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Protein

ATP-dependent RNA helicase DHX30

Gene

DHX30

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

RNA-dependent helicase (PubMed:29100085). Plays an important role in the assembly of the mitochondrial large ribosomal subunit (PubMed:25683715, PubMed:29100085). Required for optimal function of the zinc-finger antiviral protein ZC3HAV1 (By similarity). Associates with mitochondrial DNA (PubMed:18063578). Involved in nervous system development and differentiation through its involvement in the up-regulation of a number of genes which are required for neurogenesis, including GSC, NCAM1, neurogenin, and NEUROD (By similarity).By similarity3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi457 – 464ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

  • central nervous system development Source: UniProtKB
  • mitochondrial large ribosomal subunit assembly Source: UniProtKB

Keywordsi

Molecular functionHelicase, Hydrolase, RNA-binding
Biological processRibosome biogenesis
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DHX30Curated (EC:3.6.4.131 Publication)
Alternative name(s):
DEAH box protein 30
Gene namesi
Name:DHX30
Synonyms:DDX30, KIAA0890
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000132153.14
HGNCiHGNC:16716 DHX30
MIMi616423 gene
neXtProtiNX_Q7L2E3

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Mitochondrion nucleoid

Pathology & Biotechi

Involvement in diseasei

Neurodevelopmental disorder with severe motor impairment and absent language (NEDMIAL)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant neurodevelopmental disorder characterized by global developmental delay, intellectual disability, severe speech impairment and gait abnormalities.
See also OMIM:617804
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_080611493R → H in NEDMIAL; changed localization to stress granules; decreased RNA-binding; no effect on RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. 2 Publications1
Natural variantiVAR_080612562H → R in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. 2 Publications1
Natural variantiVAR_080613781G → D in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. 1 Publication1
Natural variantiVAR_080614782R → W in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. 2 Publications1
Natural variantiVAR_080615785R → C in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. 1 Publication1
Natural variantiVAR_080616785R → H in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi22907
MalaCardsiDHX30
MIMi617804 phenotype
OpenTargetsiENSG00000132153
PharmGKBiPA27217

Polymorphism and mutation databases

BioMutaiDHX30
DMDMi74758997

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002455381 – 1194ATP-dependent RNA helicase DHX30Add BLAST1194

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei6PhosphoserineCombined sources1
Modified residuei226PhosphoserineBy similarity1
Modified residuei380PhosphoserineCombined sources1
Isoform 2 (identifier: Q7L2E3-2)
Modified residuei15PhosphoserineCombined sources1

Post-translational modificationi

Isoform 2: Phosphorylated on Ser-15.Combined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7L2E3
MaxQBiQ7L2E3
PaxDbiQ7L2E3
PeptideAtlasiQ7L2E3
PRIDEiQ7L2E3
ProteomicsDBi68758
68759 [Q7L2E3-2]
68760 [Q7L2E3-3]

PTM databases

CarbonylDBiQ7L2E3
iPTMnetiQ7L2E3
PhosphoSitePlusiQ7L2E3
SwissPalmiQ7L2E3

Expressioni

Gene expression databases

BgeeiENSG00000132153 Expressed in 197 organ(s), highest expression level in testis
CleanExiHS_DHX30
ExpressionAtlasiQ7L2E3 baseline and differential
GenevisibleiQ7L2E3 HS

Organism-specific databases

HPAiHPA034806

Interactioni

Subunit structurei

Identified in a complex with TFAM and SSBP1. Interacts with AGO1 and AGO2. Interacts (via N-terminus) with ZC3HAV1 (via N-terminal domain) in an RNA-independent manner (By similarity). Found in a complex with GRSF1, DDX28, FASTKD2 and FASTKD5 (PubMed:25683715).By similarity3 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi116571, 107 interactors
CORUMiQ7L2E3
IntActiQ7L2E3, 60 interactors
MINTiQ7L2E3
STRINGi9606.ENSP00000405620

Structurei

Secondary structure

11194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ7L2E3
SMRiQ7L2E3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7L2E3

