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Transcription factor E2-alpha (Class B basic helix-loop-helix protein 21) (bHLHb21) (Immunoglobulin enhancer-binding factor E12/E47) (Immunoglobulin transcription factor 1) (Kappa-E2-binding factor) (Transcription factor 3) (TCF-3) (Transcription factor ITF-1)

 TFE2_HUMAN              Reviewed;         654 AA.
P15923; P15883; Q14208; Q14635; Q14636; Q2TB39; Q2TB40; Q9UPI9;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
25-OCT-2017, entry version 207.
RecName: Full=Transcription factor E2-alpha;
AltName: Full=Class B basic helix-loop-helix protein 21;
Short=bHLHb21;
AltName: Full=Immunoglobulin enhancer-binding factor E12/E47;
AltName: Full=Immunoglobulin transcription factor 1;
AltName: Full=Kappa-E2-binding factor;
AltName: Full=Transcription factor 3;
Short=TCF-3;
AltName: Full=Transcription factor ITF-1;
Name=TCF3; Synonyms=BHLHB21, E2A, ITF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E12), AND CHROMOSOMAL
TRANSLOCATION WITH PBX1.
PubMed=1967983; DOI=10.1016/0092-8674(90)90658-2;
Kamps M.P., Murre C., Sun X.-H., Baltimore D.;
"A new homeobox gene contributes the DNA binding domain of the t(1;19)
translocation protein in pre-B ALL.";
Cell 60:547-555(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E12).
PubMed=1967982; DOI=10.1016/0092-8674(90)90657-Z;
Nourse J., Mellentin J.D., Galili N., Wilkinson J., Stanbridge E.,
Smith S.D., Cleary M.L.;
"Chromosomal translocation t(1;19) results in synthesis of a homeobox
fusion mRNA that codes for a potential chimeric transcription
factor.";
Cell 60:535-545(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS E47 AND 3).
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 214-654 (ISOFORMS E12 AND E47), AND
DOMAIN BHLH.
TISSUE=Lymphoma;
PubMed=2493990; DOI=10.1016/0092-8674(89)90682-X;
Murre C., McCaw P.S., Baltimore D.;
"A new DNA binding and dimerization motif in immunoglobulin enhancer
binding, daughterless, MyoD, and myc proteins.";
Cell 56:777-783(1989).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 69-654 (ISOFORM E47).
PubMed=2308859; DOI=10.1093/nar/18.3.677;
Henthorn P., McCarrick-Walmsley R., Kadesch T.;
"Sequence of the cDNA encoding ITF-1, a positive-acting transcription
factor.";
Nucleic Acids Res. 18:677-677(1990).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 511-654 (ISOFORM E47).
PubMed=1818757; DOI=10.3109/10425179109039690;
Zhang Y., Bina M.;
"Sequence of a HeLa cDNA provides the DNA binding domain and carboxy
terminus of HE47: a human helix-loop-helix protein related to the
enhancer binding factor E47.";
DNA Seq. 2:197-202(1991).
[8]
DISCUSSION OF SEQUENCE.
PubMed=2105528; DOI=10.1126/science.2105528;
Henthorn P., Kiledjian M., Kadesch T.;
"Two distinct transcription factors that bind the immunoglobulin
enhancer microE5/kappa 2 motif.";
Science 247:467-470(1990).
[9]
MUTAGENESIS, DNA-BINDING, AND HOMODIMERIZATION.
PubMed=2112746; DOI=10.1073/pnas.87.12.4722;
Voronova A., Baltimore D.;
"Mutations that disrupt DNA binding and dimer formation in the E47
helix-loop-helix protein map to distinct domains.";
Proc. Natl. Acad. Sci. U.S.A. 87:4722-4726(1990).
[10]
CHROMOSOMAL TRANSLOCATION WITH PBX1.
PubMed=1671560;
Hunger S.P., Galili N., Carroll A.J., Crist W.M., Link M.P.,
Cleary M.L.;
"The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1
coding sequences in acute lymphoblastic leukemias.";
Blood 77:687-693(1991).
[11]
CHROMOSOMAL TRANSLOCATION WITH HLF.
PubMed=1386162; DOI=10.1126/science.1386162;
Inaba T., Roberts W.M., Shapiro L.H., Jolly K.W., Raimondi S.C.,
Smith S.D., Look A.T.;
"Fusion of the leucine zipper gene HLF to the E2A gene in human acute
B-lineage leukemia.";
Science 257:531-534(1992).
[12]
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).
