P15923 (TFE2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor E2-alpha

Alternative name(s):
Class B basic helix-loop-helix protein 21
Short name=bHLHb21
Immunoglobulin enhancer-binding factor E12/E47
Immunoglobulin transcription factor 1
Kappa-E2-binding factor
Transcription factor 3
Short name=TCF-3
Transcription factor ITF-1

Gene names

Name:	TCF3
Synonyms:	BHLHB21, E2A, ITF1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	654 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	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 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. Ref.9 Ref.12 Ref.14 Ref.15
Subcellular location	Nucleus.
Domain	the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. Ref.5 Ref.23
Post-translational modification	Phosphorylated following NGF stimulation By similarity.
Involvement in disease	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. Translocation t(17;19)(q22;p13.3) with HLF. Inversion inv19(p13;q13) with TFPT.
Sequence similarities	Contains 1 bHLH (basic helix-loop-helix) domain.
Sequence caution	The sequence AAA52331.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell lineage commitment Inferred from direct assay PubMed 15030778. Source: UniProtKB G1 phase of mitotic cell cycle Inferred from direct assay PubMed 11509675. Source: UniProtKB Peyer's patch development Inferred from electronic annotation. Source: Compara T cell differentiation in thymus Inferred from electronic annotation. Source: Compara cell development Inferred from electronic annotation. Source: Compara histone H3 acetylation Inferred from electronic annotation. Source: Compara histone H4 acetylation Inferred from electronic annotation. Source: Compara immunoglobulin V(D)J recombination Inferred from direct assay PubMed 16428437. Source: MGI muscle cell differentiation Traceable author statement. Source: Reactome natural killer cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of B cell proliferation Inferred from mutant phenotype PubMed 11509675. Source: UniProtKB positive regulation of cell cycle Inferred from direct assay PubMed 11509675. Source: UniProtKB positive regulation of muscle cell differentiation Traceable author statement. Source: Reactome positive regulation of neuron differentiation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay Ref.14. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 16043483PubMed 16043483. Source: BHF-UCL protein stabilization Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from direct assay PubMed 10775504. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay PubMed 12435739. Source: UniProtKB nuclear nucleosome Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 12435739. Source: UniProtKB protein complex Inferred from direct assay PubMed 12435739. Source: UniProtKB transcription factor complex Inferred from direct assay PubMed 10775504Ref.15PubMed 2503252. Source: UniProtKB
Molecular_function	DNA binding Inferred from direct assay PubMed 8759016. Source: UniProtKB E-box binding Inferred from direct assay PubMed 7933101. Source: UniProtKB chromatin binding Inferred from electronic annotation. Source: Compara protein heterodimerization activity Inferred from direct assay PubMed 10775504Ref.14. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 10958665Ref.14PubMed 8759016. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 11802795PubMed 15509787. Source: BHF-UCL transcription coactivator activity Inferred from direct assay Ref.14. Source: UniProtKB vitamin D response element binding Inferred from direct assay PubMed 17426122. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ASCL1	P50553	3	EBI-769630,EBI-957042
CCNDBP1	O95273	3	EBI-769645,EBI-748961
ID2	Q02363	3	EBI-769645,EBI-713450
MYOD1	P15172	2	EBI-769645,EBI-488878
TAL1	P17542	4	EBI-769630,EBI-1753878

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform E12 (identifier: P15923-1)

Also known as: PAN-2;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform E47 (identifier: P15923-2)

Also known as: PAN-1;

The sequence of this isoform differs from the canonical sequence as follows:
     530-601: PDEDEDDLLP...LHQAVSVILN → STDEVLSLEE...LQQAVQVILG

Note: Contains a phosphothreonine at position 531. 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 654

654

Transcription factor E2-alpha

PRO_0000127466

Regions

Domain

549 – 602

54

bHLH

Region

389 – 425

37

Leucine-zipper

Motif

19 – 27

9

9aaTAD

Motif

170 – 176

7

Nuclear localization signal Potential

Sites

Site

483 – 484

2

Breakpoint for translocation to form TCF3-PBX1 oncogene

Amino acid modifications

Modified residue

134

1

Phosphoserine Ref.19

Modified residue

139

1

Phosphoserine Ref.18

Modified residue

359

1

Phosphoserine Ref.18

Natural variations

Alternative sequence

530 – 601

72

PDEDE…SVILN → STDEVLSLEEKDLRDRERRM ANNARERVRVRDINEAFREL GRMCQMHLKSDKAQTKLLIL QQAVQVILG in isoform E47.

