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P20651

- PP2BB_RAT

UniProt

P20651 - PP2BB_RAT

Protein

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

Gene

Ppp3cb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      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-dependent protein serine/threonine phosphatase activity Source: RGD
    2. calcium ion binding Source: UniProtKB
    3. calmodulin binding Source: RGD
    4. calmodulin-dependent protein phosphatase activity Source: UniProtKB
    5. drug binding Source: UniProtKB
    6. enzyme binding Source: UniProtKB
    7. protein binding Source: IntAct
    8. protein heterodimerization activity Source: RGD
    9. protein phosphatase 2B binding Source: UniProtKB
    10. protein serine/threonine phosphatase activity Source: Reactome

    GO - Biological processi

    1. calcium ion-dependent exocytosis Source: UniProtKB
    2. cellular response to drug Source: UniProtKB
    3. muscle cell cellular homeostasis Source: RGD
    4. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
    5. protein dephosphorylation Source: RGD
    6. protein phosphorylation Source: UniProtKB
    7. regulation of insulin secretion Source: UniProtKB
    8. response to amphetamine Source: RGD

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Calmodulin-binding, Iron, Metal-binding, Zinc

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3383. Ppp3cb.

    Subcellular locationi

    GO - Cellular componenti

    1. calcineurin complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. plasma membrane Source: UniProtKB
    4. protein complex Source: RGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 525524Serine/threonine-protein phosphatase 2B catalytic subunit beta isoformPRO_0000058827Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP20651.
    PRIDEiP20651.

    PTM databases

    PhosphoSiteiP20651.

    Expressioni

    Gene expression databases

    GenevestigatoriP20651.

    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
    Akap6Q9WVC72EBI-7400670,EBI-7559840

    Protein-protein interaction databases

    BioGridi246807. 1 interaction.
    DIPiDIP-66N.
    IntActiP20651. 4 interactions.
    MINTiMINT-4589009.
    STRINGi10116.ENSRNOP00000010476.

    Structurei

    3D structure databases

    ProteinModelPortaliP20651.
    SMRiP20651. Positions 24-381.
    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
    Regioni402 – 42423Calmodulin-bindingSequence AnalysisAdd
    BLAST
    Regioni475 – 49723Inhibitory domainAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi11 – 2010Poly-Pro

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172699.
    HOVERGENiHBG002819.
    InParanoidiP20651.
    KOiK04348.
    PhylomeDBiP20651.

    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]

    Sequencei

    Sequence statusi: Complete.

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

    P20651-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAPEPARAA PPPPPPPPPP LGADRVVKAV PFPPTHRLTS EEVFDMDGIP    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 EDQFDVGSAA 400
    ARKEIIRNKI RAIGKMARVF SVLREESESV LTLKGLTPTG MLPSGVLAGG 450
    RQTLQSATVE AIEAEKAIRG SSPPHRICSF EEAKGLDRIN ERMPPRKDAV 500
    QQDGFNSLNT AHTTENHGTG NHSAQ 525
    Length:525
    Mass (Da):59,113
    Last modified:February 1, 1991 - v1
    Checksum:i5E66AF3100BE3987
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31809 mRNA. Translation: AAA40848.1.
    D90036 mRNA. Translation: BAA14084.1.
    M58441 mRNA. Translation: AAA41915.1.
    PIRiA33794.
    RefSeqiNP_058738.1. NM_017042.2.
    UniGeneiRn.11063.

    Genome annotation databases

    GeneIDi24675.
    KEGGirno:24675.
    UCSCiRGD:3383. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31809 mRNA. Translation: AAA40848.1 .
    D90036 mRNA. Translation: BAA14084.1 .
    M58441 mRNA. Translation: AAA41915.1 .
    PIRi A33794.
    RefSeqi NP_058738.1. NM_017042.2.
    UniGenei Rn.11063.

    3D structure databases

    ProteinModelPortali P20651.
    SMRi P20651. Positions 24-381.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246807. 1 interaction.
    DIPi DIP-66N.
    IntActi P20651. 4 interactions.
    MINTi MINT-4589009.
    STRINGi 10116.ENSRNOP00000010476.

    PTM databases

    PhosphoSitei P20651.

    Proteomic databases

    PaxDbi P20651.
    PRIDEi P20651.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24675.
    KEGGi rno:24675.
    UCSCi RGD:3383. rat.

    Organism-specific databases

    CTDi 5532.
    RGDi 3383. Ppp3cb.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172699.
    HOVERGENi HBG002819.
    InParanoidi P20651.
    KOi K04348.
    PhylomeDBi P20651.

    Miscellaneous databases

    NextBioi 604059.

    Gene expression databases

    Genevestigatori P20651.

    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. "Evidence for a second isoform of the catalytic subunit of calmodulin-dependent protein phosphatase (calcineurin A)."
      Kuno T., Takeda T., Hirai M., Ito A., Mukai H., Tanaka C.
      Biochem. Biophys. Res. Commun. 165:1352-1358(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Multiplicity of protein serine-threonine phosphatases in PC12 pheochromocytoma and FTO-2B hepatoma cells."
      Wadzinski B.E., Heasley L.E., Johnson G.L.
      J. Biol. Chem. 265:21504-21508(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 245-315.

    Entry informationi

    Entry nameiPP2BB_RAT
    AccessioniPrimary (citable) accession number: P20651
    Secondary accession number(s): Q6LDJ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3