Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P38169 (KMO_YEAST)

Entry version 181 (02 Dec 2020)
Sequence version 1 (01 Oct 1994)
Previous versions | rss
Add a publicationFeedback
Protein

Kynurenine 3-monooxygenase

Gene

BNA4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.UniRule annotation3 Publications

Miscellaneous

Present with 556 molecules/cell in log phase SD medium.1 Publication
Deletion of BNA4 suppresses the toxicity of a mutant HD/HTT fragment.

<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

FAD1 Publication

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

This protein is involved in step 1 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation2 Publications
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Kynurenine 3-monooxygenase (BNA4)
  2. Kynureninase (BNA5)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (BNA1)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section 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 sitei13FAD; via amide nitrogenCombined sources1
Binding sitei53FAD; via amide nitrogen and carbonyl oxygenCombined sources1
Binding sitei83L-kynurenineBy similarity1
Binding sitei97L-kynurenineBy similarity1
Binding sitei109FADCombined sources1
Binding sitei133FAD; via amide nitrogen and carbonyl oxygenCombined sources1
Binding sitei195FADCombined sources1
Binding sitei314FADCombined sources1
Binding sitei373L-kynurenineBy similarity1
Binding sitei408L-kynurenineBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi32 – 34FADCombined sources3
Nucleotide bindingi325 – 328FADCombined sources4

<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 functionMonooxygenase, Oxidoreductase
Biological processPyridine nucleotide biosynthesis
LigandFAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:YBL098W-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.14.13.9, 984

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-71240, Tryptophan catabolism

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

More...UniPathwayi		UPA00253;UER00328

<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:
Kynurenine 3-monooxygenaseUniRule annotation (EC:1.14.13.9UniRule annotation)
Alternative name(s):
Biosynthesis of nicotinic acid protein 4UniRule annotation
Kynurenine 3-hydroxylaseUniRule annotation
<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:BNA4UniRule annotation
Ordered Locus Names:YBL098W
ORF Names:YBL0828
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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
  • UP000002311 <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 II

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		FungiDB:YBL098W

Saccharomyces Genome Database

More...SGDi		S000000194, BNA4

<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 Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer 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

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>Mutagenesisi83R → A: Strongly decreases enzymatic activity. 1 Publication1
Mutagenesisi83R → M: Abolsihes enzymatic activity. 1 Publication1
Mutagenesisi322 – 323FY → AA: Abolishes NADPH oxidase activity. 1 Publication2

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3627588

<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_00000208231 – 460Kynurenine 3-monooxygenaseAdd BLAST460

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P38169

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

More...PaxDbi		P38169

PRoteomics IDEntifications database

More...PRIDEi		P38169

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P38169

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		32607, 96 interactors

Database of interacting proteins

More...DIPi		DIP-5165N

Protein interaction database and analysis system

More...IntActi		P38169, 2 interactors

STRING: functional protein association networks

More...STRINGi		4932.YBL098W

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P38169

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P38169, protein

<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

1460
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		P38169

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

<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 aromatic-ring hydroxylase family. KMO subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2614, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000000747

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_023210_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P38169

Identification of Orthologs from Complete Genome Data

More...OMAi		NLAMSNR

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.50.50.60, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01971, Kynurenine_monooxygenase, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002938, FAD-bd
IPR036188, FAD/NAD-bd_sf
IPR027545, Kynurenine_monooxygenase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01494, FAD_binding_3, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51905, SSF51905, 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.

