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Q66K89

- E4F1_HUMAN

UniProt

Q66K89 - E4F1_HUMAN

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Protein

Transcription factor E4F1

Gene

E4F1

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

Functioni

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.
Identified as a cellular target of the adenoviral oncoprotein E1A, it is required for both transcriptional activation and repression of viral genes.

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri192 – 21423C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri220 – 24223C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri248 – 27225C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri435 – 45723C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri463 – 48523C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri491 – 51323C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri519 – 54123C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri547 – 56923C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri575 – 59723C2H2-type 9; degeneratePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. cAMP response element binding Source: UniProtKB
  2. DNA binding Source: ProtInc
  3. ligase activity Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
  5. RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  6. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
  7. sequence-specific DNA binding transcription factor activity Source: ProtInc
  8. transcription coactivator activity Source: ProtInc
  9. transcription corepressor activity Source: ProtInc

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. DNA replication Source: Ensembl
  3. mitotic cell cycle arrest Source: UniProtKB
  4. mitotic nuclear division Source: UniProtKB-KW
  5. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  6. protein ubiquitination Source: UniProtKB-UniPathway
  7. regulation of cell cycle process Source: UniProtKB
  8. regulation of growth Source: UniProtKB-KW
  9. regulation of mitotic cell cycle, embryonic Source: Ensembl
  10. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Cell cycle, Cell division, Growth regulation, Host-virus interaction, Mitosis, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ66K89.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:E4F1
Synonyms:E4F
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:3121. E4F1.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: HPA
  3. spindle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi194 – 1941C → S: Increases DNA-binding; when associated with S-197. 1 Publication
Mutagenesisi197 – 1971C → S: Increases DNA-binding; when associated with S-194. 1 Publication
Mutagenesisi210 – 2101H → A: Alters DNA-binding. 1 Publication
Mutagenesisi237 – 2371R → L: Alters DNA-binding; when associated with N-238. 1 Publication
Mutagenesisi238 – 2381H → N: Alters DNA-binding; when associated with L-237. 1 Publication
Mutagenesisi249 – 2491K → M: Alters DNA-binding; when associated with S-250. 1 Publication
Mutagenesisi250 – 2501C → S: Alters DNA-binding; when associated with M-249. 1 Publication

Organism-specific databases

PharmGKBiPA27579.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 784784Transcription factor E4F1PRO_0000324307Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501Phosphoserine2 Publications

Post-translational modificationi

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.1 Publication
Phosphorylated; p120E4F and p50E4F are both phosphorylated. Phosphorylation is cell cycle-dependent and differentially regulates DNA-binding activity and function of both forms.4 Publications
May be sumoylated by UBE2I upon interaction with CDKN2A.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ66K89.
PaxDbiQ66K89.
PRIDEiQ66K89.

PTM databases

PhosphoSiteiQ66K89.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Developmental stagei

Expressed in a variety of fetal tissues.1 Publication

Inductioni

Up-regulated by estrogen.1 Publication

Gene expression databases

BgeeiQ66K89.
CleanExiHS_E4F1.
ExpressionAtlasiQ66K89. baseline.
GenevestigatoriQ66K89.

Organism-specific databases

HPAiHPA052042.

Interactioni

Subunit structurei

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.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
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.

Protein-protein interaction databases

BioGridi108209. 12 interactions.
IntActiQ66K89. 11 interactions.
MINTiMINT-137139.
STRINGi9606.ENSP00000301727.

Structurei

3D structure databases

ProteinModelPortaliQ66K89.
SMRiQ66K89. Positions 192-269, 433-599.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 8545Required for ubiquitin ligase activityAdd
BLAST
Regioni184 – 26380Mediates dimerization, DNA-binding, transcription repression of CCNA2 and interaction with HMGA2Add
BLAST
Regioni369 – 566198Mediates interaction with CDKN2AAdd
BLAST
Regioni435 – 599165Interaction with BMI1Add
BLAST
Regioni521 – 58060Mediates interaction with TP53Add
BLAST
Regioni575 – 59723Mediates interaction with RASSF1Add
BLAST

Sequence similaritiesi

Contains 9 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri192 – 21423C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri220 – 24223C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri248 – 27225C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri435 – 45723C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri463 – 48523C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri491 – 51323C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri519 – 54123C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri547 – 56923C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri575 – 59723C2H2-type 9; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00390000006768.
HOGENOMiHOG000168447.
HOVERGENiHBG052707.
InParanoidiQ66K89.
OMAiCQFCSRG.
OrthoDBiEOG761BT6.
PhylomeDBiQ66K89.
TreeFamiTF315387.

Family and domain databases

Gene3Di3.30.160.60. 9 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 10 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q66K89-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEGAMAVRVT AAHTAEAQAE AGREAGEGAV AAVAAALAPS GFLGLPAPFS
60 70 80 90 100
EEDEDDVHRC GRCQAEFTAL EDFVQHKIQK ACQRAPPEAL PATPATTALL
110 120 130 140 150
GQEVVPAAPG PEEPITVAHI VVEAASLAAD ISHASDLVGG GHIKEVIVAA
160 170 180 190 200
EAELGDGEMA EAPGSPRQQG LGLAGEGEQA QVKLLVNKDG RYVCALCHKT
210 220 230 240 250
FKTGSILKAH MVTHSSRKDH ECKLCGASFR TKGSLIRHHR RHTDERPYKC
260 270 280 290 300
SKCGKSFRES GALTRHLKSL TPCTEKIRFS VSKDVVVSKE DARAGSGAGA
310 320 330 340 350
AGLGTATSSV TGEPIETSPV IHLVTDAKGT VIHEVHVQMQ ELSLGMKALA
360 370 380 390 400
PEPPVSQELP CSSEGSRENL LHQAMQNSGI VLERAAGEEG ALEPAPAAGS
410 420 430 440 450
SPQPLAVAAP QLPVLEVQPL ETQVASEASA VPRTHPCPQC SETFPTAATL
460 470 480 490 500
EAHKRGHTGP RPFACAQCGK AFPKAYLLKK HQEVHVRERR FRCGDCGKLY
510 520 530 540 550
KTIAHVRGHR RVHSDERPYP CPKCGKRYKT KNAQQVHFRT HLEEKPHVCQ
560 570 580 590 600
FCSRGFREKG SLVRHVRHHT GEKPFKCYKC GRGFAEHGTL NRHLRTKGGC
610 620 630 640 650
LLEVEELLVS EDSPAAATTV LTEDPHTVLV EFSSVVADTQ EYIIEATADD
660 670 680 690 700
AETSEATEII EGTQTEVDSH IMKVVQQIVH QASAGHQIIV QNVTMDEETA
710 720 730 740 750
LGPEAAAADT ITIATPESLT EQVAMTLASA ISEGTVLAAR AGTSGTEQAT
760 770 780
VTMVSSEDIE ILEHAGELVI ASPEGQLEVQ TVIV
Length:784
Mass (Da):83,496
Last modified:May 18, 2010 - v2
Checksum:i60F6E711F2748FD8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41A → E in AAD09139. (PubMed:9121437)Curated
Sequence conflicti363 – 3642SE → RK in AAD09139. (PubMed:9121437)Curated
Sequence conflicti425 – 4251A → V in BAF83018. (PubMed:14702039)Curated
Sequence conflicti480 – 4812KH → TD in AAD09139. (PubMed:9121437)Curated
Sequence conflicti544 – 5441E → D in BAF83018. (PubMed:14702039)Curated
Sequence conflicti681 – 6822QA → PR in AAD09139. (PubMed:9121437)Curated
Sequence conflicti704 – 7052EA → RG in AAD09139. (PubMed:9121437)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671R → H.4 Publications
Corresponds to variant rs26839 [ dbSNP | Ensembl ].
VAR_060270
Natural varianti355 – 3551V → I.
Corresponds to variant rs59784157 [ dbSNP | Ensembl ].
VAR_060271

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS32370.1.
RefSeqiNP_001275705.1. NM_001288776.1.
NP_001275707.1. NM_001288778.1.
NP_004415.3. NM_004424.4.
UniGeneiHs.513268.

Genome annotation databases

EnsembliENST00000301727; ENSP00000301727; ENSG00000167967.
GeneIDi1877.
KEGGihsa:1877.
UCSCiuc002cpm.3. human.

Polymorphism databases

DMDMi296434488.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS32370.1.
RefSeqi NP_001275705.1. NM_001288776.1.
NP_001275707.1. NM_001288778.1.
NP_004415.3. NM_004424.4.
UniGenei Hs.513268.

3D structure databases

ProteinModelPortali Q66K89.
SMRi Q66K89. Positions 192-269, 433-599.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108209. 12 interactions.
IntActi Q66K89. 11 interactions.
MINTi MINT-137139.
STRINGi 9606.ENSP00000301727.

PTM databases

PhosphoSitei Q66K89.

Polymorphism databases

DMDMi 296434488.

Proteomic databases

MaxQBi Q66K89.
PaxDbi Q66K89.
PRIDEi Q66K89.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301727 ; ENSP00000301727 ; ENSG00000167967 .
GeneIDi 1877.
KEGGi hsa:1877.
UCSCi uc002cpm.3. human.

Organism-specific databases

CTDi 1877.
GeneCardsi GC16P002276.
HGNCi HGNC:3121. E4F1.
HPAi HPA052042.
MIMi 603022. gene.
neXtProti NX_Q66K89.
PharmGKBi PA27579.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5048.
GeneTreei ENSGT00390000006768.
HOGENOMi HOG000168447.
HOVERGENi HBG052707.
InParanoidi Q66K89.
OMAi CQFCSRG.
OrthoDBi EOG761BT6.
PhylomeDBi Q66K89.
TreeFami TF315387.

Enzyme and pathway databases

UniPathwayi UPA00143 .
SignaLinki Q66K89.

Miscellaneous databases

GeneWikii E4F1.
GenomeRNAii 1877.
NextBioi 7679.
PROi Q66K89.
SOURCEi Search...

Gene expression databases

Bgeei Q66K89.
CleanExi HS_E4F1.
ExpressionAtlasi Q66K89. baseline.
Genevestigatori Q66K89.

Family and domain databases

Gene3Di 3.30.160.60. 9 hits.
InterProi IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view ]
Pfami PF00096. zf-C2H2. 1 hit.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 10 hits.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 9 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiE4F1_HUMAN
AccessioniPrimary (citable) accession number: Q66K89
Secondary accession number(s): A8K2R4, O00146
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 112 of the entry and version 2 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 16
    Human chromosome 16: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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