Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 198 (18 Sep 2019)
Sequence version 2 (14 Oct 2008)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Serine/threonine-protein kinase D1

Gene

PRKD1

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

Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-463 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenetic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor. Plays a role in activated KRAS-mediated stabilization of ZNF304 in colorectal cancer (CRC) cells (PubMed:24623306). Regulates nuclear translocation of transcription factor TFEB in macrophages upon live S.enterica infection (By similarity).By similarity11 Publications

<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

Mg2+

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domain 1 binds DAG with high affinity and appears to play the dominant role in mediating translocation to the cell membrane and trans-Golgi network. Phorbol-ester/DAG-type domain 2 binds phorbol ester with higher affinity. Autophosphorylation of Ser-742 and phosphorylation of Ser-738 by PKC relieves auto-inhibition by the PH domain. Phosphorylation on Tyr-463 by the SRC-ABL1 pathway in response to oxidative stress, is also required for activation. Activated by DAPK1 under oxidative stress.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei612ATP1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei706Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri146 – 196Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri270 – 320Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi589 – 597ATPPROSITE-ProRule annotation9

<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 functionKinase, Serine/threonine-protein kinase, Transferase
Biological processAngiogenesis, Apoptosis, Differentiation, Immunity, Inflammatory response, Innate immunity, Neurogenesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.13 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1660661 Sphingolipid de novo biosynthesis

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

More...
SignaLinki
Q15139

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q15139

<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:
Serine/threonine-protein kinase D1 (EC:2.7.11.13)
Alternative name(s):
Protein kinase C mu type
Protein kinase D
nPKC-D1
nPKC-mu
<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:PRKD1
Synonyms:PKD, PKD1, PRKCM
<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 14

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:9407 PRKD1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
605435 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q15139

<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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Congenital heart defects and ectodermal dysplasia (CHDED)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant syndrome characterized by atrial and/or ventricular septal congenital heart defects and variable features of ectodermal dysplasia, including sparse hair, dry skin, thin skin, fragile nails, premature loss of primary teeth, and small widely spaced teeth. Patients manifest developmental disabilities ranging from motor delay and delayed speech to global developmental retardation.
Related information in OMIM
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_078602299L → W in CHDED. 1 PublicationCorresponds to variant dbSNP:rs1057519636Ensembl.1
Natural variantiVAR_078603592G → R in CHDED. 1 PublicationCorresponds to variant dbSNP:rs1057519635Ensembl.1

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>Mutagenesisi157P → G: Increase in ability to bind phorbol ester, loss of ability to bind DAG. 1 Publication1
Mutagenesisi281P → G: No effect on ability to bind phorbol ester, slight increase in ability to bind DAG. 1 Publication1
Mutagenesisi432Y → E: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. 1 Publication1
Mutagenesisi432Y → F: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. Unaltered kinase activity. Decreased kinase activity; when associated with F-463 and F-502. 1 Publication1
Mutagenesisi463Y → E: Constitutive activation and constitutive phosphorylation of S-738 and S-742. 1 Publication1
Mutagenesisi463Y → F: Decreased phosphorylation level when coexpressed with either SRC or ABL in HeLa cells. Decreased kinase activity. 1 Publication1
Mutagenesisi502Y → E: Loss of activation. 1 Publication1
Mutagenesisi502Y → F: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. Unaltered kinase activity. Decreased kinase activity; when associated with F-432 and F-502. 1 Publication1
Mutagenesisi612K → W: Loss of kinase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Ectodermal dysplasia

Organism-specific databases

DisGeNET

More...
DisGeNETi
5587

MalaCards human disease database

More...
MalaCardsi
PRKD1
MIMi617364 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000184304

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
276145 Malignant epithelial tumor of salivary glands

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA33771

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q15139

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3863

Drug and drug target database

More...
DrugBanki
DB12010 Fostamatinib

DrugCentral

More...
DrugCentrali
Q15139

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1489

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PRKD1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
209572639

<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_00000557141 – 912Serine/threonine-protein kinase D1Add BLAST912

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 residuei95Phosphotyrosine1 Publication1
Modified residuei205PhosphoserineCombined sources1
Modified residuei208PhosphoserineCombined sources1
Modified residuei219PhosphoserineBy similarity1
Modified residuei223PhosphoserineBy similarity1
Modified residuei345PhosphoserineCombined sources1
Modified residuei397Phosphoserine; by MAPK131 Publication1
Modified residuei401Phosphoserine; by MAPK131 Publication1
Modified residuei432Phosphotyrosine1 Publication1
Modified residuei448PhosphoserineCombined sources1
Modified residuei463Phosphotyrosine; by ABL2 Publications1
Modified residuei473PhosphoserineCombined sources1
Modified residuei502Phosphotyrosine1 Publication1
Modified residuei548PhosphoserineBy similarity1
Modified residuei738Phosphoserine; by PKC/PRKCD1 Publication1
Modified residuei742Phosphoserine; by autocatalysis and PKC/PRKCD1 Publication1
Modified residuei749PhosphotyrosineBy similarity1
Modified residuei910Phosphoserine; by autocatalysis1 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

Phosphorylated at Ser-397 and Ser-401 by MAPK13 during regulation of insulin secretion in pancreatic beta cells (PubMed:19135240). Phosphorylated by DAPK1 (PubMed:17703233). Phosphorylated at Tyr-95 and by ABL at Tyr-463, which primes the kinase in response to oxidative stress, and promotes a second step activating phosphorylation at Ser-738/Ser-742 by PKRD (PubMed:12637538, PubMed:15024053, PubMed:17804414). Phosphorylated on Ser-910 upon S.enterica infection in macrophages (By similarity).By similarity5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q15139

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q15139

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q15139

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q15139

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

More...
PaxDbi
Q15139

PeptideAtlas

More...
PeptideAtlasi
Q15139

PRoteomics IDEntifications database

More...
PRIDEi
Q15139

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
60458

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q15139

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

More...
PhosphoSitePlusi
Q15139

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by the intestine-specific transcription factor CDX1 in an activated KRAS-dependent manner in colorectal cancer (CRC) cells (PubMed:24623306).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000184304 Expressed in 184 organ(s), highest expression level in urinary bladder

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q15139 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q15139 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB018367
HPA029834

<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 (via N-terminus) with ADAP1/CENTA1 (PubMed:12893243).

Interacts with MAPK13 (PubMed:19135240).

Interacts with DAPK1 in an oxidative stress-regulated manner (PubMed:17703233).

Interacts with USP28; the interaction induces phosphorylation of USP28 and activated KRAS-mediated stabilization of ZNF304 (PubMed:24623306).

Interacts with AKAP13 (via C-terminal domain) (By similarity).

By similarity4 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
111573, 38 interactors

Database of interacting proteins

More...
DIPi
DIP-38481N

Protein interaction database and analysis system

More...
IntActi
Q15139, 13 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000333568

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q15139

<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
Q15139

Database of comparative protein structure models

More...
ModBasei
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>Domaini422 – 541PHPROSITE-ProRule annotationAdd BLAST120
Domaini583 – 839Protein kinasePROSITE-ProRule annotationAdd BLAST257

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi17 – 26Poly-Ala10
Compositional biasi200 – 203Poly-Arg4

<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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri146 – 196Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri270 – 320Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4236 Eukaryota
ENOG410XQZ3 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183024

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q15139

KEGG Orthology (KO)

More...
KOi
K06070

Database of Orthologous Groups

More...
OrthoDBi
1444458at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q15139

TreeFam database of animal gene trees

More...
TreeFami
TF314320

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00029 C1, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR020454 DAG/PE-bd
IPR011009 Kinase-like_dom_sf
IPR002219 PE/DAG-bd
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR015727 Protein_Kinase_C_mu-related
IPR008271 Ser/Thr_kinase_AS

The PANTHER Classification System

More...
PANTHERi
PTHR22968 PTHR22968, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00130 C1_1, 2 hits
PF00169 PH, 1 hit
PF00069 Pkinase, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000552 PKC_mu_nu_D2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00008 DAGPEDOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00109 C1, 2 hits
SM00233 PH, 1 hit
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50003 PH_DOMAIN, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
PS00479 ZF_DAG_PE_1, 2 hits
PS50081 ZF_DAG_PE_2, 2 hits

<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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All

