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Q16254

- E2F4_HUMAN

UniProt

Q16254 - E2F4_HUMAN

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Protein

Transcription factor E2F4

Gene

E2F4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. Specifically required for multiciliate cell differentiation: together with MCIDAS and E2F5, binds and activate genes required for centriole biogenesis.By similarity2 Publications

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  1. blood circulation Source: Ensembl
  2. cell volume homeostasis Source: Ensembl
  3. cilium assembly Source: Ensembl
  4. epithelial cell development Source: Ensembl
  5. gene expression Source: Reactome
  6. mitotic cell cycle Source: Reactome
  7. organ morphogenesis Source: Ensembl
  8. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
  9. regulation of cell proliferation Source: Ensembl
  10. regulation of cell size Source: Ensembl
  11. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Ensembl
  12. transcription, DNA-templated Source: Reactome
  13. transcription initiation from RNA polymerase II promoter Source: Reactome
  14. transforming growth factor beta receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell cycle, Cilium biogenesis/degradation, 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.
SignaLinkiQ16254.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor E2F4
Short name:
E2F-4
Gene namesi
Name:E2F4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:3118. E2F4.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
  4. transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27576.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 413412Transcription factor E2F4PRO_0000219468Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Post-translational modificationi

Differentially phosphorylated in vivo.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ16254.
PaxDbiQ16254.
PRIDEiQ16254.

PTM databases

PhosphoSiteiQ16254.

Expressioni

Tissue specificityi

Found in all tissue examined including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Developmental stagei

Present in the growth-arrested state, its abundance does not change significantly as cells move into and through the cell cycle.

Gene expression databases

BgeeiQ16254.
CleanExiHS_E2F4.
ExpressionAtlasiQ16254. baseline and differential.
GenevestigatoriQ16254.

Organism-specific databases

HPAiCAB016523.
HPA054128.

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. Interacts with PML (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5).9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LIN9Q5TKA13EBI-448943,EBI-1389424

Protein-protein interaction databases

BioGridi108206. 61 interactions.
DIPiDIP-24185N.
IntActiQ16254. 20 interactions.
MINTiMINT-88123.
STRINGi9606.ENSP00000368686.

Structurei

Secondary structure

1
413
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni17 – 204Combined sources
Helixi22 – 3514Combined sources
Beta strandi40 – 423Combined sources
Helixi43 – 497Combined sources
Turni50 – 523Combined sources
Helixi56 – 6813Combined sources
Beta strandi70 – 756Combined sources
Beta strandi78 – 814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CF7X-ray2.60A11-86[»]
ProteinModelPortaliQ16254.
SMRiQ16254. Positions 16-82.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16254.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 6523Leucine-zipperAdd
BLAST
Regioni86 – 18196DimerizationSequence AnalysisAdd
BLAST
Regioni337 – 41377TransactivationSequence AnalysisAdd
BLAST
Regioni390 – 40718Interaction with RBL1 and RBL2Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi48 – 8538DEF boxAdd
BLAST
Motifi389 – 3924HCFC1-binding-motif (HBM)

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 124Poly-Pro
Compositional biasi307 – 32721Poly-SerAdd
BLAST

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiNOG289227.
GeneTreeiENSGT00550000074403.
HOGENOMiHOG000232045.
HOVERGENiHBG002227.
InParanoidiQ16254.
KOiK04682.
OMAiPHTLAYV.
OrthoDBiEOG7WHHB1.
PhylomeDBiQ16254.
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.

Q16254-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEAGPQAPP PPGTPSRHEK SLGLLTTKFV SLLQEAKDGV LDLKLAADTL
60 70 80 90 100
AVRQKRRIYD ITNVLEGIGL IEKKSKNSIQ WKGVGPGCNT REIADKLIEL
110 120 130 140 150
KAEIEELQQR EQELDQHKVW VQQSIRNVTE DVQNSCLAYV THEDICRCFA
160 170 180 190 200
GDTLLAIRAP SGTSLEVPIP EGLNGQKKYQ IHLKSVSGPI EVLLVNKEAW
210 220 230 240 250
SSPPVAVPVP PPEDLLQSPS AVSTPPPLPK PALAQSQEAS RPNSPQLTPT
260 270 280 290 300
AVPGSAEVQG MAGPAAEITV SGGPGTDSKD SGELSSLPLG PTTLDTRPLQ
310 320 330 340 350
SSALLDSSSS SSSSSSSSSN SNSSSSSGPN PSTSFEPIKA DPTGVLELPK
360 370 380 390 400
ELSEIFDPTR ECMSSELLEE LMSSEVFAPL LRLSPPPGDH DYIYNLDESE
410
GVCDLFDVPV LNL
Length:413
Mass (Da):43,960
Last modified:November 1, 1997 - v2
Checksum:iBAAC95DE1B7E0832
GO

Polymorphismi

The poly-Ser region of E2F4 is polymorphic and the number of Ser varies in the population (from 8 to 17). The variation might be associated with tumorigenesis.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti293 – 2931T → P.
Corresponds to variant rs1801013 [ dbSNP | Ensembl ].
VAR_014936
Natural varianti319 – 3191S → SSSS.
VAR_014024

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S75174 mRNA. Translation: AAB32597.1.
X86096 mRNA. Translation: CAA60050.2.
U15641 mRNA. Translation: AAC50119.1.
AF250378 Genomic DNA. Translation: AAF65226.1.
AB451292 mRNA. Translation: BAG70106.1.
AB451425 mRNA. Translation: BAG70239.1.
AF527540 Genomic DNA. Translation: AAM77918.1.
AC040160 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83094.1.
BC033180 mRNA. Translation: AAH33180.1.
CCDSiCCDS32464.1.
PIRiA55237.
RefSeqiNP_001941.2. NM_001950.3.
UniGeneiHs.108371.

Genome annotation databases

EnsembliENST00000379378; ENSP00000368686; ENSG00000205250.
GeneIDi1874.
KEGGihsa:1874.
UCSCiuc002erz.3. human.

Polymorphism databases

DMDMi2494229.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S75174 mRNA. Translation: AAB32597.1 .
X86096 mRNA. Translation: CAA60050.2 .
U15641 mRNA. Translation: AAC50119.1 .
AF250378 Genomic DNA. Translation: AAF65226.1 .
AB451292 mRNA. Translation: BAG70106.1 .
AB451425 mRNA. Translation: BAG70239.1 .
AF527540 Genomic DNA. Translation: AAM77918.1 .
AC040160 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83094.1 .
BC033180 mRNA. Translation: AAH33180.1 .
CCDSi CCDS32464.1.
PIRi A55237.
RefSeqi NP_001941.2. NM_001950.3.
UniGenei Hs.108371.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CF7 X-ray 2.60 A 11-86 [» ]
ProteinModelPortali Q16254.
SMRi Q16254. Positions 16-82.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108206. 61 interactions.
DIPi DIP-24185N.
IntActi Q16254. 20 interactions.
MINTi MINT-88123.
STRINGi 9606.ENSP00000368686.

PTM databases

PhosphoSitei Q16254.

Polymorphism databases

DMDMi 2494229.

Proteomic databases

MaxQBi Q16254.
PaxDbi Q16254.
PRIDEi Q16254.

Protocols and materials databases

DNASUi 1874.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379378 ; ENSP00000368686 ; ENSG00000205250 .
GeneIDi 1874.
KEGGi hsa:1874.
UCSCi uc002erz.3. human.

Organism-specific databases

CTDi 1874.
GeneCardsi GC16P067226.
HGNCi HGNC:3118. E2F4.
HPAi CAB016523.
HPA054128.
MIMi 600659. gene.
neXtProti NX_Q16254.
PharmGKBi PA27576.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG289227.
GeneTreei ENSGT00550000074403.
HOGENOMi HOG000232045.
HOVERGENi HBG002227.
InParanoidi Q16254.
KOi K04682.
OMAi PHTLAYV.
OrthoDBi EOG7WHHB1.
PhylomeDBi Q16254.
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 Q16254.

Miscellaneous databases

ChiTaRSi E2F4. human.
EvolutionaryTracei Q16254.
GeneWikii E2F4.
GenomeRNAii 1874.
NextBioi 7659.
PROi Q16254.
SOURCEi Search...

Gene expression databases

Bgeei Q16254.
CleanExi HS_E2F4.
ExpressionAtlasi Q16254. baseline and differential.
Genevestigatori Q16254.

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

« Hide 'large scale' publications
  1. "E2F-4, a new member of the E2F transcription factor family, interacts with p107."
    Ginsberg D., Vairo G., Chittenden T., Xiao Z.-X., Xu G., Wydner K.L., Decaprio J.A., Lawrence J.B., Livingston D.M.
    Genes Dev. 8:2665-2679(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-319 INS, INTERACTION WITH RBL1, FUNCTION.
    Tissue: Cervix carcinoma.
  2. "E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo."
    Beijersbergen R.L., Kerkhoven R.M., Zhu L., Carlee L., Voorhoeve P.M., Bernards R.
    Genes Dev. 8:2680-2690(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RBL1, FUNCTION.
    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].
  4. "Genomic structure and mutation screening of the E2F4 gene in human tumors."
    Schwemmle S., Pfeifer G.P.
    Int. J. Cancer 86:672-677(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. NIEHS SNPs program
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "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].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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].
    Tissue: Kidney.
  10. "The predominant E2F complex in human primary haemopoietic cells and in AML blasts contains E2F-4, DP-1 and p130."
    Williams C.D., Linch D.C., Soerensen T.S., La Thangue N.B., Thomas N.S.B.
    Br. J. Haematol. 96:688-696(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBL2.
  11. "E2F transcriptional activation requires TRRAP and GCN5 cofactors."
    Lang S.E., McMahon S.B., Cole M.D., Hearing P.
    J. Biol. Chem. 276:32627-32634(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRRAP.
  12. "HCF-1 functions as a coactivator for the zinc finger protein Krox20."
    Luciano R.L., Wilson A.C.
    J. Biol. Chem. 278:51116-51124(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCFC1.
  13. "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; RBL1; TFDP1 AND TFDP2.
  14. "LINC, a human complex that is related to pRB-containing complexes in invertebrates regulates the expression of G2/M genes."
    Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S.
    Cell Cycle 6:1903-1913(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
  15. "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.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. "Physical and functional interaction between PML and TBX2 in the establishment of cellular senescence."
    Martin N., Benhamed M., Nacerddine K., Demarque M.D., van Lohuizen M., Dejean A., Bischof O.
    EMBO J. 31:95-109(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PML.
  18. "Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP."
    Zheng N., Fraenkel E., Pabo C.O., Pavletich N.P.
    Genes Dev. 13:666-674(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 11-86.
  19. "Various AGC repeat numbers in the coding region of the human transcription factor gene E2F-4."
    Zhong X., Hemmi H., Koike J., Tsujita K., Shimatake H.
    Hum. Mutat. 15:296-297(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYMORPHISM.

Entry informationi

Entry nameiE2F4_HUMAN
AccessioniPrimary (citable) accession number: Q16254
Secondary accession number(s): A6NGR8
, B5BU56, Q12991, Q15328
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 151 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3