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Entry version 170 (29 Sep 2021)
Sequence version 1 (01 Oct 1996)
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Protein

Serine/threonine-protein phosphatase 5

Gene

Ppp5c

Organism
Rattus norvegicus (Rat)
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:11523989, PubMed:12176367, PubMed:15546861, PubMed:16892053, PubMed:16549782).

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 (By similarity).

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 (By similarity).

Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress (By similarity).

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 (By similarity).

Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E (By similarity).

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

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 (PubMed:16549782).

Dephosphorylate FNIP1, disrupting interaction with HSP90AA1/Hsp90 (By similarity).

By similarity5 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+2 Publications, Mn2+2 PublicationsNote: Binds 2 magnesium or manganese ions per subunit.2 Publications

<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.3 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=12.1 µM for MAPT/TAU (at pH 7.4 and 30 degrees Celsius)1 Publication

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 bindingi242Magnesium 1Combined sources1 Publication1
Metal bindingi244Magnesium 1; via tele nitrogenCombined sources1 Publication1
<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 sitei244SubstrateBy similarity1
Metal bindingi271Magnesium 1Combined sources1 Publication1
Metal bindingi271Magnesium 2Combined sources1 Publication1
Binding sitei275SubstrateBy similarity1
Metal bindingi303Magnesium 2Combined sources1 Publication1
<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/acceptorBy similarity1
Metal bindingi352Magnesium 2; via tele nitrogenCombined sources1 Publication1
Binding sitei400SubstrateBy similarity1
Metal bindingi427Magnesium 2; via pros nitrogenCombined sources1 Publication1
Binding sitei427SubstrateBy similarity1

<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

<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
LigandMagnesium, Manganese, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.3.16, 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-5675221, Negative regulation of MAPK pathway
R-RNO-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-RNO-8939211, ESR-mediated signaling

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P53042

<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:3.1.3.162 Publications)
Short name:
PP5
Alternative name(s):
Protein phosphatase 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
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 1

Organism-specific databases

Rat genome database

More...
RGDi
68415, Ppp5c

<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

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>Mutagenesisi29E → A: No effect on phosphatase activity. 1 Publication1
Mutagenesisi32K → A: No effect on phosphatase activity. 1 Publication1
Mutagenesisi40K → A: Slightly reduces activation by arachidonic acid. 1
Mutagenesisi56E → A: No effect on phosphatase activity. 1 Publication1
Mutagenesisi63I → A: No effect on phosphatase activity. 1 Publication1
Mutagenesisi74R → A: No effect on phosphatase activity. 1 Publication1
Mutagenesisi76E → A: Increases basal phosphatase activity. 1 Publication1
Mutagenesisi77C → A: No effect on phosphatase activity. 1 Publication1
Mutagenesisi80Y → A: No effect on phosphatase activity. 1 Publication1
Mutagenesisi93K → E: Loss of inhibition of KCNH2 channel stimulation. 1 Publication1
Mutagenesisi97K → A: No effect on phosphatase activity. 1 Publication1
Mutagenesisi101R → A: No effect on phosphatase activity. 1 Publication1
Mutagenesisi126K → A: Loss of inhibition of KCNH2 channel stimulation. 1 Publication1
Mutagenesisi451Y → A: Insensitive to okadaic acid. 1 Publication1

<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 methionineiRemovedBy similarity
<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_00000588972 – 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-acetylalanineBy similarity1

<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.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P53042

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

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PaxDbi
P53042

PRoteomics IDEntifications database

More...
PRIDEi
P53042

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P53042

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

More...
PhosphoSitePlusi
P53042

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P53042

<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

Predominantly found in brain and, in lower levels, in testis, but was nearly undetectable in spleen, lung, skeletal muscle, kidney and liver.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000016907, Expressed in cerebellum and 21 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P53042, RN

<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 (By similarity). 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 (By similarity).

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:26182372). Dissociates from HSPA1A/HSPA1B and HSP90AA1 in response to arachidonic acid (By similarity).

Interacts with CPNE1 (via VWFA domain) (By similarity).

Interacts with CDC16, CDC27 (By similarity).

Interacts with KLHDC10 (via the 6 Kelch repeats); inhibits the phosphatase activity on MAP3K5 (By similarity).

Interacts with ATM and ATR; both interactions are induced by DNA damage and enhance ATM and ATR kinase activity (By similarity).

Interacts with RAD17; reduced by DNA damage (By similarity).

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 (By similarity).

Interacts with SMAD2 and SMAD3 but not with SMAD1; decreases SMAD3 phosphorylation and protein levels (By similarity).

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:12176367, PubMed:16549782).

Interacts with FLCN (By similarity).

By similarity4 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
249291, 3 interactors

Database of interacting proteins

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DIPi
DIP-61212N

Protein interaction database and analysis system

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IntActi
P53042, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000023078

<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

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

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SMRi
P53042

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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
Regioni200 – 499CatalyticAdd BLAST300
Regioni303 – 304Substrate bindingBy similarity2
Regioni495 – 499Required for autoinhibition1 Publication5

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

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0376, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000158785

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_004962_5_2_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P53042

Identification of Orthologs from Complete Genome Data

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OMAi
NHFFMSR

Database of Orthologous Groups

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OrthoDBi
671536at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P53042

TreeFam database of animal gene trees

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TreeFami
TF105562

Family and domain databases

Conserved Domains Database

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CDDi
cd07417, MPP_PP5_C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.40.10, 1 hit
3.60.21.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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PANTHERi
PTHR45668:SF5, PTHR45668:SF5, 1 hit

Pfam protein domain database

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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

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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>Sequencei

<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.

P53042-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAMAEGERTE CAEPPRDEPP AEGTLKRAEE LKTQANDYFK AKDYENAIKF
60 70 80 90 100
YSQAIELNPS NAIYYGNRSL AYLRTECYGY ALGDATRAIE LDKKYIKGYY
110 120 130 140 150
RRAASNMALG KFRAALRDYE TVVKVKPNDK DAKMKYQECS KIVKQKAFER
160 170 180 190 200
AIAGDEHRRS VVDSLDIESM TIEDEYSGPK LEDGKVTITF MKDLMQWYKD
210 220 230 240 250
QKKLHRKCAY QILVQVKEVL CKLSTLVETT 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 PQNGRSVSKR
410 420 430 440 450
GVSCQFGPDV TKAFLEENQL DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN
460 470 480 490
YCDQMGNKAS YIHLQGSDLR PQFHQFTAVP HPNVKPMAYA NTLLQLGMM
Length:499
Mass (Da):56,917
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:i720A7FB7AFC701D2
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X77237 mRNA Translation: CAA54454.1

Protein sequence database of the Protein Information Resource

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PIRi
A55346

NCBI Reference Sequences

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RefSeqi
NP_113917.1, NM_031729.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000023078; ENSRNOP00000023078; ENSRNOG00000016907

Database of genes from NCBI RefSeq genomes

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GeneIDi
65179

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:65179

UCSC genome browser

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UCSCi
RGD:68415, rat

<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
X77237 mRNA Translation: CAA54454.1
PIRiA55346
RefSeqiNP_113917.1, NM_031729.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4JA7X-ray2.00A16-499[»]
4JA9X-ray2.30A16-499[»]
SMRiP53042
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi249291, 3 interactors
DIPiDIP-61212N
IntActiP53042, 2 interactors
STRINGi10116.ENSRNOP00000023078

PTM databases

iPTMnetiP53042
PhosphoSitePlusiP53042
SwissPalmiP53042

Proteomic databases

jPOSTiP53042
PaxDbiP53042
PRIDEiP53042

Genome annotation databases

EnsembliENSRNOT00000023078; ENSRNOP00000023078; ENSRNOG00000016907
GeneIDi65179
KEGGirno:65179
UCSCiRGD:68415, rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5536
RGDi68415, Ppp5c

Phylogenomic databases

eggNOGiKOG0376, Eukaryota
GeneTreeiENSGT00940000158785
HOGENOMiCLU_004962_5_2_1
InParanoidiP53042
OMAiNHFFMSR
OrthoDBi671536at2759
PhylomeDBiP53042
TreeFamiTF105562

Enzyme and pathway databases

BRENDAi3.1.3.16, 5301
ReactomeiR-RNO-5675221, Negative regulation of MAPK pathway
R-RNO-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-RNO-8939211, ESR-mediated signaling
SABIO-RKiP53042

Miscellaneous databases

Protein Ontology

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PROi
PR:P53042

Gene expression databases

BgeeiENSRNOG00000016907, Expressed in cerebellum and 21 other tissues
GenevisibleiP53042, RN

Family and domain databases

CDDicd07417, MPP_PP5_C, 1 hit
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

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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_RAT
<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: P53042
<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 170 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

<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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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