Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q15329 (E2F5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor E2F5

Short name=E2F-5
Gene names
Name:E2F5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional activator that binds to E2F sites, these sites are present in the promoter of many genes whose products are involved in cell proliferation. May mediate growth factor-initiated signal transduction. It is likely involved in the early responses of resting cells to growth factor stimulation.

Subunit structure

Component of the DRTF1/E2F transcription factor complex. Binds cooperatively with DP-1 to E2F sites. Interaction with retinoblastoma protein RB1 or proteins RBL1 and RBL2 inhibits the E2F transactivation domain. 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. Ref.9

Subcellular location

Nucleus.

Sequence similarities

Belongs to the E2F/DP family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
   Molecular functionActivator
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgene expression

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

regulation of cell cycle

Inferred from electronic annotation. Source: InterPro

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

transcription factor complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Non-traceable author statement Ref.3. Source: ProtInc

transcription factor binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15329-1)

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.
Isoform 2 (identifier: Q15329-2)

The sequence of this isoform differs from the canonical sequence as follows:
     295-295: Missing.
Isoform 3 (identifier: Q15329-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Transcription factor E2F5
PRO_0000219469

Regions

DNA binding47 – 11872 Potential
Region76 – 9823Leucine-zipper
Region119 – 21597Dimerization Potential
Region287 – 34660Transactivation Potential
Region323 – 34018RBL2 association Potential
Motif81 – 11838DEF box
Compositional bias33 – 397Poly-Pro
Compositional bias233 – 2364Poly-Ser

Natural variations

Alternative sequence1 – 161161Missing in isoform 3.
VSP_044660
Alternative sequence2951Missing in isoform 2.
VSP_040098
Natural variant181G → A. Ref.5
Corresponds to variant rs4150841 [ dbSNP | Ensembl ].
VAR_014348

Experimental info

Sequence conflict1531W → L in CAB01634. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F1408A755E67D879

FASTA34637,610
        10         20         30         40         50         60 
MAAAEPASSG QQAPAGQGQG QRPPPQPPQA QAPQPPPPPQ LGGAGGGSSR HEKSLGLLTT 

        70         80         90        100        110        120 
KFVSLLQEAK DGVLDLKAAA DTLAVRQKRR IYDITNVLEG IDLIEKKSKN SIQWKGVGAG 

       130        140        150        160        170        180 
CNTKEVIDRL RYLKAEIEDL ELKERELDQQ KLWLQQSIKN VMDDSINNRF SYVTHEDICN 

       190        200        210        220        230        240 
CFNGDTLLAI QAPSGTQLEV PIPEMGQNGQ KKYQINLKSH SGPIHVLLIN KESSSSKPVV 

       250        260        270        280        290        300 
FPVPPPDDLT QPSSQSLTPV TPQKSSMATQ NLPEQHVSER SQALQQTSAT DISSAGSISG 

       310        320        330        340 
DIIDELMSSD VFPLLRLSPT PADDYNFNLD DNEGVCDLFD VQILNY 

« Hide

Isoform 2 [UniParc].

Checksum: 0CBCD335800F4863
Show »

FASTA34537,539
Isoform 3 [UniParc].

Checksum: AECF4C7A7000F8BD
Show »

FASTA18520,192

References

« Hide 'large scale' references
[1]"Structural characterization and specificity of expression of E2F-5: a new member of the E2F family of transcription factors."
Itoh A., Levinson S.F., Morita T., Kourembanas S., Brody J.S., Mitsialis S.A.
Cell. Mol. Biol. Res. 41:147-154(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Fetal lung and Placenta.
[2]"E2F-5, a new E2F family member that interacts with p130 in vivo."
Hijmans E.M., Voorhoeve P.M., Beijersbergen R.L., van 't Veer L.J., Bernards R.
Mol. Cell. Biol. 15:3082-3089(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RBL2.
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] (ISOFORM 2).
[4]"The molecular and functional characterization of E2F-5 transcription factor."
Vaishnav Y.N., Vaishnav M.Y., Pant V.
Biochem. Biophys. Res. Commun. 242:586-592(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]NIEHS SNPs program
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-18.
[6]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: B-cell.
[7]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 AND TFDP1.
[9]"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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31556 mRNA. Translation: AAB00179.1.
X86097 mRNA. Translation: CAA60051.1.
U15642 mRNA. Translation: AAC50120.1.
Z78409 mRNA. Translation: CAB01634.1.
AY162833 Genomic DNA. Translation: AAN46737.1.
AL583354 mRNA. No translation available.
AC011773 Genomic DNA. No translation available.
CCDSCCDS47885.1. [Q15329-1]
CCDS47886.1. [Q15329-2]
CCDS55254.1. [Q15329-3]
PIRJC5833.
RefSeqNP_001077057.1. NM_001083588.1. [Q15329-2]
NP_001077058.1. NM_001083589.1. [Q15329-3]
NP_001942.2. NM_001951.3. [Q15329-1]
XP_006716497.1. XM_006716434.1. [Q15329-3]
UniGeneHs.445758.

3D structure databases

ProteinModelPortalQ15329.
SMRQ15329. Positions 49-115.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108207. 6 interactions.
DIPDIP-24229N.
IntActQ15329. 4 interactions.
STRING9606.ENSP00000398124.

PTM databases

PhosphoSiteQ15329.

Polymorphism databases

DMDM2494230.

Proteomic databases

MaxQBQ15329.
PaxDbQ15329.
PRIDEQ15329.

Protocols and materials databases

DNASU1875.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000416274; ENSP00000398124; ENSG00000133740. [Q15329-1]
ENST00000418930; ENSP00000414312; ENSG00000133740. [Q15329-2]
ENST00000517476; ENSP00000429120; ENSG00000133740. [Q15329-3]
GeneID1875.
KEGGhsa:1875.
UCSCuc003ycz.4. human. [Q15329-1]
uc003yda.4. human. [Q15329-2]

Organism-specific databases

CTD1875.
GeneCardsGC08P086089.
HGNCHGNC:3119. E2F5.
MIM600967. gene.
neXtProtNX_Q15329.
PharmGKBPA27577.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289227.
HOGENOMHOG000232045.
HOVERGENHBG002227.
InParanoidQ15329.
KOK04682.
OrthoDBEOG7WHHB1.
PhylomeDBQ15329.
TreeFamTF105566.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_71. Gene Expression.
SignaLinkQ15329.

Gene expression databases

ArrayExpressQ15329.
BgeeQ15329.
CleanExHS_E2F5.
GenevestigatorQ15329.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR015633. E2F.
IPR028316. E2F5.
IPR003316. E2F_TDP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR12081. PTHR12081. 1 hit.
PTHR12081:SF35. PTHR12081:SF35. 1 hit.
PfamPF02319. E2F_TDP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSE2F5. human.
GeneWikiE2F5.
GenomeRNAi1875.
NextBio7663.
PROQ15329.
SOURCESearch...

Entry information

Entry nameE2F5_HUMAN
AccessionPrimary (citable) accession number: Q15329
Secondary accession number(s): E9PBN9, Q16601, Q92756
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM