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Entry version 229 (08 May 2019)
Sequence version 2 (01 Apr 1990)
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Protein

Furin

Gene

FURIN

Organism
Homo sapiens (Human)
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

Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif (PubMed:11799113, PubMed:1629222, PubMed:1713771, PubMed:2251280, PubMed:24666235, PubMed:25974265, PubMed:7592877, PubMed:7690548, PubMed:9130696). Mediates processing of TGFB1, an essential step in TGF-beta-1 activation (PubMed:7737999).10 Publications
(Microbial infection) Probably cleaves and activates anthrax and diphtheria toxins.
(Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin.1 Publication
(Microbial infection) Able to cleave S.pneumoniae serine-rich repeat protein PsrP.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

Ca2+3 PublicationsNote: Binds 3 calcium ions per subunit.3 Publications

<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 the not secondly cleaved propeptide (PubMed:9130696, PubMed:11799113). Inhibited by m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine (m-guanidinomethyl-Phac-RVR-Amb) and 4-guanidinomethyl-phenylacteyl-Arg-Tle-Arg-4-amidinobenzylamide (MI-1148) (PubMed:24666235, PubMed:25974265).4 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 6.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi115Calcium 1Combined sources2 Publications1
<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 sitei153Charge relay systemPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei154SubstrateCombined sources2 Publications1
Metal bindingi162Calcium 1Combined sources2 Publications1
Metal bindingi174Calcium 2Combined sources2 Publications1
Metal bindingi179Calcium 2Combined sources2 Publications1
Metal bindingi181Calcium 2; via carbonyl oxygenCombined sources2 Publications1
Active sitei194Charge relay systemPROSITE-ProRule annotation1
Metal bindingi205Calcium 1; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi208Calcium 1Combined sources2 Publications1
Metal bindingi210Calcium 1; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi212Calcium 1; via carbonyl oxygenCombined sources2 Publications1
Binding sitei236SubstrateCombined sources2 Publications1
Metal bindingi258Calcium 3Combined sources2 Publications1
Binding sitei264SubstrateCombined sources2 Publications1
Metal bindingi301Calcium 3Combined sources2 Publications1
Binding sitei306SubstrateCombined sources2 Publications1
Binding sitei308SubstrateCombined sources2 Publications1
Metal bindingi331Calcium 3Combined sources2 Publications1
Active sitei368Charge relay systemPROSITE-ProRule annotation1
Binding sitei368SubstrateCombined sources2 Publications1

<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 functionHydrolase, Protease, Serine protease
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1181150 Signaling by NODAL
R-HSA-1442490 Collagen degradation
R-HSA-1566948 Elastic fibre formation
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins
R-HSA-167060 NGF processing
R-HSA-171286 Synthesis and processing of ENV and VPU
R-HSA-186797 Signaling by PDGF
R-HSA-1912420 Pre-NOTCH Processing in Golgi
R-HSA-2173789 TGF-beta receptor signaling activates SMADs
R-HSA-5210891 Uptake and function of anthrax toxins
R-HSA-6809371 Formation of the cornified envelope
R-HSA-8963889 Assembly of active LPL and LIPC lipase complexes
R-HSA-977225 Amyloid fiber formation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P09958

SIGNOR Signaling Network Open Resource

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SIGNORi
P09958

Protein family/group databases

MEROPS protease database

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MEROPSi
S08.071

<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:
Furin (EC:3.4.21.758 Publications)
Alternative name(s):
Dibasic-processing enzyme
Paired basic amino acid residue-cleaving enzyme
Short name:
PACE
<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:FURIN
Synonyms:FUR, PACE, PCSK3
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 15

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:8568 FURIN

Online Mendelian Inheritance in Man (OMIM)

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MIMi
136950 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P09958

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini108 – 715LumenalCuratedAdd BLAST608
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei716 – 738HelicalSequence analysisAdd BLAST23
Topological domaini739 – 794CytoplasmicCuratedAdd BLAST56

Keywords - Cellular componenti

Cell membrane, Endosome, Golgi apparatus, Membrane, Secreted

<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>Mutagenesisi72V → R: Loss of catalytic activity and propeptide second cleavage and removal. Abnormal accumulation in the early secretory pathway. 1 Publication1
Mutagenesisi75R → A: Loss of catalytic activity and, propeptide second cleavage and removal. Normal trafficking to the Golgi. 1 Publication1
Mutagenesisi153D → N: Loss of catalytic activity and propeptide first cleavage. Abnormal accumulation in the early secretory pathway. 2 Publications1
Mutagenesisi773 – 775SDS → DDD: Phosphomimetic mutant. Localization in early endosome is increased. 1 Publication3
Mutagenesisi773S → A: Slight reduction in phosphorylation. Loss of phosphorylation and abnormal accumulation in the early secretory pathway; when associated with A-775. 1 Publication1
Mutagenesisi775S → A: Slight reduction in phosphorylation. Loss of phosphorylation and abnormal accumulation in the early secretory pathway; when associated with A-773. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
5045

Open Targets

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OpenTargetsi
ENSG00000140564

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA32894

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2611

Drug and drug target database

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DrugBanki
DB03600 Decanoic Acid
DB04951 Pirfenidone

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2366

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
FURIN

Domain mapping of disease mutations (DMDM)

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DMDMi
120611

<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 – 26Sequence analysisAdd BLAST26
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002702827 – 107Inhibition peptide1 PublicationAdd BLAST81
<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_0000027029108 – 794FurinAdd BLAST687

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 bondi211 ↔ 3602 Publications
Disulfide bondi303 ↔ 3332 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi387N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi440N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi450 ↔ 4742 Publications
Glycosylationi553N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei773Phosphoserine; by CK21 Publication1
Modified residuei775Phosphoserine; by CK21 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 inhibition peptide, which plays the role of an intramolecular chaperone, is autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound to furin as a potent autoinhibitor. Following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in propeptide dissociation and furin activation.2 Publications
Phosphorylation is required for TGN localization of the endoprotease. In vivo, exists as di-, mono- and non-phosphorylated forms.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei75 – 76Cleavage, second; by autolysis1 Publication2
Sitei107 – 108Cleavage, first; by autolysis2 Publications2

Keywords - PTMi

Autocatalytic cleavage, Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P09958

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P09958

MaxQB - The MaxQuant DataBase

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MaxQBi
P09958

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

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PaxDbi
P09958

PeptideAtlas

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PeptideAtlasi
P09958

PRoteomics IDEntifications database

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PRIDEi
P09958

ProteomicsDB human proteome resource

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ProteomicsDBi
52283

2D gel databases

USC-OGP 2-DE database

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OGPi
P09958

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P09958

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P09958

SwissPalm database of S-palmitoylation events

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SwissPalmi
P09958

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P09958

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Seems to be expressed ubiquitously.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000140564 Expressed in 223 organ(s), highest expression level in right lobe of liver

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P09958 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P09958 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB009499

<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 FLNA (By similarity). Binds to PACS1 which mediates TGN localization and connection to clathrin adapters (PubMed:11331585).By similarity1 Publication

<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)

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BioGridi
111082, 41 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P09958

Database of interacting proteins

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DIPi
DIP-29904N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P09958

Protein interaction database and analysis system

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IntActi
P09958, 16 interactors

Molecular INTeraction database

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MINTi
P09958

STRING: functional protein association networks

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STRINGi
9606.ENSP00000483552

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P09958

<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

Secondary structure

1794
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OMCX-ray2.30A/B/C/D/E/F108-574[»]
4OMDX-ray2.70A/B/C/D/E/F108-574[»]
4RYDX-ray2.15A/B/C/D/E/F108-574[»]
4Z2AX-ray1.89A110-574[»]
5JMOX-ray2.00A/B108-574[»]
5JXGX-ray1.80A108-574[»]
5JXHX-ray2.00A108-574[»]
5JXIX-ray2.00A108-574[»]
5JXJX-ray2.00A108-574[»]
5MIMX-ray1.90A108-574[»]
6EQVX-ray1.90A108-574[»]
6EQWX-ray1.99A108-574[»]
6EQXX-ray1.99A108-567[»]
6HLBX-ray2.00A108-574[»]
6HLDX-ray2.10A108-574[»]
6HLEX-ray1.99A108-574[»]
6HZAX-ray1.90A108-574[»]
6HZBX-ray1.90A108-574[»]
6HZCX-ray1.90A108-574[»]
6HZDX-ray1.90A108-574[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P09958

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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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>Domaini144 – 427Peptidase S8Sequence analysisAdd BLAST284
Domaini444 – 576P/Homo BPROSITE-ProRule annotationAdd BLAST133
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati577 – 620FU 1Sequence analysisAdd BLAST44
Repeati638 – 681FU 2Sequence analysisAdd BLAST44

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>Regioni191 – 192Substrate bindingCombined sources2 Publications2
Regioni253 – 258Substrate bindingCombined sources2 Publications6
Regioni292 – 295Substrate bindingCombined sources2 Publications4
Regioni759 – 762Cell surface signal1 Publication4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi498 – 500Cell attachment siteSequence analysis3
Motifi773 – 779Trans Golgi network signal1 Publication7

<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

Contains a cytoplasmic domain responsible for its TGN localization and recycling from the cell surface.1 Publication

<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 peptidase S8 family. Furin subfamily.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3525 Eukaryota
COG1404 LUCA
COG4935 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157220

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000192536

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P09958

KEGG Orthology (KO)

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KOi
K01349

Identification of Orthologs from Complete Genome Data

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OMAi
GPQRKCV

Database of Orthologous Groups

More...
OrthoDBi
473018at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P09958

TreeFam database of animal gene trees

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TreeFami
TF314277

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00064 FU, 2 hits
cd04059 Peptidases_S8_Protein_converta, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.260, 1 hit
3.30.70.850, 1 hit
3.40.50.200, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006212 Furin_repeat
IPR008979 Galactose-bd-like_sf
IPR009030 Growth_fac_rcpt_cys_sf
IPR034182 Kexin/furin
IPR002884 P_dom
IPR000209 Peptidase_S8/S53_dom
IPR036852 Peptidase_S8/S53_dom_sf
IPR023827 Peptidase_S8_Asp-AS
IPR022398 Peptidase_S8_His-AS
IPR023828 Peptidase_S8_Ser-AS
IPR015500 Peptidase_S8_subtilisin-rel
IPR032815 S8_pro-domain
IPR038466 S8_pro-domain_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01483 P_proprotein, 1 hit
PF00082 Peptidase_S8, 1 hit
PF16470 S8_pro-domain, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00723 SUBTILISIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00261 FU, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49785 SSF49785, 1 hit
SSF52743 SSF52743, 1 hit
SSF57184 SSF57184, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51829 P_HOMO_B, 1 hit
PS00136 SUBTILASE_ASP, 1 hit
PS00137 SUBTILASE_HIS, 1 hit
PS00138 SUBTILASE_SER, 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P09958-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELRPWLLWV VAATGTLVLL AADAQGQKVF TNTWAVRIPG GPAVANSVAR
60 70 80 90 100
KHGFLNLGQI FGDYYHFWHR GVTKRSLSPH RPRHSRLQRE PQVQWLEQQV
110 120 130 140 150
AKRRTKRDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS
160 170 180 190 200
ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG
210 220 230 240 250
EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY
260 270 280 290 300
SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH
310 320 330 340 350
DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ
360 370 380 390 400
IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT
410 420 430 440 450
SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC
460 470 480 490 500
IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD
510 520 530 540 550
LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE
560 570 580 590 600
IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE
610 620 630 640 650
EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT
660 670 680 690 700
CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA
710 720 730 740 750
GQRLRAGLLP SHLPEVVAGL SCAFIVLVFV TVFLVLQLRS GFSFRGVKVY
760 770 780 790
TMDRGLISYK GLPPEAWQEE CPSDSEEDEG RGERTAFIKD QSAL
Length:794
Mass (Da):86,678
Last modified:April 1, 1990 - v2
<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:i10C44DD5892EF85D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YLH7H0YLH7_HUMAN
Furin
FURIN
175Annotation score:

Annotation score:1 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>
H0YKB2H0YKB2_HUMAN
Furin
FURIN
69Annotation score:

Annotation score:1 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>
H0YNB5H0YNB5_HUMAN
Furin
FURIN
216Annotation score:

Annotation score:1 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>
A0A1W2PPZ9A0A1W2PPZ9_HUMAN
Furin
FURIN
69Annotation score:

Annotation score:1 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_05182143A → V. Corresponds to variant dbSNP:rs16944971Ensembl.1
Natural variantiVAR_055343547W → R in cell line LoVo; does not undergo autocatalytic activation and is not transported to the Golgi apparatus. 1 Publication1

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
X17094 mRNA Translation: CAA34948.1
BC012181 mRNA Translation: AAH12181.1
X15723 Genomic DNA Translation: CAA33745.1
X04329 Genomic DNA Translation: CAA27860.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS10364.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A39552 KXHUF

NCBI Reference Sequences

More...
RefSeqi
NP_001276752.1, NM_001289823.1
NP_001276753.1, NM_001289824.1
NP_002560.1, NM_002569.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000268171; ENSP00000268171; ENSG00000140564
ENST00000610579; ENSP00000484952; ENSG00000140564
ENST00000618099; ENSP00000483552; ENSG00000140564

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5045

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5045

UCSC genome browser

More...
UCSCi
uc002bpu.2 human

Keywords - Coding sequence diversityi

Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17094 mRNA Translation: CAA34948.1
BC012181 mRNA Translation: AAH12181.1
X15723 Genomic DNA Translation: CAA33745.1
X04329 Genomic DNA Translation: CAA27860.1
CCDSiCCDS10364.1
PIRiA39552 KXHUF
RefSeqiNP_001276752.1, NM_001289823.1
NP_001276753.1, NM_001289824.1
NP_002560.1, NM_002569.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OMCX-ray2.30A/B/C/D/E/F108-574[»]
4OMDX-ray2.70A/B/C/D/E/F108-574[»]
4RYDX-ray2.15A/B/C/D/E/F108-574[»]
4Z2AX-ray1.89A110-574[»]
5JMOX-ray2.00A/B108-574[»]
5JXGX-ray1.80A108-574[»]
5JXHX-ray2.00A108-574[»]
5JXIX-ray2.00A108-574[»]
5JXJX-ray2.00A108-574[»]
5MIMX-ray1.90A108-574[»]
6EQVX-ray1.90A108-574[»]
6EQWX-ray1.99A108-574[»]
6EQXX-ray1.99A108-567[»]
6HLBX-ray2.00A108-574[»]
6HLDX-ray2.10A108-574[»]
6HLEX-ray1.99A108-574[»]
6HZAX-ray1.90A108-574[»]
6HZBX-ray1.90A108-574[»]
6HZCX-ray1.90A108-574[»]
6HZDX-ray1.90A108-574[»]
SMRiP09958
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111082, 41 interactors
CORUMiP09958
DIPiDIP-29904N
ELMiP09958
IntActiP09958, 16 interactors
MINTiP09958
STRINGi9606.ENSP00000483552

Chemistry databases

BindingDBiP09958
ChEMBLiCHEMBL2611
DrugBankiDB03600 Decanoic Acid
DB04951 Pirfenidone
GuidetoPHARMACOLOGYi2366

Protein family/group databases

MEROPSiS08.071

PTM databases

iPTMnetiP09958
PhosphoSitePlusiP09958
SwissPalmiP09958

Polymorphism and mutation databases

BioMutaiFURIN
DMDMi120611

2D gel databases

OGPiP09958

Proteomic databases

EPDiP09958
jPOSTiP09958
MaxQBiP09958
PaxDbiP09958
PeptideAtlasiP09958
PRIDEiP09958
ProteomicsDBi52283

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268171; ENSP00000268171; ENSG00000140564
ENST00000610579; ENSP00000484952; ENSG00000140564
ENST00000618099; ENSP00000483552; ENSG00000140564
GeneIDi5045
KEGGihsa:5045
UCSCiuc002bpu.2 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5045
DisGeNETi5045

GeneCards: human genes, protein and diseases

More...
GeneCardsi
FURIN
HGNCiHGNC:8568 FURIN
HPAiCAB009499
MIMi136950 gene
neXtProtiNX_P09958
OpenTargetsiENSG00000140564
PharmGKBiPA32894

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3525 Eukaryota
COG1404 LUCA
COG4935 LUCA
GeneTreeiENSGT00940000157220
HOGENOMiHOG000192536
InParanoidiP09958
KOiK01349
OMAiGPQRKCV
OrthoDBi473018at2759
PhylomeDBiP09958
TreeFamiTF314277

Enzyme and pathway databases

ReactomeiR-HSA-1181150 Signaling by NODAL
R-HSA-1442490 Collagen degradation
R-HSA-1566948 Elastic fibre formation
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins
R-HSA-167060 NGF processing
R-HSA-171286 Synthesis and processing of ENV and VPU
R-HSA-186797 Signaling by PDGF
R-HSA-1912420 Pre-NOTCH Processing in Golgi
R-HSA-2173789 TGF-beta receptor signaling activates SMADs
R-HSA-5210891 Uptake and function of anthrax toxins
R-HSA-6809371 Formation of the cornified envelope
R-HSA-8963889 Assembly of active LPL and LIPC lipase complexes
R-HSA-977225 Amyloid fiber formation
SignaLinkiP09958
SIGNORiP09958

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
FURIN human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Furin

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5045
PMAP-CutDBiP09958

Protein Ontology

More...
PROi
PR:P09958

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000140564 Expressed in 223 organ(s), highest expression level in right lobe of liver
ExpressionAtlasiP09958 baseline and differential
GenevisibleiP09958 HS

Family and domain databases

CDDicd00064 FU, 2 hits
cd04059 Peptidases_S8_Protein_converta, 1 hit
Gene3Di2.60.120.260, 1 hit
3.30.70.850, 1 hit
3.40.50.200, 1 hit
InterProiView protein in InterPro
IPR006212 Furin_repeat
IPR008979 Galactose-bd-like_sf
IPR009030 Growth_fac_rcpt_cys_sf
IPR034182 Kexin/furin
IPR002884 P_dom
IPR000209 Peptidase_S8/S53_dom
IPR036852 Peptidase_S8/S53_dom_sf
IPR023827 Peptidase_S8_Asp-AS
IPR022398 Peptidase_S8_His-AS
IPR023828 Peptidase_S8_Ser-AS
IPR015500 Peptidase_S8_subtilisin-rel
IPR032815 S8_pro-domain
IPR038466 S8_pro-domain_sf
PfamiView protein in Pfam
PF01483 P_proprotein, 1 hit
PF00082 Peptidase_S8, 1 hit
PF16470 S8_pro-domain, 1 hit
PRINTSiPR00723 SUBTILISIN
SMARTiView protein in SMART
SM00261 FU, 2 hits
SUPFAMiSSF49785 SSF49785, 1 hit
SSF52743 SSF52743, 1 hit
SSF57184 SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS51829 P_HOMO_B, 1 hit
PS00136 SUBTILASE_ASP, 1 hit
PS00137 SUBTILASE_HIS, 1 hit
PS00138 SUBTILASE_SER, 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 nameiFURIN_HUMAN
<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: P09958
Secondary accession number(s): Q14336, Q6LBS3, Q9UCZ5
<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: July 1, 1989
Last sequence update: April 1, 1990
Last modified: May 8, 2019
This is version 229 of the entry and version 2 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
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.

<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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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