[13]
CHROMOSOMAL TRANSLOCATION WITH TFPT.
PubMed=10086727; DOI=10.1038/sj/leu/2401338;
Brambillasca F., Mosna G., Colombo M., Rivolta A., Caslini C.,
Minuzzo M., Giudici G., Mizzi L., Biondi A., Privitera E.;
"Identification of a novel molecular partner of the E2A gene in
childhood leukemia.";
Leukemia 13:369-375(1999).
[14]
INTERACTION WITH NEUROD1 AND EP300, HOMODIMERIZATION, AND
HETERODIMERIZATION.
PubMed=14752053; DOI=10.1210/me.2003-0311;
Kim J.Y., Chu K., Kim H.J., Seong H.A., Park K.C., Sanyal S.,
Takeda J., Ha H., Shong M., Tsai M.J., Choi H.S.;
"Orphan nuclear receptor small heterodimer partner, a novel
corepressor for a basic helix-loop-helix transcription factor
BETA2/neuroD.";
Mol. Endocrinol. 18:776-790(2004).
[15]
INTERACTION WITH FIGLA.
PubMed=15044608; DOI=10.1093/molehr/gah056;
Bayne R.A.L., Martins da Silva S.J., Anderson R.A.;
"Increased expression of the FIGLA transcription factor is associated
with primordial follicle formation in the human fetal ovary.";
Mol. Hum. Reprod. 10:373-381(2004).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-531 (ISOFORM E47), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND SER-359, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379 AND SER-529, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
INTERACTION WITH BHLHA9.
PubMed=25466284; DOI=10.1016/j.ajhg.2014.10.012;
Malik S., Percin F.E., Bornholdt D., Albrecht B., Percesepe A.,
Koch M.C., Landi A., Fritz B., Khan R., Mumtaz S., Akarsu N.A.,
Grzeschik K.H.;
"Mutations affecting the BHLHA9 DNA-binding domain cause MSSD,
mesoaxial synostotic syndactyly with phalangeal reduction, Malik-
Percin type.";
Am. J. Hum. Genet. 95:649-659(2014).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-498, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-498, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-498 AND LYS-625, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[26]
3D-STRUCTURE MODELING OF 549-610.
PubMed=8433970; DOI=10.1093/protein/6.1.41;
Gibson T.J., Thompson J.D., Abagyan R.A.;
"Proposed structure for the DNA-binding domain of the helix-loop-helix
family of eukaryotic gene regulatory proteins.";
Protein Eng. 6:41-50(1993).
[27]
VARIANT [LARGE SCALE ANALYSIS] VAL-8.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[28]
DOMAIN.
PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P.,
Piskacek M.;
"Nine-amino-acid transactivation domain: establishment and prediction
utilities.";
Genomics 89:756-768(2007).
[29]
INVOLVEMENT IN AGM8, VARIANT AGM8 LYS-555 (ISOFORM E47), AND
CHARACTERIZATION OF VARIANT AGM8 (ISOFORM E47) LYS-555.
PubMed=24216514; DOI=10.1172/JCI71927;
Boisson B., Wang Y.D., Bosompem A., Ma C.S., Lim A., Kochetkov T.,
Tangye S.G., Casanova J.L., Conley M.E.;
"A recurrent dominant negative E47 mutation causes agammaglobulinemia
and BCR(-) B cells.";
J. Clin. Invest. 123:4781-4786(2013).
-!- 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:0000250|UniProtKB:P15806}.
-!- SUBUNIT: Forms a heterodimer with ASH1 and TWIST2. Isoform E12
interacts with RALGAPA1 and FIGLA. Efficient DNA binding requires
dimerization with another bHLH protein. Component of a nuclear
TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3.
Interacts with NEUROD2, PTF1A and TGFB1I1. Forms a heterodimer
with MYOG; heterodimerization enhances MYOG DNA-binding and
transcriptional activities (By similarity). Homodimer.
Heterodimer. Forms a heterodimer with NEUROD1; the heterodimer is
inhibited in presence of ID2, but not NR0B2, to E-box element.
Interacts with EP300 and UBE2I. Interacts with BHLHA9
(PubMed:25466284). Forms a heterodimer with ATOH8; repress
transcription of TCF3 and TCF3/NEUROG3 dimer-induced
transactivation of E box-dependent promoters (By similarity).
{ECO:0000250|UniProtKB:P15806, ECO:0000269|PubMed:14752053,
ECO:0000269|PubMed:15044608, ECO:0000269|PubMed:25466284,
ECO:0000269|PubMed:9409784}.
-!- INTERACTION:
P50553:ASCL1; NbExp=3; IntAct=EBI-769630, EBI-957042;
O95273:CCNDBP1; NbExp=3; IntAct=EBI-769645, EBI-748961;
O75593:FOXH1; NbExp=2; IntAct=EBI-769630, EBI-1759806;
Q02363:ID2; NbExp=3; IntAct=EBI-769645, EBI-713450;
Q02535:ID3; NbExp=3; IntAct=EBI-769630, EBI-1387094;
P15172:MYOD1; NbExp=2; IntAct=EBI-769645, EBI-488878;
P17542:TAL1; NbExp=7; IntAct=EBI-769630, EBI-1753878;
Q9Y4C2:TCAF1; NbExp=3; IntAct=EBI-769630, EBI-750484;
Q8WVJ9:TWIST2; NbExp=4; IntAct=EBI-12000326, EBI-1797313;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=E12; Synonyms=PAN-2;
IsoId=P15923-1; Sequence=Displayed;
Name=E47; Synonyms=PAN-1;
IsoId=P15923-2; Sequence=VSP_002155;
Note=The bHLH domain encompassing amino acids 546 to 599 is
sufficient to mediate DNA-binding and homodimerization. Combined
mutagenesis of Phe-566 and Leu-569 to Asp-566 and Glu-569,
mutagenesis of Lys-585 to Ala-585 or combined mutagenesis of
Ile-588 and Leu-589 to Asp-588 and Glu-589 prevents DNA-binding
and homodimerization. Mutagenesis of Arg-548 to Lys-548,
combined mutagenesis of Arg-547 and Arg-548 to Gly-547 and
Gly-548, mutagenesis of Arg-556 to Lys-556, mutagenesis of
Arg-558 to Lys-558, or combined mutagenesis of Arg-556 and
Arg-558 to Gly-556 and Gly-558, alter DNA-binding but not
dimerization. Variant in position: 555:E->K (in AGM8, localizes
normally to the nucleus, does not perform proper DNA binding,
acts in a dominant-negative manner when coexpressed with
wild-type) (Ref.29). Contains a phosphothreonine at position
531. {ECO:0000244|PubMed:18669648, ECO:0000269|PubMed:24216514};
Name=3;
IsoId=P15923-3; Sequence=VSP_057277, VSP_057278;
Note=No experimental confirmation available.;
-!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a
large number of yeast and animal transcription factors.
{ECO:0000269|PubMed:17467953, ECO:0000269|PubMed:2493990}.
-!- PTM: Phosphorylated following NGF stimulation. {ECO:0000250}.
-!- DISEASE: Note=Chromosomal aberrations involving TCF3 are cause of
forms of pre-B-cell acute lymphoblastic leukemia (B-ALL).
Translocation t(1;19)(q23;p13.3) with PBX1. TCF3-PBX1 transforms
cells by constitutively activating transcription of genes
regulated by PBX1 or by other members of the PBX protein family
(PubMed:1967983, PubMed:1671560). Translocation
t(17;19)(q22;p13.3) with HLF (PubMed:1386162). Inversion
inv(19)(p13;q13) with TFPT (PubMed:10086727).
{ECO:0000269|PubMed:10086727, ECO:0000269|PubMed:1386162,
ECO:0000269|PubMed:1671560, ECO:0000269|PubMed:1967983}.
-!- DISEASE: Agammaglobulinemia 8, autosomal dominant (AGM8)
[MIM:616941]: A form of agammaglobulinemia, a primary
immunodeficiency characterized by profoundly low or absent serum
antibodies and low or absent circulating B-cells due to an early
block of B-cell development. Affected individuals develop severe
infections in the first years of life.
{ECO:0000269|PubMed:24216514}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAA52331.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/E2AID50.html";
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EMBL; M31523; AAA61146.1; -; mRNA.
EMBL; M31522; AAA36764.1; ALT_TERM; mRNA.
EMBL; M31222; AAA52331.1; ALT_INIT; mRNA.
EMBL; AC006274; AAC99797.1; -; Genomic_DNA.
EMBL; AC005321; AAC27373.1; -; Genomic_DNA.
EMBL; KC877695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC110579; AAI10580.1; -; mRNA.
EMBL; BC110580; AAI10581.1; -; mRNA.
EMBL; M24404; AAA56829.1; -; mRNA.
EMBL; M24405; AAA56830.1; -; mRNA.
EMBL; X52078; CAA36297.1; -; mRNA.
EMBL; M65214; AAC41693.1; -; mRNA.
CCDS; CCDS12074.1; -. [P15923-1]
CCDS; CCDS45899.1; -. [P15923-2]
PIR; A34734; A34734.
PIR; S10099; S10099.
RefSeq; NP_001129611.1; NM_001136139.2. [P15923-2]
RefSeq; NP_003191.1; NM_003200.3. [P15923-1]
RefSeq; XP_016882669.1; XM_017027180.1. [P15923-3]
RefSeq; XP_016882670.1; XM_017027181.1. [P15923-1]
RefSeq; XP_016882671.1; XM_017027182.1. [P15923-2]
UniGene; Hs.371282; -.
UniGene; Hs.657044; -.
PDB; 1HLH; Model; -; A/B=549-610.
PDB; 2MH0; NMR; -; A=1-37.
PDB; 2YPA; X-ray; 2.80 A; B=546-616.
PDB; 2YPB; X-ray; 2.87 A; B=546-616.
PDB; 3U5V; X-ray; 1.70 A; A=563-613.
PDBsum; 1HLH; -.
PDBsum; 2MH0; -.
PDBsum; 2YPA; -.
PDBsum; 2YPB; -.
PDBsum; 3U5V; -.
ProteinModelPortal; P15923; -.
SMR; P15923; -.
BioGrid; 112791; 158.
CORUM; P15923; -.
DIP; DIP-74N; -.
IntAct; P15923; 30.
MINT; MINT-190187; -.
STRING; 9606.ENSP00000262965; -.
iPTMnet; P15923; -.
PhosphoSitePlus; P15923; -.
BioMuta; TCF3; -.
DMDM; 135655; -.
EPD; P15923; -.
MaxQB; P15923; -.
PaxDb; P15923; -.
PeptideAtlas; P15923; -.
PRIDE; P15923; -.
Ensembl; ENST00000262965; ENSP00000262965; ENSG00000071564. [P15923-1]
Ensembl; ENST00000395423; ENSP00000378813; ENSG00000071564. [P15923-3]
Ensembl; ENST00000588136; ENSP00000468487; ENSG00000071564. [P15923-2]
Ensembl; ENST00000611869; ENSP00000480564; ENSG00000071564. [P15923-1]
GeneID; 6929; -.
KEGG; hsa:6929; -.
UCSC; uc002ltr.3; human. [P15923-1]
CTD; 6929; -.
DisGeNET; 6929; -.
EuPathDB; HostDB:ENSG00000071564.14; -.
GeneCards; TCF3; -.
HGNC; HGNC:11633; TCF3.
HPA; CAB018351; -.
HPA; HPA049808; -.
HPA; HPA062476; -.
MalaCards; TCF3; -.
MIM; 147141; gene.
MIM; 616941; phenotype.
neXtProt; NX_P15923; -.
OpenTargets; ENSG00000071564; -.
Orphanet; 33110; Autosomal agammaglobulinemia.
Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
PharmGKB; PA164742580; -.
eggNOG; KOG3910; Eukaryota.
eggNOG; ENOG410XYUA; LUCA.
GeneTree; ENSGT00510000046438; -.
HOGENOM; HOG000234180; -.
HOVERGEN; HBG003854; -.
InParanoid; P15923; -.
KO; K09063; -.
OMA; KGGSQYY; -.
PhylomeDB; P15923; -.
TreeFam; TF321672; -.
Reactome; R-HSA-375170; CDO in myogenesis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
SignaLink; P15923; -.
SIGNOR; P15923; -.
ChiTaRS; TCF3; human.
GeneWiki; TCF3; -.
GenomeRNAi; 6929; -.
PRO; PR:P15923; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000071564; -.
CleanEx; HS_TCF3; -.
ExpressionAtlas; P15923; baseline and differential.
Genevisible; P15923; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL.
GO; GO:0005667; C:transcription factor complex; IDA:UniProtKB.
GO; GO:0043425; F:bHLH transcription factor binding; IPI:BHF-UCL.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
GO; GO:0035326; F:enhancer binding; IC:BHF-UCL.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0070644; F:vitamin D response element binding; IDA:BHF-UCL.
GO; GO:0030183; P:B cell differentiation; NAS:UniProtKB.
GO; GO:0002326; P:B cell lineage commitment; IDA:UniProtKB.
GO; GO:0033152; P:immunoglobulin V(D)J recombination; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
GO; GO:0045787; P:positive regulation of cell cycle; IDA:UniProtKB.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA: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:2000045; P:regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
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; Chromosomal rearrangement;
Complete proteome; Differentiation; Disease mutation; DNA-binding;
Isopeptide bond; Methylation; Neurogenesis; Nucleus; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 654 Transcription factor E2-alpha.
/FTId=PRO_0000127466.
DOMAIN 549 602 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 389 425 Leucine-zipper.
MOTIF 19 27 9aaTAD.
MOTIF 170 176 Nuclear localization signal.
{ECO:0000255}.
SITE 483 484 Breakpoint for translocation to form
TCF3-PBX1 oncogene.
MOD_RES 134 134 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 355 355 Phosphothreonine.
{ECO:0000250|UniProtKB:P15806}.
MOD_RES 359 359 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 371 371 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P15806}.
MOD_RES 379 379 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 529 529 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 498 498 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 625 625 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 49 99 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057277.
VAR_SEQ 528 528 T -> TRCQPTPRHSPPSPHQDAHVHRPHAHRTHTGRPSAG
PTLFPQPHCLPLAPSRRPPH (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057278.
VAR_SEQ 530 601 PDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFK
ELGRMCQLHLNSEKPQTKLLILHQAVSVILN -> STDEVL
SLEEKDLRDRERRMANNARERVRVRDINEAFRELGRMCQMH
LKSDKAQTKLLILQQAVQVILG (in isoform E47).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1818757,
ECO:0000303|PubMed:2308859,
ECO:0000303|PubMed:2493990}.
/FTId=VSP_002155.
VARIANT 8 8 A -> V (in a colorectal cancer sample;
somatic mutation; dbSNP:rs376780559).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036396.
VARIANT 120 120 L -> P (in dbSNP:rs35354874).
/FTId=VAR_049552.
VARIANT 198 198 T -> A (in dbSNP:rs11879402).
/FTId=VAR_049553.
VARIANT 431 431 G -> S (in dbSNP:rs1052692).
/FTId=VAR_049554.
CONFLICT 69 99 FDPSRTFSEGTHFTESHSSLSSSTFLGPGLG -> GGGECL
AWCGPSAVHRCADVGLGMVSARTAP (in Ref. 6;
CAA36297). {ECO:0000305}.
CONFLICT 214 216 FYV -> EFR (in Ref. 5; AAA56830).
{ECO:0000305}.
CONFLICT 302 302 Missing (in Ref. 1; AAA36764).
{ECO:0000305}.
CONFLICT 390 390 Missing (in Ref. 5; AAA56830).
{ECO:0000305}.
HELIX 12 25 {ECO:0000244|PDB:2MH0}.
HELIX 563 580 {ECO:0000244|PDB:3U5V}.
HELIX 588 608 {ECO:0000244|PDB:3U5V}.
SEQUENCE 654 AA; 67600 MW; 52F5E3DE1890AE13 CRC64;
MNQPQRMAPV GTDKELSDLL DFSMMFPLPV TNGKGRPASL AGAQFGGSGL EDRPSSGSWG
SGDQSSSSFD PSRTFSEGTH FTESHSSLSS STFLGPGLGG KSGERGAYAS FGRDAGVGGL
TQAGFLSGEL ALNSPGPLSP SGMKGTSQYY PSYSGSSRRR AADGSLDTQP KKVRKVPPGL
PSSVYPPSSG EDYGRDATAY PSAKTPSSTY PAPFYVADGS LHPSAELWSP PGQAGFGPML
GGGSSPLPLP PGSGPVGSSG SSSTFGGLHQ HERMGYQLHG AEVNGGLPSA SSFSSAPGAT
YGGVSSHTPP VSGADSLLGS RGTTAGSSGD ALGKALASIY SPDHSSNNFS SSPSTPVGSP
QGLAGTSQWP RAGAPGALSP SYDGGLHGLQ SKIEDHLDEA IHVLRSHAVG TAGDMHTLLP
GHGALASGFT GPMSLGGRHA GLVGGSHPED GLAGSTSLMH NHAALPSQPG TLPDLSRPPD
SYSGLGRAGA TAAASEIKRE EKEDEENTSA ADHSEEEKKE LKAPRARTSP DEDEDDLLPP
EQKAEREKER RVANNARERL RVRDINEAFK ELGRMCQLHL NSEKPQTKLL ILHQAVSVIL
NLEQQVRERN LNPKAACLKR REEEKVSGVV GDPQMVLSAP HPGLSEAHNP AGHM


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