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P15923

- TFE2_HUMAN

UniProt

P15923 - TFE2_HUMAN

Protein

Transcription factor E2-alpha

Gene

TCF3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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 binding Source: UniProtKB
    8. protein heterodimerization activity Source: UniProtKB
    9. protein homodimerization activity Source: UniProtKB
    10. repressing transcription factor binding Source: UniProtKB
    11. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    12. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
    13. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    14. transcription coactivator activity Source: UniProtKB
    15. transcription factor binding Source: BHF-UCL
    16. 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

    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

    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

    ArrayExpressiP15923.
    BgeeiP15923.
    CleanExiHS_TCF3.
    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. 143 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.
    HOVERGENiHBG003854.
    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

    MNQPQRMAPV GTDKELSDLL DFSMMFPLPV TNGKGRPASL AGAQFGGSGL    50
    EDRPSSGSWG SGDQSSSSFD PSRTFSEGTH FTESHSSLSS STFLGPGLGG 100
    KSGERGAYAS FGRDAGVGGL TQAGFLSGEL ALNSPGPLSP SGMKGTSQYY 150
    PSYSGSSRRR AADGSLDTQP KKVRKVPPGL PSSVYPPSSG EDYGRDATAY 200
    PSAKTPSSTY PAPFYVADGS LHPSAELWSP PGQAGFGPML GGGSSPLPLP 250
    PGSGPVGSSG SSSTFGGLHQ HERMGYQLHG AEVNGGLPSA SSFSSAPGAT 300
    YGGVSSHTPP VSGADSLLGS RGTTAGSSGD ALGKALASIY SPDHSSNNFS 350
    SSPSTPVGSP QGLAGTSQWP RAGAPGALSP SYDGGLHGLQ SKIEDHLDEA 400
    IHVLRSHAVG TAGDMHTLLP GHGALASGFT GPMSLGGRHA GLVGGSHPED 450
    GLAGSTSLMH NHAALPSQPG TLPDLSRPPD SYSGLGRAGA TAAASEIKRE 500
    EKEDEENTSA ADHSEEEKKE LKAPRARTSP DEDEDDLLPP EQKAEREKER 550
    RVANNARERL RVRDINEAFK ELGRMCQLHL NSEKPQTKLL ILHQAVSVIL 600
    NLEQQVRERN LNPKAACLKR REEEKVSGVV GDPQMVLSAP HPGLSEAHNP 650
    AGHM 654
    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]
    ENST00000344749; ENSP00000344375; ENSG00000071564. [P15923-2]
    ENST00000585731; ENSP00000465510; ENSG00000071564.
    ENST00000588136; ENSP00000468487; ENSG00000071564. [P15923-2]
    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. 143 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 ]
    ENST00000344749 ; ENSP00000344375 ; ENSG00000071564 . [P15923-2 ]
    ENST00000585731 ; ENSP00000465510 ; ENSG00000071564 .
    ENST00000588136 ; ENSP00000468487 ; ENSG00000071564 . [P15923-2 ]
    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.
    HOVERGENi HBG003854.
    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

    ArrayExpressi P15923.
    Bgeei P15923.
    CleanExi HS_TCF3.
    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

    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 1, 2014
    This is version 175 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