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Entry version 74 (07 Apr 2021)
Sequence version 2 (01 Oct 2014)
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Protein

Hexose oxidase

Gene

HOX

Organism
Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa)
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 selective oxidation of C1 hydroxyl moieties on mono- and disaccharides with concomitant reduction of molecular oxygen to hydrogen peroxide. This results in the formation of the corresponding lactones, which typically undergo spontaneous hydrolysis. Hexose oxidase is able to oxidize a variety of substrates including D-glucose, D-galactose, maltose, cellobiose, and lactose.

2 Publications

Caution

Was initially reported to use Cu2+ as a cofactor (PubMed:4708670). However, cofactor composition could not be confirmed later (PubMed:9108257), and the discrepancies in the reported characteristics of the enzyme were suggested to originate from the characterization of a contaminating protein in PubMed:4708670.2 Publications

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

FAD2 PublicationsNote: Binds 1 FAD per subunit in a bicovalent manner.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=0.3 mM for oxygen (at pH 5.8 and 25 degrees Celsius)1 Publication
  2. KM=2.7 mM for D-glucose (at pH 6.3 and 25 degrees Celsius)1 Publication
  3. KM=3.8 mM for D-galactose (at pH 6.3 and 25 degrees Celsius)1 Publication
  4. KM=8.5 mM for glucose (at pH 5.8 and 25 degrees Celsius)1 Publication
  5. KM=1.7 mM for lactose (at pH 5.8 and 25 degrees Celsius)1 Publication
  6. KM=20 mM for galactose (at pH 5.8 and 25 degrees Celsius)1 Publication
  7. KM=12.5 mM for cellobiose (at pH 5.8 and 25 degrees Celsius)1 Publication
  8. KM=28 mM for maltose (at pH 5.8 and 25 degrees Celsius)1 Publication
  9. KM=2.5 mM for glucose (at pH 6 and 26 degrees Celsius)1 Publication
  10. KM=97 mM for lactose (at pH 6 and 26 degrees Celsius)1 Publication
  11. KM=3.2 mM for galactose (at pH 6 and 26 degrees Celsius)1 Publication
  12. KM=27 mM for cellobiose (at pH 6 and 26 degrees Celsius)1 Publication
  13. KM=50 mM for maltose (at pH 6 and 26 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 6 (PubMed:9108257, PubMed:11427234). A second pH optimum was found at pH 10 (PubMed:9108257, PubMed:11427234).2 Publications

    <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

    <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 functionOxidoreductase
    LigandFAD, Flavoprotein

    <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:
    Hexose oxidase (EC:1.1.3.51 Publication)
    Short name:
    HOx
    Cleaved into the following 2 chains:
    <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:HOX
    ORF Names:CHC_T00009130001
    <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>OrganismiChondrus crispus (Carrageen Irish moss) (Polymorpha crispa)
    <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 identifieri2769 [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 lineageiEukaryotaRhodophytaFlorideophyceaeRhodymeniophycidaeGigartinalesGigartinaceaeChondrus
    <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
    • UP000012073 <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 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>Mutagenesisi79H → K: Loss of activity due to the absence of FAD cofactor. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004304601 – 546Hexose oxidaseAdd BLAST546
    ChainiPRO_00004304614 – 337Hexose oxidase, 40 kDa form1 PublicationAdd BLAST334
    ChainiPRO_0000430462338 – 546Hexose oxidase, 29 kDa form2 PublicationsAdd BLAST209

    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 describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki79 ↔ 1386-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys)1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi95N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
    Glycosylationi358N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Cleaved into 40 kDa and 29 kDa cleavage products, but the 2 polypeptide chains do not separate and seem to be physically linked together.2 Publications
    The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage.By similarity

    Keywords - PTMi

    Glycoprotein

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    1 Publication

    GO - Molecular functioni

    <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
    P93762

    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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini40 – 222FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST183

    <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

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    CIVMAKK

    Database of Orthologous Groups

    More...
    OrthoDBi
    1049549at2759

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR012951, BBE
    IPR016166, FAD-bd_PCMH
    IPR036318, FAD-bd_PCMH-like_sf
    IPR006094, Oxid_FAD_bind_N

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF08031, BBE, 1 hit
    PF01565, FAD_binding_4, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56176, SSF56176, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51387, FAD_PCMH, 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.

    <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.

    P93762-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MATLPQKDPG YIVIDVNAGT PDKPDPRLPS MKQGFNRRWI GTNIDFVYVV
    60 70 80 90 100
    YTPQGACTAL DRAMEKCSPG TVRIVSGGHC YEDFVFDECV KAIINVTGLV
    110 120 130 140 150
    ESGYDDDRGY FVSSGDTNWG SFKTLFRDHG RVLPGGSCYS VGLGGHIVGG
    160 170 180 190 200
    GDGILARLHG LPVDWLSGVE VVVKPVLTED SVLKYVHKDS EGDDGDLFWA
    210 220 230 240 250
    HTGGGGGNFG IITKYYFKDL PMSPRGVIAS NLHFSWDGFT RDALQDLLTK
    260 270 280 290 300
    YFKLARCDWK NTVGKFQIFH QAAEEFVMYL YTSYSNDAER EVAQDRHYHL
    310 320 330 340 350
    EADIEQIYKT CEPTKALGGH AGWAPFPVRP RKRHTSKTSY IHDETMDYPF
    360 370 380 390 400
    YALTETINGS GPNQRGKYKS AYMIKDFPDL QIDVIWKYLT EVPDGLTSAE
    410 420 430 440 450
    MKDALLQVDM FGGEIHNVAW DATAVAQRKY IIKLQYQTYW QEEDKDAVNL
    460 470 480 490 500
    KWIRDFYEEM YEPYGGVPDP NTQVESGKGV FEGCYFNYPD VDLNNWKNGK
    510 520 530 540
    YGALELYFLG NLNRLIKAKK LWDPNEIFTN KQSIPTKSLK EYKQTK
    Length:546
    Mass (Da):61,789
    Last modified:October 1, 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:i60091F260819853A
    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 conflicti4L → K AA sequence (PubMed:11427234).Curated1
    Sequence conflicti12 – 13IV → AI AA sequence (PubMed:11427234).Curated2
    Sequence conflicti193D → N in AAB49376 (PubMed:9111074).Curated1
    Sequence conflicti193D → N AA sequence (PubMed:9111074).Curated1
    Sequence conflicti196D → E in AAB49376 (PubMed:9111074).Curated1
    Sequence conflicti196D → E AA sequence (PubMed:9111074).Curated1
    Sequence conflicti339 – 340Missing AA sequence (PubMed:11427234).Curated2
    Sequence conflicti341I → M in AAB49376 (PubMed:9111074).Curated1
    Sequence conflicti341I → M AA sequence (PubMed:9111074).Curated1
    Sequence conflicti341I → M AA sequence (PubMed:11427234).Curated1
    Sequence conflicti345T → R AA sequence (PubMed:11427234).Curated1
    Sequence conflicti380L → F in AAB49376 (PubMed:9111074).Curated1
    Sequence conflicti417N → K in AAB49376 (PubMed:9111074).Curated1
    Sequence conflicti419A → V in AAB49376 (PubMed:9111074).Curated1
    Sequence conflicti429K → E in AAB49376 (PubMed:9111074).Curated1
    Sequence conflicti520K → W in AAB49376 (PubMed:9111074).Curated1
    Sequence conflicti538S → P in AAB49376 (PubMed:9111074).Curated1
    Sequence conflicti542Y → P in AAB49376 (PubMed:9111074).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
    U89770 mRNA Translation: AAB49376.1
    HG001523 Genomic DNA Translation: CDF77476.1

    NCBI Reference Sequences

    More...
    RefSeqi
    XP_005712350.1, XM_005712293.1

    Genome annotation databases

    Ensembl plant genome annotation project

    More...
    EnsemblPlantsi
    CDF77476; CDF77476; CHC_T00009130001

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    17320065

    Gramene; a comparative resource for plants

    More...
    Gramenei
    CDF77476; CDF77476; CHC_T00009130001

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ccp:CHC_T00009130001

    <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
    U89770 mRNA Translation: AAB49376.1
    HG001523 Genomic DNA Translation: CDF77476.1
    RefSeqiXP_005712350.1, XM_005712293.1

    3D structure databases

    SMRiP93762
    ModBaseiSearch...

    Genome annotation databases

    EnsemblPlantsiCDF77476; CDF77476; CHC_T00009130001
    GeneIDi17320065
    GrameneiCDF77476; CDF77476; CHC_T00009130001
    KEGGiccp:CHC_T00009130001

    Phylogenomic databases

    OMAiCIVMAKK
    OrthoDBi1049549at2759

    Family and domain databases

    InterProiView protein in InterPro
    IPR012951, BBE
    IPR016166, FAD-bd_PCMH
    IPR036318, FAD-bd_PCMH-like_sf
    IPR006094, Oxid_FAD_bind_N
    PfamiView protein in Pfam
    PF08031, BBE, 1 hit
    PF01565, FAD_binding_4, 1 hit
    SUPFAMiSSF56176, SSF56176, 1 hit
    PROSITEiView protein in PROSITE
    PS51387, FAD_PCMH, 1 hit

    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 nameiHOX_CHOCR
    <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: P93762
    Secondary accession number(s): S0F2V9
    <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: October 1, 2014
    Last sequence update: October 1, 2014
    Last modified: April 7, 2021
    This is version 74 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)

    <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

    Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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