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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform

Gene

PPP3CB

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

Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca2+-mediated signals (PubMed:19154138, PubMed:26794871). Dephosphorylates and activates transcription factor NFATC1 (PubMed:19154138). Dephosphorylates and inactivates transcription factor ELK1 (PubMed:19154138). Dephosphorylates DARPP32 (PubMed:19154138).2 Publications

Miscellaneous

Unlike for protein substrates, PPP3CB activity towards synthetic phosphatase substrate p-nitrophenyl phosphate (pNPP) is increased in presence of the immunosuppressant complex FKBP12-FK506.1 Publication

<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

Protein has several cofactor binding sites:
  • Fe3+1 PublicationNote: Binds 1 Fe3+ ion per subunit.1 Publication
  • Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

<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

Activated by Ca2+-bound calmodulin following an increase in intracellular Ca2+. At low Ca2+ concentrations, the catalytic subunit (also known as calcineurin A) is inactive and is bound to the regulatory subunit (also known as calcineurin B) in which only two high-affinity binding sites are occupied by Ca2+. In response to elevated calcium levels, the occupancy of the low-affinity sites on calcineurin B by Ca2+ causes a conformational change of the C-terminal regulatory domain of calcineurin A, resulting in the exposure of the calmodulin-binding domain and in the partial activation of calcineurin A. The subsequent binding of Ca2+-bound calmodulin leads to the displacement of the autoinhibitory domain from the active site and possibly of the autoinhibitory segment from the substrate binding site which fully activates calcineurin A.2 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=0.69 µM for NFATC11 Publication
  2. KM=0.7 µM for DARPP321 Publication

    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 bindingi99IronCombined sources1 Publication1
    Metal bindingi101Iron; via tele nitrogenCombined sources1 Publication1
    Metal bindingi127IronCombined sources1 Publication1
    Metal bindingi127ZincCombined sources1 Publication1
    Metal bindingi159ZincCombined sources1 Publication1
    <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 sitei160Proton donorBy similarity1
    Metal bindingi208Zinc; via tele nitrogenCombined sources1 Publication1
    Metal bindingi290Zinc; via pros nitrogenCombined sources1 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

    • calcium ion binding Source: UniProtKB
    • calmodulin binding Source: UniProtKB
    • calmodulin-dependent protein phosphatase activity Source: UniProtKB
    • drug binding Source: UniProtKB
    • enzyme binding Source: UniProtKB
    • protein dimerization activity Source: UniProtKB
    • protein phosphatase 2B binding Source: UniProtKB
    • protein serine/threonine phosphatase activity Source: UniProtKB

    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 functionCalmodulin-binding, Hydrolase, Protein phosphatase
    LigandIron, Metal-binding, Zinc

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-180024 DARPP-32 events
    R-HSA-2025928 Calcineurin activates NFAT
    R-HSA-2871809 FCERI mediated Ca+2 mobilization
    R-HSA-4086398 Ca2+ pathway
    R-HSA-5607763 CLEC7A (Dectin-1) induces NFAT activation
    R-HSA-9010642 ROBO receptors bind AKAP5

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P16298

    <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 2B catalytic subunit beta isoform (EC:3.1.3.162 Publications)
    Alternative name(s):
    CAM-PRP catalytic subunit
    Calmodulin-dependent calcineurin A subunit beta isoform
    Short name:
    CNA beta1 Publication
    <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:PPP3CB
    Synonyms:CALNA2, CALNB, CNA2
    <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 10

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000107758.15

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:9315 PPP3CB

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    114106 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P16298

    <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

    Cytoplasm

    <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>Mutagenesisi2 – 21Missing : Increases catalytic efficiency towards NFATC1 and DARPP32 but not towards a peptide substrate. Does not affect cytoplasmic localization and activation by calmodulin. 1 PublicationAdd BLAST20
    Mutagenesisi352L → A: Severe loss of calmodulin-mediated activation. Probably prevents recognition of substrates. 1 Publication1
    Mutagenesisi353P → A: Reduction of basal catalytic activity in absence of calmodulin. 1 Publication1
    Mutagenesisi356M → A: Modest increase in catalytic activity in absence of calmodulin. 1 Publication1
    Mutagenesisi357 – 524Missing : Loss of catalytic activity. Loss of interaction with PPP3R1/calreticulin B and calmodulin. 1 PublicationAdd BLAST168
    Mutagenesisi361W → A: Severe reduction of basal catalytic activity in absence of calmodulin. Severe loss of calmodulin-mediated activation. Probably prevents recognition of substrates. 1 Publication1
    Mutagenesisi365F → A: Moderate loss of calmodulin-mediated activation. Probably prevents recognition of substrates. 1 Publication1
    Mutagenesisi398 – 524Missing : Increases catalytic activity independently of calmodulin. Loss of interaction with calmodulin. Does not affect interaction with PPP3R1/calreticulin B. 1 PublicationAdd BLAST127
    Mutagenesisi415 – 524Missing : Increases catalytic activity independently of calmodulin. Does not affect interaction with PPP3R1/calreticulin B and calmodulin. 1 PublicationAdd BLAST110
    Mutagenesisi417R → A: Modest increase in catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
    Mutagenesisi418V → A: Does not affect catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
    Mutagenesisi419F → A: Modest increase in catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
    Mutagenesisi420S → A: Does not affect catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
    Mutagenesisi421V → A: Modest increase in catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
    Mutagenesisi422L → A: Modest increase in catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
    Mutagenesisi423R → A: Modest increase in catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
    Mutagenesisi451 – 524Missing : Increases basal catalytic activity. Does not affect interaction with PPP3R1/calreticulin B and calmodulin. 1 PublicationAdd BLAST74

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    5532

    Open Targets

    More...
    OpenTargetsi
    ENSG00000107758

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA33679

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5278

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    PPP3CB

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    60659599

    <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_00000588252 – 524Serine/threonine-protein phosphatase 2B catalytic subunit beta isoformAdd BLAST523

    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
    Modified residuei478PhosphoserineBy similarity1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P16298

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P16298

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

    More...
    PaxDbi
    P16298

    PeptideAtlas

    More...
    PeptideAtlasi
    P16298

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P16298

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    53341
    53342 [P16298-2]
    53343 [P16298-3]
    53344 [P16298-4]

    PTM databases

    DEPOD human dephosphorylation database

    More...
    DEPODi
    P16298

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P16298

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

    More...
    PhosphoSitePlusi
    P16298

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P16298

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

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000107758 Expressed in 242 organ(s), highest expression level in frontal cortex

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_PPP3CB

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P16298 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P16298 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA008233
    HPA008823

    <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

    Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca2+-binding subunit (also known as calcineurin B). There are three catalytic subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded by separate genes (PPP3R1 and PPP3R2). In response to an increase in Ca2+ intracellular levels, forms a complex composed of PPP3CB/calcineurin A, calcineurin B and calmodulin. Interacts (via calcineurin B binding domain) with regulatory subunit PPP3R1/calcineurin B. Interacts (via calmodulin-binding domain) with calmodulin; the interaction depends on calmodulin binding to Ca2+.1 Publication

    <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
    111524, 50 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-1002 Calcineurin-Calmodulin complex, beta-R2 variant
    CPX-1009 Calcineurin-Calmodulin complex, beta-R1 variant
    CPX-1116 Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant
    CPX-998 Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    P16298

    Database of interacting proteins

    More...
    DIPi
    DIP-52337N

    Protein interaction database and analysis system

    More...
    IntActi
    P16298, 15 interactors

    Molecular INTeraction database

    More...
    MINTi
    P16298

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000378306

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P16298

    <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

    1524
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P16298

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

    More...
    SMRi
    P16298

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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

    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>Regioni65 – 356CatalyticCuratedAdd BLAST292
    Regioni357 – 379Calcineurin B binding1 PublicationAdd BLAST23
    Regioni401 – 415Calmodulin-binding1 PublicationAdd BLAST15
    Regioni416 – 423Autoinhibitory segment1 Publication8
    Regioni474 – 496Autoinhibitory domain1 PublicationAdd BLAST23

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi316 – 320SAPNY motifBy 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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi11 – 21Poly-ProSequence analysisAdd BLAST11

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The poly-Pro domain may confer substrate specificity.1 Publication
    The autoinhibitory domain prevents access to the catalytic site.1 Publication
    The autoinhibitory segment prevents access to the substrate binding site.1 Publication
    Possible isomerization of Pro-318 within the SAPNY motif triggers a conformation switch which affects the organization and thus accessibility of the active site and the substrate binding region (PxIxIF motif). The trans- to cis-transition may favor calcineurin A activation and substrate binding. The reverse cis- to trans-transition may be enhanced by peptidyl-prolyl isomerases such as PPIA.By similarity

    <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-2B subfamily.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0375 Eukaryota
    COG0639 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000154115

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000172699

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG002819

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P16298

    KEGG Orthology (KO)

    More...
    KOi
    K04348

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    QFDVKVG

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G094R

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF105557

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    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
    IPR006186 Ser/Thr-sp_prot-phosphatase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00149 Metallophos, 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

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00125 SER_THR_PHOSPHATASE, 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>Sequences (4+)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 describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
    Note: Additional isoforms seem to exist. Calcineurin A beta isoform consists of at least two isoenzymes that may result from alternative splicing events.

    This entry has 4 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P16298-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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    MAAPEPARAA PPPPPPPPPP PGADRVVKAV PFPPTHRLTS EEVFDLDGIP
    60 70 80 90 100
    RVDVLKNHLV KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI
    110 120 130 140 150
    HGQFFDLMKL FEVGGSPANT RYLFLGDYVD RGYFSIECVL YLWVLKILYP
    160 170 180 190 200
    STLFLLRGNH ECRHLTEYFT FKQECKIKYS ERVYEACMEA FDSLPLAALL
    210 220 230 240 250
    NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL WSDPSEDFGN
    260 270 280 290 300
    EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY
    310 320 330 340 350
    RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY
    360 370 380 390 400
    WLPNFMDVFT WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDGSAAA
    410 420 430 440 450
    RKEIIRNKIR AIGKMARVFS VLREESESVL TLKGLTPTGM LPSGVLAGGR
    460 470 480 490 500
    QTLQSATVEA IEAEKAIRGF SPPHRICSFE EAKGLDRINE RMPPRKDAVQ
    510 520
    QDGFNSLNTA HATENHGTGN HTAQ
    Length:524
    Mass (Da):59,024
    Last modified:February 1, 2005 - v2
    <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:i7661183F3C2362C8
    GO
    Isoform 2 (identifier: P16298-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         137-137: E → EHVLGTEDISINPHNNINE
         456-524: ATVEAIEAEK...NHGTGNHTAQ → GNDVMQLAVP...LLFFSSCLSS

    Show »
    Length:514
    Mass (Da):58,013
    Checksum:i1B0BFA63FB98E06D
    GO
    Isoform 3 (identifier: P16298-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         395-395: D → DV
         456-465: Missing.

    Show »
    Length:515
    Mass (Da):58,081
    Checksum:iA6762D9468A09B51
    GO
    Isoform 4 (identifier: P16298-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         395-395: D → DV

    Note: No experimental confirmation available.
    Show »
    Length:525
    Mass (Da):59,123
    Checksum:iADB0ECB75371B574
    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
    Q5F2F8Q5F2F8_HUMAN
    Serine/threonine-protein phosphatas...
    PPP3CB hCG_18332
    496Annotation 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>
    Q5F2G0Q5F2G0_HUMAN
    Serine/threonine-protein phosphatas...
    PPP3CB
    187Annotation score:

    Annotation score:1 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>

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005096137E → EHVLGTEDISINPHNNINE in isoform 2. 1 Publication1
    Alternative sequenceiVSP_043803395D → DV in isoform 3 and isoform 4. 2 Publications1
    Alternative sequenceiVSP_005097456 – 524ATVEA…NHTAQ → GNDVMQLAVPQMDWGTPHSF ANNSHNACREFLLFFSSCLS S in isoform 2. 1 PublicationAdd BLAST69
    Alternative sequenceiVSP_012617456 – 465Missing in isoform 3. 1 Publication10

    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
    M29551 mRNA Translation: AAA35706.1
    M29550 mRNA Translation: AAA35705.1
    AJ488506 mRNA Translation: CAD32694.1
    AL353731 Genomic DNA No translation available.
    AL359074 Genomic DNA No translation available.
    CH471083 Genomic DNA Translation: EAW54497.1
    CH471083 Genomic DNA Translation: EAW54498.1
    BC028049 mRNA Translation: AAH28049.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS44436.1 [P16298-3]
    CCDS44437.1 [P16298-4]
    CCDS7328.1 [P16298-1]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A36222
    B36222

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001135825.1, NM_001142353.2 [P16298-4]
    NP_001135826.1, NM_001142354.2 [P16298-3]
    NP_001276897.1, NM_001289968.1 [P16298-2]
    NP_001276898.1, NM_001289969.1
    NP_066955.1, NM_021132.3 [P16298-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.500067

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000360663; ENSP00000353881; ENSG00000107758 [P16298-1]
    ENST00000394828; ENSP00000378305; ENSG00000107758 [P16298-3]
    ENST00000394829; ENSP00000378306; ENSG00000107758 [P16298-4]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    5532

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:5532

    UCSC genome browser

    More...
    UCSCi
    uc001jue.4 human [P16298-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <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
    M29551 mRNA Translation: AAA35706.1
    M29550 mRNA Translation: AAA35705.1
    AJ488506 mRNA Translation: CAD32694.1
    AL353731 Genomic DNA No translation available.
    AL359074 Genomic DNA No translation available.
    CH471083 Genomic DNA Translation: EAW54497.1
    CH471083 Genomic DNA Translation: EAW54498.1
    BC028049 mRNA Translation: AAH28049.1
    CCDSiCCDS44436.1 [P16298-3]
    CCDS44437.1 [P16298-4]
    CCDS7328.1 [P16298-1]
    PIRiA36222
    B36222
    RefSeqiNP_001135825.1, NM_001142353.2 [P16298-4]
    NP_001135826.1, NM_001142354.2 [P16298-3]
    NP_001276897.1, NM_001289968.1 [P16298-2]
    NP_001276898.1, NM_001289969.1
    NP_066955.1, NM_021132.3 [P16298-1]
    UniGeneiHs.500067

