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Q66K89

- E4F1_HUMAN

UniProt

Q66K89 - E4F1_HUMAN

Protein

Transcription factor E4F1

Gene

E4F1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      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.
    Identified as a cellular target of the adenoviral oncoprotein E1A, it is required for both transcriptional activation and repression of viral genes.

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri192 – 21423C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri220 – 24223C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri248 – 27225C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri435 – 45723C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri463 – 48523C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri491 – 51323C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri519 – 54123C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri547 – 56923C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri575 – 59723C2H2-type 9; degeneratePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cAMP response element binding Source: UniProtKB
    2. DNA binding Source: ProtInc
    3. ligase activity Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: UniProtKB
    6. RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
    7. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
    8. sequence-specific DNA binding transcription factor activity Source: ProtInc
    9. transcription coactivator activity Source: ProtInc
    10. transcription corepressor activity Source: ProtInc

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. DNA replication Source: Ensembl
    3. embryo development Source: Ensembl
    4. mitotic cell cycle arrest Source: UniProtKB
    5. mitotic nuclear division Source: UniProtKB-KW
    6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. protein ubiquitination Source: UniProtKB-UniPathway
    8. regulation of cell cycle process Source: UniProtKB
    9. regulation of growth Source: UniProtKB-KW
    10. regulation of mitotic cell cycle, embryonic Source: Ensembl
    11. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase, Repressor

    Keywords - Biological processi

    Cell cycle, Cell division, Growth regulation, Host-virus interaction, Mitosis, Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ66K89.
    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
    p120E4F
    p50E4F
    Gene namesi
    Name:E4F1
    Synonyms:E4F
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:3121. E4F1.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi194 – 1941C → S: Increases DNA-binding; when associated with S-197. 1 Publication
    Mutagenesisi197 – 1971C → S: Increases DNA-binding; when associated with S-194. 1 Publication
    Mutagenesisi210 – 2101H → A: Alters DNA-binding. 1 Publication
    Mutagenesisi237 – 2371R → L: Alters DNA-binding; when associated with N-238. 1 Publication
    Mutagenesisi238 – 2381H → N: Alters DNA-binding; when associated with L-237. 1 Publication
    Mutagenesisi249 – 2491K → M: Alters DNA-binding; when associated with S-250. 1 Publication
    Mutagenesisi250 – 2501C → S: Alters DNA-binding; when associated with M-249. 1 Publication

    Organism-specific databases

    PharmGKBiPA27579.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 784784Transcription factor E4F1PRO_0000324307Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 501Phosphoserine2 Publications

    Post-translational modificationi

    Proteolytic cleavage produces a 50 kDa N-terminal peptide (p50E4F) which has a DNA-binding activity and activates transcription in presence of the adenoviral E1A protein. The major full length protein (p120E4F) functions as a repressor of transcription.1 Publication
    Phosphorylated; p120E4F and p50E4F are both phosphorylated. Phosphorylation is cell cycle-dependent and differentially regulates DNA-binding activity and function of both forms.4 Publications
    May be sumoylated by UBE2I upon interaction with CDKN2A.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ66K89.
    PaxDbiQ66K89.
    PRIDEiQ66K89.

    PTM databases

    PhosphoSiteiQ66K89.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Developmental stagei

    Expressed in a variety of fetal tissues.1 Publication

    Inductioni

    Up-regulated by estrogen.1 Publication

    Gene expression databases

    ArrayExpressiQ66K89.
    BgeeiQ66K89.
    CleanExiHS_E4F1.
    GenevestigatoriQ66K89.

    Organism-specific databases

    HPAiHPA052042.

    Interactioni

    Subunit structurei

    Homodimer; binds DNA as a dimer. Forms a complex with CDKN2A and TP53. Interactions with TP53, RB1, ANP32A, BMI1 and FHL2 regulate E4F1 activity. Interacts with HDAC1, HMGA2 and RASSF1. Interacts with HBV protein X.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    8Q647704EBI-1227043,EBI-8642971From a different organism.
    ANP32AP396873EBI-1227043,EBI-359234
    HDAC1Q135473EBI-1227043,EBI-301834
    HDAC1Q6IT962EBI-1227043,EBI-6979193
    lnx2bA4VCF73EBI-1227043,EBI-6979266From a different organism.
    RASSF1Q9NS23-27EBI-1227043,EBI-438698
    tcf7l1aQ9YHE82EBI-1227043,EBI-6979298From a different organism.

    Protein-protein interaction databases

    BioGridi108209. 12 interactions.
    IntActiQ66K89. 11 interactions.
    MINTiMINT-137139.
    STRINGi9606.ENSP00000301727.

    Structurei

    3D structure databases

    ProteinModelPortaliQ66K89.
    SMRiQ66K89. Positions 191-296, 405-599.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni41 – 8545Required for ubiquitin ligase activityAdd
    BLAST
    Regioni184 – 26380Mediates dimerization, DNA-binding, transcription repression of CCNA2 and interaction with HMGA2Add
    BLAST
    Regioni369 – 566198Mediates interaction with CDKN2AAdd
    BLAST
    Regioni435 – 599165Interaction with BMI1Add
    BLAST
    Regioni521 – 58060Mediates interaction with TP53Add
    BLAST
    Regioni575 – 59723Mediates interaction with RASSF1Add
    BLAST

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri192 – 21423C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri220 – 24223C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri248 – 27225C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri435 – 45723C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri463 – 48523C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri491 – 51323C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri519 – 54123C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri547 – 56923C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri575 – 59723C2H2-type 9; degeneratePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    HOGENOMiHOG000168447.
    HOVERGENiHBG052707.
    InParanoidiQ66K89.
    OMAiCQFCSRG.
    OrthoDBiEOG761BT6.
    PhylomeDBiQ66K89.
    TreeFamiTF315387.

    Family and domain databases

    Gene3Di3.30.160.60. 9 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF00096. zf-C2H2. 1 hit.
    [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]

    Sequencei

    Sequence statusi: Complete.

    Q66K89-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGAMAVRVT AAHTAEAQAE AGREAGEGAV AAVAAALAPS GFLGLPAPFS    50
    EEDEDDVHRC GRCQAEFTAL EDFVQHKIQK ACQRAPPEAL PATPATTALL 100
    GQEVVPAAPG PEEPITVAHI VVEAASLAAD ISHASDLVGG GHIKEVIVAA 150
    EAELGDGEMA EAPGSPRQQG LGLAGEGEQA QVKLLVNKDG RYVCALCHKT 200
    FKTGSILKAH MVTHSSRKDH ECKLCGASFR TKGSLIRHHR RHTDERPYKC 250
    SKCGKSFRES GALTRHLKSL TPCTEKIRFS VSKDVVVSKE DARAGSGAGA 300
    AGLGTATSSV TGEPIETSPV IHLVTDAKGT VIHEVHVQMQ ELSLGMKALA 350
    PEPPVSQELP CSSEGSRENL LHQAMQNSGI VLERAAGEEG ALEPAPAAGS 400
    SPQPLAVAAP QLPVLEVQPL ETQVASEASA VPRTHPCPQC SETFPTAATL 450
    EAHKRGHTGP RPFACAQCGK AFPKAYLLKK HQEVHVRERR FRCGDCGKLY 500
    KTIAHVRGHR RVHSDERPYP CPKCGKRYKT KNAQQVHFRT HLEEKPHVCQ 550
    FCSRGFREKG SLVRHVRHHT GEKPFKCYKC GRGFAEHGTL NRHLRTKGGC 600
    LLEVEELLVS EDSPAAATTV LTEDPHTVLV EFSSVVADTQ EYIIEATADD 650
    AETSEATEII EGTQTEVDSH IMKVVQQIVH QASAGHQIIV QNVTMDEETA 700
    LGPEAAAADT ITIATPESLT EQVAMTLASA ISEGTVLAAR AGTSGTEQAT 750
    VTMVSSEDIE ILEHAGELVI ASPEGQLEVQ TVIV 784
    Length:784
    Mass (Da):83,496
    Last modified:May 18, 2010 - v2
    Checksum:i60F6E711F2748FD8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41A → E in AAD09139. (PubMed:9121437)Curated
    Sequence conflicti363 – 3642SE → RK in AAD09139. (PubMed:9121437)Curated
    Sequence conflicti425 – 4251A → V in BAF83018. (PubMed:14702039)Curated
    Sequence conflicti480 – 4812KH → TD in AAD09139. (PubMed:9121437)Curated
    Sequence conflicti544 – 5441E → D in BAF83018. (PubMed:14702039)Curated
    Sequence conflicti681 – 6822QA → PR in AAD09139. (PubMed:9121437)Curated
    Sequence conflicti704 – 7052EA → RG in AAD09139. (PubMed:9121437)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671R → H.4 Publications
    Corresponds to variant rs26839 [ dbSNP | Ensembl ].
    VAR_060270
    Natural varianti355 – 3551V → I.
    Corresponds to variant rs59784157 [ dbSNP | Ensembl ].
    VAR_060271

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U87269 mRNA. Translation: AAD09139.1.
    AK290329 mRNA. Translation: BAF83018.1.
    AC009065 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85532.1.
    BC080524 mRNA. Translation: AAH80524.1.
    CCDSiCCDS32370.1.
    RefSeqiNP_001275705.1. NM_001288776.1.
    NP_001275707.1. NM_001288778.1.
    NP_004415.3. NM_004424.4.
    UniGeneiHs.513268.

    Genome annotation databases

    EnsembliENST00000301727; ENSP00000301727; ENSG00000167967.
    GeneIDi1877.
    KEGGihsa:1877.
    UCSCiuc002cpm.3. human.

    Polymorphism databases

    DMDMi296434488.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U87269 mRNA. Translation: AAD09139.1 .
    AK290329 mRNA. Translation: BAF83018.1 .
    AC009065 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85532.1 .
    BC080524 mRNA. Translation: AAH80524.1 .
    CCDSi CCDS32370.1.
    RefSeqi NP_001275705.1. NM_001288776.1.
    NP_001275707.1. NM_001288778.1.
    NP_004415.3. NM_004424.4.
    UniGenei Hs.513268.

    3D structure databases

    ProteinModelPortali Q66K89.
    SMRi Q66K89. Positions 191-296, 405-599.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108209. 12 interactions.
    IntActi Q66K89. 11 interactions.
    MINTi MINT-137139.
    STRINGi 9606.ENSP00000301727.

    PTM databases

    PhosphoSitei Q66K89.

    Polymorphism databases

    DMDMi 296434488.

    Proteomic databases

    MaxQBi Q66K89.
    PaxDbi Q66K89.
    PRIDEi Q66K89.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301727 ; ENSP00000301727 ; ENSG00000167967 .
    GeneIDi 1877.
    KEGGi hsa:1877.
    UCSCi uc002cpm.3. human.

    Organism-specific databases

    CTDi 1877.
    GeneCardsi GC16P002276.
    HGNCi HGNC:3121. E4F1.
    HPAi HPA052042.
    MIMi 603022. gene.
    neXtProti NX_Q66K89.
    PharmGKBi PA27579.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOGENOMi HOG000168447.
    HOVERGENi HBG052707.
    InParanoidi Q66K89.
    OMAi CQFCSRG.
    OrthoDBi EOG761BT6.
    PhylomeDBi Q66K89.
    TreeFami TF315387.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    SignaLinki Q66K89.

    Miscellaneous databases

    GeneWikii E4F1.
    GenomeRNAii 1877.
    NextBioi 7679.
    PROi Q66K89.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q66K89.
    Bgeei Q66K89.
    CleanExi HS_E4F1.
    Genevestigatori Q66K89.

