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Protein

Serine/threonine-protein phosphatase 5

Gene

PPP5C

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

Functioni

Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses. Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress. Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function. Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1. Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E. May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels. Dephosphorylates and may play a role in the regulation of TAU/MAPT. Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2.15 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Mg2+, Mn2+Note: Binds 2 Mg2+ or Mn2+ cations per subunit.

Activity regulationi

Autoinhibited. In the autoinhibited state, the TPR domain interacts with the catalytic region and prevents substrate access to the catalytic pocket. Allosterically activated by various polyunsaturated fatty acids, free long-chain fatty-acids and long-chain fatty acyl-CoA esters, arachidonic acid being the most effective activator. HSP90A and probably RAC1, GNA12 and GNA13 can also release the autoinhibition by the TPR repeat. Activation by RAC1, GNA12 and GNA13 is synergistic with the one produced by fatty acids binding. Inhibited by okadaic acid.6 Publications

Kineticsi

  1. KM=1.847 µM for CSNK1E (at 30 degrees Celsius)2 Publications
  2. KM=13.2 µM for MAPT/TAU (at pH 7.4 and 30 degrees Celsius)2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi242Manganese 1Combined sources3 Publications1
    Metal bindingi244Manganese 1; via tele nitrogenCombined sources3 Publications1
    Binding sitei244Substrate1 Publication1
    Metal bindingi271Manganese 1Combined sources3 Publications1
    Metal bindingi271Manganese 2Combined sources3 Publications1
    Binding sitei275Substrate1 Publication1
    Metal bindingi303Manganese 2Combined sources3 Publications1
    Active sitei304Proton donor/acceptor1 Publication1
    Metal bindingi352Manganese 2; via tele nitrogenCombined sources3 Publications1
    Binding sitei400Substrate1 Publication1
    Metal bindingi427Manganese 2; via pros nitrogenCombined sources3 Publications1
    Binding sitei427Substrate1 Publication1

    GO - Molecular functioni

    • ADP binding Source: MGI
    • ATP binding Source: MGI
    • G-protein alpha-subunit binding Source: Ensembl
    • Hsp90 protein binding Source: CAFA
    • identical protein binding Source: IntAct
    • lipid binding Source: UniProtKB-KW
    • metal ion binding Source: UniProtKB-KW
    • microtubule binding Source: Ensembl
    • phosphatase activity Source: ARUK-UCL
    • phosphoprotein phosphatase activity Source: UniProtKB
    • protein serine/threonine phosphatase activity Source: ARUK-UCL
    • RNA binding Source: Ensembl

    GO - Biological processi

    Keywordsi

    Molecular functionHydrolase, Protein phosphatase
    Biological processDNA damage, DNA repair
    LigandLipid-binding, Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.3.16 2681
    ReactomeiR-HSA-5675221 Negative regulation of MAPK pathway
    R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
    R-HSA-8939211 ESR-mediated signaling
    SABIO-RKiP53041
    SignaLinkiP53041
    SIGNORiP53041

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 5 (EC:3.1.3.16)
    Short name:
    PP5
    Alternative name(s):
    Protein phosphatase T
    Short name:
    PP-T
    Short name:
    PPT
    Gene namesi
    Name:PPP5C
    Synonyms:PPP5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 19

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000011485.14
    HGNCiHGNC:9322 PPP5C
    MIMi600658 gene
    neXtProtiNX_P53041

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Amyloid, Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi32K → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. 1 Publication1
    Mutagenesisi74R → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. 1 Publication1
    Mutagenesisi83G → N: No effect on interaction with HSP90AA1. 1 Publication1
    Mutagenesisi93K → E: Decreases interaction with RAC1 and translocation to the membrane in presence of active RAC1. 1 Publication1
    Mutagenesisi97K → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. Loss of interaction with RAF1. 2 Publications1
    Mutagenesisi101R → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. 1 Publication1
    Mutagenesisi304H → Q: Catalytically inactive; no effect on interaction with CRY2 but increases the stability of the interaction with CSNK1E. No effect on RAF1 phosphorylation. 3 Publications1

    Keywords - Diseasei

    Alzheimer disease, Amyloidosis, Neurodegeneration

    Organism-specific databases

    DisGeNETi5536
    OpenTargetsiENSG00000011485
    PharmGKBiPA33686

    Chemistry databases

    ChEMBLiCHEMBL3425389

    Polymorphism and mutation databases

    BioMutaiPPP5C
    DMDMi1709744

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00000588942 – 499Serine/threonine-protein phosphatase 5Add BLAST498

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1

    Post-translational modificationi

    Activated by at least two different proteolytic cleavages producing a 56 kDa and a 50 kDa form.2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiP53041
    MaxQBiP53041
    PaxDbiP53041
    PeptideAtlasiP53041
    PRIDEiP53041
    ProteomicsDBi56568

    PTM databases

    DEPODiP53041
    iPTMnetiP53041
    PhosphoSitePlusiP53041

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    BgeeiENSG00000011485 Expressed in 160 organ(s), highest expression level in frontal cortex
    CleanExiHS_PPP5C
    ExpressionAtlasiP53041 baseline and differential
    GenevisibleiP53041 HS

    Organism-specific databases

    HPAiCAB022641
    HPA029065
    HPA056933

    Interactioni

    Subunit structurei

    Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (PubMed:29127155). Part of a complex with HSP90/HSP90AA1 and steroid receptors (By similarity). Interacts (via TPR repeats) with HSP90AA1 (via TPR repeat-binding motif) or HSPA1A/HSPA1B; the interaction is direct and activates the phosphatase activity (PubMed:15383005, PubMed:15577939, PubMed:16531226). Dissociates from HSPA1A/HSPA1B and HSP90AA1 in response to arachidonic acid (PubMed:15383005). Interacts with CPNE1 (via VWFA domain) (By similarity). Interacts with CDC16, CDC27 (PubMed:9405394). Interacts with KLHDC10 (via the 6 Kelch repeats); inhibits the phosphatase activity on MAP3K5 (PubMed:23102700). Interacts with ATM and ATR; both interactions are induced by DNA damage and enhance ATM and ATR kinase activity (PubMed:14871926). Interacts with RAD17; reduced by DNA damage (PubMed:14871926). Interacts with nuclear receptors such as NR3C1/GCR and PPARG (activated by agonist); regulates their transactivation activities (By similarity). Interacts (via TPR repeats) with S100 proteins S100A1, S100A2, S100A6, S100B and S100P; the interactions are calcium-dependent, strongly activate PPP5C phosphatase activity and compete with HSP90AA1 and MAP3K5 interactions (PubMed:22399290). Interacts with SMAD2 and SMAD3 but not with SMAD1; decreases SMAD3 phosphorylation and protein levels (PubMed:22781750). Interacts (via TPR repeats) with CRY1 and CRY2; the interaction with CRY2 downregulates the phosphatase activity on CSNK1E (PubMed:16790549). Interacts (via TPR repeats) with the active form of RAC1, GNA12 or GNA13; these interactions activate the phosphatase activity and translocate PPP5C to the cell membrane (PubMed:19948726). Interacts with FLCN (PubMed:27353360).By similarity12 Publications

    Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    BioGridi111528, 87 interactors
    DIPiDIP-29043N
    IntActiP53041, 64 interactors
    MINTiP53041
    STRINGi9606.ENSP00000012443

    Chemistry databases

    BindingDBiP53041

    Structurei

    Secondary structure

    1499
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    DisProtiDP00365
    ProteinModelPortaliP53041
    SMRiP53041
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53041

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Repeati28 – 61TPR 1Add BLAST34
    Repeati62 – 95TPR 2Add BLAST34
    Repeati96 – 129TPR 3Add BLAST34

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni184 – 499CatalyticAdd BLAST316
    Regioni303 – 304Substrate binding1 Publication2
    Regioni495 – 499Required for autoinhibitionBy similarity5

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiKOG0376 Eukaryota
    COG0639 LUCA
    GeneTreeiENSGT00530000063173
    HOGENOMiHOG000172698
    HOVERGENiHBG000216
    InParanoidiP53041
    KOiK04460
    OMAiLYPNHFF
    OrthoDBiEOG091G0589
    PhylomeDBiP53041
    TreeFamiTF105562

    Family and domain databases

    Gene3Di1.25.40.10, 1 hit
    3.60.21.10, 1 hit
    InterProiView protein in InterPro
    IPR004843 Calcineurin-like_PHP_ApaH
    IPR029052 Metallo-depent_PP-like
    IPR013235 PPP_dom
    IPR006186 Ser/Thr-sp_prot-phosphatase
    IPR011236 Ser/Thr_PPase_5
    IPR013026 TPR-contain_dom
    IPR011990 TPR-like_helical_dom_sf
    IPR001440 TPR_1
    IPR019734 TPR_repeat
    PANTHERiPTHR11668:SF391 PTHR11668:SF391, 1 hit
    PfamiView protein in Pfam
    PF00149 Metallophos, 1 hit
    PF08321 PPP5, 1 hit
    PF00515 TPR_1, 1 hit
    PRINTSiPR00114 STPHPHTASE
    SMARTiView protein in SMART
    SM00156 PP2Ac, 1 hit
    SM00028 TPR, 3 hits
    SUPFAMiSSF48452 SSF48452, 1 hit
    PROSITEiView protein in PROSITE
    PS00125 SER_THR_PHOSPHATASE, 1 hit
    PS50005 TPR, 3 hits
    PS50293 TPR_REGION, 1 hit

    Sequence (1+)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

    P53041-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAMAEGERTE CAEPPRDEPP ADGALKRAEE LKTQANDYFK AKDYENAIKF
    60 70 80 90 100
    YSQAIELNPS NAIYYGNRSL AYLRTECYGY ALGDATRAIE LDKKYIKGYY
    110 120 130 140 150
    RRAASNMALG KFRAALRDYE TVVKVKPHDK DAKMKYQECN KIVKQKAFER
    160 170 180 190 200
    AIAGDEHKRS VVDSLDIESM TIEDEYSGPK LEDGKVTISF MKELMQWYKD
    210 220 230 240 250
    QKKLHRKCAY QILVQVKEVL SKLSTLVETT LKETEKITVC GDTHGQFYDL
    260 270 280 290 300
    LNIFELNGLP SETNPYIFNG DFVDRGSFSV EVILTLFGFK LLYPDHFHLL
    310 320 330 340 350
    RGNHETDNMN QIYGFEGEVK AKYTAQMYEL FSEVFEWLPL AQCINGKVLI
    360 370 380 390 400
    MHGGLFSEDG VTLDDIRKIE RNRQPPDSGP MCDLLWSDPQ PQNGRSISKR
    410 420 430 440 450
    GVSCQFGPDV TKAFLEENNL DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN
    460 470 480 490
    YCDQMGNKAS YIHLQGSDLR PQFHQFTAVP HPNVKPMAYA NTLLQLGMM
    Length:499
    Mass (Da):56,879
    Last modified:October 1, 1996 - v1
    Checksum:iDB3B2090D8658BB3
    GO

    Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    H0YDU8H0YDU8_HUMAN
    Serine/threonine-protein phosphatas...
    PPP5C
    485Annotation score:
    A8MU39A8MU39_HUMAN
    Serine/threonine-protein phosphatas...
    PPP5C
    371Annotation score:

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti403S → T in AAB60384 (PubMed:8666404).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BT007275 mRNA Translation: AAP35939.1
    X89416 mRNA Translation: CAA61595.1
    U25174 mRNA Translation: AAB60384.1
    AC007193 Genomic DNA Translation: AAD22669.1
    CH471126 Genomic DNA Translation: EAW57416.1
    BC001970 mRNA Translation: AAH01970.1
    X92121 mRNA Translation: CAA63089.1
    CCDSiCCDS12684.1
    PIRiS52570
    RefSeqiNP_006238.1, NM_006247.3
    UniGeneiHs.654604

    Genome annotation databases

    EnsembliENST00000012443; ENSP00000012443; ENSG00000011485
    GeneIDi5536
    KEGGihsa:5536
    UCSCiuc002pem.4 human

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BT007275 mRNA Translation: AAP35939.1
    X89416 mRNA Translation: CAA61595.1
    U25174 mRNA Translation: AAB60384.1
    AC007193 Genomic DNA Translation: AAD22669.1
    CH471126 Genomic DNA Translation: EAW57416.1
    BC001970 mRNA Translation: AAH01970.1
    X92121 mRNA Translation: CAA63089.1
    CCDSiCCDS12684.1
    PIRiS52570
    RefSeqiNP_006238.1, NM_006247.3
    UniGeneiHs.654604

