Q8CCE9 (E4F1_MOUSE) 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
Transcription factor phi AP3
p120E4F

Gene names

Name:

E4f1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	783 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.4 Ref.6 Ref.8 Ref.9
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Homodimer; binds DNA as a dimer By similarity. Forms a complex with CDKN2A and TP53. Interacts with HDAC1, HMGA2 and RASSF1 By similarity. Interactions with TP53, RB1, ANP32A and probably BMI1 and FHL2 regulate E4F1 activity. Ref.6 Ref.7 Ref.9
Subcellular location	Nucleus › nucleoplasm. Cytoplasm By similarity. Note: A small fraction is detected in the cytoplasm By similarity. Excluded from the nucleolus where it is targeted upon CDKN2A overexpression. Localizes to the mitotic spindle during embryogenesis. Ref.4 Ref.8
Tissue specificity	Ubiquitously expressed. Ref.4 Ref.5
Developmental stage	Continuously expressed during embryogenesis. Ref.5
Post-translational modification	Phosphorylated; phosphorylation is cell cycle-dependent and regulates DNA-binding activity and function. Ref.4 May be sumoylated by UBE2I upon interaction with CDKN2A By similarity.
Disruption phenotype	Death before E7.5 probably at the peri-implantation stage. Blastocysts display defects in mitotic progression and chromosomal segregation and increased apoptosis. Ref.8
Sequence similarities	Contains 9 C2H2-type zinc fingers.
Sequence caution	The sequence AAF22563.1 differs from that shown. Reason: Frameshift at positions 230 and 235. The sequence AAH71228.1 differs from that shown. Reason: Frameshift at position 94. The sequence BAE25748.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA54188.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle Cell division Growth regulation Mitosis Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
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 mutant phenotype Ref.8. Source: MGI cell division Inferred from electronic annotation. Source: UniProtKB-KW embryo development Inferred from mutant phenotype Ref.8. Source: MGI mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of cell cycle process Inferred from direct assay PubMed 14645522. Source: UniProtKB regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW regulation of mitotic cell cycle, embryonic Inferred from mutant phenotype Ref.8. Source: MGI regulation of transcription, DNA-dependent Traceable author statement Ref.8. Source: MGI transcription, DNA-dependent 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 nucleus Inferred from direct assay Ref.8. Source: MGI spindle Inferred from direct assay Ref.8. Source: MGI
Molecular_function	DNA binding Inferred from direct assay Ref.8. Source: MGI cAMP response element binding Inferred from electronic annotation. Source: Compara ligase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8CCE9-1)

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: Q8CCE9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     667-684: DSHIMKVVQQIVHQAGAG → RVWVRDGRITGLLGSPSG
     685-783: Missing.

Isoform 3 (identifier: Q8CCE9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     422-422: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q8CCE9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     458-458: A → VWQGLPQSLP...AWHTQPAPAH
     459-783: Missing.

Note: No experimental confirmation available.

Isoform 5 (identifier: Q8CCE9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     244-274: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 783	783	Transcription factor E4F1		PRO_0000324308
Regions
	Zinc finger	193 – 215	23	C2H2-type 1
	Zinc finger	221 – 243	23	C2H2-type 2
	Zinc finger	249 – 273	25	C2H2-type 3; degenerate
	Zinc finger	434 – 456	23	C2H2-type 4
	Zinc finger	462 – 484	23	C2H2-type 5
	Zinc finger	490 – 512	23	C2H2-type 6
	Zinc finger	518 – 540	23	C2H2-type 7
	Zinc finger	546 – 568	23	C2H2-type 8
	Zinc finger	574 – 596	23	C2H2-type 9; degenerate
	Region	40 – 84	45	Required for ubiquitin ligase activity By similarity
	Region	185 – 264	80	Mediates dimerization, DNA-binding, transcription repression of CCNA2 and interaction with HMGA2 By similarity
	Region	368 – 565	198	Mediates interaction with CDKN2A By similarity
	Region	434 – 598	165	Interaction with BMI1 By similarity
	Region	520 – 579	60	Mediates interaction with TP53 By similarity
	Region	574 – 596	23	Mediates interaction with RASSF1 By similarity
Amino acid modifications
	Modified residue	49	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	244 – 274	31	Missing in isoform 5.		VSP_032192
	Alternative sequence	422	1	Missing in isoform 3.		VSP_032193
	Alternative sequence	458	1	A → VWQGLPQSLPAQEAPGGARA RAPLPLWRLWEALQDHRSCA GPPACSLRREAFPLSPVRQA LQNQECPASTLPDTSGRKAP RVPVLQPRLPGEGLSGAACE APHRRETFQVLQVWPWLRGA WHTQPAPAH in isoform 4.		VSP_032194
	Alternative sequence	459 – 783	325	Missing in isoform 4.		VSP_032195
	Alternative sequence	667 – 684	18	DSHIM…QAGAG → RVWVRDGRITGLLGSPSG in isoform 2.		VSP_032196
	Alternative sequence	685 – 783	99	Missing in isoform 2.		VSP_032197
Experimental info
	Sequence conflict	13	1	H → D in BAE25748. Ref.2
	Sequence conflict	18	1	R → G in AAF22563. Ref.1
	Sequence conflict	18	1	R → G in BAE25748. Ref.2
	Sequence conflict	18	1	R → G in AAH46459. Ref.3
	Sequence conflict	18	1	R → G in AAH71228. Ref.3
	Sequence conflict	30	1	V → VA in AAF22563. Ref.1
	Sequence conflict	30	1	V → VA in BAE25748. Ref.2
	Sequence conflict	62	1	C → F in BAE25748. Ref.2
	Sequence conflict	139	1	V → A in CAA54188. Ref.4
	Sequence conflict	148	1	I → V in CAA54188. Ref.4
	Sequence conflict	158	1	V → G in AAF22563. Ref.1
	Sequence conflict	158	1	V → G in BAE25748. Ref.2
	Sequence conflict	158	1	V → G in AAH46459. Ref.3
	Sequence conflict	158	1	V → G in AAH71228. Ref.3
	Sequence conflict	158	1	V → G in CAA54188. Ref.4
	Sequence conflict	224 – 225	2	KL → NF in AAF22563. Ref.1
	Sequence conflict	281	1	S → N in AAF22563. Ref.1
	Sequence conflict	281	1	S → N in BAE25748. Ref.2
	Sequence conflict	380	1	V → L in AAF22563. Ref.1
	Sequence conflict	390	1	A → V in AAF22563. Ref.1
	Sequence conflict	395 – 400	6	PPSGSS → LPFGST in AAF22563. Ref.1
	Sequence conflict	412	1	P → L in AAF22563. Ref.1
	Sequence conflict	479 – 480	2	KH → ND in CAA54188. Ref.4
	Sequence conflict	585 – 586	2	EH → DD in CAA54188. Ref.4
	Sequence conflict	630	1	E → Q in AAF22563. Ref.1
	Sequence conflict	630	1	E → Q in BAE25748. Ref.2
	Sequence conflict	630	1	E → Q in AAH46459. Ref.3
