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Entry version 135 (23 Feb 2022)
Sequence version 1 (01 Nov 1996)
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Protein

Quinohemoprotein alcohol dehydrogenase

Gene

qheDH

Organism
Comamonas testosteroni (Pseudomonas testosteroni)
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 dye-linked oxidation of primary alcohols to the corresponding aldehydes and the (subsequent) oxidation of the aldehydes to carboxylic acids. Methanol is not a substrate.

1 Publication1 Publication

Caution

The oxidation form of Trp-543 is subject of controversy and could be the artifactual result of sample handling.1 Publication

<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

Protein has several cofactor binding sites:

<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=5 µM for benzyl alcohol1 Publication
  2. KM=5 µM for butan-1-ol1 Publication
  3. KM=5 µM for pentan-1-ol1 Publication
  4. KM=5 µM for octan-1-ol1 Publication
  5. KM=40 µM for octanal1 Publication
  6. KM=60 µM for propan-1-ol1 Publication
  7. KM=100 µM for butyraldehyde1 Publication
  8. KM=200 µM for 6-aminohexan-1-ol1 Publication
  9. KM=280 µM for butan-1,3-diol1 Publication
  10. KM=900 µM for acetaldehyde1 Publication
  11. KM=3 mM for formaldehyde1 Publication
  12. KM=5 mM for ethanol1 Publication

pH dependencei

Optimum pH is 7.7.1 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 sitei101Pyrroloquinoline quinoneCombined sources1 Publication1
Binding sitei153Pyrroloquinoline quinoneCombined sources1 Publication1
Binding sitei198Pyrroloquinoline quinoneCombined 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 bindingi216CalciumCombined sources1 Publication1
Binding sitei274Pyrroloquinoline quinoneCombined sources1 Publication1
Metal bindingi294CalciumCombined 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 sitei339Proton acceptor1 Publication1
Metal bindingi339CalciumCombined sources1 Publication1
Binding sitei366Pyrroloquinoline quinoneCombined sources1 Publication1
Binding sitei575Pyrroloquinoline quinone; via amide nitrogenCombined sources1 Publication1
Binding sitei635Heme c; covalentCombined sources1 Publication1
Binding sitei638Heme c; covalentCombined sources1 Publication1
Metal bindingi639Iron (heme axial ligand); via tele nitrogenCombined sources1 Publication1
Metal bindingi678Iron (heme axial ligand)Combined 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

<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
LigandCalcium, Heme, Iron, Metal-binding, PQQ

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.9.1, 1590

<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:
Quinohemoprotein alcohol dehydrogenase1 Publication (EC:1.1.9.11 Publication)
Short name:
QH-ADH1 Publication
Alternative name(s):
Alcohol dehydrogenase (azurin)Curated
PQQ-containing alcohol dehydrogenase1 Publication
PQQ-dependent ADH1 Publication
Quinohaemoprotein ethanol dehydrogenase type I1 Publication
Short name:
QH-EDHI1 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
Name:qheDH1 Publication
<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>OrganismiComamonas testosteroni (Pseudomonas testosteroni)
<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 identifieri285 [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 lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

<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

Keywords - Cellular componenti

Periplasm

<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

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03051, (S)-2-Tetrahydrofuroic acid
DB03679, 2-Hydroxy-Tryptophan
DB03317, Ferroheme C
DB03205, Pyrroloquinoline Quinone

<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 – 312 PublicationsAdd BLAST31
<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_000002556332 – 708Quinohemoprotein alcohol dehydrogenaseAdd BLAST677

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi147 ↔ 148Combined sources1 Publication

<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

In the crystallographic structures Trp-543 is oxidized to 2'-hydroxytryptophan.1 Publication

Keywords - PTMi

Disulfide bond

<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

By ethanol and butanol.1 Publication

<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

Monomer.

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

1708
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
Q46444

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q46444

<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>Domaini619 – 708Cytochrome cPROSITE-ProRule annotationAdd BLAST90

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni214 – 215Pyrroloquinoline quinone bindingCombined sources1 Publication2
Regioni425 – 426Pyrroloquinoline quinone bindingCombined sources1 Publication2

<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 bacterial PQQ dehydrogenase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.760.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009056, Cyt_c-like_dom
IPR036909, Cyt_c-like_dom_sf
IPR018391, PQQ_beta_propeller_repeat
IPR017512, PQQ_MeOH/EtOH_DH
IPR002372, PQQ_repeat
IPR011047, Quinoprotein_ADH-like_supfam
IPR001479, Quinoprotein_DH_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13442, Cytochrome_CBB3, 1 hit
PF13360, PQQ_2, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00564, PQQ, 5 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46626, SSF46626, 1 hit
SSF50998, SSF50998, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03075, PQQ_enz_alc_DH, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00364, BACTERIAL_PQQ_2, 1 hit
PS51007, CYTC, 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.

