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Q8R0K9 (E2F4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor E2F4

Short name=E2F-4
Gene names
Name:E2f4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity.

Subunit structure

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.

Subcellular location

Nucleus By similarity.

Post-translational modification

Differentially phosphorylated in vivo By similarity.

Sequence similarities

Belongs to the E2F/DP family.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood circulation

Inferred from mutant phenotype PubMed 10983977. Source: MGI

cell volume homeostasis

Inferred from mutant phenotype PubMed 10983976. Source: MGI

cilium assembly

Inferred from mutant phenotype PubMed 17383628. Source: MGI

epithelial cell development

Inferred from mutant phenotype PubMed 17383628. Source: MGI

organ morphogenesis

Inferred from mutant phenotype PubMed 10983976PubMed 10983977. Source: MGI

regulation of cell cycle

Traceable author statement PubMed 10983977. Source: MGI

regulation of cell proliferation

Inferred from direct assay PubMed 10779331. Source: MGI

regulation of cell size

Inferred from mutant phenotype PubMed 10983976. Source: MGI

regulation of transcription involved in G1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 11004506. Source: MGI

regulation of transcription, DNA-templated

Traceable author statement PubMed 10983976PubMed 10983977. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Traceable author statement PubMed 10983976. Source: MGI

nucleus

Inferred from direct assay PubMed 10779331PubMed 15574595PubMed 17383628. Source: MGI

transcription factor complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionDNA binding

Inferred from direct assay PubMed 10779331PubMed 11004506PubMed 15574595. Source: MGI

protein binding

Inferred from physical interaction PubMed 15448153. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15574595. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 410409Transcription factor E2F4
PRO_0000322638

Regions

DNA binding16 – 8570 Potential
Region43 – 6523Leucine-zipper
Region86 – 18196Dimerization Potential
Region334 – 41077Transactivation Potential
Region387 – 40418Interaction with RBL1 and RBL2 Potential
Motif48 – 8538DEF box By similarity
Motif386 – 3894HCFC1-binding-motif (HBM) By similarity
Compositional bias9 – 124Poly-Pro
Compositional bias308 – 32417Poly-Ser

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict3261P → T in AAH27048. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8R0K9 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: A8BD1A24B38C2B01

FASTA41043,833
        10         20         30         40         50         60 
MAEAGPQAPP PPGTPSRHEK SLGLLTTKFV SLLQEAKDGV LDLKLAADTL AVRQKRRIYD 

        70         80         90        100        110        120 
ITNVLEGIGL IEKKSKNSIQ WKGVGPGCNT REIADKLIEL KAEIEELQQR EQELDQHKVW 

       130        140        150        160        170        180 
VQQSIRNVTE DVQNSCLAYV THEDICRCFA GDTLLAIRAP SGTSLEVPIP EGLNGQKKYQ 

       190        200        210        220        230        240 
IHLKSMSGPI EVLLVNKEAW SSPPVAVPVP PPDDLLQSPP AVSTPPPLPK PALAQPQESS 

       250        260        270        280        290        300 
PPSSPQLTTP TPVLGSTQVS EVACQTSEIA VSGSPGTENK DSGEVSSLPL GLTALDTRPL 

       310        320        330        340        350        360 
QSSALLDSSS SSSSSSSSSS SSSSGPNPST SFEPIKADPT GVLDLPKELS EIFDPTRECM 

       370        380        390        400        410 
SSELLEELMS SEVFAPLLRL SPPPGDHDYI YNLDESEGVC DLFDVPVLKL 

« Hide

References

[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS40456.1.
RefSeqNP_683754.1. NM_148952.1.
UniGeneMm.34554.

3D structure databases

ProteinModelPortalQ8R0K9.
SMRQ8R0K9. Positions 16-82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid222608. 4 interactions.
IntActQ8R0K9. 10 interactions.
MINTMINT-4301946.
STRING10090.ENSMUSP00000015003.

PTM databases

PhosphoSiteQ8R0K9.

Proteomic databases

MaxQBQ8R0K9.
PaxDbQ8R0K9.
PRIDEQ8R0K9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015003; ENSMUSP00000015003; ENSMUSG00000014859.
GeneID104394.
KEGGmmu:104394.
UCSCuc009ncl.1. mouse.

Organism-specific databases

CTD1874.
MGIMGI:103012. E2f4.

Phylogenomic databases

eggNOGNOG289227.
GeneTreeENSGT00550000074403.
HOGENOMHOG000232045.
HOVERGENHBG002227.
InParanoidQ8R0K9.
KOK04682.
OMAPHTLAYV.
OrthoDBEOG7WHHB1.
PhylomeDBQ8R0K9.
TreeFamTF105566.

Gene expression databases

BgeeQ8R0K9.
CleanExMM_E2F4.
GenevestigatorQ8R0K9.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR015633. E2F.
IPR028312. E2F4.
IPR003316. E2F_TDP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR12081. PTHR12081. 1 hit.
PTHR12081:SF42. PTHR12081:SF42. 1 hit.
PfamPF02319. E2F_TDP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSE2F4. mouse.
NextBio357065.
PROQ8R0K9.
SOURCESearch...

Entry information

Entry nameE2F4_MOUSE
AccessionPrimary (citable) accession number: Q8R0K9
Secondary accession number(s): Q8R2X6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot