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P16298 (PP2BB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:CALNA2, CALNB, CNA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length524 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.

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_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

T cell differentiation

Inferred from electronic annotation. Source: Ensembl

T cell homeostasis

Inferred from electronic annotation. Source: Ensembl

T cell proliferation

Non-traceable author statement PubMed 8978785. Source: UniProtKB

axon extension

Traceable author statement PubMed 21531385. Source: UniProtKB

calcium ion-dependent exocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to drug

Inferred from direct assay PubMed 11005320. Source: UniProtKB

heart development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

learning

Traceable author statement PubMed 21531385. Source: UniProtKB

memory

Traceable author statement PubMed 21531385. Source: UniProtKB

negative regulation of T cell mediated cytotoxicity

Inferred from electronic annotation. Source: Ensembl

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

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Non-traceable author statement PubMed 8978785. Source: UniProtKB

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of synaptic plasticity

Traceable author statement PubMed 21531385. Source: UniProtKB

response to cytokine

Inferred from electronic annotation. Source: Ensembl

social behavior

Inferred from expression pattern PubMed 21531385. Source: UniProtKB

   Cellular_componentcalcineurin complex

Inferred from direct assay PubMed 8524402. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from direct assay PubMed 8524402. Source: UniProtKB

calmodulin binding

Inferred from direct assay PubMed 11005320Ref.1. Source: UniProtKB

calmodulin-dependent protein phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

drug binding

Inferred from direct assay PubMed 11005320. Source: UniProtKB

protein phosphatase 2B binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Irak1Q99J342EBI-1759540,EBI-6117042From a different organism.
IRF2P143162EBI-1759540,EBI-2866589

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. Calcineurin A beta isoform consists of at least two isoenzymes that may result from alternative splicing events.
Isoform 1 (identifier: P16298-1)

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 2 (identifier: P16298-2)

The sequence of this isoform differs from the canonical sequence as follows:
     137-137: E → EHVLGTEDISINPHNNINE
     456-524: ATVEAIEAEK...NHGTGNHTAQ → GNDVMQLAVP...LLFFSSCLSS
Isoform 3 (identifier: P16298-3)

The sequence of this isoform differs from the canonical sequence as follows:
     395-395: D → DV
     456-465: Missing.
Isoform 4 (identifier: P16298-4)

The sequence of this isoform differs from the canonical sequence as follows:
     395-395: D → DV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 524523Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
PRO_0000058825

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 – 2111Poly-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 Ref.6

Natural variations

Alternative sequence1371E → EHVLGTEDISINPHNNINE in isoform 2.
VSP_005096
Alternative sequence3951D → DV in isoform 3 and isoform 4.
VSP_043803
Alternative sequence456 – 52469ATVEA…NHTAQ → GNDVMQLAVPQMDWGTPHSF ANNSHNACREFLLFFSSCLS S in isoform 2.
VSP_005097
Alternative sequence456 – 46510Missing in isoform 3.
VSP_012617

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: 7661183F3C2362C8

FASTA52459,024
        10         20         30         40         50         60 
MAAPEPARAA PPPPPPPPPP PGADRVVKAV PFPPTHRLTS EEVFDLDGIP 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 EDQFDGSAAA RKEIIRNKIR AIGKMARVFS 

       430        440        450        460        470        480 
VLREESESVL TLKGLTPTGM LPSGVLAGGR QTLQSATVEA IEAEKAIRGF SPPHRICSFE 

       490        500        510        520 
EAKGLDRINE RMPPRKDAVQ QDGFNSLNTA HATENHGTGN HTAQ 

« Hide

Isoform 2 [UniParc].

Checksum: 1B0BFA63FB98E06D
Show »

FASTA51458,013
Isoform 3 [UniParc].

Checksum: A6762D9468A09B51
Show »

FASTA51558,081
Isoform 4 [UniParc].

Checksum: ADB0ECB75371B574
Show »

FASTA52559,123

References

« Hide 'large scale' references
[1]"Cloning of human calcineurin A: evidence for two isozymes and identification of a polyproline structural domain."
Guerini D., Klee C.B.
Proc. Natl. Acad. Sci. U.S.A. 86:9183-9187(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"Identification of a third alternatively spliced cDNA encoding the catalytic subunit of protein phosphatase 2B beta."
McPartlin A.E., Barker H.M., Cohen P.T.W.
Biochim. Biophys. Acta 1088:308-310(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Teratocarcinoma.
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 4).
Tissue: Testis.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29551 mRNA. Translation: AAA35706.1.
M29550 mRNA. Translation: AAA35705.1.
AJ488506 mRNA. Translation: CAD32694.1.
AL353731, AL359074 Genomic DNA. Translation: CAI52487.1.
AL359074, AL353731 Genomic DNA. Translation: CAI52473.1.
CH471083 Genomic DNA. Translation: EAW54497.1.
CH471083 Genomic DNA. Translation: EAW54498.1.
BC028049 mRNA. Translation: AAH28049.1.
PIRA36222.
B36222.
RefSeqNP_001135825.1. NM_001142353.1.
NP_001135826.1. NM_001142354.1.
NP_066955.1. NM_021132.2.
UniGeneHs.500067.

3D structure databases

ProteinModelPortalP16298.
SMRP16298. Positions 24-420.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111524. 13 interactions.
DIPDIP-52337N.
IntActP16298. 7 interactions.
STRING9606.ENSP00000378306.

Chemistry

BindingDBP16298.
ChEMBLCHEMBL5278.

PTM databases

PhosphoSiteP16298.

Polymorphism databases

DMDM60659599.

Proteomic databases

PaxDbP16298.
PRIDEP16298.

Protocols and materials databases

DNASU5532.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360663; ENSP00000353881; ENSG00000107758. [P16298-1]
ENST00000394822; ENSP00000378299; ENSG00000107758. [P16298-2]
ENST00000394828; ENSP00000378305; ENSG00000107758. [P16298-3]
ENST00000394829; ENSP00000378306; ENSG00000107758. [P16298-4]
GeneID5532.
KEGGhsa:5532.
UCSCuc001jue.3. human. [P16298-1]
uc001juf.3. human. [P16298-4]
uc001jug.3. human. [P16298-3]
uc001jui.2. human. [P16298-2]

Organism-specific databases

CTD5532.
GeneCardsGC10M075196.
HGNCHGNC:9315. PPP3CB.
HPAHPA008233.
MIM114106. gene.
neXtProtNX_P16298.
PharmGKBPA33679.
GenAtlasSearch...

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_118664. Calcineurin Dephosphorylates NFATC1,2,3.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP16298.
BgeeP16298.
CleanExHS_PPP3CB.
GenevestigatorP16298.

Family and domain databases

InterProIPR004843. PEstase_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP3CB. human.
GeneWikiPPP3CB.
GenomeRNAi5532.
NextBio21430.
PROP16298.
SOURCESearch...

Entry information

Entry namePP2BB_HUMAN
AccessionPrimary (citable) accession number: P16298
Secondary accession number(s): P16299 expand/collapse secondary AC list , Q5F2F9, Q8N1F0, Q8N3W4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 2005
Last modified: March 19, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM