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P16298

- PP2BB_HUMAN

UniProt

P16298 - PP2BB_HUMAN

Protein

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

Gene

PPP3CB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (01 Feb 2005)
      Previous versions | rss
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    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

    Binds 1 Fe3+ ion per subunit.By similarity
    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 binding Source: IntAct
    7. protein dimerization activity Source: UniProtKB
    8. protein phosphatase 2B binding Source: UniProtKB
    9. protein serine/threonine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. axon extension Source: UniProtKB
    2. calcium ion-dependent exocytosis Source: UniProtKB
    3. cellular response to drug Source: UniProtKB
    4. dephosphorylation Source: UniProtKB
    5. Fc-epsilon receptor signaling pathway Source: Reactome
    6. heart development Source: Ensembl
    7. innate immune response Source: Reactome
    8. learning Source: UniProtKB
    9. memory Source: UniProtKB
    10. negative regulation of T cell mediated cytotoxicity Source: Ensembl
    11. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
    12. positive regulation of transcription, DNA-templated Source: UniProtKB
    13. protein dephosphorylation Source: UniProtKB
    14. protein phosphorylation Source: UniProtKB
    15. regulation of insulin secretion Source: UniProtKB
    16. regulation of synaptic plasticity Source: UniProtKB
    17. response to cytokine Source: Ensembl
    18. signal transduction Source: UniProtKB
    19. social behavior Source: UniProtKB
    20. T cell activation Source: UniProtKB
    21. T cell differentiation Source: Ensembl
    22. T cell homeostasis Source: Ensembl
    23. T cell proliferation Source: UniProtKB

    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_172761. 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: 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

    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

    PhosphoSiteiP16298.

    Expressioni

    Gene expression databases

    ArrayExpressiP16298.
    BgeeiP16298.
    CleanExiHS_PPP3CB.
    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. 13 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.
    HOGENOMiHOG000172699.
    HOVERGENiHBG002819.
    KOiK04348.
    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. Align

    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

    MAAPEPARAA PPPPPPPPPP PGADRVVKAV PFPPTHRLTS EEVFDLDGIP    50
    RVDVLKNHLV KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI 100
    HGQFFDLMKL FEVGGSPANT RYLFLGDYVD RGYFSIECVL YLWVLKILYP 150
    STLFLLRGNH ECRHLTEYFT FKQECKIKYS ERVYEACMEA FDSLPLAALL 200
    NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL WSDPSEDFGN 250
    EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY 300
    RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY 350
    WLPNFMDVFT WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDGSAAA 400
    RKEIIRNKIR AIGKMARVFS VLREESESVL TLKGLTPTGM LPSGVLAGGR 450
    QTLQSATVEA IEAEKAIRGF SPPHRICSFE EAKGLDRINE RMPPRKDAVQ 500
    QDGFNSLNTA HATENHGTGN HTAQ 524
    Length:524
    Mass (Da):59,024
    Last modified:February 1, 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS44436.1. [P16298-3 ]
    CCDS44437.1. [P16298-4 ]
    CCDS7328.1. [P16298-1 ]
    PIRi A36222.
    B36222.
    RefSeqi NP_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 ]
    UniGenei Hs.500067.

    3D structure databases

    ProteinModelPortali P16298.
    SMRi P16298. Positions 24-420.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111524. 13 interactions.
    DIPi DIP-52337N.
    IntActi P16298. 7 interactions.
    STRINGi 9606.ENSP00000378306.

    Chemistry

    BindingDBi P16298.
    ChEMBLi CHEMBL5278.

    PTM databases

    PhosphoSitei P16298.

    Polymorphism databases

    DMDMi 60659599.

    Proteomic databases

    MaxQBi P16298.
    PaxDbi P16298.
    PRIDEi P16298.

    Protocols and materials databases

    DNASUi 5532.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360663 ; ENSP00000353881 ; ENSG00000107758 . [P16298-1 ]
    ENST00000394828 ; ENSP00000378305 ; ENSG00000107758 . [P16298-3 ]
    ENST00000394829 ; ENSP00000378306 ; ENSG00000107758 . [P16298-4 ]
    GeneIDi 5532.
    KEGGi hsa:5532.
    UCSCi uc001jue.3. human. [P16298-1 ]
    uc001juf.3. human. [P16298-4 ]
    uc001jug.3. human. [P16298-3 ]
    uc001jui.2. human. [P16298-2 ]

    Organism-specific databases

    CTDi 5532.
    GeneCardsi GC10M075196.
    HGNCi HGNC:9315. PPP3CB.
    HPAi HPA008233.
    MIMi 114106. gene.
    neXtProti NX_P16298.
    PharmGKBi PA33679.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172699.
    HOVERGENi HBG002819.
    KOi K04348.
    OrthoDBi EOG7BZVSC.
    TreeFami TF105557.

    Enzyme and pathway databases

    Reactomei REACT_15334. DARPP-32 events.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_172761. Ca2+ pathway.

    Miscellaneous databases

    ChiTaRSi PPP3CB. human.
    GeneWikii PPP3CB.
    GenomeRNAii 5532.
    NextBioi 21430.
    PROi P16298.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16298.
    Bgeei P16298.
    CleanExi HS_PPP3CB.
    Genevestigatori P16298.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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].

    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: August 1, 1990
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 118 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