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Protein

Transcription factor E2F7

Gene

E2F7

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

Functioni

Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Also involved in DNA damage response: up-regulated by p53/TP53 following genotoxic stress and acts as a downstream effector of p53/TP53-dependent repression by mediating repression of indirect p53/TP53 target genes involved in DNA replication. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene. Acts as a negative regulator of keratinocyte differentiation.8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi142 – 21170Sequence analysisAdd
BLAST
DNA bindingi282 – 36786Sequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Cell cycle, DNA damage, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor E2F7
Short name:
E2F-7
Gene namesi
Name:E2F7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:23820. E2F7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi147 – 1482LG → EE: Loss of DNA-binding and E2F-dependent repression. 1 Publication
Mutagenesisi185 – 1851R → A: Loss of DNA-binding and inhibition of E2F1-dependent activation. Impairs DNA-binding and dimerization; when associated with A-334. 2 Publications
Mutagenesisi334 – 3341R → A: Loss of DNA-binding and inhibition of E2F1-dependent activation. Impairs DNA-binding and dimerization; when associated with A-185. 2 Publications

Polymorphism and mutation databases

BioMutaiE2F7.
DMDMi311033456.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 911911Transcription factor E2F7PRO_0000298907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei410 – 4101PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96AV8.
PaxDbiQ96AV8.
PRIDEiQ96AV8.

PTM databases

iPTMnetiQ96AV8.
PhosphoSiteiQ96AV8.

Expressioni

Inductioni

By p53/TP53 following DNA damage: expression is directly activated by p53/TP53 (at protein level).3 Publications

Gene expression databases

BgeeiQ96AV8.
CleanExiHS_E2F7.
ExpressionAtlasiQ96AV8. baseline and differential.
GenevisibleiQ96AV8. HS.

Interactioni

Subunit structurei

Homodimer and heterodimer: mainly forms homodimers and, to a lesser extent, heterodimers with E2F8. Dimerization is important for DNA-binding. Interacts with HIF1A.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1386765,EBI-1386765
E2F8A0AVK64EBI-1386765,EBI-7779316

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi126855. 8 interactions.
IntActiQ96AV8. 3 interactions.
MINTiMINT-6541592.
STRINGi9606.ENSP00000323246.

Structurei

3D structure databases

ProteinModelPortaliQ96AV8.
SMRiQ96AV8. Positions 141-209.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

In contrast to classical members of the E2F transcription factor, atypical members contain 2 DNA-binding domains and regulate transcription in a DP-independent manner. 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 (PubMed:14633988).1 Publication

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiKOG2578. Eukaryota.
ENOG4111IGY. LUCA.
GeneTreeiENSGT00530000063616.
HOGENOMiHOG000013193.
HOVERGENiHBG063270.
InParanoidiQ96AV8.
KOiK09391.
OMAiSLVMPKK.
OrthoDBiEOG7HHWSG.
PhylomeDBiQ96AV8.
TreeFamiTF105567.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR015633. E2F.
IPR003316. E2F_WHTH_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 3 hits.
PfamiPF02319. E2F_TDP. 2 hits.
[Graphical view]
SMARTiSM01372. E2F_TDP. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q96AV8-1) [UniParc]FASTAAdd to basket