    Family and domain databases

    Gene3Di 3.30.160.60. 9 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF00096. zf-C2H2. 1 hit.
    [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. "The adenovirus E1A-regulated transcription factor E4F is generated from the human homolog of nuclear factor phiAP3."
      Fernandes E.R., Rooney R.J.
      Mol. Cell. Biol. 17:1890-1903(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEOLYTIC PROCESSING, PHOSPHORYLATION, DNA-BINDING, VARIANT HIS-167.
      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], VARIANT HIS-167.
      Tissue: Tongue.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT HIS-167.
    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-167.
      Tissue: Uterus.
    6. "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.
    7. "Adenovirus E1A-regulated transcription factor p120E4F inhibits cell growth and induces the stabilization of the cdk inhibitor p21WAF1."
      Fernandes E.R., Zhang J.Y., Rooney R.J.
      Mol. Cell. Biol. 18:459-467(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Mutational analysis of p50E4F suggests that DNA binding activity is mediated through an alternative structure in a zinc finger domain that is regulated by phosphorylation."
      Rooney R.J., Rothammer K., Fernandes E.R.
      Nucleic Acids Res. 26:1681-1688(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: OLIGOMERIZATION, PHOSPHORYLATION, DNA-BINDING, MUTAGENESIS OF CYS-194; CYS-197; HIS-210; ARG-237; HIS-238; LYS-249 AND CYS-250.
    9. "Suppression of E1A-mediated transformation by the p50E4F transcription factor."
      Fernandes E.R., Rooney R.J.
      Mol. Cell. Biol. 19:4739-4749(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: FUNCTION, INTERACTION WITH TP53.
    11. "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: FUNCTION, REGULATION BY RB1, INTERACTION WITH RB1.
    12. "Cyclin A is a mediator of p120E4F-dependent cell cycle arrest in G1."
      Fajas L., Paul C., Vie A., Estrach S., Medema R., Blanchard J.M., Sardet C., Vignais M.-L.
      Mol. Cell. Biol. 21:2956-2966(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Association of p14ARF with the p120E4F transcriptional repressor enhances cell cycle inhibition."
      Rizos H., Diefenbach E., Badhwar P., Woodruff S., Becker T.M., Rooney R.J., Kefford R.F.
      J. Biol. Chem. 278:4981-4989(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH CDKN2A AND TP53, SUBCELLULAR LOCATION.
    14. "Transcriptional activation of the cyclin A gene by the architectural transcription factor HMGA2."
      Tessari M.A., Gostissa M., Altamura S., Sgarra R., Rustighi A., Salvagno C., Caretti G., Imbriano C., Mantovani R., Del Sal G., Giancotti V., Manfioletti G.
      Mol. Cell. Biol. 23:9104-9116(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HMGA2.
    15. "Modulation of p120E4F transcriptional activity by the Gam1 adenoviral early protein."
      Colombo R., Draetta G.F., Chiocca S.
      Oncogene 22:2541-2547(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC1.
    16. Cited for: INDUCTION BY ESTROGEN.
    17. "Identification of the E1A-regulated transcription factor p120 E4F as an interacting partner of the RASSF1A candidate tumor suppressor gene."
      Fenton S.L., Dallol A., Agathanggelou A., Hesson L., Ahmed-Choudhury J., Baksh S., Sardet C., Dammann R., Minna J.D., Downward J., Maher E.R., Latif F.
      Cancer Res. 64:102-107(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RASSF1.
    18. "Transcriptional regulation of cyclin A2 by RASSF1A through the enhanced binding of p120E4F to the cyclin A2 promoter."
      Ahmed-Choudhury J., Agathanggelou A., Fenton S.L., Ricketts C., Clark G.J., Maher E.R., Latif F.
      Cancer Res. 65:2690-2697(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "p14ARF interacts with the SUMO-conjugating enzyme Ubc9 and promotes the sumoylation of its binding partners."
      Rizos H., Woodruff S., Kefford R.F.
      Cell Cycle 4:597-603(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION.
    20. "E4F1 is an atypical ubiquitin ligase that modulates p53 effector functions independently of degradation."
      Le Cam L., Linares L.K., Paul C., Julien E., Lacroix M., Hatchi E., Triboulet R., Bossis G., Shmueli A., Rodriguez M.S., Coux O., Sardet C.
      Cell 127:775-788(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TP53.
    21. "E4F1: a novel candidate factor for mediating BMI1 function in primitive hematopoietic cells."
      Chagraoui J., Niessen S.L., Lessard J., Girard S., Coulombe P., Sauvageau M., Meloche S., Sauvageau G.
      Genes Dev. 20:2110-2120(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BMI1, SUBCELLULAR LOCATION.
    22. Cited for: FUNCTION, INTERACTION WITH FHL2.
    23. "Interaction of the hepatitis B virus protein HBx with the human transcription regulatory protein p120E4F in vitro."
      Rui E., Moura P.R., Goncalves K.A., Rooney R.J., Kobarg J.
      Virus Res. 115:31-42(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HBV PROTEIN X.
    24. "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: INTERACTION WITH ANP32A.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    27. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiE4F1_HUMAN
    AccessioniPrimary (citable) accession number: Q66K89
    Secondary accession number(s): A8K2R4, O00146
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 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 16
      Human chromosome 16: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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