GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Transcription factor E2-alpha (Immunoglobulin enhancer-binding factor E12/E47) (Transcription factor 3) (TCF-3) (Transcription factor A1)

 TFE2_MOUSE              Reviewed;         651 AA.
P15806; Q3U153; Q8CAH9; Q8VCY4; Q922S2; Q99MB8; Q9CYJ4;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
07-APR-2021, entry version 202.
RecName: Full=Transcription factor E2-alpha;
AltName: Full=Immunoglobulin enhancer-binding factor E12/E47;
AltName: Full=Transcription factor 3;
Short=TCF-3;
AltName: Full=Transcription factor A1;
Name=Tcf3; Synonyms=Alf2, Me2, Tcfe2a;
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 E47), AND FUNCTION.
STRAIN=NIH Swiss;
PubMed=11309385; DOI=10.1074/jbc.m100827200;
Perez-Moreno M.A., Locascio A., Rodrigo I., Dhondt G., Portillo F.,
Nieto M.A., Cano A.;
"A new role for E12/E47 in the repression of E-cadherin expression and
epithelial-mesenchymal transitions.";
J. Biol. Chem. 276:27424-27431(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS E12 AND E47).
STRAIN=C57BL/6J, and NOD; TISSUE=Hypothalamus, and Spleen;
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 E12 AND E47).
STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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 369-651 (ISOFORM E47), AND FUNCTION.
TISSUE=Pancreas;
PubMed=2181401; DOI=10.1093/nar/18.5.1159;
Walker M.D., Park C.W., Rosen A., Aronheim A.;
"A cDNA from a mouse pancreatic beta cell encoding a putative transcription
factor of the insulin gene.";
Nucleic Acids Res. 18:1159-1166(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 386-493, AND VARIANT GLN-387 INS.
TISSUE=Adipocyte;
PubMed=8112613; DOI=10.1016/0378-1119(94)90764-1;
Kajimoto Y., Kawamori R., Umayahara Y., Watada H., Iwama N., Morishima T.,
Yamasaki Y., Kamada T.;
"Identification of amino-acid polymorphism within the leucine zipper motif
of mouse transcription factor A1.";
Gene 139:247-249(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 485-651 (ISOFORM E12).
STRAIN=C57BL/6J;
PubMed=7875598; DOI=10.1016/0378-1119(94)00765-k;
Watada H., Kajimoto Y., Umayahara Y., Matsuoka T., Morishima T.,
Yamasaki Y., Kawamori R., Kamada T.;
"Ubiquitous, but variable, expression of two alternatively spliced mRNAs
encoding mouse homologues of transcription factors E47 and E12.";
Gene 153:255-259(1995).
[7]
INTERACTION WITH TWIST2.
STRAIN=SWR/J; TISSUE=Brain, and Embryonic head;
PubMed=7589808; DOI=10.1006/dbio.1995.0023;
Li L., Cserjesi P., Olson E.N.;
"Dermo-1: a novel twist-related bHLH protein expressed in the developing
dermis.";
Dev. Biol. 172:280-292(1995).
[8]
INTERACTION WITH UBE2I.
PubMed=9409784; DOI=10.1016/s0378-1119(97)00444-7;
Loveys D.A., Streiff M.B., Schaefer T.S., Kato G.J.;
"The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A
transcription factors.";
Gene 201:169-177(1997).
[9]
INTERACTION WITH PTF1A.
PubMed=11318877; DOI=10.1046/j.1365-2443.2001.00422.x;
Obata J., Yano M., Mimura H., Goto T., Nakayama R., Mibu Y., Oka C.,
Kawaichi M.;
"p48 subunit of mouse PTF1 binds to RBP-Jkappa/CBF-1, the intracellular
mediator of Notch signalling, and is expressed in the neural tube of early
stage embryos.";
Genes Cells 6:345-360(2001).
[10]
SUBUNIT.
PubMed=12196028; DOI=10.1021/bi025528q;
Maleki S.J., Royer C.A., Hurlburt B.K.;
"Analysis of the DNA-binding properties of MyoD, myogenin, and E12 by
fluorescence anisotropy.";
Biochemistry 41:10888-10894(2002).
