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Q66K89 (E4F1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor E4F1

EC=6.3.2.-
Alternative name(s):
E4F transcription factor 1
Putative E3 ubiquitin-protein ligase E4F1
Transcription factor E4F
p120E4F
p50E4F
Gene names
Name:E4F1
Synonyms:E4F
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function as a transcriptional repressor. May also function as a ubiquitin ligase mediating ubiquitination of chromatin-associated TP53. Functions in cell survival and proliferation through control of the cell cycle. Functions in the p53 and pRB tumor suppressor pathways and regulates the cyclin CCNA2 transcription. Ref.1 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.18 Ref.20 Ref.21 Ref.22

Identified as a cellular target of the adenoviral oncoprotein E1A, it is required for both transcriptional activation and repression of viral genes. Ref.1 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.18 Ref.20 Ref.21 Ref.22

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Homodimer; binds DNA as a dimer. Forms a complex with CDKN2A and TP53. Interactions with TP53, RB1, ANP32A, BMI1 and FHL2 regulate E4F1 activity. Interacts with HDAC1, HMGA2 and RASSF1. Interacts with HBV protein X. Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24

Subcellular location

Nucleusnucleoplasm. Cytoplasm. Note: A small fraction is detected in the cytoplasm. Excluded from the nucleolus where it is targeted upon CDKN2A overexpression. Localizes to the mitotic spindle during embryogenesis By similarity. Ref.13 Ref.21

Tissue specificity

Ubiquitously expressed. Ref.6

Developmental stage

Expressed in a variety of fetal tissues. Ref.6

Induction

Up-regulated by estrogen. Ref.11 Ref.16

Post-translational modification

Proteolytic cleavage produces a 50 kDa N-terminal peptide (p50E4F) which has a DNA-binding activity and activates transcription in presence of the adenoviral E1A protein. The major full length protein (p120E4F) functions as a repressor of transcription.

Phosphorylated; p120E4F and p50E4F are both phosphorylated. Phosphorylation is cell cycle-dependent and differentially regulates DNA-binding activity and function of both forms. Ref.1 Ref.8

May be sumoylated by UBE2I upon interaction with CDKN2A. Ref.19

Sequence similarities

Contains 9 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Growth regulation
Host-virus interaction
Mitosis
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionLigase
Repressor
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Traceable author statement Ref.11. Source: ProtInc

embryo development

Inferred from electronic annotation. Source: Ensembl

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle arrest

Traceable author statement Ref.14. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.14. Source: UniProtKB

protein ubiquitination

Inferred from electronic annotation. Source: UniProtKB-UniPathway

regulation of cell cycle process

Inferred from direct assay Ref.14. Source: UniProtKB

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of mitotic cell cycle, embryonic

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

spindle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Traceable author statement Ref.11. Source: ProtInc

cAMP response element binding

Inferred from direct assay Ref.14. Source: UniProtKB

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.11Ref.1. Source: ProtInc

transcription coactivator activity

Traceable author statement Ref.1. Source: ProtInc

transcription corepressor activity

Traceable author statement Ref.11. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

8Q647704EBI-1227043,EBI-8642971From a different organism.
ANP32AP396873EBI-1227043,EBI-359234
HDAC1Q135473EBI-1227043,EBI-301834
HDAC1Q6IT962EBI-1227043,EBI-6979193
lnx2bA4VCF73EBI-1227043,EBI-6979266From a different organism.
RASSF1Q9NS23-27EBI-1227043,EBI-438698
tcf7l1aQ9YHE82EBI-1227043,EBI-6979298From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 784784Transcription factor E4F1
PRO_0000324307

Regions

Zinc finger192 – 21423C2H2-type 1
Zinc finger220 – 24223C2H2-type 2
Zinc finger248 – 27225C2H2-type 3; degenerate
Zinc finger435 – 45723C2H2-type 4
Zinc finger463 – 48523C2H2-type 5
Zinc finger491 – 51323C2H2-type 6
Zinc finger519 – 54123C2H2-type 7
Zinc finger547 – 56923C2H2-type 8
Zinc finger575 – 59723C2H2-type 9; degenerate
Region41 – 8545Required for ubiquitin ligase activity
Region184 – 26380Mediates dimerization, DNA-binding, transcription repression of CCNA2 and interaction with HMGA2
Region369 – 566198Mediates interaction with CDKN2A
Region435 – 599165Interaction with BMI1
Region521 – 58060Mediates interaction with TP53
Region575 – 59723Mediates interaction with RASSF1

Amino acid modifications

Modified residue501Phosphoserine Ref.26 Ref.27

Natural variations

Natural variant1671R → H. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs26839 [ dbSNP | Ensembl ].
VAR_060270
Natural variant3551V → I.
Corresponds to variant rs59784157 [ dbSNP | Ensembl ].
VAR_060271

Experimental info

Mutagenesis1941C → S: Increases DNA-binding; when associated with S-197. Ref.8
Mutagenesis1971C → S: Increases DNA-binding; when associated with S-194. Ref.8
Mutagenesis2101H → A: Alters DNA-binding. Ref.8
Mutagenesis2371R → L: Alters DNA-binding; when associated with N-238. Ref.8
Mutagenesis2381H → N: Alters DNA-binding; when associated with L-237. Ref.8
Mutagenesis2491K → M: Alters DNA-binding; when associated with S-250. Ref.8
Mutagenesis2501C → S: Alters DNA-binding; when associated with M-249. Ref.8
Sequence conflict41A → E in AAD09139. Ref.1
Sequence conflict363 – 3642SE → RK in AAD09139. Ref.1
Sequence conflict4251A → V in BAF83018. Ref.2
Sequence conflict480 – 4812KH → TD in AAD09139. Ref.1
Sequence conflict5441E → D in BAF83018. Ref.2
Sequence conflict681 – 6822QA → PR in AAD09139. Ref.1
Sequence conflict704 – 7052EA → RG in AAD09139. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q66K89 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 60F6E711F2748FD8

FASTA78483,496
        10         20         30         40         50         60 
MEGAMAVRVT AAHTAEAQAE AGREAGEGAV AAVAAALAPS GFLGLPAPFS EEDEDDVHRC 

        70         80         90        100        110        120 
GRCQAEFTAL EDFVQHKIQK ACQRAPPEAL PATPATTALL GQEVVPAAPG PEEPITVAHI 

       130        140        150        160        170        180 
VVEAASLAAD ISHASDLVGG GHIKEVIVAA EAELGDGEMA EAPGSPRQQG LGLAGEGEQA 

       190        200        210        220        230        240 
QVKLLVNKDG RYVCALCHKT FKTGSILKAH MVTHSSRKDH ECKLCGASFR TKGSLIRHHR 

       250        260        270        280        290        300 
RHTDERPYKC SKCGKSFRES GALTRHLKSL TPCTEKIRFS VSKDVVVSKE DARAGSGAGA 

       310        320        330        340        350        360 
AGLGTATSSV TGEPIETSPV IHLVTDAKGT VIHEVHVQMQ ELSLGMKALA PEPPVSQELP 

       370        380        390        400        410        420 
CSSEGSRENL LHQAMQNSGI VLERAAGEEG ALEPAPAAGS SPQPLAVAAP QLPVLEVQPL 

       430        440        450        460        470        480 
ETQVASEASA VPRTHPCPQC SETFPTAATL EAHKRGHTGP RPFACAQCGK AFPKAYLLKK 

       490        500        510        520        530        540 
HQEVHVRERR FRCGDCGKLY KTIAHVRGHR RVHSDERPYP CPKCGKRYKT KNAQQVHFRT 

       550        560        570        580        590        600 
HLEEKPHVCQ FCSRGFREKG SLVRHVRHHT GEKPFKCYKC GRGFAEHGTL NRHLRTKGGC 

       610        620        630        640        650        660 
LLEVEELLVS EDSPAAATTV LTEDPHTVLV EFSSVVADTQ EYIIEATADD AETSEATEII 

       670        680        690        700        710        720 
EGTQTEVDSH IMKVVQQIVH QASAGHQIIV QNVTMDEETA LGPEAAAADT ITIATPESLT 

       730        740        750        760        770        780 
EQVAMTLASA ISEGTVLAAR AGTSGTEQAT VTMVSSEDIE ILEHAGELVI ASPEGQLEVQ 


