Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P67775

- PP2AA_HUMAN

UniProt

P67775 - PP2AA_HUMAN

Protein

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

Gene

PPP2CA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGOL2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I By similarity. Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259'.By similarity3 Publications

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.1 Publication

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. ceramide metabolic process Source: UniProtKB
    3. fibroblast growth factor receptor signaling pathway Source: Reactome
    4. gene expression Source: Reactome
    5. inactivation of MAPK activity Source: UniProtKB
    6. meiotic nuclear division Source: UniProtKB-KW
    7. mesoderm development Source: Ensembl
    8. mitotic cell cycle Source: Reactome
    9. mitotic nuclear envelope reassembly Source: Reactome
    10. mRNA metabolic process Source: Reactome
    11. negative regulation of cell growth Source: UniProtKB
    12. negative regulation of epithelial to mesenchymal transition Source: BHF-UCL
    13. negative regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
    14. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    15. positive regulation of protein serine/threonine kinase activity Source: BHF-UCL
    16. protein dephosphorylation Source: UniProtKB
    17. protein heterotrimerization Source: Ensembl
    18. regulation of cell adhesion Source: UniProtKB
    19. regulation of cell differentiation Source: UniProtKB
    20. regulation of DNA replication Source: UniProtKB
    21. regulation of growth Source: UniProtKB
    22. regulation of protein autophosphorylation Source: Ensembl
    23. regulation of protein catabolic process Source: Ensembl
    24. regulation of receptor activity Source: Ensembl
    25. regulation of transcription, DNA-templated Source: UniProtKB
    26. regulation of Wnt signaling pathway Source: UniProtKB
    27. response to organic substance Source: UniProtKB
    28. RNA metabolic process Source: Reactome
    29. RNA splicing Source: UniProtKB
    30. second-messenger-mediated signaling Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Meiosis

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03696-MONOMER.
    ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_111080. Spry regulation of FGF signaling.
    REACT_12436. ERKs are inactivated.
    REACT_12599. ERK/MAPK targets.
    REACT_1383. Glycolysis.
    REACT_150182. MASTL Facilitates Mitotic Progression.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_1505. Integration of energy metabolism.
    REACT_15334. DARPP-32 events.
    REACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_23879. Platelet sensitization by LDL.
    REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
    REACT_682. Mitotic Prometaphase.
    REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_821. Cyclin D associated events in G1.
    SignaLinkiP67775.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (EC:3.1.3.16)
    Short name:
    PP2A-alpha
    Alternative name(s):
    Replication protein C
    Short name:
    RP-C
    Gene namesi
    Name:PPP2CA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:9299. PPP2CA.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. Chromosomecentromere 1 Publication. Cytoplasmcytoskeletonspindle pole 1 Publication
    Note: In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. Centromeric localization requires the presence of SGOL2 By similarity.By similarity

    GO - Cellular componenti

    1. chromosome, centromeric region Source: UniProtKB-SubCell
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. microtubule cytoskeleton Source: UniProtKB
    6. mitochondrion Source: UniProtKB
    7. nucleus Source: UniProtKB
    8. plasma membrane Source: Ensembl
    9. protein phosphatase type 2A complex Source: UniProtKB
    10. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

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

    Organism-specific databases

    PharmGKBiPA33663.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoformPRO_0000058839Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei307 – 3071Phosphotyrosine
    Modified residuei309 – 3091Leucine methyl ester1 Publication

    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.1 Publication
    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.

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP67775.
    PaxDbiP67775.
    PRIDEiP67775.

    PTM databases

    PhosphoSiteiP67775.

    Expressioni

    Gene expression databases

    ArrayExpressiP67775.
    BgeeiP67775.
    CleanExiHS_PPP2CA.
    GenevestigatoriP67775.

    Organism-specific databases

    HPAiCAB003848.

    Interactioni

    Subunit structurei

    PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or 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. Interacts with NXN; the interaction is direct By similarity. Interacts with TP53, SGOL1 and SGOL2. Interacts with AXIN1; the interaction dephosphorylates AXIN1. Interacts with PIM3; this interaction promotes dephosphorylation, ubiquitination and proteasomal degradation of PIM3. Interacts with RAF1. Interaction with IGBP1 protects unassembled PPP2CA from degradative ubiquitination. Interacts with GSK3B (via C2 domain).By similarity13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AKT1P317495EBI-712311,EBI-296087
    ANP32AP396872EBI-712311,EBI-359234
    E7P031293EBI-712311,EBI-866453From a different organism.
    E7P040202EBI-712311,EBI-7005254From a different organism.
    IER3P466952EBI-712311,EBI-1748945
    IGBP1P7831810EBI-712311,EBI-1055954
    Igbp1Q612493EBI-712311,EBI-7002233From a different organism.
    IKBKBO149203EBI-712311,EBI-81266
    IKBKGQ9Y6K94EBI-712311,EBI-81279
    KISS1RQ969F83EBI-712311,EBI-8481408
    NxnP973462EBI-712311,EBI-309684From a different organism.
    PPP2R1AP3015314EBI-712311,EBI-302388
    PPP2R1BP301547EBI-712311,EBI-357094
    PPP2R2CQ9Y2T43EBI-712311,EBI-1774058
    PPP2R5AQ151723EBI-712311,EBI-641666
    PPP2R5BQ151734EBI-712311,EBI-1369497
    PPP2R5CQ133627EBI-712311,EBI-1266156
    RBL1P287492EBI-712311,EBI-971402
    RBL2Q089992EBI-712311,EBI-971439
    RELAQ042064EBI-712311,EBI-73886
    STRNO438153EBI-712311,EBI-1046642
    TIPRLO756633EBI-712311,EBI-1054735
    TRIP13Q156453EBI-712311,EBI-358993

    Protein-protein interaction databases

    BioGridi111507. 159 interactions.
    DIPiDIP-29395N.
    IntActiP67775. 115 interactions.
    MINTiMINT-215645.
    STRINGi9606.ENSP00000418447.

    Structurei

    Secondary structure

    1
    309
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1816
    Helixi25 – 3915
    Beta strandi44 – 485
    Beta strandi50 – 556
    Helixi62 – 7211
    Turni75 – 773
    Beta strandi80 – 823
    Beta strandi87 – 915
    Helixi93 – 10614
    Turni108 – 1103
    Beta strandi111 – 1133
    Helixi121 – 1277
    Helixi129 – 1379
    Beta strandi138 – 1403
    Helixi141 – 15010
    Beta strandi155 – 1595
    Turni160 – 1623
    Beta strandi163 – 1686
    Helixi177 – 1826
    Beta strandi186 – 1883
    Beta strandi191 – 1933
    Helixi194 – 2007
    Beta strandi205 – 2117
    Beta strandi215 – 2206
    Helixi222 – 23211
    Beta strandi235 – 2395
    Beta strandi247 – 2515
    Turni252 – 2554
    Beta strandi256 – 2594
    Helixi265 – 2673
    Beta strandi273 – 2786
    Beta strandi284 – 2896

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IAEX-ray3.50C/F1-309[»]
    2IE3X-ray2.80C1-309[»]
    2IE4X-ray2.60C1-309[»]
    2NPPX-ray3.30C/F1-309[»]
    2NYLX-ray3.80C/F2-294[»]
    2NYMX-ray3.60C/F2-294[»]
    3C5WX-ray2.80C1-309[»]
    3DW8X-ray2.85C/F1-309[»]
    3FGAX-ray2.70C1-309[»]
    3K7VX-ray2.85C1-309[»]
    3K7WX-ray2.96C1-309[»]
    3P71X-ray2.70C1-309[»]
    4I5LX-ray2.43C/F1-309[»]
    4I5NX-ray2.80C/F1-309[»]
    4IYPX-ray2.80C6-153[»]
    4LACX-ray2.82C1-309[»]
    ProteinModelPortaliP67775.
    SMRiP67775. Positions 2-296.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP67775.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172696.
    HOVERGENiHBG000216.
    InParanoidiP67775.
    KOiK04382.
    OMAiQVKTLCD.
    OrthoDBiEOG74N5H2.
    PhylomeDBiP67775.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P67775-1) [UniParc]FASTAAdd to Basket

    Also known as: PP2Acalpha1

    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

    MDEKVFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC    50
    PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL 100
    VALKVRYRER 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):35,594
    Last modified:October 11, 2004 - v1
    Checksum:iC602291F78F34555
    GO
    Isoform 2 (identifier: P67775-2) [UniParc]FASTAAdd to Basket

    Also known as: PP2Acalpha2

    The sequence of this isoform differs from the canonical sequence as follows:
         193-246: Missing.

    Note: Catalytically inactive, shows enhanced binding to IGBP1, and does not interact with the scaffolding subunit PPP2R1A.

    Show »
    Length:255
    Mass (Da):29,735
    Checksum:iB50450F64CB286AB
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti52 – 521V → A.
    Corresponds to variant rs11552681 [ dbSNP | Ensembl ].
    VAR_051735

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei193 – 24654Missing in isoform 2. CuratedVSP_044320Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12646 mRNA. Translation: CAA31176.1.
    J03804 mRNA. Translation: AAB38019.1.
    M60483 Genomic DNA. Translation: AAA36466.1.
    BC000400 mRNA. Translation: AAH00400.1.
    BC002657 mRNA. Translation: AAH02657.1.
    BC019275 mRNA. Translation: AAH19275.1.
    BC031696 mRNA. Translation: AAH31696.1.
    CCDSiCCDS4173.1. [P67775-1]
    PIRiS01986. PAHU2A.
    RefSeqiNP_002706.1. NM_002715.2. [P67775-1]
    UniGeneiHs.105818.

    Genome annotation databases

    EnsembliENST00000481195; ENSP00000418447; ENSG00000113575. [P67775-1]
    GeneIDi5515.
    KEGGihsa:5515.
    UCSCiuc003kze.3. human. [P67775-1]

    Polymorphism databases

    DMDMi54038809.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12646 mRNA. Translation: CAA31176.1 .
    J03804 mRNA. Translation: AAB38019.1 .
    M60483 Genomic DNA. Translation: AAA36466.1 .
    BC000400 mRNA. Translation: AAH00400.1 .
    BC002657 mRNA. Translation: AAH02657.1 .
    BC019275 mRNA. Translation: AAH19275.1 .
    BC031696 mRNA. Translation: AAH31696.1 .
    CCDSi CCDS4173.1. [P67775-1 ]
    PIRi S01986. PAHU2A.
    RefSeqi NP_002706.1. NM_002715.2. [P67775-1 ]
    UniGenei Hs.105818.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IAE X-ray 3.50 C/F 1-309 [» ]
    2IE3 X-ray 2.80 C 1-309 [» ]
    2IE4 X-ray 2.60 C 1-309 [» ]
    2NPP X-ray 3.30 C/F 1-309 [» ]
    2NYL X-ray 3.80 C/F 2-294 [» ]
    2NYM X-ray 3.60 C/F 2-294 [» ]
    3C5W X-ray 2.80 C 1-309 [» ]
    3DW8 X-ray 2.85 C/F 1-309 [» ]
    3FGA X-ray 2.70 C 1-309 [» ]
    3K7V X-ray 2.85 C 1-309 [» ]
    3K7W X-ray 2.96 C 1-309 [» ]
    3P71 X-ray 2.70 C 1-309 [» ]
    4I5L X-ray 2.43 C/F 1-309 [» ]
    4I5N X-ray 2.80 C/F 1-309 [» ]
    4IYP X-ray 2.80 C 6-153 [» ]
    4LAC X-ray 2.82 C 1-309 [» ]
    ProteinModelPortali P67775.
    SMRi P67775. Positions 2-296.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111507. 159 interactions.
    DIPi DIP-29395N.
    IntActi P67775. 115 interactions.
    MINTi MINT-215645.
    STRINGi 9606.ENSP00000418447.

    Chemistry

    BindingDBi P67775.
    ChEMBLi CHEMBL4703.
    DrugBanki DB00163. Vitamin E.

    PTM databases

    PhosphoSitei P67775.

    Polymorphism databases

    DMDMi 54038809.

    Proteomic databases

    MaxQBi P67775.
    PaxDbi P67775.
    PRIDEi P67775.

    Protocols and materials databases

    DNASUi 5515.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000481195 ; ENSP00000418447 ; ENSG00000113575 . [P67775-1 ]
    GeneIDi 5515.
    KEGGi hsa:5515.
    UCSCi uc003kze.3. human. [P67775-1 ]

    Organism-specific databases

    CTDi 5515.
    GeneCardsi GC05M133530.
    HGNCi HGNC:9299. PPP2CA.
    HPAi CAB003848.
    MIMi 176915. gene.
    neXtProti NX_P67775.
    PharmGKBi PA33663.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172696.
    HOVERGENi HBG000216.
    InParanoidi P67775.
    KOi K04382.
    OMAi QVKTLCD.
    OrthoDBi EOG74N5H2.
    PhylomeDBi P67775.
    TreeFami TF105559.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03696-MONOMER.
    Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_111080. Spry regulation of FGF signaling.
    REACT_12436. ERKs are inactivated.
    REACT_12599. ERK/MAPK targets.
    REACT_1383. Glycolysis.
    REACT_150182. MASTL Facilitates Mitotic Progression.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_1505. Integration of energy metabolism.
    REACT_15334. DARPP-32 events.
    REACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_23879. Platelet sensitization by LDL.
    REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
    REACT_682. Mitotic Prometaphase.
    REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_821. Cyclin D associated events in G1.
    SignaLinki P67775.

    Miscellaneous databases

    EvolutionaryTracei P67775.
    GeneWikii PPP2CA.
    GenomeRNAii 5515.
    NextBioi 21330.
    PROi P67775.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P67775.
    Bgeei P67775.
    CleanExi HS_PPP2CA.
    Genevestigatori P67775.

    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. "The nucleotide sequence of the cDNA encoding the human lung protein phosphatase 2A alpha catalytic subunit."
      Stone S.R., Mayer R., Wernet W., Maurer F., Hofsteenge J., Hemmings B.A.
      Nucleic Acids Res. 16:11365-11365(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fibroblast.
    2. "Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes."
      Arino J., Woon C.W., Brautigan D.L., Miller T.B. Jr., Johnson G.L.
      Proc. Natl. Acad. Sci. U.S.A. 85:4252-4256(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "Structure and transcriptional regulation of protein phosphatase 2A catalytic subunit genes."
      Khew-Goodall Y., Mayer R.E., Maurer F., Stone S.R., Hemmings B.A.
      Biochemistry 30:89-97(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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 1).
      Tissue: Lung, Placenta and Uterus.
    5. "Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: inhibition by small-t antigen."
      Scheidtmann K.H., Mumby M.C., Rundell K., Walter G.
      Mol. Cell. Biol. 11:1996-2003(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEPHOSPHORYLATION OF SV40 LARGE-T ANTIGEN AND P53 PROTEIN.
    6. "The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo."
      Favre B., Zolnierowicz S., Turowski P., Hemmings B.A.
      J. Biol. Chem. 269:16311-16317(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LEU-309.
    7. "Alpha 4 associates with protein phosphatases 2A, 4, and 6."
      Chen J., Peterson R.T., Schreiber S.L.
      Biochem. Biophys. Res. Commun. 247:827-832(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGBP1.
    8. "Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Balpha subunit."
      Bryant J.C., Westphal R.S., Wadzinski B.E.
      Biochem. J. 339:241-246(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LEU-309.
    9. "Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A."
      Virshup D.M., Kauffman M.G., Kelly T.J.
      EMBO J. 8:3891-3898(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, ACTIVATION OF SV40 REPLICATION.
    10. "Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain."
      Hsu W., Zeng L., Costantini F.
      J. Biol. Chem. 274:3439-3445(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AXIN1, FUNCTION.
    11. "Raf-1-associated protein phosphatase 2A as a positive regulator of kinase activation."
      Abraham D., Podar K., Pacher M., Kubicek M., Welzel N., Hemmings B.A., Dilworth S.M., Mischak H., Kolch W., Baccarini M.
      J. Biol. Chem. 275:22300-22304(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RAF1.
    12. "PP2A is required for centromeric localization of Sgo1 and proper chromosome segregation."
      Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.
      Dev. Cell 10:575-585(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SGOL1.
    13. "Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
      Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
      Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SGOL1.
    14. "Protein phosphatase 2A regulates the stability of Pim protein kinases."
      Losman J.A., Chen X.P., Vuong B.Q., Fay S., Rothman P.B.
      J. Biol. Chem. 278:4800-4805(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIM3.
    15. "A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced dephosphorylation of p53 at Thr55."
      Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.
      EMBO J. 26:402-411(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP53.
    16. "Tripin/hSgo2 recruits MCAK to the inner centromere to correct defective kinetochore attachments."
      Huang H., Feng J., Famulski J., Rattner J.B., Liu S.T., Kao G.D., Muschel R., Chan G.K., Yen T.J.
      J. Cell Biol. 177:413-424(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SGOL2.
    17. "Alpha4 is an essential regulator of PP2A phosphatase activity."
      Kong M., Ditsworth D., Lindsten T., Thompson C.B.
      Mol. Cell 36:51-60(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGBP1.
    18. "Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination."
      McConnell J.L., Watkins G.R., Soss S.E., Franz H.S., McCorvey L.R., Spiller B.W., Chazin W.J., Wadzinski B.E.
      Biochemistry 49:1713-1718(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGBP1.
    19. "Role of DAB2IP in modulating epithelial-to-mesenchymal transition and prostate cancer metastasis."
      Xie D., Gore C., Liu J., Pong R.C., Mason R., Hao G., Long M., Kabbani W., Yu L., Zhang H., Chen H., Sun X., Boothman D.A., Min W., Hsieh J.T.
      Proc. Natl. Acad. Sci. U.S.A. 107:2485-2490(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GSK3B.
    20. "Identification and characterization of an alternatively spliced isoform of the human protein phosphatase 2Aalpha catalytic subunit."
      Migueleti D.L., Smetana J.H., Nunes H.F., Kobarg J., Zanchin N.I.
      J. Biol. Chem. 287:4853-4862(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2).
    21. "Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit alpha4, altering PP2A stability and microtubule-associated protein phosphorylation."
      Watkins G.R., Wang N., Mazalouskas M.D., Gomez R.J., Guthrie C.R., Kraemer B.C., Schweiger S., Spiller B.W., Wadzinski B.E.
      J. Biol. Chem. 287:24207-24215(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins."
      Xing Y., Xu Y., Chen Y., Jeffrey P.D., Chao Y., Lin Z., Li Z., Strack S., Stock J.B., Shi Y.
      Cell 127:341-353(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, COFACTOR.
    23. "Structural mechanism of demethylation and inactivation of protein phosphatase 2A."
      Xing Y., Li Z., Chen Y., Stock J.B., Jeffrey P.D., Shi Y.
      Cell 133:154-163(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PPP2R1A AND PPME1.

    Entry informationi

    Entry nameiPP2AA_HUMAN
    AccessioniPrimary (citable) accession number: P67775
    Secondary accession number(s): P05323, P13197
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3