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Q8CCE9

- E4F1_MOUSE

UniProt

Q8CCE9 - E4F1_MOUSE

Protein

Transcription factor E4F1

Gene

E4f1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (18 Mar 2008)
      Previous versions | rss
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    Functioni

    May function as a transcriptional repressor. May also function as a ubiquitin ligase mediating ubiquitination of chromatin-associated TP53. Functions in cell survival and proliferation through control of the cell cycle. Functions in the p53 and pRB tumor suppressor pathways and regulates the cyclin CCNA2 transcription.4 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri193 – 21523C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri221 – 24323C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri249 – 27325C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri434 – 45623C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri462 – 48423C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri490 – 51223C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri518 – 54023C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri546 – 56823C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri574 – 59623C2H2-type 9; degeneratePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cAMP response element binding Source: Ensembl
    2. DNA binding Source: MGI
    3. ligase activity Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: IntAct

    GO - Biological processi

    1. DNA replication Source: MGI
    2. mitotic nuclear division Source: UniProtKB-KW
    3. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    4. protein ubiquitination Source: UniProtKB-UniPathway
    5. regulation of cell cycle process Source: UniProtKB
    6. regulation of growth Source: UniProtKB-KW
    7. regulation of mitotic cell cycle, embryonic Source: MGI
    8. regulation of transcription, DNA-templated Source: MGI
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase, Repressor

    Keywords - Biological processi

    Cell cycle, Cell division, Growth regulation, Mitosis, Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor E4F1 (EC:6.3.2.-)
    Alternative name(s):
    E4F transcription factor 1
    Putative E3 ubiquitin-protein ligase E4F1
    Transcription factor E4F
    Transcription factor phi AP3
    p120E4F
    Gene namesi
    Name:E4f1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:109530. E4f1.

    Subcellular locationi

    Nucleusnucleoplasm 2 Publications. Cytoplasm By similarity
    Note: A small fraction is detected in the cytoplasm By similarity. Excluded from the nucleolus where it is targeted upon CDKN2A overexpression. Localizes to the mitotic spindle during embryogenesis.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleoplasm Source: UniProtKB-SubCell
    3. nucleus Source: MGI
    4. spindle Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Death before E7.5 probably at the peri-implantation stage. Blastocysts display defects in mitotic progression and chromosomal segregation and increased apoptosis.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 783783Transcription factor E4F1PRO_0000324308Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei49 – 491PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated; phosphorylation is cell cycle-dependent and regulates DNA-binding activity and function.1 Publication
    May be sumoylated by UBE2I upon interaction with CDKN2A.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ8CCE9.

    PTM databases

    PhosphoSiteiQ8CCE9.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.2 Publications

    Developmental stagei

    Continuously expressed during embryogenesis.1 Publication

    Gene expression databases

    BgeeiQ8CCE9.
    CleanExiMM_E4F1.
    GenevestigatoriQ8CCE9.

    Interactioni

    Subunit structurei

    Homodimer; binds DNA as a dimer By similarity. Forms a complex with CDKN2A and TP53. Interacts with HDAC1, HMGA2 and RASSF1 By similarity. Interactions with TP53, RB1, ANP32A and probably BMI1 and FHL2 regulate E4F1 activity.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Anp32aO353812EBI-7450874,EBI-643140

    Protein-protein interaction databases

    BioGridi199353. 2 interactions.
    IntActiQ8CCE9. 1 interaction.
    MINTiMINT-4979074.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CCE9.
    SMRiQ8CCE9. Positions 182-271, 443-634.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 8445Required for ubiquitin ligase activityBy similarityAdd
    BLAST
    Regioni185 – 26480Mediates dimerization, DNA-binding, transcription repression of CCNA2 and interaction with HMGA2By similarityAdd
    BLAST
    Regioni368 – 565198Mediates interaction with CDKN2ABy similarityAdd
    BLAST
    Regioni434 – 598165Interaction with BMI1By similarityAdd
    BLAST
    Regioni520 – 57960Mediates interaction with TP53By similarityAdd
    BLAST
    Regioni574 – 59623Mediates interaction with RASSF1By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 9 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri193 – 21523C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri221 – 24323C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri249 – 27325C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri434 – 45623C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri462 – 48423C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri490 – 51223C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri518 – 54023C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri546 – 56823C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri574 – 59623C2H2-type 9; degeneratePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    GeneTreeiENSGT00390000006768.
    HOVERGENiHBG052707.
    InParanoidiQ8CCE9.
    OMAiCQFCSRG.
    OrthoDBiEOG761BT6.
    PhylomeDBiQ8CCE9.
    TreeFamiTF315387.

    Family and domain databases

    Gene3Di3.30.160.60. 8 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF00096. zf-C2H2. 2 hits.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 10 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 7 hits.
    PS50157. ZINC_FINGER_C2H2_2. 9 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8CCE9-1) [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

    MEGAMAVRVT AAHTAEARAE AGREAGEGGV AAAAALSSGG FLGLPAPFSE    50
    EDEDDVHRCG RCQVEFTALE DFVQHKIQKT CHRAPQEALP TTPAATALLD 100
    QEVVPTAAEG GPDEPITVAH IVVEATSLAE DISHAPDLVG SGHIKEVIVA 150
    AEAEPGDVEM AEAPGSPNHQ ELGLLGEGEQ AHVKLLVNKE GRYVCMLCHK 200
    TFKTGSILKA HMVTHSSRKD HECKLCGASF RTKGSLIRHH RRHTDERPYK 250
    CAKCGKSFRE SGALTRHLKS LTPCTEKIRF SISKDTAVGK EEVPAGSSAS 300
    TVGTVTSSVA GDPMETSPVI HLVTDAKGTV IHEVHVQMQE LPLGMKALTP 350
    ESPDSEELPC SSENSRENLL HQAMQNSGIV LERVAGEESA LEPAPPSGSS 400
    PQCLGDGSPE LPLLKVEQIE TQVASEAATV PRTHPCPQCS ETFPTAATLE 450
    AHKRGHIAPR PFTCTQCGKA FPKAYLLKKH QEVHVHERRF RCGDCGKLYK 500
    TIAHVRGHRR VHSDERPFPC PQCGKRYKTK NAQQVHFRTH LEEKPHVCQF 550
    CSRGFREKGS LVRHVRHHTG EKPFKCYKCG RGFAEHGTLN RHLRTKGGCL 600
    LEVEELLVSE ESPSAAATVL AEDPHTVLVE FSSVVADTQE YIIEATADDT 650
    ETSEATEIIE GTQTEVDSHI MKVVQQIVHQ AGAGHQIIVQ NVTMDQETAL 700
    GSEATAADTI TIATPESLTE QVAMTLASAI SEGTVLTARA GPNSTEQATV 750
    TMVSSEDIEI LEHGGELVIA SPEGQLEVQT VIV 783
    Length:783
    Mass (Da):84,296
    Last modified:March 18, 2008 - v2
    Checksum:i59E47F7A64A224A4
    GO
    Isoform 2 (identifier: Q8CCE9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         667-684: DSHIMKVVQQIVHQAGAG → RVWVRDGRITGLLGSPSG
         685-783: Missing.

    Show »
    Length:684
    Mass (Da):74,060
    Checksum:i62B9E2973ACA07C3
    GO
    Isoform 3 (identifier: Q8CCE9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         422-422: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:782
    Mass (Da):84,168
    Checksum:iF0CEA4AC61FE5BDA
    GO
    Isoform 4 (identifier: Q8CCE9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         458-458: A → VWQGLPQSLP...AWHTQPAPAH
         459-783: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:586
    Mass (Da):62,553
    Checksum:i03DE21745C393119
    GO
    Isoform 5 (identifier: Q8CCE9-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         244-274: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:752
    Mass (Da):80,830
    Checksum:iBC7A27C32B98E325
    GO

    Sequence cautioni

    The sequence AAF22563.1 differs from that shown. Reason: Frameshift at positions 230 and 235.
    The sequence AAH71228.1 differs from that shown. Reason: Frameshift at position 94.
    The sequence BAE25748.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA54188.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131H → D in BAE25748. (PubMed:16141072)Curated
    Sequence conflicti18 – 181R → G in AAF22563. 1 PublicationCurated
    Sequence conflicti18 – 181R → G in BAE25748. (PubMed:16141072)Curated
    Sequence conflicti18 – 181R → G in AAH46459. (PubMed:15489334)Curated
    Sequence conflicti18 – 181R → G in AAH71228. (PubMed:15489334)Curated
    Sequence conflicti30 – 301V → VA in AAF22563. 1 PublicationCurated
    Sequence conflicti30 – 301V → VA in BAE25748. (PubMed:16141072)Curated
    Sequence conflicti62 – 621C → F in BAE25748. (PubMed:16141072)Curated
    Sequence conflicti139 – 1391V → A in CAA54188. (PubMed:8262041)Curated
    Sequence conflicti148 – 1481I → V in CAA54188. (PubMed:8262041)Curated
    Sequence conflicti158 – 1581V → G in AAF22563. 1 PublicationCurated
    Sequence conflicti158 – 1581V → G in BAE25748. (PubMed:16141072)Curated
    Sequence conflicti158 – 1581V → G in AAH46459. (PubMed:15489334)Curated
    Sequence conflicti158 – 1581V → G in AAH71228. (PubMed:15489334)Curated
    Sequence conflicti158 – 1581V → G in CAA54188. (PubMed:8262041)Curated
    Sequence conflicti224 – 2252KL → NF in AAF22563. 1 PublicationCurated
    Sequence conflicti281 – 2811S → N in AAF22563. 1 PublicationCurated
    Sequence conflicti281 – 2811S → N in BAE25748. (PubMed:16141072)Curated
    Sequence conflicti380 – 3801V → L in AAF22563. 1 PublicationCurated
    Sequence conflicti390 – 3901A → V in AAF22563. 1 PublicationCurated
    Sequence conflicti395 – 4006PPSGSS → LPFGST in AAF22563. 1 PublicationCurated
    Sequence conflicti412 – 4121P → L in AAF22563. 1 PublicationCurated
    Sequence conflicti479 – 4802KH → ND in CAA54188. (PubMed:8262041)Curated
    Sequence conflicti585 – 5862EH → DD in CAA54188. (PubMed:8262041)Curated
    Sequence conflicti630 – 6301E → Q in AAF22563. 1 PublicationCurated
    Sequence conflicti630 – 6301E → Q in BAE25748. (PubMed:16141072)Curated
    Sequence conflicti630 – 6301E → Q in AAH46459. (PubMed:15489334)Curated
    Sequence conflicti630 – 6301E → Q in CAA54188. (PubMed:8262041)Curated
    Sequence conflicti705 – 7051T → A in AAF22563. 1 PublicationCurated
    Sequence conflicti705 – 7051T → A in BAE25748. (PubMed:16141072)Curated
    Sequence conflicti705 – 7051T → A in CAA54188. (PubMed:8262041)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei244 – 27431Missing in isoform 5. 1 PublicationVSP_032192Add
    BLAST
    Alternative sequencei422 – 4221Missing in isoform 3. 1 PublicationVSP_032193
    Alternative sequencei458 – 4581A → VWQGLPQSLPAQEAPGGARA RAPLPLWRLWEALQDHRSCA GPPACSLRREAFPLSPVRQA LQNQECPASTLPDTSGRKAP RVPVLQPRLPGEGLSGAACE APHRRETFQVLQVWPWLRGA WHTQPAPAH in isoform 4. 1 PublicationVSP_032194
    Alternative sequencei459 – 783325Missing in isoform 4. 1 PublicationVSP_032195Add
    BLAST
    Alternative sequencei667 – 68418DSHIM…QAGAG → RVWVRDGRITGLLGSPSG in isoform 2. 1 PublicationVSP_032196Add
    BLAST
    Alternative sequencei685 – 78399Missing in isoform 2. 1 PublicationVSP_032197Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126967 mRNA. Translation: AAF22563.1. Frameshift.
    AK033285 mRNA. Translation: BAC28222.1.
    AK144176 mRNA. Translation: BAE25748.1. Different initiation.
    BC046459 mRNA. Translation: AAH46459.1.
    BC057011 mRNA. Translation: AAH57011.1.
    BC071228 mRNA. Translation: AAH71228.1. Frameshift.
    X76858 mRNA. Translation: CAA54188.1. Different initiation.
    CCDSiCCDS28481.1. [Q8CCE9-3]
    PIRiS41688.
    RefSeqiNP_031919.2. NM_007893.3. [Q8CCE9-3]
    XP_006523657.1. XM_006523594.1. [Q8CCE9-1]
    UniGeneiMm.163132.

    Genome annotation databases

    EnsembliENSMUST00000056032; ENSMUSP00000062344; ENSMUSG00000024137. [Q8CCE9-3]
    GeneIDi13560.
    KEGGimmu:13560.
    UCSCiuc008avy.1. mouse. [Q8CCE9-3]
    uc008awa.1. mouse. [Q8CCE9-1]
    uc008awb.1. mouse. [Q8CCE9-2]
    uc012ami.1. mouse. [Q8CCE9-5]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126967 mRNA. Translation: AAF22563.1 . Frameshift.
    AK033285 mRNA. Translation: BAC28222.1 .
    AK144176 mRNA. Translation: BAE25748.1 . Different initiation.
    BC046459 mRNA. Translation: AAH46459.1 .
    BC057011 mRNA. Translation: AAH57011.1 .
    BC071228 mRNA. Translation: AAH71228.1 . Frameshift.
    X76858 mRNA. Translation: CAA54188.1 . Different initiation.
    CCDSi CCDS28481.1. [Q8CCE9-3 ]
    PIRi S41688.
    RefSeqi NP_031919.2. NM_007893.3. [Q8CCE9-3 ]
    XP_006523657.1. XM_006523594.1. [Q8CCE9-1 ]
    UniGenei Mm.163132.

    3D structure databases

    ProteinModelPortali Q8CCE9.
    SMRi Q8CCE9. Positions 182-271, 443-634.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199353. 2 interactions.
    IntActi Q8CCE9. 1 interaction.
    MINTi MINT-4979074.

    PTM databases

    PhosphoSitei Q8CCE9.

    Proteomic databases

    PRIDEi Q8CCE9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000056032 ; ENSMUSP00000062344 ; ENSMUSG00000024137 . [Q8CCE9-3 ]
    GeneIDi 13560.
    KEGGi mmu:13560.
    UCSCi uc008avy.1. mouse. [Q8CCE9-3 ]
    uc008awa.1. mouse. [Q8CCE9-1 ]
    uc008awb.1. mouse. [Q8CCE9-2 ]
    uc012ami.1. mouse. [Q8CCE9-5 ]

    Organism-specific databases

    CTDi 1877.
    MGIi MGI:109530. E4f1.

    Phylogenomic databases

    eggNOGi COG5048.
    GeneTreei ENSGT00390000006768.
    HOVERGENi HBG052707.
    InParanoidi Q8CCE9.
    OMAi CQFCSRG.
    OrthoDBi EOG761BT6.
    PhylomeDBi Q8CCE9.
    TreeFami TF315387.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    NextBioi 284182.
    PROi Q8CCE9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8CCE9.
    CleanExi MM_E4F1.
    Genevestigatori Q8CCE9.

    Family and domain databases

    Gene3Di 3.30.160.60. 8 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF00096. zf-C2H2. 2 hits.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 10 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 7 hits.
    PS50157. ZINC_FINGER_C2H2_2. 9 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Repression of the murine Il-1 beta expression by the murine analog of E4F transcription factor."
      Lebedeva T.V., Singh A.K.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-783 (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Embryonic testis.
    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] (ISOFORMS 2 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-783 (ISOFORM 5).
      Strain: C57BL/6, FVB/N and NMRI.
      Tissue: Brain and Mammary tumor.
    4. "Repression of adenovirus E1A enhancer activity by a novel zinc finger-containing DNA-binding protein related to the GLI-Kruppel protein."
      Fognani C., Della Valle G., Babiss L.E.
      EMBO J. 12:4985-4992(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 65-783 (ISOFORM 1), FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, PHOSPHORYLATION, TISSUE SPECIFICITY.
      Strain: BALB/c.
      Tissue: Liver.
    5. "Chromosomal location and tissue expression of the gene encoding the adenovirus E1A-regulated transcription factor E4F in humans and mice."
      Rooney R.J., Daniels R.R., Jenkins N.A., Gilbert D.J., Rothammer K., Morris S.W., Higgs D.R., Copeland N.G.
      Mamm. Genome 9:320-323(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    6. Cited for: FUNCTION, INTERACTION WITH TP53.
    7. "pRB binds to and modulates the transrepressing activity of the E1A-regulated transcription factor p120E4F."
      Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E., Medema R., Vignais M.-L., Sardet C.
      Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RB1.
    8. "The E4F protein is required for mitotic progression during embryonic cell cycles."
      Le Cam L., Lacroix M., Ciemerych M.A., Sardet C., Sicinski P.
      Mol. Cell. Biol. 24:6467-6475(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION.
    9. "The role of LANP and ataxin 1 in E4F-mediated transcriptional repression."
      Cvetanovic M., Rooney R.J., Garcia J.J., Toporovskaya N., Zoghbi H.Y., Opal P.
      EMBO Rep. 8:671-677(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ANP32A.

    Entry informationi

    Entry nameiE4F1_MOUSE
    AccessioniPrimary (citable) accession number: Q8CCE9
    Secondary accession number(s): Q05BH7
    , Q3UNJ9, Q62065, Q6IR08, Q6PGI1, Q9QY56
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 110 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
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3