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Protein

26S proteasome non-ATPase regulatory subunit 3

Gene

PSMD3

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

Functioni

Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.1 Publication

GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974 ER-Phagosome pathway
R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534 Vpu mediated degradation of CD4
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-202424 Downstream TCR signaling
R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
R-HSA-382556 ABC-family proteins mediated transport
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870 Asymmetric localization of PCP proteins
R-HSA-4641257 Degradation of AXIN
R-HSA-4641258 Degradation of DVL
R-HSA-5358346 Hedgehog ligand biogenesis
R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
R-HSA-5678895 Defective CFTR causes cystic fibrosis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-6798695 Neutrophil degranulation
R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1
R-HSA-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-9604323 Negative regulation of NOTCH4 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 3
Alternative name(s):
26S proteasome regulatory subunit RPN3
26S proteasome regulatory subunit S3
Proteasome subunit p58
Gene namesi
Name:PSMD3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000108344.14
HGNCiHGNC:9560 PSMD3
MIMi617676 gene
neXtProtiNX_O43242

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

Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5709
OpenTargetsiENSG00000108344
PharmGKBiPA38123

Chemistry databases

ChEMBLiCHEMBL2364701

Polymorphism and mutation databases

BioMutaiPSMD3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001738161 – 53426S proteasome non-ATPase regulatory subunit 3Add BLAST534

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei418PhosphoserineCombined sources1
Modified residuei430PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO43242
MaxQBiO43242
PaxDbiO43242
PeptideAtlasiO43242
PRIDEiO43242
ProteomicsDBi48822

PTM databases

iPTMnetiO43242
PhosphoSitePlusiO43242
SwissPalmiO43242

Expressioni

Gene expression databases

BgeeiENSG00000108344 Expressed in 230 organ(s), highest expression level in gastrocnemius
CleanExiHS_PSMD3
ExpressionAtlasiO43242 baseline and differential
GenevisibleiO43242 HS

Organism-specific databases

HPAiCAB017038
HPA048972

Interactioni

Subunit structurei

Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD3, a base containing 6 ATPases and few additional components (PubMed:27428775, PubMed:27342858). Interacts with UBQLN1 (via ubiquitin-like domain) (PubMed:15147878).3 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi111682, 152 interactors
CORUMiO43242
DIPiDIP-27571N
IntActiO43242, 51 interactors
MINTiO43242
STRINGi9606.ENSP00000264639

Structurei

3D structure databases

ProteinModelPortaliO43242
SMRiO43242
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini286 – 465PCIPROSITE-ProRule annotationAdd BLAST180

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi26 – 32Poly-Pro7

Sequence similaritiesi

Belongs to the proteasome subunit S3 family.Curated

Phylogenomic databases

eggNOGiKOG2581 Eukaryota
ENOG410XS40 LUCA
GeneTreeiENSGT00490000043406
HOGENOMiHOG000193909
HOVERGENiHBG000703
InParanoidiO43242
KOiK03033
OMAiFRQTVQK
OrthoDBiEOG091G05QN
PhylomeDBiO43242
TreeFamiTF106110

Family and domain databases

InterProiView protein in InterPro
IPR013586 26S_Psome_reg_C
IPR000717 PCI_dom
IPR035267 PSMD3
IPR036390 WH_DNA-bd_sf
PANTHERiPTHR10758:SF2 PTHR10758:SF2, 1 hit
PfamiView protein in Pfam
PF01399 PCI, 1 hit
PF08375 Rpn3_C, 1 hit
SMARTiView protein in SMART
SM00088 PINT, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS50250 PCI, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

Isoform 1 (identifier: O43242-1) [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
MKQEGSARRR GADKAKPPPG GGEQEPPPPP APQDVEMKEE AATGGGSTGE
60 70 80 90 100
ADGKTAAAAA EHSQRELDTV TLEDIKEHVK QLEKAVSGKE PRFVLRALRM
110 120 130 140 150
LPSTSRRLNH YVLYKAVQGF FTSNNATRDF LLPFLEEPMD TEADLQFRPR
160 170 180 190 200
TGKAASTPLL PEVEAYLQLL VVIFMMNSKR YKEAQKISDD LMQKISTQNR
210 220 230 240 250
RALDLVAAKC YYYHARVYEF LDKLDVVRSF LHARLRTATL RHDADGQATL
260 270 280 290 300
LNLLLRNYLH YSLYDQAEKL VSKSVFPEQA NNNEWARYLY YTGRIKAIQL
310 320 330 340 350
EYSEARRTMT NALRKAPQHT AVGFKQTVHK LLIVVELLLG EIPDRLQFRQ
360 370 380 390 400
PSLKRSLMPY FLLTQAVRTG NLAKFNQVLD QFGEKFQADG TYTLIIRLRH
410 420 430 440 450
NVIKTGVRMI SLSYSRISLA DIAQKLQLDS PEDAEFIVAK AIRDGVIEAS
460 470 480 490 500
INHEKGYVQS KEMIDIYSTR EPQLAFHQRI SFCLDIHNMS VKAMRFPPKS
510 520 530
YNKDLESAEE RREREQQDLE FAKEMAEDDD DSFP
Length:534
Mass (Da):60,978
Last modified:May 10, 2002 - v2
Checksum:i3B3FB5593542C078
GO
Isoform 2 (identifier: O43242-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: Missing.
     493-534: AMRFPPKSYNKDLESAEERREREQQDLEFAKEMAEDDDDSFP → GW

Note: No experimental confirmation available.
Show »
Length:356
Mass (Da):41,184
Checksum:i62E7EA02B14DAE1B
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YGV8H0YGV8_HUMAN
26S proteasome non-ATPase regulator...
PSMD3
117Annotation score:
F5H8K4F5H8K4_HUMAN
26S proteasome non-ATPase regulator...
PSMD3
86Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti60A → V in BAA23651 (PubMed:9017604).Curated1
Sequence conflicti157 – 158TP → NT in AAH12302 (PubMed:15489334).Curated2
Sequence conflicti304E → V in AAH12302 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0563621 – 138Missing in isoform 2. 1 PublicationAdd BLAST138
Alternative sequenceiVSP_056363493 – 534AMRFP…DDSFP → GW in isoform 2. 1 PublicationAdd BLAST42

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D67025 mRNA Translation: BAA23651.1
BT007217 mRNA Translation: AAP35881.1
AK022896 mRNA Translation: BAG51131.1
AK300081 mRNA Translation: BAG61884.1
AC090844 Genomic DNA No translation available.
CH471152 Genomic DNA Translation: EAW60625.1
BC000074 mRNA Translation: AAH00074.1
BC004859 mRNA Translation: AAH04859.1
BC012302 mRNA Translation: AAH12302.1
BC020518 mRNA Translation: AAH20518.1
BC025686 mRNA Translation: AAH25686.1
CCDSiCCDS11356.1 [O43242-1]
RefSeqiNP_002800.2, NM_002809.3 [O43242-1]
UniGeneiHs.12970

Genome annotation databases

EnsembliENST00000264639; ENSP00000264639; ENSG00000108344 [O43242-1]
GeneIDi5709
KEGGihsa:5709
UCSCiuc002htn.3 human [O43242-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D67025 mRNA Translation: BAA23651.1
BT007217 mRNA Translation: AAP35881.1
AK022896 mRNA Translation: BAG51131.1
AK300081 mRNA Translation: BAG61884.1
AC090844 Genomic DNA No translation available.
CH471152 Genomic DNA Translation: EAW60625.1
BC000074 mRNA Translation: AAH00074.1
BC004859 mRNA Translation: AAH04859.1
BC012302 mRNA Translation: AAH12302.1
BC020518 mRNA Translation: AAH20518.1
BC025686 mRNA Translation: AAH25686.1
CCDSiCCDS11356.1 [O43242-1]
RefSeqiNP_002800.2, NM_002809.3 [O43242-1]
UniGeneiHs.12970

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GJQelectron microscopy4.50S1-534[»]
5GJRelectron microscopy3.506/S1-525[»]
5L4Kelectron microscopy4.50S1-534[»]
5LN3electron microscopy6.80S1-534[»]
5M32electron microscopy3.80j1-534[»]
5T0Celectron microscopy3.80AV/BV2-534[»]
5T0Gelectron microscopy4.40V2-534[»]
5T0Helectron microscopy6.80V2-534[»]
5T0Ielectron microscopy8.00V2-534[»]
5T0Jelectron microscopy8.00V2-534[»]
5VFPelectron microscopy4.20V18-497[»]
5VFQelectron microscopy4.20V18-497[»]
5VFRelectron microscopy4.90V18-497[»]
5VFSelectron microscopy3.60V18-497[»]
5VFTelectron microscopy7.00V18-497[»]
5VFUelectron microscopy5.80V18-497[»]
5VGZelectron microscopy3.70V18-505[»]
5VHFelectron microscopy5.70V323-505[»]
5VHHelectron microscopy6.10V18-505[»]
5VHIelectron microscopy6.80V18-505[»]
5VHSelectron microscopy8.80V18-505[»]
ProteinModelPortaliO43242
SMRiO43242
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111682, 152 interactors
CORUMiO43242
DIPiDIP-27571N
IntActiO43242, 51 interactors
MINTiO43242
STRINGi9606.ENSP00000264639

Chemistry databases

ChEMBLiCHEMBL2364701

PTM databases

iPTMnetiO43242
PhosphoSitePlusiO43242
SwissPalmiO43242

Polymorphism and mutation databases

BioMutaiPSMD3

Proteomic databases

EPDiO43242
MaxQBiO43242
PaxDbiO43242
PeptideAtlasiO43242
PRIDEiO43242
ProteomicsDBi48822

Protocols and materials databases

DNASUi5709
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264639; ENSP00000264639; ENSG00000108344 [O43242-1]
GeneIDi5709
KEGGihsa:5709
UCSCiuc002htn.3 human [O43242-1]

Organism-specific databases

CTDi5709
DisGeNETi5709
EuPathDBiHostDB:ENSG00000108344.14
GeneCardsiPSMD3
HGNCiHGNC:9560 PSMD3
HPAiCAB017038
HPA048972
MIMi617676 gene
neXtProtiNX_O43242
OpenTargetsiENSG00000108344
PharmGKBiPA38123
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2581 Eukaryota
ENOG410XS40 LUCA
GeneTreeiENSGT00490000043406
HOGENOMiHOG000193909
HOVERGENiHBG000703
InParanoidiO43242
KOiK03033
OMAiFRQTVQK
OrthoDBiEOG091G05QN
PhylomeDBiO43242
TreeFamiTF106110

Enzyme and pathway databases

ReactomeiR-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974 ER-Phagosome pathway
R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534 Vpu mediated degradation of CD4
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-202424 Downstream TCR signaling
R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
R-HSA-382556 ABC-family proteins mediated transport
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870 Asymmetric localization of PCP proteins
R-HSA-4641257 Degradation of AXIN
R-HSA-4641258 Degradation of DVL
R-HSA-5358346 Hedgehog ligand biogenesis
R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
R-HSA-5678895 Defective CFTR causes cystic fibrosis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-6798695 Neutrophil degranulation
R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1
R-HSA-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-9604323 Negative regulation of NOTCH4 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

ChiTaRSiPSMD3 human
GeneWikiiPSMD3
GenomeRNAii5709
PROiPR:O43242
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000108344 Expressed in 230 organ(s), highest expression level in gastrocnemius
CleanExiHS_PSMD3
ExpressionAtlasiO43242 baseline and differential
GenevisibleiO43242 HS

Family and domain databases

InterProiView protein in InterPro
IPR013586 26S_Psome_reg_C
IPR000717 PCI_dom
IPR035267 PSMD3
IPR036390 WH_DNA-bd_sf
PANTHERiPTHR10758:SF2 PTHR10758:SF2, 1 hit
PfamiView protein in Pfam
PF01399 PCI, 1 hit
PF08375 Rpn3_C, 1 hit
SMARTiView protein in SMART
SM00088 PINT, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS50250 PCI, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPSMD3_HUMAN
AccessioniPrimary (citable) accession number: O43242
Secondary accession number(s): B3KMW9
, B4DT72, Q96EI2, Q9BQA4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 10, 2002
Last modified: November 7, 2018
This is version 181 of the entry and version 2 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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