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Q58FA4

- E2F8_MOUSE

UniProt

Q58FA4 - E2F8_MOUSE

Protein

Transcription factor E2F8

Gene

E2f8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      Previous versions | rss
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    Functioni

    Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1: component of a feedback loop in S phase by repressing the expression of E2F1, thereby preventing p53/TP53-dependent apoptosis. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene.5 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi113 – 18270Sequence AnalysisAdd
    BLAST
    DNA bindingi261 – 34787Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. core promoter binding Source: Ensembl
    2. DNA binding Source: MGI
    3. identical protein binding Source: IntAct
    4. protein homodimerization activity Source: MGI
    5. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    6. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle comprising mitosis without cytokinesis Source: UniProtKB
    2. cell proliferation Source: MGI
    3. chorionic trophoblast cell differentiation Source: UniProtKB
    4. hepatocyte differentiation Source: UniProtKB
    5. negative regulation of cytokinesis Source: UniProtKB
    6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. placenta development Source: UniProtKB
    8. positive regulation of DNA endoreduplication Source: UniProtKB
    9. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    10. sprouting angiogenesis Source: UniProtKB
    11. transcription, DNA-templated Source: UniProtKB-KW
    12. trophoblast giant cell differentiation Source: UniProtKB

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor E2F8
    Short name:
    E2F-8
    Gene namesi
    Name:E2f8
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1922038. E2f8.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: MGI
    2. transcription factor complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype; mice develop normally and live to old age. E2f7 and E2f8 double knockout embryos die by 11.5 dpc of massive apoptosis and dilation of blood vessels and show increased expression of E2f1 and p53/Tp53, as well as many stress-related genes.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi118 – 1192LG → EF: Loss of DNA-binding. 1 Publication
    Mutagenesisi266 – 2672LR → EF: Loss of DNA-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 860860Transcription factor E2F8PRO_0000298910Add
    BLAST

    Proteomic databases

    PRIDEiQ58FA4.

    PTM databases

    PhosphoSiteiQ58FA4.

    Expressioni

    Tissue specificityi

    Highly expressed in liver, skin, thymus and testis. Expressed in trophoblast giant cells throughout placenta development (at protein level).3 Publications

    Inductioni

    Induced at the onset of hepatocyte polyploidization.1 Publication

    Gene expression databases

    BgeeiQ58FA4.
    CleanExiMM_E2F8.
    GenevestigatoriQ58FA4.

    Interactioni

    Subunit structurei

    Interacts with HIF1A By similarity. Homodimer and heterodimer: mainly forms homodimers and, to a lesser extent, heterodimers with E2F8. Dimerization is important for DNA-binding.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-1390691,EBI-1390691

    Protein-protein interaction databases

    BioGridi224496. 1 interaction.
    IntActiQ58FA4. 2 interactions.
    MINTiMINT-8410110.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WZHmodel-A263-341[»]
    F112-181[»]
    ProteinModelPortaliQ58FA4.
    SMRiQ58FA4. Positions 112-180.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    In contrast to classical members of the E2F transcription factor, atypical members contain 2 DNA-binding domains and regulate transcription in a DP-independent manner. Both DNA-binding domains are required for DNA-binding and are proposed to form an intramolecular structure that is similar to the winged helix structure of the E2F-DP heterodimer By similarity.By similarity

    Sequence similaritiesi

    Belongs to the E2F/DP family.Curated

    Phylogenomic databases

    eggNOGiNOG320276.
    GeneTreeiENSGT00530000063616.
    HOGENOMiHOG000013193.
    HOVERGENiHBG063270.
    InParanoidiQ58FA4.
    KOiK09391.
    OMAiLIPLTQC.
    OrthoDBiEOG7HHWSG.
    PhylomeDBiQ58FA4.
    TreeFamiTF105567.

    Family and domain databases

    Gene3Di1.10.10.10. 2 hits.
    InterProiIPR015633. E2F.
    IPR003316. E2F_TDP.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR12081. PTHR12081. 1 hit.
    PfamiPF02319. E2F_TDP. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q58FA4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENQKENLFS EPHKRGLMKS PLHPSSKANM VLAEIQPDLG PLTTPTKPKE    50
    VSQGEPWTPT ANLKMLISAV SPEIRSRDQK RGLSDNRSAL PEARDCLHEH 100
    LSGDEFEKSQ PSRKEKSLGL LCHKFLARYP KYPNPAVNND ICLDEVAEEL 150
    NVERRRIYDI VNVLESLHMV SRLAKNRYTW HGRHNLTKTL GTLKSVGEEN 200
    KYAEQIMMIK RKEYEQEFDF IKSCGIEDHV IKSHTGQNGH SDMCFVELPG 250
    VEFRAASVNS RKDKSLRVMS QKFVMLFLVS TPQIVSLEIA AKILIGEDHV 300
    EDLDKSKYKT KIRRLYDIAN VLSSLDLIKK VHVTEERGRK PAFKWTGPEI 350
    SPNNSGSSPI MPLPASLEAE QSAKENCAKN LFSTRGKPSF TRHPSLIKLV 400
    KSIENDRRKI SSAPSSPVKS NKAESSQNSP PVPNKMAQLA AICKMQLEEQ 450
    SSEPRKKVKV NLARSGHYKP LAPLDPTVNT ELELLTPSLI QPLGVVPLIP 500
    SPLSSAVPVI LPQAPSGPSY AIYLQPAQAQ MLTPPPGLSP TVCPTQPSNA 550
    TGSKDPTDAP AEKTATDAAT TGSLQPAPER HGAKHRSKET TGDRGTKRMI 600
    TAEDSGPSSV KKPKEDLKAL ENVPTPTPLF PSGYLIPLTQ CSSLGPDSVL 650
    SNTENSGTPS PNHRIYGSPI AGVIPVASSE LTAVNFPPFH VTPLKLMVSP 700
    TSMAAVPVGN SPALNSGHPA PAQNPSSAIV NFTLQHLGLI SPGVQMSASP 750
    GPGAGTVPVS PRVEADNLSS RQRRATNHDS PVLGQSQLNG QPVAGTGAQQ 800
    PVPVTPKGSQ LVAENFFRTP GGPTKPTSSP YTDFDGANKT SFGTLFVPQR 850
    KLEVSTEDIH 860
    Length:860
    Mass (Da):93,276
    Last modified:April 26, 2005 - v1
    Checksum:i792E3DDCA299ACE7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651M → T in BAC33794. (PubMed:16141072)Curated
    Sequence conflicti138 – 1381N → Y in AAH86675. (PubMed:15489334)Curated
    Sequence conflicti155 – 1551R → Q in BAC39205. (PubMed:16141072)Curated
    Sequence conflicti209 – 2091I → T in BAC39205. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY957576 mRNA. Translation: AAX49603.1.
    AK049525 mRNA. Translation: BAC33794.1.
    AK084513 mRNA. Translation: BAC39205.1.
    AK154018 mRNA. Translation: BAE32318.1.
    AK157235 mRNA. Translation: BAE34010.1.
    AK160240 mRNA. Translation: BAE35708.1.
    BC086675 mRNA. Translation: AAH86675.1.
    BC100357 mRNA. Translation: AAI00358.1.
    CCDSiCCDS39967.1.
    RefSeqiNP_001013386.2. NM_001013368.5.
    XP_006540616.1. XM_006540553.1.
    XP_006540617.1. XM_006540554.1.
    UniGeneiMm.240566.

    Genome annotation databases

    EnsembliENSMUST00000058745; ENSMUSP00000056778; ENSMUSG00000046179.
    ENSMUST00000119223; ENSMUSP00000112883; ENSMUSG00000046179.
    GeneIDi108961.
    KEGGimmu:108961.
    UCSCiuc009haz.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY957576 mRNA. Translation: AAX49603.1 .
    AK049525 mRNA. Translation: BAC33794.1 .
    AK084513 mRNA. Translation: BAC39205.1 .
    AK154018 mRNA. Translation: BAE32318.1 .
    AK157235 mRNA. Translation: BAE34010.1 .
    AK160240 mRNA. Translation: BAE35708.1 .
    BC086675 mRNA. Translation: AAH86675.1 .
    BC100357 mRNA. Translation: AAI00358.1 .
    CCDSi CCDS39967.1.
    RefSeqi NP_001013386.2. NM_001013368.5.
    XP_006540616.1. XM_006540553.1.
    XP_006540617.1. XM_006540554.1.
    UniGenei Mm.240566.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WZH model - A 263-341 [» ]
    F 112-181 [» ]
    ProteinModelPortali Q58FA4.
    SMRi Q58FA4. Positions 112-180.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 224496. 1 interaction.
    IntActi Q58FA4. 2 interactions.
    MINTi MINT-8410110.

    PTM databases

    PhosphoSitei Q58FA4.

    Proteomic databases

    PRIDEi Q58FA4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000058745 ; ENSMUSP00000056778 ; ENSMUSG00000046179 .
    ENSMUST00000119223 ; ENSMUSP00000112883 ; ENSMUSG00000046179 .
    GeneIDi 108961.
    KEGGi mmu:108961.
    UCSCi uc009haz.2. mouse.

    Organism-specific databases

    CTDi 79733.
    MGIi MGI:1922038. E2f8.

    Phylogenomic databases

    eggNOGi NOG320276.
    GeneTreei ENSGT00530000063616.
    HOGENOMi HOG000013193.
    HOVERGENi HBG063270.
    InParanoidi Q58FA4.
    KOi K09391.
    OMAi LIPLTQC.
    OrthoDBi EOG7HHWSG.
    PhylomeDBi Q58FA4.
    TreeFami TF105567.

    Miscellaneous databases

    ChiTaRSi E2F8. mouse.
    NextBioi 361528.
    PROi Q58FA4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q58FA4.
    CleanExi MM_E2F8.
    Genevestigatori Q58FA4.

    Family and domain databases

    Gene3Di 1.10.10.10. 2 hits.
    InterProi IPR015633. E2F.
    IPR003316. E2F_TDP.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR12081. PTHR12081. 1 hit.
    Pfami PF02319. E2F_TDP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of mouse E2F8, a novel mammalian E2F family member capable of blocking cellular proliferation."
      Maiti B., Li J., de Bruin A., Gordon F., Timmers C., Opavsky R., Patil K., Tuttle J., Cleghorn W., Leone G.
      J. Biol. Chem. 280:18211-18220(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SELF-ASSOCIATION, MUTAGENESIS OF 118-LEU-GLY-119 AND 266-LEU-ARG-267.
      Strain: Swiss Webster.
    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 and NOD.
      Tissue: Heart, Liver, Spleen and Thymus.
    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: C57BL/6.
      Tissue: Head and Placenta.
    4. "Synergistic function of E2F7 and E2F8 is essential for cell survival and embryonic development."
      Li J., Ran C., Li E., Gordon F., Comstock G., Siddiqui H., Cleghorn W., Chen H.-Z., Kornacker K., Liu C.-G., Pandit S.K., Khanizadeh M., Weinstein M., Leone G., de Bruin A.
      Dev. Cell 14:62-75(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    5. "E2F7 and E2F8 promote angiogenesis through transcriptional activation of VEGFA in cooperation with HIF1."
      Weijts B.G., Bakker W.J., Cornelissen P.W., Liang K.H., Schaftenaar F.H., Westendorp B., de Wolf C.A., Paciejewska M., Scheele C.L., Kent L., Leone G., Schulte-Merker S., de Bruin A.
      EMBO J. 31:3871-3884(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. Cited for: FUNCTION, TISSUE SPECIFICITY.
    7. Cited for: FUNCTION, INDUCTION.
    8. Cited for: FUNCTION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiE2F8_MOUSE
    AccessioniPrimary (citable) accession number: Q58FA4
    Secondary accession number(s): Q3U4W2
    , Q497V7, Q5PRE4, Q8BQJ5, Q8C3Y5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 21, 2007
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 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