Also known as: E2F7b

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
MEVNCLTLKD LISPRQPRLD FAVEDGENAQ KENIFVDRSR MAPKTPIKNE
60 70 80 90 100
PIDLSKQKKF TPERNPITPV KFVDRQQAEP WTPTANLKML ISAASPDIRD
110 120 130 140 150
REKKKGLFRP IENKDDAFTD SLQLDVVGDS AVDEFEKQRP SRKQKSLGLL
160 170 180 190 200
CQKFLARYPS YPLSTEKTTI SLDEVAVSLG VERRRIYDIV NVLESLHLVS
210 220 230 240 250
RVAKNQYGWH GRHSLPKTLR NLQRLGEEQK YEEQMAYLQQ KELDLIDYKF
260 270 280 290 300
GERKKDGDPD SQEQQLLDFS EPDCPSSSAN SRKDKSLRIM SQKFVMLFLV
310 320 330 340 350
SKTKIVTLDV AAKILIEESQ DAPDHSKFKT KVRRLYDIAN VLTSLALIKK
360 370 380 390 400
VHVTEERGRK PAFKWIGPVD FSSSDEELVD VSASVLPELK RETYGQIQVC
410 420 430 440 450
AKQKLARHGS FNTVQASERI QRKVNSEPSS PYREEQGSGG YSLEIGSLAA
460 470 480 490 500
VYRQKIEDNS QGKAFASKRV VPPSSSLDPV APFPVLSVDP EYCVNPLAHP
510 520 530 540 550
VFSVAQTDLQ AFSMQNGLNG QVDVSLASAA SAVESLKPAL LAGQPLVYVP
560 570 580 590 600
SASLFMLYGS LQEGPASGSG SERDDRSSEA PATVELSSAP SAQKRLCEER
610 620 630 640 650
KPQEEDEPAT KRQSREYEDG PLSLVMPKKP SDSTDLASPK TMGNRASIPL
660 670 680 690 700
KDIHVNGQLP AAEEISGKAT ANSLVSSEWG NPSRNTDVEK PSKENESTKE
710 720 730 740 750
PSLLQYLCVQ SPAGLNGFNV LLSGSQTPPT VGPSSGQLPS FSVPCMVLPS
760 770 780 790 800
PPLGPFPVLY SPAMPGPVSS TLGALPNTGP VNFSLPGLGS IAQLLVGPTA
810 820 830 840 850
VVNPKSSTLP SADPQLQSQP SLNLSPVMSR SHSVVQQPES PVYVGHPVSV
860 870 880 890 900
VKLHQSPVPV TPKSIQRTHR ETFFKTPGSL GDPVLKRRER NQSRNTSSAQ
910
RRLEIPSGGA D
Length:911
Mass (Da):99,888
Last modified:November 2, 2010 - v3
Checksum:i748FEC8F24EAC5D8
GO
Isoform 2 (identifier: Q96AV8-2) [UniParc]FASTAAdd to basket

Also known as: E2F7a

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

Show »
Length:728
Mass (Da):80,866
Checksum:iB3C8896A9619917B
GO
Isoform 3 (identifier: Q96AV8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     772-787: Missing.

Note: No experimental confirmation available.
Show »
Length:895
Mass (Da):98,352
Checksum:i8731DF9891154110
GO

Sequence cautioni

The sequence BAG53257.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG53510.1 differs from that shown. Reason: Frameshift at position 229. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721F → L.2 Publications
Corresponds to variant rs310791 [ dbSNP | Ensembl ].
VAR_034732
Natural varianti626 – 6261M → V.
Corresponds to variant rs3829295 [ dbSNP | Ensembl ].
VAR_034733
Natural varianti854 – 8541H → Q.
Corresponds to variant rs310831 [ dbSNP | Ensembl ].
VAR_034734

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei714 – 845132GLNGF…PVYVG → VTSSSDPQEHPTHTS in isoform 2. 1 PublicationVSP_027473Add
BLAST
Alternative sequencei772 – 78716Missing in isoform 3. 1 PublicationVSP_044617Add
BLAST
Alternative sequencei846 – 91166Missing in isoform 2. 1 PublicationVSP_027474Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK096316 mRNA. Translation: BAG53257.1. Different initiation.
CCDSiCCDS9016.1. [Q96AV8-1]
RefSeqiNP_976328.2. NM_203394.2. [Q96AV8-1]
UniGeneiHs.416375.

Genome annotation databases

EnsembliENST00000322886; ENSP00000323246; ENSG00000165891. [Q96AV8-1]
ENST00000416496; ENSP00000393639; ENSG00000165891. [Q96AV8-2]
GeneIDi144455.
KEGGihsa:144455.
UCSCiuc001sym.5. human. [Q96AV8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK096316 mRNA. Translation: BAG53257.1. Different initiation.
CCDSiCCDS9016.1. [Q96AV8-1]
RefSeqiNP_976328.2. NM_203394.2. [Q96AV8-1]
UniGeneiHs.416375.

3D structure databases

ProteinModelPortaliQ96AV8.
SMRiQ96AV8. Positions 141-209.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126855. 8 interactions.
IntActiQ96AV8. 3 interactions.
MINTiMINT-6541592.
STRINGi9606.ENSP00000323246.

PTM databases

iPTMnetiQ96AV8.
PhosphoSiteiQ96AV8.

Polymorphism and mutation databases

BioMutaiE2F7.
DMDMi311033456.

Proteomic databases

MaxQBiQ96AV8.
PaxDbiQ96AV8.
PRIDEiQ96AV8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322886; ENSP00000323246; ENSG00000165891. [Q96AV8-1]
ENST00000416496; ENSP00000393639; ENSG00000165891. [Q96AV8-2]
GeneIDi144455.
KEGGihsa:144455.
UCSCiuc001sym.5. human. [Q96AV8-1]

Organism-specific databases

CTDi144455.
GeneCardsiE2F7.
H-InvDBHIX0010843.
HGNCiHGNC:23820. E2F7.
MIMi612046. gene.
neXtProtiNX_Q96AV8.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2578. Eukaryota.
ENOG4111IGY. LUCA.
GeneTreeiENSGT00530000063616.
HOGENOMiHOG000013193.
HOVERGENiHBG063270.
InParanoidiQ96AV8.
KOiK09391.
OMAiSLVMPKK.
OrthoDBiEOG7HHWSG.
PhylomeDBiQ96AV8.
TreeFamiTF105567.

Miscellaneous databases

ChiTaRSiE2F7. human.
GeneWikiiE2F7.
GenomeRNAii144455.
NextBioi35469993.
PROiQ96AV8.
SOURCEiSearch...

Gene expression databases

BgeeiQ96AV8.
CleanExiHS_E2F7.
ExpressionAtlasiQ96AV8. baseline and differential.
GenevisibleiQ96AV8. HS.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR015633. E2F.
IPR003316. E2F_WHTH_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 3 hits.
PfamiPF02319. E2F_TDP. 2 hits.
[Graphical view]
SMARTiSM01372. E2F_TDP. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-911 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 504-911 (ISOFORM 3), 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  7. Cited for: FUNCTION, INDUCTION, SUBUNIT, MUTAGENESIS OF ARG-185 AND ARG-334.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "E2F7 and E2F8 promote angiogenesis through transcriptional activation of VEGFA in cooperation with HIF1."
    Weijts B.G., Bakker W.J., Cornelissen P.W., Liang K.H., Schaftenaar F.H., Westendorp B., de Wolf C.A., Paciejewska M., Scheele C.L., Kent L., Leone G., Schulte-Merker S., de Bruin A.
    EMBO J. 31:3871-3884(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIF1A.
  11. "E2F7 can regulate proliferation, differentiation, and apoptotic responses in human keratinocytes: implications for cutaneous squamous cell carcinoma formation."
    Endo-Munoz L., Dahler A., Teakle N., Rickwood D., Hazar-Rethinam M., Abdul-Jabbar I., Sommerville S., Dickinson I., Kaur P., Paquet-Fifield S., Saunders N.
    Cancer Res. 69:1800-1808(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Loss of E2F7 expression is an early event in squamous differentiation and causes derepression of the key differentiation activator Sp1."
    Hazar-Rethinam M., Cameron S.R., Dahler A.L., Endo-Munoz L.B., Smith L., Rickwood D., Saunders N.A.
    J. Invest. Dermatol. 131:1077-1084(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "E2F7, a novel target, is up-regulated by p53 and mediates DNA damage-dependent transcriptional repression."
    Carvajal L.A., Hamard P.J., Tonnessen C., Manfredi J.J.
    Genes Dev. 26:1533-1545(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  14. "The atypical E2F family member E2F7 couples the p53 and RB pathways during cellular senescence."
    Aksoy O., Chicas A., Zeng T., Zhao Z., McCurrach M., Wang X., Lowe S.W.
    Genes Dev. 26:1546-1557(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.

Entry informationi

Entry nameiE2F7_HUMAN
AccessioniPrimary (citable) accession number: Q96AV8
Secondary accession number(s): A6NC74
, B2RMR7, B3KTZ5, B3KUP8, B5MED9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: November 2, 2010
Last modified: May 11, 2016
This is version 107 of the entry and version 3 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 12
    Human chromosome 12: 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

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 one 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.