VSP_002155

Natural variant

8

1

A → V in a colorectal cancer sample; somatic mutation. Ref.22

VAR_036396

Natural variant

120

1

L → P.
Corresponds to variant rs35354874 [ dbSNP | Ensembl ].

VAR_049552

Natural variant

198

1

T → A.
Corresponds to variant rs11879402 [ dbSNP | Ensembl ].

VAR_049553

Natural variant

431

1

G → S.
Corresponds to variant rs1052692 [ dbSNP | Ensembl ].

VAR_049554

Experimental info

Sequence conflict

69 – 99

31

FDPSR…GPGLG → GGGECLAWCGPSAVHRCADV GLGMVSARTAP in CAA36297. Ref.6

Sequence conflict

214 – 216

3

FYV → EFR in AAA56830. Ref.5

Sequence conflict

302

1

Missing in AAA36764. Ref.1

Sequence conflict

390

1

Missing in AAA56830. Ref.5

Secondary structure

1

.

.

.

.

.

654

Helix Strand Turn

Details...

Helix

563 – 580

18

Helix

588 – 608

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform E12 (PAN-2) [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 52F5E3DE1890AE13	FASTA	654	67,600
	10 20 30 40 50 60 MNQPQRMAPV GTDKELSDLL DFSMMFPLPV TNGKGRPASL AGAQFGGSGL EDRPSSGSWG 70 80 90 100 110 120 SGDQSSSSFD PSRTFSEGTH FTESHSSLSS STFLGPGLGG KSGERGAYAS FGRDAGVGGL 130 140 150 160 170 180 TQAGFLSGEL ALNSPGPLSP SGMKGTSQYY PSYSGSSRRR AADGSLDTQP KKVRKVPPGL 190 200 210 220 230 240 PSSVYPPSSG EDYGRDATAY PSAKTPSSTY PAPFYVADGS LHPSAELWSP PGQAGFGPML 250 260 270 280 290 300 GGGSSPLPLP PGSGPVGSSG SSSTFGGLHQ HERMGYQLHG AEVNGGLPSA SSFSSAPGAT 310 320 330 340 350 360 YGGVSSHTPP VSGADSLLGS RGTTAGSSGD ALGKALASIY SPDHSSNNFS SSPSTPVGSP 370 380 390 400 410 420 QGLAGTSQWP RAGAPGALSP SYDGGLHGLQ SKIEDHLDEA IHVLRSHAVG TAGDMHTLLP 430 440 450 460 470 480 GHGALASGFT GPMSLGGRHA GLVGGSHPED GLAGSTSLMH NHAALPSQPG TLPDLSRPPD 490 500 510 520 530 540 SYSGLGRAGA TAAASEIKRE EKEDEENTSA ADHSEEEKKE LKAPRARTSP DEDEDDLLPP 550 560 570 580 590 600 EQKAEREKER RVANNARERL RVRDINEAFK ELGRMCQLHL NSEKPQTKLL ILHQAVSVIL 610 620 630 640 650 NLEQQVRERN LNPKAACLKR REEEKVSGVV GDPQMVLSAP HPGLSEAHNP AGHM
	Isoform E47 (PAN-1) [UniParc]. Checksum: F5F11C462351FFD6	FASTA	651	67,265
	10 20 30 40 50 60 MNQPQRMAPV GTDKELSDLL DFSMMFPLPV TNGKGRPASL AGAQFGGSGL EDRPSSGSWG 70 80 90 100 110 120 SGDQSSSSFD PSRTFSEGTH FTESHSSLSS STFLGPGLGG KSGERGAYAS FGRDAGVGGL 130 140 150 160 170 180 TQAGFLSGEL ALNSPGPLSP SGMKGTSQYY PSYSGSSRRR AADGSLDTQP KKVRKVPPGL 190 200 210 220 230 240 PSSVYPPSSG EDYGRDATAY PSAKTPSSTY PAPFYVADGS LHPSAELWSP PGQAGFGPML 250 260 270 280 290 300 GGGSSPLPLP PGSGPVGSSG SSSTFGGLHQ HERMGYQLHG AEVNGGLPSA SSFSSAPGAT 310 320 330 340 350 360 YGGVSSHTPP VSGADSLLGS RGTTAGSSGD ALGKALASIY SPDHSSNNFS SSPSTPVGSP 370 380 390 400 410 420 QGLAGTSQWP RAGAPGALSP SYDGGLHGLQ SKIEDHLDEA IHVLRSHAVG TAGDMHTLLP 430 440 450 460 470 480 GHGALASGFT GPMSLGGRHA GLVGGSHPED GLAGSTSLMH NHAALPSQPG TLPDLSRPPD 490 500 510 520 530 540 SYSGLGRAGA TAAASEIKRE EKEDEENTSA ADHSEEEKKE LKAPRARTSS TDEVLSLEEK 550 560 570 580 590 600 DLRDRERRMA NNARERVRVR DINEAFRELG RMCQMHLKSD KAQTKLLILQ QAVQVILGLE 610 620 630 640 650 QQVRERNLNP KAACLKRREE EKVSGVVGDP QMVLSAPHPG LSEAHNPAGH M

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new homeobox gene contributes the DNA binding domain of the t(1;19) translocation protein in pre-B ALL." Kamps M.P., Murre C., Sun X.-H., Baltimore D. Cell 60:547-555(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E12), CHROMOSOMAL TRANSLOCATION WITH PBX1.
[2]	"Chromosomal translocation t(1;19) results in synthesis of a homeobox fusion mRNA that codes for a potential chimeric transcription factor." Nourse J., Mellentin J.D., Galili N., Wilkinson J., Stanbridge E., Smith S.D., Cleary M.L. Cell 60:535-545(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E12).
[3]	"The DNA sequence and biology of human chromosome 19." 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. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E47).
[5]	"A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins." Murre C., McCaw P.S., Baltimore D. Cell 56:777-783(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 214-654 (ISOFORMS E12 AND E47), DOMAIN BHLH. Tissue: Lymphoma.
[6]	"Sequence of the cDNA encoding ITF-1, a positive-acting transcription factor." Henthorn P., McCarrick-Walmsley R., Kadesch T. Nucleic Acids Res. 18:677-677(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-654 (ISOFORM E47).
[7]	"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." Zhang Y., Bina M. DNA Seq. 2:197-202(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 511-654 (ISOFORM E47).
[8]	"Two distinct transcription factors that bind the immunoglobulin enhancer microE5/kappa 2 motif." Henthorn P., Kiledjian M., Kadesch T. Science 247:467-470(1990) [PubMed] [Europe PMC] [Abstract] Cited for: DISCUSSION OF SEQUENCE.
[9]	"Mutations that disrupt DNA binding and dimer formation in the E47 helix-loop-helix protein map to distinct domains." Voronova A., Baltimore D. Proc. Natl. Acad. Sci. U.S.A. 87:4722-4726(1990) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS, DNA-BINDING, HOMODIMERIZATION.
[10]	"The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1 coding sequences in acute lymphoblastic leukemias." Hunger S.P., Galili N., Carroll A.J., Crist W.M., Link M.P., Cleary M.L. Blood 77:687-693(1991) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH PBX1.
[11]	"Fusion of the leucine zipper gene HLF to the E2A gene in human acute B-lineage leukemia." Inaba T., Roberts W.M., Shapiro L.H., Jolly K.W., Raimondi S.C., Smith S.D., Look A.T. Science 257:531-534(1992) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH HLF.
[12]	"The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A transcription factors." Loveys D.A., Streiff M.B., Schaefer T.S., Kato G.J. Gene 201:169-177(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UBE2I.
[13]	"Identification of a novel molecular partner of the E2A gene in childhood leukemia." Brambillasca F., Mosna G., Colombo M., Rivolta A., Caslini C., Minuzzo M., Giudici G., Mizzi L., Biondi A., Privitera E. Leukemia 13:369-375(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH TFPT.
[14]	"Orphan nuclear receptor small heterodimer partner, a novel corepressor for a basic helix-loop-helix transcription factor BETA2/neuroD." 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. Mol. Endocrinol. 18:776-790(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NEUROD1 AND EP300, HOMODIMERIZATION, HETERODIMERIZATION.
[15]	"Increased expression of the FIGLA transcription factor is associated with primordial follicle formation in the human fetal ovary." Bayne R.A.L., Martins da Silva S.J., Anderson R.A. Mol. Hum. Reprod. 10:373-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FIGLA.
[16]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-531 (ISOFORM E47), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND SER-359, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"Proposed structure for the DNA-binding domain of the helix-loop-helix family of eukaryotic gene regulatory proteins." Gibson T.J., Thompson J.D., Abagyan R.A. Protein Eng. 6:41-50(1993) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 549-610.
[22]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-8.
[23]	"Nine-amino-acid transactivation domain: establishment and prediction utilities." Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M. Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M31523 mRNA. Translation: AAA61146.1.
M31522 mRNA. Translation: AAA36764.1. Different termination.
M31222 mRNA. Translation: AAA52331.1. Different initiation.
AC006274 Genomic DNA. Translation: AAC99797.1.
AC005321 Genomic DNA. Translation: AAC27373.1.
BC110579 mRNA. Translation: AAI10580.1.
M24404 mRNA. Translation: AAA56829.1.
M24405 mRNA. Translation: AAA56830.1.
X52078 mRNA. Translation: CAA36297.1.
M65214 mRNA. Translation: AAC41693.1.

IPI

IPI00013929.
IPI00216911.

PIR

A34734.
S10099.

RefSeq

NP_001129611.1. NM_001136139.2.
NP_003191.1. NM_003200.3.

UniGene

Hs.371282.
Hs.657044.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HLH	model	-	A/B	549-610	[»]
3U5V	X-ray	1.70	A	563-610	[»]

ProteinModelPortal

P15923.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-74N.

IntAct

P15923. 16 interactions.

STRING

9606.ENSP00000262965.

PTM databases

PhosphoSite

P15923.

Polymorphism databases

DMDM

135655.

Proteomic databases

PaxDb

P15923.

PRIDE

P15923.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262965; ENSP00000262965; ENSG00000071564.
ENST00000344749; ENSP00000344375; ENSG00000071564.
ENST00000585731; ENSP00000465510; ENSG00000071564.
ENST00000588136; ENSP00000468487; ENSG00000071564.

GeneID

6929.

KEGG

hsa:6929.

UCSC

uc002lto.3. human.
uc002lts.1. human.

Organism-specific databases

CTD

6929.

GeneCards

GC19M001609.

HGNC

HGNC:11633. TCF3.

HPA

CAB018351.

MIM

147141. gene.

neXtProt

NX_P15923.

Orphanet

99860. Precursor B-cell acute lymphoblastic leukemia.

PharmGKB

PA164742580.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG282899.

HOVERGEN

HBG003854.

KO

K09063.

PhylomeDB

P15923.

Enzyme and pathway databases

Pathway_Interaction_DB

wnt_canonical_pathway. Canonical Wnt signaling pathway.
p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

P15923.

Bgee

P15923.

CleanEx

HS_TCF3.

Genevestigator

P15923.

GermOnline

ENSG00000071564. Homo sapiens.

Family and domain databases

Gene3D

4.10.280.10. 1 hit.

InterPro

IPR011598. bHLH_dom.
[Graphical view]

Pfam

PF00010. HLH. 1 hit.
[Graphical view]

SMART

SM00353. HLH. 1 hit.
[Graphical view]

SUPFAM

SSF47459. HLH_basic. 1 hit.

PROSITE

PS50888. BHLH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TCF3. human.

GenomeRNAi

6929.

NextBio

27113.

SOURCE

Search...

Entry information

Entry name

TFE2_HUMAN

Accession

Primary (citable) accession number: P15923
Secondary accession number(s): P15883 , Q14208, Q14635, Q14636, Q2TB40, Q9UPI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 161 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.