	Sequence conflict	630	1	E → Q in CAA54188. Ref.4
	Sequence conflict	705	1	T → A in AAF22563. Ref.1
	Sequence conflict	705	1	T → A in BAE25748. Ref.2
	Sequence conflict	705	1	T → A in CAA54188. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 18, 2008. Version 2. Checksum: 59E47F7A64A224A4	FASTA	783	84,296
	10 20 30 40 50 60 MEGAMAVRVT AAHTAEARAE AGREAGEGGV AAAAALSSGG FLGLPAPFSE EDEDDVHRCG 70 80 90 100 110 120 RCQVEFTALE DFVQHKIQKT CHRAPQEALP TTPAATALLD QEVVPTAAEG GPDEPITVAH 130 140 150 160 170 180 IVVEATSLAE DISHAPDLVG SGHIKEVIVA AEAEPGDVEM AEAPGSPNHQ ELGLLGEGEQ 190 200 210 220 230 240 AHVKLLVNKE GRYVCMLCHK TFKTGSILKA HMVTHSSRKD HECKLCGASF RTKGSLIRHH 250 260 270 280 290 300 RRHTDERPYK CAKCGKSFRE SGALTRHLKS LTPCTEKIRF SISKDTAVGK EEVPAGSSAS 310 320 330 340 350 360 TVGTVTSSVA GDPMETSPVI HLVTDAKGTV IHEVHVQMQE LPLGMKALTP ESPDSEELPC 370 380 390 400 410 420 SSENSRENLL HQAMQNSGIV LERVAGEESA LEPAPPSGSS PQCLGDGSPE LPLLKVEQIE 430 440 450 460 470 480 TQVASEAATV PRTHPCPQCS ETFPTAATLE AHKRGHIAPR PFTCTQCGKA FPKAYLLKKH 490 500 510 520 530 540 QEVHVHERRF RCGDCGKLYK TIAHVRGHRR VHSDERPFPC PQCGKRYKTK NAQQVHFRTH 550 560 570 580 590 600 LEEKPHVCQF CSRGFREKGS LVRHVRHHTG EKPFKCYKCG RGFAEHGTLN RHLRTKGGCL 610 620 630 640 650 660 LEVEELLVSE ESPSAAATVL AEDPHTVLVE FSSVVADTQE YIIEATADDT ETSEATEIIE 670 680 690 700 710 720 GTQTEVDSHI MKVVQQIVHQ AGAGHQIIVQ NVTMDQETAL GSEATAADTI TIATPESLTE 730 740 750 760 770 780 QVAMTLASAI SEGTVLTARA GPNSTEQATV TMVSSEDIEI LEHGGELVIA SPEGQLEVQT VIV
	Isoform 2 [UniParc]. Checksum: 62B9E2973ACA07C3	FASTA	684	74,060
	10 20 30 40 50 60 MEGAMAVRVT AAHTAEARAE AGREAGEGGV AAAAALSSGG FLGLPAPFSE EDEDDVHRCG 70 80 90 100 110 120 RCQVEFTALE DFVQHKIQKT CHRAPQEALP TTPAATALLD QEVVPTAAEG GPDEPITVAH 130 140 150 160 170 180 IVVEATSLAE DISHAPDLVG SGHIKEVIVA AEAEPGDVEM AEAPGSPNHQ ELGLLGEGEQ 190 200 210 220 230 240 AHVKLLVNKE GRYVCMLCHK TFKTGSILKA HMVTHSSRKD HECKLCGASF RTKGSLIRHH 250 260 270 280 290 300 RRHTDERPYK CAKCGKSFRE SGALTRHLKS LTPCTEKIRF SISKDTAVGK EEVPAGSSAS 310 320 330 340 350 360 TVGTVTSSVA GDPMETSPVI HLVTDAKGTV IHEVHVQMQE LPLGMKALTP ESPDSEELPC 370 380 390 400 410 420 SSENSRENLL HQAMQNSGIV LERVAGEESA LEPAPPSGSS PQCLGDGSPE LPLLKVEQIE 430 440 450 460 470 480 TQVASEAATV PRTHPCPQCS ETFPTAATLE AHKRGHIAPR PFTCTQCGKA FPKAYLLKKH 490 500 510 520 530 540 QEVHVHERRF RCGDCGKLYK TIAHVRGHRR VHSDERPFPC PQCGKRYKTK NAQQVHFRTH 550 560 570 580 590 600 LEEKPHVCQF CSRGFREKGS LVRHVRHHTG EKPFKCYKCG RGFAEHGTLN RHLRTKGGCL 610 620 630 640 650 660 LEVEELLVSE ESPSAAATVL AEDPHTVLVE FSSVVADTQE YIIEATADDT ETSEATEIIE 670 680 GTQTEVRVWV RDGRITGLLG SPSG
	Isoform 3 [UniParc]. Checksum: F0CEA4AC61FE5BDA	FASTA	782	84,168
	10 20 30 40 50 60 MEGAMAVRVT AAHTAEARAE AGREAGEGGV AAAAALSSGG FLGLPAPFSE EDEDDVHRCG 70 80 90 100 110 120 RCQVEFTALE DFVQHKIQKT CHRAPQEALP TTPAATALLD QEVVPTAAEG GPDEPITVAH 130 140 150 160 170 180 IVVEATSLAE DISHAPDLVG SGHIKEVIVA AEAEPGDVEM AEAPGSPNHQ ELGLLGEGEQ 190 200 210 220 230 240 AHVKLLVNKE GRYVCMLCHK TFKTGSILKA HMVTHSSRKD HECKLCGASF RTKGSLIRHH 250 260 270 280 290 300 RRHTDERPYK CAKCGKSFRE SGALTRHLKS LTPCTEKIRF SISKDTAVGK EEVPAGSSAS 310 320 330 340 350 360 TVGTVTSSVA GDPMETSPVI HLVTDAKGTV IHEVHVQMQE LPLGMKALTP ESPDSEELPC 370 380 390 400 410 420 SSENSRENLL HQAMQNSGIV LERVAGEESA LEPAPPSGSS PQCLGDGSPE LPLLKVEQIE 430 440 450 460 470 480 TVASEAATVP RTHPCPQCSE TFPTAATLEA HKRGHIAPRP FTCTQCGKAF PKAYLLKKHQ 490 500 510 520 530 540 EVHVHERRFR CGDCGKLYKT IAHVRGHRRV HSDERPFPCP QCGKRYKTKN AQQVHFRTHL 550 560 570 580 590 600 EEKPHVCQFC SRGFREKGSL VRHVRHHTGE KPFKCYKCGR GFAEHGTLNR HLRTKGGCLL 610 620 630 640 650 660 EVEELLVSEE SPSAAATVLA EDPHTVLVEF SSVVADTQEY IIEATADDTE TSEATEIIEG 670 680 690 700 710 720 TQTEVDSHIM KVVQQIVHQA GAGHQIIVQN VTMDQETALG SEATAADTIT IATPESLTEQ 730 740 750 760 770 780 VAMTLASAIS EGTVLTARAG PNSTEQATVT MVSSEDIEIL EHGGELVIAS PEGQLEVQTV IV
	Isoform 4 [UniParc]. Checksum: 03DE21745C393119	FASTA	586	62,553
	10 20 30 40 50 60 MEGAMAVRVT AAHTAEARAE AGREAGEGGV AAAAALSSGG FLGLPAPFSE EDEDDVHRCG 70 80 90 100 110 120 RCQVEFTALE DFVQHKIQKT CHRAPQEALP TTPAATALLD QEVVPTAAEG GPDEPITVAH 130 140 150 160 170 180 IVVEATSLAE DISHAPDLVG SGHIKEVIVA AEAEPGDVEM AEAPGSPNHQ ELGLLGEGEQ 190 200 210 220 230 240 AHVKLLVNKE GRYVCMLCHK TFKTGSILKA HMVTHSSRKD HECKLCGASF RTKGSLIRHH 250 260 270 280 290 300 RRHTDERPYK CAKCGKSFRE SGALTRHLKS LTPCTEKIRF SISKDTAVGK EEVPAGSSAS 310 320 330 340 350 360 TVGTVTSSVA GDPMETSPVI HLVTDAKGTV IHEVHVQMQE LPLGMKALTP ESPDSEELPC 370 380 390 400 410 420 SSENSRENLL HQAMQNSGIV LERVAGEESA LEPAPPSGSS PQCLGDGSPE LPLLKVEQIE 430 440 450 460 470 480 TQVASEAATV PRTHPCPQCS ETFPTAATLE AHKRGHIVWQ GLPQSLPAQE APGGARARAP 490 500 510 520 530 540 LPLWRLWEAL QDHRSCAGPP ACSLRREAFP LSPVRQALQN QECPASTLPD TSGRKAPRVP 550 560 570 580 VLQPRLPGEG LSGAACEAPH RRETFQVLQV WPWLRGAWHT QPAPAH
	Isoform 5 [UniParc]. Checksum: BC7A27C32B98E325	FASTA	752	80,830
	10 20 30 40 50 60 MEGAMAVRVT AAHTAEARAE AGREAGEGGV AAAAALSSGG FLGLPAPFSE EDEDDVHRCG 70 80 90 100 110 120 RCQVEFTALE DFVQHKIQKT CHRAPQEALP TTPAATALLD QEVVPTAAEG GPDEPITVAH 130 140 150 160 170 180 IVVEATSLAE DISHAPDLVG SGHIKEVIVA AEAEPGDVEM AEAPGSPNHQ ELGLLGEGEQ 190 200 210 220 230 240 AHVKLLVNKE GRYVCMLCHK TFKTGSILKA HMVTHSSRKD HECKLCGASF RTKGSLIRHH 250 260 270 280 290 300 RRHTEKIRFS ISKDTAVGKE EVPAGSSAST VGTVTSSVAG DPMETSPVIH LVTDAKGTVI 310 320 330 340 350 360 HEVHVQMQEL PLGMKALTPE SPDSEELPCS SENSRENLLH QAMQNSGIVL ERVAGEESAL 370 380 390 400 410 420 EPAPPSGSSP QCLGDGSPEL PLLKVEQIET QVASEAATVP RTHPCPQCSE TFPTAATLEA 430 440 450 460 470 480 HKRGHIAPRP FTCTQCGKAF PKAYLLKKHQ EVHVHERRFR CGDCGKLYKT IAHVRGHRRV 490 500 510 520 530 540 HSDERPFPCP QCGKRYKTKN AQQVHFRTHL EEKPHVCQFC SRGFREKGSL VRHVRHHTGE 550 560 570 580 590 600 KPFKCYKCGR GFAEHGTLNR HLRTKGGCLL EVEELLVSEE SPSAAATVLA EDPHTVLVEF 610 620 630 640 650 660 SSVVADTQEY IIEATADDTE TSEATEIIEG TQTEVDSHIM KVVQQIVHQA GAGHQIIVQN 670 680 690 700 710 720 VTMDQETALG SEATAADTIT IATPESLTEQ VAMTLASAIS EGTVLTARAG PNSTEQATVT 730 740 750 MVSSEDIEIL EHGGELVIAS PEGQLEVQTV IV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Repression of the murine Il-1 beta expression by the murine analog of E4F transcription factor." Lebedeva T.V., Singh A.K. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"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. , 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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-783 (ISOFORM 1). Strain: C57BL/6J. Tissue: Embryonic testis.
