Q66K89 (E4F1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	784 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleoplasm. 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 process	Cell cycle Cell division Growth regulation Host-virus interaction Mitosis Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Ligase Repressor
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: Compara cell division Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Traceable author statement Ref.11. Source: ProtInc embryo development Inferred from electronic annotation. Source: Compara 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: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell spindle Inferred from electronic annotation. Source: Compara
Molecular_function	cAMP response element binding Inferred from direct assay Ref.14. Source: UniProtKB ligase activity 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 zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RASSF1	Q9NS23-2	7	EBI-1227043,EBI-438698

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 784	784	Transcription factor E4F1		PRO_0000324307
Regions
	Zinc finger	192 – 214	23	C2H2-type 1
	Zinc finger	220 – 242	23	C2H2-type 2
	Zinc finger	248 – 272	25	C2H2-type 3; degenerate
	Zinc finger	435 – 457	23	C2H2-type 4
	Zinc finger	463 – 485	23	C2H2-type 5
	Zinc finger	491 – 513	23	C2H2-type 6
	Zinc finger	519 – 541	23	C2H2-type 7
	Zinc finger	547 – 569	23	C2H2-type 8
	Zinc finger	575 – 597	23	C2H2-type 9; degenerate
	Region	41 – 85	45	Required for ubiquitin ligase activity
	Region	184 – 263	80	Mediates dimerization, DNA-binding, transcription repression of CCNA2 and interaction with HMGA2
	Region	369 – 566	198	Mediates interaction with CDKN2A
	Region	435 – 599	165	Interaction with BMI1
	Region	521 – 580	60	Mediates interaction with TP53
	Region	575 – 597	23	Mediates interaction with RASSF1
Amino acid modifications
	Modified residue	50	1	Phosphoserine Ref.26 Ref.27
Natural variations
	Natural variant	167	1	R → H. Ref.1 Ref.2 Ref.4 Ref.5 Corresponds to variant rs26839 [ dbSNP | Ensembl ].		VAR_060270
	Natural variant	355	1	V → I. Corresponds to variant rs59784157 [ dbSNP | Ensembl ].		VAR_060271
Experimental info
	Mutagenesis	194	1	C → S: Increases DNA-binding; when associated with S-197. Ref.8
	Mutagenesis	197	1	C → S: Increases DNA-binding; when associated with S-194. Ref.8
	Mutagenesis	210	1	H → A: Alters DNA-binding. Ref.8
	Mutagenesis	237	1	R → L: Alters DNA-binding; when associated with N-238. Ref.8
	Mutagenesis	238	1	H → N: Alters DNA-binding; when associated with L-237. Ref.8
	Mutagenesis	249	1	K → M: Alters DNA-binding; when associated with S-250. Ref.8
	Mutagenesis	250	1	C → S: Alters DNA-binding; when associated with M-249. Ref.8
	Sequence conflict	4	1	A → E in AAD09139. Ref.1
	Sequence conflict	363 – 364	2	SE → RK in AAD09139. Ref.1
	Sequence conflict	425	1	A → V in BAF83018. Ref.2
	Sequence conflict	480 – 481	2	KH → TD in AAD09139. Ref.1
	Sequence conflict	544	1	E → D in BAF83018. Ref.2
	Sequence conflict	681 – 682	2	QA → PR in AAD09139. Ref.1
	Sequence conflict	704 – 705	2	EA → RG in AAD09139. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q66K89 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 60F6E711F2748FD8	FASTA	784	83,496
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
IPI	IPI00184135.
RefSeq	NP_004415.2. NM_004424.3.
UniGene	Hs.513268. Hs.615283.
3D structure databases
HSSP	HSSP built from PDB template 3ZNF based on UniProtKB P15822.
ProteinModelPortal	Q66K89.
SMR	Q66K89. Positions 192-269, 433-599.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q66K89. 1 interaction.
MINT	MINT-137139.
STRING	9606.ENSP00000301727.
PTM databases
PhosphoSite	Q66K89.
Polymorphism databases
DMDM	296434488.
Proteomic databases
PaxDb	Q66K89.
PRIDE	Q66K89.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000301727; ENSP00000301727; ENSG00000167967.
GeneID	1877.
KEGG	hsa:1877.
UCSC	uc002cpm.3. human.
Organism-specific databases
CTD	1877.
GeneCards	GC16P002276.
HGNC	HGNC:3121. E4F1.
MIM	603022. gene.
neXtProt	NX_Q66K89.
PharmGKB	PA27579.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5048.
HOGENOM	HOG000168447.
HOVERGEN	HBG052707.
InParanoid	Q66K89.
OMA	RERRFRC.
OrthoDB	EOG4PZJ8D.
PhylomeDB	Q66K89.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q66K89.
Bgee	Q66K89.
CleanEx	HS_E4F1.
Genevestigator	Q66K89.
Family and domain databases
Gene3D	3.30.160.60. 9 hits.
InterPro	IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
SMART	SM00355. ZnF_C2H2. 10 hits. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 7 hits. PS50157. ZINC_FINGER_C2H2_2. 9 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1877.
NextBio	7679.
SOURCE	Search...

Entry information

Entry name

E4F1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.