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Q13362

- 2A5G_HUMAN

UniProt

Q13362 - 2A5G_HUMAN

Protein

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform

Gene

PPP2R5C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein phosphatase type 2A regulator activity Source: UniProtKB

    GO - Biological processi

    1. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: UniProtKB
    2. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
    3. negative regulation of cell proliferation Source: UniProtKB
    4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
    5. regulation of catalytic activity Source: GOC
    6. signal transduction Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    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_682. Mitotic Prometaphase.
    SignaLinkiQ13362.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
    Alternative name(s):
    PP2A B subunit isoform B'-gamma
    PP2A B subunit isoform B56-gamma
    PP2A B subunit isoform PR61-gamma
    PP2A B subunit isoform R5-gamma
    Renal carcinoma antigen NY-REN-29
    Gene namesi
    Name:PPP2R5C
    Synonyms:KIAA0044
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9311. PPP2R5C.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33674.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 524524Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoformPRO_0000071457Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Post-translational modificationi

    Isoform Gamma-3 is phosphorylated on serine residues. Isoform Gamma-1 phosphorylation by ERK2 is IER3-dependent and inhibits ERK dephosphorylation by PP2A-PPP2R5C.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13362.
    PaxDbiQ13362.
    PRIDEiQ13362.

    PTM databases

    PhosphoSiteiQ13362.

    Miscellaneous databases

    PMAP-CutDBQ13362.

    Expressioni

    Tissue specificityi

    Highest levels in heart, skeletal muscle and brain. Lower levels in pancreas, kidney, lung and placenta. Very low levels in liver.

    Inductioni

    Up-regulated upon DNA damage.1 Publication

    Gene expression databases

    ArrayExpressiQ13362.
    BgeeiQ13362.
    CleanExiHS_PPP2R5C.
    GenevestigatoriQ13362.

    Organism-specific databases

    HPAiHPA027553.

    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 PPP2CA AND PPP2R1A; the interaction is direct. Interacts with SGOL1; the interaction is direct. Isoform 1 and isoform 2 interact with TP53 (phosphorylated at Ser-15 by ATM); increased upon DNA damage it drives PP2A-mediated dephosphorylation of TP53 at Thr-55. Interacts with IER3 and/or ERK kinases; regulates ERK dephosphorylation.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CHEK2O960174EBI-1266176,EBI-1180783
    IER3P466952EBI-1266156,EBI-1748945
    MDM2Q009875EBI-1266156,EBI-389668
    PPP2CAP677757EBI-1266156,EBI-712311
    PPP2R1AP301536EBI-1266156,EBI-302388
    PPP2R1BP301542EBI-1266156,EBI-357094
    TP53P046374EBI-1266156,EBI-366083

    Protein-protein interaction databases

    BioGridi111519. 27 interactions.
    DIPiDIP-39401N.
    IntActiQ13362. 18 interactions.
    MINTiMINT-2835438.
    STRINGi9606.ENSP00000333905.

    Structurei

    Secondary structure

    1
    524
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 489
    Beta strandi55 – 584
    Beta strandi59 – 624
    Helixi63 – 8018
    Beta strandi83 – 853
    Helixi91 – 10313
    Beta strandi115 – 1184
    Helixi120 – 1223
    Helixi131 – 14616
    Helixi152 – 1554
    Turni156 – 1583
    Helixi161 – 17010
    Helixi176 – 19217
    Helixi194 – 1963
    Helixi197 – 21216
    Turni213 – 2153
    Helixi221 – 23313
    Helixi241 – 2499
    Helixi252 – 2554
    Helixi258 – 2625
    Helixi264 – 27714
    Helixi279 – 2813
    Helixi282 – 29110
    Helixi301 – 31313
    Helixi317 – 33519
    Helixi340 – 3478
    Helixi348 – 3514
    Helixi353 – 3619
    Helixi363 – 3664
    Turni367 – 3693
    Turni372 – 3776
    Helixi384 – 39815
    Helixi409 – 43022

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IAEX-ray3.50B/E30-436[»]
    2JAKX-ray2.60A11-380[»]
    2NPPX-ray3.30B/E1-442[»]
    2NYLX-ray3.80B/E38-425[»]
    2NYMX-ray3.60B/E38-425[»]
    3FGAX-ray2.70B34-436[»]
    ProteinModelPortaliQ13362.
    SMRiQ13362. Positions 34-436.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13362.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi416 – 4227Nuclear localization signalSequence Analysis

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG264925.
    HOGENOMiHOG000067326.
    HOVERGENiHBG000009.
    KOiK11584.
    OMAiSERWEAD.
    PhylomeDBiQ13362.
    TreeFamiTF105556.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR002554. PP2A_B56.
    [Graphical view]
    PANTHERiPTHR10257. PTHR10257. 1 hit.
    PfamiPF01603. B56. 1 hit.
    [Graphical view]
    PIRSFiPIRSF028043. PP2A_B56. 1 hit.
    SUPFAMiSSF48371. SSF48371. 1 hit.

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform Gamma-3 (identifier: Q13362-1) [UniParc]FASTAAdd to Basket

    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

    MLTCNKAGSR MVVDAANSNG PFQPVVLLHI RDVPPADQEK LFIQKLRQCC    50
    VLFDFVSDPL SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA 100
    VNMFRTLPPS SNPTGAEFDP EEDEPTLEAA WPHLQLVYEF FLRFLESPDF 150
    QPNIAKKYID QKFVLQLLEL FDSEDPRERD FLKTTLHRIY GKFLGLRAYI 200
    RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK EEHKIFLLKV 250
    LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK 300
    EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW 350
    NNEYIMSLIS DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM 400
    NQKLFDDCTQ QFKAEKLKEK LKMKEREEAW VKIENLAKAN PQYTVYSQAS 450
    TMSIPVAMET DGPLFEDVQM LRKTVKDEAH QAQKDPKKDR PLARRKSELP 500
    QDPHTKKALE AHCRADELAS QDGR 524
    Length:524
    Mass (Da):61,061
    Last modified:October 17, 2006 - v3
    Checksum:iB9CBF54550D713F8
    GO
    Isoform Gamma-1 (identifier: Q13362-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         443-524: YTVYSQASTM...ADELASQDGR → VLKKRIT

    Show »
    Length:449
    Mass (Da):52,625
    Checksum:i73CE22E378289FE8
    GO
    Isoform Gamma-2 (identifier: Q13362-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         443-481: Missing.

    Show »
    Length:485
    Mass (Da):56,661
    Checksum:i64F2D9D78F9D35B6
    GO
    Isoform 4 (identifier: Q13362-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-31: MLTCNKAGSRMVVDAANSNGPFQPVVLLHIR → MPNKNKKEKE...RELQKLPSLK
         443-481: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:540
    Mass (Da):62,755
    Checksum:i30B98C5AED1A4466
    GO
    Isoform 5 (identifier: Q13362-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-30: MLTCNKAGSRMVVDAANSNGPFQPVVLLHI → MPNKNKKEKE...LVLIFGGLQG

    Note: No experimental confirmation available.Curated

    Show »
    Length:555
    Mass (Da):64,292
    Checksum:i1C4C9780CF86FF71
    GO

    Sequence cautioni

    The sequence AAC50387.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAG63760.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti494 – 4941R → L in AAC50387. (PubMed:8617797)Curated
    Isoform 5 (identifier: Q13362-5)
    Sequence conflicti3 – 31N → K in BAG63760. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti515 – 5151A → P.
    Corresponds to variant rs3742424 [ dbSNP | Ensembl ].
    VAR_051745

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3131MLTCN…LLHIR → MPNKNKKEKESPKAGKSGKS SKEGQDTVESEQISVRKNSL VAVPSTVSAKIKVPVSQPIV KKDKRQNSSRFSASNNRELQ KLPSLK in isoform 4. 1 PublicationVSP_043645Add
    BLAST
    Alternative sequencei1 – 3030MLTCN…VLLHI → MPNKNKKEKESPKAGKSGKS SKEGQDTVESEGTSPEEPSS PKVPPPLLPELLVLIFGGLQ G in isoform 5. CuratedVSP_046768Add
    BLAST
    Alternative sequencei443 – 52482YTVYS…SQDGR → VLKKRIT in isoform Gamma-1. 2 PublicationsVSP_005112Add
    BLAST
    Alternative sequencei443 – 48139Missing in isoform Gamma-2 and isoform 4. 2 PublicationsVSP_005113Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37352 mRNA. Translation: AAC50387.1. Different initiation.
    Z69030 mRNA. Translation: CAA93154.1.
    AK131391 mRNA. Translation: BAD18542.1.
    AK302470 mRNA. Translation: BAG63760.1. Different initiation.
    AB451341 mRNA. Translation: BAG70155.1.
    AL118558 Genomic DNA. No translation available.
    AL137779 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW81756.1.
    D26445 mRNA. Translation: BAA05465.1.
    L42375 mRNA. Translation: AAC37603.1.
    CCDSiCCDS45163.1. [Q13362-2]
    CCDS53911.1. [Q13362-4]
    CCDS53912.1. [Q13362-5]
    CCDS9964.1. [Q13362-1]
    CCDS9965.1. [Q13362-3]
    RefSeqiNP_001155197.1. NM_001161725.1. [Q13362-5]
    NP_001155198.1. NM_001161726.1. [Q13362-4]
    NP_002710.2. NM_002719.3. [Q13362-1]
    NP_848701.1. NM_178586.2. [Q13362-3]
    NP_848702.1. NM_178587.2. [Q13362-2]
    XP_005267884.1. XM_005267827.1.
    UniGeneiHs.368264.

    Genome annotation databases

    EnsembliENST00000328724; ENSP00000329009; ENSG00000078304. [Q13362-4]
    ENST00000334743; ENSP00000333905; ENSG00000078304. [Q13362-1]
    ENST00000350249; ENSP00000262239; ENSG00000078304. [Q13362-3]
    ENST00000422945; ENSP00000412324; ENSG00000078304. [Q13362-5]
    ENST00000445439; ENSP00000408389; ENSG00000078304. [Q13362-2]
    GeneIDi5527.
    KEGGihsa:5527.
    UCSCiuc001ykk.3. human. [Q13362-4]
    uc001ykn.3. human. [Q13362-2]
    uc001yko.3. human. [Q13362-1]
    uc001ykp.3. human. [Q13362-3]

    Polymorphism databases

    DMDMi116241235.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37352 mRNA. Translation: AAC50387.1 . Different initiation.
    Z69030 mRNA. Translation: CAA93154.1 .
    AK131391 mRNA. Translation: BAD18542.1 .
    AK302470 mRNA. Translation: BAG63760.1 . Different initiation.
    AB451341 mRNA. Translation: BAG70155.1 .
    AL118558 Genomic DNA. No translation available.
    AL137779 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW81756.1 .
    D26445 mRNA. Translation: BAA05465.1 .
    L42375 mRNA. Translation: AAC37603.1 .
    CCDSi CCDS45163.1. [Q13362-2 ]
    CCDS53911.1. [Q13362-4 ]
    CCDS53912.1. [Q13362-5 ]
    CCDS9964.1. [Q13362-1 ]
    CCDS9965.1. [Q13362-3 ]
    RefSeqi NP_001155197.1. NM_001161725.1. [Q13362-5 ]
    NP_001155198.1. NM_001161726.1. [Q13362-4 ]
    NP_002710.2. NM_002719.3. [Q13362-1 ]
    NP_848701.1. NM_178586.2. [Q13362-3 ]
    NP_848702.1. NM_178587.2. [Q13362-2 ]
    XP_005267884.1. XM_005267827.1.
    UniGenei Hs.368264.

    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 B/E 30-436 [» ]
    2JAK X-ray 2.60 A 11-380 [» ]
    2NPP X-ray 3.30 B/E 1-442 [» ]
    2NYL X-ray 3.80 B/E 38-425 [» ]
    2NYM X-ray 3.60 B/E 38-425 [» ]
    3FGA X-ray 2.70 B 34-436 [» ]
    ProteinModelPortali Q13362.
    SMRi Q13362. Positions 34-436.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111519. 27 interactions.
    DIPi DIP-39401N.
    IntActi Q13362. 18 interactions.
    MINTi MINT-2835438.
    STRINGi 9606.ENSP00000333905.

    PTM databases

    PhosphoSitei Q13362.

    Polymorphism databases

    DMDMi 116241235.

    Proteomic databases

    MaxQBi Q13362.
    PaxDbi Q13362.
    PRIDEi Q13362.

    Protocols and materials databases

    DNASUi 5527.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328724 ; ENSP00000329009 ; ENSG00000078304 . [Q13362-4 ]
    ENST00000334743 ; ENSP00000333905 ; ENSG00000078304 . [Q13362-1 ]
    ENST00000350249 ; ENSP00000262239 ; ENSG00000078304 . [Q13362-3 ]
    ENST00000422945 ; ENSP00000412324 ; ENSG00000078304 . [Q13362-5 ]
    ENST00000445439 ; ENSP00000408389 ; ENSG00000078304 . [Q13362-2 ]
    GeneIDi 5527.
    KEGGi hsa:5527.
    UCSCi uc001ykk.3. human. [Q13362-4 ]
    uc001ykn.3. human. [Q13362-2 ]
    uc001yko.3. human. [Q13362-1 ]
    uc001ykp.3. human. [Q13362-3 ]

    Organism-specific databases

    CTDi 5527.
    GeneCardsi GC14P102228.
    HGNCi HGNC:9311. PPP2R5C.
    HPAi HPA027553.
    MIMi 601645. gene.
    neXtProti NX_Q13362.
    PharmGKBi PA33674.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264925.
    HOGENOMi HOG000067326.
    HOVERGENi HBG000009.
    KOi K11584.
    OMAi SERWEAD.
    PhylomeDBi Q13362.
    TreeFami TF105556.

    Enzyme and pathway databases

    Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    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_682. Mitotic Prometaphase.
    SignaLinki Q13362.

    Miscellaneous databases

    ChiTaRSi PPP2R5C. human.
    EvolutionaryTracei Q13362.
    GeneWikii PPP2R5C.
    GenomeRNAii 5527.
    NextBioi 21400.
    PMAP-CutDB Q13362.
    PROi Q13362.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13362.
    Bgeei Q13362.
    CleanExi HS_PPP2R5C.
    Genevestigatori Q13362.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR002554. PP2A_B56.
    [Graphical view ]
    PANTHERi PTHR10257. PTHR10257. 1 hit.
    Pfami PF01603. B56. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF028043. PP2A_B56. 1 hit.
    SUPFAMi SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel protein phosphatase 2A regulatory subunit highly expressed in muscle."
      Tehrani M.A., Mumby M.C., Kamibayashi C.
      J. Biol. Chem. 271:5164-5170(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-3).
      Tissue: Umbilical vein.
    2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-1).
      Tissue: Fetal retina.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Hippocampus and Testis.
    4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-3).
    5. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-524 (ISOFORM GAMMA-2).
      Tissue: Bone marrow.
    8. "Identification of a new family of protein phosphatase 2A regulatory subunits."
      McCright B., Virshup D.M.
      J. Biol. Chem. 270:26123-26128(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-524 (ISOFORM GAMMA-1).
    9. "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm."
      McCright B., Rivers A.M., Audlin S., Virshup D.M.
      J. Biol. Chem. 271:22081-22089(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
    10. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    11. "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, SUBCELLULAR LOCATION.
    12. "B56-containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX-1 and ERK."
      Letourneux C., Rocher G., Porteu F.
      EMBO J. 25:727-738(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IER3 AND ERK KINASES, PHOSPHORYLATION.
    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: INTERACTION WITH SGOL1.
    14. "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: FUNCTION, INTERACTION WITH TP53, INDUCTION.
    15. "Serine 15 phosphorylation of p53 directs its interaction with B56gamma and the tumor suppressor activity of B56gamma-specific protein phosphatase 2A."
      Shouse G.P., Cai X., Liu X.
      Mol. Cell. Biol. 28:448-456(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP53.
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Structure of the protein phosphatase 2A holoenzyme."
      Xu Y., Xing Y., Chen Y., Chao Y., Lin Z., Fan E., Yu J.W., Strack S., Jeffrey P.D., Shi Y.
      Cell 127:1239-1251(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-442 IN COMPLEX WITH PPP2CA AND PPP2R1A.
    18. "Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme."
      Cho U.S., Xu W.
      Nature 445:53-57(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 30-436 IN COMPLEX WITH PPP2CA AND PPP2R1A.
    19. "Structure and function of the PP2A-shugoshin interaction."
      Xu Z., Cetin B., Anger M., Cho U.S., Helmhart W., Nasmyth K., Xu W.
      Mol. Cell 35:426-441(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 34-436 IN COMPLEX WITH PPP2CA; PPP2R1A AND SGOL1.
    20. "The structure of the PP2A regulatory subunit B56 gamma: the remaining piece of the PP2A jigsaw puzzle."
      Magnusdottir A., Stenmark P., Flodin S., Nyman T., Kotenyova T., Graeslund S., Ogg D., Nordlund P.
      Proteins 74:212-221(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 11-380.

    Entry informationi

    Entry namei2A5G_HUMAN
    AccessioniPrimary (citable) accession number: Q13362
    Secondary accession number(s): B4DYJ8
    , B5BUA5, F5GWP3, Q14391, Q15060, Q15174, Q6ZN33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 147 of the entry and version 3 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, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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