    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
    4OR9X-ray2.23A1-524[»]
    4ORAX-ray2.75A1-524[»]
    4ORCX-ray2.70A1-524[»]
    ProteinModelPortaliP16298
    SMRiP16298
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111524, 50 interactors
    ComplexPortaliCPX-1002 Calcineurin-Calmodulin complex, beta-R2 variant
    CPX-1009 Calcineurin-Calmodulin complex, beta-R1 variant
    CPX-1116 Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant
    CPX-998 Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant
    CORUMiP16298
    DIPiDIP-52337N
    IntActiP16298, 15 interactors
    MINTiP16298
    STRINGi9606.ENSP00000378306

    Chemistry databases

    BindingDBiP16298
    ChEMBLiCHEMBL5278

    PTM databases

    DEPODiP16298
    iPTMnetiP16298
    PhosphoSitePlusiP16298
    SwissPalmiP16298

    Polymorphism and mutation databases

    BioMutaiPPP3CB
    DMDMi60659599

    Proteomic databases

    EPDiP16298
    MaxQBiP16298
    PaxDbiP16298
    PeptideAtlasiP16298
    PRIDEiP16298
    ProteomicsDBi53341
    53342 [P16298-2]
    53343 [P16298-3]
    53344 [P16298-4]

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    5532
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000360663; ENSP00000353881; ENSG00000107758 [P16298-1]
    ENST00000394828; ENSP00000378305; ENSG00000107758 [P16298-3]
    ENST00000394829; ENSP00000378306; ENSG00000107758 [P16298-4]
    GeneIDi5532
    KEGGihsa:5532
    UCSCiuc001jue.4 human [P16298-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    5532
    DisGeNETi5532
    EuPathDBiHostDB:ENSG00000107758.15

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    PPP3CB
    HGNCiHGNC:9315 PPP3CB
    HPAiHPA008233
    HPA008823
    MIMi114106 gene
    neXtProtiNX_P16298
    OpenTargetsiENSG00000107758
    PharmGKBiPA33679

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0375 Eukaryota
    COG0639 LUCA
    GeneTreeiENSGT00940000154115
    HOGENOMiHOG000172699
    HOVERGENiHBG002819
    InParanoidiP16298
    KOiK04348
    OMAiQFDVKVG
    OrthoDBiEOG091G094R
    TreeFamiTF105557

    Enzyme and pathway databases

    ReactomeiR-HSA-180024 DARPP-32 events
    R-HSA-2025928 Calcineurin activates NFAT
    R-HSA-2871809 FCERI mediated Ca+2 mobilization
    R-HSA-4086398 Ca2+ pathway
    R-HSA-5607763 CLEC7A (Dectin-1) induces NFAT activation
    R-HSA-9010642 ROBO receptors bind AKAP5
    SIGNORiP16298

    Miscellaneous databases

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

    More...
    ChiTaRSi
    PPP3CB human

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    PPP3CB

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

    More...
    GenomeRNAii
    5532

    Protein Ontology

    More...
    PROi
    PR:P16298

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000107758 Expressed in 242 organ(s), highest expression level in frontal cortex
    CleanExiHS_PPP3CB
    ExpressionAtlasiP16298 baseline and differential
    GenevisibleiP16298 HS

    Family and domain databases

    Gene3Di3.60.21.10, 1 hit
    InterProiView protein in InterPro
    IPR004843 Calcineurin-like_PHP_ApaH
    IPR029052 Metallo-depent_PP-like
    IPR006186 Ser/Thr-sp_prot-phosphatase
    PfamiView protein in Pfam
    PF00149 Metallophos, 1 hit
    PRINTSiPR00114 STPHPHTASE
    SMARTiView protein in SMART
    SM00156 PP2Ac, 1 hit
    PROSITEiView protein in PROSITE
    PS00125 SER_THR_PHOSPHATASE, 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 nameiPP2BB_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: P16298
    Secondary accession number(s): P16299
    , Q5F2F9, Q8N1F0, Q8N3W4
    <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: August 1, 1990
    Last sequence update: February 1, 2005
    Last modified: December 5, 2018
    This is version 159 of the entry and version 2 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 10
      Human chromosome 10: 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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