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1A17X-ray2.45A16-181[»]
    1S95X-ray1.60A/B169-499[»]
    1WAOX-ray2.901/2/3/423-499[»]
    2BUGNMR-A19-147[»]
    3H60X-ray2.00A/B176-490[»]
    3H61X-ray1.45A/D176-490[»]
    3H62X-ray1.40B/C176-490[»]
    3H63X-ray1.30A/C176-490[»]
    3H64X-ray1.90A/D176-490[»]
    3H66X-ray2.59A/B176-490[»]
    3H67X-ray1.65A/D176-490[»]
    3H68X-ray1.50A/D176-490[»]
    3H69X-ray2.10A/D176-490[»]
    4ZVZX-ray2.00A/B/C/D169-499[»]
    4ZX2X-ray1.23A169-499[»]
    5HPEX-ray2.27A175-499[»]
    5UI1X-ray1.96A/B/C/D169-499[»]
    5WG8X-ray1.65A169-499[»]
    DisProtiDP00365
    ProteinModelPortaliP53041
    SMRiP53041
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111528, 87 interactors
    DIPiDIP-29043N
    IntActiP53041, 64 interactors
    MINTiP53041
    STRINGi9606.ENSP00000012443

    Chemistry databases

    BindingDBiP53041
    ChEMBLiCHEMBL3425389

    PTM databases

    DEPODiP53041
    iPTMnetiP53041
    PhosphoSitePlusiP53041

    Polymorphism and mutation databases

    BioMutaiPPP5C
    DMDMi1709744

    Proteomic databases

    EPDiP53041
    MaxQBiP53041
    PaxDbiP53041
    PeptideAtlasiP53041
    PRIDEiP53041
    ProteomicsDBi56568

    Protocols and materials databases

    DNASUi5536
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000012443; ENSP00000012443; ENSG00000011485
    GeneIDi5536
    KEGGihsa:5536
    UCSCiuc002pem.4 human

    Organism-specific databases

    CTDi5536
    DisGeNETi5536
    EuPathDBiHostDB:ENSG00000011485.14
    GeneCardsiPPP5C
    HGNCiHGNC:9322 PPP5C
    HPAiCAB022641
    HPA029065
    HPA056933
    MIMi600658 gene
    neXtProtiNX_P53041
    OpenTargetsiENSG00000011485
    PharmGKBiPA33686
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0376 Eukaryota
    COG0639 LUCA
    GeneTreeiENSGT00530000063173
    HOGENOMiHOG000172698
    HOVERGENiHBG000216
    InParanoidiP53041
    KOiK04460
    OMAiLYPNHFF
    OrthoDBiEOG091G0589
    PhylomeDBiP53041
    TreeFamiTF105562

    Enzyme and pathway databases

    BRENDAi3.1.3.16 2681
    ReactomeiR-HSA-5675221 Negative regulation of MAPK pathway
    R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
    R-HSA-8939211 ESR-mediated signaling
    SABIO-RKiP53041
    SignaLinkiP53041
    SIGNORiP53041

    Miscellaneous databases

    ChiTaRSiPPP5C human
    EvolutionaryTraceiP53041
    GeneWikiiPPP5C
    GenomeRNAii5536
    PROiPR:P53041
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000011485 Expressed in 160 organ(s), highest expression level in frontal cortex
    CleanExiHS_PPP5C
    ExpressionAtlasiP53041 baseline and differential
    GenevisibleiP53041 HS

    Family and domain databases

    Gene3Di1.25.40.10, 1 hit
    3.60.21.10, 1 hit
    InterProiView protein in InterPro
    IPR004843 Calcineurin-like_PHP_ApaH
    IPR029052 Metallo-depent_PP-like
    IPR013235 PPP_dom
    IPR006186 Ser/Thr-sp_prot-phosphatase
    IPR011236 Ser/Thr_PPase_5
    IPR013026 TPR-contain_dom
    IPR011990 TPR-like_helical_dom_sf
    IPR001440 TPR_1
    IPR019734 TPR_repeat
    PANTHERiPTHR11668:SF391 PTHR11668:SF391, 1 hit
    PfamiView protein in Pfam
    PF00149 Metallophos, 1 hit
    PF08321 PPP5, 1 hit
    PF00515 TPR_1, 1 hit
    PRINTSiPR00114 STPHPHTASE
    SMARTiView protein in SMART
    SM00156 PP2Ac, 1 hit
    SM00028 TPR, 3 hits
    SUPFAMiSSF48452 SSF48452, 1 hit
    PROSITEiView protein in PROSITE
    PS00125 SER_THR_PHOSPHATASE, 1 hit
    PS50005 TPR, 3 hits
    PS50293 TPR_REGION, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPPP5_HUMAN
    AccessioniPrimary (citable) accession number: P53041
    Secondary accession number(s): Q16722, Q53XV2
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: November 7, 2018
    This is version 208 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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