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Entry version 177 (29 Sep 2021)
Sequence version 2 (01 Feb 2005)
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Protein

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

Gene

PPP3CB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca2+-mediated signals (PubMed:19154138, PubMed:26794871).

Dephosphorylates and activates transcription factor NFATC1 (PubMed:19154138).

Dephosphorylates and inactivates transcription factor ELK1 (PubMed:19154138).

Dephosphorylates DARPP32 (PubMed:19154138).

2 Publications

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the <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.2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.69 µM for NFATC11 Publication
  2. KM=0.7 µM for DARPP321 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <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 bindingi99IronCombined sources1 Publication1
Metal bindingi101Iron; via tele nitrogenCombined sources1 Publication1
Metal bindingi127IronCombined sources1 Publication1
Metal bindingi127ZincCombined sources1 Publication1
Metal bindingi159ZincCombined sources1 Publication1
<p>This subsection of the <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 sitei160Proton donorBy similarity1
Metal bindingi208Zinc; via tele nitrogenCombined sources1 Publication1
Metal bindingi290Zinc; via pros nitrogenCombined sources1 Publication1

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

GO - Biological processi

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

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

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
P16298

Reactome - a knowledgebase of biological pathways and processes

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

SIGNOR Signaling Network Open Resource

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SIGNORi
P16298

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (EC:3.1.3.162 Publications)
Alternative name(s):
CAM-PRP catalytic subunit
Calmodulin-dependent calcineurin A subunit beta isoform
Short name:
CNA beta1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PPP3CB
Synonyms:CALNA2, CALNB, CNA2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:9315, PPP3CB

Online Mendelian Inheritance in Man (OMIM)

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MIMi
114106, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P16298

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000107758

<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

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2 – 21Missing : Increases catalytic efficiency towards NFATC1 and DARPP32 but not towards a peptide substrate. Does not affect cytoplasmic localization and activation by calmodulin. 1 PublicationAdd BLAST20
Mutagenesisi352L → A: Severe loss of calmodulin-mediated activation. Probably prevents recognition of substrates. 1 Publication1
Mutagenesisi353P → A: Reduction of basal catalytic activity in absence of calmodulin. 1 Publication1
Mutagenesisi356M → A: Modest increase in catalytic activity in absence of calmodulin. 1 Publication1
Mutagenesisi357 – 524Missing : Loss of catalytic activity. Loss of interaction with PPP3R1/calreticulin B and calmodulin. 1 PublicationAdd BLAST168
Mutagenesisi361W → A: Severe reduction of basal catalytic activity in absence of calmodulin. Severe loss of calmodulin-mediated activation. Probably prevents recognition of substrates. 1 Publication1
Mutagenesisi365F → A: Moderate loss of calmodulin-mediated activation. Probably prevents recognition of substrates. 1 Publication1
Mutagenesisi398 – 524Missing : Increases catalytic activity independently of calmodulin. Loss of interaction with calmodulin. Does not affect interaction with PPP3R1/calreticulin B. 1 PublicationAdd BLAST127
Mutagenesisi415 – 524Missing : Increases catalytic activity independently of calmodulin. Does not affect interaction with PPP3R1/calreticulin B and calmodulin. 1 PublicationAdd BLAST110
Mutagenesisi417R → A: Modest increase in catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
Mutagenesisi418V → A: Does not affect catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
Mutagenesisi419F → A: Modest increase in catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
Mutagenesisi420S → A: Does not affect catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
Mutagenesisi421V → A: Modest increase in catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
Mutagenesisi422L → A: Modest increase in catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
Mutagenesisi423R → A: Modest increase in catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin. 1 Publication1
Mutagenesisi451 – 524Missing : Increases basal catalytic activity. Does not affect interaction with PPP3R1/calreticulin B and calmodulin. 1 PublicationAdd BLAST74

Organism-specific databases

DisGeNET

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DisGeNETi
5532

Open Targets

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OpenTargetsi
ENSG00000107758

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33679

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P16298, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5278

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PPP3CB

Domain mapping of disease mutations (DMDM)

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DMDMi
60659599

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000588252 – 524Serine/threonine-protein phosphatase 2B catalytic subunit beta isoformAdd BLAST523

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1
Modified residuei478PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P16298

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P16298

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P16298

MaxQB - The MaxQuant DataBase

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MaxQBi
P16298

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

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PaxDbi
P16298

PeptideAtlas

More...
PeptideAtlasi
P16298

PRoteomics IDEntifications database

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PRIDEi
P16298

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
53341 [P16298-1]
53342 [P16298-2]
53343 [P16298-3]
53344 [P16298-4]

PTM databases

DEPOD human dephosphorylation database

More...
DEPODi
PPP3CB

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P16298

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

More...
PhosphoSitePlusi
P16298

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P16298

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000107758, Expressed in frontal cortex and 254 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P16298, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P16298, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000107758, Tissue enhanced (skeletal)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

Interacts (via calcineurin B binding domain) with regulatory subunit PPP3R1/calcineurin B.

Interacts (via calmodulin-binding domain) with calmodulin; the interaction depends on calmodulin binding to Ca2+.

Interacts with SLC12A1 (By similarity).

Interacts with SORL1 (By similarity).

Interacts with UNC119 (By similarity).

By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
111524, 59 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P16298

Database of interacting proteins

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DIPi
DIP-52337N

Protein interaction database and analysis system

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IntActi
P16298, 34 interactors

Molecular INTeraction database

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MINTi
P16298

STRING: functional protein association networks

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STRINGi
9606.ENSP00000378306

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P16298

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P16298, 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

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

3D structure databases

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

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SMRi
P16298

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 25DisorderedSequence analysisAdd BLAST25
Regioni65 – 356CatalyticCuratedAdd BLAST292
Regioni357 – 379Calcineurin B binding1 PublicationAdd BLAST23
Regioni401 – 415Calmodulin-binding1 PublicationAdd BLAST15
Regioni416 – 423Autoinhibitory segment1 Publication8
Regioni474 – 496Autoinhibitory domain1 PublicationAdd BLAST23

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi316 – 320SAPNY motifBy similarity5

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

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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-2B subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0375, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000154115

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P16298

Identification of Orthologs from Complete Genome Data

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OMAi
TNRRIMN

Database of Orthologous Groups

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OrthoDBi
463522at2759

TreeFam database of animal gene trees

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TreeFami
TF105557

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07416, MPP_PP2B, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.60.21.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004843, Calcineurin-like_PHP_ApaH
IPR029052, Metallo-depent_PP-like
IPR041751, MPP_PP2B
IPR043360, PP2B
IPR006186, Ser/Thr-sp_prot-phosphatase

The PANTHER Classification System

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PANTHERi
PTHR45673, PTHR45673, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00149, Metallophos, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00114, STPHPHTASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00156, PP2Ac, 1 hit

Superfamily database of structural and functional annotation

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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_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 (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

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

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

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

This isoform has been chosen as the <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
MAAPEPARAA PPPPPPPPPP PGADRVVKAV PFPPTHRLTS EEVFDLDGIP
60 70 80 90 100
RVDVLKNHLV KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI
110 120 130 140 150
HGQFFDLMKL FEVGGSPANT RYLFLGDYVD RGYFSIECVL YLWVLKILYP
160 170 180 190 200
STLFLLRGNH ECRHLTEYFT FKQECKIKYS ERVYEACMEA FDSLPLAALL
210 220 230 240 250
NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL WSDPSEDFGN
260 270 280 290 300
EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY
310 320 330 340 350
RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY
360 370 380 390 400
WLPNFMDVFT WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDGSAAA
410 420 430 440 450
RKEIIRNKIR AIGKMARVFS VLREESESVL TLKGLTPTGM LPSGVLAGGR
460 470 480 490 500
QTLQSATVEA IEAEKAIRGF SPPHRICSFE EAKGLDRINE RMPPRKDAVQ
510 520
QDGFNSLNTA HATENHGTGN HTAQ
Length:524
Mass (Da):59,024
Last modified:February 1, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7661183F3C2362C8
GO
Isoform 2 (identifier: P16298-2) [UniParc]FASTAAdd to basket

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

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

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

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

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

Show »
Length:525
Mass (Da):59,123
Checksum:iADB0ECB75371B574
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5F2F8Q5F2F8_HUMAN
Serine/threonine-protein phosphatas...
PPP3CB hCG_18332
496Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5F2G0Q5F2G0_HUMAN
Serine/threonine-protein phosphatas...
PPP3CB
187Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Alternative sequence

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

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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

The Consensus CDS (CCDS) project

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

Protein sequence database of the Protein Information Resource

More...
PIRi
A36222
B36222

NCBI Reference Sequences

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

Genome annotation databases

Ensembl eukaryotic genome annotation project

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

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5532

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5532

UCSC genome browser

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

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29551 mRNA Translation: AAA35706.1
M29550 mRNA Translation: AAA35705.1
AJ488506 mRNA Translation: CAD32694.1
AL353731 Genomic DNA No translation available.
AL359074 Genomic DNA No translation available.
CH471083 Genomic DNA Translation: EAW54497.1
CH471083 Genomic DNA Translation: EAW54498.1
BC028049 mRNA Translation: AAH28049.1
CCDSiCCDS44436.1 [P16298-3]
CCDS44437.1 [P16298-4]
CCDS7328.1 [P16298-1]
PIRiA36222
B36222
RefSeqiNP_001135825.1, NM_001142353.2 [P16298-4]
NP_001135826.1, NM_001142354.2 [P16298-3]
NP_001276897.1, NM_001289968.1 [P16298-2]
NP_001276898.1, NM_001289969.1
NP_066955.1, NM_021132.3 [P16298-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OR9X-ray2.23A1-524[»]
4ORAX-ray2.75A1-524[»]
4ORCX-ray2.70A1-524[»]
SMRiP16298
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111524, 59 interactors
ComplexPortaliCPX-1002, Calcineurin-Calmodulin complex, beta-R2 variant
CPX-1009, Calcineurin-Calmodulin complex, beta-R1 variant
CPX-1116, Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant
CPX-998, Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant
CORUMiP16298
DIPiDIP-52337N
IntActiP16298, 34 interactors
MINTiP16298
STRINGi9606.ENSP00000378306

Chemistry databases

BindingDBiP16298
ChEMBLiCHEMBL5278

PTM databases

DEPODiPPP3CB
iPTMnetiP16298
PhosphoSitePlusiP16298
SwissPalmiP16298

Genetic variation databases

BioMutaiPPP3CB
DMDMi60659599

Proteomic databases

EPDiP16298
jPOSTiP16298
MassIVEiP16298
MaxQBiP16298
PaxDbiP16298
PeptideAtlasiP16298
PRIDEiP16298
ProteomicsDBi53341 [P16298-1]
53342 [P16298-2]
53343 [P16298-3]
53344 [P16298-4]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
1918, 209 antibodies

The DNASU plasmid repository

More...
DNASUi
5532

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5532
DisGeNETi5532

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PPP3CB
HGNCiHGNC:9315, PPP3CB
HPAiENSG00000107758, Tissue enhanced (skeletal)
MIMi114106, gene
neXtProtiNX_P16298
OpenTargetsiENSG00000107758
PharmGKBiPA33679
VEuPathDBiHostDB:ENSG00000107758

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0375, Eukaryota
GeneTreeiENSGT00940000154115
InParanoidiP16298
OMAiTNRRIMN
OrthoDBi463522at2759
TreeFamiTF105557

Enzyme and pathway databases

PathwayCommonsiP16298
ReactomeiR-HSA-180024, DARPP-32 events
R-HSA-2025928, Calcineurin activates NFAT
R-HSA-2871809, FCERI mediated Ca+2 mobilization
R-HSA-4086398, Ca2+ pathway
R-HSA-5607763, CLEC7A (Dectin-1) induces NFAT activation
R-HSA-9010642, ROBO receptors bind AKAP5
SIGNORiP16298

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
5532, 66 hits in 1018 CRISPR screens

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

More...
ChiTaRSi
PPP3CB, human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PPP3CB

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

More...
GenomeRNAii
5532
PharosiP16298, Tbio

Protein Ontology

More...
PROi
PR:P16298
RNActiP16298, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000107758, Expressed in frontal cortex and 254 other tissues
ExpressionAtlasiP16298, baseline and differential
GenevisibleiP16298, HS

Family and domain databases

CDDicd07416, MPP_PP2B, 1 hit
Gene3Di3.60.21.10, 1 hit
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 nameiPP2BB_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P16298
Secondary accession number(s): P16299
, Q5F2F9, Q8N1F0, Q8N3W4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 2005
Last modified: September 29, 2021
This is version 177 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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