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P15923

- TFE2_HUMAN

UniProt

P15923 - TFE2_HUMAN

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Protein

Transcription factor E2-alpha

Gene

TCF3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei483 – 4842Breakpoint for translocation to form TCF3-PBX1 oncogene

GO - Molecular functioni

  1. bHLH transcription factor binding Source: BHF-UCL
  2. chromatin binding Source: Ensembl
  3. DNA binding Source: UniProtKB
  4. E-box binding Source: UniProtKB
  5. enhancer binding Source: BHF-UCL
  6. mitogen-activated protein kinase kinase kinase binding Source: UniProtKB
  7. protein heterodimerization activity Source: UniProtKB
  8. protein homodimerization activity Source: UniProtKB
  9. repressing transcription factor binding Source: UniProtKB
  10. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  11. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
  12. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  13. transcription coactivator activity Source: UniProtKB
  14. transcription factor binding Source: BHF-UCL
  15. vitamin D response element binding Source: BHF-UCL

GO - Biological processi

  1. B cell differentiation Source: UniProtKB
  2. B cell lineage commitment Source: UniProtKB
  3. cell development Source: Ensembl
  4. histone H3 acetylation Source: Ensembl
  5. histone H4 acetylation Source: Ensembl
  6. immunoglobulin V(D)J recombination Source: MGI
  7. muscle cell differentiation Source: Reactome
  8. natural killer cell differentiation Source: Ensembl
  9. negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  10. Peyer's patch development Source: Ensembl
  11. positive regulation of B cell proliferation Source: UniProtKB
  12. positive regulation of cell cycle Source: UniProtKB
  13. positive regulation of muscle cell differentiation Source: Reactome
  14. positive regulation of neuron differentiation Source: UniProtKB
  15. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  16. positive regulation of transcription, DNA-templated Source: BHF-UCL
  17. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  18. protein stabilization Source: Ensembl
  19. regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  20. regulation of transcription, DNA-templated Source: UniProtKB
  21. response to drug Source: Ensembl
  22. response to lipopolysaccharide Source: Ensembl
  23. T cell differentiation in thymus Source: Ensembl
  24. transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Differentiation, Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_21402. CDO in myogenesis.
SignaLinkiP15923.

Names & Taxonomyi

Protein namesi
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 namesi
Name:TCF3
Synonyms:BHLHB21, E2A, ITF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:11633. TCF3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. nuclear chromatin Source: BHF-UCL
  3. nuclear nucleosome Source: Ensembl
  4. nucleoplasm Source: Reactome
  5. nucleus Source: BHF-UCL
  6. protein complex Source: UniProtKB
  7. transcription factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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 inv(19)(p13;q13) with TFPT.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti33110. Autosomal agammaglobulinemia.
99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBiPA164742580.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 654654Transcription factor E2-alphaPRO_0000127466Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei134 – 1341Phosphoserine1 Publication
Modified residuei139 – 1391Phosphoserine1 Publication
Modified residuei359 – 3591Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated following NGF stimulation.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15923.
PaxDbiP15923.
PRIDEiP15923.

PTM databases

PhosphoSiteiP15923.

Expressioni

Gene expression databases

BgeeiP15923.
CleanExiHS_TCF3.
ExpressionAtlasiP15923. baseline and differential.
GenevestigatoriP15923.

Organism-specific databases

HPAiCAB018351.
HPA049808.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ASCL1P505533EBI-769630,EBI-957042
CCNDBP1O952733EBI-769645,EBI-748961
FOXH1O755932EBI-769630,EBI-1759806
ID2Q023633EBI-769645,EBI-713450
MYOD1P151722EBI-769645,EBI-488878
TAL1P175425EBI-769630,EBI-1753878

Protein-protein interaction databases

BioGridi112791. 146 interactions.
DIPiDIP-74N.
IntActiP15923. 18 interactions.
MINTiMINT-190187.
STRINGi9606.ENSP00000262965.

Structurei

Secondary structure

1
654
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi563 – 58018
Helixi588 – 60821

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HLHmodel-A/B549-610[»]
2YPAX-ray2.80B546-616[»]
2YPBX-ray2.87B546-616[»]
3U5VX-ray1.70A563-613[»]
ProteinModelPortaliP15923.
SMRiP15923. Positions 550-609.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini549 – 60254bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni389 – 42537Leucine-zipperAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi19 – 2799aaTAD
Motifi170 – 1767Nuclear localization signalSequence Analysis

Domaini

the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.2 Publications

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG282899.
GeneTreeiENSGT00510000046438.
HOVERGENiHBG003854.
InParanoidiP15923.
KOiK09063.
OrthoDBiEOG72G16Q.
PhylomeDBiP15923.
TreeFamiTF321672.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform E12 (identifier: P15923-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MNQPQRMAPV GTDKELSDLL DFSMMFPLPV TNGKGRPASL AGAQFGGSGL
60 70 80 90 100
EDRPSSGSWG SGDQSSSSFD PSRTFSEGTH FTESHSSLSS STFLGPGLGG
110 120 130 140 150
KSGERGAYAS FGRDAGVGGL TQAGFLSGEL ALNSPGPLSP SGMKGTSQYY
160 170 180 190 200
PSYSGSSRRR AADGSLDTQP KKVRKVPPGL PSSVYPPSSG EDYGRDATAY
210 220 230 240 250
PSAKTPSSTY PAPFYVADGS LHPSAELWSP PGQAGFGPML GGGSSPLPLP
260 270 280 290 300
PGSGPVGSSG SSSTFGGLHQ HERMGYQLHG AEVNGGLPSA SSFSSAPGAT
310 320 330 340 350
YGGVSSHTPP VSGADSLLGS RGTTAGSSGD ALGKALASIY SPDHSSNNFS
360 370 380 390 400
SSPSTPVGSP QGLAGTSQWP RAGAPGALSP SYDGGLHGLQ SKIEDHLDEA
410 420 430 440 450
IHVLRSHAVG TAGDMHTLLP GHGALASGFT GPMSLGGRHA GLVGGSHPED
460 470 480 490 500
GLAGSTSLMH NHAALPSQPG TLPDLSRPPD SYSGLGRAGA TAAASEIKRE
510 520 530 540 550
EKEDEENTSA ADHSEEEKKE LKAPRARTSP DEDEDDLLPP EQKAEREKER
560 570 580 590 600
RVANNARERL RVRDINEAFK ELGRMCQLHL NSEKPQTKLL ILHQAVSVIL
610 620 630 640 650
NLEQQVRERN LNPKAACLKR REEEKVSGVV GDPQMVLSAP HPGLSEAHNP

AGHM
Length:654
Mass (Da):67,600
Last modified:April 1, 1990 - v1
Checksum:i52F5E3DE1890AE13
GO
Isoform E47 (identifier: P15923-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:651
Mass (Da):67,265
Checksum:iF5F11C462351FFD6
GO

Sequence cautioni

The sequence AAA52331.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 9931FDPSR…GPGLG → GGGECLAWCGPSAVHRCADV GLGMVSARTAP in CAA36297. (PubMed:2308859)CuratedAdd
BLAST
Sequence conflicti214 – 2163FYV → EFR in AAA56830. (PubMed:2493990)Curated
Sequence conflicti302 – 3021Missing in AAA36764. (PubMed:1967983)Curated
Sequence conflicti390 – 3901Missing in AAA56830. (PubMed:2493990)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81A → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036396
Natural varianti120 – 1201L → P.
Corresponds to variant rs35354874 [ dbSNP | Ensembl ].
VAR_049552
Natural varianti198 – 1981T → A.
Corresponds to variant rs11879402 [ dbSNP | Ensembl ].
VAR_049553
Natural varianti431 – 4311G → S.
Corresponds to variant rs1052692 [ dbSNP | Ensembl ].
VAR_049554

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei530 – 60172PDEDE…SVILN → STDEVLSLEEKDLRDRERRM ANNARERVRVRDINEAFREL GRMCQMHLKSDKAQTKLLIL QQAVQVILG in isoform E47. 4 PublicationsVSP_002155Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS12074.1. [P15923-1]
CCDS45899.1. [P15923-2]
PIRiA34734.
S10099.
RefSeqiNP_001129611.1. NM_001136139.2. [P15923-2]
NP_003191.1. NM_003200.3. [P15923-1]
UniGeneiHs.371282.
Hs.657044.

