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Q8R0K9

- E2F4_MOUSE

UniProt

Q8R0K9 - E2F4_MOUSE

Protein

Transcription factor E2F4

Gene

E2f4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F4 binds with high affinity to RBL1 and RBL2. In some instances, can also bind RB1 By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi16 – 8570Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. protein binding Source: MGI
    3. sequence-specific DNA binding transcription factor activity Source: MGI

    GO - Biological processi

    1. blood circulation Source: MGI
    2. cell volume homeostasis Source: MGI
    3. cilium assembly Source: MGI
    4. epithelial cell development Source: MGI
    5. organ morphogenesis Source: MGI
    6. regulation of cell cycle Source: MGI
    7. regulation of cell proliferation Source: MGI
    8. regulation of cell size Source: MGI
    9. regulation of transcription, DNA-templated Source: MGI
    10. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: MGI
    11. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_199110. G0 and Early G1.
    REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor E2F4
    Short name:
    E2F-4
    Gene namesi
    Name:E2f4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:103012. E2f4.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 410409Transcription factor E2F4PRO_0000322638Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Post-translational modificationi

    Differentially phosphorylated in vivo.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8R0K9.
    PaxDbiQ8R0K9.
    PRIDEiQ8R0K9.

    PTM databases

    PhosphoSiteiQ8R0K9.

    Expressioni

    Gene expression databases

    BgeeiQ8R0K9.
    CleanExiMM_E2F4.
    GenevestigatoriQ8R0K9.

    Interactioni

    Subunit structurei

    Component of the DRTF1/E2F transcription factor complex. Binds cooperatively with TFDP1/Dp-1 to E2F sites. The E2F4/TFDP1 dimer interacts preferentially with pocket protein RBL1, which inhibits the E2F transactivation domain. Lower affinity interaction has been found with retinoblastoma protein RB1. Interacts with TRRAP, which probably mediates its interaction with histone acetyltransferase complexes, leading to transcription activation. Interacts with HCFC1. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2 By similarity. Interacts with PML By similarity.By similarity

    Protein-protein interaction databases

    BioGridi222608. 4 interactions.
    IntActiQ8R0K9. 10 interactions.
    MINTiMINT-4301946.
    STRINGi10090.ENSMUSP00000015003.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8R0K9.
    SMRiQ8R0K9. Positions 16-82.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni43 – 6523Leucine-zipperAdd
    BLAST
    Regioni86 – 18196DimerizationSequence AnalysisAdd
    BLAST
    Regioni334 – 41077TransactivationSequence AnalysisAdd
    BLAST
    Regioni387 – 40418Interaction with RBL1 and RBL2Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi48 – 8538DEF boxBy similarityAdd
    BLAST
    Motifi386 – 3894HCFC1-binding-motif (HBM)By similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 124Poly-Pro
    Compositional biasi308 – 32417Poly-SerAdd
    BLAST

    Sequence similaritiesi

    Belongs to the E2F/DP family.Curated

    Phylogenomic databases

    eggNOGiNOG289227.
    GeneTreeiENSGT00550000074403.
    HOGENOMiHOG000232045.
    HOVERGENiHBG002227.
    InParanoidiQ8R0K9.
    KOiK04682.
    OMAiPHTLAYV.
    OrthoDBiEOG7WHHB1.
    PhylomeDBiQ8R0K9.
    TreeFamiTF105566.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR015633. E2F.
    IPR028312. E2F4.
    IPR003316. E2F_TDP.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR12081. PTHR12081. 1 hit.
    PTHR12081:SF42. PTHR12081:SF42. 1 hit.
    PfamiPF02319. E2F_TDP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8R0K9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEAGPQAPP PPGTPSRHEK SLGLLTTKFV SLLQEAKDGV LDLKLAADTL    50
    AVRQKRRIYD ITNVLEGIGL IEKKSKNSIQ WKGVGPGCNT REIADKLIEL 100
    KAEIEELQQR EQELDQHKVW VQQSIRNVTE DVQNSCLAYV THEDICRCFA 150
    GDTLLAIRAP SGTSLEVPIP EGLNGQKKYQ IHLKSMSGPI EVLLVNKEAW 200
    SSPPVAVPVP PPDDLLQSPP AVSTPPPLPK PALAQPQESS PPSSPQLTTP 250
    TPVLGSTQVS EVACQTSEIA VSGSPGTENK DSGEVSSLPL GLTALDTRPL 300
    QSSALLDSSS SSSSSSSSSS SSSSGPNPST SFEPIKADPT GVLDLPKELS 350
    EIFDPTRECM SSELLEELMS SEVFAPLLRL SPPPGDHDYI YNLDESEGVC 400
    DLFDVPVLKL 410
    Length:410
    Mass (Da):43,833
    Last modified:June 1, 2002 - v1
    Checksum:iA8BD1A24B38C2B01
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti326 – 3261P → T in AAH27048. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK145950 mRNA. Translation: BAE26778.1.
    AK157028 mRNA. Translation: BAE33937.1.
    BC023859 mRNA. Translation: AAH23859.1.
    BC026649 mRNA. Translation: AAH26649.1.
    BC027048 mRNA. Translation: AAH27048.1.
    CCDSiCCDS40456.1.
    RefSeqiNP_683754.1. NM_148952.1.
    UniGeneiMm.34554.

    Genome annotation databases

    EnsembliENSMUST00000015003; ENSMUSP00000015003; ENSMUSG00000014859.
    GeneIDi104394.
    KEGGimmu:104394.
    UCSCiuc009ncl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK145950 mRNA. Translation: BAE26778.1 .
    AK157028 mRNA. Translation: BAE33937.1 .
    BC023859 mRNA. Translation: AAH23859.1 .
    BC026649 mRNA. Translation: AAH26649.1 .
    BC027048 mRNA. Translation: AAH27048.1 .
    CCDSi CCDS40456.1.
    RefSeqi NP_683754.1. NM_148952.1.
    UniGenei Mm.34554.

    3D structure databases

    ProteinModelPortali Q8R0K9.
    SMRi Q8R0K9. Positions 16-82.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 222608. 4 interactions.
    IntActi Q8R0K9. 10 interactions.
    MINTi MINT-4301946.
    STRINGi 10090.ENSMUSP00000015003.

    PTM databases

    PhosphoSitei Q8R0K9.

    Proteomic databases

    MaxQBi Q8R0K9.
    PaxDbi Q8R0K9.
    PRIDEi Q8R0K9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000015003 ; ENSMUSP00000015003 ; ENSMUSG00000014859 .
    GeneIDi 104394.
    KEGGi mmu:104394.
    UCSCi uc009ncl.1. mouse.

    Organism-specific databases

    CTDi 1874.
    MGIi MGI:103012. E2f4.

    Phylogenomic databases

    eggNOGi NOG289227.
    GeneTreei ENSGT00550000074403.
    HOGENOMi HOG000232045.
    HOVERGENi HBG002227.
    InParanoidi Q8R0K9.
    KOi K04682.
    OMAi PHTLAYV.
    OrthoDBi EOG7WHHB1.
    PhylomeDBi Q8R0K9.
    TreeFami TF105566.

    Enzyme and pathway databases

    Reactomei REACT_199110. G0 and Early G1.
    REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.

    Miscellaneous databases

    ChiTaRSi E2F4. mouse.
    NextBioi 357065.
    PROi Q8R0K9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8R0K9.
    CleanExi MM_E2F4.
    Genevestigatori Q8R0K9.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR015633. E2F.
    IPR028312. E2F4.
    IPR003316. E2F_TDP.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR12081. PTHR12081. 1 hit.
    PTHR12081:SF42. PTHR12081:SF42. 1 hit.
    Pfami PF02319. E2F_TDP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Liver and Spleen.
    2. "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: Czech II and FVB/N.
      Tissue: Colon and Mammary tumor.

    Entry informationi

    Entry nameiE2F4_MOUSE
    AccessioniPrimary (citable) accession number: Q8R0K9
    Secondary accession number(s): Q8R2X6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 114 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

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3