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Entry version 72 (26 Feb 2020)
Sequence version 1 (31 Oct 2006)
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Protein

Lysyl oxidase homolog 2

Gene

loxl2

Organism
Xenopus laevis (African clawed frog)
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 transcript 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

Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription. LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency. Involved in epithelial to mesenchymal transition (EMT) and participates in repression of E-cadherin, probably by mediating deamination of histone H3. When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation.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 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:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi540CalciumBy similarity1
Metal bindingi541Calcium; via carbonyl oxygenBy similarity1
Metal bindingi617CopperBy similarity1
Metal bindingi619CopperBy similarity1
Metal bindingi621CopperBy similarity1
Metal bindingi713CalciumBy similarity1
Metal bindingi715Calcium; via carbonyl oxygenBy similarity1
Metal bindingi718CalciumBy similarity1
Metal bindingi719CalciumBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator, Oxidoreductase, Repressor
Biological processTranscription, Transcription regulation
LigandCalcium, Copper, Metal-binding

<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:
Lysyl oxidase homolog 2 (EC:1.4.3.13By similarity)
Alternative name(s):
Lysyl oxidase-like protein 2
<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:loxl2
<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>OrganismiXenopus laevis (African clawed frog)
<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 identifieri8355 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-1010778 loxl2

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

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

Keywords - Cellular componenti

Basement membrane, Chromosome, Endoplasmic reticulum, Extracellular matrix, Nucleus, Secreted

<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 – 19Sequence analysisAdd BLAST19
<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_000041800620 – 765Lysyl oxidase homolog 2Add BLAST746

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 bondi75 ↔ 139PROSITE-ProRule annotation
Disulfide bondi88 ↔ 149PROSITE-ProRule annotation
Disulfide bondi119 ↔ 129PROSITE-ProRule annotation
Disulfide bondi209 ↔ 282PROSITE-ProRule annotation
Disulfide bondi222 ↔ 292PROSITE-ProRule annotation
Disulfide bondi256 ↔ 266PROSITE-ProRule annotation
<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>Glycosylationi279N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi342 ↔ 405PROSITE-ProRule annotation
Disulfide bondi355 ↔ 415PROSITE-ProRule annotation
Disulfide bondi386 ↔ 396PROSITE-ProRule annotation
Glycosylationi446N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi455 ↔ 521PROSITE-ProRule annotation
Disulfide bondi468 ↔ 534PROSITE-ProRule annotation
Disulfide bondi502 ↔ 512PROSITE-ProRule annotation
Disulfide bondi564 ↔ 616By similarity
Disulfide bondi570 ↔ 686By similarity
Glycosylationi635N-linked (GlcNAc...) asparagineSequence analysis1
<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-linki644 ↔ 680Lysine tyrosylquinone (Lys-Tyr)By similarity
Disulfide bondi648 ↔ 664By similarity
Disulfide bondi654 ↔ 676By similarity
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei6802',4',5'-topaquinoneBy similarity1
Disulfide bondi723 ↔ 737PROSITE-ProRule annotation

<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

The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, LTQ, TPQ

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q08B63

<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
Q08B63

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>Domaini49 – 150SRCR 1PROSITE-ProRule annotationAdd BLAST102
Domaini179 – 293SRCR 2PROSITE-ProRule annotationAdd BLAST115
Domaini317 – 416SRCR 3PROSITE-ProRule annotationAdd BLAST100
Domaini426 – 535SRCR 4PROSITE-ProRule annotationAdd BLAST110

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>Regioni539 – 742Lysyl-oxidase likeBy similarityAdd BLAST204

<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 lysyl oxidase family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K00280

Database of Orthologous Groups

More...
OrthoDBi
815466at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.250.10, 4 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001695 Lysyl_oxidase
IPR019828 Lysyl_oxidase_CS
IPR001190 SRCR
IPR017448 SRCR-like_dom
IPR036772 SRCR-like_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01186 Lysyl_oxidase, 1 hit
PF00530 SRCR, 4 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00074 LYSYLOXIDASE
PR00258 SPERACTRCPTR

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00202 SR, 4 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56487 SSF56487, 4 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00926 LYSYL_OXIDASE, 1 hit
PS00420 SRCR_1, 1 hit
PS50287 SRCR_2, 4 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.

Q08B63-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLVSHVFLLT LSLSVPSLGQ YEHWPYYPEY QGPPEPPPTQ PKIVPQIHVR
60 70 80 90 100
LAGEKRKHNE GRVEVYYEGE WGTVCDDDFS MYAAHIVCRE LGYQEAVSWS
110 120 130 140 150
PSSKYGKGEG RIWLDNVNCN GRERSIASCS SNGWGVTDCK HSEDVGVQCS
160 170 180 190 200
DRRIPGFKVS NELPGHLEGL NIQVEDVRIR PILSAYRKRV PVTEGFAEVK
210 220 230 240 250
VQGSWRQVCN TQWSSKNSRV VCGMFGFPSE KKYNTKVYKM FSSRRKHTYW
260 270 280 290 300
QFSANCTGNE PHLSSCKVGG VLSPDPKTNQ TCSDGAPAVV SCTPGRAFAP
310 320 330 340 350
SPGTGFRKAF RQEQPLVRLR GGANVGEGRV EVLKNGEWGT VCDDKWNLVT
360 370 380 390 400
ASVICRELGF GSAKEALVGA QLGQGMGQIH MSEIQCNGFE KSLTDCKFNI
410 420 430 440 450
HSQGCNHEED AAVRCNVPAM GFENQVRLSG GRHPTEGRVE VLMERNGTLR
460 470 480 490 500
WGTVCSETWG TMEAMIVCRQ LGLGFASHAF QETWYWQGDI NADDVVMSGV
510 520 530 540 550
KCSGTEMSLA HCRHDGANVN CPRGGGRFAA GVSCVETAPD LVLNAALVEQ
560 570 580 590 600
TTYLEDRPMF MLQCAHEEQC LASSADRTSP TTGYRRLLRF SSQIHNNGQA
610 620 630 640 650
DFRPKTGRHA WIWHDCHRHY HSMEVFTHYD LLTLNGTKVA EGHKASFCLE
660 670 680 690 700
DSECEADIQK QYVCANFGEQ GITVGCWDLY RHDIDCQWVD ITDVAPGDYF
710 720 730 740 750
FQIIINPNQE VAESDYTNNI MKCRCRYDGQ RIWMYNCHIG GSYSTETEEK
760
FEHFSGLLNN QLSTR
Length:765
Mass (Da):85,656
Last modified:October 31, 2006 - 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:i978C9ACDFEDFDE51
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
BC124862 mRNA Translation: AAI24863.1

NCBI Reference Sequences

More...
RefSeqi
NP_001121257.1, NM_001127785.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100158339

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xla:100158339

<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
BC124862 mRNA Translation: AAI24863.1
RefSeqiNP_001121257.1, NM_001127785.1

3D structure databases

SMRiQ08B63
ModBaseiSearch...

Proteomic databases

PRIDEiQ08B63

Genome annotation databases

GeneIDi100158339
KEGGixla:100158339

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
100158339
XenbaseiXB-GENE-1010778 loxl2

Phylogenomic databases

KOiK00280
OrthoDBi815466at2759

Family and domain databases

Gene3Di3.10.250.10, 4 hits
InterProiView protein in InterPro
IPR001695 Lysyl_oxidase
IPR019828 Lysyl_oxidase_CS
IPR001190 SRCR
IPR017448 SRCR-like_dom
IPR036772 SRCR-like_dom_sf
PfamiView protein in Pfam
PF01186 Lysyl_oxidase, 1 hit
PF00530 SRCR, 4 hits
PRINTSiPR00074 LYSYLOXIDASE
PR00258 SPERACTRCPTR
SMARTiView protein in SMART
SM00202 SR, 4 hits
SUPFAMiSSF56487 SSF56487, 4 hits
PROSITEiView protein in PROSITE
PS00926 LYSYL_OXIDASE, 1 hit
PS00420 SRCR_1, 1 hit
PS50287 SRCR_2, 4 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 nameiLOXL2_XENLA
<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: Q08B63
<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: June 13, 2012
Last sequence update: October 31, 2006
Last modified: February 26, 2020
This is version 72 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 programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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