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UniProtKB - Q08209 (PP2BA_HUMAN)

Entry version 207 (31 Jul 2019)
Sequence version 1 (01 Feb 1996)
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Protein

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

Gene

PPP3CA

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:15671020, PubMed:18838687, PubMed:19154138, PubMed:23468591). Many of the substrates contain a PxIxIT motif and/or a LxVP motif (PubMed:17498738, PubMed:17502104, PubMed:23468591, PubMed:27974827, PubMed:22343722). In response to increased Ca2+ levels, dephosphorylates and activates phosphatase SSH1 which results in cofilin dephosphorylation (PubMed:15671020). In response to increased Ca2+ levels following mitochondrial depolarization, dephosphorylates DNM1L inducing DNM1L translocation to the mitochondrion (PubMed:18838687). Dephosphorylates heat shock protein HSPB1 (By similarity). Dephosphorylates and activates transcription factor NFATC1 (PubMed:19154138). In response to increased Ca2+ levels, regulates NFAT-mediated transcription probably by dephosphorylating NFAT and promoting its nuclear translocation (PubMed:26248042). Dephosphorylates and inactivates transcription factor ELK1 (PubMed:19154138). Dephosphorylates DARPP32 (PubMed:19154138). May dephosphorylate CRTC2 at 'Ser-171' resulting in CRTC2 dissociation from 14-3-3 proteins (PubMed:30611118).By similarity10 Publications

Miscellaneous

Although African swine fever virus infects pigs and not humans, human PPP3CA has been used for the crystallization. PPP3CA interacts with African swine fever virus Mal-047/A238L (via PKIIIT and FLCVK motifs); the interaction does not block catalytic activity per se but inhibits PPP3CA function by blocking the access to the two substrate recognition sites.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:

<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

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. Inhibited by immunosuppressant drug FK506 (tacrolimus) in complex with FKBP12 and also by immunosuppressant drug cyclosporin A (CsA) in complex with PPIA/cyclophilin A; the inhibition is Ca2+-dependent (PubMed:26248042).By similarity1 Publication

<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=2.04 µM for NFATC11 Publication
  2. KM=2.22 µM for DARPP321 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 bindingi90IronCombined sources6 Publications1
    Metal bindingi92Iron; via tele nitrogenCombined sources6 Publications1
    Metal bindingi118IronCombined sources6 Publications1
    Metal bindingi118ZincCombined sources6 Publications1
    Metal bindingi150ZincCombined sources6 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei151Proton donor1 Publication1
    Metal bindingi199Zinc; via tele nitrogenCombined sources6 Publications1
    Metal bindingi281Zinc; via pros nitrogenCombined sources6 Publications1

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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

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

    Molecular 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

    SIGNOR Signaling Network Open Resource

    More...    SIGNORi    		Q08209

    <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 alpha isoform (EC:3.1.3.161 Publication4 Publications)
    Alternative name(s):
    CAM-PRP catalytic subunit
    Calmodulin-dependent calcineurin A subunit alpha isoform
    <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:PPP3CAImported
    Synonyms:CALNA, CNA
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

    Organism-specific databases

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:9314 PPP3CA

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		114105 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_Q08209

    <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 & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Membrane

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Epileptic encephalopathy, infantile or early childhood, 1 (IECEE1)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. IECEE1 is an autosomal dominant condition with onset of seizures between the first weeks and first years of life.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_08034892H → R in IECEE1. 2 PublicationsCorresponds to variant dbSNP:rs1553925558EnsemblClinVar.1
    Natural variantiVAR_081900150N → I in IECEE1. 1 Publication1
    Natural variantiVAR_081901234D → E in IECEE1. 1 Publication1
    Natural variantiVAR_080349281H → Q in IECEE1. 1 Publication1
    Natural variantiVAR_080350282E → K in IECEE1. 1 PublicationCorresponds to variant dbSNP:rs1553923787EnsemblClinVar.1
    Natural variantiVAR_080351445 – 521Missing in IECEE1. 1 PublicationAdd BLAST77
    Natural variantiVAR_080352447A → T in IECEE1; unknown pathological significance. 1 Publication1
    Arthrogryposis, cleft palate, craniosynostosis, and impaired intellectual development (ACCIID)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn autosomal dominant disease characterized by moderate to severe intellectual disability, craniosynostosis, cleft palate, micrognathia, arthrogryposis, and short stature. Some patients may present bone abnormalities and generalized seizures.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_081902470F → L in ACCIID. 1 Publication1
    Natural variantiVAR_081903473A → T in ACCIID. 1 Publication1

    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>Mutagenesisi288Y → F: Partial loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with F-341. 1 Publication1
    Mutagenesisi288Y → N or A: Loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with F-341. 1 Publication1
    Mutagenesisi328 – 332Missing : Loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with F-341. 1 Publication5
    Mutagenesisi341Y → F: Resistant to cyclosporin A-mediated inhibition. Loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with N-288, A-228 or 328-V--R-332 DEL. Partial loss in Ca(2+)-mediated transcription factor NFAT activation; when associated with F-288. 1 Publication1

    Keywords - Diseasei

    Craniosynostosis, Disease mutation, Dwarfism, Epilepsy, Mental retardation

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		5530

    MalaCards human disease database

    More...    MalaCardsi    		PPP3CA
    MIMi617711 phenotype
    618265 phenotype

    Open Targets

    More...    OpenTargetsi    		ENSG00000138814

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...    Orphaneti    		178469 Autosomal dominant non-syndromic intellectual disability
    442835 Undetermined early-onset epileptic encephalopathy

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA33678

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL4445

    Drug and drug target database

    More...    DrugBanki    		DB08231 MYRISTIC ACID

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		PPP3CA

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		1352673

    <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_00000588222 – 521Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoformAdd BLAST520

    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-acetylserineCombined sources1
    Modified residuei224Nitrated tyrosineBy similarity1
    Modified residuei469PhosphoserineBy similarity1
    Modified residuei492PhosphoserineCombined sources1

    Keywords - PTMi

    Acetylation, Nitration, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		Q08209

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		Q08209

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		Q08209

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

    More...    PaxDbi    		Q08209

    PeptideAtlas

    More...    PeptideAtlasi    		Q08209

    PRoteomics IDEntifications database

    More...    PRIDEi    		Q08209

    ProteomicsDB human proteome resource

    More...    ProteomicsDBi    		2488
    58579 [Q08209-1]
    58580 [Q08209-2]
    58581 [Q08209-3]
    88

    PTM databases

    DEPOD human dephosphorylation database

    More...    DEPODi    		Q08209

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		Q08209

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

    More...    PhosphoSitePlusi    		Q08209

    SwissPalm database of S-palmitoylation events

    More...    SwissPalmi    		Q08209

    Miscellaneous databases

    CutDB - Proteolytic event database

    More...    PMAP-CutDBi    		Q08209

    <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

    Expressed in keratinocytes (at protein level).1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000138814 Expressed in 244 organ(s), highest expression level in caudate nucleus

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		Q08209 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		Q08209 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		CAB018581
    HPA012778

    <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) (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:27974827). 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 PPP3CA/calcineurin A, calcineurin B and calmodulin (By similarity).

    Interacts (via calcineurin B binding domain) with regulatory subunit PPP3R1/calcineurin B (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:27974827).

    Interacts (via calmodulin-binding domain) with CALM1/calmodulin; the interaction depends on calmodulin binding to Ca2+ (PubMed:18384083, Ref. 30, PubMed:19404396, PubMed:25144868).

    Forms a complex composed of MYOZ2 and ACTN1 (By similarity). Within the complex interacts with MYOZ2 (PubMed:11114196).

    Interacts with MYOZ1 (PubMed:11114196).

    Interacts with MYOZ3 (PubMed:11842093).

    Interacts with CIB1; the interaction increases upon cardiomyocyte hypertrophy (By similarity).

    Interacts with CHP1 and CHP2 (By similarity).

    Interacts with CRTC1 (PubMed:30611118).

    Interacts with CRTC2 (PubMed:15454081, PubMed:30611118).

    Interacts with DNM1L; the interaction dephosphorylates DNM1L and promotes its translocation to mitochondria (PubMed:18838687).

    Interacts with CMYA5; this interaction represses calcineurin activity in muscle (By similarity).

    Interacts (constitutively active form) with SYNPO2 (PubMed:17923693).

    Interacts with scaffold protein AKAP5 (via IAIIIT motif); the interaction recruits PPP3CA to the plasma membrane following L-type Ca2+-channel activation (PubMed:22343722).

    Interacts with NFATC2 (PubMed:26248042).

    Interacts with RCAN3 (PubMed:26248042).

    Interacts with PPIA (PubMed:12218175, PubMed:12357034).

    Interacts with RCAN1 (PubMed:12809556).

    By similarity19 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei352Interaction with PxVP motif in substrate2 Publications1

    <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

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		111522, 71 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...    ComplexPortali    		CPX-1003 Calcineurin-Calmodulin complex, alpha-R1 variant
    CPX-1048 Calcineurin-Calmodulin complex, alpha-R2 variant
    CPX-1114 Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant
    CPX-674 Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant

    CORUM comprehensive resource of mammalian protein complexes

    More...    CORUMi    		Q08209

    Database of interacting proteins

    More...    DIPi    		DIP-6095N

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...    ELMi    		Q08209

    Protein interaction database and analysis system

    More...    IntActi    		Q08209, 31 interactors

    Molecular INTeraction database

    More...    MINTi    		Q08209

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000378323

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		Q08209

    <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

    1521
    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

    More...    SMRi    		Q08209

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		Q08209

    <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>Regioni56 – 340CatalyticCuratedAdd BLAST285
    Regioni327 – 336Interaction with PxIxIF motif in substrate5 Publications10
    Regioni341 – 369Calcineurin B binding6 PublicationsAdd BLAST29
    Regioni392 – 406Calmodulin-binding4 PublicationsAdd BLAST15
    Regioni407 – 414Autoinhibitory segmentBy similarity8
    Regioni465 – 487Autoinhibitory 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>Motifi307 – 311SAPNY motif1 Publication5

    <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 autoinhibitory domain prevents access to the catalytic site.By similarity
    The autoinhibitory segment prevents access to the substrate binding site.By similarity
    Possible isomerization of Pro-309 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.1 Publication

    <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    		ENSGT00940000156306

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000172699

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		Q08209

    KEGG Orthology (KO)

    More...    KOi    		K04348

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		LWSLKIW

    Database of Orthologous Groups

    More...    OrthoDBi    		463522at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		Q08209

    TreeFam database of animal gene trees

    More...    TreeFami    		TF105557

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd07416 MPP_PP2B, 1 hit

    Database of protein disorder

    More...    DisProti    		DP00092

    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
    IPR041751 MPP_PP2B
    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>. 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>Sequences (5+)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 5 <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

    This entry has 5 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q08209-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL 
            60         70         80         90        100
    MKEGRLEESV ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK 
           110        120        130        140        150
    LFEVGGSPAN TRYLFLGDYV DRGYFSIECV LYLWALKILY PKTLFLLRGN 
           160        170        180        190        200
    HECRHLTEYF TFKQECKIKY SERVYDACMD AFDCLPLAAL MNQQFLCVHG 
           210        220        230        240        250
    GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG NEKTQEHFTH 
           260        270        280        290        300
    NTVRGCSYFY SYPAVCEFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP 
           310        320        330        340        350
    SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF 
           360        370        380        390        400
    TWSLPFVGEK VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI 
           410        420        430        440        450
    RAIGKMARVF SVLREESESV LTLKGLTPTG MLPSGVLSGG KQTLQSATVE 
           460        470        480        490        500
    AIEADEAIKG FSPQHKITSF EEAKGLDRIN ERMPPRRDAM PSDANLNSIN 
           510        520 
    KALTSETNGT DSNGSNSSNI Q
    Length:521
    Mass (Da):58,688
    Last modified:February 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:i16480D62DDBF1F40
    GO
    Isoform 2 (identifier: Q08209-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         448-457: Missing.

    Show »
    Length:511
    Mass (Da):57,659
    Checksum:iB1E98CC0D6034CCC
    GO
    Isoform 3 (identifier: Q08209-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         318-359: Missing.
         448-457: Missing.

    Show »
    Length:469
    Mass (Da):52,672
    Checksum:iA3365471746633B7
    GO
    Isoform 4 (identifier: Q08209-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         87-318: Missing.

    Show »
    Length:289
    Mass (Da):31,736
    Checksum:iB3AEE20F6A4F19B7
    GO
    Isoform 5 (identifier: Q08209-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         20-86: Missing.

