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Entry version 161 (16 Oct 2019)
Sequence version 1 (11 Oct 2004)
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Protein

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

Gene

Ppp3ca

Organism
Mus musculus (Mouse)
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:7791792, PubMed:26794871). Many of the substrates contain a PxIxIT motif and/or a LxVP motif (By similarity). In response to increased Ca2+ levels, dephosphorylates and activates phosphatase SSH1 which results in cofilin dephosphorylation (By similarity). In response to increased Ca2+ levels following mitochondrial depolarization, dephosphorylates DNM1L inducing DNM1L translocation to the mitochondrion (By similarity). Dephosphorylates heat shock protein HSPB1 (By similarity). Dephosphorylates and activates transcription factor NFATC1 (By similarity). Dephosphorylates and inactivates transcription factor ELK1 (By similarity). Dephosphorylates DARPP32 (By similarity). May dephosphorylate CRTC2 at 'Ser-171' resulting in CRTC2 dissociation from 14-3-3 proteins (By similarity).By similarity2 Publications

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

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

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by Ca2+-bound calmodulin following an increase in intracellular Ca2+ (PubMed:26794871). 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+ (PubMed:26794871). 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 (PubMed:26794871). 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 (PubMed:26794871). 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 (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi90IronCombined sources1 Publication1
Metal bindingi92Iron; via tele nitrogenCombined sources1 Publication1
Metal bindingi118IronCombined sources1 Publication1
Metal bindingi118ZincCombined sources1 Publication1
Metal bindingi150ZincCombined 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 sitei151Proton donorBy similarity1
Metal bindingi199Zinc; via tele nitrogenCombined sources1 Publication1
Metal bindingi281Zinc; 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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-2025928 Calcineurin activates NFAT
R-MMU-2871809 FCERI mediated Ca+2 mobilization
R-MMU-4086398 Ca2+ pathway
R-MMU-5607763 CLEC7A (Dectin-1) induces NFAT activation

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC:3.1.3.162 Publications)
Alternative name(s):
CAM-PRP catalytic subunit
Calmodulin-dependent calcineurin A subunit alpha isoform
Short name:
CNA alpha1 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:Ppp3ca
Synonyms:Calna
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 3

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:107164 Ppp3ca

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell 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

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>Mutagenesisi348 – 521Missing : Loss of catalytic activity. Loss of interaction with PPP3R1/calreticulin B and calmodulin. 1 PublicationAdd BLAST174
Mutagenesisi389 – 521Missing : Increases catalytic activity independently of calmodulin. Loss of interaction with calmodulin. Does not affect interaction with PPP3R1/calreticulin B. 1 PublicationAdd BLAST133
Mutagenesisi406 – 521Missing : Increases catalytic activity independently of calmodulin. Does not affect interaction with PPP3R1/calreticulin B and calmodulin. 1 PublicationAdd BLAST116
Mutagenesisi442 – 521Missing : Increases basal catalytic activity. Does not affect interaction with PPP3R1/calreticulin B and calmodulin. 1 PublicationAdd BLAST80
Mutagenesisi477D → N: Greatly reduces inhibition of calcineurin phosphatase activity. 1 Publication1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000588232 – 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-acetylserineBy similarity1
Modified residuei224Nitrated tyrosineCombined sources1
Modified residuei469PhosphoserineBy similarity1
Modified residuei492PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P63328

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

More...
PaxDbi
P63328

PeptideAtlas

More...
PeptideAtlasi
P63328

PRoteomics IDEntifications database

More...
PRIDEi
P63328

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P63328

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

More...
PhosphoSitePlusi
P63328

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P63328

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000028161 Expressed in 294 organ(s), highest expression level in caudate-putamen

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P63328 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P63328 MM

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

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

Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca2+-binding subunit (also known as calcineurin B) (PubMed:26794871). 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:26794871).

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

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

Interacts with MYOZ1 (PubMed:11114196).

Interacts with MYOZ3 (By similarity).

Interacts with CIB1; the interaction increases upon cardiomyocyte hypertrophy (PubMed:20639889).

Interacts with CHP1 and CHP2 (By similarity).

Interacts with CRTC1 (PubMed:30611118).

Interacts with CRTC2 (PubMed:30611118).

Interacts with DNM1L; the interaction dephosphorylates DNM1L and promotes its translocation to mitochondria (By similarity).

Interacts with CMYA5; this interaction represses calcineurin activity in muscle (PubMed:21427212).

Interacts (constitutively active form) with SYNPO2 (By similarity).

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

Interacts with NFATC2 (By similarity).

Interacts with RCAN3 (By similarity).

Interacts with PPIA (By similarity).

Interacts with RCAN1 (PubMed:12809556).

By similarity6 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 substrateBy similarity1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Crtc2Q3U1822EBI-397208,EBI-8018890

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
202344, 19 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1010 Calcineurin-Calmodulin complex, alpha-R1 variant
CPX-1049 Calcineurin-Calmodulin complex, alpha-R2 variant
CPX-1115 Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant
CPX-881 Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant

Database of interacting proteins

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DIPi
DIP-31543N

Protein interaction database and analysis system

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IntActi
P63328, 15 interactors

Molecular INTeraction database

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MINTi
P63328

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000053101

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

Secondary structure

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

3D structure databases

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

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SMRi
P63328

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

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

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 substrateBy similarity10
Regioni341 – 369Calcineurin B binding1 PublicationAdd BLAST29
Regioni392 – 406Calmodulin-binding1 PublicationAdd BLAST15
Regioni407 – 414Autoinhibitory segment1 Publication8
Regioni465 – 487Autoinhibitory domain1 PublicationAdd BLAST23

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi307 – 311SAPNY 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 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-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.By similarity

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

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0375 Eukaryota
COG0639 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156306

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000172699

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P63328

KEGG Orthology (KO)

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KOi
K04348

Identification of Orthologs from Complete Genome Data

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OMAi
LWSLKIW

Database of Orthologous Groups

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OrthoDBi
335949at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P63328

TreeFam database of animal gene trees

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TreeFami
TF105557

Family and domain databases

Conserved Domains Database

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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
IPR006186 Ser/Thr-sp_prot-phosphatase

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

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 (2)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 2 <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
Isoform 1 (identifier: P63328-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL
60 70 80 90 100
MKEGRLEESV ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK
110 120 130 140 150
LFEVGGSPAN TRYLFLGDYV DRGYFSIECV LYLWALKILY PKTLFLLRGN
160 170 180 190 200
HECRHLTEYF TFKQECKIKY SERVYDACMD AFDCLPLAAL MNQQFLCVHG
210 220 230 240 250
GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG NEKTQEHFTH
260 270 280 290 300
NTVRGCSYFY SYPAVCDFLQ 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
KALASETNGT DSNGSNSSNI Q
Length:521
Mass (Da):58,644
Last modified:October 11, 2004 - 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:i16530C27DDBF1F05
GO
Isoform 2 (identifier: P63328-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:511
Mass (Da):57,615
Checksum:i01428D70D67450BD
GO

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_018563448 – 457Missing in isoform 2. 1 Publication10

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
J05479 mRNA Translation: AAA37359.1
AK146387 mRNA Translation: BAE27131.1
AK150393 mRNA Translation: BAE29521.1
J04134 mRNA Translation: AAA37432.1
S78668 mRNA Translation: AAB34675.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS17860.1 [P63328-1]
CCDS80027.1 [P63328-2]

Protein sequence database of the Protein Information Resource

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PIRi
A42232 A31257

NCBI Reference Sequences

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RefSeqi
NP_001280551.1, NM_001293622.1 [P63328-2]
NP_032939.1, NM_008913.5 [P63328-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000056758; ENSMUSP00000053101; ENSMUSG00000028161 [P63328-1]
ENSMUST00000070198; ENSMUSP00000071040; ENSMUSG00000028161 [P63328-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
19055

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:19055

UCSC genome browser

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UCSCi
uc008rmg.2 mouse [P63328-1]
uc008rmh.2 mouse [P63328-2]

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
J05479 mRNA Translation: AAA37359.1
AK146387 mRNA Translation: BAE27131.1
AK150393 mRNA Translation: BAE29521.1
J04134 mRNA Translation: AAA37432.1
S78668 mRNA Translation: AAB34675.1
CCDSiCCDS17860.1 [P63328-1]
CCDS80027.1 [P63328-2]
PIRiA42232 A31257
RefSeqiNP_001280551.1, NM_001293622.1 [P63328-2]
NP_032939.1, NM_008913.5 [P63328-1]

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ORBX-ray3.11A1-521[»]
SMRiP63328
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi202344, 19 interactors
ComplexPortaliCPX-1010 Calcineurin-Calmodulin complex, alpha-R1 variant
CPX-1049 Calcineurin-Calmodulin complex, alpha-R2 variant
CPX-1115 Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant
CPX-881 Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant
DIPiDIP-31543N
IntActiP63328, 15 interactors
MINTiP63328
STRINGi10090.ENSMUSP00000053101

PTM databases

iPTMnetiP63328
PhosphoSitePlusiP63328
SwissPalmiP63328

Proteomic databases

MaxQBiP63328
PaxDbiP63328
PeptideAtlasiP63328
PRIDEiP63328

Genome annotation databases

EnsembliENSMUST00000056758; ENSMUSP00000053101; ENSMUSG00000028161 [P63328-1]
ENSMUST00000070198; ENSMUSP00000071040; ENSMUSG00000028161 [P63328-2]
GeneIDi19055
KEGGimmu:19055
UCSCiuc008rmg.2 mouse [P63328-1]
uc008rmh.2 mouse [P63328-2]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5530
MGIiMGI:107164 Ppp3ca

Phylogenomic databases

eggNOGiKOG0375 Eukaryota
COG0639 LUCA
GeneTreeiENSGT00940000156306
HOGENOMiHOG000172699
InParanoidiP63328
KOiK04348
OMAiLWSLKIW
OrthoDBi335949at2759
PhylomeDBiP63328
TreeFamiTF105557

Enzyme and pathway databases

ReactomeiR-MMU-2025928 Calcineurin activates NFAT
R-MMU-2871809 FCERI mediated Ca+2 mobilization
R-MMU-4086398 Ca2+ pathway
R-MMU-5607763 CLEC7A (Dectin-1) induces NFAT activation

Miscellaneous databases

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

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ChiTaRSi
Ppp3ca mouse

Protein Ontology

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PROi
PR:P63328

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028161 Expressed in 294 organ(s), highest expression level in caudate-putamen
ExpressionAtlasiP63328 baseline and differential
GenevisibleiP63328 MM

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
IPR006186 Ser/Thr-sp_prot-phosphatase
PfamiView protein in Pfam
PF00149 Metallophos, 1 hit
PRINTSiPR00114 STPHPHTASE
SMARTiView protein in SMART
SM00156 PP2Ac, 1 hit
PROSITEiView protein in PROSITE
PS00125 SER_THR_PHOSPHATASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPP2BA_MOUSE
<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: P63328
Secondary accession number(s): P12816
, P20652, Q3UCU1, Q64135
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: October 16, 2019
This is version 161 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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