Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Fe3+By similarityNote: Binds 1 Fe3+ ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991IronBy similarity
Metal bindingi101 – 1011IronBy similarity
Metal bindingi127 – 1271IronBy similarity
Metal bindingi127 – 1271ZincBy similarity
Metal bindingi159 – 1591ZincBy similarity
Active sitei160 – 1601Proton donorBy similarity
Metal bindingi208 – 2081ZincBy similarity
Metal bindingi290 – 2901ZincBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. calmodulin binding Source: UniProtKB
  3. calmodulin-dependent protein phosphatase activity Source: UniProtKB
  4. drug binding Source: UniProtKB
  5. enzyme binding Source: UniProtKB
  6. protein dimerization activity Source: UniProtKB
  7. protein phosphatase 2B binding Source: UniProtKB
  8. protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. axon extension Source: UniProtKB
  2. calcineurin-NFAT signaling cascade Source: BHF-UCL
  3. calcium ion-dependent exocytosis Source: UniProtKB
  4. cellular response to drug Source: UniProtKB
  5. dephosphorylation Source: UniProtKB
  6. Fc-epsilon receptor signaling pathway Source: Reactome
  7. heart development Source: Ensembl
  8. innate immune response Source: Reactome
  9. learning Source: UniProtKB
  10. locomotion involved in locomotory behavior Source: Ensembl
  11. memory Source: UniProtKB
  12. negative regulation of T cell mediated cytotoxicity Source: Ensembl
  13. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  14. positive regulation of NFAT protein import into nucleus Source: BHF-UCL
  15. positive regulation of transcription, DNA-templated Source: UniProtKB
  16. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  17. protein dephosphorylation Source: UniProtKB
  18. protein phosphorylation Source: UniProtKB
  19. regulation of insulin secretion Source: UniProtKB
  20. regulation of synaptic plasticity Source: UniProtKB
  21. response to cytokine Source: Ensembl
  22. signal transduction Source: UniProtKB
  23. social behavior Source: UniProtKB
  24. T cell activation Source: UniProtKB
  25. T cell differentiation Source: Ensembl
  26. T cell homeostasis Source: Ensembl
  27. T cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calmodulin-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_15334. DARPP-32 events.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_263982. Ca2+ pathway.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PPP3CB
Synonyms:CALNA2, CALNB, CNA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:9315. PPP3CB.

Subcellular locationi

GO - Cellular componenti

  1. calcineurin complex Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. plasma membrane Source: UniProtKB
  5. T-tubule Source: Ensembl
  6. Z disc Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33679.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 524523Serine/threonine-protein phosphatase 2B catalytic subunit beta isoformPRO_0000058825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP16298.
PaxDbiP16298.
PRIDEiP16298.

PTM databases

DEPODiP16298.
PhosphoSiteiP16298.

Expressioni

Gene expression databases

BgeeiP16298.
CleanExiHS_PPP3CB.
ExpressionAtlasiP16298. baseline and differential.
GenevestigatoriP16298.

Organism-specific databases

HPAiHPA008233.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
Irak1Q99J342EBI-1759540,EBI-6117042From a different organism.
IRF2P143162EBI-1759540,EBI-2866589

Protein-protein interaction databases

BioGridi111524. 21 interactions.
DIPiDIP-52337N.
IntActiP16298. 7 interactions.
STRINGi9606.ENSP00000378306.

Structurei

3D structure databases

ProteinModelPortaliP16298.
SMRiP16298. Positions 24-420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 310309CatalyticAdd
BLAST
Regioni256 – 2627Calcineurin B binding-site 1Sequence Analysis
Regioni305 – 3106Calcineurin B binding-site 2Sequence Analysis
Regioni401 – 42323Calmodulin-bindingSequence AnalysisAdd
BLAST
Regioni474 – 49623Inhibitory domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 2111Poly-ProAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
HOGENOMiHOG000172699.
HOVERGENiHBG002819.
InParanoidiP16298.
KOiK04348.
OMAiAHTTENH.
OrthoDBiEOG7BZVSC.
TreeFamiTF105557.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 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.

