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P62715

- PP2AB_MOUSE

UniProt

P62715 - PP2AB_MOUSE

Protein

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

Gene

Ppp2cb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase.

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi57 – 571Manganese 1By similarity
    Metal bindingi59 – 591Manganese 1By similarity
    Metal bindingi85 – 851Manganese 1By similarity
    Metal bindingi85 – 851Manganese 2By similarity
    Metal bindingi117 – 1171Manganese 2By similarity
    Active sitei118 – 1181Proton donorBy similarity
    Metal bindingi167 – 1671Manganese 2By similarity
    Metal bindingi241 – 2411Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: MGI
    3. protein serine/threonine phosphatase activity Source: Ensembl

    GO - Biological processi

    1. apoptotic mitochondrial changes Source: MGI
    2. negative regulation of Ras protein signal transduction Source: Ensembl
    3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
    4. protein dephosphorylation Source: Ensembl
    5. regulation of gene expression Source: MGI
    6. response to antibiotic Source: MGI
    7. response to endoplasmic reticulum stress Source: MGI
    8. response to hydrogen peroxide Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196577. MASTL Facilitates Mitotic Progression.
    REACT_198526. Spry regulation of FGF signaling.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_203336. Degradation of beta-catenin by the destruction complex.
    REACT_203795. DARPP-32 events.
    REACT_206803. Cyclin A/B1 associated events during G2/M transition.
    REACT_207679. Separation of Sister Chromatids.
    REACT_208887. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
    REACT_210064. ERKs are inactivated.
    REACT_215063. ERK/MAPK targets.
    REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_217323. Integration of energy metabolism.
    REACT_218396. Beta-catenin phosphorylation cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform (EC:3.1.3.16)
    Short name:
    PP2A-beta
    Gene namesi
    Name:Ppp2cb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1321161. Ppp2cb.

    Subcellular locationi

    Cytoplasm. Nucleus By similarity. Chromosomecentromere By similarity. Cytoplasmcytoskeletonspindle pole By similarity
    Note: In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles By similarity.By similarity

    GO - Cellular componenti

    1. chromosome, centromeric region Source: UniProtKB-SubCell
    2. cytoplasm Source: MGI
    3. nucleus Source: MGI
    4. protein phosphatase type 2A complex Source: MGI
    5. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi307 – 3071Y → Q: Loss of trimeric subunit ABC assembly. 1 Publication
    Mutagenesisi309 – 3091L → A: Loss of binding to PP2A B-alpha regulatory subunit. 1 Publication
    Mutagenesisi309 – 3091L → Q: Loss of trimeric subunit ABC assembly. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309Serine/threonine-protein phosphatase 2A catalytic subunit beta isoformPRO_0000058846Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei307 – 3071Phosphotyrosine1 Publication
    Modified residuei309 – 3091Leucine methyl esterBy similarity

    Post-translational modificationi

    Reversibly methyl esterified on Leu-309 by leucine carboxyl methyltransferase 1 (Lcmt1) and protein phosphatase methylesterase 1 (Ppme1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization By similarity.By similarity
    Phosphorylation of either threonine (by autophosphorylation-activated protein kinase) or tyrosine results in inactivation of the phosphatase. Auto-dephosphorylation has been suggested as a mechanism for reactivation By similarity.By similarity

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP62715.
    PaxDbiP62715.
    PRIDEiP62715.

    PTM databases

    PhosphoSiteiP62715.

    Expressioni

    Gene expression databases

    BgeeiP62715.
    GenevestigatoriP62715.

    Interactioni

    Subunit structurei

    PP2A consists of a common heterodimeric core enzyme (composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65) (subunit A)) that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Binds PPME1 By similarity. May indirectly interact with SGOL1, most probably through regulatory B56 subunits. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD By similarity. Interacts with CTTNBP2NL By similarity.By similarity

    Protein-protein interaction databases

    BioGridi202342. 11 interactions.
    IntActiP62715. 2 interactions.
    STRINGi10090.ENSMUSP00000009774.

    Structurei

    3D structure databases

    ProteinModelPortaliP62715.
    SMRiP62715. Positions 6-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00550000074618.
    HOGENOMiHOG000172696.
    HOVERGENiHBG000216.
    InParanoidiP62715.
    KOiK04382.
    OMAiRPPDYFL.
    OrthoDBiEOG74N5H2.
    PhylomeDBiP62715.
    TreeFamiTF105559.

    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.

    P62715-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDDKAFTKEL DQWVEQLNEC KQLNENQVRT LCEKAKEILT KESNVQEVRC    50
    PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL 100
    VALKVRYPER ITILRGNHES RQITQVYGFY DECLRKYGNA NVWKYFTDLF 150
    DYLPLTALVD GQIFCLHGGL SPSIDTLDHI RALDRLQEVP HEGPMCDLLW 200
    SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA HQLVMEGYNW 250
    CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV 300
    TRRTPDYFL 309
    Length:309
    Mass (Da):35,575
    Last modified:July 19, 2004 - v1
    Checksum:i51DA9EB0633FC191
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z67746 mRNA. Translation: CAA91559.1.
    BC058582 mRNA. Translation: AAH58582.1.
    CCDSiCCDS22233.1.
    RefSeqiNP_059070.1. NM_017374.3.
    UniGeneiMm.288765.
    Mm.29301.

    Genome annotation databases

    EnsembliENSMUST00000009774; ENSMUSP00000009774; ENSMUSG00000009630.
    GeneIDi19053.
    KEGGimmu:19053.
    UCSCiuc009lkd.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z67746 mRNA. Translation: CAA91559.1 .
    BC058582 mRNA. Translation: AAH58582.1 .
    CCDSi CCDS22233.1.
    RefSeqi NP_059070.1. NM_017374.3.
    UniGenei Mm.288765.
    Mm.29301.

    3D structure databases

    ProteinModelPortali P62715.
    SMRi P62715. Positions 6-293.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202342. 11 interactions.
    IntActi P62715. 2 interactions.
    STRINGi 10090.ENSMUSP00000009774.

    Chemistry

    BindingDBi P62715.

    PTM databases

    PhosphoSitei P62715.

    Proteomic databases

    MaxQBi P62715.
    PaxDbi P62715.
    PRIDEi P62715.

    Protocols and materials databases

    DNASUi 19053.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000009774 ; ENSMUSP00000009774 ; ENSMUSG00000009630 .
    GeneIDi 19053.
    KEGGi mmu:19053.
    UCSCi uc009lkd.1. mouse.

    Organism-specific databases

    CTDi 5516.
    MGIi MGI:1321161. Ppp2cb.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00550000074618.
    HOGENOMi HOG000172696.
    HOVERGENi HBG000216.
    InParanoidi P62715.
    KOi K04382.
    OMAi RPPDYFL.
    OrthoDBi EOG74N5H2.
    PhylomeDBi P62715.
    TreeFami TF105559.

    Enzyme and pathway databases

    Reactomei REACT_196577. MASTL Facilitates Mitotic Progression.
    REACT_198526. Spry regulation of FGF signaling.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_203336. Degradation of beta-catenin by the destruction complex.
    REACT_203795. DARPP-32 events.
    REACT_206803. Cyclin A/B1 associated events during G2/M transition.
    REACT_207679. Separation of Sister Chromatids.
    REACT_208887. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
    REACT_210064. ERKs are inactivated.
    REACT_215063. ERK/MAPK targets.
    REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_217323. Integration of energy metabolism.
    REACT_218396. Beta-catenin phosphorylation cascade.

    Miscellaneous databases

    ChiTaRSi PPP2CB. mouse.
    NextBioi 21334.
    PROi P62715.
    SOURCEi Search...

    Gene expression databases

    Bgeei P62715.
    Genevestigatori P62715.

    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. Goetz J.M., Kues W.
      Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6 X DBA/2.
      Tissue: Brain.
    2. "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].
      Strain: FVB/N-3.
      Tissue: Mammary gland.
    3. "Molecular cloning of a protein serine/threonine phosphatase containing a putative regulatory tetratricopeptide repeat domain."
      Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.
      J. Biol. Chem. 269:22586-22592(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-83.
    4. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 284-294, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    5. "Tyrosine phosphorylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts."
      Chen J., Parsons S., Brautigan D.L.
      J. Biol. Chem. 269:7957-7962(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-307.
    6. "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2."
      Chung H., Nairn A.C., Murata K., Brautigan D.L.
      Biochemistry 38:10371-10376(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-307 AND LEU-309.

    Entry informationi

    Entry nameiPP2AB_MOUSE
    AccessioniPrimary (citable) accession number: P62715
    Secondary accession number(s): P11082
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 92 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, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3