PPP5C

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 Mg²⁺ or Mn²⁺ cations per subunit.

Activity 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

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	242	Manganese 1Combined sources3 Publications	1
Metal bindingⁱ	244	Manganese 1; via tele nitrogenCombined sources3 Publications	1
Binding siteⁱ	244	Substrate1 Publication	1
Metal bindingⁱ	271	Manganese 1Combined sources3 Publications	1
Metal bindingⁱ	271	Manganese 2Combined sources3 Publications	1
Binding siteⁱ	275	Substrate1 Publication	1
Metal bindingⁱ	303	Manganese 2Combined sources3 Publications	1
Active siteⁱ	304	Proton donor/acceptor1 Publication	1
Metal bindingⁱ	352	Manganese 2; via tele nitrogenCombined sources3 Publications	1
Binding siteⁱ	400	Substrate1 Publication	1
Metal bindingⁱ	427	Manganese 2; via pros nitrogenCombined sources3 Publications	1
Binding siteⁱ	427	Substrate1 Publication	1

GO - Molecular functionⁱ

ADP binding
Source: MGI
Inferred from direct assayⁱ
- 23184943
ATP binding
Source: MGI
Inferred from direct assayⁱ
- 23184943
G-protein alpha-subunit binding Source: Ensembl
Hsp90 protein binding
Source: CAFA
Inferred from physical interactionⁱ
- 15713458
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 21360678
lipid binding Source: UniProtKB-KW
metal ion binding Source: UniProtKB-KW
microtubule binding Source: Ensembl
phosphatase activity
Source: ARUK-UCL
Inferred from direct assayⁱ
- 15546861
phosphoprotein phosphatase activity
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
- 9383998
protein serine/threonine phosphatase activity
Source: ARUK-UCL
Inferred from sequence or structural similarityⁱ
- 15546861
RNA binding Source: Ensembl

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to cadmium ion Source: Ensembl
cellular response to hydrogen peroxide Source: Ensembl
DNA repair Source: UniProtKB-KW
histone dephosphorylation Source: Ensembl
MAPK cascade Source: Reactome
mitotic cell cycle
Source: ProtInc
Traceable author statementⁱ
- 7925273
negative regulation of neuron death Source: Ensembl
negative regulation of protein phosphorylation Source: Ensembl
peptidyl-serine dephosphorylation
Source: ARUK-UCL
Traceable author statementⁱ
- 16262633
peptidyl-threonine dephosphorylation
Source: ARUK-UCL
Traceable author statementⁱ
- 16262633
positive regulation of glucocorticoid receptor signaling pathway Source: Ensembl
positive regulation of I-kappaB kinase/NF-kappaB signaling
Source: UniProtKB
Inferred from high throughput mutant phenotypeⁱ
- 12761501
protein dephosphorylation
Source: ProtInc
Traceable author statementⁱ
- 7925273
protein heterooligomerization Source: Ensembl
response to arachidonic acid
Source: ARUK-UCL
Inferred from sequence or structural similarityⁱ
- 15546861
response to lead ion Source: ARUK-UCL
response to morphine Source: Ensembl
transcription, DNA-templated
Source: ProtInc
Traceable author statementⁱ
- 7925273

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Protein phosphatase
Biological process	DNA damage, DNA repair
Ligand	Lipid-binding, Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	3.1.3.16 2681
Reactomeⁱ	R-HSA-5675221 Negative regulation of MAPK pathway R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks R-HSA-8939211 ESR-mediated signaling
SABIO-RKⁱ	P53041
SignaLinkⁱ	P53041
SIGNORⁱ	P53041

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 19

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000011485.14
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9322 PPP5C
MIMⁱ	600658 gene
neXtProtⁱ	NX_P53041

Keywords - Cellular componentⁱ

Amyloid, Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	32	K → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. 1 Publication	1
Mutagenesisⁱ	74	R → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. 1 Publication	1
Mutagenesisⁱ	83	G → N: No effect on interaction with HSP90AA1. 1 Publication	1
Mutagenesisⁱ	93	K → E: Decreases interaction with RAC1 and translocation to the membrane in presence of active RAC1. 1 Publication	1
Mutagenesisⁱ	97	K → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. Loss of interaction with RAF1. 2 Publications	1
Mutagenesisⁱ	101	R → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. 1 Publication	1
Mutagenesisⁱ	304	H → 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	1

Keywords - Diseaseⁱ

Alzheimer disease, Amyloidosis, Neurodegeneration

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5536
Open Targets More...OpenTargetsⁱ	ENSG00000011485
PharmGKBⁱ	PA33686

Chemistry databases

ChEMBLⁱ	CHEMBL3425389

ChEMBLⁱ

CHEMBL3425389

Polymorphism and mutation databases

BioMutaⁱ	PPP5C
DMDMⁱ	1709744

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000058894	2 – 499	Serine/threonine-protein phosphatase 5Add BLAST		498

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	2	N-acetylalanineCombined sources		1

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

EPDⁱ	P53041
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P53041
PaxDbⁱ	P53041
PeptideAtlas More...PeptideAtlasⁱ	P53041
PRIDEⁱ	P53041
ProteomicsDBⁱ	56568

PTM databases

DEPODⁱ	P53041
iPTMnetⁱ	P53041
PhosphoSitePlusⁱ	P53041

Expressionⁱ

Tissue specificityⁱ

Ubiquitous.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000011485 Expressed in 160 organ(s), highest expression level in frontal cortex
CleanExⁱ	HS_PPP5C
ExpressionAtlasⁱ	P53041 baseline and differential
Genevisibleⁱ	P53041 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB022641 HPA029065 HPA056933

HPAⁱ

CAB022641
HPA029065
HPA056933

Interactionⁱ

Subunit structureⁱ

Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (PubMed:29127155). Part of a complex with HSP90/HSP90AA1 and steroid receptors (By similarity). Interacts (via TPR repeats) with HSP90AA1 (via TPR repeat-binding motif) or HSPA1A/HSPA1B; the interaction is direct and activates the phosphatase activity (PubMed:15383005, PubMed:15577939, PubMed:16531226). Dissociates from HSPA1A/HSPA1B and HSP90AA1 in response to arachidonic acid (PubMed:15383005). Interacts with CPNE1 (via VWFA domain) (By similarity). Interacts with CDC16, CDC27 (PubMed:9405394). Interacts with KLHDC10 (via the 6 Kelch repeats); inhibits the phosphatase activity on MAP3K5 (PubMed:23102700). Interacts with ATM and ATR; both interactions are induced by DNA damage and enhance ATM and ATR kinase activity (PubMed:14871926). Interacts with RAD17; reduced by DNA damage (PubMed:14871926). Interacts with nuclear receptors such as NR3C1/GCR and PPARG (activated by agonist); regulates their transactivation activities (By similarity). 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 (PubMed:22399290). Interacts with SMAD2 and SMAD3 but not with SMAD1; decreases SMAD3 phosphorylation and protein levels (PubMed:22781750). Interacts (via TPR repeats) with CRY1 and CRY2; the interaction with CRY2 downregulates the phosphatase activity on CSNK1E (PubMed:16790549). 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 (PubMed:19948726). Interacts with FLCN (PubMed:27353360).By similarity12 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
itself		2	EBI-716663,EBI-716663
AGO1	Q9UL18	2	EBI-716663,EBI-527363
AGO3	Q9H9G7	2	EBI-716663,EBI-2267883
CDC37	Q16543	5	EBI-716663,EBI-295634
CDK9	P50750	3	EBI-716663,EBI-1383449
CRY2	Q49AN0	3	EBI-716663,EBI-2212355
ESR1	P03372	4	EBI-716663,EBI-78473
ESR2	Q92731	4	EBI-716663,EBI-78505
HSP90AA1	P07900	11	EBI-716663,EBI-296047
HSP90AB1	P08238	7	EBI-716663,EBI-352572
NOL9	Q5SY16	2	EBI-716663,EBI-1055462
PPP2R1A	P30153	3	EBI-716663,EBI-302388
STIP1	P31948	4	EBI-716663,EBI-1054052

