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Protein

Serine/threonine-protein phosphatase 5

Gene

PPP5C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi242 – 2421Magnesium or manganese 1
    Metal bindingi244 – 2441Magnesium or manganese 1
    Binding sitei244 – 2441Substrate1 Publication
    Metal bindingi271 – 2711Magnesium or manganese 1
    Metal bindingi271 – 2711Magnesium or manganese 2
    Binding sitei275 – 2751Substrate1 Publication
    Metal bindingi303 – 3031Magnesium or manganese 2
    Active sitei304 – 3041Proton donor/acceptor1 Publication
    Metal bindingi352 – 3521Magnesium or manganese 2
    Binding sitei400 – 4001Substrate1 Publication
    Metal bindingi427 – 4271Magnesium or manganese 2
    Binding sitei427 – 4271Substrate1 Publication

    GO - Molecular functioni

    • ADP binding Source: MGI
    • ATP binding Source: MGI
    • identical protein binding Source: IntAct
    • lipid binding Source: UniProtKB-KW
    • metal ion binding Source: UniProtKB-KW
    • phosphoprotein phosphatase activity Source: UniProtKB
    • protein serine/threonine phosphatase activity Source: Reactome
    • RNA binding Source: Ensembl
    • signal transducer activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    Lipid-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.
    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

    HGNCiHGNC:9322. PPP5C.

    Subcellular locationi

    • Nucleus 1 Publication
    • Cytoplasm 2 Publications
    • Cell membrane 1 Publication

    • Note: Predominantly nuclear (PubMed:15383005). But also present in the cytoplasm (PubMed:15383005). Translocates from the cytoplasm to the plasma membrane in a RAC1-dependent manner (PubMed:19948726).2 Publications

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: Reactome
    • intracellular membrane-bounded organelle Source: HPA
    • nucleoplasm Source: HPA
    • nucleus Source: ProtInc
    • perikaryon Source: Ensembl
    • plasma membrane Source: UniProtKB-SubCell
    • protein complex Source: MGI
    • proximal dendrite Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Amyloid, Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 321K → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. 1 Publication
    Mutagenesisi74 – 741R → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. 1 Publication
    Mutagenesisi83 – 831G → N: No effect on interaction with HSP90AA1. 1 Publication
    Mutagenesisi93 – 931K → E: Decreases interaction with RAC1 and translocation to the membrane in presence of active RAC1. 1 Publication
    Mutagenesisi97 – 971K → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. Loss of interaction with RAF1. 2 Publications
    Mutagenesisi101 – 1011R → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. 1 Publication
    Mutagenesisi304 – 3041H → Q: Catalytically inactive; no effect on interaction with CRY2 but increases the stability of the interaction with CSNK1E. No effect on RAF1 phosphorylation. 3 Publications

    Keywords - Diseasei

    Alzheimer disease, Amyloidosis, Neurodegeneration

    Organism-specific databases

    PharmGKBiPA33686.

    Chemistry

    ChEMBLiCHEMBL3425389.

    Polymorphism and mutation databases

    BioMutaiPPP5C.
    DMDMi1709744.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedCombined sources
    Chaini2 – 499498Serine/threonine-protein phosphatase 5PRO_0000058894Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineCombined sources

    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.

    PTM databases

    DEPODiP53041.
    iPTMnetiP53041.
    PhosphoSiteiP53041.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    BgeeiENSG00000011485.
    CleanExiHS_PPP5C.
    ExpressionAtlasiP53041. baseline and differential.
    GenevisibleiP53041. HS.

    Organism-specific databases

    HPAiCAB022641.
    HPA029065.
    HPA056933.

    Interactioni

    Subunit structurei

    Interacts with CPNE1 (via VWFA domain) (By similarity). Part of a complex with HSP90/HSP90AA1 and steroid receptors. Interacts with CDC16, CDC27. Interacts with KLHDC10 (via the 6 Kelch repeats); inhibits the phosphatase activity on MAP3K5. Interacts (via TPR repeats) with HSP90AA1 (via TPR repeat-binding motif) or HSPA1A/HSPA1B; the interaction is direct and activates the phosphatase activity. Dissociates from HSPA1A/HSPA1B and HSP90AA1 in response to arachidonic acid. Interacts with ATM and ATR; both interactions are induced by DNA damage and enhance ATM and ATR kinase activity. Interacts with RAD17; reduced by DNA damage. Interacts with nuclear receptors such as NR3C1/GCR and PPARG (activated by agonist); regulates their transactivation activities. 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. Interacts with SMAD2 and SMAD3 but not with SMAD1; decreases SMAD3 phosphorylation and protein levels. Interacts (via TPR repeats) with CRY1 and CRY2; the interaction with CRY2 downregulates the phosphatase activity on CSNK1E. 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.By similarity12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-716663,EBI-716663
    CDC37Q165434EBI-716663,EBI-295634
    ESR1P033724EBI-716663,EBI-78473
    ESR2Q927314EBI-716663,EBI-78505
    HSP90AA1P079009EBI-716663,EBI-296047
    PPP2R1AP301533EBI-716663,EBI-302388

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi111528. 79 interactions.
    DIPiDIP-29043N.
    IntActiP53041. 34 interactions.
    MINTiMINT-1411788.
    STRINGi9606.ENSP00000012443.

    Structurei

    Secondary structure

    1
    499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 4019Combined sources
    Helixi44 – 5714Combined sources
    Helixi62 – 7413Combined sources
    Helixi78 – 9114Combined sources
    Beta strandi92 – 943Combined sources
    Helixi96 – 10813Combined sources
    Helixi112 – 12514Combined sources
    Helixi130 – 16435Combined sources
    Helixi182 – 1843Combined sources
    Helixi188 – 19912Combined sources
    Helixi206 – 22116Combined sources
    Beta strandi225 – 2295Combined sources
    Beta strandi236 – 2405Combined sources
    Helixi247 – 25711Combined sources
    Beta strandi262 – 2643Combined sources
    Beta strandi266 – 2705Combined sources
    Beta strandi273 – 2764Combined sources
    Helixi279 – 29214Combined sources
    Turni294 – 2963Combined sources
    Beta strandi297 – 3004Combined sources
    Beta strandi303 – 3064Combined sources
    Helixi307 – 3137Combined sources
    Helixi315 – 3228Combined sources
    Helixi325 – 33511Combined sources
    Beta strandi340 – 3445Combined sources
    Turni345 – 3473Combined sources
    Beta strandi348 – 3503Combined sources
    Beta strandi357 – 3593Combined sources
    Helixi363 – 3675Combined sources
    Beta strandi372 – 3743Combined sources
    Beta strandi377 – 3793Combined sources
    Helixi380 – 3867Combined sources
    Beta strandi391 – 3977Combined sources
    Beta strandi401 – 4066Combined sources
    Helixi408 – 41710Combined sources
    Beta strandi422 – 4254Combined sources
    Beta strandi433 – 4375Combined sources
    Helixi438 – 4403Combined sources
    Beta strandi442 – 4465Combined sources
    Helixi451 – 4533Combined sources
    Beta strandi459 – 4657Combined sources
    Beta strandi468 – 4769Combined sources
    Turni486 – 4894Combined sources
    Helixi492 – 4954Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    DisProtiDP00365.
    ProteinModelPortaliP53041.
    SMRiP53041. Positions 19-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53041.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati28 – 6134TPR 1Add
    BLAST
    Repeati62 – 9534TPR 2Add
    BLAST
    Repeati96 – 12934TPR 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni184 – 499316CatalyticAdd
    BLAST
    Regioni303 – 3042Substrate binding
    Regioni495 – 4995Required for autoinhibitionBy similarity

    Sequence similaritiesi

    Contains 3 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

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

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    3.60.21.10. 1 hit.
    InterProiIPR004843. 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.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR11668:SF21. PTHR11668:SF21. 2 hits.
    PfamiPF00149. Metallophos. 1 hit.
    PF08321. PPP5. 1 hit.
    PF00515. TPR_1. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    SM00028. TPR. 3 hits.
    [Graphical view]
    SUPFAMiSSF48452. SSF48452. 1 hit.
    SSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti403 – 4031S → T in AAB60384 (PubMed:8666404).Curated

    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.

    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
    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[»]
    DisProtiDP00365.
    ProteinModelPortaliP53041.
    SMRiP53041. Positions 19-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111528. 79 interactions.
    DIPiDIP-29043N.
    IntActiP53041. 34 interactions.
    MINTiMINT-1411788.
    STRINGi9606.ENSP00000012443.

    Chemistry

    ChEMBLiCHEMBL3425389.

    PTM databases

    DEPODiP53041.
    iPTMnetiP53041.
    PhosphoSiteiP53041.

    Polymorphism and mutation databases

    BioMutaiPPP5C.
    DMDMi1709744.

    Proteomic databases

    EPDiP53041.
    MaxQBiP53041.
    PaxDbiP53041.
    PeptideAtlasiP53041.
    PRIDEiP53041.

    Protocols and materials databases

    DNASUi5536.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi5536.
    GeneCardsiPPP5C.
    HGNCiHGNC:9322. PPP5C.
    HPAiCAB022641.
    HPA029065.
    HPA056933.
    MIMi600658. gene.
    neXtProtiNX_P53041.
    PharmGKBiPA33686.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0376. Eukaryota.
    COG0639. LUCA.
    GeneTreeiENSGT00530000063173.
    HOGENOMiHOG000172698.
    HOVERGENiHBG000216.
    InParanoidiP53041.
    KOiK04460.
    OMAiWMGRGPS.
    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.
    SignaLinkiP53041.
    SIGNORiP53041.

    Miscellaneous databases

    ChiTaRSiPPP5C. human.
    EvolutionaryTraceiP53041.
    GeneWikiiPPP5C.
    GenomeRNAii5536.
    PROiP53041.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000011485.
    CleanExiHS_PPP5C.
    ExpressionAtlasiP53041. baseline and differential.
    GenevisibleiP53041. HS.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    3.60.21.10. 1 hit.
    InterProiIPR004843. 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.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR11668:SF21. PTHR11668:SF21. 2 hits.
    PfamiPF00149. Metallophos. 1 hit.
    PF08321. PPP5. 1 hit.
    PF00515. TPR_1. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    SM00028. TPR. 3 hits.
    [Graphical view]
    SUPFAMiSSF48452. SSF48452. 1 hit.
    SSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPPP5_HUMAN
    AccessioniPrimary (citable) accession number: P53041
    Secondary accession number(s): Q16722, Q53XV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: September 7, 2016
    This is version 187 of the entry and version 1 of the sequence. [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. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.