[11]
INTERACTION WITH RALGAPA1, AND SUBCELLULAR LOCATION.
PubMed=12200424; DOI=10.1074/jbc.m204858200;
Heng J.I.T., Tan S.-S.;
"Cloning and characterization of GRIPE, a novel interacting partner of the
transcription factor E12 in developing mouse forebrain.";
J. Biol. Chem. 277:43152-43159(2002).
[12]
FUNCTION, DNA-BINDING, AND INTERACTION WITH TCF15.
PubMed=15226298; DOI=10.1074/jbc.m401319200;
Wilson-Rawls J., Rhee J.M., Rawls A.;
"Paraxis is a basic helix-loop-helix protein that positively regulates
transcription through binding to specific E-box elements.";
J. Biol. Chem. 279:37685-37692(2004).
[13]
IDENTIFICATION IN A NUCLEAR TAL-1 COMPLEX.
PubMed=16407974; DOI=10.1038/sj.emboj.7600934;
Goardon N., Lambert J.A., Rodriguez P., Nissaire P., Herblot S.,
Thibault P., Dumenil D., Strouboulis J., Romeo P.-H., Hoang T.;
"ETO2 coordinates cellular proliferation and differentiation during
erythropoiesis.";
EMBO J. 25:357-366(2006).
[14]
INTERACTION WITH TGFB1I1.
PubMed=16291758; DOI=10.1074/jbc.m505869200;
Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., Gradl D.;
"HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor-
driven transcription.";
J. Biol. Chem. 281:1755-1764(2006).
[15]
FUNCTION, INTERACTION WITH NEUROD2, DNA-BINDING, DISRUPTION PHENOTYPE, AND
DEVELOPMENTAL STAGE.
PubMed=18214987; DOI=10.1002/jnr.21615;
Ravanpay A.C., Olson J.M.;
"E protein dosage influences brain development more than family member
identity.";
J. Neurosci. Res. 86:1472-1481(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-353 AND SER-357,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-528 AND SER-533 (ISOFORM
E47), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[17]
INTERACTION WITH ATOH8.
PubMed=23938248; DOI=10.1016/j.bbagrm.2013.08.003;
Ejarque M., Altirriba J., Gomis R., Gasa R.;
"Characterization of the transcriptional activity of the basic helix-loop-
helix (bHLH) transcription factor Atoh8.";
Biochim. Biophys. Acta 1829:1175-1183(2013).
[18]
INTERACTION WITH TCF15; NEUROD1 AND TWIST1.
PubMed=23395635; DOI=10.1016/j.celrep.2013.01.017;
Davies O.R., Lin C.Y., Radzisheuskaya A., Zhou X., Taube J., Blin G.,
Waterhouse A., Smith A.J., Lowell S.;
"Tcf15 primes pluripotent cells for differentiation.";
Cell Rep. 3:472-484(2013).
[19]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-369, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[20]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 547-606 IN COMPLEX WITH NEUROD1
AND PROMOTER E-BOX DNA SEQUENCE, AND SUBUNIT.
PubMed=18069799; DOI=10.1021/bi701527r;
Longo A., Guanga G.P., Rose R.B.;
"Crystal structure of E47-NeuroD1/beta2 bHLH domain-DNA complex:
heterodimer selectivity and DNA recognition.";
Biochemistry 47:218-229(2008).
-!- FUNCTION: Transcriptional regulator involved in the initiation of
neuronal differentiation and mesenchymal to epithelial transition
(PubMed:15226298, PubMed:18214987). Heterodimers between TCF3 and
tissue-specific basic helix-loop-helix (bHLH) proteins play major roles
in determining tissue-specific cell fate during embryogenesis, like
muscle or early B-cell differentiation (PubMed:18214987). Together with
TCF15, required for the mesenchymal to epithelial transition
(PubMed:11309385, PubMed:15226298). Dimers bind DNA on E-box motifs:
5'-CANNTG-3' (PubMed:15226298, PubMed:18214987). Binds to the kappa-E2
site in the kappa immunoglobulin gene enhancer (By similarity). Binds
to IEB1 and IEB2, which are short DNA sequences in the insulin gene
transcription control region (PubMed:2181401).
{ECO:0000250|UniProtKB:P15923, ECO:0000269|PubMed:11309385,
ECO:0000269|PubMed:15226298, ECO:0000269|PubMed:18214987,
ECO:0000269|PubMed:2181401}.
-!- SUBUNIT: Homodimer (PubMed:12196028). Heterodimer; efficient DNA
binding requires dimerization with another bHLH protein
(PubMed:15226298). Forms a heterodimer with TWIST1 and TWIST2
(PubMed:7589808, PubMed:23395635). Forms a heterodimer with NEUROD1;
the heterodimer is inhibited in presence of ID2, but not NR0B2, to E-
box element (PubMed:23395635, PubMed:18069799). Forms a heterodimer
with TCF15; the heterodimer binds E-box element (PubMed:15226298,
PubMed:23395635). Forms a heterodimer with MYOG; heterodimerization
enhances MYOG DNA-binding and transcriptional activities
(PubMed:12196028). Forms a heterodimer with ATOH8; repress
transcription of TCF3 and TCF3-NEUROG3 dimer-induced transactivation of
E box-dependent promoters (PubMed:23938248). Component of a nuclear
TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3
(PubMed:16407974). Interacts with NEUROD2 (PubMed:18214987). Interacts
with EP300 (By similarity). Interacts with PTF1A, TGFB1I1 and UBE2I
(PubMed:9409784, PubMed:11318877, PubMed:16291758). Interacts with
BHLHA9 (By similarity). {ECO:0000250|UniProtKB:P15923,
ECO:0000269|PubMed:11318877, ECO:0000269|PubMed:12196028,
ECO:0000269|PubMed:15226298, ECO:0000269|PubMed:16291758,
ECO:0000269|PubMed:16407974, ECO:0000269|PubMed:18069799,
ECO:0000269|PubMed:18214987, ECO:0000269|PubMed:23395635,
ECO:0000269|PubMed:23938248, ECO:0000269|PubMed:7589808,
ECO:0000269|PubMed:9409784}.
-!- SUBUNIT: [Isoform E12]: Interacts with RALGAPA1 (PubMed:12200424).
Interacts with FIGLA (By similarity). {ECO:0000250|UniProtKB:P15923,
ECO:0000269|PubMed:12200424}.
-!- INTERACTION:
P15806; Q64279: Hand1; NbExp=2; IntAct=EBI-81370, EBI-81361;
P15806; Q61039: Hand2; NbExp=2; IntAct=EBI-81370, EBI-81388;
P15806; P41136: Id2; NbExp=2; IntAct=EBI-81370, EBI-309167;
P15806; P22091: Tal1; NbExp=4; IntAct=EBI-81370, EBI-8006437;
P15806-2; P41136: Id2; NbExp=6; IntAct=EBI-413585, EBI-309167;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12200424}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=E12;
IsoId=P15806-1; Sequence=Displayed;
Name=E47;
IsoId=P15806-2; Sequence=VSP_011354;
-!- DEVELOPMENTAL STAGE: Expressed during the development of the nervous
system. {ECO:0000269|PubMed:18214987}.
-!- PTM: Phosphorylated following NGF stimulation. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice are smaller than their wild-type littermates
and fail to thrive 14 days after birth. {ECO:0000269|PubMed:18214987}.
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; AF352579; AAK18618.1; -; mRNA.
EMBL; AK017617; BAB30842.1; -; mRNA.
EMBL; AK038738; BAC30118.1; -; mRNA.
EMBL; AK156265; BAE33647.1; -; mRNA.
EMBL; BC006860; AAH06860.1; -; mRNA.
EMBL; BC018260; AAH18260.1; -; mRNA.
EMBL; X17500; CAA35541.1; -; mRNA.
EMBL; D16631; BAA04057.1; -; mRNA.
EMBL; D16632; BAA04058.1; -; mRNA.
EMBL; D16633; BAA04059.1; -; mRNA.
EMBL; D16634; BAA04060.1; -; mRNA.
EMBL; D16635; BAA04061.1; -; mRNA.
EMBL; D16636; BAA04062.1; -; mRNA.
EMBL; D16637; BAA04063.1; -; mRNA.
EMBL; D16638; BAA04064.1; -; mRNA.
EMBL; D29919; BAA06218.1; -; mRNA.
CCDS; CCDS24022.1; -. [P15806-2]
CCDS; CCDS48630.1; -. [P15806-1]
PIR; S08410; S08410.
RefSeq; NP_001157620.1; NM_001164148.1.
RefSeq; NP_001157621.1; NM_001164149.1. [P15806-1]
RefSeq; NP_001157623.1; NM_001164151.1.
RefSeq; NP_035678.3; NM_011548.4. [P15806-2]
PDB; 2QL2; X-ray; 2.50 A; A/C=547-606.
PDBsum; 2QL2; -.
SMR; P15806; -.
BioGRID; 204015; 103.
CORUM; P15806; -.
DIP; DIP-30940N; -.
IntAct; P15806; 15.
MINT; P15806; -.
STRING; 10090.ENSMUSP00000100979; -.
iPTMnet; P15806; -.
PhosphoSitePlus; P15806; -.
jPOST; P15806; -.
MaxQB; P15806; -.
PaxDb; P15806; -.
PRIDE; P15806; -.
ProteomicsDB; 262797; -. [P15806-1]
ProteomicsDB; 262798; -. [P15806-2]
Antibodypedia; 4332; 574 antibodies.
Ensembl; ENSMUST00000105345; ENSMUSP00000100982; ENSMUSG00000020167. [P15806-2]
Ensembl; ENSMUST00000105346; ENSMUSP00000100983; ENSMUSG00000020167. [P15806-1]
GeneID; 21423; -.
KEGG; mmu:21423; -.
UCSC; uc007gdg.2; mouse. [P15806-2]
UCSC; uc007gdi.2; mouse. [P15806-1]
CTD; 6929; -.
MGI; MGI:98510; Tcf3.
eggNOG; KOG3910; Eukaryota.
GeneTree; ENSGT00940000157036; -.
InParanoid; P15806; -.
PhylomeDB; P15806; -.
Reactome; R-MMU-525793; Myogenesis. [P15806-2]
Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. [P15806-2]
BioGRID-ORCS; 21423; 4 hits in 54 CRISPR screens.
ChiTaRS; Tcf3; mouse.
EvolutionaryTrace; P15806; -.
PRO; PR:P15806; -.
Proteomes; UP000000589; Chromosome 10.
RNAct; P15806; protein.
Bgee; ENSMUSG00000020167; Expressed in bone marrow and 291 other tissues.
Genevisible; P15806; MM.
GO; GO:0000785; C:chromatin; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0000791; C:euchromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0000786; C:nucleosome; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:NTNU_SB.
GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
GO; GO:0043425; F:bHLH transcription factor binding; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0070644; F:vitamin D response element binding; ISO:MGI.
GO; GO:0002326; P:B cell lineage commitment; ISS:UniProtKB.
GO; GO:0048468; P:cell development; IGI:MGI.
GO; GO:0030218; P:erythrocyte differentiation; TAS:MGI.
GO; GO:0007369; P:gastrulation; IGI:BHF-UCL.
GO; GO:0043966; P:histone H3 acetylation; IMP:MGI.
GO; GO:0043967; P:histone H4 acetylation; IMP:MGI.
GO; GO:0033152; P:immunoglobulin V(D)J recombination; IMP:MGI.
GO; GO:0030098; P:lymphocyte differentiation; IMP:MGI.
GO; GO:0001779; P:natural killer cell differentiation; IGI:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0048541; P:Peyer's patch development; IGI:MGI.
GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB.
GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:MGI.
GO; GO:0050821; P:protein stabilization; IDA:MGI.
GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0042493; P:response to drug; IMP:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Differentiation; DNA-binding;
Isopeptide bond; Methylation; Neurogenesis; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1..651
/note="Transcription factor E2-alpha"
/id="PRO_0000127468"
DOMAIN 546..599
/note="bHLH"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
REGION 387..422
/note="Leucine-zipper"
MOD_RES 135
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P15923"
MOD_RES 140
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P15923"
MOD_RES 353
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 357
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 369
/note="Omega-N-methylarginine"
/evidence="ECO:0007744|PubMed:24129315"
MOD_RES 377
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P15923"
MOD_RES 526
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P15923"
CROSSLNK 496
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P15923"
CROSSLNK 622
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P15923"
VAR_SEQ 527..598
/note="PDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLS
SEKPQTKLLILHQAVAVILS -> STDEVLSLEEKDLRDRERRMANNARERVRVRDINE
AFRELGRMCQLHLKSDKAQTKLLILQQAVQVILG (in isoform E47)"
/evidence="ECO:0000303|PubMed:11309385,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:2181401"
/id="VSP_011354"
VARIANT 387
/note="L -> LQ"
/evidence="ECO:0000269|PubMed:8112613"
CONFLICT 156
/note="S -> N (in Ref. 1; AAK18618)"
/evidence="ECO:0000305"
CONFLICT 164
/note="D -> N (in Ref. 1; AAK18618)"
/evidence="ECO:0000305"
CONFLICT 167
/note="L -> LA (in Ref. 3; AAH18260)"
/evidence="ECO:0000305"
CONFLICT 294
/note="P -> T (in Ref. 2; BAB30842)"
/evidence="ECO:0000305"
CONFLICT 633
/note="A -> P (in Ref. 3; AAH06860)"
/evidence="ECO:0000305"
HELIX 548..574
/evidence="ECO:0007744|PDB:2QL2"
HELIX 585..602
/evidence="ECO:0007744|PDB:2QL2"
MOD_RES P15806-2:528
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES P15806-2:533
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
SEQUENCE 651 AA; 67701 MW; 7904ABB37B8D39CB CRC64;
MMNQSQRMAP VGSDKELSDL LDFSMMFPLP VANGKSRPAS LGGTQFAGSG LEDRPSSGSW
GSSDQNSSSF DPSRTYSEGA HFSDSHSSLP PSTFLGAGLG GKGSERNAYA TFGRDTSVGT
LSQAGFLPGE LSLSSPGPLS PSGIKSSSQY YPSFPSNPRR RAADGGLDTQ PKKVRKVPPG
LPSSVYPPSS GDSYSRDAAA YPSAKTPSSA YPSPFYVADG SLHPSAELWS TPSQVGFGPM
LGDGSSPLPL APGSSSVGSG TFGGLQQQDR MGYQLHGSEV NGSLPAVSSF SAAPGTYSGT
SGHTPPVSGA AAESLLGTRG TTASSSGDAL GKALASIYSP DHSSNNFSPS PSTPVGSPQG
LPGTSQWPRA GAPSALSPNY DAGLHGLSKM EDRLDEAIHV LRSHAVGTAS DLHGLLPGHG
ALTTSFTGPM SLGGRHAGLV GGSHPEEGLT SGASLLHNHA SLPSQPSSLP DLSQRPPDSY
SGLGRAGTTA GASEIKREEK EDEEIASVAD AEEDKKDLKV PRTRTSPDED EDDLLPPEQK
AEREKERRVA NNARERLRVR DINEAFKELG RMCQLHLSSE KPQTKLLILH QAVAVILSLE
QQVRERNLNP KAACLKRREE EKVSGVVGDP QLALSAAHPG LGEAHNPAGH L


Related products :

Catalog number Product name Quantity
EIAAB42103 Immunoglobulin enhancer-binding factor E12_E47,Pan,Pancreas specific transcription factor 1c,Ptf1c,Rat,Rattus norvegicus,Tcf3,TCF-3,Tcfe2a,Transcription factor 3,Transcription factor E2-alpha,Transcri
EIAAB42104 Alf2,Immunoglobulin enhancer-binding factor E12_E47,Me2,Mouse,Mus musculus,Tcf3,TCF-3,Tcfe2a,Transcription factor 3,Transcription factor A1,Transcription factor E2-alpha
18-003-44075 Transcription factor E2-alpha - Immunoglobulin enhancer-binding factor E12_E47; Transcription factor 3; TCF-3; Immunoglobulin transcription factor 1; Transcription factor ITF-1; Kappa-E2-binding facto 0.1 mg Protein A
18-272-195373 TCF3 ( phospho T355 ) - Rabbit polyclonal to TCF3 ( phospho T355 ); Immunoglobulin enhancer-binding factor E12_E47; Transcription factor 3; TCF-3; Immunoglobulin transcription factor 1; Transcription 0.05 mg
EIAAB42096 Alpha-globin transcription factor CP2,Homo sapiens,Human,LSF,SAA3 enhancer factor,SEF,TFCP2,Transcription factor LSF
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
EIAAB27823 Alpha-1-fetoprotein transcription factor,B1-binding factor,B1F,CPF,CYP7A promoter-binding factor,FTF,hB1F,Hepatocytic transcription factor,Homo sapiens,Human,Liver receptor homolog 1,LRH-1,NR5A2,Nucle
EIAAB32964 bHLH transcription factor p48,Mouse,Mus musculus,p48 DNA-binding subunit of transcription factor PTF1,Pancreas transcription factor 1 subunit alpha,Pancreas-specific transcription factor 1a,Ptf1a,Ptf1
EIAAB47163 CREB_ATF bZIP transcription factor,Crebzf,HCF-binding transcription factor Zhangfei,Host cell factor-binding transcription factor Zhangfei,Mouse,Mus musculus,Tyrosine kinase-associated leucine zipper
18-003-43009 Transcription factor 4 - Immunoglobulin transcription factor 2; ITF-2; SL3-3 enhancer factor 2; SEF-2 Polyclonal 0.05 mg Aff Pur
EIAAB32963 bHLH transcription factor p48,p48 DNA-binding subunit of transcription factor PTF1,Pancreas transcription factor 1 subunit alpha,Pancreas-specific transcription factor 1a,Ptf1a,Ptf1p48,PTF1-p48,Rat,Ra
EIAAB47164 CREB_ATF bZIP transcription factor,CREBZF,HCF-binding transcription factor Zhangfei,Homo sapiens,Host cell factor-binding transcription factor Zhangfei,Human,ZF
18-461-10169 Orphan nuclear receptor NR5A2 - Alpha-1-fetoprotein transcription factor; Hepatocytic transcription factor; B1-binding factor; hB1F; CYP7A promoter-binding factor; Liver receptor homolog 1; LRH-1 Poly 0.05 ml
EIAAB25650 Homo sapiens,Human,Metal regulatory transcription factor 1,MRE-binding transcription factor,MTF1,Transcription factor MTF-1
18-003-42098 Ets domain transcription factor - ESE3 transcription factor; EHF protein; DJ875K15.1.2 (Ets homologous factor (Ets-domain transcription factor. ESE-3B (Isoform 2))); ETS-family transcription factor EH 0.1 mg Protein A
18-003-42089 Pancreas transcription factor 1 subunit alpha - Pancreas-specific transcription factor 1a; bHLH transcription factor p48; p48 DNA-binding subunit of transcription factor PTF1; PTF1-p48 Polyclonal 0.1 mg Protein A
EIAAB36445 Cbfa1,CBF-alpha-1,Core-binding factor subunit alpha-1,Osf2,OSF-2,Osteoblast-specific transcription factor 2,Rat,Rattus norvegicus,Runt-related transcription factor 2,Runx2
EIAAB42084 Homo sapiens,Human,Mitochondrial transcription factor 1,MtTF1,mtTFA,TCF6,TCF-6,TCF6L2,TFAM,Transcription factor 6,Transcription factor 6-like 2,Transcription factor A, mitochondrial
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
18-003-42234 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
18-003-42235 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
EIAAB25651 Metal regulatory transcription factor 1,Mouse,MRE-binding transcription factor,Mtf1,Mtf-1,Mus musculus,Transcription factor MTF-1
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
EIAAB41858 Homo sapiens,Human,RTEF1,TCF13L1,TEA domain family member 4,TEAD4,TEAD-4,TEF3,Transcription factor 13-like 1,Transcription factor RTEF-1,Transcriptional enhancer factor TEF-3
31-162 Transcription Factor AREB6 _ transcription factor 8 _zinc finger homeodomain enhancer-binding protein inhibits interleukin-2 (IL-2) gene expression. May be responsible for transcriptional repression o 0.05 mg
Pathways :
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP272: Blood Clotting Cascade
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP1983: Splicing factor NOVA regulated synpatic proteins
WP2148: Brain derived neurotrophic factor
WP830: Eukaryotic Transcription Initiation
WP405: Eukaryotic Transcription Initiation
WP1066: Eukaryotic Transcription Initiation
WP1541: Energy Metabolism
WP1906: RNA Polymerase II Transcription
WP518: Eukaryotic Transcription Initiation
WP567: Eukaryotic Transcription Initiation
WP948: Eukaryotic Transcription Initiation
WP1905: RNA Polymerase I, RNA Polymerase III, and Mitochondrial Transcription
WP491: Eukaryotic Transcription Initiation

Related Genes :
[Tcf3 Alf2 Me2 Tcfe2a] Transcription factor E2-alpha (Immunoglobulin enhancer-binding factor E12/E47) (Transcription factor 3) (TCF-3) (Transcription factor A1)
[TCF3 BHLHB21 E2A ITF1] Transcription factor E2-alpha (Class B basic helix-loop-helix protein 21) (bHLHb21) (Immunoglobulin enhancer-binding factor E12/E47) (Immunoglobulin transcription factor 1) (Kappa-E2-binding factor) (Transcription factor 3) (TCF-3) (Transcription factor ITF-1)
[Tcf3 Pan Ptf1c Tcfe2a] Transcription factor E2-alpha (Immunoglobulin enhancer-binding factor E12/E47) (Pancreas specific transcription factor 1c) (Transcription factor 3) (TCF-3) (Transcription regulator Pan)
[TCF3 PAN] Transcription factor E2-alpha (Immunoglobulin-enhancer-binding factor E12/E47) (Transcription factor 3) (TCF-3) (Transcription regulator Pan)
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[TCF4 BHLHB19 ITF2 SEF2] Transcription factor 4 (TCF-4) (Class B basic helix-loop-helix protein 19) (bHLHb19) (Immunoglobulin transcription factor 2) (ITF-2) (SL3-3 enhancer factor 2) (SEF-2)
[Tcf4 Itf2 Sef2] Transcription factor 4 (TCF-4) (Immunoglobulin transcription factor 2) (ITF-2) (RITF-2) (R8f DNA-binding protein) (SL3-3 enhancer factor 2) (SEF-2)
[tat] Protein Tat (Transactivating regulatory protein)
[FOXA1 HNF3A TCF3A] Hepatocyte nuclear factor 3-alpha (HNF-3-alpha) (HNF-3A) (Forkhead box protein A1) (Transcription factor 3A) (TCF-3A)
[NFE2L1 HBZ17 NRF1 TCF11] Endoplasmic reticulum membrane sensor NFE2L1 (Locus control region-factor 1) (LCR-F1) (Nuclear factor erythroid 2-related factor 1) (NF-E2-related factor 1) (NFE2-related factor 1) (Nuclear factor, erythroid derived 2, like 1) (Protein NRF1, p120 form) (Transcription factor 11) (TCF-11) [Cleaved into: Transcription factor NRF1 (Protein NRF1, p110 form)]
[RUNX3 AML2 CBFA3 PEBP2A3] Runt-related transcription factor 3 (Acute myeloid leukemia 2 protein) (Core-binding factor subunit alpha-3) (CBF-alpha-3) (Oncogene AML-2) (Polyomavirus enhancer-binding protein 2 alpha C subunit) (PEA2-alpha C) (PEBP2-alpha C) (SL3-3 enhancer factor 1 alpha C subunit) (SL3/AKV core-binding factor alpha C subunit)
