Q96AV8 (E2F7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor E2F7
Short name=E2F-7

Gene names

Name:

E2F7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	911 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Along with E2F8, inhibitor of E2F-dependent transcription that is important for the control of the E2F1-TP53 apoptotic pathway. Directly represses E2F1 transcription By similarity. Binds DNA independently of DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3'. Appears to regulate a subset of E2F-dependent genes whose products are required for normal cell cycle progession. Ref.4 Ref.5
Subunit structure	Forms homodimers and, to a lesser extent, heterodimers with E2F8. Dimerization is important for DNA binding. Ref.6
Subcellular location	Nucleus Ref.5.
Domain	Both DNA-binding domains are required for DNA-binding and are proposed to form an intramolecular structure that is similar to the winged helix structure of the E2F-DP heterodimer.
Sequence similarities	Belongs to the E2F/DP family.
Sequence caution	The sequence BAG53510.1 differs from that shown. Reason: Frameshift at position 229.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	transcription factor complex Inferred from electronic annotation. Source: InterPro
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction Ref.5. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-1386765,EBI-1386765

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96AV8-1)

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: Q96AV8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     714-845: GLNGFNVLLS...QQPESPVYVG → VTSSSDPQEHPTHTS
     846-911: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 911	911	Transcription factor E2F7		PRO_0000298907
Regions
	DNA binding	142 – 211	70	Potential
	DNA binding	282 – 367	86	Potential
Amino acid modifications
	Modified residue	95	1	Phosphoserine Ref.8
	Modified residue	410	1	Phosphoserine Ref.7
Natural variations
	Alternative sequence	714 – 845	132	GLNGF…PVYVG → VTSSSDPQEHPTHTS in isoform 2.		VSP_027473
	Alternative sequence	846 – 911	66	Missing in isoform 2.		VSP_027474
	Natural variant	72	1	F → L. Ref.2 Ref.3 Corresponds to variant rs310791 [ dbSNP | Ensembl ].		VAR_034732
	Natural variant	626	1	M → V. Corresponds to variant rs3829295 [ dbSNP | Ensembl ].		VAR_034733
	Natural variant	854	1	H → Q. Corresponds to variant rs310831 [ dbSNP | Ensembl ].		VAR_034734
Experimental info
	Mutagenesis	147 – 148	2	LG → EE: Loss of DNA-binding and E2F-dependent repression. Ref.4
	Mutagenesis	185	1	R → A: Loss of DNA-binding and inhibition of E2F1-dependent activation. Ref.4 Ref.5
	Mutagenesis	334	1	R → A: Loss of DNA-binding and inhibition of E2F1-dependent activation. Ref.4 Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 2, 2010. Version 3. Checksum: 748FEC8F24EAC5D8	FASTA	911	99,888
	10 20 30 40 50 60 MEVNCLTLKD LISPRQPRLD FAVEDGENAQ KENIFVDRSR MAPKTPIKNE PIDLSKQKKF 70 80 90 100 110 120 TPERNPITPV KFVDRQQAEP WTPTANLKML ISAASPDIRD REKKKGLFRP IENKDDAFTD 130 140 150 160 170 180 SLQLDVVGDS AVDEFEKQRP SRKQKSLGLL CQKFLARYPS YPLSTEKTTI SLDEVAVSLG 190 200 210 220 230 240 VERRRIYDIV NVLESLHLVS RVAKNQYGWH GRHSLPKTLR NLQRLGEEQK YEEQMAYLQQ 250 260 270 280 290 300 KELDLIDYKF GERKKDGDPD SQEQQLLDFS EPDCPSSSAN SRKDKSLRIM SQKFVMLFLV 310 320 330 340 350 360 SKTKIVTLDV AAKILIEESQ DAPDHSKFKT KVRRLYDIAN VLTSLALIKK VHVTEERGRK 370 380 390 400 410 420 PAFKWIGPVD FSSSDEELVD VSASVLPELK RETYGQIQVC AKQKLARHGS FNTVQASERI 430 440 450 460 470 480 QRKVNSEPSS PYREEQGSGG YSLEIGSLAA VYRQKIEDNS QGKAFASKRV VPPSSSLDPV 490 500 510 520 530 540 APFPVLSVDP EYCVNPLAHP VFSVAQTDLQ AFSMQNGLNG QVDVSLASAA SAVESLKPAL 550 560 570 580 590 600 LAGQPLVYVP SASLFMLYGS LQEGPASGSG SERDDRSSEA PATVELSSAP SAQKRLCEER 610 620 630 640 650 660 KPQEEDEPAT KRQSREYEDG PLSLVMPKKP SDSTDLASPK TMGNRASIPL KDIHVNGQLP 670 680 690 700 710 720 AAEEISGKAT ANSLVSSEWG NPSRNTDVEK PSKENESTKE PSLLQYLCVQ SPAGLNGFNV 730 740 750 760 770 780 LLSGSQTPPT VGPSSGQLPS FSVPCMVLPS PPLGPFPVLY SPAMPGPVSS TLGALPNTGP 790 800 810 820 830 840 VNFSLPGLGS IAQLLVGPTA VVNPKSSTLP SADPQLQSQP SLNLSPVMSR SHSVVQQPES 850 860 870 880 890 900 PVYVGHPVSV VKLHQSPVPV TPKSIQRTHR ETFFKTPGSL GDPVLKRRER NQSRNTSSAQ 910 RRLEIPSGGA D
	Isoform 2 [UniParc]. Checksum: B3C8896A9619917B	FASTA	728	80,866
