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Transcription factor E4F1 (EC 2.3.2.27) (E4F transcription factor 1) (Putative E3 ubiquitin-protein ligase E4F1) (RING-type E3 ubiquitin transferase E4F1) (Transcription factor E4F) (Transcription factor phi AP3) (p120E4F)

 E4F1_MOUSE              Reviewed;         783 AA.
Q8CCE9; Q05BH7; Q3UNJ9; Q62065; Q6IR08; Q6PGI1; Q9QY56;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 2.
12-SEP-2018, entry version 142.
RecName: Full=Transcription factor E4F1;
EC=2.3.2.27 {ECO:0000250|UniProtKB:Q66K89};
AltName: Full=E4F transcription factor 1;
AltName: Full=Putative E3 ubiquitin-protein ligase E4F1;
AltName: Full=RING-type E3 ubiquitin transferase E4F1 {ECO:0000305};
AltName: Full=Transcription factor E4F;
AltName: Full=Transcription factor phi AP3;
AltName: Full=p120E4F;
Name=E4f1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Lebedeva T.V., Singh A.K.;
"Repression of the murine Il-1 beta expression by the murine analog of
E4F transcription factor.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 14-783 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryonic testis;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-783 (ISOFORM 5).
STRAIN=C57BL/6J, FVB/N, and NMRI; TISSUE=Brain, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 65-783 (ISOFORM 1), FUNCTION,
DNA-BINDING, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND TISSUE
SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=8262041;
Fognani C., Della Valle G., Babiss L.E.;
"Repression of adenovirus E1A enhancer activity by a novel zinc
finger-containing DNA-binding protein related to the GLI-Kruppel
protein.";
EMBO J. 12:4985-4992(1993).
[5]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9530632; DOI=10.1007/s003359900758;
Rooney R.J., Daniels R.R., Jenkins N.A., Gilbert D.J., Rothammer K.,
Morris S.W., Higgs D.R., Copeland N.G.;
"Chromosomal location and tissue expression of the gene encoding the
adenovirus E1A-regulated transcription factor E4F in humans and
mice.";
Mamm. Genome 9:320-323(1998).
[6]
FUNCTION, AND INTERACTION WITH TP53.
PubMed=10644996; DOI=10.1038/sj.onc.1203250;
Sandy P., Gostissa M., Fogal V., Cecco L.D., Szalay K., Rooney R.J.,
Schneider C., Del Sal G.;
"p53 is involved in the p120E4F-mediated growth arrest.";
Oncogene 19:188-199(2000).
[7]
INTERACTION WITH RB1.
PubMed=10869426; DOI=10.1073/pnas.130198397;
Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E.,
Medema R., Vignais M.-L., Sardet C.;
"pRB binds to and modulates the transrepressing activity of the E1A-
regulated transcription factor p120E4F.";
Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000).
[8]
DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15226446; DOI=10.1128/MCB.24.14.6467-6475.2004;
Le Cam L., Lacroix M., Ciemerych M.A., Sardet C., Sicinski P.;
"The E4F protein is required for mitotic progression during embryonic
cell cycles.";
Mol. Cell. Biol. 24:6467-6475(2004).
[9]
FUNCTION, AND INTERACTION WITH ANP32A.
PubMed=17557114; DOI=10.1038/sj.embor.7400983;
Cvetanovic M., Rooney R.J., Garcia J.J., Toporovskaya N., Zoghbi H.Y.,
Opal P.;
"The role of LANP and ataxin 1 in E4F-mediated transcriptional
repression.";
EMBO Rep. 8:671-677(2007).
-!- 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. {ECO:0000269|PubMed:10644996,
ECO:0000269|PubMed:15226446, ECO:0000269|PubMed:17557114,
ECO:0000269|PubMed:8262041}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000250|UniProtKB:Q66K89}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: 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.
{ECO:0000250|UniProtKB:Q66K89, ECO:0000269|PubMed:10644996,
ECO:0000269|PubMed:10869426, ECO:0000269|PubMed:17557114}.
-!- INTERACTION:
O35381:Anp32a; NbExp=2; IntAct=EBI-7450874, EBI-643140;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:15226446, ECO:0000269|PubMed:8262041}.
Cytoplasm {ECO:0000250}. 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. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q8CCE9-1; Sequence=Displayed;
Name=2;
IsoId=Q8CCE9-2; Sequence=VSP_032196, VSP_032197;
Name=3;
IsoId=Q8CCE9-3; Sequence=VSP_032193;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q8CCE9-4; Sequence=VSP_032194, VSP_032195;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q8CCE9-5; Sequence=VSP_032192;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:8262041, ECO:0000269|PubMed:9530632}.
-!- DEVELOPMENTAL STAGE: Continuously expressed during embryogenesis.
{ECO:0000269|PubMed:9530632}.
-!- PTM: Phosphorylated; phosphorylation is cell cycle-dependent and
regulates DNA-binding activity and function.
{ECO:0000269|PubMed:8262041}.
-!- PTM: May be sumoylated by UBE2I upon interaction with CDKN2A.
{ECO:0000250|UniProtKB:Q66K89}.
-!- DISRUPTION PHENOTYPE: Death before E7.5 probably at the peri-
implantation stage. Blastocysts display defects in mitotic
progression and chromosomal segregation and increased apoptosis.
{ECO:0000269|PubMed:15226446}.
-!- SEQUENCE CAUTION:
Sequence=AAF22563.1; Type=Frameshift; Positions=230, 235; Evidence={ECO:0000305};
Sequence=AAH71228.1; Type=Frameshift; Positions=94; Evidence={ECO:0000305};
Sequence=BAE25748.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA54188.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF126967; AAF22563.1; ALT_FRAME; mRNA.
EMBL; AK033285; BAC28222.1; -; mRNA.
EMBL; AK144176; BAE25748.1; ALT_INIT; mRNA.
EMBL; BC046459; AAH46459.1; -; mRNA.
EMBL; BC057011; AAH57011.1; -; mRNA.
EMBL; BC071228; AAH71228.1; ALT_FRAME; mRNA.
EMBL; X76858; CAA54188.1; ALT_INIT; mRNA.
CCDS; CCDS28481.1; -. [Q8CCE9-3]
PIR; S41688; S41688.
RefSeq; NP_001288713.1; NM_001301784.1. [Q8CCE9-1]
RefSeq; NP_031919.2; NM_007893.4. [Q8CCE9-3]
RefSeq; XP_011244570.1; XM_011246268.2. [Q8CCE9-5]
UniGene; Mm.163132; -.
UniGene; Mm.445985; -.
ProteinModelPortal; Q8CCE9; -.
SMR; Q8CCE9; -.
BioGrid; 199353; 4.
IntAct; Q8CCE9; 1.
MINT; Q8CCE9; -.
STRING; 10090.ENSMUSP00000062344; -.
iPTMnet; Q8CCE9; -.
PhosphoSitePlus; Q8CCE9; -.
PaxDb; Q8CCE9; -.
PRIDE; Q8CCE9; -.
Ensembl; ENSMUST00000056032; ENSMUSP00000062344; ENSMUSG00000024137. [Q8CCE9-3]
Ensembl; ENSMUST00000226941; ENSMUSP00000154444; ENSMUSG00000024137. [Q8CCE9-2]
GeneID; 13560; -.
KEGG; mmu:13560; -.
UCSC; uc008avy.2; mouse. [Q8CCE9-3]
UCSC; uc008awa.2; mouse. [Q8CCE9-1]
UCSC; uc008awb.2; mouse. [Q8CCE9-2]
UCSC; uc012ami.2; mouse. [Q8CCE9-5]
CTD; 1877; -.
MGI; MGI:109530; E4f1.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00840000129970; -.
HOVERGEN; HBG052707; -.
InParanoid; Q8CCE9; -.
KO; K22401; -.
OMA; SGHQIIV; -.
OrthoDB; EOG091G03X5; -.
PhylomeDB; Q8CCE9; -.
TreeFam; TF315387; -.
UniPathway; UPA00143; -.
PRO; PR:Q8CCE9; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024137; Expressed in 302 organ(s), highest expression level in head.
CleanEx; MM_E4F1; -.
Genevisible; Q8CCE9; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005819; C:spindle; IDA:MGI.
GO; GO:0035497; F:cAMP response element binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0010564; P:regulation of cell cycle process; IDA:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 10.
SUPFAM; SSF57667; SSF57667; 6.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Complete proteome;
Cytoplasm; DNA-binding; Growth regulation; Metal-binding; Mitosis;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 783 Transcription factor E4F1.
/FTId=PRO_0000324308.
ZN_FING 193 215 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 221 243 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 249 273 C2H2-type 3; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 434 456 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 462 484 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 490 512 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 518 540 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 546 568 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 574 596 C2H2-type 9; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
REGION 40 84 Required for ubiquitin ligase activity.
{ECO:0000250}.
REGION 185 264 Mediates dimerization, DNA-binding,
transcription repression of CCNA2 and
interaction with HMGA2. {ECO:0000250}.
REGION 368 565 Mediates interaction with CDKN2A.
{ECO:0000250}.
REGION 434 598 Interaction with BMI1. {ECO:0000250}.
REGION 520 579 Mediates interaction with TP53.
{ECO:0000250}.
REGION 574 596 Mediates interaction with RASSF1.
{ECO:0000250}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000250|UniProtKB:Q66K89}.
VAR_SEQ 244 274 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_032192.
VAR_SEQ 422 422 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_032193.
VAR_SEQ 458 458 A -> VWQGLPQSLPAQEAPGGARARAPLPLWRLWEALQDH
RSCAGPPACSLRREAFPLSPVRQALQNQECPASTLPDTSGR
KAPRVPVLQPRLPGEGLSGAACEAPHRRETFQVLQVWPWLR
GAWHTQPAPAH (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_032194.
VAR_SEQ 459 783 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_032195.
VAR_SEQ 667 684 DSHIMKVVQQIVHQAGAG -> RVWVRDGRITGLLGSPSG
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_032196.
VAR_SEQ 685 783 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_032197.
CONFLICT 13 13 H -> D (in Ref. 2; BAE25748).
{ECO:0000305}.
CONFLICT 18 18 R -> G (in Ref. 1; AAF22563, 2; BAE25748
and 3; AAH46459/AAH71228). {ECO:0000305}.
CONFLICT 30 30 V -> VA (in Ref. 1; AAF22563 and 2;
BAE25748). {ECO:0000305}.
CONFLICT 62 62 C -> F (in Ref. 2; BAE25748).
{ECO:0000305}.
CONFLICT 139 139 V -> A (in Ref. 4; CAA54188).
{ECO:0000305}.
CONFLICT 148 148 I -> V (in Ref. 4; CAA54188).
{ECO:0000305}.
CONFLICT 158 158 V -> G (in Ref. 1; AAF22563, 2; BAE25748,
3; AAH46459/AAH71228 and 4; CAA54188).
{ECO:0000305}.
CONFLICT 224 225 KL -> NF (in Ref. 1; AAF22563).
{ECO:0000305}.
CONFLICT 281 281 S -> N (in Ref. 1; AAF22563 and 2;
BAE25748). {ECO:0000305}.
CONFLICT 380 380 V -> L (in Ref. 1; AAF22563).
{ECO:0000305}.
CONFLICT 390 390 A -> V (in Ref. 1; AAF22563).
{ECO:0000305}.
CONFLICT 395 400 PPSGSS -> LPFGST (in Ref. 1; AAF22563).
{ECO:0000305}.
CONFLICT 412 412 P -> L (in Ref. 1; AAF22563).
{ECO:0000305}.
CONFLICT 479 480 KH -> ND (in Ref. 4; CAA54188).
{ECO:0000305}.
CONFLICT 585 586 EH -> DD (in Ref. 4; CAA54188).
{ECO:0000305}.
CONFLICT 630 630 E -> Q (in Ref. 1; AAF22563, 2; BAE25748,
3; AAH46459 and 4; CAA54188).
{ECO:0000305}.
CONFLICT 705 705 T -> A (in Ref. 1; AAF22563, 2; BAE25748
and 4; CAA54188). {ECO:0000305}.
SEQUENCE 783 AA; 84296 MW; 59E47F7A64A224A4 CRC64;
MEGAMAVRVT AAHTAEARAE AGREAGEGGV AAAAALSSGG FLGLPAPFSE EDEDDVHRCG
RCQVEFTALE DFVQHKIQKT CHRAPQEALP TTPAATALLD QEVVPTAAEG GPDEPITVAH
IVVEATSLAE DISHAPDLVG SGHIKEVIVA AEAEPGDVEM AEAPGSPNHQ ELGLLGEGEQ
AHVKLLVNKE GRYVCMLCHK TFKTGSILKA HMVTHSSRKD HECKLCGASF RTKGSLIRHH
RRHTDERPYK CAKCGKSFRE SGALTRHLKS LTPCTEKIRF SISKDTAVGK EEVPAGSSAS
TVGTVTSSVA GDPMETSPVI HLVTDAKGTV IHEVHVQMQE LPLGMKALTP ESPDSEELPC
SSENSRENLL HQAMQNSGIV LERVAGEESA LEPAPPSGSS PQCLGDGSPE LPLLKVEQIE
TQVASEAATV PRTHPCPQCS ETFPTAATLE AHKRGHIAPR PFTCTQCGKA FPKAYLLKKH
QEVHVHERRF RCGDCGKLYK TIAHVRGHRR VHSDERPFPC PQCGKRYKTK NAQQVHFRTH
LEEKPHVCQF CSRGFREKGS LVRHVRHHTG EKPFKCYKCG RGFAEHGTLN RHLRTKGGCL
LEVEELLVSE ESPSAAATVL AEDPHTVLVE FSSVVADTQE YIIEATADDT ETSEATEIIE
GTQTEVDSHI MKVVQQIVHQ AGAGHQIIVQ NVTMDQETAL GSEATAADTI TIATPESLTE
QVAMTLASAI SEGTVLTARA GPNSTEQATV TMVSSEDIEI LEHGGELVIA SPEGQLEVQT
VIV


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CSB-EL007350MO Mouse E4F transcription factor 1 (E4F1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
31-248 Transcription initiation factor IIA . and . chains (GTranscription Factor Antibodies2A1, Transcription Factor AntibodiesIIA p35 and p19 subunits, Transcription Factor AntibodiesIIAL) binding ability o 0.05 mg
18-003-43070 T-box transcription factor TBX21 - T-box protein 21; Transcription factor TBLYM; T-cell-specific T-box transcription factor T-bet Polyclonal 0.1 mg Protein A
18-003-42234 POU domain. class 2. transcription factor 3 - Octamer-binding transcription factor 11; Oct-11; Transcription factor Skn-1; PLA-1 protein Polyclonal 0.1 mg Protein A
18-003-42234 POU domain. class 2. transcription factor 3 - Octamer-binding transcription factor 11; Oct-11; Transcription factor Skn-1; PLA-1 protein Polyclonal 0.05 mg Aff Pur
18-003-42235 POU domain. class 2. transcription factor 3 - Octamer-binding transcription factor 11; Oct-11; Transcription factor Skn-1; PLA-1 protein Polyclonal 0.1 mg Protein A
18-003-42235 POU domain. class 2. transcription factor 3 - Octamer-binding transcription factor 11; Oct-11; Transcription factor Skn-1; PLA-1 protein Polyclonal 0.05 mg Aff Pur
E1346h ELISA Activating transcription factor 1,ATF1,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1,Homo sapiens,Human,Protein TREB36 96T
E1346h ELISA kit Activating transcription factor 1,ATF1,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1,Homo sapiens,Human,Protein TREB36 96T


 

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