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P15923 (TFE2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length654 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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. 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 processDifferentiation
Neurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   LigandDNA-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Non-traceable author statement PubMed 12435739. Source: UniProtKB

B cell lineage commitment

Inferred from direct assay PubMed 15030778. Source: UniProtKB

Peyer's patch development

Inferred from electronic annotation. Source: Ensembl

T cell differentiation in thymus

Inferred from electronic annotation. Source: Ensembl

cell development

Inferred from electronic annotation. Source: Ensembl

histone H3 acetylation

Inferred from electronic annotation. Source: Ensembl

histone H4 acetylation

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

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

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15509787. Source: BHF-UCL

protein stabilization

Inferred from electronic annotation. Source: Ensembl

regulation of G1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 11509675. Source: UniProtKB

regulation of transcription, DNA-templated

Non-traceable author statement Ref.5. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from direct assay PubMed 10775504. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 12435739. Source: UniProtKB

nuclear nucleosome

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 10749989. Source: BHF-UCL

protein complex

Inferred from direct assay PubMed 12435739. Source: UniProtKB

transcription factor complex

Inferred from direct assay PubMed 10775504Ref.15PubMed 2503252. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 10958665PubMed 8759016. Source: UniProtKB

E-box binding

Inferred from direct assay PubMed 7933101. Source: UniProtKB

bHLH transcription factor binding

Inferred from physical interaction PubMed 10749989. Source: BHF-UCL

chromatin binding

Inferred from electronic annotation. Source: Ensembl

mitogen-activated protein kinase kinase kinase binding

Inferred from physical interaction PubMed 19801649. Source: UniProtKB

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

repressing transcription factor binding

Inferred from physical interaction PubMed 12493738. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

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

transcription factor binding

Inferred from physical interaction Ref.15PubMed 2503252. Source: UniProtKB

vitamin D response element binding

Inferred from direct assay PubMed 17426122. Source: BHF-UCL

Complete GO annotation...

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: 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. Contains a phosphothreonine at position 531.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 654654Transcription factor E2-alpha
PRO_0000127466

Regions

Domain549 – 60254bHLH
Region389 – 42537Leucine-zipper
Motif19 – 2799aaTAD
Motif170 – 1767Nuclear localization signal Potential

Sites

Site483 – 4842Breakpoint for translocation to form TCF3-PBX1 oncogene

Amino acid modifications

Modified residue1341Phosphoserine Ref.19
Modified residue1391Phosphoserine Ref.18
Modified residue3591Phosphoserine Ref.18

Natural variations

Alternative sequence530 – 60172PDEDE…SVILN → STDEVLSLEEKDLRDRERRM ANNARERVRVRDINEAFREL GRMCQMHLKSDKAQTKLLIL QQAVQVILG in isoform E47.
VSP_002155
Natural variant81A → V in a colorectal cancer sample; somatic mutation. Ref.22
VAR_036396
Natural variant1201L → P.
Corresponds to variant rs35354874 [ dbSNP | Ensembl ].
VAR_049552
Natural variant1981T → A.
Corresponds to variant rs11879402 [ dbSNP | Ensembl ].
VAR_049553
Natural variant4311G → S.
Corresponds to variant rs1052692 [ dbSNP | Ensembl ].
VAR_049554

Experimental info

Sequence conflict69 – 9931FDPSR…GPGLG → GGGECLAWCGPSAVHRCADV GLGMVSARTAP in CAA36297. Ref.6
Sequence conflict214 – 2163FYV → EFR in AAA56830. Ref.5
Sequence conflict3021Missing in AAA36764. Ref.1
Sequence conflict3901Missing in AAA56830. Ref.5

Secondary structure

..... 654
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform E12 (PAN-2) [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 52F5E3DE1890AE13

FASTA65467,600
        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 

« Hide

Isoform E47 (PAN-1) [UniParc].

Checksum: F5F11C462351FFD6
Show »

FASTA65167,265

References

« Hide '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. expand/collapse author list , 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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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. expand/collapse author list , 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.

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.
PIRA34734.
S10099.
RefSeqNP_001129611.1. NM_001136139.2.
NP_003191.1. NM_003200.3.
UniGeneHs.371282.
Hs.657044.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HLHmodel-A/B549-610[»]
2YPAX-ray2.80B538-616[»]
2YPBX-ray2.87B538-616[»]
3U5VX-ray1.70A563-610[»]
ProteinModelPortalP15923.
SMRP15923. Positions 550-609.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112791. 143 interactions.
DIPDIP-74N.
IntActP15923. 16 interactions.
MINTMINT-190187.
STRING9606.ENSP00000262965.

PTM databases

PhosphoSiteP15923.

Polymorphism databases

DMDM135655.

Proteomic databases

PaxDbP15923.
PRIDEP15923.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262965; ENSP00000262965; ENSG00000071564. [P15923-1]
ENST00000344749; ENSP00000344375; ENSG00000071564. [P15923-2]
ENST00000585731; ENSP00000465510; ENSG00000071564.
ENST00000588136; ENSP00000468487; ENSG00000071564. [P15923-2]
GeneID6929.
KEGGhsa:6929.
UCSCuc002lto.3. human. [P15923-1]
uc002lts.1. human. [P15923-2]

Organism-specific databases

CTD6929.
GeneCardsGC19M001609.
HGNCHGNC:11633. TCF3.
HPACAB018351.
HPA049808.
MIM147141. gene.
neXtProtNX_P15923.
Orphanet33110. Autosomal agammaglobulinemia.
99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBPA164742580.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282899.
HOVERGENHBG003854.
KOK09063.
OrthoDBEOG72G16Q.
PhylomeDBP15923.
TreeFamTF321672.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
SignaLinkP15923.

Gene expression databases

ArrayExpressP15923.
BgeeP15923.
CleanExHS_TCF3.
GenevestigatorP15923.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
[Graphical view]
PfamPF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTCF3. human.
GeneWikiTCF3.
GenomeRNAi6929.
NextBio27113.
PROP15923.
SOURCESearch...

Entry information

Entry nameTFE2_HUMAN
AccessionPrimary (citable) accession number: P15923
Secondary accession number(s): P15883 expand/collapse secondary AC list , Q14208, Q14635, Q14636, Q2TB40, Q9UPI9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM