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UniProtKB - P53041 (PPP5_HUMAN)

Entry version 226 (29 Sep 2021)
Sequence version 1 (01 Oct 1996)
Previous versions | rss
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Protein

Serine/threonine-protein phosphatase 5

Gene

PPP5C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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 (PubMed:14734805, PubMed:14764652, PubMed:14871926, PubMed:15383005, PubMed:15546861, PubMed:16260606, PubMed:16790549, PubMed:16892053, PubMed:19176521, PubMed:19948726, PubMed:21144835, PubMed:22399290, PubMed:22781750, PubMed:23102700, PubMed:9000529, PubMed:30699359).

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 (PubMed:14734805, PubMed:14764652, PubMed:14871926, PubMed:15383005, PubMed:15546861, PubMed:16260606, PubMed:16790549, PubMed:16892053, PubMed:19176521, PubMed:19948726, PubMed:21144835, PubMed:22399290, PubMed:22781750, PubMed:23102700, PubMed:9000529, PubMed:30699359).

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 (PubMed:14871926, PubMed:16260606, PubMed:21144835).

Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress (PubMed:23102700).

Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function (By similarity).

Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1 (By similarity).

Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E (PubMed:16790549).

May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels (PubMed:22781750).

Dephosphorylates and may play a role in the regulation of TAU/MAPT (PubMed:15546861).

Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2 (By similarity).

Dephosphorylate FNIP1, disrupting interaction with HSP90AA1/Hsp90 (PubMed:30699359).

By similarity16 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+, Mn2+Note: Binds 2 Mg2+ or Mn2+ cations per subunit.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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

<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

  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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi242Manganese 1Combined sources3 Publications1
Metal bindingi244Manganese 1; via tele nitrogenCombined sources3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei244Substrate1 Publication1
Metal bindingi271Manganese 1Combined sources3 Publications1
Metal bindingi271Manganese 2Combined sources3 Publications1
Binding sitei275Substrate1 Publication1
Metal bindingi303Manganese 2Combined sources3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei304Proton donor/acceptor1 Publication1
Metal bindingi352Manganese 2; via tele nitrogenCombined sources3 Publications1
Binding sitei400Substrate1 Publication1
Metal bindingi427Manganese 2; via pros nitrogenCombined sources3 Publications1
Binding sitei427Substrate1 Publication1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protein phosphatase
Biological processDNA damage, DNA repair
LigandLipid-binding, Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.1.3.16, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P53041

Reactome - a knowledgebase of biological pathways and processes

More...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-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P53041

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P53041

SIGNOR Signaling Network Open Resource

More...SIGNORi		P53041

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 5 (EC:3.1.3.167 Publications)
Short name:
PP5
Alternative name(s):
Protein phosphatase T
Short name:
PP-T
Short name:
PPT
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PPP5C
Synonyms:PPP5
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9322, PPP5C

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600658, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P53041

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000011485

<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

Keywords - Cellular componenti

Amyloid, Cell membrane, Cytoplasm, Membrane, Nucleus

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi32K → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. 1 Publication1
Mutagenesisi74R → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. 1 Publication1
Mutagenesisi83G → N: No effect on interaction with HSP90AA1. 1 Publication1
Mutagenesisi93K → E: Decreases interaction with RAC1 and translocation to the membrane in presence of active RAC1. 1 Publication1
Mutagenesisi97K → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. Loss of interaction with RAF1. 2 Publications1
Mutagenesisi101R → A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. 1 Publication1
Mutagenesisi304H → Q: Catalytically inactive; no effect on interaction with CRY2 but increases the stability of the interaction with CSNK1E. No effect on RAF1 phosphorylation. 3 Publications1

Keywords - Diseasei

Alzheimer disease, Amyloidosis, Neurodegeneration

Organism-specific databases

DisGeNET

More...DisGeNETi		5536

Open Targets

More...OpenTargetsi		ENSG00000011485

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33686

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P53041, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3425389