    Show »
    Length:454
    Mass (Da):51,245
    Checksum:iE28DCB758984D380
    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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    E7ETC2E7ETC2_HUMAN
    Serine/threonine-protein phosphatas...
    PPP3CA
    		423Annotation 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>
    E9PPC8E9PPC8_HUMAN
    Serine/threonine-protein phosphatas...
    PPP3CA
    		132Annotation 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>
    E9PK68E9PK68_HUMAN
    Serine/threonine-protein phosphatas...
    PPP3CA
    		147Annotation 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>
    H0YAB4H0YAB4_HUMAN
    Serine/threonine-protein phosphatas...
    PPP3CA
    		16Annotation 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>

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_08034892H → R in IECEE1. 2 PublicationsCorresponds to variant dbSNP:rs1553925558EnsemblClinVar.1
    Natural variantiVAR_081900150N → I in IECEE1. 1 Publication1
    Natural variantiVAR_081901234D → E in IECEE1. 1 Publication1
    Natural variantiVAR_080349281H → Q in IECEE1. 1 Publication1
    Natural variantiVAR_080350282E → K in IECEE1. 1 PublicationCorresponds to variant dbSNP:rs1553923787EnsemblClinVar.1
    Natural variantiVAR_080351445 – 521Missing in IECEE1. 1 PublicationAdd BLAST77
    Natural variantiVAR_080352447A → T in IECEE1; unknown pathological significance. 1 Publication1
    Natural variantiVAR_081902470F → L in ACCIID. 1 Publication1
    Natural variantiVAR_081903473A → T in ACCIID. 1 Publication1

    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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_05446720 – 86Missing in isoform 5. 1 PublicationAdd BLAST67
    Alternative sequenceiVSP_04775587 – 318Missing in isoform 4. 1 PublicationAdd BLAST232
    Alternative sequenceiVSP_043378318 – 359Missing in isoform 3. 1 PublicationAdd BLAST42
    Alternative sequenceiVSP_018562448 – 457Missing in isoform 2 and isoform 3. 3 Publications10

    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
    		L14778 mRNA Translation: AAA02631.1
    EU192652 mRNA Translation: ABW74484.1
    EU192653 mRNA Translation: ABW74485.1
    AY904364 mRNA Translation: AAY17314.1
    AK290532 mRNA Translation: BAF83221.1
    AL353950 mRNA Translation: CAB89253.1
    AB451338 mRNA Translation: BAG70152.1
    AB451487 mRNA Translation: BAG70301.1
    AC092671 Genomic DNA No translation available.
    AP001816 Genomic DNA No translation available.
    AP001870 Genomic DNA No translation available.
    AP001939 Genomic DNA No translation available.
    CH471057 Genomic DNA Translation: EAX06125.1
    CH471057 Genomic DNA Translation: EAX06124.1
    BC025714 mRNA Translation: AAH25714.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS34037.1 [Q08209-1]
    CCDS47113.1 [Q08209-3]
    CCDS47114.1 [Q08209-2]

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S35067

    NCBI Reference Sequences

    More...    RefSeqi    		NP_000935.1, NM_000944.4 [Q08209-1]
    NP_001124163.1, NM_001130691.1 [Q08209-2]
    NP_001124164.1, NM_001130692.1 [Q08209-3]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000323055; ENSP00000320580; ENSG00000138814 [Q08209-3]
    ENST00000394853; ENSP00000378322; ENSG00000138814 [Q08209-2]
    ENST00000394854; ENSP00000378323; ENSG00000138814 [Q08209-1]
    ENST00000512215; ENSP00000422781; ENSG00000138814 [Q08209-4]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		5530

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:5530

    UCSC genome browser

    More...    UCSCi    		uc003hvu.3 human [Q08209-1]

    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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Wikipedia

    Calcineurin entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		L14778 mRNA Translation: AAA02631.1
    EU192652 mRNA Translation: ABW74484.1
    EU192653 mRNA Translation: ABW74485.1
    AY904364 mRNA Translation: AAY17314.1
    AK290532 mRNA Translation: BAF83221.1
    AL353950 mRNA Translation: CAB89253.1
    AB451338 mRNA Translation: BAG70152.1
    AB451487 mRNA Translation: BAG70301.1
    AC092671 Genomic DNA No translation available.
    AP001816 Genomic DNA No translation available.
    AP001870 Genomic DNA No translation available.
    AP001939 Genomic DNA No translation available.
    CH471057 Genomic DNA Translation: EAX06125.1
    CH471057 Genomic DNA Translation: EAX06124.1
    BC025714 mRNA Translation: AAH25714.1
    CCDSiCCDS34037.1 [Q08209-1]
    CCDS47113.1 [Q08209-3]
    CCDS47114.1 [Q08209-2]
    PIRiS35067
    RefSeqiNP_000935.1, NM_000944.4 [Q08209-1]
    NP_001124163.1, NM_001130691.1 [Q08209-2]
    NP_001124164.1, NM_001130692.1 [Q08209-3]

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1AUIX-ray2.10A1-521[»]
    1M63X-ray2.80A/E1-372[»]
    1MF8X-ray3.10A20-392[»]
    2JOGNMR-A21-347[»]
    2JZINMR-B391-414[»]
    2P6BX-ray2.30A/C1-380[»]
    2R28X-ray1.86C/D389-413[»]
    2W73X-ray1.45K/L/M/O395-411[»]
    3LL8X-ray2.00A/C14-370[»]
    4F0ZX-ray1.70A1-370[»]
    4Q5UX-ray1.95C391-414[»]
    5C1VX-ray3.35A/B2-346[»]
    5SVEX-ray2.60A1-370[»]
    SMRiQ08209
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi111522, 71 interactors
    ComplexPortaliCPX-1003 Calcineurin-Calmodulin complex, alpha-R1 variant
    CPX-1048 Calcineurin-Calmodulin complex, alpha-R2 variant
    CPX-1114 Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant
    CPX-674 Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant
    CORUMiQ08209
    DIPiDIP-6095N
    ELMiQ08209
    IntActiQ08209, 31 interactors
    MINTiQ08209
    STRINGi9606.ENSP00000378323

    Chemistry databases

    BindingDBiQ08209
    ChEMBLiCHEMBL4445
    DrugBankiDB08231 MYRISTIC ACID

    PTM databases

    DEPODiQ08209
    iPTMnetiQ08209
    PhosphoSitePlusiQ08209
    SwissPalmiQ08209

    Polymorphism and mutation databases

    BioMutaiPPP3CA
    DMDMi1352673

    Proteomic databases

    EPDiQ08209
    jPOSTiQ08209
    MaxQBiQ08209
    PaxDbiQ08209
    PeptideAtlasiQ08209
    PRIDEiQ08209
    ProteomicsDBi2488
    58579 [Q08209-1]
    58580 [Q08209-2]
    58581 [Q08209-3]
    88

    Protocols and materials databases

    The DNASU plasmid repository

    More...    DNASUi    		5530
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000323055; ENSP00000320580; ENSG00000138814 [Q08209-3]
    ENST00000394853; ENSP00000378322; ENSG00000138814 [Q08209-2]
    ENST00000394854; ENSP00000378323; ENSG00000138814 [Q08209-1]
    ENST00000512215; ENSP00000422781; ENSG00000138814 [Q08209-4]
    GeneIDi5530
    KEGGihsa:5530
    UCSCiuc003hvu.3 human [Q08209-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		5530
    DisGeNETi5530

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		PPP3CA
    HGNCiHGNC:9314 PPP3CA
    HPAiCAB018581
    HPA012778
    MalaCardsiPPP3CA
    MIMi114105 gene
    617711 phenotype
    618265 phenotype
    neXtProtiNX_Q08209
    OpenTargetsiENSG00000138814
    Orphaneti178469 Autosomal dominant non-syndromic intellectual disability
    442835 Undetermined early-onset epileptic encephalopathy
    PharmGKBiPA33678

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG0375 Eukaryota
    COG0639 LUCA
    GeneTreeiENSGT00940000156306
    HOGENOMiHOG000172699
    InParanoidiQ08209
    KOiK04348
    OMAiLWSLKIW
    OrthoDBi463522at2759
    PhylomeDBiQ08209
    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
    SIGNORiQ08209

    Miscellaneous databases

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

    More...    ChiTaRSi    		PPP3CA human
    EvolutionaryTraceiQ08209

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		PPP3CA

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

    More...    GenomeRNAii    		5530
    PMAP-CutDBiQ08209

    Protein Ontology

    More...    PROi    		PR:Q08209

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000138814 Expressed in 244 organ(s), highest expression level in caudate nucleus
    ExpressionAtlasiQ08209 baseline and differential
    GenevisibleiQ08209 HS

    Family and domain databases

    CDDicd07416 MPP_PP2B, 1 hit
    DisProtiDP00092
    Gene3Di3.60.21.10, 1 hit
    InterProiView protein in InterPro
    IPR004843 Calcineurin-like_PHP_ApaH
    IPR029052 Metallo-depent_PP-like
    IPR041751 MPP_PP2B
    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...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

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

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPP2BA_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: Q08209
    Secondary accession number(s): A1A441
    , A8K3B7, A8W6Z7, A8W6Z8, B5BUA2, Q8TAW9
    <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: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: July 31, 2019
    This is version 207 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 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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