Q46444-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MERLIDNSHG WPGRMVWLLA ACLGSAAAFA QTGPAAQAAA AVQRVDGDFI
60 70 80 90 100
RANAARTPDW PTIGVDYAET RYSRLDQINA ANVKDLGLAW SYNLESTRGV
110 120 130 140 150
EATPVVVDGI MYVSASWSVV HAIDTRTGNR IWTYDPQIDR STGFKGCCDV
160 170 180 190 200
VNRGVALWKG KVYVGAWDGR LIALDAATGK EVWHQNTFEG QKGSLTITGA
210 220 230 240 250
PRVFKGKVII GKRGAEYGVR GYITAYDAET GERKWRWFSV PGDPSKPFED
260 270 280 290 300
ESMKRAARTW DPSGKWWEAG GGGTMWDSMT FDAELNTMYV GTGNGSPWSH
310 320 330 340 350
KVRSPKGGDN LYLASIVALD PDTGKYKWHY QETPGDNWDY TSTQPMILAD
360 370 380 390 400
IKIAGKPRKV ILHAPKNGFF FVLDRTNGKF ISAKNFVPVN WASGYDKHGK
410 420 430 440 450
PIGIAAARDG SKPQDAVPGP YGAHNWHPMS FNPQTGLVYL PAQNVPVNLM
460 470 480 490 500
DDKKWEFNQA GPGKPQSGTG WNTAKFFNAE PPKSKPFGRL LAWDPVAQKA
510 520 530 540 550
AWSVEHVSPW NGGTLTTAGN VVFQGTADGR LVAYHAATGE KLWEAPTGTG
560 570 580 590 600
VVAAPSTYMV DGRQYVSVAV GWGGVYGLAA RATERQGPGT VYTFVVAGKA
610 620 630 640 650
RMPEFVAQRT GQLLQGVKYD PAKVEAGTML YVANCVFCHG VPGVDRGGNI
660 670 680 690 700
PNLGYMDASY IENLPNFVFK GPAMVRGMPD FTGKLSGDDV ESLKAFIQGT

ADAIRPKP
Length:708
Mass (Da):76,823
Last modified:November 1, 1996 - 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:i99AB54BDD6ACCAB3
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
X81880 Genomic DNA Translation: CAA57464.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S62366, S52317

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:CAA57464

<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
X81880 Genomic DNA Translation: CAA57464.1
PIRiS62366, S52317

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
1KB0X-ray1.44A32-708[»]
SMRiQ46444
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

DrugBankiDB03051, (S)-2-Tetrahydrofuroic acid
DB03679, 2-Hydroxy-Tryptophan
DB03317, Ferroheme C
DB03205, Pyrroloquinoline Quinone

Genome annotation databases

KEGGiag:CAA57464

Enzyme and pathway databases

BRENDAi1.1.9.1, 1590

Miscellaneous databases

EvolutionaryTraceiQ46444

Family and domain databases

Gene3Di1.10.760.10, 1 hit
InterProiView protein in InterPro
IPR009056, Cyt_c-like_dom
IPR036909, Cyt_c-like_dom_sf
IPR018391, PQQ_beta_propeller_repeat
IPR017512, PQQ_MeOH/EtOH_DH
IPR002372, PQQ_repeat
IPR011047, Quinoprotein_ADH-like_supfam
IPR001479, Quinoprotein_DH_CS
PfamiView protein in Pfam
PF13442, Cytochrome_CBB3, 1 hit
PF13360, PQQ_2, 2 hits
SMARTiView protein in SMART
SM00564, PQQ, 5 hits
SUPFAMiSSF46626, SSF46626, 1 hit
SSF50998, SSF50998, 1 hit
TIGRFAMsiTIGR03075, PQQ_enz_alc_DH, 1 hit
PROSITEiView protein in PROSITE
PS00364, BACTERIAL_PQQ_2, 1 hit
PS51007, CYTC, 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 nameiQHED_COMTE
<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: Q46444
<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 17, 2003
Last sequence update: November 1, 1996
Last modified: February 23, 2022
This is version 135 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, Direct protein sequencing

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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