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UniProtKB - Q08209 (PP2BA_HUMAN)

Entry version 222 (23 Feb 2022)
Sequence version 1 (01 Feb 1996)
Previous versions | rss
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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).

Dephosphorylates transcription factor TFEB at 'Ser-211' following Coxsackievirus B3 infection, promoting nuclear translocation (PubMed:33691586).

By similarity11 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%5Fsection">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%5Fsection">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%5Fsection">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%5Fsection">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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.1.3.16, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q08209

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

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

More...SignaLinki		Q08209

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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000138814

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Synapse

<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 variants 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 PublicationCorresponds to variant dbSNP:rs199706529EnsemblClinVar.1
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 PublicationCorresponds to variant dbSNP:rs1553920374EnsemblClinVar.1
Arthrogryposis, cleft palate, craniosynostosis, and impaired intellectual development (ACCIID)1 Publication
The disease is caused by variants 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 PublicationCorresponds to variant dbSNP:rs1560567347EnsemblClinVar.1
Natural variantiVAR_081903473A → T in ACCIID. 1 PublicationCorresponds to variant dbSNP:rs1560567337EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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 variant, 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
565858, Craniosynostosis-microretrognathia-severe intellectual disability syndrome
442835, Non-specific early-onset epileptic encephalopathy

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33678

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q08209, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4445

Drug and drug target database

More...DrugBanki		DB08231, Myristic acid

DrugCentral

More...DrugCentrali		Q08209

Genetic variation 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%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_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 residuei2243'-nitrotyrosineBy 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

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		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: a multi-organism proteome resource

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

PTM databases

DEPOD human dephosphorylation database

More...DEPODi		PPP3CA

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q08209

MetOSite database of methionine sulfoxide sites

More...MetOSitei		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

<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 caudate nucleus and 254 other tissues

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		ENSG00000138814, Tissue enhanced (brain)

<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%5Fsection">'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%5Fsection">'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. 31, 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).

Interacts with UNC119 (By similarity).

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%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111522, 106 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, 60 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

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q08209, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1521
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q08209

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

More...SMRi		Q08209

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		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
Regioni475 – 521DisorderedSequence analysisAdd BLAST47

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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi493 – 521Polar residuesSequence analysisAdd BLAST29

<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

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156306

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_962966_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q08209

Identification of Orthologs from Complete Genome Data

More...OMAi		MESFCCL

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

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00069

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
IPR043360, PP2B
IPR006186, Ser/Thr-sp_prot-phosphatase

The PANTHER Classification System

More...PANTHERi		PTHR45673, PTHR45673, 1 hit

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

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56300, SSF56300, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 <p><strong>What is the canonical sequence?</strong><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:3 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>
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>
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 PublicationCorresponds to variant dbSNP:rs199706529EnsemblClinVar.1
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 PublicationCorresponds to variant dbSNP:rs1553920374EnsemblClinVar.1
Natural variantiVAR_081902470F → L in ACCIID. 1 PublicationCorresponds to variant dbSNP:rs1560567347EnsemblClinVar.1
Natural variantiVAR_081903473A → T in ACCIID. 1 PublicationCorresponds to variant dbSNP:rs1560567337EnsemblClinVar.1

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
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

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000394854.8; ENSP00000378323.3; NM_000944.5; NP_000935.1

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%5Freferences%5Fsection">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[»]
6NUCX-ray1.90A1-370[»]
6NUFX-ray1.90A1-370[»]
6NUUX-ray2.30A1-370[»]
6UUQX-ray1.85A26-339[»]
BMRBiQ08209
SMRiQ08209
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111522, 106 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, 60 interactors
MINTiQ08209
STRINGi9606.ENSP00000378323

Chemistry databases

BindingDBiQ08209
ChEMBLiCHEMBL4445
DrugBankiDB08231, Myristic acid
DrugCentraliQ08209

PTM databases

DEPODiPPP3CA
iPTMnetiQ08209
MetOSiteiQ08209
PhosphoSitePlusiQ08209
SwissPalmiQ08209

Genetic variation databases

BioMutaiPPP3CA
DMDMi1352673

Proteomic databases

EPDiQ08209
jPOSTiQ08209
MassIVEiQ08209
MaxQBiQ08209
PaxDbiQ08209
PeptideAtlasiQ08209
PRIDEiQ08209
ProteomicsDBi2488
58579 [Q08209-1]
58580 [Q08209-2]
58581 [Q08209-3]
88

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		2193, 592 antibodies from 44 providers

The DNASU plasmid repository

More...DNASUi		5530

Genome annotation databases

EnsembliENST00000323055; ENSP00000320580; ENSG00000138814 [Q08209-3]
ENST00000394853; ENSP00000378322; ENSG00000138814 [Q08209-2]
ENST00000394854; ENSP00000378323; ENSG00000138814
ENST00000512215; ENSP00000422781; ENSG00000138814 [Q08209-4]
GeneIDi5530
KEGGihsa:5530
MANE-SelectiENST00000394854.8; ENSP00000378323.3; NM_000944.5; NP_000935.1
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
HPAiENSG00000138814, Tissue enhanced (brain)
MalaCardsiPPP3CA
MIMi114105, gene
617711, phenotype
618265, phenotype
neXtProtiNX_Q08209
OpenTargetsiENSG00000138814
Orphaneti178469, Autosomal dominant non-syndromic intellectual disability
565858, Craniosynostosis-microretrognathia-severe intellectual disability syndrome
442835, Non-specific early-onset epileptic encephalopathy
PharmGKBiPA33678
VEuPathDBiHostDB:ENSG00000138814

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0375, Eukaryota
GeneTreeiENSGT00940000156306
HOGENOMiCLU_962966_0_0_1
InParanoidiQ08209
OMAiMESFCCL
PhylomeDBiQ08209
TreeFamiTF105557

Enzyme and pathway databases

BRENDAi3.1.3.16, 2681
PathwayCommonsiQ08209
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
SignaLinkiQ08209
SIGNORiQ08209

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5530, 3 hits in 1049 CRISPR screens

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
PharosiQ08209, Tchem

Protein Ontology

More...PROi		PR:Q08209
RNActiQ08209, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000138814, Expressed in caudate nucleus and 254 other tissues
ExpressionAtlasiQ08209, baseline and differential
GenevisibleiQ08209, HS

Family and domain databases

CDDicd07416, MPP_PP2B, 1 hit
DisProtiDP00092
Gene3Di3.60.21.10, 1 hit
IDEALiIID00069
InterProiView protein in InterPro
IPR004843, Calcineurin-like_PHP_ApaH
IPR029052, Metallo-depent_PP-like
IPR041751, MPP_PP2B
IPR043360, PP2B
IPR006186, Ser/Thr-sp_prot-phosphatase
PANTHERiPTHR45673, PTHR45673, 1 hit
PfamiView protein in Pfam
PF00149, Metallophos, 1 hit
PRINTSiPR00114, STPHPHTASE
SMARTiView protein in SMART
SM00156, PP2Ac, 1 hit
SUPFAMiSSF56300, SSF56300, 1 hit
PROSITEiView protein in PROSITE
PS00125, SER_THR_PHOSPHATASE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry 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%5Fand%5Fisoforms">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: February 23, 2022
This is version 222 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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