ID PPP5_HUMAN Reviewed; 499 AA.
AC P53041; Q16722; Q53XV2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 01-MAY-2013, entry version 152.
DE RecName: Full=Serine/threonine-protein phosphatase 5;
DE Short=PP5;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase T;
DE Short=PP-T;
DE Short=PPT;
GN Name=PPP5C; Synonyms=PPP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-499.
RX PubMed=7925273;
RA Chen M.X., McPartlin A.E., Brown L., Chen Y.H., Barker H.M.,
RA Cohen P.T.W.;
RT "A novel human protein serine/threonine phosphatase, which possesses
RT four tetratricopeptide repeat motifs and localizes to the nucleus.";
RL EMBO J. 13:4278-4290(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-499.
RC TISSUE=Fetal brain;
RX PubMed=8666404; DOI=10.1006/geno.1995.9972;
RA Yong W.H., Ueki K., Chou D., Reeves S.A., von Deimling A.,
RA Gusella J.F., Mohrenweiser H.W., Buckler A.J., Louis D.N.;
RT "Cloning of a highly conserved human protein serine-threonine
RT phosphatase gene from the glioma candidate region on chromosome
RT 19q13.3.";
RL Genomics 29:533-536(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-37.
RC TISSUE=Fetal brain;
RX PubMed=8561788; DOI=10.1006/bbrc.1996.0092;
RA Xu X., Lagercrantz J., Zickert P., Bajalica-Lagercrantz S.,
RA Zetterberg A.;
RT "Chromosomal localization and 5' sequence of the human protein
RT serine/threonine phosphatase 5' gene.";
RL Biochem. Biophys. Res. Commun. 218:514-517(1996).
RN [8]
RP INTERACTION WITH CDC16 AND CDC27.
RX PubMed=9405394; DOI=10.1074/jbc.272.51.32011;
RA Ollendorff V., Donoghue D.J.;
RT "The serine/threonine phosphatase PP5 interacts with CDC16 and CDC27,
RT two tetratricopeptide repeat-containing subunits of the anaphase-
RT promoting complex.";
RL J. Biol. Chem. 272:32011-32018(1997).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 19-177.
RX PubMed=9482716; DOI=10.1093/emboj/17.5.1192;
RA Das A.K., Cohen P.T.W., Barford D.;
RT "The structure of the tetratricopeptide repeats of protein phosphatase
RT 5: implications for TPR-mediated protein-protein interactions.";
RL EMBO J. 17:1192-1199(1998).
CC -!- FUNCTION: May play a role in the regulation of RNA biogenesis
CC and/or mitosis. In vitro, dephosphorylates serine residues of
CC skeletal muscle phosphorylase and histone H1.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC -!- SUBUNIT: Interacts with CDC16 and CDC27.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-716663, EBI-716663;
CC Q16543:CDC37; NbExp=2; IntAct=EBI-716663, EBI-295634;
CC P03372:ESR1; NbExp=4; IntAct=EBI-716663, EBI-78473;
CC Q92731:ESR2; NbExp=4; IntAct=EBI-716663, EBI-78505;
CC P07900:HSP90AA1; NbExp=8; IntAct=EBI-716663, EBI-296047;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly
CC nuclear. But also present in the cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T)
CC subfamily.
CC -!- SIMILARITY: Contains 3 TPR repeats.
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DR EMBL; BT007275; AAP35939.1; -; mRNA.
DR EMBL; X89416; CAA61595.1; -; mRNA.
DR EMBL; U25174; AAB60384.1; -; mRNA.
DR EMBL; AC007193; AAD22669.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57416.1; -; Genomic_DNA.
DR EMBL; BC001970; AAH01970.1; -; mRNA.
DR EMBL; X92121; CAA63089.1; -; mRNA.
DR IPI; IPI00019812; -.
DR PIR; S52570; S52570.
DR RefSeq; NP_006238.1; NM_006247.3.
DR UniGene; Hs.654604; -.
DR PDB; 1A17; X-ray; 2.45 A; A=16-181.
DR PDB; 1S95; X-ray; 1.60 A; A/B=169-499.
DR PDB; 1WAO; X-ray; 2.90 A; 1/2/3/4=23-499.
DR PDB; 2BUG; NMR; -; A=19-147.
DR PDB; 3H60; X-ray; 2.00 A; A/B=176-490.
DR PDB; 3H61; X-ray; 1.45 A; A/D=176-490.
DR PDB; 3H62; X-ray; 1.40 A; B/C=176-490.
DR PDB; 3H63; X-ray; 1.30 A; A/C=176-490.
DR PDB; 3H64; X-ray; 1.90 A; A/D=176-490.
DR PDB; 3H66; X-ray; 2.59 A; A/B=176-490.
DR PDB; 3H67; X-ray; 1.65 A; A/D=176-490.
DR PDB; 3H68; X-ray; 1.50 A; A/D=176-490.
DR PDB; 3H69; X-ray; 2.10 A; A/D=176-490.
DR PDBsum; 1A17; -.
DR PDBsum; 1S95; -.
DR PDBsum; 1WAO; -.
DR PDBsum; 2BUG; -.
DR PDBsum; 3H60; -.
DR PDBsum; 3H61; -.
DR PDBsum; 3H62; -.
DR PDBsum; 3H63; -.
DR PDBsum; 3H64; -.
DR PDBsum; 3H66; -.
DR PDBsum; 3H67; -.
DR PDBsum; 3H68; -.
DR PDBsum; 3H69; -.
DR DisProt; DP00365; -.
DR ProteinModelPortal; P53041; -.
DR DIP; DIP-29043N; -.
DR IntAct; P53041; 19.
DR MINT; MINT-1411788; -.
DR STRING; 9606.ENSP00000012443; -.
