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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. 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

<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 ‘Function’ 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 ‘Function’ 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 ‘Function’ 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 ‘Function’ 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

    • ADP binding Source: MGI
    • ATP binding Source: MGI
    • G-protein alpha-subunit binding Source: Ensembl
    • Hsp90 protein binding Source: CAFA
    • identical protein binding Source: IntAct
    • lipid binding Source: UniProtKB-KW
    • metal ion binding Source: UniProtKB-KW
    • microtubule binding Source: Ensembl
    • phosphatase activity Source: ARUK-UCL
    • phosphoprotein phosphatase activity Source: UniProtKB
    • protein serine/threonine phosphatase activity Source: ARUK-UCL
    • RNA binding Source: Ensembl

    GO - Biological processi

    <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

    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:3.1.3.16)
    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <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

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000011485.14

    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

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    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

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3425389

    Polymorphism and mutation 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.<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

    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 human proteome resource

    More...
    ProteomicsDBi
    56568

    PTM databases

    DEPOD human dephosphorylation database

    More...
    DEPODi
    P53041

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P53041

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

    More...
    PhosphoSitePlusi
    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 160 organ(s), highest expression level in frontal cortex

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_PPP5C

    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
    CAB022641
    HPA029065
    HPA056933

    <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%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    111528, 113 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-29043N

    Protein interaction database and analysis system

    More...
    IntActi
    P53041, 64 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

    <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

    Database of protein disorder

    More...
    DisProti
    DP00365

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P53041

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

    More...
    SMRi
    P53041

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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>Regioni184 – 499CatalyticAdd BLAST316
    Regioni303 – 304Substrate binding1 Publication2
    Regioni495 – 499Required for autoinhibitionBy similarity5

    <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

    Repeat, TPR repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0376 Eukaryota
    COG0639 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000158785

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000172698

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG000216

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P53041

    KEGG Orthology (KO)

    More...
    KOi
    K04460

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    LYPNHFF

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G0589

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P53041

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF105562

    Family and domain databases

    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
    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

    The PANTHER Classification System

    More...
    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

    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

    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>.<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

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.654604

    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
    UniGeneiHs.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 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[»]
    DisProtiDP00365
    ProteinModelPortaliP53041
    SMRiP53041
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111528, 113 interactors
    DIPiDIP-29043N
    IntActiP53041, 64 interactors
    MINTiP53041
    STRINGi9606.ENSP00000012443

    Chemistry databases

    BindingDBiP53041
    ChEMBLiCHEMBL3425389

    PTM databases

    DEPODiP53041
    iPTMnetiP53041
    PhosphoSitePlusiP53041

    Polymorphism and mutation databases

    BioMutaiPPP5C
    DMDMi1709744

    Proteomic databases

    EPDiP53041
    MaxQBiP53041
    PaxDbiP53041
    PeptideAtlasiP53041
    PRIDEiP53041
    ProteomicsDBi56568

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    5536
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    5536
    DisGeNETi5536
    EuPathDBiHostDB:ENSG00000011485.14

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    PPP5C
    HGNCiHGNC:9322 PPP5C
    HPAiCAB022641
    HPA029065
    HPA056933
    MIMi600658 gene
    neXtProtiNX_P53041
    OpenTargetsiENSG00000011485
    PharmGKBiPA33686

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0376 Eukaryota
    COG0639 LUCA
    GeneTreeiENSGT00940000158785
    HOGENOMiHOG000172698
    HOVERGENiHBG000216
    InParanoidiP53041
    KOiK04460
    OMAiLYPNHFF
    OrthoDBiEOG091G0589
    PhylomeDBiP53041
    TreeFamiTF105562

    Enzyme and pathway databases

    BRENDAi3.1.3.16 2681
    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

    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

    Protein Ontology

    More...
    PROi
    PR:P53041

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000011485 Expressed in 160 organ(s), highest expression level in frontal cortex
    CleanExiHS_PPP5C
    ExpressionAtlasiP53041 baseline and differential
    GenevisibleiP53041 HS

    Family and domain databases

    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
    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
    PANTHERiPTHR11668:SF391 PTHR11668:SF391, 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
    PROSITEiView protein in PROSITE
    PS00125 SER_THR_PHOSPHATASE, 1 hit
    PS50005 TPR, 3 hits
    PS50293 TPR_REGION, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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: December 5, 2018
    This is version 209 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, Complete proteome, Reference proteome

    Documents

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