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Q8R0K9

- E2F4_MOUSE

UniProt

Q8R0K9 - E2F4_MOUSE

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Protein

Transcription factor E2F4

Gene

E2f4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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 similarity1 Publication

Regions

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

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. sequence-specific DNA binding transcription factor activity Source: MGI

GO - Biological processi

  1. blood circulation Source: MGI
  2. cell volume homeostasis Source: MGI
  3. cilium assembly Source: MGI
  4. epithelial cell development Source: MGI
  5. organ morphogenesis Source: MGI
  6. regulation of cell cycle Source: MGI
  7. regulation of cell proliferation Source: MGI
  8. regulation of cell size Source: MGI
  9. regulation of transcription, DNA-templated Source: MGI
  10. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: MGI
  11. transcription, DNA-templated Source: UniProtKB-KW
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_199110. G0 and Early G1.
REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor E2F4
Short name:
E2F-4
Gene namesi
Name:E2f4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:103012. E2f4.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleus Source: MGI
  3. transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Postnatal lethality, probably due to the absence of ciliated cells from the entire airway epithelium and the epithelium of the submucosal glands in the paranasal sinuses. In the nasal epithelium, ciliated cells are replaced by columnar secretory cells that produce mucin-like substances. In the proximal lung, reduction in Clara cell is also obrserved. The combination of no ciliated cells and excess mucous cells leads for the chronic rhinitis and increased susceptibility to opportunistic infections that cause lethality.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 410409Transcription factor E2F4PRO_0000322638Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Post-translational modificationi

Differentially phosphorylated in vivo.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8R0K9.
PaxDbiQ8R0K9.
PRIDEiQ8R0K9.

PTM databases

PhosphoSiteiQ8R0K9.

Expressioni

Gene expression databases

BgeeiQ8R0K9.
CleanExiMM_E2F4.
GenevestigatoriQ8R0K9.

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 (By similarity). Interacts with PML (By similarity).By similarity

Protein-protein interaction databases

BioGridi222608. 4 interactions.
IntActiQ8R0K9. 10 interactions.
MINTiMINT-4301946.
STRINGi10090.ENSMUSP00000015003.

Structurei

3D structure databases

ProteinModelPortaliQ8R0K9.
SMRiQ8R0K9. Positions 16-82.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 6523Leucine-zipperAdd
BLAST
Regioni86 – 18196DimerizationSequence AnalysisAdd
BLAST
Regioni334 – 41077TransactivationSequence AnalysisAdd
BLAST
Regioni387 – 40418Interaction with RBL1 and RBL2Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi48 – 8538DEF boxBy similarityAdd
BLAST
Motifi386 – 3894HCFC1-binding-motif (HBM)By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 124Poly-Pro
Compositional biasi308 – 32417Poly-SerAdd
BLAST

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiNOG289227.
GeneTreeiENSGT00550000074403.
HOGENOMiHOG000232045.
HOVERGENiHBG002227.
InParanoidiQ8R0K9.
KOiK04682.
OMAiPHTLAYV.
OrthoDBiEOG7WHHB1.
PhylomeDBiQ8R0K9.
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.

Q8R0K9 [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 IHLKSMSGPI EVLLVNKEAW
210 220 230 240 250
SSPPVAVPVP PPDDLLQSPP AVSTPPPLPK PALAQPQESS PPSSPQLTTP
260 270 280 290 300
TPVLGSTQVS EVACQTSEIA VSGSPGTENK DSGEVSSLPL GLTALDTRPL
310 320 330 340 350
QSSALLDSSS SSSSSSSSSS SSSSGPNPST SFEPIKADPT GVLDLPKELS
360 370 380 390 400
EIFDPTRECM SSELLEELMS SEVFAPLLRL SPPPGDHDYI YNLDESEGVC
410
DLFDVPVLKL
Length:410
Mass (Da):43,833
Last modified:June 1, 2002 - v1
Checksum:iA8BD1A24B38C2B01
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti326 – 3261P → T in AAH27048. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK145950 mRNA. Translation: BAE26778.1.
AK157028 mRNA. Translation: BAE33937.1.
BC023859 mRNA. Translation: AAH23859.1.
BC026649 mRNA. Translation: AAH26649.1.
BC027048 mRNA. Translation: AAH27048.1.
CCDSiCCDS40456.1.
RefSeqiNP_683754.1. NM_148952.1.
UniGeneiMm.34554.

Genome annotation databases

EnsembliENSMUST00000015003; ENSMUSP00000015003; ENSMUSG00000014859.
GeneIDi104394.
KEGGimmu:104394.
UCSCiuc009ncl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK145950 mRNA. Translation: BAE26778.1 .
AK157028 mRNA. Translation: BAE33937.1 .
BC023859 mRNA. Translation: AAH23859.1 .
BC026649 mRNA. Translation: AAH26649.1 .
BC027048 mRNA. Translation: AAH27048.1 .
CCDSi CCDS40456.1.
RefSeqi NP_683754.1. NM_148952.1.
UniGenei Mm.34554.

3D structure databases

ProteinModelPortali Q8R0K9.
SMRi Q8R0K9. Positions 16-82.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 222608. 4 interactions.
IntActi Q8R0K9. 10 interactions.
MINTi MINT-4301946.
STRINGi 10090.ENSMUSP00000015003.

PTM databases

PhosphoSitei Q8R0K9.

Proteomic databases

MaxQBi Q8R0K9.
PaxDbi Q8R0K9.
PRIDEi Q8R0K9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000015003 ; ENSMUSP00000015003 ; ENSMUSG00000014859 .
GeneIDi 104394.
KEGGi mmu:104394.
UCSCi uc009ncl.1. mouse.

Organism-specific databases

CTDi 1874.
MGIi MGI:103012. E2f4.

Phylogenomic databases

eggNOGi NOG289227.
GeneTreei ENSGT00550000074403.
HOGENOMi HOG000232045.
HOVERGENi HBG002227.
InParanoidi Q8R0K9.
KOi K04682.
OMAi PHTLAYV.
OrthoDBi EOG7WHHB1.
PhylomeDBi Q8R0K9.
TreeFami TF105566.

Enzyme and pathway databases

Reactomei REACT_199110. G0 and Early G1.
REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.

Miscellaneous databases

ChiTaRSi E2F4. mouse.
NextBioi 357065.
PROi Q8R0K9.
SOURCEi Search...

Gene expression databases

Bgeei Q8R0K9.
CleanExi MM_E2F4.
Genevestigatori Q8R0K9.

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. "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].
    Strain: C57BL/6J and NOD.
    Tissue: Liver and Spleen.
  2. "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].
    Strain: Czech II and FVB/N.
    Tissue: Colon and Mammary tumor.
  3. "E2f4 is required for normal development of the airway epithelium."
    Danielian P.S., Bender Kim C.F., Caron A.M., Vasile E., Bronson R.T., Lees J.A.
    Dev. Biol. 305:564-576(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.

Entry informationi

Entry nameiE2F4_MOUSE
AccessioniPrimary (citable) accession number: Q8R0K9
Secondary accession number(s): Q8R2X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 1, 2002
Last modified: October 29, 2014
This is version 115 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3