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Entry version 198 (08 May 2019)
Sequence version 1 (01 Oct 1989)
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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

LAT1

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

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.1 Publication

Miscellaneous

The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.
Present with 5440 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 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

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei455Sequence analysis1
Active sitei459Sequence analysis1

<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

  • dihydrolipoyllysine-residue acetyltransferase activity Source: SGD

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 functionAcyltransferase, Transferase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YNL071W-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-389661 Glyoxylate metabolism and glycine degradation
R-SCE-70268 Pyruvate metabolism

<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:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2
Short name:
PDC-E2
Short name:
PDCE2
<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:LAT1
Synonyms:ODP2, PDA2
Ordered Locus Names:YNL071W
ORF Names:N2374
<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 XIV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YNL071W

Saccharomyces Genome Database

More...
SGDi
S000005015 LAT1

<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

Mitochondrion

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 28Mitochondrion1 PublicationAdd BLAST28
<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_000002048329 – 482Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialAdd BLAST454

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 residuei75N6-lipoyllysinePROSITE-ProRule annotation1 Publication1

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P12695

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

More...
PaxDbi
P12695

PRoteomics IDEntifications database

More...
PRIDEi
P12695

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P12695

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P12695

<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

Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
35752, 330 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3207 Mitochondrial pyruvate dehydrogenase complex

Database of interacting proteins

More...
DIPi
DIP-6782N

Protein interaction database and analysis system

More...
IntActi
P12695, 61 interactors

Molecular INTeraction database

More...
MINTi
P12695

STRING: functional protein association networks

More...
STRINGi
4932.YNL071W

<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
P12695

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>Domaini34 – 110Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST77
Domaini175 – 212Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

<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 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154943

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000281566

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P12695

KEGG Orthology (KO)

More...
KOi
K00627

Identification of Orthologs from Complete Genome Data

More...
OMAi
TMEFESF

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.559.10, 1 hit
4.10.320.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR006257 LAT1
IPR004167 PSBD
IPR011053 Single_hybrid_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02817 E3_binding, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01349 PDHac_trf_mito, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit
PS51826 PSBD, 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.

<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 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.

P12695-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSAFVRVVPR ISRSSVLTRS LRLQLRCYAS YPEHTIIGMP ALSPTMTQGN
60 70 80 90 100
LAAWTKKEGD QLSPGEVIAE IETDKAQMDF EFQEDGYLAK ILVPEGTKDI
110 120 130 140 150
PVNKPIAVYV EDKADVPAFK DFKLEDSGSD SKTSTKAQPA EPQAEKKQEA
160 170 180 190 200
PAEETKTSAP EAKKSDVAAP QGRIFASPLA KTIALEKGIS LKDVHGTGPR
210 220 230 240 250
GRITKADIES YLEKSSKQSS QTSGAAAATP AAATSSTTAG SAPSPSSTAS
260 270 280 290 300
YEDVPISTMR SIIGERLLQS TQGIPSYIVS SKISISKLLK LRQSLNATAN
310 320 330 340 350
DKYKLSINDL LVKAITVAAK RVPDANAYWL PNENVIRKFK NVDVSVAVAT
360 370 380 390 400
PTGLLTPIVK NCEAKGLSQI SNEIKELVKR ARINKLAPEE FQGGTICISN
410 420 430 440 450
MGMNNAVNMF TSIINPPQST ILAIATVERV AVEDAAAENG FSFDNQVTIT
460 470 480
GTFDHRTIDG AKGAEFMKEL KTVIENPLEM LL
Length:482
Mass (Da):51,818
Last modified:October 1, 1989 - 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:i49D64C738926E784
GO

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
J04096 Genomic DNA Translation: AAA34385.1
X86470 Genomic DNA Translation: CAA60189.1
Z71347 Genomic DNA Translation: CAA95945.1
AY693185 Genomic DNA Translation: AAT93204.1
BK006947 Genomic DNA Translation: DAA10474.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A30198

NCBI Reference Sequences

More...
RefSeqi
NP_014328.3, NM_001182909.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YNL071W_mRNA; YNL071W_mRNA; YNL071W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855653

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YNL071W

<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
J04096 Genomic DNA Translation: AAA34385.1
X86470 Genomic DNA Translation: CAA60189.1
Z71347 Genomic DNA Translation: CAA95945.1
AY693185 Genomic DNA Translation: AAT93204.1
BK006947 Genomic DNA Translation: DAA10474.1
PIRiA30198
RefSeqiNP_014328.3, NM_001182909.3

3D structure databases

SMRiP12695
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35752, 330 interactors
ComplexPortaliCPX-3207 Mitochondrial pyruvate dehydrogenase complex
DIPiDIP-6782N
IntActiP12695, 61 interactors
MINTiP12695
STRINGi4932.YNL071W

PTM databases

iPTMnetiP12695
SwissPalmiP12695

Proteomic databases

MaxQBiP12695
PaxDbiP12695
PRIDEiP12695

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL071W_mRNA; YNL071W_mRNA; YNL071W
GeneIDi855653
KEGGisce:YNL071W

Organism-specific databases

EuPathDBiFungiDB:YNL071W
SGDiS000005015 LAT1

Phylogenomic databases

GeneTreeiENSGT00940000154943
HOGENOMiHOG000281566
InParanoidiP12695
KOiK00627
OMAiTMEFESF

Enzyme and pathway databases

BioCyciYEAST:YNL071W-MONOMER
ReactomeiR-SCE-389661 Glyoxylate metabolism and glycine degradation
R-SCE-70268 Pyruvate metabolism

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P12695

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR006257 LAT1
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 1 hit
TIGRFAMsiTIGR01349 PDHac_trf_mito, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit
PS51826 PSBD, 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 nameiODP2_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: P12695
Secondary accession number(s): D6W1A8
<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: October 1, 1989
Last sequence update: October 1, 1989
Last modified: May 8, 2019
This is version 198 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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