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Q8CCE9

- E4F1_MOUSE

UniProt

Q8CCE9 - E4F1_MOUSE

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Protein

Transcription factor E4F1

Gene

E4f1

Organism
Mus musculus (Mouse)
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.4 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri193 – 21523C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri221 – 24323C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri249 – 27325C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri434 – 45623C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri462 – 48423C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri490 – 51223C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri518 – 54023C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri546 – 56823C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri574 – 59623C2H2-type 9; degeneratePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. cAMP response element binding Source: Ensembl
  2. DNA binding Source: MGI
  3. ligase activity Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
  5. RNA polymerase II regulatory region sequence-specific DNA binding Source: Ensembl

GO - Biological processi

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

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Cell cycle, Cell division, Growth regulation, Mitosis, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

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
Transcription factor phi AP3
p120E4F
Gene namesi
Name:E4f1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:109530. E4f1.

Subcellular locationi

Nucleusnucleoplasm 2 Publications. 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.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Death before E7.5 probably at the peri-implantation stage. Blastocysts display defects in mitotic progression and chromosomal segregation and increased apoptosis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 783783Transcription factor E4F1PRO_0000324308Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated; phosphorylation is cell cycle-dependent and regulates DNA-binding activity and function.1 Publication
May be sumoylated by UBE2I upon interaction with CDKN2A.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ8CCE9.

PTM databases

PhosphoSiteiQ8CCE9.

Expressioni

Tissue specificityi

Ubiquitously expressed.2 Publications

Developmental stagei

Continuously expressed during embryogenesis.1 Publication

Gene expression databases

BgeeiQ8CCE9.
CleanExiMM_E4F1.
GenevestigatoriQ8CCE9.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Anp32aO353812EBI-7450874,EBI-643140

Protein-protein interaction databases

BioGridi199353. 2 interactions.
IntActiQ8CCE9. 1 interaction.
MINTiMINT-4979074.

Structurei

3D structure databases

ProteinModelPortaliQ8CCE9.
SMRiQ8CCE9. Positions 182-271, 443-595.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 8445Required for ubiquitin ligase activityBy similarityAdd
BLAST
Regioni185 – 26480Mediates dimerization, DNA-binding, transcription repression of CCNA2 and interaction with HMGA2By similarityAdd
BLAST
Regioni368 – 565198Mediates interaction with CDKN2ABy similarityAdd
BLAST
Regioni434 – 598165Interaction with BMI1By similarityAdd
BLAST
Regioni520 – 57960Mediates interaction with TP53By similarityAdd
BLAST
Regioni574 – 59623Mediates interaction with RASSF1By similarityAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri193 – 21523C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri221 – 24323C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri249 – 27325C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri434 – 45623C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri462 – 48423C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri490 – 51223C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri518 – 54023C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri546 – 56823C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri574 – 59623C2H2-type 9; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00390000006768.
HOVERGENiHBG052707.
InParanoidiQ8CCE9.
OMAiCQFCSRG.
OrthoDBiEOG761BT6.
PhylomeDBiQ8CCE9.
TreeFamiTF315387.

Family and domain databases

Gene3Di3.30.160.60. 8 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 2 hits.
[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]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8CCE9-1) [UniParc]FASTAAdd to Basket

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
MEGAMAVRVT AAHTAEARAE AGREAGEGGV AAAAALSSGG FLGLPAPFSE
60 70 80 90 100
EDEDDVHRCG RCQVEFTALE DFVQHKIQKT CHRAPQEALP TTPAATALLD
110 120 130 140 150
QEVVPTAAEG GPDEPITVAH IVVEATSLAE DISHAPDLVG SGHIKEVIVA
160 170 180 190 200
AEAEPGDVEM AEAPGSPNHQ ELGLLGEGEQ AHVKLLVNKE GRYVCMLCHK
210 220 230 240 250
TFKTGSILKA HMVTHSSRKD HECKLCGASF RTKGSLIRHH RRHTDERPYK
260 270 280 290 300
CAKCGKSFRE SGALTRHLKS LTPCTEKIRF SISKDTAVGK EEVPAGSSAS
310 320 330 340 350
TVGTVTSSVA GDPMETSPVI HLVTDAKGTV IHEVHVQMQE LPLGMKALTP
360 370 380 390 400
ESPDSEELPC SSENSRENLL HQAMQNSGIV LERVAGEESA LEPAPPSGSS
410 420 430 440 450
PQCLGDGSPE LPLLKVEQIE TQVASEAATV PRTHPCPQCS ETFPTAATLE
460 470 480 490 500
AHKRGHIAPR PFTCTQCGKA FPKAYLLKKH QEVHVHERRF RCGDCGKLYK
510 520 530 540 550
TIAHVRGHRR VHSDERPFPC PQCGKRYKTK NAQQVHFRTH LEEKPHVCQF
560 570 580 590 600
CSRGFREKGS LVRHVRHHTG EKPFKCYKCG RGFAEHGTLN RHLRTKGGCL
610 620 630 640 650
LEVEELLVSE ESPSAAATVL AEDPHTVLVE FSSVVADTQE YIIEATADDT
660 670 680 690 700
ETSEATEIIE GTQTEVDSHI MKVVQQIVHQ AGAGHQIIVQ NVTMDQETAL
710 720 730 740 750
GSEATAADTI TIATPESLTE QVAMTLASAI SEGTVLTARA GPNSTEQATV
760 770 780
TMVSSEDIEI LEHGGELVIA SPEGQLEVQT VIV
Length:783
Mass (Da):84,296
Last modified:March 18, 2008 - v2
Checksum:i59E47F7A64A224A4
GO
Isoform 2 (identifier: Q8CCE9-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:684
Mass (Da):74,060
Checksum:i62B9E2973ACA07C3
GO
Isoform 3 (identifier: Q8CCE9-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:782
Mass (Da):84,168
Checksum:iF0CEA4AC61FE5BDA
GO
Isoform 4 (identifier: Q8CCE9-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:586
Mass (Da):62,553
Checksum:i03DE21745C393119
GO
Isoform 5 (identifier: Q8CCE9-5) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:752
Mass (Da):80,830
Checksum:iBC7A27C32B98E325
GO

Sequence cautioni

The sequence AAF22563.1 differs from that shown. Reason: Frameshift at positions 230 and 235. Curated
The sequence AAH71228.1 differs from that shown. Reason: Frameshift at position 94. Curated
The sequence BAE25748.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA54188.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131H → D in BAE25748. (PubMed:16141072)Curated
Sequence conflicti18 – 181R → G in AAF22563. 1 PublicationCurated
Sequence conflicti18 – 181R → G in BAE25748. (PubMed:16141072)Curated
Sequence conflicti18 – 181R → G in AAH46459. (PubMed:15489334)Curated
Sequence conflicti18 – 181R → G in AAH71228. (PubMed:15489334)Curated
Sequence conflicti30 – 301V → VA in AAF22563. 1 PublicationCurated
Sequence conflicti30 – 301V → VA in BAE25748. (PubMed:16141072)Curated
Sequence conflicti62 – 621C → F in BAE25748. (PubMed:16141072)Curated
Sequence conflicti139 – 1391V → A in CAA54188. (PubMed:8262041)Curated
Sequence conflicti148 – 1481I → V in CAA54188. (PubMed:8262041)Curated
Sequence conflicti158 – 1581V → G in AAF22563. 1 PublicationCurated
Sequence conflicti158 – 1581V → G in BAE25748. (PubMed:16141072)Curated
Sequence conflicti158 – 1581V → G in AAH46459. (PubMed:15489334)Curated
Sequence conflicti158 – 1581V → G in AAH71228. (PubMed:15489334)Curated
Sequence conflicti158 – 1581V → G in CAA54188. (PubMed:8262041)Curated
Sequence conflicti224 – 2252KL → NF in AAF22563. 1 PublicationCurated
Sequence conflicti281 – 2811S → N in AAF22563. 1 PublicationCurated
Sequence conflicti281 – 2811S → N in BAE25748. (PubMed:16141072)Curated
Sequence conflicti380 – 3801V → L in AAF22563. 1 PublicationCurated
Sequence conflicti390 – 3901A → V in AAF22563. 1 PublicationCurated
Sequence conflicti395 – 4006PPSGSS → LPFGST in AAF22563. 1 PublicationCurated
Sequence conflicti412 – 4121P → L in AAF22563. 1 PublicationCurated
Sequence conflicti479 – 4802KH → ND in CAA54188. (PubMed:8262041)Curated
Sequence conflicti585 – 5862EH → DD in CAA54188. (PubMed:8262041)Curated
Sequence conflicti630 – 6301E → Q in AAF22563. 1 PublicationCurated
Sequence conflicti630 – 6301E → Q in BAE25748. (PubMed:16141072)Curated
Sequence conflicti630 – 6301E → Q in AAH46459. (PubMed:15489334)Curated
Sequence conflicti630 – 6301E → Q in CAA54188. (PubMed:8262041)Curated
Sequence conflicti705 – 7051T → A in AAF22563. 1 PublicationCurated
Sequence conflicti705 – 7051T → A in BAE25748. (PubMed:16141072)Curated
Sequence conflicti705 – 7051T → A in CAA54188. (PubMed:8262041)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei244 – 27431Missing in isoform 5. 1 PublicationVSP_032192Add
BLAST
Alternative sequencei422 – 4221Missing in isoform 3. 1 PublicationVSP_032193
Alternative sequencei458 – 4581A → VWQGLPQSLPAQEAPGGARA RAPLPLWRLWEALQDHRSCA GPPACSLRREAFPLSPVRQA LQNQECPASTLPDTSGRKAP RVPVLQPRLPGEGLSGAACE APHRRETFQVLQVWPWLRGA WHTQPAPAH in isoform 4. 1 PublicationVSP_032194
Alternative sequencei459 – 783325Missing in isoform 4. 1 PublicationVSP_032195Add
BLAST
Alternative sequencei667 – 68418DSHIM…QAGAG → RVWVRDGRITGLLGSPSG in isoform 2. 1 PublicationVSP_032196Add
BLAST
Alternative sequencei685 – 78399Missing in isoform 2. 1 PublicationVSP_032197Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS28481.1. [Q8CCE9-3]
PIRiS41688.
RefSeqiNP_031919.2. NM_007893.4. [Q8CCE9-3]
UniGeneiMm.163132.

