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Entry version 70 (26 Feb 2020)
Sequence version 2 (14 May 2014)
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Protein

Polyamine deacetylase HDAC10

Gene

hdac10

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
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

Polyamine deacetylase (PDAC), which acts preferentially on N8-acetylspermidine, and also on acetylcadaverine and acetylputrescine (PubMed:28516954). Exhibits attenuated catalytic activity toward N1,N8-diacetylspermidine and very low activity, if any, toward N1-acetylspermidine (PubMed:28516954). Has a very weak lysine deacetylase, if any (PubMed:28516954).1 Publication

Caution

Originally thought to be a histone deacetylase and shown in vitro to have this activity (By similarity). Has also been shown to be involved in MSH2 deacetylation (By similarity). However, protein deacetylase activity is a matter of debate, as 3D structure analysis shows that a glutamate gatekeeper and a sterically constricted active site confer specificity for N8-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. Supporting this observation, has been shown to exhibit only very low activity, if any, towards acetyl-lysine peptide substrates (By similarity).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 '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=90 µM for acetylcadaverine1 Publication
  2. KM=160 µM for acetylputrescine1 Publication
  3. KM=130 µM for N8-acetylspermidine1 Publication
  4. KM=180 µM for N1,N8-diacetylspermidine1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei22SubstrateCombined sources1 Publication1
    Binding sitei94SubstrateCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei137Proton donor/acceptorCombined sources1 Publication1
    <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 bindingi174ZincCombined sources1 Publication1
    Metal bindingi176Zinc; via pros nitrogenCombined sources1 Publication1
    Metal bindingi267ZincCombined sources1 Publication1
    <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>Sitei274Substrate specificity1 Publication1
    Binding sitei307SubstrateCombined sources1 Publication1

    <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
    LigandMetal-binding, Zinc

    <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:
    Polyamine deacetylase HDAC10 (EC:3.5.1.481 Publication, EC:3.5.1.621 Publication)
    Alternative name(s):
    Histone deacetylase 10
    <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:hdac10
    <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>OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
    <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 identifieri7955 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
    <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
    • UP000000437 <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 25

    Organism-specific databases

    Zebrafish Information Network genome database

    More...
    ZFINi
    ZDB-GENE-030131-5464 hdac10

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    <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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi93N → A: No effect on steady-state kinetic parameters. 1 Publication1
    Mutagenesisi94D → A: No effect on steady-state kinetic parameters. 1 Publication1
    Mutagenesisi274E → L: Affects substrate specificity, diminishing N(8)-acetyl-spermidine deacetylase activity by 20-fold and enhancing acetyl-lysine deacetylase activity by about 100-fold. 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_00004460651 – 675Polyamine deacetylase HDAC10Add BLAST675

    Proteomic databases

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

    More...
    PaxDbi
    F1QCV2

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSDARG00000086458 Expressed in mature ovarian follicle and 27 other tissues

    <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

    STRING: functional protein association networks

    More...
    STRINGi
    7955.ENSDARP00000109870

    <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

    1675
    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
    F1QCV2

    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

    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>Motifi23 – 26Substrate specificity1 Publication4

    <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
    KOG1343 Eukaryota
    COG0123 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000160061

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_007727_6_0_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    F1QCV2

    KEGG Orthology (KO)

    More...
    KOi
    K18671

    Database of Orthologous Groups

    More...
    OrthoDBi
    1484694at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    F1QCV2

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF106173

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.800.20, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000286 His_deacetylse
    IPR023801 His_deacetylse_dom
    IPR037138 His_deacetylse_dom_sf
    IPR023696 Ureohydrolase_dom_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00850 Hist_deacetyl, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01270 HDASUPER

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52768 SSF52768, 2 hits

    <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.