TVIV 

« Hide

References

« Hide 'large scale' references
[1]"The adenovirus E1A-regulated transcription factor E4F is generated from the human homolog of nuclear factor phiAP3."
Fernandes E.R., Rooney R.J.
Mol. Cell. Biol. 17:1890-1903(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEOLYTIC PROCESSING, PHOSPHORYLATION, DNA-BINDING, VARIANT HIS-167.
Tissue: Cervix carcinoma.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-167.
Tissue: Tongue.
[3]"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. expand/collapse author list , 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].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT HIS-167.
[5]"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], VARIANT HIS-167.
Tissue: Uterus.
[6]"Chromosomal location and tissue expression of the gene encoding the adenovirus E1A-regulated transcription factor E4F in humans and mice."
Rooney R.J., Daniels R.R., Jenkins N.A., Gilbert D.J., Rothammer K., Morris S.W., Higgs D.R., Copeland N.G.
Mamm. Genome 9:320-323(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"Adenovirus E1A-regulated transcription factor p120E4F inhibits cell growth and induces the stabilization of the cdk inhibitor p21WAF1."
Fernandes E.R., Zhang J.Y., Rooney R.J.
Mol. Cell. Biol. 18:459-467(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Mutational analysis of p50E4F suggests that DNA binding activity is mediated through an alternative structure in a zinc finger domain that is regulated by phosphorylation."
Rooney R.J., Rothammer K., Fernandes E.R.
Nucleic Acids Res. 26:1681-1688(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: OLIGOMERIZATION, PHOSPHORYLATION, DNA-BINDING, MUTAGENESIS OF CYS-194; CYS-197; HIS-210; ARG-237; HIS-238; LYS-249 AND CYS-250.
[9]"Suppression of E1A-mediated transformation by the p50E4F transcription factor."
Fernandes E.R., Rooney R.J.
Mol. Cell. Biol. 19:4739-4749(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"p53 is involved in the p120E4F-mediated growth arrest."
Sandy P., Gostissa M., Fogal V., Cecco L.D., Szalay K., Rooney R.J., Schneider C., Del Sal G.
Oncogene 19:188-199(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TP53.
[11]"pRB binds to and modulates the transrepressing activity of the E1A-regulated transcription factor p120E4F."
Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E., Medema R., Vignais M.-L., Sardet C.
Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, REGULATION BY RB1, INTERACTION WITH RB1.
[12]"Cyclin A is a mediator of p120E4F-dependent cell cycle arrest in G1."
Fajas L., Paul C., Vie A., Estrach S., Medema R., Blanchard J.M., Sardet C., Vignais M.-L.
Mol. Cell. Biol. 21:2956-2966(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Association of p14ARF with the p120E4F transcriptional repressor enhances cell cycle inhibition."
Rizos H., Diefenbach E., Badhwar P., Woodruff S., Becker T.M., Rooney R.J., Kefford R.F.
J. Biol. Chem. 278:4981-4989(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH CDKN2A AND TP53, SUBCELLULAR LOCATION.
[14]"Transcriptional activation of the cyclin A gene by the architectural transcription factor HMGA2."
Tessari M.A., Gostissa M., Altamura S., Sgarra R., Rustighi A., Salvagno C., Caretti G., Imbriano C., Mantovani R., Del Sal G., Giancotti V., Manfioletti G.
Mol. Cell. Biol. 23:9104-9116(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HMGA2.
[15]"Modulation of p120E4F transcriptional activity by the Gam1 adenoviral early protein."
Colombo R., Draetta G.F., Chiocca S.
Oncogene 22:2541-2547(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC1.
[16]"E4F1, a novel estrogen-responsive gene in possible atheroprotection, revealed by microarray analysis."
Nakamura Y., Igarashi K., Suzuki T., Kanno J., Inoue T., Tazawa C., Saruta M., Ando T., Moriyama N., Furukawa T., Ono M., Moriya T., Ito K., Saito H., Ishibashi T., Takahashi S., Yamada S., Sasano H.
Am. J. Pathol. 165:2019-2031(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY ESTROGEN.
[17]"Identification of the E1A-regulated transcription factor p120 E4F as an interacting partner of the RASSF1A candidate tumor suppressor gene."
Fenton S.L., Dallol A., Agathanggelou A., Hesson L., Ahmed-Choudhury J., Baksh S., Sardet C., Dammann R., Minna J.D., Downward J., Maher E.R., Latif F.
Cancer Res. 64:102-107(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RASSF1.
[18]"Transcriptional regulation of cyclin A2 by RASSF1A through the enhanced binding of p120E4F to the cyclin A2 promoter."
Ahmed-Choudhury J., Agathanggelou A., Fenton S.L., Ricketts C., Clark G.J., Maher E.R., Latif F.
Cancer Res. 65:2690-2697(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"p14ARF interacts with the SUMO-conjugating enzyme Ubc9 and promotes the sumoylation of its binding partners."
Rizos H., Woodruff S., Kefford R.F.
Cell Cycle 4:597-603(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[20]"E4F1 is an atypical ubiquitin ligase that modulates p53 effector functions independently of degradation."
Le Cam L., Linares L.K., Paul C., Julien E., Lacroix M., Hatchi E., Triboulet R., Bossis G., Shmueli A., Rodriguez M.S., Coux O., Sardet C.
Cell 127:775-788(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TP53.
[21]"E4F1: a novel candidate factor for mediating BMI1 function in primitive hematopoietic cells."
Chagraoui J., Niessen S.L., Lessard J., Girard S., Coulombe P., Sauvageau M., Meloche S., Sauvageau G.
Genes Dev. 20:2110-2120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BMI1, SUBCELLULAR LOCATION.
[22]"The LIM-only protein FHL2 is a negative regulator of E4F1."
Paul C., Lacroix M., Iankova I., Julien E., Schaefer B.W., Labalette C., Wei Y., Le Cam A., Le Cam L., Sardet C.
Oncogene 25:5475-5484(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FHL2.
[23]"Interaction of the hepatitis B virus protein HBx with the human transcription regulatory protein p120E4F in vitro."
Rui E., Moura P.R., Goncalves K.A., Rooney R.J., Kobarg J.
Virus Res. 115:31-42(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HBV PROTEIN X.
[24]"The role of LANP and ataxin 1 in E4F-mediated transcriptional repression."
Cvetanovic M., Rooney R.J., Garcia J.J., Toporovskaya N., Zoghbi H.Y., Opal P.
EMBO Rep. 8:671-677(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANP32A.
[25]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[27]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U87269 mRNA. Translation: AAD09139.1.
AK290329 mRNA. Translation: BAF83018.1.
AC009065 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85532.1.
BC080524 mRNA. Translation: AAH80524.1.
RefSeqNP_001275705.1. NM_001288776.1.
NP_001275707.1. NM_001288778.1.
NP_004415.3. NM_004424.4.
UniGeneHs.513268.

3D structure databases

ProteinModelPortalQ66K89.
SMRQ66K89. Positions 113-297, 404-596.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108209. 12 interactions.
IntActQ66K89. 11 interactions.
MINTMINT-137139.
STRING9606.ENSP00000301727.

PTM databases

PhosphoSiteQ66K89.

Polymorphism databases

DMDM296434488.

Proteomic databases

PaxDbQ66K89.
PRIDEQ66K89.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301727; ENSP00000301727; ENSG00000167967.
GeneID1877.
KEGGhsa:1877.
UCSCuc002cpm.3. human.

Organism-specific databases

CTD1877.
GeneCardsGC16P002276.
HGNCHGNC:3121. E4F1.
HPAHPA052042.
MIM603022. gene.
neXtProtNX_Q66K89.
PharmGKBPA27579.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000168447.
HOVERGENHBG052707.
InParanoidQ66K89.
OMACQFCSRG.
OrthoDBEOG761BT6.
PhylomeDBQ66K89.
TreeFamTF315387.

Enzyme and pathway databases

SignaLinkQ66K89.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ66K89.
BgeeQ66K89.
CleanExHS_E4F1.
GenevestigatorQ66K89.

Family and domain databases

Gene3D3.30.160.60. 9 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 10 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiE4F1.
GenomeRNAi1877.
NextBio7679.
PROQ66K89.
SOURCESearch...

Entry information

Entry nameE4F1_HUMAN
AccessionPrimary (citable) accession number: Q66K89
Secondary accession number(s): A8K2R4, O00146
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 106 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 16

Human chromosome 16: entries, gene names and cross-references to MIM