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P53041

- PPP5_HUMAN

UniProt

P53041 - PPP5_HUMAN

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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

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 Mg(2+) or Mn(2+) 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

  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 serine/threonine phosphatase activity Source: ProtInc
  6. RNA binding Source: Ensembl
  7. 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
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

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-KW
  5. neuronal cell body Source: Ensembl
  6. neuron projection Source: Ensembl
  7. nucleus Source: HPA
Complete GO annotation...

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

BgeeiP53041.
CleanExiHS_PPP5C.
ExpressionAtlasiP53041. baseline and differential.
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. 67 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 – 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 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 – 3686Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi377 – 3793Combined sources
Helixi380 – 3867Combined sources
Beta strandi391 – 3977Combined sources
Beta strandi401 – 4066Combined sources
Helixi408 – 41811Combined sources
Beta strandi421 – 4255Combined 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[»]
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.
GeneTreeiENSGT00530000063173.
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_dom.
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

        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.3. human.

Polymorphism databases

DMDMi1709744.

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 .
CCDSi CCDS12684.1.
PIRi S52570.
RefSeqi NP_006238.1. NM_006247.3.
UniGenei Hs.654604.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 67 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.
GeneTreei ENSGT00530000063173.
HOGENOMi HOG000172698.
HOVERGENi HBG000216.
InParanoidi P53041.
KOi K04460.
OMAi FKLLYPN.
OrthoDBi EOG7V49Z3.
PhylomeDBi P53041.
TreeFami TF105562.

Enzyme and pathway databases

SignaLinki P53041.

Miscellaneous databases

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

Gene expression databases

Bgeei P53041.
CleanExi HS_PPP5C.
ExpressionAtlasi P53041. baseline and differential.
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_dom.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 169 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