[3]	"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] (ISOFORMS 2 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-783 (ISOFORM 5). Strain: C57BL/6, FVB/N and NMRI. Tissue: Brain and Mammary tumor.
[4]	"Repression of adenovirus E1A enhancer activity by a novel zinc finger-containing DNA-binding protein related to the GLI-Kruppel protein." Fognani C., Della Valle G., Babiss L.E. EMBO J. 12:4985-4992(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 65-783 (ISOFORM 1), FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, PHOSPHORYLATION, TISSUE SPECIFICITY. Strain: BALB/c. Tissue: Liver.
[5]	"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.
[6]	"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.
[7]	"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: INTERACTION WITH RB1.
[8]	"The E4F protein is required for mitotic progression during embryonic cell cycles." Le Cam L., Lacroix M., Ciemerych M.A., Sardet C., Sicinski P. Mol. Cell. Biol. 24:6467-6475(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION.
[9]	"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: FUNCTION, INTERACTION WITH ANP32A.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF126967 mRNA. Translation: AAF22563.1. Frameshift. AK033285 mRNA. Translation: BAC28222.1. AK144176 mRNA. Translation: BAE25748.1. Different initiation. BC046459 mRNA. Translation: AAH46459.1. BC057011 mRNA. Translation: AAH57011.1. BC071228 mRNA. Translation: AAH71228.1. Frameshift. X76858 mRNA. Translation: CAA54188.1. Different initiation.
IPI	IPI00135611. IPI00463502. IPI00889215. IPI00889249. IPI00889257.
PIR	S41688.
RefSeq	NP_031919.2. NM_007893.3.
UniGene	Mm.163132.
3D structure databases
ProteinModelPortal	Q8CCE9.
SMR	Q8CCE9. Positions 182-271, 443-598.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4979074.
PTM databases
PhosphoSite	Q8CCE9.
Proteomic databases
PRIDE	Q8CCE9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000056032; ENSMUSP00000062344; ENSMUSG00000024137.
GeneID	13560.
KEGG	mmu:13560.
UCSC	uc008avy.1. mouse. uc008awa.1. mouse. uc008awb.1. mouse. uc012ami.1. mouse.
Organism-specific databases
CTD	1877.
MGI	MGI:109530. E4f1.
Phylogenomic databases
eggNOG	COG5048.
GeneTree	ENSGT00390000006768.
HOVERGEN	HBG052707.
InParanoid	Q8CCE9.
OMA	RERRFRC.
OrthoDB	EOG4N30NK.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Bgee	Q8CCE9.
CleanEx	MM_E4F1.
Genevestigator	Q8CCE9.
Family and domain databases
Gene3D	3.30.160.60. 8 hits.
InterPro	IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
Pfam	PF00096. zf-C2H2. 1 hit. [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
NextBio	284182.
SOURCE	Search...

Entry information

Entry name

E4F1_MOUSE

Accession

Primary (citable) accession number: Q8CCE9
Secondary accession number(s): Q05BH7 , Q3UNJ9, Q62065, Q6IR08, Q6PGI1, Q9QY56

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	May 29, 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