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Q66LE6

- 2ABD_HUMAN

UniProt

Q66LE6 - 2ABD_HUMAN

Protein

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform

Gene

PPP2R2D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    B regulatory subunit of protein phosphatase 2A (PP2A) that plays a key role in cell cycle by controlling mitosis entry and exit. The activity of PP2A complexes containing PPP2R2D (PR55-delta) fluctuate during the cell cycle: the activity is high in interphase and low in mitosis. During mitosis, activity of PP2A is inhibited via interaction with phosphorylated ENSA and ARPP19 inhibitors. Within the PP2A complexes, the B regulatory subunits modulate substrate selectivity and catalytic activity, and also may direct the localization of the catalytic enzyme to a particular subcellular compartment By similarity.By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. exit from mitosis Source: UniProtKB
    2. mitotic cell cycle Source: Reactome
    3. mitotic nuclear division Source: UniProtKB
    4. regulation of catalytic activity Source: GOC
    5. signal transduction Source: InterPro

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_150182. MASTL Facilitates Mitotic Progression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
    Alternative name(s):
    PP2A subunit B isoform B55-delta
    PP2A subunit B isoform PR55-delta
    PP2A subunit B isoform R2-delta
    PP2A subunit B isoform delta
    Gene namesi
    Name:PPP2R2D
    Synonyms:KIAA1541
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:23732. PPP2R2D.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. protein phosphatase type 2A complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134899040.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 453453Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoformPRO_0000071433Add
    BLAST

    Proteomic databases

    MaxQBiQ66LE6.
    PaxDbiQ66LE6.
    PRIDEiQ66LE6.

    PTM databases

    PhosphoSiteiQ66LE6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ66LE6.
    BgeeiQ66LE6.
    CleanExiHS_PPP2R2D.
    GenevestigatoriQ66LE6.

    Interactioni

    Subunit structurei

    PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 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 ENSA (when phosphorylated at 'Ser-67') and ARPP19 (when phosphorylated at 'Ser-62'), leading to inhibit PP2A activity By similarity.By similarity

    Protein-protein interaction databases

    BioGridi120946. 31 interactions.
    IntActiQ66LE6. 27 interactions.
    MINTiMINT-2820413.
    STRINGi9606.ENSP00000381100.

    Structurei

    3D structure databases

    ProteinModelPortaliQ66LE6.
    SMRiQ66LE6. Positions 14-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati32 – 7140WD 1Add
    BLAST
    Repeati97 – 13842WD 2Add
    BLAST
    Repeati181 – 21939WD 3Add
    BLAST
    Repeati230 – 27041WD 4Add
    BLAST
    Repeati289 – 32739WD 5Add
    BLAST
    Repeati344 – 38542WD 6Add
    BLAST
    Repeati420 – 45233WD 7Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi3 – 86Poly-Gly

    Sequence similaritiesi

    Contains 7 WD repeats.Curated

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG5170.
    HOGENOMiHOG000089745.
    HOVERGENiHBG000012.
    InParanoidiQ66LE6.
    KOiK04354.
    PhylomeDBiQ66LE6.
    TreeFamiTF105553.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR000009. PP2A_PR55.
    IPR018067. PP2A_PR55_CS.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PANTHERiPTHR11871. PTHR11871. 1 hit.
    PIRSFiPIRSF037309. PP2A_PR55. 1 hit.
    PRINTSiPR00600. PP2APR55.
    SMARTiSM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 3 hits.
    PROSITEiPS01024. PR55_1. 1 hit.
    PS01025. PR55_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q66LE6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGAGGGGCP AGGNDFQWCF SQVKGAIDED VAEADIISTV EFNYSGDLLA    50
    TGDKGGRVVI FQREQENKSR PHSRGEYNVY STFQSHEPEF DYLKSLEIEE 100
    KINKIRWLPQ QNAAHFLLST NDKTIKLWKI SERDKRAEGY NLKDEDGRLR 150
    DPFRITALRV PILKPMDLMV EASPRRIFAN AHTYHINSIS VNSDHETYLS 200
    ADDLRINLWH LEITDRSFNI VDIKPANMEE LTEVITAAEF HPHQCNVFVY 250
    SSSKGTIRLC DMRSSALCDR HSKFFEEPED PSSRSFFSEI ISSISDVKFS 300
    HSGRYMMTRD YLSVKVWDLN MESRPVETHQ VHEYLRSKLC SLYENDCIFD 350
    KFECCWNGSD SAIMTGSYNN FFRMFDRDTR RDVTLEASRE SSKPRASLKP 400
    RKVCTGGKRR KDEISVDSLD FNKKILHTAW HPVDNVIAVA ATNNLYIFQD 450
    KIN 453
    Length:453
    Mass (Da):52,042
    Last modified:October 11, 2004 - v1
    Checksum:i0669CDB80AF4400E
    GO

    Sequence cautioni

    The sequence BAA96065.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI16703.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti290 – 2901I → V in BAF85754. (PubMed:14702039)Curated
    Sequence conflicti311 – 3111Y → H in BAF85754. (PubMed:14702039)Curated
    Sequence conflicti321 – 3211M → T in BAF85754. (PubMed:14702039)Curated
    Sequence conflicti449 – 4491Q → R in BAF85754. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti358 – 3581G → S.
    Corresponds to variant rs34473884 [ dbSNP | Ensembl ].
    VAR_057127

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK293065 mRNA. Translation: BAF85754.1.
    AL732395 Genomic DNA. Translation: CAI16703.1. Sequence problems.
    BC047379 mRNA. Translation: AAH47379.1.
    AB040974 mRNA. Translation: BAA96065.1. Different initiation.
    RefSeqiNP_001278239.1. NM_001291310.1.
    NP_060931.2. NM_018461.4.
    UniGeneiHs.380372.
    Hs.657480.

    Genome annotation databases

    EnsembliENST00000455566; ENSP00000399970; ENSG00000175470.
    GeneIDi55844.
    KEGGihsa:55844.
    UCSCiuc001lks.3. human.

    Polymorphism databases

    DMDMi74736328.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK293065 mRNA. Translation: BAF85754.1 .
    AL732395 Genomic DNA. Translation: CAI16703.1 . Sequence problems.
    BC047379 mRNA. Translation: AAH47379.1 .
    AB040974 mRNA. Translation: BAA96065.1 . Different initiation.
    RefSeqi NP_001278239.1. NM_001291310.1.
    NP_060931.2. NM_018461.4.
    UniGenei Hs.380372.
    Hs.657480.

    3D structure databases

    ProteinModelPortali Q66LE6.
    SMRi Q66LE6. Positions 14-452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120946. 31 interactions.
    IntActi Q66LE6. 27 interactions.
    MINTi MINT-2820413.
    STRINGi 9606.ENSP00000381100.

    PTM databases

    PhosphoSitei Q66LE6.

    Polymorphism databases

    DMDMi 74736328.

    Proteomic databases

    MaxQBi Q66LE6.
    PaxDbi Q66LE6.
    PRIDEi Q66LE6.

    Protocols and materials databases

    DNASUi 55844.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000455566 ; ENSP00000399970 ; ENSG00000175470 .
    GeneIDi 55844.
    KEGGi hsa:55844.
    UCSCi uc001lks.3. human.

    Organism-specific databases

    CTDi 55844.
    GeneCardsi GC10P133747.
    H-InvDB HIX0009317.
    HGNCi HGNC:23732. PPP2R2D.
    MIMi 613992. gene.
    neXtProti NX_Q66LE6.
    PharmGKBi PA134899040.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5170.
    HOGENOMi HOG000089745.
    HOVERGENi HBG000012.
    InParanoidi Q66LE6.
    KOi K04354.
    PhylomeDBi Q66LE6.
    TreeFami TF105553.

    Enzyme and pathway databases

    Reactomei REACT_150182. MASTL Facilitates Mitotic Progression.

    Miscellaneous databases

    ChiTaRSi PPP2R2D. human.
    GenomeRNAii 55844.
    NextBioi 61085.
    PROi Q66LE6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q66LE6.
    Bgeei Q66LE6.
    CleanExi HS_PPP2R2D.
    Genevestigatori Q66LE6.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR000009. PP2A_PR55.
    IPR018067. PP2A_PR55_CS.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    PANTHERi PTHR11871. PTHR11871. 1 hit.
    PIRSFi PIRSF037309. PP2A_PR55. 1 hit.
    PRINTSi PR00600. PP2APR55.
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 3 hits.
    PROSITEi PS01024. PR55_1. 1 hit.
    PS01025. PR55_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Tissue: Uterus.
    2. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Testis.
    4. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-453.
      Tissue: Brain.

    Entry informationi

    Entry namei2ABD_HUMAN
    AccessioniPrimary (citable) accession number: Q66LE6
    Secondary accession number(s): A8KAK0, Q5SQJ2, Q9P1Y7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 104 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3