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 121DRBMAdd BLAST69
Domaini444 – 612Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST169
Domaini654 – 827Helicase C-terminalPROSITE-ProRule annotationAdd BLAST174

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi559 – 562DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi188 – 199Poly-GluAdd BLAST12

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0920 Eukaryota
COG1643 LUCA
GeneTreeiENSGT00760000119189
HOGENOMiHOG000112212
HOVERGENiHBG081437
InParanoidiQ7L2E3
KOiK13185
OMAiPLSHAMY
OrthoDBiEOG091G01RZ
PhylomeDBiQ7L2E3
TreeFamiTF352030

Family and domain databases

CDDicd00079 HELICc, 1 hit
InterProiView protein in InterPro
IPR011545 DEAD/DEAH_box_helicase_dom
IPR002464 DNA/RNA_helicase_DEAH_CS
IPR011709 DUF1605
IPR007502 Helicase-assoc_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00270 DEAD, 1 hit
PF04408 HA2, 1 hit
PF00271 Helicase_C, 1 hit
PF07717 OB_NTP_bind, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00847 HA2, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00690 DEAH_ATP_HELICASE, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit

Sequences (3+)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q7L2E3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MFSLDSFRKD RAQHRQRQCK LPPPRLPPMC VNPTPGGTIS RASRDLLKEF
60 70 80 90 100
PQPKNLLNSV IGRALGISHA KDKLVYVHTN GPKKKKVTLH IKWPKSVEVE
110 120 130 140 150
GYGSKKIDAE RQAAAAACQL FKGWGLLGPR NELFDAAKYR VLADRFGSPA
160 170 180 190 200
DSWWRPEPTM PPTSWRQLNP ESIRPGGPGG LSRSLGREEE EDEEEELEEG
210 220 230 240 250
TIDVTDFLSM TQQDSHAPLR DSRGSSFEMT DDDSAIRALT QFPLPKNLLA
260 270 280 290 300
KVIQIATSSS TAKNLMQFHT VGTKTKLSTL TLLWPCPMTF VAKGRRKAEA
310 320 330 340 350
ENKAAALACK KLKSLGLVDR NNEPLTHAMY NLASLRELGE TQRRPCTIQV
360 370 380 390 400
PEPILRKIET FLNHYPVESS WIAPELRLQS DDILPLGKDS GPLSDPITGK
410 420 430 440 450
PYVPLLEAEE VRLSQSLLEL WRRRGPVWQE APQLPVDPHR DTILNAIEQH
460 470 480 490 500
PVVVISGDTG CGKTTRIPQL LLERYVTEGR GARCNVIITQ PRRISAVSVA
510 520 530 540 550
QRVSHELGPS LRRNVGFQVR LESKPPSRGG ALLFCTVGIL LRKLQSNPSL
560 570 580 590 600
EGVSHVIVDE VHERDVNTDF LLILLKGLQR LNPALRLVLM SATGDNERFS
610 620 630 640 650
RYFGGCPVIK VPGFMYPVKE HYLEDILAKL GKHQYLHRHR HHESEDECAL
660 670 680 690 700
DLDLVTDLVL HIDARGEPGG ILCFLPGWQE IKGVQQRLQE ALGMHESKYL
710 720 730 740 750
ILPVHSNIPM MDQKAIFQQP PVGVRKIVLA TNIAETSITI NDIVHVVDSG
760 770 780 790 800
LHKEERYDLK TKVSCLETVW VSRANVIQRR GRAGRCQSGF AYHLFPRSRL
810 820 830 840 850
EKMVPFQVPE ILRTPLENLV LQAKIHMPEK TAVEFLSKAV DSPNIKAVDE
860 870 880 890 900
AVILLQEIGV LDQREYLTTL GQRLAHISTD PRLAKAIVLA AIFRCLHPLL
910 920 930 940 950
VVVSCLTRDP FSSSLQNRAE VDKVKALLSH DSGSDHLAFV RAVAGWEEVL
960 970 980 990 1000
RWQDRSSREN YLEENLLYAP SLRFIHGLIK QFSENIYEAF LVGKPSDCTL
1010 1020 1030 1040 1050
ASAQCNEYSE EEELVKGVLM AGLYPNLIQV RQGKVTRQGK FKPNSVTYRT
1060 1070 1080 1090 1100
KSGNILLHKS TINREATRLR SRWLTYFMAV KSNGSVFVRD SSQVHPLAVL
1110 1120 1130 1140 1150
LLTDGDVHIR DDGRRATISL SDSDLLRLEG DSRTVRLLKE LRRALGRMVE
1160 1170 1180 1190
RSLRSELAAL PPSVQEEHGQ LLALLAELLR GPCGSFDVRK TADD
Length:1,194
Mass (Da):133,938
Last modified:July 5, 2004 - v1
Checksum:i33D9A08799FE7A02
GO
Isoform 2 (identifier: Q7L2E3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: MFSLDSFRKD...NPTPGGTISR → MAAARRLMAL...PGEGDGSLVN

