P53041 (PPP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1.
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Subunit structure	Interacts with CDC16 and CDC27. Ref.8
Subcellular location	Nucleus. Cytoplasm. Note: Predominantly nuclear. But also present in the cytoplasm.
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily. Contains 3 TPR repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	Repeat TPR repeat
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitosis Traceable author statement Ref.3. Source: ProtInc positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB protein dephosphorylation Traceable author statement Ref.3. Source: ProtInc protein heterooligomerization Inferred from electronic annotation. Source: Compara response to morphine Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Traceable author statement Ref.3. Source: ProtInc
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA cytosol Inferred from electronic annotation. Source: Compara neuron projection Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara nucleus Traceable author statement Ref.3. Source: ProtInc
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-716663,EBI-716663
CDC37	Q16543	2	EBI-716663,EBI-295634
ESR1	P03372	4	EBI-716663,EBI-78473
ESR2	Q92731	4	EBI-716663,EBI-78505
HSP90AA1	P07900	8	EBI-716663,EBI-296047

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 499

499

Serine/threonine-protein phosphatase 5

PRO_0000058894

Regions

Repeat

28 – 61

34

TPR 1

Repeat

62 – 95

34

TPR 2

Repeat

96 – 129

34

TPR 3

Region

184 – 499

316

Catalytic

Sites

Active site

304

1

Proton donor By similarity

Metal binding

242

1

Iron By similarity

Metal binding

244

1

Iron By similarity

Metal binding

271

1

Iron By similarity

Metal binding

271

1

Manganese By similarity

Metal binding

303

1

Manganese By similarity

Metal binding

352

1

Manganese By similarity

Metal binding

427

1

Manganese By similarity

Experimental info

Sequence conflict

403

1

S → T in AAB60384. Ref.4

Secondary structure

1

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499

Helix Strand Turn

Details...

Helix

22 – 40

19

Helix

44 – 57

14

Helix

62 – 74

13

Helix

78 – 91

14

Beta strand

92 – 94

3

Helix

96 – 108

13

Helix

112 – 125

14

Helix

130 – 164

35

Helix

182 – 184

3

Helix

188 – 199

12

Helix

206 – 221

16

Beta strand

225 – 229

5

Beta strand

236 – 240

5

Helix

247 – 257

11

Beta strand

266 – 270

5

Beta strand

273 – 276

4

Helix

279 – 292

14

Turn

294 – 296

3

Beta strand

297 – 300

4

Beta strand

303 – 306

4

Helix

307 – 313

7

Helix

315 – 322

8

Helix

325 – 335

11

Beta strand

340 – 344

5

Turn

345 – 347

3

Beta strand

348 – 350

3

Beta strand

357 – 359

3

Helix

363 – 368

6

Beta strand

372 – 374

3

Beta strand

377 – 379

3

Helix

380 – 386

7

Beta strand

391 – 397

7

Beta strand

401 – 406

6

Helix

408 – 418

11

Beta strand

421 – 425

5

Beta strand

433 – 437

5

Helix

438 – 440

3

Beta strand

442 – 446

5

Helix

451 – 453

3

Beta strand

459 – 465

7

Beta strand

468 – 476

9

Turn

486 – 489

4

Helix

492 – 495

4

Sequences

	Sequence		Length	Mass (Da)
	P53041 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: DB3B2090D8658BB3	FASTA	499	56,879
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[9]	"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].
[10]	"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].
[11]	"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.
+	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.

IPI

IPI00019812.

PIR

S52570.

RefSeq

NP_006238.1. NM_006247.3.

UniGene

Hs.654604.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

DisProt

DP00365.

ProteinModelPortal

P53041.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29043N.

IntAct

P53041. 19 interactions.

MINT

MINT-1411788.

STRING

9606.ENSP00000012443.

PTM databases

PhosphoSite

P53041.

Polymorphism databases

DMDM

1709744.

Proteomic databases

PaxDb

P53041.

PRIDE

P53041.

Protocols and materials databases

DNASU

5536.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000012443; ENSP00000012443; ENSG00000011485.

GeneID

5536.

KEGG

hsa:5536.

UCSC

uc002pem.3. human.

Organism-specific databases

CTD

5536.

GeneCards

GC19P046850.

HGNC

HGNC:9322. PPP5C.

HPA

CAB022641.
HPA029065.

MIM

600658. gene.

neXtProt

NX_P53041.

PharmGKB

PA33686.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0639.

HOGENOM

HOG000172698.

HOVERGEN

HBG000216.

InParanoid

P53041.

KO

K04460.

OMA

GERTECA.

OrthoDB

EOG4PVNZ1.

PhylomeDB

P53041.

Gene expression databases

ArrayExpress

P53041.

Bgee

P53041.

CleanEx

HS_PPP5C.

Genevestigator

P53041.

GermOnline

ENSG00000011485. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 1 hit.

InterPro

IPR004843. Metallo_PEstase_dom.
IPR013235. PPP_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR011236. Ser/Thr_PPase_5.
IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

PANTHER

PTHR11668:SF12. PTHR11668:SF12. 1 hit.

Pfam

PF00149. Metallophos. 1 hit.
PF08321. PPP5. 1 hit.
PF00515. TPR_1. 2 hits.
[Graphical view]

PIRSF

PIRSF033096. PPPtase_5. 1 hit.

PRINTS

PR00114. STPHPHTASE.

SMART

SM00156. PP2Ac. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]

PROSITE

PS00125. SER_THR_PHOSPHATASE. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P53041.

GenomeRNAi

5536.

NextBio

21446.

SOURCE

Search...

Entry information

Entry name

PPP5_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 152 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.