	10 20 30 40 50 60 MEVNCLTLKD LISPRQPRLD FAVEDGENAQ KENIFVDRSR MAPKTPIKNE PIDLSKQKKF 70 80 90 100 110 120 TPERNPITPV KFVDRQQAEP WTPTANLKML ISAASPDIRD REKKKGLFRP IENKDDAFTD 130 140 150 160 170 180 SLQLDVVGDS AVDEFEKQRP SRKQKSLGLL CQKFLARYPS YPLSTEKTTI SLDEVAVSLG 190 200 210 220 230 240 VERRRIYDIV NVLESLHLVS RVAKNQYGWH GRHSLPKTLR NLQRLGEEQK YEEQMAYLQQ 250 260 270 280 290 300 KELDLIDYKF GERKKDGDPD SQEQQLLDFS EPDCPSSSAN SRKDKSLRIM SQKFVMLFLV 310 320 330 340 350 360 SKTKIVTLDV AAKILIEESQ DAPDHSKFKT KVRRLYDIAN VLTSLALIKK VHVTEERGRK 370 380 390 400 410 420 PAFKWIGPVD FSSSDEELVD VSASVLPELK RETYGQIQVC AKQKLARHGS FNTVQASERI 430 440 450 460 470 480 QRKVNSEPSS PYREEQGSGG YSLEIGSLAA VYRQKIEDNS QGKAFASKRV VPPSSSLDPV 490 500 510 520 530 540 APFPVLSVDP EYCVNPLAHP VFSVAQTDLQ AFSMQNGLNG QVDVSLASAA SAVESLKPAL 550 560 570 580 590 600 LAGQPLVYVP SASLFMLYGS LQEGPASGSG SERDDRSSEA PATVELSSAP SAQKRLCEER 610 620 630 640 650 660 KPQEEDEPAT KRQSREYEDG PLSLVMPKKP SDSTDLASPK TMGNRASIPL KDIHVNGQLP 670 680 690 700 710 720 AAEEISGKAT ANSLVSSEWG NPSRNTDVEK PSKENESTKE PSLLQYLCVQ SPAVTSSSDP QEHPTHTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-911 (ISOFORM 2), VARIANT LEU-72.
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-911 (ISOFORM 1), VARIANT LEU-72. Tissue: Testis.
[4]	"E2F7, a novel E2F featuring DP-independent repression of a subset of E2F-regulated genes." Di Stefano L., Jensen M.R., Helin K. EMBO J. 22:6289-6298(2003) [PubMed: 14633988] [Abstract] Cited for: IDENTIFICATION, FUNCTION, SELF-ASSOCIATION, MUTAGENESIS OF 147-LEU-GLY-148.
[5]	"E2F-7: a distinctive E2F family member with an unusual organization of DNA-binding domains." Logan N., Delavaine L., Graham A., Reilly C., Wilson J., Brummelkamp T.R., Hijmans E.M., Bernards R., La Thangue N.B. Oncogene 23:5138-5150(2004) [PubMed: 15133492] [Abstract] Cited for: FUNCTION, SELF-ASSOCIATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-185 AND ARG-334.
[6]	"Synergistic function of E2F7 and E2F8 is essential for cell survival and embryonic development." Li J., Ran C., Li E., Gordon F., Comstock G., Siddiqui H., Cleghorn W., Chen H.-Z., Kornacker K., Liu C.-G., Pandit S.K., Khanizadeh M., Weinstein M., Leone G., de Bruin A. Dev. Cell 14:62-75(2008) [PubMed: 18194653] [Abstract] Cited for: DIMERIZATION.
[7]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, MASS SPECTROMETRY. Tissue: Embryonic kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC025161 Genomic DNA. No translation available. AC079030 Genomic DNA. No translation available. BC016658 mRNA. Translation: AAH16658.1. BC136366 mRNA. Translation: AAI36367.1. BC136367 mRNA. Translation: AAI36368.1. BC017481 mRNA. No translation available. AK097677 mRNA. Translation: BAG53510.1. Frameshift.
IPI	IPI00414604. IPI00854868.
RefSeq	NP_976328.2. NM_203394.2.
UniGene	Hs.416375.
3D structure databases
ProteinModelPortal	Q96AV8.
SMR	Q96AV8. Positions 141-212, 281-366.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96AV8. 1 interaction.
MINT	MINT-6541592.
STRING	Q96AV8.
PTM databases
PhosphoSite	Q96AV8.
Polymorphism databases
DMDM	311033456.
Proteomic databases
PRIDE	Q96AV8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000322886; ENSP00000323246; ENSG00000165891.
GeneID	144455.
KEGG	hsa:144455.
Organism-specific databases
CTD	144455.
GeneCards	GC12M077415.
H-InvDB	HIX0010843.
HGNC	HGNC:23820. E2F7.
MIM	612046. gene.
neXtProt	NX_Q96AV8.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13390.
GeneTree	ENSGT00530000063616.
HOGENOM	HBG505309.
HOVERGEN	HBG063270.
InParanoid	Q96AV8.
OMA	QRKVNSE.
OrthoDB	EOG402WRS.
PhylomeDB	Q96AV8.
Gene expression databases
ArrayExpress	Q96AV8.
Bgee	Q96AV8.
CleanEx	HS_E2F7.
Genevestigator	Q96AV8.
Family and domain databases
InterPro	IPR015633. E2F. IPR003316. E2F_TDP. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 2 hits.
KO	K09391.
PANTHER	PTHR12081. E2F. 1 hit.
Pfam	PF02319. E2F_TDP. 2 hits. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

E2F7_HUMAN

Accession

Primary (citable) accession number: Q96AV8
Secondary accession number(s): A6NC74, B2RMR7, B3KUP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	November 2, 2010
Last modified:	January 25, 2012
This is version 65 of the entry and version 3 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.