TFE2_MOUSE
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 03-AUG-2022, entry version 207.
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]
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). Binds to the kappa-E2
CC site in the kappa immunoglobulin gene enhancer (By similarity). Binds
CC to IEB1 and IEB2, which are short DNA sequences in the insulin gene
CC 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). {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:7589808,
CC 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}.
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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 PDBsum; 2QL2; -.
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; P15806; -.
DR PRIDE; P15806; -.
DR ProteomicsDB; 262797; -. [P15806-1]
DR ProteomicsDB; 262798; -. [P15806-2]
DR Antibodypedia; 4332; 594 antibodies from 46 providers.
DR DNASU; 21423; -.
DR Ensembl; ENSMUST00000105345; ENSMUSP00000100982; ENSMUSG00000020167. [P15806-2]
DR Ensembl; ENSMUST00000105346; ENSMUSP00000100983; ENSMUSG00000020167. [P15806-1]
DR GeneID; 21423; -.
DR KEGG; mmu:21423; -.
DR UCSC; uc007gdg.2; mouse. [P15806-2]
DR UCSC; uc007gdi.2; mouse. [P15806-1]
DR CTD; 6929; -.
DR MGI; MGI:98510; Tcf3.
DR VEuPathDB; HostDB:ENSMUSG00000020167; -.
DR eggNOG; KOG3910; Eukaryota.
DR GeneTree; ENSGT00940000157036; -.
DR InParanoid; P15806; -.
DR OMA; AHVHRPH; -.
DR PhylomeDB; P15806; -.
DR Reactome; R-MMU-525793; Myogenesis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR BioGRID-ORCS; 21423; 5 hits in 77 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 249 other tissues.
DR ExpressionAtlas; P15806; baseline and differential.
DR Genevisible; P15806; MM.
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:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; 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: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:0043966; P:histone H3 acetylation; IMP:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; 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: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:0045893; P:positive regulation of transcription, DNA-templated; IGI:MGI.
DR GO; GO:0050821; P:protein stabilization; 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:0006355; P:regulation of transcription, DNA-templated; 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 Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
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 548..574
FT /evidence="ECO:0007829|PDB:2QL2"
FT HELIX 585..602
FT /evidence="ECO:0007829|PDB:2QL2"
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
