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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.
25-OCT-2017, entry version 176.
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).
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).
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.
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]
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).
[13]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
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. 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. Dimers bind DNA on E-
box motifs: 5'-CANNTG-3'. Binds to the kappa-E2 site in the kappa
immunoglobulin gene enhancer. Binds to IEB1 and IEB2, which are
short DNA sequences in the insulin gene transcription control
region. {ECO:0000269|PubMed:18214987}.
-!- SUBUNIT: Forms a heterodimer with TWIST2. Forms a heterodimer with
NEUROD1; the heterodimer is inhibited in presence of ID2, but not
NR0B2, to E-box element. Isoform E12 interacts with RALGAPA1 and
FIGLA. Interacts with EP300. Efficient DNA binding requires
dimerization with another bHLH protein (By similarity). Homodimer.
Heterodimer. Forms a heterodimer with MYOG; heterodimerization
enhances MYOG DNA-binding and transcriptional activities.
Interacts with PTF1A, TGFB1I1 and UBE2I. Component of a nuclear
TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3.
Interacts with NEUROD2. Interacts with BHLHA9. Forms a heterodimer
with ATOH8; repress transcription of TCF3 and TCF3/NEUROG3 dimer-
induced transactivation of E box-dependent promoters.
{ECO:0000250|UniProtKB:P15923, ECO:0000269|PubMed:11318877,
ECO:0000269|PubMed:12196028, ECO:0000269|PubMed:12200424,
ECO:0000269|PubMed:16291758, ECO:0000269|PubMed:16407974,
ECO:0000269|PubMed:18069799, ECO:0000269|PubMed:18214987,
ECO:0000269|PubMed:23938248, ECO:0000269|PubMed:7589808,
ECO:0000269|PubMed:9409784}.
-!- INTERACTION:
Q64279:Hand1; NbExp=2; IntAct=EBI-81370, EBI-81361;
Q61039:Hand2; NbExp=2; IntAct=EBI-81370, EBI-81388;
P41136:Id2; NbExp=6; IntAct=EBI-413585, EBI-309167;
P22091:Tal1; NbExp=4; IntAct=EBI-81370, EBI-8006437;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=E12;
IsoId=P15806-1; Sequence=Displayed;
Name=E47;
IsoId=P15806-2; Sequence=VSP_011354;
Note=Contains a phosphothreonine at position 528. Contains a
phosphoserine at position 533. {ECO:0000244|PubMed:21183079};
-!- 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]
UniGene; Mm.3406; -.
PDB; 2QL2; X-ray; 2.50 A; A/C=547-606.
PDBsum; 2QL2; -.
ProteinModelPortal; P15806; -.
SMR; P15806; -.
BioGrid; 204015; 105.
CORUM; P15806; -.
DIP; DIP-30940N; -.
IntAct; P15806; 15.
MINT; MINT-218641; -.
STRING; 10090.ENSMUSP00000100979; -.
iPTMnet; P15806; -.
PhosphoSitePlus; P15806; -.
MaxQB; P15806; -.
PaxDb; P15806; -.
PRIDE; P15806; -.
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.
eggNOG; ENOG410XYUA; LUCA.
GeneTree; ENSGT00510000046438; -.
HOVERGEN; HBG003854; -.
InParanoid; P15806; -.
KO; K09063; -.
PhylomeDB; P15806; -.
Reactome; R-MMU-375170; CDO in myogenesis.
Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
ChiTaRS; Tcf3; mouse.
EvolutionaryTrace; P15806; -.
PRO; PR:P15806; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000020167; -.
CleanEx; MM_ME2; -.
CleanEx; MM_TCF3; -.
CleanEx; MM_TCFE2A; -.
ExpressionAtlas; P15806; baseline and differential.
Genevisible; P15806; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0000788; C:nuclear nucleosome; IDA:MGI.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:NTNU_SB.
GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
GO; GO:0043425; F:bHLH transcription factor binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA: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:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IMP:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; IMP:NTNU_SB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
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: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 from RNA polymerase II promoter; ISO:MGI.
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:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
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 from RNA polymerase II promoter; 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:0006351; P:transcription, DNA-templated; ISO:MGI.
CDD; cd00083; HLH; 1.
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; Complete proteome;
Differentiation; DNA-binding; Isopeptide bond; Methylation;
Neurogenesis; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 651 Transcription factor E2-alpha.
/FTId=PRO_0000127468.
DOMAIN 546 599 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 387 422 Leucine-zipper.
MOD_RES 135 135 Phosphoserine.
{ECO:0000250|UniProtKB:P15923}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000250|UniProtKB:P15923}.
MOD_RES 353 353 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 357 357 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 369 369 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000250|UniProtKB:P15923}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000250|UniProtKB:P15923}.
CROSSLNK 496 496 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P15923}.
CROSSLNK 622 622 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P15923}.
VAR_SEQ 527 598 PDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFK
ELGRMCQLHLSSEKPQTKLLILHQAVAVILS -> STDEVL
SLEEKDLRDRERRMANNARERVRVRDINEAFRELGRMCQLH
LKSDKAQTKLLILQQAVQVILG (in isoform E47).
{ECO:0000303|PubMed:11309385,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:2181401}.
/FTId=VSP_011354.
VARIANT 387 387 L -> LQ. {ECO:0000269|PubMed:8112613}.
CONFLICT 156 156 S -> N (in Ref. 1; AAK18618).
{ECO:0000305}.
CONFLICT 164 164 D -> N (in Ref. 1; AAK18618).
{ECO:0000305}.
CONFLICT 167 167 L -> LA (in Ref. 3; AAH18260).
{ECO:0000305}.
CONFLICT 294 294 P -> T (in Ref. 2; BAB30842).
{ECO:0000305}.
CONFLICT 633 633 A -> P (in Ref. 3; AAH06860).
{ECO:0000305}.
HELIX 548 574 {ECO:0000244|PDB:2QL2}.
HELIX 585 602 {ECO:0000244|PDB:2QL2}.
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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