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

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.

« 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:January 31, 2005 - v2
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

Note: No experimental confirmation available.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei137 – 1371E → EHVLGTEDISINPHNNINE in isoform 2. 1 PublicationVSP_005096
Alternative sequencei395 – 3951D → DV in isoform 3 and isoform 4. 2 PublicationsVSP_043803
Alternative sequencei456 – 52469ATVEA…NHTAQ → GNDVMQLAVPQMDWGTPHSF ANNSHNACREFLLFFSSCLS S in isoform 2. 1 PublicationVSP_005097Add
BLAST
Alternative sequencei456 – 46510Missing in isoform 3. 1 PublicationVSP_012617

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, 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.
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]
UniGeneiHs.500067.

Genome annotation databases

EnsembliENST00000360663; ENSP00000353881; ENSG00000107758. [P16298-1]
ENST00000394828; ENSP00000378305; ENSG00000107758. [P16298-3]
ENST00000394829; ENSP00000378306; ENSG00000107758. [P16298-4]
GeneIDi5532.
KEGGihsa:5532.
UCSCiuc001jue.3. human. [P16298-1]
uc001juf.3. human. [P16298-4]
uc001jug.3. human. [P16298-3]
uc001jui.2. human. [P16298-2]

Polymorphism databases

DMDMi60659599.

Keywords - Coding sequence diversityi

Alternative splicing

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, 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.
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]
UniGeneiHs.500067.

3D structure databases

ProteinModelPortaliP16298.
SMRiP16298. Positions 24-420.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111524. 21 interactions.
DIPiDIP-52337N.
IntActiP16298. 7 interactions.
STRINGi9606.ENSP00000378306.

Chemistry

BindingDBiP16298.
ChEMBLiCHEMBL5278.

PTM databases

DEPODiP16298.
PhosphoSiteiP16298.

Polymorphism databases

DMDMi60659599.

Proteomic databases

MaxQBiP16298.
PaxDbiP16298.
PRIDEiP16298.

Protocols and materials databases

DNASUi5532.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360663; ENSP00000353881; ENSG00000107758. [P16298-1]
ENST00000394828; ENSP00000378305; ENSG00000107758. [P16298-3]
ENST00000394829; ENSP00000378306; ENSG00000107758. [P16298-4]
GeneIDi5532.
KEGGihsa:5532.
UCSCiuc001jue.3. human. [P16298-1]
uc001juf.3. human. [P16298-4]
uc001jug.3. human. [P16298-3]
uc001jui.2. human. [P16298-2]

Organism-specific databases

CTDi5532.
GeneCardsiGC10M075196.
HGNCiHGNC:9315. PPP3CB.
HPAiHPA008233.
MIMi114106. gene.
neXtProtiNX_P16298.
PharmGKBiPA33679.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
HOGENOMiHOG000172699.
HOVERGENiHBG002819.
InParanoidiP16298.
KOiK04348.
OMAiAHTTENH.
OrthoDBiEOG7BZVSC.
TreeFamiTF105557.

Enzyme and pathway databases

ReactomeiREACT_15334. DARPP-32 events.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_263982. Ca2+ pathway.

Miscellaneous databases

ChiTaRSiPPP3CB. human.
GeneWikiiPPP3CB.
GenomeRNAii5532.
NextBioi21430.
PROiP16298.
SOURCEiSearch...

Gene expression databases

BgeeiP16298.
CleanExiHS_PPP3CB.
ExpressionAtlasiP16298. baseline and differential.
GenevestigatoriP16298.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1988) [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(1990) [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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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(2003) [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(2008) [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].

Entry informationi

Entry nameiPP2BB_HUMAN
AccessioniPrimary (citable) accession number: P16298
Secondary accession number(s): P16299
, Q5F2F9, Q8N1F0, Q8N3W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1990
Last sequence update: January 31, 2005
Last modified: March 31, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.