DR PhosphoSite; P53041; -.
DR DMDM; 1709744; -.
DR PaxDb; P53041; -.
DR PRIDE; P53041; -.
DR DNASU; 5536; -.
DR Ensembl; ENST00000012443; ENSP00000012443; ENSG00000011485.
DR GeneID; 5536; -.
DR KEGG; hsa:5536; -.
DR UCSC; uc002pem.3; human.
DR CTD; 5536; -.
DR GeneCards; GC19P046850; -.
DR HGNC; HGNC:9322; PPP5C.
DR HPA; CAB022641; -.
DR HPA; HPA029065; -.
DR MIM; 600658; gene.
DR neXtProt; NX_P53041; -.
DR PharmGKB; PA33686; -.
DR eggNOG; COG0639; -.
DR HOGENOM; HOG000172698; -.
DR HOVERGEN; HBG000216; -.
DR InParanoid; P53041; -.
DR KO; K04460; -.
DR OMA; GERTECA; -.
DR OrthoDB; EOG4PVNZ1; -.
DR PhylomeDB; P53041; -.
DR EvolutionaryTrace; P53041; -.
DR GenomeRNAi; 5536; -.
DR NextBio; 21446; -.
DR ArrayExpress; P53041; -.
DR Bgee; P53041; -.
DR CleanEx; HS_PPP5C; -.
DR Genevestigator; P53041; -.
DR GermOnline; ENSG00000011485; Homo sapiens.
DR GO; GO:0005829; C:cytosol; IEA:Compara.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043005; C:neuron projection; IEA:Compara.
DR GO; GO:0043025; C:neuronal cell body; IEA:Compara.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; TAS:ProtInc.
DR GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
DR GO; GO:0007067; P:mitosis; TAS:ProtInc.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
DR GO; GO:0051291; P:protein heterooligomerization; IEA:Compara.
DR GO; GO:0043278; P:response to morphine; IEA:Compara.
DR GO; GO:0006351; P:transcription, DNA-dependent; TAS:ProtInc.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR004843; Metallo_PEstase_dom.
DR InterPro; IPR013235; PPP_dom.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR011236; Ser/Thr_PPase_5.
DR InterPro; IPR001440; TPR-1.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11668:SF12; PTHR11668:SF12; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08321; PPP5; 1.
DR Pfam; PF00515; TPR_1; 2.
DR PIRSF; PIRSF033096; PPPtase_5; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SMART; SM00028; TPR; 3.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Iron;
KW Manganese; Metal-binding; Nucleus; Protein phosphatase;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 499 Serine/threonine-protein phosphatase 5.
FT /FTId=PRO_0000058894.
FT REPEAT 28 61 TPR 1.
FT REPEAT 62 95 TPR 2.
FT REPEAT 96 129 TPR 3.
FT REGION 184 499 Catalytic.
FT ACT_SITE 304 304 Proton donor (By similarity).
FT METAL 242 242 Iron (By similarity).
FT METAL 244 244 Iron (By similarity).
FT METAL 271 271 Iron (By similarity).
FT METAL 271 271 Manganese (By similarity).
FT METAL 303 303 Manganese (By similarity).
FT METAL 352 352 Manganese (By similarity).
FT METAL 427 427 Manganese (By similarity).
FT CONFLICT 403 403 S -> T (in Ref. 4; AAB60384).
FT HELIX 22 40
FT HELIX 44 57
FT HELIX 62 74
FT HELIX 78 91
FT STRAND 92 94
FT HELIX 96 108
FT HELIX 112 125
FT HELIX 130 164
FT HELIX 182 184
FT HELIX 188 199
FT HELIX 206 221
FT STRAND 225 229
FT STRAND 236 240
FT HELIX 247 257
FT STRAND 266 270
FT STRAND 273 276
FT HELIX 279 292
FT TURN 294 296
FT STRAND 297 300
FT STRAND 303 306
FT HELIX 307 313
FT HELIX 315 322
FT HELIX 325 335
FT STRAND 340 344
FT TURN 345 347
FT STRAND 348 350
FT STRAND 357 359
FT HELIX 363 368
FT STRAND 372 374
FT STRAND 377 379
FT HELIX 380 386
FT STRAND 391 397
FT STRAND 401 406
FT HELIX 408 418
FT STRAND 421 425
FT STRAND 433 437
FT HELIX 438 440
FT STRAND 442 446
FT HELIX 451 453
FT STRAND 459 465
FT STRAND 468 476
FT TURN 486 489
FT HELIX 492 495
SQ SEQUENCE 499 AA; 56879 MW; DB3B2090D8658BB3 CRC64;
MAMAEGERTE CAEPPRDEPP ADGALKRAEE LKTQANDYFK AKDYENAIKF YSQAIELNPS
NAIYYGNRSL AYLRTECYGY ALGDATRAIE LDKKYIKGYY RRAASNMALG KFRAALRDYE
TVVKVKPHDK DAKMKYQECN KIVKQKAFER AIAGDEHKRS VVDSLDIESM TIEDEYSGPK
LEDGKVTISF MKELMQWYKD QKKLHRKCAY QILVQVKEVL SKLSTLVETT LKETEKITVC
GDTHGQFYDL LNIFELNGLP SETNPYIFNG DFVDRGSFSV EVILTLFGFK LLYPDHFHLL
RGNHETDNMN QIYGFEGEVK AKYTAQMYEL FSEVFEWLPL AQCINGKVLI MHGGLFSEDG
VTLDDIRKIE RNRQPPDSGP MCDLLWSDPQ PQNGRSISKR GVSCQFGPDV TKAFLEENNL
DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN YCDQMGNKAS YIHLQGSDLR PQFHQFTAVP
HPNVKPMAYA NTLLQLGMM
//
