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Q5BU09

- EAPP_MOUSE

UniProt

Q5BU09 - EAPP_MOUSE

Protein

E2F-associated phosphoprotein

Gene

Eapp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
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    Functioni

    May play an important role in the fine-tuning of both major E2F1 activities, the regulation of the cell-cycle and the induction of apoptosis. Promotes S-phase entry, and inhibits p14(ARP) expression By similarity.By similarity

    GO - Biological processi

    1. negative regulation of transcription elongation from RNA polymerase II promoter Source: MGI
    2. positive regulation of cell proliferation Source: MGI
    3. positive regulation of transcription elongation from RNA polymerase II promoter Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E2F-associated phosphoprotein
    Short name:
    EAPP
    Gene namesi
    Name:Eapp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1913516. Eapp.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. Golgi apparatus Source: Ensembl
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 281281E2F-associated phosphoproteinPRO_0000086905Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei17 – 171PhosphoserineBy similarity
    Modified residuei109 – 1091PhosphoserineBy similarity
    Modified residuei111 – 1111PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ5BU09.
    PRIDEiQ5BU09.

    PTM databases

    PhosphoSiteiQ5BU09.

    Expressioni

    Gene expression databases

    ArrayExpressiQ5BU09.
    BgeeiQ5BU09.
    CleanExiMM_EAPP.
    GenevestigatoriQ5BU09.

    Interactioni

    Subunit structurei

    Interacts with E2F1. The C-terminal half binds the N-terminal of E2F1. Also interacts with E2F2 and E2F3, but not E2F4.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ5BU09.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi120 – 1256Poly-Lys

    Phylogenomic databases

    eggNOGiNOG250977.
    GeneTreeiENSGT00390000001332.
    HOGENOMiHOG000068005.
    HOVERGENiHBG054593.
    InParanoidiQ5BU09.
    OMAiRGHKKMR.
    OrthoDBiEOG7SR4ND.
    PhylomeDBiQ5BU09.
    TreeFamiTF328497.

    Family and domain databases

    InterProiIPR019370. E2F-assoc_phosphoprotein.
    [Graphical view]
    PfamiPF10238. Eapp_C. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5BU09-1) [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

    MNRLQDDYDP YAVEEPSDEE PALSSSEDEL DVLLHGTPDQ KRKLIRECLT    50
    GESESSSEDE FEKEMEAELN STMKTMEDQL SSLGTGSSSG VAKVGGVTEK 100
    FYDEIYFDSD SEDEDKTVTK KKKKKQHRIP TNDELLYDPE KDNRDQAWVD 150
    AKRRGYHAFG LQRPRQKQQP VPNSDAVLNC PACMTTLCLD CQRHESYKTQ 200
    YRAMFVMNCS INREEVLRYK NPENRRKRRS AKKMRSNPED PAEREAEEIY 250
    HPVMCTECST EVAVYDKDEV FHFFNVLASH S 281
    Length:281
    Mass (Da):32,494
    Last modified:August 30, 2005 - v2
    Checksum:i269C664CA3E3C401
    GO
    Isoform 2 (identifier: Q5BU09-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         156-193: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:243
    Mass (Da):28,208
    Checksum:i5701DEB71ABCEC22
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti116 – 1161K → R in AAX20161. (PubMed:15716352)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei156 – 19338Missing in isoform 2. 1 PublicationVSP_015331Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY882557 mRNA. Translation: AAX20161.1.
    AK007442 mRNA. Translation: BAB25042.1.
    AK012800 mRNA. Translation: BAB28479.1.
    BC037622 mRNA. Translation: AAH37622.1.
    CCDSiCCDS25910.1. [Q5BU09-1]
    RefSeqiNP_079732.1. NM_025456.3. [Q5BU09-1]
    XP_006516205.1. XM_006516142.1. [Q5BU09-1]
    UniGeneiMm.156440.

    Genome annotation databases

    EnsembliENSMUST00000110713; ENSMUSP00000106341; ENSMUSG00000054302. [Q5BU09-2]
    ENSMUST00000161592; ENSMUSP00000123698; ENSMUSG00000054302. [Q5BU09-1]
    ENSMUST00000163433; ENSMUSP00000130251; ENSMUSG00000054302. [Q5BU09-1]
    GeneIDi66266.
    KEGGimmu:66266.
    UCSCiuc007nnu.1. mouse. [Q5BU09-1]
    uc011ylx.1. mouse. [Q5BU09-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY882557 mRNA. Translation: AAX20161.1 .
    AK007442 mRNA. Translation: BAB25042.1 .
    AK012800 mRNA. Translation: BAB28479.1 .
    BC037622 mRNA. Translation: AAH37622.1 .
    CCDSi CCDS25910.1. [Q5BU09-1 ]
    RefSeqi NP_079732.1. NM_025456.3. [Q5BU09-1 ]
    XP_006516205.1. XM_006516142.1. [Q5BU09-1 ]
    UniGenei Mm.156440.

    3D structure databases

    ProteinModelPortali Q5BU09.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q5BU09.

    Proteomic databases

    MaxQBi Q5BU09.
    PRIDEi Q5BU09.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000110713 ; ENSMUSP00000106341 ; ENSMUSG00000054302 . [Q5BU09-2 ]
    ENSMUST00000161592 ; ENSMUSP00000123698 ; ENSMUSG00000054302 . [Q5BU09-1 ]
    ENSMUST00000163433 ; ENSMUSP00000130251 ; ENSMUSG00000054302 . [Q5BU09-1 ]
    GeneIDi 66266.
    KEGGi mmu:66266.
    UCSCi uc007nnu.1. mouse. [Q5BU09-1 ]
    uc011ylx.1. mouse. [Q5BU09-2 ]

    Organism-specific databases

    CTDi 55837.
    MGIi MGI:1913516. Eapp.

    Phylogenomic databases

    eggNOGi NOG250977.
    GeneTreei ENSGT00390000001332.
    HOGENOMi HOG000068005.
    HOVERGENi HBG054593.
    InParanoidi Q5BU09.
    OMAi RGHKKMR.
    OrthoDBi EOG7SR4ND.
    PhylomeDBi Q5BU09.
    TreeFami TF328497.

    Miscellaneous databases

    NextBioi 321143.
    PROi Q5BU09.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5BU09.
    Bgeei Q5BU09.
    CleanExi MM_EAPP.
    Genevestigatori Q5BU09.

    Family and domain databases

    InterProi IPR019370. E2F-assoc_phosphoprotein.
    [Graphical view ]
    Pfami PF10238. Eapp_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "EAPP, a novel E2F binding protein that modulates E2F-dependent transcription."
      Novy M., Pohn R., Andorfer P., Novy-Weiland T., Galos B., Schwarzmayr L., Rotheneder H.
      Mol. Biol. Cell 16:2181-2190(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH E2F1; E2F2 AND E2F3.
    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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Pancreas.
    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] (ISOFORM 1).
      Strain: FVB/N-3.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiEAPP_MOUSE
    AccessioniPrimary (citable) accession number: Q5BU09
    Secondary accession number(s): Q9CZB5, Q9D914
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 72 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3