GO - Molecular functionⁱ

G-protein alpha-subunit binding Source: Ensembl
Hsp90 protein binding
Source: CAFA
Inferred from physical interactionⁱ
- 15713458
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 21360678
microtubule binding Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	111528, 86 interactors
Database of interacting proteins More...DIPⁱ	DIP-29043N
IntActⁱ	P53041, 64 interactors
Molecular INTeraction database More...MINTⁱ	P53041
STRINGⁱ	9606.ENSP00000012443

Chemistry databases

BindingDBⁱ

P53041

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	22 – 40	Combined sources	19
Helixⁱ	44 – 57	Combined sources	14
Helixⁱ	62 – 74	Combined sources	13
Helixⁱ	78 – 91	Combined sources	14
Beta strandⁱ	92 – 94	Combined sources	3
Helixⁱ	96 – 108	Combined sources	13
Helixⁱ	112 – 125	Combined sources	14
Helixⁱ	130 – 164	Combined sources	35
Beta strandⁱ	182 – 184	Combined sources	3
Helixⁱ	188 – 199	Combined sources	12
Helixⁱ	206 – 221	Combined sources	16
Beta strandⁱ	225 – 229	Combined sources	5
Beta strandⁱ	236 – 240	Combined sources	5
Helixⁱ	247 – 257	Combined sources	11
Beta strandⁱ	262 – 264	Combined sources	3
Beta strandⁱ	266 – 270	Combined sources	5
Beta strandⁱ	273 – 276	Combined sources	4
Helixⁱ	279 – 292	Combined sources	14
Turnⁱ	294 – 296	Combined sources	3
Beta strandⁱ	297 – 300	Combined sources	4
Beta strandⁱ	303 – 306	Combined sources	4
Helixⁱ	307 – 313	Combined sources	7
Helixⁱ	315 – 322	Combined sources	8
Helixⁱ	325 – 335	Combined sources	11
Beta strandⁱ	340 – 344	Combined sources	5
Turnⁱ	345 – 347	Combined sources	3
Beta strandⁱ	348 – 350	Combined sources	3
Beta strandⁱ	357 – 359	Combined sources	3
Helixⁱ	363 – 367	Combined sources	5
Beta strandⁱ	372 – 374	Combined sources	3
Beta strandⁱ	377 – 379	Combined sources	3
Helixⁱ	380 – 386	Combined sources	7
Beta strandⁱ	391 – 397	Combined sources	7
Beta strandⁱ	401 – 406	Combined sources	6
Helixⁱ	408 – 417	Combined sources	10
Beta strandⁱ	422 – 425	Combined sources	4
Beta strandⁱ	433 – 437	Combined sources	5
Helixⁱ	438 – 440	Combined sources	3
Beta strandⁱ	442 – 446	Combined sources	5
Helixⁱ	451 – 453	Combined sources	3
Beta strandⁱ	459 – 465	Combined sources	7
Beta strandⁱ	468 – 476	Combined sources	9
Turnⁱ	486 – 489	Combined sources	4
Helixⁱ	492 – 495	Combined sources	4

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00365
ProteinModelPortalⁱ	P53041
SMRⁱ	P53041
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P53041

EvolutionaryTraceⁱ

P53041

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	28 – 61	TPR 1Add BLAST	34
Repeatⁱ	62 – 95	TPR 2Add BLAST	34
Repeatⁱ	96 – 129	TPR 3Add BLAST	34

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	184 – 499	CatalyticAdd BLAST	316
Regionⁱ	303 – 304	Substrate binding1 Publication	2
Regionⁱ	495 – 499	Required for autoinhibitionBy similarity	5

Sequence similaritiesⁱ

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

Keywords - Domainⁱ

Repeat, TPR repeat

Phylogenomic databases

eggNOGⁱ	KOG0376 Eukaryota COG0639 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063173
HOGENOMⁱ	HOG000172698
HOVERGENⁱ	HBG000216
InParanoidⁱ	P53041
KEGG Orthology (KO) More...KOⁱ	K04460
OMAⁱ	LYPNHFF
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0589
PhylomeDBⁱ	P53041
TreeFamⁱ	TF105562

Family and domain databases

Gene3Dⁱ	1.25.40.10, 1 hit 3.60.21.10, 1 hit
InterProⁱ	View protein in InterPro 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_sf IPR001440 TPR_1 IPR019734 TPR_repeat
PANTHERⁱ	PTHR11668:SF391 PTHR11668:SF391, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00149 Metallophos, 1 hit PF08321 PPP5, 1 hit PF00515 TPR_1, 1 hit
PRINTSⁱ	PR00114 STPHPHTASE
SMARTⁱ	View protein in SMART SM00156 PP2Ac, 1 hit SM00028 TPR, 3 hits
SUPFAMⁱ	SSF48452 SSF48452, 1 hit
PROSITEⁱ	View protein in PROSITE PS00125 SER_THR_PHOSPHATASE, 1 hit PS50005 TPR, 3 hits PS50293 TPR_REGION, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show all Align All

P53041-1 [UniParc]FASTA Add 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

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H0YDU8	H0YDU8_HUMAN	Serine/threonine-protein phosphatas... Serine/threonine-protein phosphatase, EC 3.1.3.16	PPP5C	485	Annotation score:
A8MU39	A8MU39_HUMAN	Serine/threonine-protein phosphatas... Serine/threonine-protein phosphatase, EC 3.1.3.16	PPP5C	371	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	403	S → T in AAB60384 (PubMed:8666404).Curated		1

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS12684.1
PIRⁱ	S52570
NCBI Reference Sequences More...RefSeqⁱ	NP_006238.1, NM_006247.3
UniGeneⁱ	Hs.654604

Genome annotation databases

Ensemblⁱ	ENST00000012443; ENSP00000012443; ENSG00000011485
GeneIDⁱ	5536
KEGGⁱ	hsa:5536
UCSC genome browser More...UCSCⁱ	uc002pem.4 human

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P53041	Serine/threonine-protein phosphatase		HUMAN		499	UniRef100_P53041
UPI00004E17E7		HUMAN		477
UPI0001BE64D7		HUMAN		315

Protein	Similar proteins		Species	Score	Length	Source
P53041	Serine/threonine-protein phosphatase 5	)	RAT		499	UniRef90_P53041
Serine/threonine-protein phosphatase 5		MOUSE		499
Serine/threonine-protein phosphatase 5 (Fragment)		RABIT		42
Serine/threonine-protein phosphatase		HUMAN		499
Serine/threonine-protein phosphatase		PANTR		503
+125

Protein	Similar proteins		Species	Score	Length	Source
P53041	Serine/threonine-protein phosphatase 5	)	RAT		499	UniRef50_P53041
Serine/threonine-protein phosphatase 5		MOUSE		499
Serine/threonine-protein phosphatase 5 (Fragment)		RABIT		42
Serine/threonine-protein phosphatase		HUMAN		499
Serine/threonine-protein phosphatase		PANTR		503
+140

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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	4ZVZ	X-ray	2.00	A/B/C/D	169-499	[»]
	4ZX2	X-ray	1.23	A	169-499	[»]
	5HPE	X-ray	2.27	A	175-499	[»]
	5UI1	X-ray	1.96	A/B/C/D	169-499	[»]
	5WG8	X-ray	1.65	A	169-499	[»]
DisProtⁱ	DP00365
ProteinModelPortalⁱ	P53041
SMRⁱ	P53041
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111528, 86 interactors
DIPⁱ	DIP-29043N
IntActⁱ	P53041, 64 interactors
MINTⁱ	P53041
STRINGⁱ	9606.ENSP00000012443

Chemistry databases

BindingDBⁱ	P53041
ChEMBLⁱ	CHEMBL3425389

PTM databases

DEPODⁱ	P53041
iPTMnetⁱ	P53041
PhosphoSitePlusⁱ	P53041

Polymorphism and mutation databases

BioMutaⁱ	PPP5C
DMDMⁱ	1709744

Proteomic databases

EPDⁱ	P53041
MaxQBⁱ	P53041
PaxDbⁱ	P53041
PeptideAtlasⁱ	P53041
PRIDEⁱ	P53041
ProteomicsDBⁱ	56568

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	5536
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000012443; ENSP00000012443; ENSG00000011485
GeneIDⁱ	5536
KEGGⁱ	hsa:5536
UCSCⁱ	uc002pem.4 human

Organism-specific databases

CTDⁱ	5536
DisGeNETⁱ	5536
EuPathDBⁱ	HostDB:ENSG00000011485.14
GeneCardsⁱ	PPP5C
HGNCⁱ	HGNC:9322 PPP5C
HPAⁱ	CAB022641 HPA029065 HPA056933
MIMⁱ	600658 gene
neXtProtⁱ	NX_P53041
OpenTargetsⁱ	ENSG00000011485
PharmGKBⁱ	PA33686
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0376 Eukaryota COG0639 LUCA
GeneTreeⁱ	ENSGT00530000063173
HOGENOMⁱ	HOG000172698
HOVERGENⁱ	HBG000216
InParanoidⁱ	P53041
KOⁱ	K04460
OMAⁱ	LYPNHFF
OrthoDBⁱ	EOG091G0589
PhylomeDBⁱ	P53041
TreeFamⁱ	TF105562

Enzyme and pathway databases

BRENDAⁱ	3.1.3.16 2681
Reactomeⁱ	R-HSA-5675221 Negative regulation of MAPK pathway R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks R-HSA-8939211 ESR-mediated signaling
SABIO-RKⁱ	P53041
SignaLinkⁱ	P53041
SIGNORⁱ	P53041

Miscellaneous databases

ChiTaRSⁱ	PPP5C human
EvolutionaryTraceⁱ	P53041
GeneWikiⁱ	PPP5C
GenomeRNAiⁱ	5536
Protein Ontology More...PROⁱ	PR:P53041
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000011485 Expressed in 160 organ(s), highest expression level in frontal cortex
CleanExⁱ	HS_PPP5C
ExpressionAtlasⁱ	P53041 baseline and differential
Genevisibleⁱ	P53041 HS

Family and domain databases

Gene3Dⁱ	1.25.40.10, 1 hit 3.60.21.10, 1 hit
InterProⁱ	View protein in InterPro 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_sf IPR001440 TPR_1 IPR019734 TPR_repeat
PANTHERⁱ	PTHR11668:SF391 PTHR11668:SF391, 1 hit
Pfamⁱ	View protein in Pfam PF00149 Metallophos, 1 hit PF08321 PPP5, 1 hit PF00515 TPR_1, 1 hit
PRINTSⁱ	PR00114 STPHPHTASE
SMARTⁱ	View protein in SMART SM00156 PP2Ac, 1 hit SM00028 TPR, 3 hits
SUPFAMⁱ	SSF48452 SSF48452, 1 hit
PROSITEⁱ	View protein in PROSITE PS00125 SER_THR_PHOSPHATASE, 1 hit PS50005 TPR, 3 hits PS50293 TPR_REGION, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PPP5_HUMAN
Accessionⁱ	P53041Primary (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 10, 2018
	This is version 207 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB

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UniProtKB - P53041 (PPP5_HUMAN)

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Serine/threonine-protein phosphatase 5

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

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Cytosol

Nucleus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

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Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