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Protein

Transcription factor E2F5

Gene

E2F5

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

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi47 – 11872Sequence AnalysisAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • sequence-specific DNA binding transcription factor activity Source: ProtInc
  • transcription factor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

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.
SignaLinkiQ15329.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor E2F5
Short name:
E2F-5
Gene namesi
Name:E2F5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:3119. E2F5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27577.

Polymorphism and mutation databases

BioMutaiE2F5.
DMDMi2494230.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 346346Transcription factor E2F5PRO_0000219469Add
BLAST

Proteomic databases

MaxQBiQ15329.
PaxDbiQ15329.
PRIDEiQ15329.

PTM databases

PhosphoSiteiQ15329.

Expressioni

Gene expression databases

BgeeiQ15329.
CleanExiHS_E2F5.
ExpressionAtlasiQ15329. baseline and differential.
GenevisibleiQ15329. HS.

Interactioni

Subunit structurei

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 MYBL2.3 Publications

Protein-protein interaction databases

BioGridi108207. 7 interactions.
DIPiDIP-24229N.
IntActiQ15329. 4 interactions.
STRINGi9606.ENSP00000398124.

Structurei

3D structure databases

ProteinModelPortaliQ15329.
SMRiQ15329. Positions 49-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 9823Leucine-zipperAdd
BLAST
Regioni119 – 21597DimerizationSequence AnalysisAdd
BLAST
Regioni287 – 34660TransactivationSequence AnalysisAdd
BLAST
Regioni323 – 34018RBL2 associationSequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi81 – 11838DEF boxAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi33 – 397Poly-Pro
Compositional biasi233 – 2364Poly-Ser

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiNOG289227.
GeneTreeiENSGT00550000074403.
HOGENOMiHOG000232045.
HOVERGENiHBG002227.
InParanoidiQ15329.
KOiK04682.
OrthoDBiEOG7WHHB1.
PhylomeDBiQ15329.
TreeFamiTF105566.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR015633. E2F.
IPR028316. E2F5.
IPR003316. E2F_WHTH_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 1 hit.
PTHR12081:SF35. PTHR12081:SF35. 1 hit.
PfamiPF02319. E2F_TDP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15329-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAAEPASSG QQAPAGQGQG QRPPPQPPQA QAPQPPPPPQ LGGAGGGSSR
60 70 80 90 100
HEKSLGLLTT KFVSLLQEAK DGVLDLKAAA DTLAVRQKRR IYDITNVLEG
110 120 130 140 150
IDLIEKKSKN SIQWKGVGAG CNTKEVIDRL RYLKAEIEDL ELKERELDQQ
160 170 180 190 200
KLWLQQSIKN VMDDSINNRF SYVTHEDICN CFNGDTLLAI QAPSGTQLEV
210 220 230 240 250
PIPEMGQNGQ KKYQINLKSH SGPIHVLLIN KESSSSKPVV FPVPPPDDLT
260 270 280 290 300
QPSSQSLTPV TPQKSSMATQ NLPEQHVSER SQALQQTSAT DISSAGSISG
310 320 330 340
DIIDELMSSD VFPLLRLSPT PADDYNFNLD DNEGVCDLFD VQILNY
Length:346
Mass (Da):37,610
Last modified:November 1, 1996 - v1
Checksum:iF1408A755E67D879
GO
Isoform 2 (identifier: Q15329-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     295-295: Missing.

Show »
Length:345
Mass (Da):37,539
Checksum:i0CBCD335800F4863
GO
Isoform 3 (identifier: Q15329-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: Missing.

Note: No experimental confirmation available.
Show »
Length:185
Mass (Da):20,192
Checksum:iAECF4C7A7000F8BD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531W → L in CAB01634 (PubMed:9464260).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181G → A.1 Publication
Corresponds to variant rs4150841 [ dbSNP | Ensembl ].
VAR_014348

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 161161Missing in isoform 3. 1 PublicationVSP_044660Add
BLAST
Alternative sequencei295 – 2951Missing in isoform 2. 2 PublicationsVSP_040098

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47885.1. [Q15329-1]
CCDS47886.1. [Q15329-2]
CCDS55254.1. [Q15329-3]
PIRiJC5833.
RefSeqiNP_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_006716434.2. [Q15329-3]
UniGeneiHs.445758.

Genome annotation databases

EnsembliENST00000416274; ENSP00000398124; ENSG00000133740. [Q15329-1]
ENST00000418930; ENSP00000414312; ENSG00000133740. [Q15329-2]
ENST00000517476; ENSP00000429120; ENSG00000133740. [Q15329-3]
GeneIDi1875.
KEGGihsa:1875.
UCSCiuc003ycz.4. human. [Q15329-1]
uc003yda.4. human. [Q15329-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47885.1. [Q15329-1]
CCDS47886.1. [Q15329-2]
CCDS55254.1. [Q15329-3]
PIRiJC5833.
RefSeqiNP_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_006716434.2. [Q15329-3]
UniGeneiHs.445758.

3D structure databases

ProteinModelPortaliQ15329.
SMRiQ15329. Positions 49-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108207. 7 interactions.
DIPiDIP-24229N.
IntActiQ15329. 4 interactions.
STRINGi9606.ENSP00000398124.

PTM databases

PhosphoSiteiQ15329.

Polymorphism and mutation databases

BioMutaiE2F5.
DMDMi2494230.

Proteomic databases

MaxQBiQ15329.
PaxDbiQ15329.
PRIDEiQ15329.

Protocols and materials databases

DNASUi1875.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000416274; ENSP00000398124; ENSG00000133740. [Q15329-1]
ENST00000418930; ENSP00000414312; ENSG00000133740. [Q15329-2]
ENST00000517476; ENSP00000429120; ENSG00000133740. [Q15329-3]
GeneIDi1875.
KEGGihsa:1875.
UCSCiuc003ycz.4. human. [Q15329-1]
uc003yda.4. human. [Q15329-2]

Organism-specific databases

CTDi1875.
GeneCardsiGC08P086089.
HGNCiHGNC:3119. E2F5.
MIMi600967. gene.
neXtProtiNX_Q15329.
PharmGKBiPA27577.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG289227.
GeneTreeiENSGT00550000074403.
HOGENOMiHOG000232045.
HOVERGENiHBG002227.
InParanoidiQ15329.
KOiK04682.
OrthoDBiEOG7WHHB1.
PhylomeDBiQ15329.
TreeFamiTF105566.

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.
SignaLinkiQ15329.

Miscellaneous databases

ChiTaRSiE2F5. human.
GeneWikiiE2F5.
GenomeRNAii1875.
NextBioi7663.
PROiQ15329.
SOURCEiSearch...

Gene expression databases

BgeeiQ15329.
CleanExiHS_E2F5.
ExpressionAtlasiQ15329. baseline and differential.
GenevisibleiQ15329. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR015633. E2F.
IPR028316. E2F5.
IPR003316. E2F_WHTH_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 1 hit.
PTHR12081:SF35. PTHR12081:SF35. 1 hit.
PfamiPF02319. E2F_TDP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiE2F5_HUMAN
AccessioniPrimary (citable) accession number: Q15329
Secondary accession number(s): E9PBN9, Q16601, Q92756
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 142 of the entry and version 1 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 8
    Human chromosome 8: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.