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Q14209

- E2F2_HUMAN

UniProt

Q14209 - E2F2_HUMAN

Protein

Transcription factor E2F2

Gene

E2F2

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

    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. E2F2 binds specifically to RB1 in a cell-cycle dependent manner.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi107 – 19690Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. intrinsic apoptotic signaling pathway by p53 class mediator Source: Ensembl
    2. lens fiber cell apoptotic process Source: Ensembl
    3. mitotic cell cycle Source: Reactome
    4. regulation of cell cycle Source: Ensembl
    5. transcription initiation from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1181. Association of licensing factors with the pre-replicative complex.
    REACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_1707. CDC6 association with the ORC:origin complex.
    REACT_821. Cyclin D associated events in G1.
    SignaLinkiQ14209.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor E2F2
    Short name:
    E2F-2
    Gene namesi
    Name:E2F2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3114. E2F2.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. transcription factor complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27572.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 437437Transcription factor E2F2PRO_0000219464Add
    BLAST

    Post-translational modificationi

    Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ14209.
    PRIDEiQ14209.

    PTM databases

    PhosphoSiteiQ14209.

    Expressioni

    Tissue specificityi

    Highest level of expression is found in placenta, low levels are found in lung. Found as well in many immortalized cell lines derived from tumor samples.

    Gene expression databases

    BgeeiQ14209.
    CleanExiHS_E2F2.
    GenevestigatoriQ14209.

    Organism-specific databases

    HPAiCAB016313.

    Interactioni

    Subunit structurei

    Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. The E2F2 complex binds specifically hypophosphorylated retinoblastoma protein RB1. During the cell cycle, RB1 becomes phosphorylated in mid-to-late G1 phase, detaches from the DRTF1/E2F complex, rendering E2F transcriptionally active. Viral oncoproteins, notably E1A, T-antigen and HPV E7, are capable of sequestering RB1, thus releasing the active complex. Binds EAPP.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RB1P064003EBI-718476,EBI-491274

    Protein-protein interaction databases

    BioGridi108202. 18 interactions.
    DIPiDIP-258N.
    IntActiQ14209. 9 interactions.
    MINTiMINT-249663.
    STRINGi9606.ENSP00000355249.

    Structurei

    Secondary structure

    1
    437
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi422 – 4243

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N4MX-ray2.20C/D/E410-427[»]
    ProteinModelPortaliQ14209.
    SMRiQ14209. Positions 128-192, 205-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14209.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni65 – 10541Cyclin A/CDK2 bindingSequence AnalysisAdd
    BLAST
    Regioni155 – 17622Leucine-zipperAdd
    BLAST
    Regioni197 – 28993DimerizationSequence AnalysisAdd
    BLAST
    Regioni359 – 43779TransactivationSequence AnalysisAdd
    BLAST
    Regioni410 – 42718Retinoblastoma protein bindingSequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi160 – 19637DEF boxAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi360 – 3634Poly-Pro

    Sequence similaritiesi

    Belongs to the E2F/DP family.Curated

    Phylogenomic databases

    eggNOGiNOG289227.
    HOGENOMiHOG000232045.
    HOVERGENiHBG002227.
    InParanoidiQ14209.
    KOiK09389.
    OMAiKELMSME.
    OrthoDBiEOG738058.
    PhylomeDBiQ14209.
    TreeFamiTF105566.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q14209-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLQGPRALAS AAGQTPKVVP AMSPTELWPS GLSSPQLCPA TATYYTPLYP    50
    QTAPPAAAPG TCLDATPHGP EGQVVRCLPA GRLPAKRKLD LEGIGRPVVP 100
    EFPTPKGKCI RVDGLPSPKT PKSPGEKTRY DTSLGLLTKK FIYLLSESED 150
    GVLDLNWAAE VLDVQKRRIY DITNVLEGIQ LIRKKAKNNI QWVGRGMFED 200
    PTRPGKQQQL GQELKELMNT EQALDQLIQS CSLSFKHLTE DKANKRLAYV 250
    TYQDIRAVGN FKEQTVIAVK APPQTRLEVP DRTEDNLQIY LKSTQGPIEV 300
    YLCPEEVQEP DSPSEEPLPS TSTLCPSPDS AQPSSSTDPS IMEPTASSVP 350
    APAPTPQQAP PPPSLVPLEA TDSLLELPHP LLQQTEDQFL SPTLACSSPL 400
    ISFSPSLDQD DYLWGLEAGE GISDLFDSYD LGDLLIN 437
    Length:437
    Mass (Da):47,506
    Last modified:November 1, 1996 - v1
    Checksum:i60541F4235507005
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti205 – 2051G → R.1 Publication
    Corresponds to variant rs2229297 [ dbSNP | Ensembl ].
    VAR_018990
    Natural varianti226 – 2261Q → H.2 Publications
    Corresponds to variant rs2075995 [ dbSNP | Ensembl ].
    VAR_018991

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22846 mRNA. Translation: AAA16890.1.
    AK313939 mRNA. Translation: BAG36658.1.
    AF518877 Genomic DNA. Translation: AAM54044.1.
    AL021154 Genomic DNA. Translation: CAA15949.1.
    BC053676 mRNA. Translation: AAH53676.1.
    CCDSiCCDS236.1.
    PIRiA54595.
    RefSeqiNP_004082.1. NM_004091.3.
    UniGeneiHs.194333.

    Genome annotation databases

    EnsembliENST00000361729; ENSP00000355249; ENSG00000007968.
    GeneIDi1870.
    KEGGihsa:1870.
    UCSCiuc001bhe.2. human.

    Polymorphism databases

    DMDMi2494228.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22846 mRNA. Translation: AAA16890.1 .
    AK313939 mRNA. Translation: BAG36658.1 .
    AF518877 Genomic DNA. Translation: AAM54044.1 .
    AL021154 Genomic DNA. Translation: CAA15949.1 .
    BC053676 mRNA. Translation: AAH53676.1 .
    CCDSi CCDS236.1.
    PIRi A54595.
    RefSeqi NP_004082.1. NM_004091.3.
    UniGenei Hs.194333.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N4M X-ray 2.20 C/D/E 410-427 [» ]
    ProteinModelPortali Q14209.
    SMRi Q14209. Positions 128-192, 205-306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108202. 18 interactions.
    DIPi DIP-258N.
    IntActi Q14209. 9 interactions.
    MINTi MINT-249663.
    STRINGi 9606.ENSP00000355249.

    PTM databases

    PhosphoSitei Q14209.

    Polymorphism databases

    DMDMi 2494228.

    Proteomic databases

    PaxDbi Q14209.
    PRIDEi Q14209.

    Protocols and materials databases

    DNASUi 1870.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361729 ; ENSP00000355249 ; ENSG00000007968 .
    GeneIDi 1870.
    KEGGi hsa:1870.
    UCSCi uc001bhe.2. human.

    Organism-specific databases

    CTDi 1870.
    GeneCardsi GC01M023832.
    HGNCi HGNC:3114. E2F2.
    HPAi CAB016313.
    MIMi 600426. gene.
    neXtProti NX_Q14209.
    PharmGKBi PA27572.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289227.
    HOGENOMi HOG000232045.
    HOVERGENi HBG002227.
    InParanoidi Q14209.
    KOi K09389.
    OMAi KELMSME.
    OrthoDBi EOG738058.
    PhylomeDBi Q14209.
    TreeFami TF105566.

    Enzyme and pathway databases

    Reactomei REACT_1181. Association of licensing factors with the pre-replicative complex.
    REACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_1707. CDC6 association with the ORC:origin complex.
    REACT_821. Cyclin D associated events in G1.
    SignaLinki Q14209.

    Miscellaneous databases

    EvolutionaryTracei Q14209.
    GeneWikii E2F2.
    GenomeRNAii 1870.
    NextBioi 7647.
    PROi Q14209.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q14209.
    CleanExi HS_E2F2.
    Genevestigatori Q14209.

    Family and domain databases

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

    Publicationsi

    1. "Cloning and characterization of E2F-2, a novel protein with the biochemical properties of transcription factor E2F."
      Ivey-Hoyle M., Conroy R., Huber H.E., Goodhart P.J., Oliff A., Heimbrook D.C.
      Mol. Cell. Biol. 13:7802-7812(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cervix carcinoma.
    2. "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: Brain.
    3. NIEHS SNPs program
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-205 AND HIS-226.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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], VARIANT HIS-226.
      Tissue: Eye.
    6. "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.
    7. "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: INTERACTION WITH EAPP.
    8. "Structural basis for the recognition of the E2F transactivation domain by the retinoblastoma tumor suppressor."
      Lee C., Chang J.H., Lee H.S., Cho Y.
      Genes Dev. 16:3199-3212(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 410-427 IN COMPLEX WITH RB.

    Entry informationi

    Entry nameiE2F2_HUMAN
    AccessioniPrimary (citable) accession number: Q14209
    Secondary accession number(s): B2R9W1, Q7Z6H1
    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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3