Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P53041 (PPP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 5

Short name=PP5
EC=3.1.3.16
Alternative name(s):
Protein phosphatase T
Short name=PP-T
Short name=PPT
Gene names
Name:PPP5C
Synonyms:PPP5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26

Catalytic activity

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

Cofactor

Binds 2 magnesium or manganese per subunit.

Enzyme regulation

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. Ref.8 Ref.13 Ref.21 Ref.25 Ref.29 Ref.31

Subunit structure

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. Ref.9 Ref.10 Ref.13 Ref.17 Ref.21 Ref.24 Ref.25 Ref.26 Ref.29 Ref.30

Subcellular location

Nucleus. Cytoplasm. Membrane. Note: Predominantly nuclear. But also present in the cytoplasm. Ref.13 Ref.21 Ref.24

Tissue specificity

Ubiquitous. Ref.14

Post-translational modification

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

Sequence similarities

Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily.

Contains 3 TPR repeats.

Biophysicochemical properties

Kinetic parameters:

KM=1.847 µM for CSNK1E (at 30 degrees Celsius) Ref.14 Ref.17

KM=13.2 µM for MAPT/TAU (at pH 7.4 and 30 degrees Celsius)

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentAmyloid
Cytoplasm
Membrane
Nucleus
   DiseaseAlzheimer disease
Amyloidosis
Neurodegeneration
   DomainRepeat
TPR repeat
   LigandLipid-binding
Magnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic nuclear division

Traceable author statement Ref.3. Source: ProtInc

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

protein dephosphorylation

Traceable author statement Ref.3. Source: ProtInc

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

response to morphine

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from mutant phenotype PubMed 12761501. Source: GOC

transcription, DNA-templated

Traceable author statement Ref.3. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from electronic annotation. Source: Ensembl

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: Ensembl

identical protein binding

Inferred from physical interaction PubMed 21360678. Source: IntAct

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from sequence or structural similarity PubMed 9383998. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 9383998. Source: UniProtKB

protein serine/threonine phosphatase activity

Traceable author statement Ref.3. Source: ProtInc

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.18
Chain2 – 499498Serine/threonine-protein phosphatase 5
PRO_0000058894

Regions

Repeat28 – 6134TPR 1
Repeat62 – 9534TPR 2
Repeat96 – 12934TPR 3
Region184 – 499316Catalytic
Region303 – 3042Substrate binding
Region495 – 4995Required for autoinhibition By similarity

Sites

Active site3041Proton donor/acceptor Ref.28
Metal binding2421Magnesium or manganese 1
Metal binding2441Magnesium or manganese 1
Metal binding2711Magnesium or manganese 1
Metal binding2711Magnesium or manganese 2
Metal binding3031Magnesium or manganese 2
Metal binding3521Magnesium or manganese 2
Metal binding4271Magnesium or manganese 2
Binding site2441Substrate
Binding site2751Substrate
Binding site4001Substrate
Binding site4271Substrate

Amino acid modifications

Modified residue21N-acetylalanine Ref.18

Experimental info

Mutagenesis321K → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. Ref.25
Mutagenesis741R → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. Ref.25
Mutagenesis831G → N: No effect on interaction with HSP90AA1. Ref.30
Mutagenesis931K → E: Decreases interaction with RAC1 and translocation to the membrane in presence of active RAC1. Ref.21
Mutagenesis971K → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. Loss of interaction with RAF1. Ref.16 Ref.25
Mutagenesis1011R → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. Ref.25
Mutagenesis3041H → Q: Catalytically inactive; no effect on interaction with CRY2 but increases the stability of the interaction with CSNK1E. No effect on RAF1 phosphorylation. Ref.16 Ref.17 Ref.21
Sequence conflict4031S → T in AAB60384. Ref.4

Secondary structure

................................................................................ 499
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53041 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: DB3B2090D8658BB3

FASTA49956,879
        10         20         30         40         50         60 
MAMAEGERTE CAEPPRDEPP ADGALKRAEE LKTQANDYFK AKDYENAIKF YSQAIELNPS 

        70         80         90        100        110        120 
NAIYYGNRSL AYLRTECYGY ALGDATRAIE LDKKYIKGYY RRAASNMALG KFRAALRDYE 

       130        140        150        160        170        180 
TVVKVKPHDK DAKMKYQECN KIVKQKAFER AIAGDEHKRS VVDSLDIESM TIEDEYSGPK 

       190        200        210        220        230        240 
LEDGKVTISF MKELMQWYKD QKKLHRKCAY QILVQVKEVL SKLSTLVETT LKETEKITVC 

       250        260        270        280        290        300 
GDTHGQFYDL LNIFELNGLP SETNPYIFNG DFVDRGSFSV EVILTLFGFK LLYPDHFHLL 

       310        320        330        340        350        360 
RGNHETDNMN QIYGFEGEVK AKYTAQMYEL FSEVFEWLPL AQCINGKVLI MHGGLFSEDG 

       370        380        390        400        410        420 
VTLDDIRKIE RNRQPPDSGP MCDLLWSDPQ PQNGRSISKR GVSCQFGPDV TKAFLEENNL 

       430        440        450        460        470        480 
DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN YCDQMGNKAS YIHLQGSDLR PQFHQFTAVP 

       490 
HPNVKPMAYA NTLLQLGMM 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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]"DNA-PKcs function regulated specifically by protein phosphatase 5."
Wechsler T., Chen B.P., Harper R., Morotomi-Yano K., Huang B.C., Meek K., Cleaver J.E., Chen D.J., Wabl M.
Proc. Natl. Acad. Sci. U.S.A. 101:1247-1252(2004) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Protein phosphatase 5 is necessary for ATR-mediated DNA repair."
Kang Y., Cheong H.M., Lee J.H., Song P.I., Lee K.H., Kim S.Y., Jun J.Y., You H.J.
Biochem. Biophys. Res. Commun. 404:476-481(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS12684.1.
PIRS52570.
RefSeqNP_006238.1. NM_006247.3.
UniGeneHs.654604.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00365.
ProteinModelPortalP53041.
SMRP53041. Positions 19-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111528. 60 interactions.
DIPDIP-29043N.
IntActP53041. 23 interactions.
MINTMINT-1411788.
STRING9606.ENSP00000012443.

PTM databases

PhosphoSiteP53041.

Polymorphism databases

DMDM1709744.

Proteomic databases

MaxQBP53041.
PaxDbP53041.
PRIDEP53041.

Protocols and materials databases

DNASU5536.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000012443; ENSP00000012443; ENSG00000011485.
GeneID5536.
KEGGhsa:5536.
UCSCuc002pem.3. human.

Organism-specific databases

CTD5536.
GeneCardsGC19P046850.
HGNCHGNC:9322. PPP5C.
HPACAB022641.
HPA029065.
HPA056933.
MIM600658. gene.
neXtProtNX_P53041.
PharmGKBPA33686.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172698.
HOVERGENHBG000216.
InParanoidP53041.
KOK04460.
OMAFKLLYPN.
OrthoDBEOG7V49Z3.
PhylomeDBP53041.
TreeFamTF105562.

Enzyme and pathway databases

SignaLinkP53041.

Gene expression databases

ArrayExpressP53041.
BgeeP53041.
CleanExHS_PPP5C.
GenevestigatorP53041.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
3.60.21.10. 1 hit.
InterProIPR004843. 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]
PANTHERPTHR11668:SF12. PTHR11668:SF12. 1 hit.
PfamPF00149. Metallophos. 1 hit.
PF08321. PPP5. 1 hit.
PF00515. TPR_1. 2 hits.
[Graphical view]
PIRSFPIRSF033096. PPPtase_5. 1 hit.
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP53041.
GeneWikiPPP5C.
GenomeRNAi5536.
NextBio21446.
PROP53041.
SOURCESearch...

Entry information

Entry namePPP5_HUMAN
AccessionPrimary (citable) accession number: P53041
Secondary accession number(s): Q16722, Q53XV2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 165 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM