ID TFE2_MOUSE Reviewed; 651 AA. AC P15806; Q3U153; Q8CAH9; Q8VCY4; Q922S2; Q99MB8; Q9CYJ4; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 2. DT 24-JAN-2024, entry version 215. DE RecName: Full=Transcription factor E2-alpha; DE AltName: Full=Immunoglobulin enhancer-binding factor E12/E47; DE AltName: Full=Transcription factor 3; DE Short=TCF-3; DE AltName: Full=Transcription factor A1; GN Name=Tcf3; Synonyms=Alf2, Me2, Tcfe2a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E47), AND FUNCTION. RC STRAIN=NIH Swiss; RX PubMed=11309385; DOI=10.1074/jbc.m100827200; RA Perez-Moreno M.A., Locascio A., Rodrigo I., Dhondt G., Portillo F., RA Nieto M.A., Cano A.; RT "A new role for E12/E47 in the repression of E-cadherin expression and RT epithelial-mesenchymal transitions."; RL J. Biol. Chem. 276:27424-27431(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS E12 AND E47). RC STRAIN=C57BL/6J, and NOD; TISSUE=Hypothalamus, and Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS E12 AND E47). RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 369-651 (ISOFORM E47), AND FUNCTION. RC TISSUE=Pancreas; RX PubMed=2181401; DOI=10.1093/nar/18.5.1159; RA Walker M.D., Park C.W., Rosen A., Aronheim A.; RT "A cDNA from a mouse pancreatic beta cell encoding a putative transcription RT factor of the insulin gene."; RL Nucleic Acids Res. 18:1159-1166(1990). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 386-493, AND VARIANT GLN-387 INS. RC TISSUE=Adipocyte; RX PubMed=8112613; DOI=10.1016/0378-1119(94)90764-1; RA Kajimoto Y., Kawamori R., Umayahara Y., Watada H., Iwama N., Morishima T., RA Yamasaki Y., Kamada T.; RT "Identification of amino-acid polymorphism within the leucine zipper motif RT of mouse transcription factor A1."; RL Gene 139:247-249(1994). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 485-651 (ISOFORM E12). RC STRAIN=C57BL/6J; RX PubMed=7875598; DOI=10.1016/0378-1119(94)00765-k; RA Watada H., Kajimoto Y., Umayahara Y., Matsuoka T., Morishima T., RA Yamasaki Y., Kawamori R., Kamada T.; RT "Ubiquitous, but variable, expression of two alternatively spliced mRNAs RT encoding mouse homologues of transcription factors E47 and E12."; RL Gene 153:255-259(1995). RN [7] RP INTERACTION WITH TWIST2. RC STRAIN=SWR/J; TISSUE=Brain, and Embryonic head; RX PubMed=7589808; DOI=10.1006/dbio.1995.0023; RA Li L., Cserjesi P., Olson E.N.; RT "Dermo-1: a novel twist-related bHLH protein expressed in the developing RT dermis."; RL Dev. Biol. 172:280-292(1995). RN [8] RP INTERACTION WITH UBE2I. RX PubMed=9409784; DOI=10.1016/s0378-1119(97)00444-7; RA Loveys D.A., Streiff M.B., Schaefer T.S., Kato G.J.; RT "The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A RT transcription factors."; RL Gene 201:169-177(1997). RN [9] RP INTERACTION WITH PTF1A. RX PubMed=11318877; DOI=10.1046/j.1365-2443.2001.00422.x; RA Obata J., Yano M., Mimura H., Goto T., Nakayama R., Mibu Y., Oka C., RA Kawaichi M.; RT "p48 subunit of mouse PTF1 binds to RBP-Jkappa/CBF-1, the intracellular RT mediator of Notch signalling, and is expressed in the neural tube of early RT stage embryos."; RL Genes Cells 6:345-360(2001). RN [10] RP SUBUNIT. RX PubMed=12196028; DOI=10.1021/bi025528q; RA Maleki S.J., Royer C.A., Hurlburt B.K.; RT "Analysis of the DNA-binding properties of MyoD, myogenin, and E12 by RT fluorescence anisotropy."; RL Biochemistry 41:10888-10894(2002). RN [11] RP INTERACTION WITH RALGAPA1, AND SUBCELLULAR LOCATION. RX PubMed=12200424; DOI=10.1074/jbc.m204858200; RA Heng J.I.T., Tan S.-S.; RT "Cloning and characterization of GRIPE, a novel interacting partner of the RT transcription factor E12 in developing mouse forebrain."; RL J. Biol. Chem. 277:43152-43159(2002). RN [12] RP FUNCTION, DNA-BINDING, AND INTERACTION WITH TCF15. RX PubMed=15226298; DOI=10.1074/jbc.m401319200; RA Wilson-Rawls J., Rhee J.M., Rawls A.; RT "Paraxis is a basic helix-loop-helix protein that positively regulates RT transcription through binding to specific E-box elements."; RL J. Biol. Chem. 279:37685-37692(2004). RN [13] RP IDENTIFICATION IN A NUCLEAR TAL-1 COMPLEX. RX PubMed=16407974; DOI=10.1038/sj.emboj.7600934; RA Goardon N., Lambert J.A., Rodriguez P., Nissaire P., Herblot S., RA Thibault P., Dumenil D., Strouboulis J., Romeo P.-H., Hoang T.; RT "ETO2 coordinates cellular proliferation and differentiation during RT erythropoiesis."; RL EMBO J. 25:357-366(2006). RN [14] RP INTERACTION WITH TGFB1I1. RX PubMed=16291758; DOI=10.1074/jbc.m505869200; RA Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., Gradl D.; RT "HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor- RT driven transcription."; RL J. Biol. Chem. 281:1755-1764(2006). RN [15] RP FUNCTION, INTERACTION WITH NEUROD2, DNA-BINDING, DISRUPTION PHENOTYPE, AND RP DEVELOPMENTAL STAGE. RX PubMed=18214987; DOI=10.1002/jnr.21615; RA Ravanpay A.C., Olson J.M.; RT "E protein dosage influences brain development more than family member RT identity."; RL J. Neurosci. Res. 86:1472-1481(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-353 AND SER-357, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-528 AND SER-533 (ISOFORM RP E47), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [17] RP INTERACTION WITH ATOH8. RX PubMed=23938248; DOI=10.1016/j.bbagrm.2013.08.003; RA Ejarque M., Altirriba J., Gomis R., Gasa R.; RT "Characterization of the transcriptional activity of the basic helix-loop- RT helix (bHLH) transcription factor Atoh8."; RL Biochim. Biophys. Acta 1829:1175-1183(2013). RN [18] RP INTERACTION WITH TCF15; NEUROD1 AND TWIST1. RX PubMed=23395635; DOI=10.1016/j.celrep.2013.01.017; RA Davies O.R., Lin C.Y., Radzisheuskaya A., Zhou X., Taube J., Blin G., RA Waterhouse A., Smith A.J., Lowell S.; RT "Tcf15 primes pluripotent cells for differentiation."; RL Cell Rep. 3:472-484(2013). RN [19] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-369, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [20] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH ASCL5. RX PubMed=30426815; DOI=10.1177/0022034518808254; RA He B., Chiba Y., Li H., de Vega S., Tanaka K., Yoshizaki K., Ishijima M., RA Yuasa K., Ishikawa M., Rhodes C., Sakai K., Zhang P., Fukumoto S., Zhou X., RA Yamada Y.; RT "Identification of the Novel Tooth-Specific Transcription Factor AmeloD."; RL J. Dent. Res. 98:234-241(2019). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 547-606 IN COMPLEX WITH NEUROD1 RP AND PROMOTER E-BOX DNA SEQUENCE, AND SUBUNIT. RX PubMed=18069799; DOI=10.1021/bi701527r; RA Longo A., Guanga G.P., Rose R.B.; RT "Crystal structure of E47-NeuroD1/beta2 bHLH domain-DNA complex: RT heterodimer selectivity and DNA recognition."; RL Biochemistry 47:218-229(2008). CC -!- FUNCTION: Transcriptional regulator involved in the initiation of CC neuronal differentiation and mesenchymal to epithelial transition CC (PubMed:15226298, PubMed:18214987). Heterodimers between TCF3 and CC tissue-specific basic helix-loop-helix (bHLH) proteins play major roles CC in determining tissue-specific cell fate during embryogenesis, like CC muscle or early B-cell differentiation (PubMed:18214987). Together with CC TCF15, required for the mesenchymal to epithelial transition CC (PubMed:11309385, PubMed:15226298). Dimers bind DNA on E-box motifs: CC 5'-CANNTG-3' (PubMed:15226298, PubMed:18214987, PubMed:30426815). Binds CC to the kappa-E2 site in the kappa immunoglobulin gene enhancer (By CC similarity). Binds to IEB1 and IEB2, which are short DNA sequences in CC the insulin gene transcription control region (PubMed:2181401). CC {ECO:0000250|UniProtKB:P15923, ECO:0000269|PubMed:11309385, CC ECO:0000269|PubMed:15226298, ECO:0000269|PubMed:18214987, CC ECO:0000269|PubMed:2181401}. CC -!- FUNCTION: [Isoform E47]: Facilitates ATOH7 binding to DNA at the CC consensus sequence 5'-CAGGTG-3', and positively regulates CC transcriptional activity. {ECO:0000250|UniProtKB:P15923}. CC -!- SUBUNIT: Homodimer (PubMed:12196028). Heterodimer; efficient DNA CC binding requires dimerization with another bHLH protein CC (PubMed:15226298). Forms a heterodimer with TWIST1 and TWIST2 CC (PubMed:7589808, PubMed:23395635). Forms a heterodimer with NEUROD1; CC the heterodimer is inhibited in presence of ID2, but not NR0B2, to E- CC box element (PubMed:23395635, PubMed:18069799). Forms a heterodimer CC with TCF15; the heterodimer binds E-box element (PubMed:15226298, CC PubMed:23395635). Forms a heterodimer with MYOG; heterodimerization CC enhances MYOG DNA-binding and transcriptional activities CC (PubMed:12196028). Forms a heterodimer with ATOH8; repress CC transcription of TCF3 and TCF3-NEUROG3 dimer-induced transactivation of CC E box-dependent promoters (PubMed:23938248). Component of a nuclear CC TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3 CC (PubMed:16407974). Interacts with NEUROD2 (PubMed:18214987). Interacts CC with EP300 (By similarity). Interacts with PTF1A, TGFB1I1 and UBE2I CC (PubMed:9409784, PubMed:11318877, PubMed:16291758). Interacts with CC BHLHA9 (By similarity). Interacts with ASB2; the interaction is CC mediated by SKP2 and targets TCF3 for Notch-induced proteasomal CC degradation (By similarity). Interacts with transcription factor CC ASCL5/AmeloD. {ECO:0000250|UniProtKB:P15923, CC ECO:0000269|PubMed:11318877, ECO:0000269|PubMed:12196028, CC ECO:0000269|PubMed:15226298, ECO:0000269|PubMed:16291758, CC ECO:0000269|PubMed:16407974, ECO:0000269|PubMed:18069799, CC ECO:0000269|PubMed:18214987, ECO:0000269|PubMed:23395635, CC ECO:0000269|PubMed:23938248, ECO:0000269|PubMed:30426815, CC ECO:0000269|PubMed:7589808, ECO:0000269|PubMed:9409784}. CC -!- SUBUNIT: [Isoform E47]: Forms a heterodimer with ATOH7; required for CC ATOH7 DNA-binding. {ECO:0000250|UniProtKB:P15923}. CC -!- SUBUNIT: [Isoform E12]: Interacts with RALGAPA1 (PubMed:12200424). CC Interacts with FIGLA (By similarity). {ECO:0000250|UniProtKB:P15923, CC ECO:0000269|PubMed:12200424}. CC -!- INTERACTION: CC P15806; Q64279: Hand1; NbExp=2; IntAct=EBI-81370, EBI-81361; CC P15806; Q61039: Hand2; NbExp=2; IntAct=EBI-81370, EBI-81388; CC P15806; P41136: Id2; NbExp=2; IntAct=EBI-81370, EBI-309167; CC P15806; P22091: Tal1; NbExp=4; IntAct=EBI-81370, EBI-8006437; CC P15806-2; P41136: Id2; NbExp=6; IntAct=EBI-413585, EBI-309167; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12200424}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=E12; CC IsoId=P15806-1; Sequence=Displayed; CC Name=E47; CC IsoId=P15806-2; Sequence=VSP_011354; CC -!- DEVELOPMENTAL STAGE: Expressed during the development of the nervous CC system. {ECO:0000269|PubMed:18214987}. CC -!- PTM: Phosphorylated following NGF stimulation. {ECO:0000250}. CC -!- PTM: Undergoes Notch-induced ubiquitination and subsequent proteasomal CC degradation which is mediated by ASB1 or ASB2, the substrate- CC recognition components of probable ECS E3 ubiquitin-protein ligase CC complexes. {ECO:0000250|UniProtKB:P15923}. CC -!- DISRUPTION PHENOTYPE: Mice are smaller than their wild-type littermates CC and fail to thrive 14 days after birth. {ECO:0000269|PubMed:18214987}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF352579; AAK18618.1; -; mRNA. DR EMBL; AK017617; BAB30842.1; -; mRNA. DR EMBL; AK038738; BAC30118.1; -; mRNA. DR EMBL; AK156265; BAE33647.1; -; mRNA. DR EMBL; BC006860; AAH06860.1; -; mRNA. DR EMBL; BC018260; AAH18260.1; -; mRNA. DR EMBL; X17500; CAA35541.1; -; mRNA. DR EMBL; D16631; BAA04057.1; -; mRNA. DR EMBL; D16632; BAA04058.1; -; mRNA. DR EMBL; D16633; BAA04059.1; -; mRNA. DR EMBL; D16634; BAA04060.1; -; mRNA. DR EMBL; D16635; BAA04061.1; -; mRNA. DR EMBL; D16636; BAA04062.1; -; mRNA. DR EMBL; D16637; BAA04063.1; -; mRNA. DR EMBL; D16638; BAA04064.1; -; mRNA. DR EMBL; D29919; BAA06218.1; -; mRNA. DR CCDS; CCDS24022.1; -. [P15806-2] DR CCDS; CCDS48630.1; -. [P15806-1] DR PIR; S08410; S08410. DR RefSeq; NP_001157620.1; NM_001164148.1. DR RefSeq; NP_001157621.1; NM_001164149.1. [P15806-1] DR RefSeq; NP_001157623.1; NM_001164151.1. DR RefSeq; NP_035678.3; NM_011548.4. [P15806-2] DR PDB; 2QL2; X-ray; 2.50 A; A/C=547-606. DR PDB; 7WZ6; X-ray; 2.05 A; A=547-609. DR PDBsum; 2QL2; -. DR PDBsum; 7WZ6; -. DR AlphaFoldDB; P15806; -. DR SMR; P15806; -. DR BioGRID; 204015; 103. DR CORUM; P15806; -. DR DIP; DIP-30940N; -. DR IntAct; P15806; 45. DR MINT; P15806; -. DR STRING; 10090.ENSMUSP00000100979; -. DR iPTMnet; P15806; -. DR PhosphoSitePlus; P15806; -. DR EPD; P15806; -. DR jPOST; P15806; -. DR MaxQB; P15806; -. DR PaxDb; 10090-ENSMUSP00000100979; -. DR ProteomicsDB; 262797; -. [P15806-1] DR ProteomicsDB; 262798; -. [P15806-2] DR Pumba; P15806; -. DR Antibodypedia; 4332; 660 antibodies from 46 providers. DR DNASU; 21423; -. DR Ensembl; ENSMUST00000105345.10; ENSMUSP00000100982.4; ENSMUSG00000020167.15. [P15806-2] DR Ensembl; ENSMUST00000105346.10; ENSMUSP00000100983.4; ENSMUSG00000020167.15. [P15806-1] DR GeneID; 21423; -. DR KEGG; mmu:21423; -. DR UCSC; uc007gdg.2; mouse. [P15806-2] DR UCSC; uc007gdi.2; mouse. [P15806-1] DR AGR; MGI:98510; -. DR CTD; 6929; -. DR MGI; MGI:98510; Tcf3. DR VEuPathDB; HostDB:ENSMUSG00000020167; -. DR eggNOG; KOG3910; Eukaryota. DR GeneTree; ENSGT00940000157036; -. DR InParanoid; P15806; -. DR OrthoDB; 2915397at2759; -. DR PhylomeDB; P15806; -. DR Reactome; R-MMU-525793; Myogenesis. [P15806-2] DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. [P15806-2] DR BioGRID-ORCS; 21423; 5 hits in 82 CRISPR screens. DR ChiTaRS; Tcf3; mouse. DR EvolutionaryTrace; P15806; -. DR PRO; PR:P15806; -. DR Proteomes; UP000000589; Chromosome 10. DR RNAct; P15806; Protein. DR Bgee; ENSMUSG00000020167; Expressed in ventricular zone and 253 other cell types or tissues. DR ExpressionAtlas; P15806; baseline and differential. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0000791; C:euchromatin; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0000786; C:nucleosome; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:NTNU_SB. DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL. DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0070888; F:E-box binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:MGI. DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI. DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:0070644; F:vitamin D response element binding; ISO:MGI. DR GO; GO:0002326; P:B cell lineage commitment; ISS:UniProtKB. DR GO; GO:0048468; P:cell development; IGI:MGI. DR GO; GO:0006338; P:chromatin remodeling; IMP:MGI. DR GO; GO:0030218; P:erythrocyte differentiation; TAS:MGI. DR GO; GO:0007369; P:gastrulation; IGI:BHF-UCL. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0033152; P:immunoglobulin V(D)J recombination; IMP:MGI. DR GO; GO:0030098; P:lymphocyte differentiation; IMP:MGI. DR GO; GO:0001779; P:natural killer cell differentiation; IGI:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0048541; P:Peyer's patch development; IGI:MGI. DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB. DR GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IGI:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI. DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0050821; P:protein stabilization; IDA:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI. DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI. DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI. DR CDD; cd18945; bHLH_E-protein_TCF4_E2-2; 1. DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1. DR InterPro; IPR011598; bHLH_dom. DR InterPro; IPR036638; HLH_DNA-bd_sf. DR PANTHER; PTHR11793; BASIC HELIX-LOOP-HELIX TRANSCRIPTION FACTOR; 1. DR PANTHER; PTHR11793:SF7; TRANSCRIPTION FACTOR E2-ALPHA; 1. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1. DR PROSITE; PS50888; BHLH; 1. DR Genevisible; P15806; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Differentiation; DNA-binding; KW Isopeptide bond; Methylation; Neurogenesis; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..651 FT /note="Transcription factor E2-alpha" FT /id="PRO_0000127468" FT DOMAIN 546..599 FT /note="bHLH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981" FT REGION 32..107 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 131..208 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 341..378 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 387..422 FT /note="Leucine-zipper" FT REGION 457..549 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 50..92 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 131..155 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 341..364 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 457..475 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 492..549 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 135 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15923" FT MOD_RES 140 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15923" FT MOD_RES 353 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 357 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 369 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 377 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15923" FT MOD_RES 526 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15923" FT CROSSLNK 496 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P15923" FT CROSSLNK 622 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P15923" FT VAR_SEQ 527..598 FT /note="PDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLS FT SEKPQTKLLILHQAVAVILS -> STDEVLSLEEKDLRDRERRMANNARERVRVRDINE FT AFRELGRMCQLHLKSDKAQTKLLILQQAVQVILG (in isoform E47)" FT /evidence="ECO:0000303|PubMed:11309385, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:2181401" FT /id="VSP_011354" FT VARIANT 387 FT /note="L -> LQ" FT /evidence="ECO:0000269|PubMed:8112613" FT CONFLICT 156 FT /note="S -> N (in Ref. 1; AAK18618)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="D -> N (in Ref. 1; AAK18618)" FT /evidence="ECO:0000305" FT CONFLICT 167 FT /note="L -> LA (in Ref. 3; AAH18260)" FT /evidence="ECO:0000305" FT CONFLICT 294 FT /note="P -> T (in Ref. 2; BAB30842)" FT /evidence="ECO:0000305" FT CONFLICT 633 FT /note="A -> P (in Ref. 3; AAH06860)" FT /evidence="ECO:0000305" FT HELIX 547..577 FT /evidence="ECO:0007829|PDB:7WZ6" FT HELIX 585..605 FT /evidence="ECO:0007829|PDB:7WZ6" FT MOD_RES P15806-2:528 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES P15806-2:533 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" SQ 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 //