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Q76MZ3

- 2AAA_MOUSE

UniProt

Q76MZ3 - 2AAA_MOUSE

Protein

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

Gene

Ppp2r1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 3 (23 Jan 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 By similarity.By similarity

    GO - Molecular functioni

    1. antigen binding Source: Ensembl
    2. protein binding Source: IntAct
    3. protein serine/threonine phosphatase activity Source: MGI

    GO - Biological processi

    1. chromosome segregation Source: UniProtKB
    2. peptidyl-serine dephosphorylation Source: MGI
    3. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI

    Keywords - Biological processi

    Chromosome partition

    Enzyme and pathway databases

    ReactomeiREACT_196577. MASTL Facilitates Mitotic Progression.
    REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    REACT_198526. Spry regulation of FGF signaling.
    REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    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_210180. Initiation of Nuclear Envelope Reformation.
    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 65 kDa regulatory subunit A alpha isoform
    Alternative name(s):
    PP2A subunit A isoform PR65-alpha
    PP2A subunit A isoform R1-alpha
    Gene namesi
    Name:Ppp2r1a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1926334. Ppp2r1a.

    Subcellular locationi

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

    GO - Cellular componenti

    1. chromosome, centromeric region Source: UniProtKB
    2. cytosol Source: MGI
    3. protein phosphatase type 2A complex Source: MGI

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 589588Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoformPRO_0000071401Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ76MZ3.
    PaxDbiQ76MZ3.
    PRIDEiQ76MZ3.

    2D gel databases

    REPRODUCTION-2DPAGEQ76MZ3.

    PTM databases

    PhosphoSiteiQ76MZ3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ76MZ3.
    BgeeiQ76MZ3.
    GenevestigatoriQ76MZ3.

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P030812EBI-400413,EBI-1266256From a different organism.
    Ppp2caP633303EBI-400413,EBI-397144

    Protein-protein interaction databases

    BioGridi206176. 27 interactions.
    DIPiDIP-29429N.
    IntActiQ76MZ3. 46 interactions.
    MINTiMINT-135926.
    STRINGi10090.ENSMUSP00000007708.

    Structurei

    Secondary structure

    1
    589
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 2111
    Helixi25 – 339
    Helixi35 – 417
    Helixi44 – 496
    Helixi51 – 566
    Helixi63 – 7311
    Turni77 – 815
    Helixi83 – 853
    Helixi86 – 894
    Helixi90 – 989
    Helixi102 – 11615
    Helixi121 – 1266
    Helixi128 – 1369
    Helixi141 – 1477
    Turni148 – 1503
    Helixi151 – 1544
    Helixi155 – 1573
    Helixi160 – 17415
    Helixi179 – 1879
    Helixi189 – 1935
    Helixi198 – 21316
    Helixi218 – 23215
    Helixi237 – 2426
    Helixi244 – 2518
    Helixi257 – 2659
    Helixi267 – 2748
    Helixi276 – 29116
    Helixi296 – 3038
    Helixi306 – 3116
    Turni315 – 3173
    Helixi318 – 3247
    Helixi327 – 3348
    Helixi339 – 3468
    Helixi349 – 3524
    Helixi353 – 37321
    Helixi378 – 3858
    Helixi386 – 3883
    Helixi389 – 3946
    Helixi397 – 4037
    Helixi405 – 4117
    Helixi417 – 4248
    Helixi427 – 4348
    Helixi436 – 4427
    Helixi444 – 4518
    Helixi456 – 47318
    Helixi475 – 4817
    Helixi483 – 4886
    Helixi489 – 4913
    Helixi495 – 52026
    Helixi522 – 5287
    Helixi534 – 54714
    Helixi548 – 5503
    Helixi553 – 5586
    Helixi560 – 5689
    Beta strandi569 – 5713
    Helixi573 – 58513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IAEX-ray3.50A/D1-589[»]
    2PF4X-ray3.10A/B/C/D1-589[»]
    3FGAX-ray2.70A2-589[»]
    ProteinModelPortaliQ76MZ3.
    SMRiQ76MZ3. Positions 2-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ76MZ3.

    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

    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.
    GeneTreeiENSGT00730000110944.
    HOGENOMiHOG000078539.
    HOVERGENiHBG000011.
    InParanoidiQ76MZ3.
    KOiK03456.
    OMAiRNLCQDD.
    OrthoDBiEOG764722.
    PhylomeDBiQ76MZ3.
    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. 1 hit.
    [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.

    Q76MZ3-1 [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 VIMTQILPCI 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):65,323
    Last modified:January 23, 2007 - v3
    Checksum:i5175409E4D50A366
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021743 mRNA. Translation: BAA75478.1.
    AK054239 mRNA. Translation: BAC35700.1.
    AK078135 mRNA. Translation: BAC37143.1.
    BC006606 mRNA. Translation: AAH06606.1.
    CCDSiCCDS28432.1.
    RefSeqiNP_058587.1. NM_016891.3.
    UniGeneiMm.294138.

    Genome annotation databases

    EnsembliENSMUST00000007708; ENSMUSP00000007708; ENSMUSG00000007564.
    GeneIDi51792.
    KEGGimmu:51792.
    UCSCiuc008aqi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021743 mRNA. Translation: BAA75478.1 .
    AK054239 mRNA. Translation: BAC35700.1 .
    AK078135 mRNA. Translation: BAC37143.1 .
    BC006606 mRNA. Translation: AAH06606.1 .
    CCDSi CCDS28432.1.
    RefSeqi NP_058587.1. NM_016891.3.
    UniGenei Mm.294138.

    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 A/D 1-589 [» ]
    2PF4 X-ray 3.10 A/B/C/D 1-589 [» ]
    3FGA X-ray 2.70 A 2-589 [» ]
    ProteinModelPortali Q76MZ3.
    SMRi Q76MZ3. Positions 2-589.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 206176. 27 interactions.
    DIPi DIP-29429N.
    IntActi Q76MZ3. 46 interactions.
    MINTi MINT-135926.
    STRINGi 10090.ENSMUSP00000007708.

    Chemistry

    BindingDBi Q76MZ3.
    ChEMBLi CHEMBL3557.

    PTM databases

    PhosphoSitei Q76MZ3.

    2D gel databases

    REPRODUCTION-2DPAGE Q76MZ3.

    Proteomic databases

    MaxQBi Q76MZ3.
    PaxDbi Q76MZ3.
    PRIDEi Q76MZ3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000007708 ; ENSMUSP00000007708 ; ENSMUSG00000007564 .
    GeneIDi 51792.
    KEGGi mmu:51792.
    UCSCi uc008aqi.1. mouse.

    Organism-specific databases

    CTDi 5518.
    MGIi MGI:1926334. Ppp2r1a.

    Phylogenomic databases

    eggNOGi NOG247268.
    GeneTreei ENSGT00730000110944.
    HOGENOMi HOG000078539.
    HOVERGENi HBG000011.
    InParanoidi Q76MZ3.
    KOi K03456.
    OMAi RNLCQDD.
    OrthoDBi EOG764722.
    PhylomeDBi Q76MZ3.
    TreeFami TF105552.

    Enzyme and pathway databases

    Reactomei REACT_196577. MASTL Facilitates Mitotic Progression.
    REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    REACT_198526. Spry regulation of FGF signaling.
    REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    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_210180. Initiation of Nuclear Envelope Reformation.
    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 PPP2R1A. mouse.
    EvolutionaryTracei Q76MZ3.
    NextBioi 308024.
    PROi Q76MZ3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q76MZ3.
    Bgeei Q76MZ3.
    Genevestigatori Q76MZ3.

    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. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50077. HEAT_REPEAT. 11 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Alpha4 protein as a common regulator of type 2A-related serine/threonine protein phosphatases."
      Nanahoshi M., Tsujishita Y., Tokunaga C., Inui S., Sakaguchi N., Hara K., Yonezawa K.
      FEBS Lett. 446:108-112(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Medulla oblongata and Oviduct.
    3. "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.
      Tissue: Mammary tumor.
    4. "The B55alpha-containing PP2A holoenzyme dephosphorylates FOXO1 in islet beta-cells under oxidative stress."
      Yan L., Guo S., Brault M., Harmon J., Robertson R.P., Hamid R., Stein R., Yang E.
      Biochem. J. 444:239-247(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FOXO1.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry namei2AAA_MOUSE
    AccessioniPrimary (citable) accession number: Q76MZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 94 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3