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UniProtKB - A0A0K8P8E7 (MHETH_IDESA)

Entry version 27 (10 Feb 2021)
Sequence version 1 (11 Nov 2015)
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Protein

Mono(2-hydroxyethyl) terephthalate hydrolase

Gene

ISF6_0224

Organism
Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6)
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

Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with PETase to depolymerize PET. Catalyzes the hydrolysis of mono(2-hydroxyethyl) terephthalate (MHET) into its two environmentally benign monomers, terephthalate and ethylene glycol. Does not show activity against PET, bis(hydroxyethyl) terephthalate (BHET), pNP-aliphatic esters or typical aromatic ester compounds catalyzed by the tannase family enzymes, such as ethyl gallate and ethyl ferulate.1 Publication

Miscellaneous

The calcium ion is located far from the active site and appears to have a role in stabilization of the lid domain.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

kcat is 31 sec(-1) for the hydrolysis of mono(2-hydroxyethyl) terephthalate (at pH 7 and 30 degrees Celsius).1 Publication
  1. KM=7.3 µM for mono(2-hydroxyethyl) terephthalate (at pH 7 and 30 degrees Celsius)1 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 sitei1324-[(2-hydroxyethoxy)carbonyl]benzoate; via amide nitrogen1 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 sitei225Acyl-ester intermediate1 Publication1
    Binding sitei2264-[(2-hydroxyethoxy)carbonyl]benzoate; via amide nitrogen1 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 bindingi304Calcium1 Publication1
    Metal bindingi307Calcium1 Publication1
    Metal bindingi309Calcium; via carbonyl oxygen1 Publication1
    Metal bindingi311Calcium1 Publication1
    Metal bindingi313Calcium; via carbonyl oxygen1 Publication1
    Binding sitei4114-[(2-hydroxyethoxy)carbonyl]benzoate1 Publication1
    Binding sitei4164-[(2-hydroxyethoxy)carbonyl]benzoate1 Publication1
    Active sitei492Charge relay system1 Publication1
    Active sitei528Charge relay system1 Publication1
    Binding sitei5284-[(2-hydroxyethoxy)carbonyl]benzoate1 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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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, Serine esterase
    LigandCalcium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:MONOMER-19899

    Protein family/group databases

    ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

    More...    ESTHERi    		idesa-mheth, Tannase

    <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:
    Mono(2-hydroxyethyl) terephthalate hydrolase1 Publication (EC:3.1.1.1021 Publication)
    Short name:
    MHET hydrolase1 Publication
    Short name:
    MHETase1 Publication
    <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
    ORF Names:ISF6_0224Imported
    <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>OrganismiIdeonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6)
    <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 identifieri1547922 [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 lineageiBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Ideonella
    <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
    • UP000037660 <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: Unassembled WGS sequence

    <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

    GO - Cellular componenti

    Complete GO annotation on QuickGO ...

    Keywords - Cellular componenti

    Cell outer membrane, Membrane

    <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

    <p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Has potential for application in environmental remediation and biological recycling of PET waste products.1 Publication

    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>Mutagenesisi225S → A: Loss of catalytic activity towards MHET. 1 Publication1
    Mutagenesisi411R → A or Q: Almost complete loss of catalytic activity towards MHET. 1 Publication1
    Mutagenesisi416S → A: Gains a low activity towards BHET (bis-(2-hydroxyethyl) terephthalate); when associated with N-424. 1 Publication1
    Mutagenesisi424F → N: Gains a low activity towards BHET (bis-(2-hydroxyethyl) terephthalate); when associated with A-416. 1 Publication1
    Mutagenesisi492D → A: Loss of catalytic activity towards MHET. 1 Publication1
    Mutagenesisi528H → A: Loss of catalytic activity towards MHET. 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17PROSITE-ProRule annotationAdd BLAST17
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_500551385918 – 603Mono(2-hydroxyethyl) terephthalate hydrolaseAdd BLAST586

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi18N-palmitoyl cysteinePROSITE-ProRule annotation1
    Lipidationi18S-diacylglycerol cysteinePROSITE-ProRule annotation1
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi51 ↔ 921 Publication
    Disulfide bondi224 ↔ 5291 Publication
    Disulfide bondi303 ↔ 3201 Publication
    Disulfide bondi340 ↔ 3481 Publication
    Disulfide bondi577 ↔ 5991 Publication

    Keywords - PTMi

    Disulfide bond, Lipoprotein, Palmitate

    <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

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Highly up-regulated during growth on PET film.1 Publication

    <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

    1603
    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    		A0A0K8P8E7

    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

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi25 – 44Pro-richPROSITE-ProRule annotationAdd BLAST20

    <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 tannase family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR029058, AB_hydrolase
    IPR011118, Tannase/feruloyl_esterase

    The PANTHER Classification System

    More...    PANTHERi    		PTHR33938, PTHR33938, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF07519, Tannase, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF53474, SSF53474, 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.