    F1QCV2-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MASGSALIFD EEMSRYKLLW TDPACEIEVP ERLTVSYEAL RTHGLAQRCK
    60 70 80 90 100
    AVPVRQATEQ EILLAHSEEY LEAVKQTPGM NVEELMAFSK KYNDVYFHQN
    110 120 130 140 150
    IYHCAKLAAG ATLQLVDSVM KREVRNGMAL VRPPGHHSQR SAANGFCVFN
    160 170 180 190 200
    NVAIAALYAK KNYNLNRILI VDWDVHHGQG IQYCFEEDPS VLYFSWHRYE
    210 220 230 240 250
    HQSFWPNLPE SDYSSVGKGK GSGFNINLPW NKVGMTNSDY LAAFFHVLLP
    260 270 280 290 300
    VAYEFDPELV IVSAGFDSAI GDPEGEMCAL PEIFAHLTHL LMPLAAGKMC
    310 320 330 340 350
    VVLEGGYNLT SLGQSVCQTV HSLLGDPTPR ISGLGTACDS ALESIQNVRN
    360 370 380 390 400
    VQSSYWSSFK HLAQSETNPK RPRLDATNGG PKESSEPASE SNPKKTAQDI
    410 420 430 440 450
    VWPEPLKRMP ASVRTVVVPP PGVELTLPKN CQHSGDISES TAKEVQRIRD
    460 470 480 490 500
    KHFHDLTDQN ILRSLGNIIS VLDRMMRSDE VCNGCVVVSD LSVSVQCALQ
    510 520 530 540 550
    HALTEPAERV LVVYVGDGEL PVKTNDGKVF LVQICTKETE DKCVNRLSLC
    560 570 580 590 600
    LREGESLTAG FMQALLGLIL PVAYEFNPAL VLGIVGETAA KTGLMTVWGH
    610 620 630 640 650
    MTCLIQGLAR GRTLTLLQGY DKDLLELTVS ALSGASISPL GPLRALKPED
    660 670
    VEMMEKQRQR LQERWGLLRC TVSES
    Length:675
    Mass (Da):74,543
    Last modified:May 14, 2014 - v2
    <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:i4DDABEA59E275F36
    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 conflicti154I → F in AAH44446 (Ref. 2) Curated1
    Sequence conflicti548S → T in AAH44446 (Ref. 2) Curated1
    Sequence conflicti586G → E in AAH44446 (Ref. 2) Curated1
    Sequence conflicti593 – 596GLMT → RLMR in AAH44446 (Ref. 2) Curated4
    Sequence conflicti613T → M in AAH44446 (Ref. 2) Curated1
    Sequence conflicti646L → P in AAH44446 (Ref. 2) Curated1
    Sequence conflicti675S → SW in AAH44446 (Ref. 2) 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
    FP102808 Genomic DNA No translation available.
    BC044446 mRNA Translation: AAH44446.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_956069.1, NM_199775.1

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSDART00000127600; ENSDARP00000109870; ENSDARG00000086458

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    327253

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    dre:327253

    <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
    FP102808 Genomic DNA No translation available.
    BC044446 mRNA Translation: AAH44446.1
    RefSeqiNP_956069.1, NM_199775.1

    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
    5TD7X-ray2.85A2-675[»]
    SMRiF1QCV2
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi7955.ENSDARP00000109870

    Proteomic databases

    PaxDbiF1QCV2

    Genome annotation databases

    EnsembliENSDART00000127600; ENSDARP00000109870; ENSDARG00000086458
    GeneIDi327253
    KEGGidre:327253

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    83933
    ZFINiZDB-GENE-030131-5464 hdac10

    Phylogenomic databases

    eggNOGiKOG1343 Eukaryota
    COG0123 LUCA
    GeneTreeiENSGT00940000160061
    HOGENOMiCLU_007727_6_0_1
    InParanoidiF1QCV2
    KOiK18671
    OrthoDBi1484694at2759
    PhylomeDBiF1QCV2
    TreeFamiTF106173

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:F1QCV2

    Gene expression databases

    BgeeiENSDARG00000086458 Expressed in mature ovarian follicle and 27 other tissues

    Family and domain databases

    Gene3Di3.40.800.20, 2 hits
    InterProiView protein in InterPro
    IPR000286 His_deacetylse
    IPR023801 His_deacetylse_dom
    IPR037138 His_deacetylse_dom_sf
    IPR023696 Ureohydrolase_dom_sf
    PfamiView protein in Pfam
    PF00850 Hist_deacetyl, 1 hit
    PRINTSiPR01270 HDASUPER
    SUPFAMiSSF52768 SSF52768, 2 hits

    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 nameiHDA10_DANRE
    <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: F1QCV2
    Secondary accession number(s): Q803K0
    <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: January 16, 2019
    Last sequence update: May 14, 2014
    Last modified: February 26, 2020
    This is version 70 of the entry and version 2 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 programChordata 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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