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Q15329

- E2F5_HUMAN

UniProt

Q15329 - E2F5_HUMAN

Protein

Transcription factor E2F5

Gene

E2F5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Transcriptional activator that binds to E2F sites, these sites are present in the promoter of many genes whose products are involved in cell proliferation. May mediate growth factor-initiated signal transduction. It is likely involved in the early responses of resting cells to growth factor stimulation.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi47 – 11872Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. sequence-specific DNA binding transcription factor activity Source: ProtInc
    4. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mitotic cell cycle Source: Reactome
    3. organ morphogenesis Source: Ensembl
    4. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
    5. regulation of cell cycle Source: InterPro
    6. transcription, DNA-templated Source: Reactome
    7. transcription initiation from RNA polymerase II promoter Source: Reactome
    8. transforming growth factor beta receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_111214. G0 and Early G1.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_821. Cyclin D associated events in G1.
    SignaLinkiQ15329.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor E2F5
    Short name:
    E2F-5
    Gene namesi
    Name:E2F5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:3119. E2F5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleoplasm Source: Reactome
    3. transcription factor complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27577.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 346346Transcription factor E2F5PRO_0000219469Add
    BLAST

    Proteomic databases

    MaxQBiQ15329.
    PaxDbiQ15329.
    PRIDEiQ15329.

    PTM databases

    PhosphoSiteiQ15329.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15329.
    BgeeiQ15329.
    CleanExiHS_E2F5.
    GenevestigatoriQ15329.

    Interactioni

    Subunit structurei

    Component of the DRTF1/E2F transcription factor complex. Binds cooperatively with DP-1 to E2F sites. Interaction with retinoblastoma protein RB1 or proteins RBL1 and RBL2 inhibits the E2F transactivation domain. 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 MYBL2.3 Publications

    Protein-protein interaction databases

    BioGridi108207. 6 interactions.
    DIPiDIP-24229N.
    IntActiQ15329. 4 interactions.
    STRINGi9606.ENSP00000398124.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15329.
    SMRiQ15329. Positions 49-115.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni76 – 9823Leucine-zipperAdd
    BLAST
    Regioni119 – 21597DimerizationSequence AnalysisAdd
    BLAST
    Regioni287 – 34660TransactivationSequence AnalysisAdd
    BLAST
    Regioni323 – 34018RBL2 associationSequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi81 – 11838DEF boxAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi33 – 397Poly-Pro
    Compositional biasi233 – 2364Poly-Ser

    Sequence similaritiesi

    Belongs to the E2F/DP family.Curated

    Phylogenomic databases

    eggNOGiNOG289227.
    HOGENOMiHOG000232045.
    HOVERGENiHBG002227.
    InParanoidiQ15329.
    KOiK04682.
    OrthoDBiEOG7WHHB1.
    PhylomeDBiQ15329.
    TreeFamiTF105566.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR015633. E2F.
    IPR028316. E2F5.
    IPR003316. E2F_TDP.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR12081. PTHR12081. 1 hit.
    PTHR12081:SF35. PTHR12081:SF35. 1 hit.
    PfamiPF02319. E2F_TDP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15329-1) [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

    MAAAEPASSG QQAPAGQGQG QRPPPQPPQA QAPQPPPPPQ LGGAGGGSSR    50
    HEKSLGLLTT KFVSLLQEAK DGVLDLKAAA DTLAVRQKRR IYDITNVLEG 100
    IDLIEKKSKN SIQWKGVGAG CNTKEVIDRL RYLKAEIEDL ELKERELDQQ 150
    KLWLQQSIKN VMDDSINNRF SYVTHEDICN CFNGDTLLAI QAPSGTQLEV 200
    PIPEMGQNGQ KKYQINLKSH SGPIHVLLIN KESSSSKPVV FPVPPPDDLT 250
    QPSSQSLTPV TPQKSSMATQ NLPEQHVSER SQALQQTSAT DISSAGSISG 300
    DIIDELMSSD VFPLLRLSPT PADDYNFNLD DNEGVCDLFD VQILNY 346
    Length:346
    Mass (Da):37,610
    Last modified:November 1, 1996 - v1
    Checksum:iF1408A755E67D879
    GO
    Isoform 2 (identifier: Q15329-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         295-295: Missing.

    Show »
    Length:345
    Mass (Da):37,539
    Checksum:i0CBCD335800F4863
    GO
    Isoform 3 (identifier: Q15329-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-161: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:185
    Mass (Da):20,192
    Checksum:iAECF4C7A7000F8BD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531W → L in CAB01634. (PubMed:9464260)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181G → A.1 Publication
    Corresponds to variant rs4150841 [ dbSNP | Ensembl ].
    VAR_014348

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 161161Missing in isoform 3. 1 PublicationVSP_044660Add
    BLAST
    Alternative sequencei295 – 2951Missing in isoform 2. 2 PublicationsVSP_040098

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31556 mRNA. Translation: AAB00179.1.
    X86097 mRNA. Translation: CAA60051.1.
    U15642 mRNA. Translation: AAC50120.1.
    Z78409 mRNA. Translation: CAB01634.1.
    AY162833 Genomic DNA. Translation: AAN46737.1.
    AL583354 mRNA. No translation available.
    AC011773 Genomic DNA. No translation available.
    CCDSiCCDS47885.1. [Q15329-1]
    CCDS47886.1. [Q15329-2]
    CCDS55254.1. [Q15329-3]
    PIRiJC5833.
    RefSeqiNP_001077057.1. NM_001083588.1. [Q15329-2]
    NP_001077058.1. NM_001083589.1. [Q15329-3]
    NP_001942.2. NM_001951.3. [Q15329-1]
    XP_006716497.1. XM_006716434.1. [Q15329-3]
    UniGeneiHs.445758.

    Genome annotation databases

    EnsembliENST00000416274; ENSP00000398124; ENSG00000133740. [Q15329-1]
    ENST00000418930; ENSP00000414312; ENSG00000133740. [Q15329-2]
    ENST00000517476; ENSP00000429120; ENSG00000133740. [Q15329-3]
    GeneIDi1875.
    KEGGihsa:1875.
    UCSCiuc003ycz.4. human. [Q15329-1]
    uc003yda.4. human. [Q15329-2]

    Polymorphism databases

    DMDMi2494230.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31556 mRNA. Translation: AAB00179.1 .
    X86097 mRNA. Translation: CAA60051.1 .
    U15642 mRNA. Translation: AAC50120.1 .
    Z78409 mRNA. Translation: CAB01634.1 .
    AY162833 Genomic DNA. Translation: AAN46737.1 .
    AL583354 mRNA. No translation available.
    AC011773 Genomic DNA. No translation available.
    CCDSi CCDS47885.1. [Q15329-1 ]
    CCDS47886.1. [Q15329-2 ]
    CCDS55254.1. [Q15329-3 ]
    PIRi JC5833.
    RefSeqi NP_001077057.1. NM_001083588.1. [Q15329-2 ]
    NP_001077058.1. NM_001083589.1. [Q15329-3 ]
    NP_001942.2. NM_001951.3. [Q15329-1 ]
    XP_006716497.1. XM_006716434.1. [Q15329-3 ]
    UniGenei Hs.445758.

    3D structure databases

    ProteinModelPortali Q15329.
    SMRi Q15329. Positions 49-115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108207. 6 interactions.
    DIPi DIP-24229N.
    IntActi Q15329. 4 interactions.
    STRINGi 9606.ENSP00000398124.

    PTM databases

    PhosphoSitei Q15329.

    Polymorphism databases

    DMDMi 2494230.

    Proteomic databases

    MaxQBi Q15329.
    PaxDbi Q15329.
    PRIDEi Q15329.

    Protocols and materials databases

    DNASUi 1875.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000416274 ; ENSP00000398124 ; ENSG00000133740 . [Q15329-1 ]
    ENST00000418930 ; ENSP00000414312 ; ENSG00000133740 . [Q15329-2 ]
    ENST00000517476 ; ENSP00000429120 ; ENSG00000133740 . [Q15329-3 ]
    GeneIDi 1875.
    KEGGi hsa:1875.
    UCSCi uc003ycz.4. human. [Q15329-1 ]
    uc003yda.4. human. [Q15329-2 ]

    Organism-specific databases

    CTDi 1875.
    GeneCardsi GC08P086089.
    HGNCi HGNC:3119. E2F5.
    MIMi 600967. gene.
    neXtProti NX_Q15329.
    PharmGKBi PA27577.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289227.
    HOGENOMi HOG000232045.
    HOVERGENi HBG002227.
    InParanoidi Q15329.
    KOi K04682.
    OrthoDBi EOG7WHHB1.
    PhylomeDBi Q15329.
    TreeFami TF105566.

    Enzyme and pathway databases

    Reactomei REACT_111214. G0 and Early G1.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_821. Cyclin D associated events in G1.
    SignaLinki Q15329.

    Miscellaneous databases

    ChiTaRSi E2F5. human.
    GeneWikii E2F5.
    GenomeRNAii 1875.
    NextBioi 7663.
    PROi Q15329.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15329.
    Bgeei Q15329.
    CleanExi HS_E2F5.
    Genevestigatori Q15329.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR015633. E2F.
    IPR028316. E2F5.
    IPR003316. E2F_TDP.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR12081. PTHR12081. 1 hit.
    PTHR12081:SF35. PTHR12081:SF35. 1 hit.
    Pfami PF02319. E2F_TDP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural characterization and specificity of expression of E2F-5: a new member of the E2F family of transcription factors."
      Itoh A., Levinson S.F., Morita T., Kourembanas S., Brody J.S., Mitsialis S.A.
      Cell. Mol. Biol. Res. 41:147-154(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Fetal lung and Placenta.
    2. "E2F-5, a new E2F family member that interacts with p130 in vivo."
      Hijmans E.M., Voorhoeve P.M., Beijersbergen R.L., van 't Veer L.J., Bernards R.
      Mol. Cell. Biol. 15:3082-3089(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RBL2.
      Tissue: Colon carcinoma.
    3. "E2F-4 and E2F-5, two members of the E2F family, are expressed in the early phases of the cell cycle."
      Sardet C., Vidal M., Cobrinik D., Geng Y., Onufryk C., Chen A., Weinberg R.A.
      Proc. Natl. Acad. Sci. U.S.A. 92:2403-2407(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "The molecular and functional characterization of E2F-5 transcription factor."
      Vaishnav Y.N., Vaishnav M.Y., Pant V.
      Biochem. Biophys. Res. Commun. 242:586-592(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. NIEHS SNPs program
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-18.
    6. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: B-cell.
    7. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release."
      Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.
      Cell 123:1093-1106(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WITH RB1 AND TFDP1.
    9. "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence."
      Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K., Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.
      Mol. Cell 26:539-551(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE DREAM COMPLEX.

    Entry informationi

    Entry nameiE2F5_HUMAN
    AccessioniPrimary (citable) accession number: Q15329
    Secondary accession number(s): E9PBN9, Q16601, Q92756
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 136 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 8
      Human chromosome 8: 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