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Reviewed, UniProtKB/Swiss-Prot P16298 (PP2BB_HUMAN)

Last modified January 19, 2010. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
    EC=3.1.3.16
Alternative name(s):
    Calmodulin-dependent calcineurin A subunit beta isoform
    CAM-PRP catalytic subunit
Gene names
Name: PPP3CB
Synonyms: CALNA2, CALNB, CNA2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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 phosphoprotein + H2O = a protein + 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.

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Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   LigandCalmodulin-binding
Iron
Metal-binding
Zinc
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processsignal transduction

Non-traceable author statement. Source: ProtInc

   Cellular componentcalcineurin complex

Inferred from direct assay. Source: UniProtKB

cytosol

Inferred from Experiment. Source: Reactome

   Molecular functioncalcium ion binding

Inferred from direct assay. Source: UniProtKB

calmodulin binding

Non-traceable author statement. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine phosphatase activity

Non-traceable author statement. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

GRB2P629931EBI-1759540,EBI-401755

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Alternative products

This entry describes 3 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:
     456-465: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
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.5

Natural variations

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

Experimental info

Sequence conflict3951D → DV in CAD32694. Ref.2

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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.

Checksum: 1B0BFA63FB98E06D
Show »

FASTA51458,013
Isoform 3.

Checksum: BC3173C2386E4324
Show »

FASTA51457,982

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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: 2556704] [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: 1848109] [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: 15164054] [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]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
+Additional computationally mapped references.

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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: EAW54498.1.
IPIIPI00181738.
IPI00218862.
IPI00872930.
PIRA36222.
B36222.
RefSeqNP_001135826.1.
NP_066955.1.
UniGeneHs.500067

3D structure databases

SMRP16298. Positions 24-381.
ModBaseSearch...

Protein-protein interaction databases

IntActP16298. 1 interaction.
STRINGP16298.

PTM databases

PhosphoSiteP16298.

Proteomic databases

PRIDEP16298.

Genome annotation databases

EnsemblENST00000360663; ENSP00000353881; ENSG00000107758; Homo sapiens. [Genome view]
GeneID5532.
UCSCuc001jue.1. human.
uc001jug.1. human.
uc001jui.1. human.

Organism-specific databases

CTD5532.
GeneCardsGC10M074866.
H-InvDBHIX0022172.
HGNCHGNC:9315. PPP3CB.
HPAHPA008233.
MIM114106. gene.
PharmGKBPA33679.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12777.
HOVERGENP16298.
OMAEDQFDGS.
PhylomeDBP16298.

Enzyme and pathway databases

BRENDA3.1.3.16. 247.
Pathway_Interaction_DBbcr_5pathway. BCR signaling pathway.
tcrcalciumpathway. Calcium signaling in the CD4+ TCR pathway.
cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
il12_stat4pathway. IL12 signaling mediated by STAT4.
il12_2pathway. IL12-mediated signaling events.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
ReactomeREACT_15295. Opioid Signalling.

Gene expression databases

ArrayExpressP16298.
BgeeP16298.
CleanExHS_PPP3CB.
GenevestigatorP16298.
GermOnlineENSG00000107758. Homo sapiens.

Family and domain databases

InterProIPR004843. M-pesterase.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PANTHERPTHR11668. T_phtase_apaH. 1 hit.
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio21430.
SOURCESearch...

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Entry information

Entry namePP2BB_HUMAN
AccessionPrimary (citable) accession number: P16298
Secondary accession number(s): P16299, Q5F2F9, Q8N3W4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 2005
Last modified: January 19, 2010
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 10

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents