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P30153

- 2AAA_HUMAN

UniProt

P30153 - 2AAA_HUMAN

Protein

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Gene

PPP2R1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 4 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Required for proper chromosome segregation and for centromeric localization of SGOL1 in mitosis.1 Publication

    GO - Molecular functioni

    1. antigen binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein heterodimerization activity Source: UniProtKB
    4. protein phosphatase type 2A regulator activity Source: UniProtKB
    5. protein serine/threonine phosphatase activity Source: Ensembl

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. ceramide metabolic process Source: UniProtKB
    3. chromosome segregation Source: UniProtKB
    4. fibroblast growth factor receptor signaling pathway Source: Reactome
    5. G2/M transition of mitotic cell cycle Source: Reactome
    6. gene expression Source: Reactome
    7. inactivation of MAPK activity Source: UniProtKB
    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 tyrosine phosphorylation of Stat3 protein Source: UniProtKB
    13. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    14. peptidyl-serine dephosphorylation Source: Ensembl
    15. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    16. protein complex assembly Source: UniProtKB
    17. protein dephosphorylation Source: UniProtKB
    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 transcription, DNA-templated Source: UniProtKB
    23. regulation of Wnt signaling pathway Source: UniProtKB
    24. response to organic substance Source: UniProtKB
    25. RNA metabolic process Source: Reactome
    26. RNA splicing Source: UniProtKB
    27. second-messenger-mediated signaling Source: UniProtKB

    Keywords - Biological processi

    Chromosome partition

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000105568-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_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15334. DARPP-32 events.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    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.
    SignaLinkiP30153.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
    Alternative name(s):
    Medium tumor antigen-associated 61 kDa protein
    PP2A subunit A isoform PR65-alpha
    PP2A subunit A isoform R1-alpha
    Gene namesi
    Name:PPP2R1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9302. PPP2R1A.

    Subcellular locationi

    Cytoplasm By similarity. Chromosomecentromere 1 Publication
    Note: Centromeric localization requires the presence of BUB1.

    GO - Cellular componenti

    1. chromosome, centromeric region Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. membrane Source: UniProtKB
    4. microtubule cytoskeleton Source: UniProtKB
    5. mitochondrion Source: UniProtKB
    6. nucleus Source: UniProtKB
    7. protein phosphatase type 2A complex Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33666.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 589588Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoformPRO_0000071400Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei280 – 2801N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP30153.
    PaxDbiP30153.
    PRIDEiP30153.

    2D gel databases

    OGPiP30153.
    REPRODUCTION-2DPAGEIPI00554737.

    PTM databases

    PhosphoSiteiP30153.

    Miscellaneous databases

    PMAP-CutDBP30153.

    Expressioni

    Gene expression databases

    ArrayExpressiP30153.
    BgeeiP30153.
    CleanExiHS_PPP2R1A.
    GenevestigatoriP30153.

    Organism-specific databases

    HPAiCAB018599.

    Interactioni

    Subunit structurei

    Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphoylation sites By similarity. 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 IPO9. Interacts with TP53 and SGOL1. Interacts with PLA2G16; this interaction might decrease PP2A activity. Interacts with CTTNBP2NL.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P030813EBI-302388,EBI-1266256From a different organism.
    AKT1P317492EBI-302388,EBI-296087
    E7P031293EBI-302388,EBI-866453From a different organism.
    E7P040202EBI-302388,EBI-7005254From a different organism.
    KIAA1524Q8TCG14EBI-302388,EBI-1379376
    NxnP973462EBI-302388,EBI-309684From a different organism.
    PLA2G16P538167EBI-302388,EBI-746318
    PPP2CAP6777514EBI-302388,EBI-712311
    PPP2R2AP631518EBI-302388,EBI-1048931
    PPP2R2BQ000055EBI-302388,EBI-1052159
    PPP2R5AQ151723EBI-302388,EBI-641666
    PPP2R5CQ133626EBI-302388,EBI-1266156
    PPP2R5CQ13362-15EBI-302388,EBI-1266170
    PPP2R5CQ13362-22EBI-302388,EBI-1266173
    Ppp2r5cQ60996-32EBI-302388,EBI-1369292From a different organism.
    PPP2R5DQ147384EBI-302388,EBI-396563
    PPP2R5EQ165373EBI-302388,EBI-968374
    PPP4CP605103EBI-302388,EBI-1046072
    PPP5CP530413EBI-302388,EBI-716663
    RELAQ042062EBI-302388,EBI-73886
    STRNO438154EBI-302388,EBI-1046642
    TP53P046373EBI-302388,EBI-366083

    Protein-protein interaction databases

    BioGridi111510. 139 interactions.
    DIPiDIP-29394N.
    IntActiP30153. 116 interactions.
    MINTiMINT-1141071.
    STRINGi9606.ENSP00000324804.

    Structurei

    Secondary structure

    1
    589
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni6 – 83
    Helixi11 – 199
    Helixi25 – 339
    Helixi35 – 417
    Helixi44 – 496
    Helixi51 – 577
    Helixi63 – 7311
    Helixi78 – 803
    Helixi83 – 897
    Helixi90 – 967
    Beta strandi99 – 1013
    Helixi102 – 11615
    Helixi121 – 1266
    Helixi128 – 1369
    Beta strandi138 – 1403
    Helixi141 – 1477
    Helixi148 – 1503
    Helixi151 – 1544
    Turni155 – 1573
    Helixi160 – 17415
    Helixi179 – 19416
    Helixi198 – 2036
    Helixi205 – 2139
    Helixi218 – 2214
    Helixi224 – 23411
    Helixi237 – 2393
    Helixi240 – 2434
    Helixi245 – 2528
    Helixi257 – 2659
    Helixi267 – 2748
    Helixi276 – 2816
    Helixi283 – 2919
    Helixi296 – 31116
    Turni315 – 3173
    Helixi318 – 3247
    Helixi326 – 3349
    Helixi339 – 3468
    Helixi349 – 3524
    Helixi353 – 3564
    Helixi358 – 3647
    Helixi366 – 3738
    Helixi378 – 3858
    Helixi389 – 3946
    Helixi397 – 41216
    Helixi417 – 43418
    Helixi436 – 4383
    Helixi441 – 4499
    Helixi450 – 4523
    Helixi456 – 47318
    Helixi475 – 4817
    Helixi483 – 4886
    Turni489 – 4913
    Helixi495 – 52026
    Helixi522 – 5276
    Helixi528 – 5303
    Helixi534 – 54714
    Helixi548 – 5503
    Helixi553 – 56715
    Helixi573 – 58513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B3UX-ray2.30A/B2-589[»]
    2IE3X-ray2.80A1-589[»]
    2IE4X-ray2.60A1-589[»]
    2NPPX-ray3.30A/D1-589[»]
    2NYLX-ray3.80A/D8-589[»]
    2NYMX-ray3.60A/D8-589[»]
    2PKGX-ray3.30A/B10-589[»]
    3C5WX-ray2.80A9-589[»]
    3DW8X-ray2.85A/D9-589[»]
    3K7VX-ray2.85A1-589[»]
    3K7WX-ray2.96A1-589[»]
    4I5LX-ray2.43A/D6-589[»]
    4I5NX-ray2.80A/D6-589[»]
    4LACX-ray2.82A404-589[»]
    ProteinModelPortaliP30153.
    SMRiP30153. Positions 2-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30153.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati8 – 4639HEAT 1Add
    BLAST
    Repeati47 – 8438HEAT 2Add
    BLAST
    Repeati85 – 12339HEAT 3Add
    BLAST
    Repeati124 – 16138HEAT 4Add
    BLAST
    Repeati162 – 20039HEAT 5Add
    BLAST
    Repeati201 – 23939HEAT 6Add
    BLAST
    Repeati240 – 27839HEAT 7Add
    BLAST
    Repeati279 – 32143HEAT 8Add
    BLAST
    Repeati322 – 36039HEAT 9Add
    BLAST
    Repeati361 – 39939HEAT 10Add
    BLAST
    Repeati400 – 43839HEAT 11Add
    BLAST
    Repeati439 – 47739HEAT 12Add
    BLAST
    Repeati478 – 51639HEAT 13Add
    BLAST
    Repeati517 – 55539HEAT 14Add
    BLAST
    Repeati556 – 58934HEAT 15Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni8 – 399392PP2A subunit B bindingAdd
    BLAST
    Regioni47 – 321275Polyoma small and medium T antigens BindingAdd
    BLAST
    Regioni85 – 239155SV40 small T antigen bindingAdd
    BLAST
    Regioni400 – 589190PP2A subunit C bindingAdd
    BLAST

    Domaini

    Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure.

    Sequence similaritiesi

    Contains 15 HEAT repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG247268.
    HOGENOMiHOG000078539.
    HOVERGENiHBG000011.
    InParanoidiP30153.
    KOiK03456.
    OMAiRNLCQDD.
    OrthoDBiEOG764722.
    PhylomeDBiP30153.
    TreeFamiTF105552.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000357. HEAT.
    IPR021133. HEAT_type_2.
    [Graphical view]
    PfamiPF02985. HEAT. 2 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS50077. HEAT_REPEAT. 11 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P30153-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE    50
    LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE 100
    ETVVRDKAVE SLRAISHEHS PSDLEAHFVP LVKRLAGGDW FTSRTSACGL 150
    FSVCYPRVSS AVKAELRQYF RNLCSDDTPM VRRAAASKLG EFAKVLELDN 200
    VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL EALVMPTLRQ 250
    AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA 300
    AASHKVKEFC ENLSADCREN VIMSQILPCI KELVSDANQH VKSALASVIM 350
    GLSPILGKDN TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL 400
    SQSLLPAIVE LAEDAKWRVR LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW 450
    LVDHVYAIRE AATSNLKKLV EKFGKEWAHA TIIPKVLAMS GDPNYLHRMT 500
    TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV AKSLQKIGPI 550
    LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA 589
    Length:589
    Mass (Da):65,309
    Last modified:April 3, 2007 - v4
    Checksum:i5174EBE94D537836
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti130 – 1301P → A in AAA35531. (PubMed:2554323)Curated
    Sequence conflicti258 – 2581R → A in AAA36399. (PubMed:2159327)Curated
    Sequence conflicti272 – 2721K → R AA sequence (PubMed:8694763)Curated
    Sequence conflicti551 – 5511L → P in CAG29336. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31786 mRNA. Translation: AAA35531.1.
    J02902 mRNA. Translation: AAA36399.1.
    CR450340 mRNA. Translation: CAG29336.1.
    BC001537 mRNA. Translation: AAH01537.1.
    CCDSiCCDS12849.1.
    PIRiA34541.
    RefSeqiNP_055040.2. NM_014225.5.
    UniGeneiHs.467192.

    Genome annotation databases

    EnsembliENST00000322088; ENSP00000324804; ENSG00000105568.
    GeneIDi5518.
    KEGGihsa:5518.
    UCSCiuc002pyp.3. human.

    Polymorphism databases

    DMDMi143811355.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31786 mRNA. Translation: AAA35531.1 .
    J02902 mRNA. Translation: AAA36399.1 .
    CR450340 mRNA. Translation: CAG29336.1 .
    BC001537 mRNA. Translation: AAH01537.1 .
    CCDSi CCDS12849.1.
    PIRi A34541.
    RefSeqi NP_055040.2. NM_014225.5.
    UniGenei Hs.467192.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B3U X-ray 2.30 A/B 2-589 [» ]
    2IE3 X-ray 2.80 A 1-589 [» ]
    2IE4 X-ray 2.60 A 1-589 [» ]
    2NPP X-ray 3.30 A/D 1-589 [» ]
    2NYL X-ray 3.80 A/D 8-589 [» ]
    2NYM X-ray 3.60 A/D 8-589 [» ]
    2PKG X-ray 3.30 A/B 10-589 [» ]
    3C5W X-ray 2.80 A 9-589 [» ]
    3DW8 X-ray 2.85 A/D 9-589 [» ]
    3K7V X-ray 2.85 A 1-589 [» ]
    3K7W X-ray 2.96 A 1-589 [» ]
    4I5L X-ray 2.43 A/D 6-589 [» ]
    4I5N X-ray 2.80 A/D 6-589 [» ]
    4LAC X-ray 2.82 A 404-589 [» ]
    ProteinModelPortali P30153.
    SMRi P30153. Positions 2-589.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111510. 139 interactions.
    DIPi DIP-29394N.
    IntActi P30153. 116 interactions.
    MINTi MINT-1141071.
    STRINGi 9606.ENSP00000324804.

    PTM databases

    PhosphoSitei P30153.

    Polymorphism databases

    DMDMi 143811355.

    2D gel databases

    OGPi P30153.
    REPRODUCTION-2DPAGE IPI00554737.

    Proteomic databases

    MaxQBi P30153.
    PaxDbi P30153.
    PRIDEi P30153.

    Protocols and materials databases

    DNASUi 5518.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322088 ; ENSP00000324804 ; ENSG00000105568 .
    GeneIDi 5518.
    KEGGi hsa:5518.
    UCSCi uc002pyp.3. human.

    Organism-specific databases

    CTDi 5518.
    GeneCardsi GC19P052693.
    HGNCi HGNC:9302. PPP2R1A.
    HPAi CAB018599.
    MIMi 605983. gene.
    neXtProti NX_P30153.
    PharmGKBi PA33666.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG247268.
    HOGENOMi HOG000078539.
    HOVERGENi HBG000011.
    InParanoidi P30153.
    KOi K03456.
    OMAi RNLCQDD.
    OrthoDBi EOG764722.
    PhylomeDBi P30153.
    TreeFami TF105552.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000105568-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_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15334. DARPP-32 events.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    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 P30153.

    Miscellaneous databases

    EvolutionaryTracei P30153.
    GeneWikii PPP2R1A.
    GenomeRNAii 5518.
    NextBioi 21342.
    PMAP-CutDB P30153.
    PROi P30153.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30153.
    Bgeei P30153.
    CleanExi HS_PPP2R1A.
    Genevestigatori P30153.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000357. HEAT.
    IPR021133. HEAT_type_2.
    [Graphical view ]
    Pfami PF02985. HEAT. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50077. HEAT_REPEAT. 11 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and sequence of cDNA encoding polyoma medium tumor antigen-associated 61-kDa protein."
      Walter G., Ferre F., Espiritu O., Carbone-Wiley A.
      Proc. Natl. Acad. Sci. U.S.A. 86:8669-8672(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 242-255.
      Tissue: Placenta.
    2. "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure."
      Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J., Merlevede W., Hofsteenge J., Stone S.R.
      Biochemistry 29:3166-3173(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
      Tissue: Colon.
    5. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 34-46, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    6. "The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits."
      Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., Merlevede W., Goris J., Hemmings B.A.
      Biochem. J. 317:187-194(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 204-214; 261-272 AND 521-527.
    7. "Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens."
      Ruediger R., Hentz M., Fait J., Mumby M., Walter G.
      J. Virol. 68:123-129(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: BINDING DOMAINS.
    8. "Interaction between protein phosphatase 2A and members of the importin beta superfamily."
      Lubert E.J., Sarge K.D.
      Biochem. Biophys. Res. Commun. 303:908-913(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IPO9.
    9. "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, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SGOL1.
    10. "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.
    11. "Mechanisms of the HRSL3 tumor suppressor function in ovarian carcinoma cells."
      Nazarenko I., Schafer R., Sers C.
      J. Cell Sci. 120:1393-1404(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLA2G16.
    12. "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].
    13. "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein."
      Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C.
      Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTTNBP2NL.
    14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs."
      Groves M.R., Hanlon N., Turowski P., Hemmings B.A., Barford D.
      Cell 96:99-110(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    19. "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) OF 9-589 IN COMPLEX WITH WITH PPP2CA AND PPME1.

    Entry informationi

    Entry namei2AAA_HUMAN
    AccessioniPrimary (citable) accession number: P30153
    Secondary accession number(s): Q13773, Q6ICQ3, Q96DH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 152 of the entry and version 4 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 19
      Human chromosome 19: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3