurM-like_C_sf
    IPR016188 PurM-like_N
    IPR036921 PurM-like_N_sf
    IPR006283 ThiL

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR30270 PTHR30270, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00586 AIRS, 1 hit
    PF02769 AIRS_C, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF005303 Thiam_monoph_kin, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55326 SSF55326, 1 hit
    SSF56042 SSF56042, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01379 thiL, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P0AGG0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MACGEFSLIA RYFDRVRSSR LDVELGIGDD CALLNIPEKQ TLAISTDTLV
    60 70 80 90 100
    AGNHFLPDID PADLAYKALA VNLSDLAAMG ADPAWLTLAL TLPDVDEAWL
    110 120 130 140 150
    ESFSDSLFDL LNYYDMQLIG GDTTRGPLSM TLGIHGFVPM GRALTRSGAK
    160 170 180 190 200
    PGDWIYVTGT PGDSAAGLAI LQNRLQVADA KDADYLIKRH LRPSPRILQG
    210 220 230 240 250
    QALRDLANSA IDLSDGLISD LGHIVKASDC GARIDLALLP FSDALSRHVE
    260 270 280 290 300
    PEQALRWALS GGEDYELCFT VPELNRGALD VALGHLGVPF TCIGQMTADI
    310 320
    EGLCFIRDGE PVTLDWKGYD HFATP
    Length:325
    Mass (Da):35,071
    Last modified:December 20, 2005 - 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:i9955DCE2D8CFFB8F
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti254A → E in BAA21778 (Ref. 1) Curated1

    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
    D17333 Genomic DNA Translation: BAA21778.1
    U82664 Genomic DNA Translation: AAB40173.1
    U00096 Genomic DNA Translation: AAC73520.1
    AP009048 Genomic DNA Translation: BAE76197.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A64771

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_414951.1, NC_000913.3
    WP_000742109.1, NZ_SSZK01000009.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC73520; AAC73520; b0417
    BAE76197; BAE76197; BAE76197

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    947387

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW0407
    eco:b0417

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.1860

    <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
    D17333 Genomic DNA Translation: BAA21778.1
    U82664 Genomic DNA Translation: AAB40173.1
    U00096 Genomic DNA Translation: AAC73520.1
    AP009048 Genomic DNA Translation: BAE76197.1
    PIRiA64771
    RefSeqiNP_414951.1, NC_000913.3
    WP_000742109.1, NZ_SSZK01000009.1

    3D structure databases

    SMRiP0AGG0
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi4259339, 26 interactors
    851709, 6 interactors
    ComplexPortaliCPX-2140 IscS-ThiL complex
    IntActiP0AGG0, 15 interactors
    STRINGi511145.b0417

    Proteomic databases

    jPOSTiP0AGG0
    PaxDbiP0AGG0
    PRIDEiP0AGG0

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    947387

    Genome annotation databases

    EnsemblBacteriaiAAC73520; AAC73520; b0417
    BAE76197; BAE76197; BAE76197
    GeneIDi947387
    KEGGiecj:JW0407
    eco:b0417
    PATRICifig|1411691.4.peg.1860

    Organism-specific databases

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

    More...
    EchoBASEi
    EB4149

    Phylogenomic databases

    eggNOGiENOG4105CG2 Bacteria
    COG0611 LUCA
    HOGENOMiCLU_046964_3_0_6
    InParanoidiP0AGG0
    KOiK00946
    PhylomeDBiP0AGG0

    Enzyme and pathway databases

    UniPathwayiUPA00060;UER00142
    BioCyciEcoCyc:THI-P-KIN-MONOMER
    ECOL316407:JW0407-MONOMER
    MetaCyc:THI-P-KIN-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P0AGG0

    Family and domain databases

    CDDicd02194 ThiL, 1 hit
    Gene3Di3.30.1330.10, 1 hit
    3.90.650.10, 1 hit
    HAMAPiMF_02128 TMP_kinase, 1 hit
    InterProiView protein in InterPro
    IPR010918 PurM-like_C_dom
    IPR036676 PurM-like_C_sf
    IPR016188 PurM-like_N
    IPR036921 PurM-like_N_sf
    IPR006283 ThiL
    PANTHERiPTHR30270 PTHR30270, 1 hit
    PfamiView protein in Pfam
    PF00586 AIRS, 1 hit
    PF02769 AIRS_C, 1 hit
    PIRSFiPIRSF005303 Thiam_monoph_kin, 1 hit
    SUPFAMiSSF55326 SSF55326, 1 hit
    SSF56042 SSF56042, 1 hit
    TIGRFAMsiTIGR01379 thiL, 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 nameiTHIL_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: P0AGG0
    Secondary accession number(s): O32380, P77785, Q2MC09
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: February 26, 2020
    This is version 111 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

    Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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