Show »
Length:1,222
Mass (Da):136,115
Checksum:iBEEE9D1C88DAFCA7
GO
Isoform 3 (identifier: Q7L2E3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     40-41: SR → MA

Show »
Length:1,155
Mass (Da):129,438
Checksum:iD3417B4C609F6360
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7BXY3H7BXY3_HUMAN
ATP-dependent RNA helicase DHX30
DHX30
1,166Annotation score:
F6R0H4F6R0H4_HUMAN
Putative ATP-dependent RNA helicase...
DHX30
42Annotation score:

Sequence cautioni

The sequence BAA74913 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA92071 differs from that shown. Probable cloning artifact.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti557I → T in BAF83955 (PubMed:14702039).Curated1
Sequence conflicti1136R → W in AAH14237 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_080611493R → H in NEDMIAL; changed localization to stress granules; decreased RNA-binding; no effect on RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. 2 Publications1
Natural variantiVAR_080612562H → R in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. 2 Publications1
Natural variantiVAR_080613781G → D in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. 1 Publication1
Natural variantiVAR_080614782R → W in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. 2 Publications1
Natural variantiVAR_080615785R → C in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. 1 Publication1
Natural variantiVAR_080616785R → H in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0221181 – 41MFSLD…GTISR → MAAARRLMALAAGISPRLQP LGPRAAGRQGRSRGFSSSCA HPDHTKEAAEAESGMAPGGP GEGDGSLVN in isoform 2. 1 PublicationAdd BLAST41
Alternative sequenceiVSP_0368911 – 39Missing in isoform 3. 2 PublicationsAdd BLAST39
Alternative sequenceiVSP_03689240 – 41SR → MA in isoform 3. 2 Publications2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020697 mRNA Translation: BAA74913.2 Different initiation.
AK002076 mRNA Translation: BAA92071.1 Sequence problems.
AK291266 mRNA Translation: BAF83955.1
BC014237 mRNA Translation: AAH14237.1
BC015029 mRNA Translation: AAH15029.1
BC020126 mRNA Translation: AAH20126.1
BC038417 mRNA Translation: AAH38417.1
CCDSiCCDS2759.1 [Q7L2E3-1]
PIRiE56236
RefSeqiNP_055781.2, NM_014966.3 [Q7L2E3-3]
NP_619520.1, NM_138615.2 [Q7L2E3-1]
XP_011531796.1, XM_011533494.2 [Q7L2E3-1]
XP_011531797.1, XM_011533495.1 [Q7L2E3-1]
XP_016861406.1, XM_017005917.1 [Q7L2E3-3]
UniGeneiHs.517948