P38169-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSESVAIIGA GLVGCLAALA FSKEGYNVTL YDFRQDPRLD TTKNKNLKSI 
        60         70         80         90        100
NLAISARGID ALKSIDPDAC EHILQDMIPM KGRMIHDLKG RQESQLYGLH 
       110        120        130        140        150
GEAINSINRS VLNNSLLDEL EKSTTELKFG HKLVKIEWTD DKQICHFAIG 
       160        170        180        190        200
EDLKTPHTEK YDFVIGCDGA YSATRSQMQR KVEMDFSQEY MNLRYIELYI 
       210        220        230        240        250
PPTEEFKPNY GGNFAIAPDH LHIWPRHKFM LIALANSDGS FTSTFFGSKD 
       260        270        280        290        300
QISDLITSKS RVREFLIENF PDIINIMDLD DAVKRFITYP KESLVCVNCK 
       310        320        330        340        350
PYDVPGGKAI LLGDAAHAMV PFYGQGMNCG FEDVRILMAL LKKHSGDRSR 
       360        370        380        390        400
AFTEYTQTRH KDLVSITELA KRNYKEMSHD VTSKRFLLRK KLDALFSIIM 
       410        420        430        440        450
KDKWIPLYTM ISFRSDISYS RALERAGKQT RILKFLESLT LGMLSIGGYK 
       460
LFKFLTRERS
Length:460
Mass (Da):52,429
Last modified:October 1, 1994 - 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:i5340CC6C9D901D17
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
X79489 Genomic DNA Translation: CAA56002.1
Z35859 Genomic DNA Translation: CAA84920.1
AY692951 Genomic DNA Translation: AAT92970.1
BK006936 Genomic DNA Translation: DAA07027.1

Protein sequence database of the Protein Information Resource

More...PIRi		S45402

NCBI Reference Sequences

More...RefSeqi		NP_009454.1, NM_001178338.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YBL098W_mRNA; YBL098W; YBL098W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		852179

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YBL098W

<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
X79489 Genomic DNA Translation: CAA56002.1
Z35859 Genomic DNA Translation: CAA84920.1
AY692951 Genomic DNA Translation: AAT92970.1
BK006936 Genomic DNA Translation: DAA07027.1
PIRiS45402
RefSeqiNP_009454.1, NM_001178338.1

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
4J2WX-ray2.60A/B1-396[»]
4J31X-ray2.40A/B1-396[»]
4J33X-ray1.82A/B1-394[»]
4J34X-ray2.03A/B1-394[»]
4J36X-ray2.13A/B1-394[»]
5X6RX-ray1.91A/B1-394[»]
SMRiP38169
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi32607, 96 interactors
DIPiDIP-5165N
IntActiP38169, 2 interactors
STRINGi4932.YBL098W

Chemistry databases

BindingDBiP38169
ChEMBLiCHEMBL3627588

PTM databases

iPTMnetiP38169

Proteomic databases

MaxQBiP38169
PaxDbiP38169
PRIDEiP38169

Genome annotation databases

EnsemblFungiiYBL098W_mRNA; YBL098W; YBL098W
GeneIDi852179
KEGGisce:YBL098W

Organism-specific databases

EuPathDBiFungiDB:YBL098W
SGDiS000000194, BNA4

Phylogenomic databases

eggNOGiKOG2614, Eukaryota
GeneTreeiENSGT00390000000747
HOGENOMiCLU_023210_0_1_1
InParanoidiP38169
OMAiNLAMSNR

Enzyme and pathway databases

UniPathwayiUPA00253;UER00328
BioCyciMetaCyc:YBL098W-MONOMER
BRENDAi1.14.13.9, 984
ReactomeiR-SCE-71240, Tryptophan catabolism

Miscellaneous databases

Protein Ontology

More...PROi		PR:P38169
RNActiP38169, protein

Family and domain databases

Gene3Di3.50.50.60, 1 hit
HAMAPiMF_01971, Kynurenine_monooxygenase, 1 hit
InterProiView protein in InterPro
IPR002938, FAD-bd
IPR036188, FAD/NAD-bd_sf
IPR027545, Kynurenine_monooxygenase
PfamiView protein in Pfam
PF01494, FAD_binding_3, 1 hit
SUPFAMiSSF51905, SSF51905, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKMO_YEAST
<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: P38169
Secondary accession number(s): D6VPQ7
<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, 1994
Last sequence update: October 1, 1994
Last modified: December 2, 2020
This is version 181 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 programFungal 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again