Q15139-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSAPPVLRPP SPLLPVAAAA AAAAAALVPG SGPGPAPFLA PVAAPVGGIS
60 70 80 90 100
FHLQIGLSRE PVLLLQDSSG DYSLAHVREM ACSIVDQKFP ECGFYGMYDK
110 120 130 140 150
ILLFRHDPTS ENILQLVKAA SDIQEGDLIE VVLSASATFE DFQIRPHALF
160 170 180 190 200
VHSYRAPAFC DHCGEMLWGL VRQGLKCEGC GLNYHKRCAF KIPNNCSGVR
210 220 230 240 250
RRRLSNVSLT GVSTIRTSSA ELSTSAPDEP LLQKSPSESF IGREKRSNSQ
260 270 280 290 300
SYIGRPIHLD KILMSKVKVP HTFVIHSYTR PTVCQYCKKL LKGLFRQGLQ
310 320 330 340 350
CKDCRFNCHK RCAPKVPNNC LGEVTINGDL LSPGAESDVV MEEGSDDNDS
360 370 380 390 400
ERNSGLMDDM EEAMVQDAEM AMAECQNDSG EMQDPDPDHE DANRTISPST
410 420 430 440 450
SNNIPLMRVV QSVKHTKRKS STVMKEGWMV HYTSKDTLRK RHYWRLDSKC
460 470 480 490 500
ITLFQNDTGS RYYKEIPLSE ILSLEPVKTS ALIPNGANPH CFEITTANVV
510 520 530 540 550
YYVGENVVNP SSPSPNNSVL TSGVGADVAR MWEIAIQHAL MPVIPKGSSV
560 570 580 590 600
GTGTNLHRDI SVSISVSNCQ IQENVDISTV YQIFPDEVLG SGQFGIVYGG
610 620 630 640 650
KHRKTGRDVA IKIIDKLRFP TKQESQLRNE VAILQNLHHP GVVNLECMFE
660 670 680 690 700
TPERVFVVME KLHGDMLEMI LSSEKGRLPE HITKFLITQI LVALRHLHFK
710 720 730 740 750
NIVHCDLKPE NVLLASADPF PQVKLCDFGF ARIIGEKSFR RSVVGTPAYL
760 770 780 790 800
APEVLRNKGY NRSLDMWSVG VIIYVSLSGT FPFNEDEDIH DQIQNAAFMY
810 820 830 840 850
PPNPWKEISH EAIDLINNLL QVKMRKRYSV DKTLSHPWLQ DYQTWLDLRE
860 870 880 890 900
LECKIGERYI THESDDLRWE KYAGEQGLQY PTHLINPSAS HSDTPETEET
910
EMKALGERVS IL
Length:912
Mass (Da):101,704
Last modified:October 14, 2008 - 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:i0BC9414C335D2DBB
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 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8WBA3F8WBA3_HUMAN
Serine/threonine-protein kinase
PRKD1
920Annotation score:

Annotation score:4 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>
F8VZ98F8VZ98_HUMAN
Serine/threonine-protein kinase D1
PRKD1
117Annotation 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>
A0A494C0Q1A0A494C0Q1_HUMAN
Serine/threonine-protein kinase D1
PRKD1
158Annotation 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>
H0YHL5H0YHL5_HUMAN
Serine/threonine-protein kinase D1
PRKD1
157Annotation 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>
H0YHS9H0YHS9_HUMAN
Serine/threonine-protein kinase D1
PRKD1
80Annotation 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>
A0A494C196A0A494C196_HUMAN
Serine/threonine-protein kinase D1
PRKD1
48Annotation 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>

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 conflicti135A → R in CAA53384 (PubMed:8119958).Curated1
Sequence conflicti877G → R in CAA53384 (PubMed:8119958).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035468152H → Y in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1383618278Ensembl.1
Natural variantiVAR_042324225S → P1 Publication1
Natural variantiVAR_078602299L → W in CHDED. 1 PublicationCorresponds to variant dbSNP:rs1057519636Ensembl.1
Natural variantiVAR_042325478K → Q1 PublicationCorresponds to variant dbSNP:rs55852813Ensembl.1
Natural variantiVAR_042326585P → S in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_078603592G → R in CHDED. 1 PublicationCorresponds to variant dbSNP:rs1057519635Ensembl.1
Natural variantiVAR_042327677R → M in a lung bronchoalveolar carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042328679P → L1 PublicationCorresponds to variant dbSNP:rs34588699Ensembl.1
Natural variantiVAR_046988825R → K. Corresponds to variant dbSNP:rs11161065Ensembl.1
Natural variantiVAR_035469857E → K in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_042329891H → R1 PublicationCorresponds to variant dbSNP:rs45582934Ensembl.1

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
X75756 mRNA Translation: CAA53384.1
AK314170 mRNA Translation: BAG36853.1
AL135858 Genomic DNA No translation available.
CH471078 Genomic DNA Translation: EAW65971.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS9637.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A53215

NCBI Reference Sequences

More...
RefSeqi
NP_002733.2, NM_002742.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000331968; ENSP00000333568; ENSG00000184304
ENST00000616995; ENSP00000482645; ENSG00000184304

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5587

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5587

UCSC genome browser

More...
UCSCi
uc001wqh.4 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
X75756 mRNA Translation: CAA53384.1
AK314170 mRNA Translation: BAG36853.1
AL135858 Genomic DNA No translation available.
CH471078 Genomic DNA Translation: EAW65971.1
CCDSiCCDS9637.1
PIRiA53215
RefSeqiNP_002733.2, NM_002742.2

3D structure databases

SMRiQ15139
ModBaseiSearch...

Protein-protein interaction databases

BioGridi111573, 38 interactors
DIPiDIP-38481N
IntActiQ15139, 13 interactors
STRINGi9606.ENSP00000333568

Chemistry databases

BindingDBiQ15139
ChEMBLiCHEMBL3863
DrugBankiDB12010 Fostamatinib
DrugCentraliQ15139
GuidetoPHARMACOLOGYi1489

PTM databases

iPTMnetiQ15139
PhosphoSitePlusiQ15139

Polymorphism and mutation databases

BioMutaiPRKD1
DMDMi209572639

Proteomic databases

EPDiQ15139
jPOSTiQ15139
MassIVEiQ15139
MaxQBiQ15139
PaxDbiQ15139
PeptideAtlasiQ15139
PRIDEiQ15139
ProteomicsDBi60458

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5587

Genome annotation databases

EnsembliENST00000331968; ENSP00000333568; ENSG00000184304
ENST00000616995; ENSP00000482645; ENSG00000184304
GeneIDi5587
KEGGihsa:5587
UCSCiuc001wqh.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5587
DisGeNETi5587

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PRKD1
HGNCiHGNC:9407 PRKD1
HPAiCAB018367
HPA029834
MalaCardsiPRKD1
MIMi605435 gene
617364 phenotype
neXtProtiNX_Q15139
OpenTargetsiENSG00000184304
Orphaneti276145 Malignant epithelial tumor of salivary glands
PharmGKBiPA33771

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4236 Eukaryota
ENOG410XQZ3 LUCA
GeneTreeiENSGT00950000183024
InParanoidiQ15139
KOiK06070
OrthoDBi1444458at2759
PhylomeDBiQ15139
TreeFamiTF314320

Enzyme and pathway databases

BRENDAi2.7.11.13 2681
ReactomeiR-HSA-1660661 Sphingolipid de novo biosynthesis
SignaLinkiQ15139
SIGNORiQ15139

Miscellaneous databases

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

More...
ChiTaRSi
PRKD1 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Protein_kinase_D1

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

More...
GenomeRNAii
5587
PharosiQ15139

Protein Ontology

More...
PROi
PR:Q15139

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000184304 Expressed in 184 organ(s), highest expression level in urinary bladder
ExpressionAtlasiQ15139 baseline and differential
GenevisibleiQ15139 HS

Family and domain databases

CDDicd00029 C1, 2 hits
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR020454 DAG/PE-bd
IPR011009 Kinase-like_dom_sf
IPR002219 PE/DAG-bd
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR015727 Protein_Kinase_C_mu-related
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR22968 PTHR22968, 1 hit
PfamiView protein in Pfam
PF00130 C1_1, 2 hits
PF00169 PH, 1 hit
PF00069 Pkinase, 1 hit
PIRSFiPIRSF000552 PKC_mu_nu_D2, 1 hit
PRINTSiPR00008 DAGPEDOMAIN
SMARTiView protein in SMART
SM00109 C1, 2 hits
SM00233 PH, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50003 PH_DOMAIN, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
PS00479 ZF_DAG_PE_1, 2 hits
PS50081 ZF_DAG_PE_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiKPCD1_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: Q15139
Secondary accession number(s): A6NL64, B2RAF6
<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: November 1, 1997
Last sequence update: October 14, 2008
Last modified: September 18, 2019
This is version 198 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again