Genome annotation databases

EnsembliENSMUST00000056032; ENSMUSP00000062344; ENSMUSG00000024137. [Q8CCE9-3]
GeneIDi13560.
KEGGimmu:13560.
UCSCiuc008avy.1. mouse. [Q8CCE9-3]
uc008awa.1. mouse. [Q8CCE9-1]
uc008awb.1. mouse. [Q8CCE9-2]
uc012ami.1. mouse. [Q8CCE9-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS28481.1. [Q8CCE9-3 ]
PIRi S41688.
RefSeqi NP_031919.2. NM_007893.4. [Q8CCE9-3 ]
UniGenei Mm.163132.

3D structure databases

ProteinModelPortali Q8CCE9.
SMRi Q8CCE9. Positions 182-271, 443-595.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199353. 2 interactions.
IntActi Q8CCE9. 1 interaction.
MINTi MINT-4979074.

PTM databases

PhosphoSitei Q8CCE9.

Proteomic databases

PRIDEi Q8CCE9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000056032 ; ENSMUSP00000062344 ; ENSMUSG00000024137 . [Q8CCE9-3 ]
GeneIDi 13560.
KEGGi mmu:13560.
UCSCi uc008avy.1. mouse. [Q8CCE9-3 ]
uc008awa.1. mouse. [Q8CCE9-1 ]
uc008awb.1. mouse. [Q8CCE9-2 ]
uc012ami.1. mouse. [Q8CCE9-5 ]

Organism-specific databases

CTDi 1877.
MGIi MGI:109530. E4f1.

Phylogenomic databases

eggNOGi COG5048.
GeneTreei ENSGT00390000006768.
HOVERGENi HBG052707.
InParanoidi Q8CCE9.
OMAi CQFCSRG.
OrthoDBi EOG761BT6.
PhylomeDBi Q8CCE9.
TreeFami TF315387.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

NextBioi 284182.
PROi Q8CCE9.
SOURCEi Search...

Gene expression databases

Bgeei Q8CCE9.
CleanExi MM_E4F1.
Genevestigatori Q8CCE9.

Family and domain databases

Gene3Di 3.30.160.60. 8 hits.
InterProi IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view ]
Pfami PF00096. zf-C2H2. 2 hits.
[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. "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. 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.

Entry informationi

Entry nameiE4F1_MOUSE
AccessioniPrimary (citable) accession number: Q8CCE9
Secondary accession number(s): Q05BH7
, Q3UNJ9, Q62065, Q6IR08, Q6PGI1, Q9QY56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: November 26, 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

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3