Drug and drug target database

More...DrugBanki		DB00171, ATP

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PPP5C

Domain mapping of disease mutations (DMDM)

More...DMDMi		1709744

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000588942 – 499Serine/threonine-protein phosphatase 5Add BLAST498

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		P53041

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P53041

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P53041

MaxQB - The MaxQuant DataBase

More...MaxQBi		P53041

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P53041

PeptideAtlas

More...PeptideAtlasi		P53041

PRoteomics IDEntifications database

More...PRIDEi		P53041

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		56568

PTM databases

DEPOD human dephosphorylation database

More...DEPODi		PPP5C

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P53041, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P53041

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P53041

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P53041

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P53041

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000011485, Expressed in frontal cortex and 177 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P53041, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P53041, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000011485, Low tissue specificity

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111528, 134 interactors

Database of interacting proteins

More...DIPi		DIP-29043N

Protein interaction database and analysis system

More...IntActi		P53041, 70 interactors

Molecular INTeraction database

More...MINTi		P53041

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000012443

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P53041

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P53041, protein

<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

1499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P53041

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P53041

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P53041

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati28 – 61TPR 1Add BLAST34
Repeati62 – 95TPR 2Add BLAST34
Repeati96 – 129TPR 3Add BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 23DisorderedSequence analysisAdd BLAST23
Regioni184 – 499CatalyticAdd BLAST316
Regioni303 – 304Substrate binding1 Publication2
Regioni495 – 499Required for autoinhibitionBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi9 – 23Basic and acidic residuesSequence analysisAdd BLAST15

<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

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

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0376, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000158785

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P53041

Identification of Orthologs from Complete Genome Data

More...OMAi		NHFFMSR

Database of Orthologous Groups

More...OrthoDBi		671536at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P53041

TreeFam database of animal gene trees

More...TreeFami		TF105562

Family and domain databases

Conserved Domains Database

More...CDDi		cd07417, MPP_PP5_C, 1 hit

Database of protein disorder

More...DisProti		DP00365

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.40.10, 1 hit
3.60.21.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR004843, Calcineurin-like_PHP_ApaH
IPR029052, Metallo-depent_PP-like
IPR041753, PP5_C
IPR013235, PPP_dom
IPR006186, Ser/Thr-sp_prot-phosphatase
IPR011236, Ser/Thr_PPase_5
IPR011990, TPR-like_helical_dom_sf
IPR001440, TPR_1
IPR019734, TPR_repeat

The PANTHER Classification System

More...PANTHERi		PTHR45668:SF5, PTHR45668:SF5, 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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00114, STPHPHTASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00156, PP2Ac, 1 hit
SM00028, TPR, 3 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48452, SSF48452, 1 hit
SSF56300, SSF56300, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00125, SER_THR_PHOSPHATASE, 1 hit
PS50005, TPR, 3 hits
PS50293, TPR_REGION, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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 allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDB3B2090D8658BB3
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YDU8H0YDU8_HUMAN
Serine/threonine-protein phosphatas...
PPP5C
485Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A8MU39A8MU39_HUMAN
Serine/threonine-protein phosphatas...
PPP5C
371Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti403S → T in AAB60384 (PubMed:8666404).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

Protein sequence database of the Protein Information Resource

More...PIRi		S52570

NCBI Reference Sequences

More...RefSeqi		NP_006238.1, NM_006247.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000012443; ENSP00000012443; ENSG00000011485

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5536

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5536

UCSC genome browser

More...UCSCi		uc002pem.4, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
CCDSiCCDS12684.1
PIRiS52570
RefSeqiNP_006238.1, NM_006247.3

