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Entry version 181 (08 May 2019)
Sequence version 3 (25 Oct 2005)
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Protein

Peptidyl-prolyl cis-trans isomerase ESS1

Gene

ESS1

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

Essential PPIase specific for phosphoserine and phosphothreonine N-terminal to the proline residue. Required for efficient pre-mRNA 3'-end processing and transcription termination, probably by inducing conformational changes by proline-directed isomerization in the C-terminal domain (CTD) of RPB1, thereby altering cofactor binding with the RNA polymerase II transcription complex. Also targets the SIN3-RPD3 histone deacetylase complex (HDAC).

Miscellaneous

Present with 4401 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by 5-hydroxy-1,4-naphthoquinone (juglone), but not by FK506 or cyclosporin A.1 Publication

<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 functionIsomerase, Rotamase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YJR017C-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-5668599 RHO GTPases Activate NADPH Oxidases
R-SCE-6811555 PI5P Regulates TP53 Acetylation

<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_and_taxonomy_section">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:
Peptidyl-prolyl cis-trans isomerase ESS1 (EC:5.2.1.8)
Short name:
PPIase ESS1
Alternative name(s):
Parvulin ESS1
Processing/termination factor 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:ESS1
Synonyms:PIN1, PTF1
Ordered Locus Names:YJR017C
ORF Names:J1452
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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 X

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YJR017C

Saccharomyces Genome Database

More...
SGDi
S000003778 ESS1

<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

Cytoplasm, Nucleus

<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_and_biotech_section">'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>Mutagenesisi120C → R: Abolishes PPIase activity. 1 Publication1
Mutagenesisi122S → P: Abolishes PPIase activity. 1 Publication1
Mutagenesisi127G → D in PTF1-2; decreases the catalytic efficiency 20-fold. 1 Publication1
Mutagenesisi162G → S in PTF1-5; decreases the catalytic efficiency 12-fold. 1 Publication1
Mutagenesisi164H → R: Abolishes PPIase activity. 1 Publication1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001934331 – 170Peptidyl-prolyl cis-trans isomerase ESS1Add BLAST170

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei161PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P22696

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

More...
PaxDbi
P22696

PRoteomics IDEntifications database

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PRIDEi
P22696

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P22696

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22696

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with the RNA polymerase II largest subunit (RPB1) and with the SIN1-RDP3 HDAC subunit SIN3.2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33773, 1009 interactors

Database of interacting proteins

More...
DIPi
DIP-3856N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P22696

Protein interaction database and analysis system

More...
IntActi
P22696, 115 interactors

Molecular INTeraction database

More...
MINTi
P22696

STRING: functional protein association networks

More...
STRINGi
4932.YJR017C

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P22696

<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
P22696

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_and_domains_section">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>Domaini9 – 43WWPROSITE-ProRule annotationAdd BLAST35
Domaini57 – 170PpiCPROSITE-ProRule annotationAdd BLAST114

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The WW domain binds to the phosphorylated tandem 7 residues repeats of RPB1.

<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 PpiC/parvulin rotamase family.Curated

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00640000091578

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000275331

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P22696

KEGG Orthology (KO)

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KOi
K09578

Identification of Orthologs from Complete Genome Data

More...
OMAi
DEVQCLH

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00201 WW, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000297 PPIase_PpiC
IPR023058 PPIase_PpiC_CS
IPR001202 WW_dom
IPR036020 WW_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00639 Rotamase, 1 hit
PF00397 WW, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00456 WW, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51045 SSF51045, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01096 PPIC_PPIASE_1, 1 hit
PS50198 PPIC_PPIASE_2, 1 hit
PS01159 WW_DOMAIN_1, 1 hit
PS50020 WW_DOMAIN_2, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P22696-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPSDVASRTG LPTPWTVRYS KSKKREYFFN PETKHSQWEE PEGTNKDQLH
60 70 80 90 100
KHLRDHPVRV RCLHILIKHK DSRRPASHRS ENITISKQDA TDELKTLITR
110 120 130 140 150
LDDDSKTNSF EALAKERSDC SSYKRGGDLG WFGRGEMQPS FEDAAFQLKV
160 170
GEVSDIVESG SGVHVIKRVG
Length:170
Mass (Da):19,405
Last modified:October 25, 2005 - v3
<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:i18D3EC02E8395175
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA60941 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA89541 differs from that shown. Reason: Erroneous initiation.Curated
The sequence described in PubMed:2648698 differs from that shown. Reason: Frameshift at position 127.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti8R → S (PubMed:2648698).Curated1
Sequence conflicti17V → A (PubMed:2648698).Curated1
Sequence conflicti128D → G (PubMed:2648698).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X85972 Genomic DNA Translation: CAA59961.1
X87611 Genomic DNA Translation: CAA60941.1 Different initiation.
Z49517 Genomic DNA Translation: CAA89541.1 Different initiation.
BK006943 Genomic DNA Translation: DAA08809.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S52764

NCBI Reference Sequences

More...
RefSeqi
NP_012551.2, NM_001181675.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YJR017C_mRNA; YJR017C_mRNA; YJR017C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853475

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YJR017C

<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
X85972 Genomic DNA Translation: CAA59961.1
X87611 Genomic DNA Translation: CAA60941.1 Different initiation.
Z49517 Genomic DNA Translation: CAA89541.1 Different initiation.
BK006943 Genomic DNA Translation: DAA08809.1
PIRiS52764
RefSeqiNP_012551.2, NM_001181675.1

3D structure databases

SMRiP22696
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33773, 1009 interactors
DIPiDIP-3856N
ELMiP22696
IntActiP22696, 115 interactors
MINTiP22696
STRINGi4932.YJR017C

Chemistry databases

BindingDBiP22696

PTM databases

iPTMnetiP22696

Proteomic databases

MaxQBiP22696
PaxDbiP22696
PRIDEiP22696
TopDownProteomicsiP22696

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR017C_mRNA; YJR017C_mRNA; YJR017C
GeneIDi853475
KEGGisce:YJR017C

Organism-specific databases

EuPathDBiFungiDB:YJR017C
SGDiS000003778 ESS1

Phylogenomic databases

GeneTreeiENSGT00640000091578
HOGENOMiHOG000275331
InParanoidiP22696
KOiK09578
OMAiDEVQCLH

Enzyme and pathway databases

BioCyciYEAST:YJR017C-MONOMER
ReactomeiR-SCE-5668599 RHO GTPases Activate NADPH Oxidases
R-SCE-6811555 PI5P Regulates TP53 Acetylation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P22696

Family and domain databases

CDDicd00201 WW, 1 hit
InterProiView protein in InterPro
IPR000297 PPIase_PpiC
IPR023058 PPIase_PpiC_CS
IPR001202 WW_dom
IPR036020 WW_dom_sf
PfamiView protein in Pfam
PF00639 Rotamase, 1 hit
PF00397 WW, 1 hit
SMARTiView protein in SMART
SM00456 WW, 1 hit
SUPFAMiSSF51045 SSF51045, 1 hit
PROSITEiView protein in PROSITE
PS01096 PPIC_PPIASE_1, 1 hit
PS50198 PPIC_PPIASE_2, 1 hit
PS01159 WW_DOMAIN_1, 1 hit
PS50020 WW_DOMAIN_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiESS1_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: P22696
Secondary accession number(s): D6VWJ3
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 25, 2005
Last modified: May 8, 2019
This is version 181 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
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