Genome annotation databases

EnsembliENST00000445061; ENSP00000405620; ENSG00000132153 [Q7L2E3-1]
ENST00000446256; ENSP00000392601; ENSG00000132153 [Q7L2E3-1]
ENST00000457607; ENSP00000394682; ENSG00000132153 [Q7L2E3-2]
ENST00000619982; ENSP00000483160; ENSG00000132153 [Q7L2E3-3]
GeneIDi22907
KEGGihsa:22907
UCSCiuc003cru.4 human [Q7L2E3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020697 mRNA Translation: BAA74913.2 Different initiation.
AK002076 mRNA Translation: BAA92071.1 Sequence problems.
AK291266 mRNA Translation: BAF83955.1
BC014237 mRNA Translation: AAH14237.1
BC015029 mRNA Translation: AAH15029.1
BC020126 mRNA Translation: AAH20126.1
BC038417 mRNA Translation: AAH38417.1
CCDSiCCDS2759.1 [Q7L2E3-1]
PIRiE56236
RefSeqiNP_055781.2, NM_014966.3 [Q7L2E3-3]
NP_619520.1, NM_138615.2 [Q7L2E3-1]
XP_011531796.1, XM_011533494.2 [Q7L2E3-1]
XP_011531797.1, XM_011533495.1 [Q7L2E3-1]
XP_016861406.1, XM_017005917.1 [Q7L2E3-3]
UniGeneiHs.517948

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DB2NMR-A42-147[»]
ProteinModelPortaliQ7L2E3
SMRiQ7L2E3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116571, 107 interactors
CORUMiQ7L2E3
IntActiQ7L2E3, 60 interactors
MINTiQ7L2E3
STRINGi9606.ENSP00000405620

PTM databases

CarbonylDBiQ7L2E3
iPTMnetiQ7L2E3
PhosphoSitePlusiQ7L2E3
SwissPalmiQ7L2E3

Polymorphism and mutation databases

BioMutaiDHX30
DMDMi74758997

Proteomic databases

EPDiQ7L2E3
MaxQBiQ7L2E3
PaxDbiQ7L2E3
PeptideAtlasiQ7L2E3
PRIDEiQ7L2E3
ProteomicsDBi68758
68759 [Q7L2E3-2]
68760 [Q7L2E3-3]

Protocols and materials databases

DNASUi22907
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000445061; ENSP00000405620; ENSG00000132153 [Q7L2E3-1]
ENST00000446256; ENSP00000392601; ENSG00000132153 [Q7L2E3-1]
ENST00000457607; ENSP00000394682; ENSG00000132153 [Q7L2E3-2]
ENST00000619982; ENSP00000483160; ENSG00000132153 [Q7L2E3-3]
GeneIDi22907
KEGGihsa:22907
UCSCiuc003cru.4 human [Q7L2E3-1]

Organism-specific databases

CTDi22907
DisGeNETi22907
EuPathDBiHostDB:ENSG00000132153.14
GeneCardsiDHX30
HGNCiHGNC:16716 DHX30
HPAiHPA034806
MalaCardsiDHX30
MIMi616423 gene
617804 phenotype
neXtProtiNX_Q7L2E3
OpenTargetsiENSG00000132153
PharmGKBiPA27217
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0920 Eukaryota
COG1643 LUCA
GeneTreeiENSGT00760000119189
HOGENOMiHOG000112212
HOVERGENiHBG081437
InParanoidiQ7L2E3
KOiK13185
OMAiPLSHAMY
OrthoDBiEOG091G01RZ
PhylomeDBiQ7L2E3
TreeFamiTF352030

Miscellaneous databases

ChiTaRSiDHX30 human
EvolutionaryTraceiQ7L2E3
GenomeRNAii22907
PROiPR:Q7L2E3
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000132153 Expressed in 197 organ(s), highest expression level in testis
CleanExiHS_DHX30
ExpressionAtlasiQ7L2E3 baseline and differential
GenevisibleiQ7L2E3 HS

Family and domain databases

CDDicd00079 HELICc, 1 hit
InterProiView protein in InterPro
IPR011545 DEAD/DEAH_box_helicase_dom
IPR002464 DNA/RNA_helicase_DEAH_CS
IPR011709 DUF1605
IPR007502 Helicase-assoc_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00270 DEAD, 1 hit
PF04408 HA2, 1 hit
PF00271 Helicase_C, 1 hit
PF07717 OB_NTP_bind, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00847 HA2, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00690 DEAH_ATP_HELICASE, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiDHX30_HUMAN
AccessioniPrimary (citable) accession number: Q7L2E3
Secondary accession number(s): A8K5F1
, O94965, Q7Z753, Q96CH4, Q9NUQ0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 5, 2004
Last modified: November 7, 2018
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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