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}.
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 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

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