Genome annotation databases

EnsembliENST00000262965; ENSP00000262965; ENSG00000071564. [P15923-1]
ENST00000588136; ENSP00000468487; ENSG00000071564. [P15923-2]
ENST00000611869; ENSP00000480564; ENSG00000071564. [P15923-1]
GeneIDi6929.
KEGGihsa:6929.
UCSCiuc002lto.3. human. [P15923-1]
uc002lts.1. human. [P15923-2]

Polymorphism databases

DMDMi135655.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS12074.1. [P15923-1 ]
CCDS45899.1. [P15923-2 ]
PIRi A34734.
S10099.
RefSeqi NP_001129611.1. NM_001136139.2. [P15923-2 ]
NP_003191.1. NM_003200.3. [P15923-1 ]
UniGenei Hs.371282.
Hs.657044.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HLH model - A/B 549-610 [» ]
2YPA X-ray 2.80 B 546-616 [» ]
2YPB X-ray 2.87 B 546-616 [» ]
3U5V X-ray 1.70 A 563-613 [» ]
ProteinModelPortali P15923.
SMRi P15923. Positions 550-609.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112791. 146 interactions.
DIPi DIP-74N.
IntActi P15923. 18 interactions.
MINTi MINT-190187.
STRINGi 9606.ENSP00000262965.

PTM databases

PhosphoSitei P15923.

Polymorphism databases

DMDMi 135655.

Proteomic databases

MaxQBi P15923.
PaxDbi P15923.
PRIDEi P15923.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262965 ; ENSP00000262965 ; ENSG00000071564 . [P15923-1 ]
ENST00000588136 ; ENSP00000468487 ; ENSG00000071564 . [P15923-2 ]
ENST00000611869 ; ENSP00000480564 ; ENSG00000071564 . [P15923-1 ]
GeneIDi 6929.
KEGGi hsa:6929.
UCSCi uc002lto.3. human. [P15923-1 ]
uc002lts.1. human. [P15923-2 ]

Organism-specific databases

CTDi 6929.
GeneCardsi GC19M001609.
HGNCi HGNC:11633. TCF3.
HPAi CAB018351.
HPA049808.
MIMi 147141. gene.
neXtProti NX_P15923.
Orphaneti 33110. Autosomal agammaglobulinemia.
99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBi PA164742580.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG282899.
GeneTreei ENSGT00510000046438.
HOVERGENi HBG003854.
InParanoidi P15923.
KOi K09063.
OrthoDBi EOG72G16Q.
PhylomeDBi P15923.
TreeFami TF321672.

Enzyme and pathway databases

Reactomei REACT_21402. CDO in myogenesis.
SignaLinki P15923.

Miscellaneous databases

ChiTaRSi TCF3. human.
GeneWikii TCF3.
GenomeRNAii 6929.
NextBioi 27113.
PROi P15923.
SOURCEi Search...

Gene expression databases

Bgeei P15923.
CleanExi HS_TCF3.
ExpressionAtlasi P15923. baseline and differential.
Genevestigatori P15923.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
InterProi IPR011598. bHLH_dom.
[Graphical view ]
Pfami PF00010. HLH. 1 hit.
[Graphical view ]
SMARTi SM00353. HLH. 1 hit.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
PROSITEi PS50888. BHLH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiTFE2_HUMAN
AccessioniPrimary (citable) accession number: P15923
Secondary accession number(s): P15883
, Q14208, Q14635, Q14636, Q2TB40, Q9UPI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 176 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3