[RUNX1 AML1 CBFA2] Runt-related transcription factor 1 (Acute myeloid leukemia 1 protein) (Core-binding factor subunit alpha-2) (CBF-alpha-2) (Oncogene AML-1) (Polyomavirus enhancer-binding protein 2 alpha B subunit) (PEA2-alpha B) (PEBP2-alpha B) (SL3-3 enhancer factor 1 alpha B subunit) (SL3/AKV core-binding factor alpha B subunit)
[RUNX2 AML3 CBFA1 OSF2 PEBP2A] Runt-related transcription factor 2 (Acute myeloid leukemia 3 protein) (Core-binding factor subunit alpha-1) (CBF-alpha-1) (Oncogene AML-3) (Osteoblast-specific transcription factor 2) (OSF-2) (Polyomavirus enhancer-binding protein 2 alpha A subunit) (PEA2-alpha A) (PEBP2-alpha A) (SL3-3 enhancer factor 1 alpha A subunit) (SL3/AKV core-binding factor alpha A subunit)
[LEF1] Lymphoid enhancer-binding factor 1 (LEF-1) (T cell-specific transcription factor 1-alpha) (TCF1-alpha)
[CEBPB TCF5 PP9092] CCAAT/enhancer-binding protein beta (C/EBP beta) (Liver activator protein) (LAP) (Liver-enriched inhibitory protein) (LIP) (Nuclear factor NF-IL6) (Transcription factor 5) (TCF-5)
[Tcf12 Alf1 Meb] Transcription factor 12 (TCF-12) (Class A helix-loop-helix transcription factor ME1) (DNA-binding protein HTF4) (E-box-binding protein) (Transcription factor HTF-4)
[HNF4A HNF4 NR2A1 TCF14] Hepatocyte nuclear factor 4-alpha (HNF-4-alpha) (Nuclear receptor subfamily 2 group A member 1) (Transcription factor 14) (TCF-14) (Transcription factor HNF-4)
[tcf3 e2a] Transcription factor E2-alpha (Transcription factor 3) (TCF-3) (Transcription factor XE12/XE47)
[Runx1 Aml1 Cbfa2 Pebp2ab] Runt-related transcription factor 1 (Acute myeloid leukemia 1 protein) (Core-binding factor subunit alpha-2) (CBF-alpha-2) (Oncogene AML-1) (Polyomavirus enhancer-binding protein 2 alpha B subunit) (PEA2-alpha B) (PEBP2-alpha B) (SL3-3 enhancer factor 1 alpha B subunit) (SL3/AKV core-binding factor alpha B subunit)
[Tcf12] Transcription factor 12 (TCF-12) (DNA-binding protein HTF4) (E-box-binding protein) (Salivary-specific cAMP response element-binding protein alpha) (SCBP-alpha) (Transcription factor HTF-4)
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[TCF12 BHLHB20 HEB HTF4] Transcription factor 12 (TCF-12) (Class B basic helix-loop-helix protein 20) (bHLHb20) (DNA-binding protein HTF4) (E-box-binding protein) (Transcription factor HTF-4)
[Hnf4a Hnf-4 Hnf4 Nr2a1 Tcf14] Hepatocyte nuclear factor 4-alpha (HNF-4-alpha) (Nuclear receptor subfamily 2 group A member 1) (Transcription factor 14) (TCF-14) (Transcription factor HNF-4)
[Runx3 Aml2 Cbfa3 Pebp2a3] Runt-related transcription factor 3 (Acute myeloid leukemia 2 protein) (Core-binding factor subunit alpha-3) (CBF-alpha-3) (Oncogene AML-2) (Polyomavirus enhancer-binding protein 2 alpha C subunit) (PEA2-alpha C) (PEBP2-alpha C) (SL3-3 enhancer factor 1 alpha C subunit) (SL3/AKV core-binding factor alpha C subunit)
[TCF7L2 TCF4] Transcription factor 7-like 2 (HMG box transcription factor 4) (T-cell-specific transcription factor 4) (T-cell factor 4) (TCF-4) (hTCF-4)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[Tcf7l2 Tcf4] Transcription factor 7-like 2 (HMG box transcription factor 4) (T-cell-specific transcription factor 4) (T-cell factor 4) (TCF-4) (mTCF-4)
[TFCP2 LSF SEF] Alpha-globin transcription factor CP2 (SAA3 enhancer factor) (Transcription factor LSF)
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]

Bibliography :