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P53041

- PPP5_HUMAN

UniProt

P53041 - PPP5_HUMAN

Protein

Serine/threonine-protein phosphatase 5

Gene

PPP5C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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

    Binds 2 magnesium or manganese 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

    1. identical protein binding Source: IntAct
    2. lipid binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. phosphoprotein phosphatase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein serine/threonine phosphatase activity Source: ProtInc
    7. RNA binding Source: Ensembl
    8. signal transducer activity Source: UniProtKB

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. DNA repair Source: UniProtKB-KW
    3. mitotic nuclear division Source: ProtInc
    4. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    5. protein dephosphorylation Source: ProtInc
    6. protein heterooligomerization Source: Ensembl
    7. response to morphine Source: Ensembl
    8. signal transduction Source: GOC
    9. transcription, DNA-templated Source: ProtInc

    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

    SignaLinkiP53041.

    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
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9322. PPP5C.

    Subcellular locationi

    Nucleus. Cytoplasm. Membrane
    Note: Predominantly nuclear. But also present in the cytoplasm.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Ensembl
    3. intracellular membrane-bounded organelle Source: HPA
    4. membrane Source: UniProtKB-SubCell
    5. neuronal cell body Source: Ensembl
    6. neuron projection Source: Ensembl
    7. nucleus Source: HPA

    Keywords - Cellular componenti

    Amyloid, 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.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 499498Serine/threonine-protein phosphatase 5PRO_0000058894Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    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

    MaxQBiP53041.
    PaxDbiP53041.
    PRIDEiP53041.

    PTM databases

    PhosphoSiteiP53041.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiP53041.
    BgeeiP53041.
    CleanExiHS_PPP5C.
    GenevestigatoriP53041.

    Organism-specific databases

    HPAiCAB022641.
    HPA029065.
    HPA056933.

    Interactioni

    Subunit structurei

    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.12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-716663,EBI-716663
    CDC37Q165434EBI-716663,EBI-295634
    ESR1P033724EBI-716663,EBI-78473
    ESR2Q927314EBI-716663,EBI-78505
    HSP90AA1P079008EBI-716663,EBI-296047
    PPP2R1AP301533EBI-716663,EBI-302388

    Protein-protein interaction databases

    BioGridi111528. 62 interactions.
    DIPiDIP-29043N.
    IntActiP53041. 29 interactions.
    MINTiMINT-1411788.
    STRINGi9606.ENSP00000012443.

    Structurei

    Secondary structure

    1
    499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 4019
    Helixi44 – 5714
    Helixi62 – 7413
    Helixi78 – 9114
    Beta strandi92 – 943
    Helixi96 – 10813
    Helixi112 – 12514
    Helixi130 – 16435
    Helixi182 – 1843
    Helixi188 – 19912
    Helixi206 – 22116
    Beta strandi225 – 2295
    Beta strandi236 – 2405
    Helixi247 – 25711
    Beta strandi266 – 2705
    Beta strandi273 – 2764
    Helixi279 – 29214
    Turni294 – 2963
    Beta strandi297 – 3004
    Beta strandi303 – 3064
    Helixi307 – 3137
    Helixi315 – 3228
    Helixi325 – 33511
    Beta strandi340 – 3445
    Turni345 – 3473
    Beta strandi348 – 3503
    Beta strandi357 – 3593
    Helixi363 – 3686
    Beta strandi372 – 3743
    Beta strandi377 – 3793
    Helixi380 – 3867
    Beta strandi391 – 3977
    Beta strandi401 – 4066
    Helixi408 – 41811
    Beta strandi421 – 4255
    Beta strandi433 – 4375
    Helixi438 – 4403
    Beta strandi442 – 4465
    Helixi451 – 4533
    Beta strandi459 – 4657
    Beta strandi468 – 4769
    Turni486 – 4894
    Helixi492 – 4954

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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

    eggNOGiCOG0639.
    HOGENOMiHOG000172698.
    HOVERGENiHBG000216.
    InParanoidiP53041.
    KOiK04460.
    OMAiFKLLYPN.
    OrthoDBiEOG7V49Z3.
    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.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR11668:SF12. PTHR11668:SF12. 1 hit.
    PfamiPF00149. Metallophos. 1 hit.
    PF08321. PPP5. 1 hit.
    PF00515. TPR_1. 2 hits.
    [Graphical view]
    PIRSFiPIRSF033096. PPPtase_5. 1 hit.
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    SM00028. TPR. 3 hits.
    [Graphical view]
    SUPFAMiSSF56300. 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

    MAMAEGERTE CAEPPRDEPP ADGALKRAEE LKTQANDYFK AKDYENAIKF    50
    YSQAIELNPS NAIYYGNRSL AYLRTECYGY ALGDATRAIE LDKKYIKGYY 100
    RRAASNMALG KFRAALRDYE TVVKVKPHDK DAKMKYQECN KIVKQKAFER 150
    AIAGDEHKRS VVDSLDIESM TIEDEYSGPK LEDGKVTISF MKELMQWYKD 200
    QKKLHRKCAY QILVQVKEVL SKLSTLVETT LKETEKITVC GDTHGQFYDL 250
    LNIFELNGLP SETNPYIFNG DFVDRGSFSV EVILTLFGFK LLYPDHFHLL 300
    RGNHETDNMN QIYGFEGEVK AKYTAQMYEL FSEVFEWLPL AQCINGKVLI 350
    MHGGLFSEDG VTLDDIRKIE RNRQPPDSGP MCDLLWSDPQ PQNGRSISKR 400
    GVSCQFGPDV TKAFLEENNL DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN 450
    YCDQMGNKAS YIHLQGSDLR PQFHQFTAVP HPNVKPMAYA NTLLQLGMM 499
    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:
    EMBL
    GenBank
    DDBJ
    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.3. human.

    Polymorphism databases

    DMDMi1709744.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS12684.1.
    PIRi S52570.
    RefSeqi NP_006238.1. NM_006247.3.
    UniGenei Hs.654604.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A17 X-ray 2.45 A 16-181 [» ]
    1S95 X-ray 1.60 A/B 169-499 [» ]
    1WAO X-ray 2.90 1/2/3/4 23-499 [» ]
    2BUG NMR - A 19-147 [» ]
    3H60 X-ray 2.00 A/B 176-490 [» ]
    3H61 X-ray 1.45 A/D 176-490 [» ]
    3H62 X-ray 1.40 B/C 176-490 [» ]
    3H63 X-ray 1.30 A/C 176-490 [» ]
    3H64 X-ray 1.90 A/D 176-490 [» ]
    3H66 X-ray 2.59 A/B 176-490 [» ]
    3H67 X-ray 1.65 A/D 176-490 [» ]
    3H68 X-ray 1.50 A/D 176-490 [» ]
    3H69 X-ray 2.10 A/D 176-490 [» ]
    DisProti DP00365.
    ProteinModelPortali P53041.
    SMRi P53041. Positions 19-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111528. 62 interactions.
    DIPi DIP-29043N.
    IntActi P53041. 29 interactions.
    MINTi MINT-1411788.
    STRINGi 9606.ENSP00000012443.

    PTM databases

    PhosphoSitei P53041.

    Polymorphism databases

    DMDMi 1709744.

    Proteomic databases

    MaxQBi P53041.
    PaxDbi P53041.
    PRIDEi P53041.

    Protocols and materials databases

    DNASUi 5536.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000012443 ; ENSP00000012443 ; ENSG00000011485 .
    GeneIDi 5536.
    KEGGi hsa:5536.
    UCSCi uc002pem.3. human.

    Organism-specific databases

    CTDi 5536.
    GeneCardsi GC19P046850.
    HGNCi HGNC:9322. PPP5C.
    HPAi CAB022641.
    HPA029065.
    HPA056933.
    MIMi 600658. gene.
    neXtProti NX_P53041.
    PharmGKBi PA33686.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172698.
    HOVERGENi HBG000216.
    InParanoidi P53041.
    KOi K04460.
    OMAi FKLLYPN.
    OrthoDBi EOG7V49Z3.
    PhylomeDBi P53041.
    TreeFami TF105562.

    Enzyme and pathway databases

    SignaLinki P53041.

    Miscellaneous databases

    EvolutionaryTracei P53041.
    GeneWikii PPP5C.
    GenomeRNAii 5536.
    NextBioi 21446.
    PROi P53041.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53041.
    Bgeei P53041.
    CleanExi HS_PPP5C.
    Genevestigatori P53041.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    3.60.21.10. 1 hit.
    InterProi 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.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    PANTHERi PTHR11668:SF12. PTHR11668:SF12. 1 hit.
    Pfami PF00149. Metallophos. 1 hit.
    PF08321. PPP5. 1 hit.
    PF00515. TPR_1. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF033096. PPPtase_5. 1 hit.
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    SM00028. TPR. 3 hits.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus."
      Chen M.X., McPartlin A.E., Brown L., Chen Y.H., Barker H.M., Cohen P.T.W.
      EMBO J. 13:4278-4290(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-499.
    4. "Cloning of a highly conserved human protein serine-threonine phosphatase gene from the glioma candidate region on chromosome 19q13.3."
      Yong W.H., Ueki K., Chou D., Reeves S.A., von Deimling A., Gusella J.F., Mohrenweiser H.W., Buckler A.J., Louis D.N.
      Genomics 29:533-536(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-499.
      Tissue: Fetal brain.
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cervix.
    7. "Chromosomal localization and 5' sequence of the human protein serine/threonine phosphatase 5' gene."
      Xu X., Lagercrantz J., Zickert P., Bajalica-Lagercrantz S., Zetterberg A.
      Biochem. Biophys. Res. Commun. 218:514-517(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-37.
      Tissue: Fetal brain.
    8. "Activation of protein phosphatase 5 by limited proteolysis or the binding of polyunsaturated fatty acids to the TPR domain."
      Chen M.X., Cohen P.T.
      FEBS Lett. 400:136-140(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, LIPID-BINDING.
    9. "The serine/threonine phosphatase PP5 interacts with CDC16 and CDC27, two tetratricopeptide repeat-containing subunits of the anaphase-promoting complex."
      Ollendorff V., Donoghue D.J.
      J. Biol. Chem. 272:32011-32018(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC16 AND CDC27.
    10. "Requirement of protein phosphatase 5 in DNA-damage-induced ATM activation."
      Ali A., Zhang J., Bao S., Liu I., Otterness D., Dean N.M., Abraham R.T., Wang X.F.
      Genes Dev. 18:249-254(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA DAMAGE RESPONSE, INTERACTION WITH ATM AND RAD17.
    11. "Protein phosphatase 5 is a negative regulator of estrogen receptor-mediated transcription."
      Ikeda K., Ogawa S., Tsukui T., Horie-Inoue K., Ouchi Y., Kato S., Muramatsu M., Inoue S.
      Mol. Endocrinol. 18:1131-1143(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF ESR1 AND ESR2.
    12. Cited for: FUNCTION IN DEPHOSPHORYLATION OF PRKDC.
    13. "Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole."
      Zeke T., Morrice N., Vazquez-Martin C., Cohen P.T.
      Biochem. J. 385:45-56(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSP90AA1 AND HSPA1A, LIPID-BINDING, ENZYME REGULATION, SUBCELLULAR LOCATION, CLEAVAGE, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Dephosphorylation of tau by protein phosphatase 5: impairment in Alzheimer's disease."
      Liu F., Iqbal K., Grundke-Iqbal I., Rossie S., Gong C.X.
      J. Biol. Chem. 280:1790-1796(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF MAPT, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    15. "Protein phosphatase 5 is required for ATR-mediated checkpoint activation."
      Zhang J., Bao S., Furumai R., Kucera K.S., Ali A., Dean N.M., Wang X.F.
      Mol. Cell. Biol. 25:9910-9919(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA DAMAGE RESPONSE.
    16. "Regulation of the Raf-MEK-ERK pathway by protein phosphatase 5."
      von Kriegsheim A., Pitt A., Grindlay G.J., Kolch W., Dhillon A.S.
      Nat. Cell Biol. 8:1011-1016(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MAPK SIGNALING, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-97 AND HIS-304.
    17. "Posttranslational regulation of the mammalian circadian clock by cryptochrome and protein phosphatase 5."
      Partch C.L., Shields K.F., Thompson C.L., Selby C.P., Sancar A.
      Proc. Natl. Acad. Sci. U.S.A. 103:10467-10472(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF CSNK1E, INTERACTION WITH CRY1 AND CRY2, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-304.
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    19. "Protein phosphatase 5 regulates the function of 53BP1 after neocarzinostatin-induced DNA damage."
      Kang Y., Lee J.H., Hoan N.N., Sohn H.M., Chang I.Y., You H.J.
      J. Biol. Chem. 284:9845-9853(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF TP53BP1.
    20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Activated Rac1 GTPase translocates protein phosphatase 5 to the cell membrane and stimulates phosphatase activity in vitro."
      Chatterjee A., Wang L., Armstrong D.L., Rossie S.
      J. Biol. Chem. 285:3872-3882(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PHOSPHATASE, INTERACTION WITH RAC1, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-93 AND HIS-304.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: FUNCTION IN DNA DAMAGE RESPONSE.
    24. "Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway."
      Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.
      Cell. Signal. 24:1999-2006(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TGF-BETA SIGNALING, INTERACTION WITH SMAD2 AND SMAD3, SUBCELLULAR LOCATION.
    25. "S100 proteins modulate protein phosphatase 5 function: a link between CA2+ signal transduction and protein dephosphorylation."
      Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H., Tokuda M., Kobayashi R.
      J. Biol. Chem. 287:13787-13798(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PHOSPHATASE, INTERACTION WITH S100A1; S100A2; S100A6 AND S100B, ENZYME REGULATION, MUTAGENESIS OF LYS-32; ARG-74; LYS-97 AND ARG-101.
    26. "The Kelch repeat protein KLHDC10 regulates oxidative stress-induced ASK1 activation by suppressing PP5."
      Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T., Kuranaga E., Miura M., Takeda K., Ichijo H.
      Mol. Cell 48:692-704(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF MAP3K5, INTERACTION WITH KLHDC10, CLEAVAGE.
    27. "The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions."
      Das A.K., Cohen P.T.W., Barford D.
      EMBO J. 17:1192-1199(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 19-177.
    28. "Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5."
      Swingle M.R., Honkanen R.E., Ciszak E.M.
      J. Biol. Chem. 279:33992-33999(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 169-499 IN COMPLEX WITH SUBSTRATE AND MAGNESIUM OR MANGANESES, ACTIVE SITE, MAGNESIUM OR MANGANESE-BINDING SITES.
    29. "Molecular basis for TPR domain-mediated regulation of protein phosphatase 5."
      Yang J., Roe S.M., Cliff M.J., Williams M.A., Ladbury J.E., Cohen P.T., Barford D.
      EMBO J. 24:1-10(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 23-499 IN COMPLEX WITH MANGANESE IONS, INTERACTION WITH HSP90AA1, LIPID-BINDING, MAGNESIUM OR MANGANESE-BINDING SITES, ENZYME REGULATION.
    30. "Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90."
      Cliff M.J., Harris R., Barford D., Ladbury J.E., Williams M.A.
      Structure 14:415-426(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 19-147 IN COMPLEX WITH HSP90AA1 PEPTIDE, INTERACTION WITH HSP90AA1, MUTAGENESIS OF GLY-83.
    31. "Structural basis of serine/threonine phosphatase inhibition by the archetypal small molecules cantharidin and norcantharidin."
      Bertini I., Calderone V., Fragai M., Luchinat C., Talluri E.
      J. Med. Chem. 52:4838-4843(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 176-490 IN COMPLEX WITH INHIBITORS AND MANGANESE, MANGANESE-BINDING SITES, ENZYME REGULATION.

    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: October 1, 2014
    This is version 167 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

    External Data

    Dasty 3