    <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 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.

    A0A0K8P8E7-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MQTTVTTMLL ASVALAACAG GGSTPLPLPQ QQPPQQEPPP PPVPLASRAA 
            60         70         80         90        100
    CEALKDGNGD MVWPNAATVV EVAAWRDAAP ATASAAALPE HCEVSGAIAK 
           110        120        130        140        150
    RTGIDGYPYE IKFRLRMPAE WNGRFFMEGG SGTNGSLSAA TGSIGGGQIA 
           160        170        180        190        200
    SALSRNFATI ATDGGHDNAV NDNPDALGTV AFGLDPQARL DMGYNSYDQV 
           210        220        230        240        250
    TQAGKAAVAR FYGRAADKSY FIGCSEGGRE GMMLSQRFPS HYDGIVAGAP 
           260        270        280        290        300
    GYQLPKAGIS GAWTTQSLAP AAVGLDAQGV PLINKSFSDA DLHLLSQAIL 
           310        320        330        340        350
    GTCDALDGLA DGIVDNYRAC QAAFDPATAA NPANGQALQC VGAKTADCLS 
           360        370        380        390        400
    PVQVTAIKRA MAGPVNSAGT PLYNRWAWDA GMSGLSGTTY NQGWRSWWLG 
           410        420        430        440        450
    SFNSSANNAQ RVSGFSARSW LVDFATPPEP MPMTQVAARM MKFDFDIDPL 
           460        470        480        490        500
    KIWATSGQFT QSSMDWHGAT STDLAAFRDR GGKMILYHGM SDAAFSALDT 
           510        520        530        540        550
    ADYYERLGAA MPGAAGFARL FLVPGMNHCS GGPGTDRFDM LTPLVAWVER 
           560        570        580        590        600
    GEAPDQISAW SGTPGYFGVA ARTRPLCPYP QIARYKGSGD INTEANFACA 

    APP
    Length:603
    Mass (Da):63,103
    Last modified:November 11, 2015 - 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:iE9317BE82796A187
    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
    		BBYR01000104 Genomic DNA Translation: GAP38911.1

    NCBI Reference Sequences

    More...    RefSeqi    		WP_054022745.1, NZ_BBYR01000104.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		GAP38911; GAP38911; ISF6_0224

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ag:GAP38911

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Protein Spotlight

    Of plastic and men - Issue 181 of July 2016

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		BBYR01000104 Genomic DNA Translation: GAP38911.1
    RefSeqiWP_054022745.1, NZ_BBYR01000104.1

    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
    6JTTX-ray2.51A/B/C17-603[»]
    6JTUX-ray2.10A/B/C17-603[»]
    6QG9X-ray2.05A/B/C/D/E/F/G/H/I/J20-603[»]
    6QGAX-ray2.10A/B/C/D/E/F20-603[»]
    6QGBX-ray2.20A/B/C/D/E/F20-603[»]
    6QZ1X-ray1.70A40-603[»]
    6QZ2X-ray1.90A/B/C/D/E/F/G/H/I/J1-603[»]
    6QZ3X-ray1.60A1-603[»]
    6QZ4X-ray1.80A/B1-603[»]
    SMRiA0A0K8P8E7
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein family/group databases

    ESTHERiidesa-mheth, Tannase

    Genome annotation databases

    EnsemblBacteriaiGAP38911; GAP38911; ISF6_0224
    KEGGiag:GAP38911

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-19899

    Family and domain databases

    InterProiView protein in InterPro
    IPR029058, AB_hydrolase
    IPR011118, Tannase/feruloyl_esterase
    PANTHERiPTHR33938, PTHR33938, 1 hit
    PfamiView protein in Pfam
    PF07519, Tannase, 1 hit
    SUPFAMiSSF53474, SSF53474, 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 nameiMHETH_IDESA
    <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: A0A0K8P8E7
    <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: May 11, 2016
    Last sequence update: November 11, 2015
    Last modified: February 10, 2021
    This is version 27 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
    3. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    UniProt is an ELIXIR core data resource
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