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 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[»]
4ZVZX-ray2.00A/B/C/D169-499[»]
4ZX2X-ray1.23A169-499[»]
5HPEX-ray2.27A175-499[»]
5UI1X-ray1.96A/B/C/D169-499[»]
5WG8X-ray1.65A169-499[»]
BMRBiP53041
SMRiP53041
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111528, 134 interactors
DIPiDIP-29043N
IntActiP53041, 70 interactors
MINTiP53041
STRINGi9606.ENSP00000012443

Chemistry databases

BindingDBiP53041
ChEMBLiCHEMBL3425389
DrugBankiDB00171, ATP

PTM databases

DEPODiPPP5C
GlyGeniP53041, 1 site, 1 O-linked glycan (1 site)
iPTMnetiP53041
MetOSiteiP53041
PhosphoSitePlusiP53041
SwissPalmiP53041

Genetic variation databases

BioMutaiPPP5C
DMDMi1709744

Proteomic databases

EPDiP53041
jPOSTiP53041
MassIVEiP53041
MaxQBiP53041
PaxDbiP53041
PeptideAtlasiP53041
PRIDEiP53041
ProteomicsDBi56568

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		31446, 676 antibodies

The DNASU plasmid repository

More...DNASUi		5536

Genome annotation databases

EnsembliENST00000012443; ENSP00000012443; ENSG00000011485
GeneIDi5536
KEGGihsa:5536
UCSCiuc002pem.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5536
DisGeNETi5536

GeneCards: human genes, protein and diseases

More...GeneCardsi		PPP5C
HGNCiHGNC:9322, PPP5C
HPAiENSG00000011485, Low tissue specificity
MIMi600658, gene
neXtProtiNX_P53041
OpenTargetsiENSG00000011485
PharmGKBiPA33686
VEuPathDBiHostDB:ENSG00000011485

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0376, Eukaryota
GeneTreeiENSGT00940000158785
InParanoidiP53041
OMAiNHFFMSR
OrthoDBi671536at2759
PhylomeDBiP53041
TreeFamiTF105562

Enzyme and pathway databases

BRENDAi3.1.3.16, 2681
PathwayCommonsiP53041
ReactomeiR-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-RKiP53041
SignaLinkiP53041
SIGNORiP53041

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5536, 19 hits in 1023 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		PPP5C, human
EvolutionaryTraceiP53041

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PPP5C

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		5536
PharosiP53041, Tbio

Protein Ontology

More...PROi		PR:P53041
RNActiP53041, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000011485, Expressed in frontal cortex and 177 other tissues
ExpressionAtlasiP53041, baseline and differential
GenevisibleiP53041, HS

Family and domain databases

CDDicd07417, MPP_PP5_C, 1 hit
DisProtiDP00365
Gene3Di1.25.40.10, 1 hit
3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR004843, Calcineurin-like_PHP_ApaH
IPR029052, Metallo-depent_PP-like
IPR041753, PP5_C
IPR013235, PPP_dom
IPR006186, Ser/Thr-sp_prot-phosphatase
IPR011236, Ser/Thr_PPase_5
IPR011990, TPR-like_helical_dom_sf
IPR001440, TPR_1
IPR019734, TPR_repeat
PANTHERiPTHR45668:SF5, PTHR45668:SF5, 1 hit
PfamiView protein in Pfam
PF00149, Metallophos, 1 hit
PF08321, PPP5, 1 hit
PF00515, TPR_1, 1 hit
PRINTSiPR00114, STPHPHTASE
SMARTiView protein in SMART
SM00156, PP2Ac, 1 hit
SM00028, TPR, 3 hits
SUPFAMiSSF48452, SSF48452, 1 hit
SSF56300, SSF56300, 1 hit
PROSITEiView protein in PROSITE
PS00125, SER_THR_PHOSPHATASE, 1 hit
PS50005, TPR, 3 hits
PS50293, TPR_REGION, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPPP5_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P53041
Secondary accession number(s): Q16722, Q53XV2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 29, 2021
This is version 226 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<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

Keywords - Technical termi

3D-structure, 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
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