Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P48453 (PP2BB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform

EC=3.1.3.16
Alternative name(s):
CAM-PRP catalytic subunit
Calmodulin-dependent calcineurin A subunit beta isoform
Gene names
Name:Ppp3cb
Synonyms:Calnb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 1 Fe3+ ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.

Tissue specificity

Two isoforms in Ehrlich ascites tumor (EAT) is demonstrated by polymerase chain reaction specific primers to the catalytic and calmodulin-binding domain, respectively. Isoform 1 is of medium abundance in EAT cells. Ref.3

Sequence similarities

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

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   LigandCalmodulin-binding
Iron
Metal-binding
Zinc
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell differentiation

Inferred from mutant phenotype PubMed 12091710. Source: MGI

T cell homeostasis

Inferred from mutant phenotype PubMed 18097009. Source: MGI

calcium ion-dependent exocytosis

Inferred from direct assay PubMed 11978799. Source: UniProtKB

cellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

heart development

Inferred from mutant phenotype PubMed 11904392. Source: MGI

locomotion involved in locomotory behavior

Inferred from mutant phenotype PubMed 16648267. Source: MGI

negative regulation of T cell mediated cytotoxicity

Inferred from mutant phenotype PubMed 18097009. Source: MGI

positive regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from mutant phenotype PubMed 11978799. Source: UniProtKB

protein dephosphorylation

Inferred from mutant phenotype PubMed 11978799. Source: UniProtKB

protein phosphorylation

Inferred from mutant phenotype PubMed 11978799. Source: UniProtKB

regulation of gene expression

Inferred from mutant phenotype PubMed 18097009. Source: MGI

regulation of insulin secretion

Inferred from sequence or structural similarity. Source: UniProtKB

response to cytokine

Inferred from mutant phenotype PubMed 18097009. Source: MGI

social behavior

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcalcineurin complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

plasma membrane

Inferred from direct assay PubMed 11978799. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-dependent protein serine/threonine phosphatase activity

Traceable author statement. Source: Reactome

calmodulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

calmodulin-dependent protein phosphatase activity

Inferred from mutant phenotype PubMed 11978799. Source: UniProtKB

drug binding

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 19883655PubMed 22940692. Source: IntAct

protein phosphatase 2B binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine phosphatase activity

Inferred from direct assay PubMed 11904392PubMed 12091710. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Akap5D3YVF03EBI-642618,EBI-7091108
Akap6Q9WVC72EBI-642618,EBI-7559840From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P48453-1)

Also known as: 2B2;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: P48453-2)

Also known as: 2B1;

The sequence of this isoform differs from the canonical sequence as follows:
     387-406: MTEGEDQFDVGSAAARKEII → GSEEDGFDGATAAARKEVI

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 525524Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
PRO_0000058826

Regions

Region2 – 310309Catalytic
Region256 – 2627Calcineurin B binding-site 1 Potential
Region305 – 3106Calcineurin B binding-site 2 Potential
Region401 – 42323Calmodulin-binding Potential
Region474 – 49623Inhibitory domain
Compositional bias11 – 2010Poly-Pro

Sites

Active site1601Proton donor By similarity
Metal binding991Iron By similarity
Metal binding1011Iron By similarity
Metal binding1271Iron By similarity
Metal binding1271Zinc By similarity
Metal binding1591Zinc By similarity
Metal binding2081Zinc By similarity
Metal binding2901Zinc By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Natural variations

Alternative sequence387 – 40620MTEGE…RKEII → GSEEDGFDGATAAARKEVI in isoform 1.
VSP_011856

Experimental info

Sequence conflict4811E → G in AAA37411. Ref.2
Sequence conflict523 – 5242SA → TP in AAA37411. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (2B2) [UniParc].

Last modified November 9, 2004. Version 2.
Checksum: 5E73BA3100BE2337

FASTA52559,173
        10         20         30         40         50         60 
MAAPEPARAA PPPPPPPPPP LGADRVVKAV PFPPTHRLTS EEVFDMDGIP RVDVLKNHLV 

        70         80         90        100        110        120 
KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI HGQFFDLMKL FEVGGSPANT 

       130        140        150        160        170        180 
RYLFLGDYVD RGYFSIECVL YLWVLKILYP STLFLLRGNH ECRHLTEYFT FKQECKIKYS 

       190        200        210        220        230        240 
ERVYEACMEA FDSLPLAALL NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL 

       250        260        270        280        290        300 
WSDPSEDFGN EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY 

       310        320        330        340        350        360 
RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY WLPNFMDVFT 

       370        380        390        400        410        420 
WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDVGSAA ARKEIIRNKI RAIGKMARVF 

       430        440        450        460        470        480 
SVLREESESV LTLKGLTPTG MLPSGVLAGG RQTLQSATVE AIEAEKAIRG FSPPHRICSF 

       490        500        510        520 
EEAKGLDRIN ERMPPRKDAV QQDGFNSLNT AHTTENHGTG NHSAQ 

« Hide

Isoform 1 (2B1) [UniParc].

Checksum: D5348F544E5ACB35
Show »

FASTA52458,929

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6.
Tissue: Brain.
[2]"Chromosomal mapping of the human genes for the calmodulin-dependent protein phosphatase (calcineurin) catalytic subunit."
Giri P.R., Higuchi S., Kincaid R.L.
Biochem. Biophys. Res. Commun. 181:252-258(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-525 (ISOFORM 2).
[3]"Dephosphorylation of the small heat shock protein hsp25 by calcium/calmodulin-dependent (type 2B) protein phosphatase."
Gaestel M., Benndorf R., Hayess K., Priemer E., Engel K.
J. Biol. Chem. 267:21607-21611(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 320-416 (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC066000 mRNA. Translation: AAH66000.1.
M81483 mRNA. Translation: AAA37411.1.
CCDSCCDS26846.1. [P48453-1]
PIRJT0976.
RefSeqNP_032940.1. NM_008914.2. [P48453-1]
UniGeneMm.274432.

3D structure databases

ProteinModelPortalP48453.
SMRP48453. Positions 24-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202345. 2 interactions.
IntActP48453. 8 interactions.
MINTMINT-1676111.

PTM databases

PhosphoSiteP48453.

Proteomic databases

MaxQBP48453.
PaxDbP48453.
PRIDEP48453.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000159027; ENSMUSP00000125722; ENSMUSG00000021816. [P48453-1]
GeneID19056.
KEGGmmu:19056.
UCSCuc007sjx.2. mouse. [P48453-1]

Organism-specific databases

CTD5532.
MGIMGI:107163. Ppp3cb.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000063087.
HOGENOMHOG000172699.
HOVERGENHBG002819.
InParanoidP48453.
KOK04348.
OMAAHTTENH.
OrthoDBEOG7BZVSC.
TreeFamTF105557.

Enzyme and pathway databases

ReactomeREACT_118809. Calcineurin Dephosphorylates Nfatc2.

Gene expression databases

ArrayExpressP48453.
BgeeP48453.
GenevestigatorP48453.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP3CB. mouse.
NextBio295546.
PROP48453.
SOURCESearch...

Entry information

Entry namePP2BB_MOUSE
AccessionPrimary (citable) accession number: P48453
Secondary accession number(s): Q6NZR4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 9, 2004
Last modified: July 9, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot