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P15806

- TFE2_MOUSE

UniProt

P15806 - TFE2_MOUSE

Protein

Transcription factor E2-alpha

Gene

Tcf3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      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.1 Publication

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. DNA binding Source: UniProtKB
    3. E-box binding Source: UniProtKB
    4. protein binding Source: BHF-UCL
    5. protein heterodimerization activity Source: UniProtKB
    6. protein homodimerization activity Source: UniProtKB
    7. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    9. RNA polymerase II distal enhancer sequence-specific DNA binding Source: NTNU_SB
    10. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    11. sequence-specific DNA binding Source: MGI
    12. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    13. transcription coactivator activity Source: UniProtKB
    14. transcription factor binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Biological processi

    Differentiation, Neurogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor E2-alpha
    Alternative name(s):
    Immunoglobulin enhancer-binding factor E12/E47
    Transcription factor 3
    Short name:
    TCF-3
    Transcription factor A1
    Gene namesi
    Name:Tcf3
    Synonyms:Alf2, Me2, Tcfe2a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:98510. Tcf3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nuclear nucleosome Source: MGI
    3. nucleoplasm Source: Reactome
    4. nucleus Source: MGI
    5. protein complex Source: UniProtKB
    6. transcription factor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice are smaller than their wild-type littermates and fail to thrive 14 days after birth.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 651651Transcription factor E2-alphaPRO_0000127468Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei135 – 1351PhosphoserineBy similarity
    Modified residuei140 – 1401PhosphoserineBy similarity
    Modified residuei357 – 3571PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated following NGF stimulation.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP15806.
    PaxDbiP15806.
    PRIDEiP15806.

    PTM databases

    PhosphoSiteiP15806.

    Expressioni

    Developmental stagei

    Expressed during the development of the nervous system.1 Publication

    Gene expression databases

    ArrayExpressiP15806.
    BgeeiP15806.
    CleanExiMM_ME2.
    MM_TCF3.
    MM_TCFE2A.
    GenevestigatoriP15806.

    Interactioni

    Subunit structurei

    Forms a heterodimer with TWIST2. Forms a heterodimer with NEUROD1; the heterodimer is inhibited in presence of ID2, but not NR0B2, to E-box element. Isoform E12 interacts with RALGAPA1 and FIGLA. Interacts with EP300. Efficient DNA binding requires dimerization with another bHLH protein By similarity. Homodimer. Heterodimer. Forms a heterodimer with MYOG; heterodimerization enhances MYOG DNA-binding and transcriptional activities. Interacts with PTF1A, TGFB1I1 and UBE2I. Component of a nuclear TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3. Interacts with NEUROD2.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Hand1Q642792EBI-81370,EBI-81361
    Hand2Q610392EBI-81370,EBI-81388
    Tal1P220914EBI-81370,EBI-8006437

    Protein-protein interaction databases

    BioGridi204015. 99 interactions.
    DIPiDIP-30940N.
    IntActiP15806. 13 interactions.
    MINTiMINT-218641.

    Structurei

    Secondary structure

    1
    651
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi548 – 57427
    Helixi585 – 60218

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QL2X-ray2.50A/C547-606[»]
    ProteinModelPortaliP15806.
    SMRiP15806. Positions 547-606.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15806.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini546 – 59954bHLHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni387 – 42236Leucine-zipperAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG282899.
    GeneTreeiENSGT00510000046438.
    HOVERGENiHBG003854.
    KOiK09063.
    PhylomeDBiP15806.

    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: P15806-1) [UniParc]FASTAAdd to Basket

    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

    MMNQSQRMAP VGSDKELSDL LDFSMMFPLP VANGKSRPAS LGGTQFAGSG    50
    LEDRPSSGSW GSSDQNSSSF DPSRTYSEGA HFSDSHSSLP PSTFLGAGLG 100
    GKGSERNAYA TFGRDTSVGT LSQAGFLPGE LSLSSPGPLS PSGIKSSSQY 150
    YPSFPSNPRR RAADGGLDTQ PKKVRKVPPG LPSSVYPPSS GDSYSRDAAA 200
    YPSAKTPSSA YPSPFYVADG SLHPSAELWS TPSQVGFGPM LGDGSSPLPL 250
    APGSSSVGSG TFGGLQQQDR MGYQLHGSEV NGSLPAVSSF SAAPGTYSGT 300
    SGHTPPVSGA AAESLLGTRG TTASSSGDAL GKALASIYSP DHSSNNFSPS 350
    PSTPVGSPQG LPGTSQWPRA GAPSALSPNY DAGLHGLSKM EDRLDEAIHV 400
    LRSHAVGTAS DLHGLLPGHG ALTTSFTGPM SLGGRHAGLV GGSHPEEGLT 450
    SGASLLHNHA SLPSQPSSLP DLSQRPPDSY SGLGRAGTTA GASEIKREEK 500
    EDEEIASVAD AEEDKKDLKV PRTRTSPDED EDDLLPPEQK AEREKERRVA 550
    NNARERLRVR DINEAFKELG RMCQLHLSSE KPQTKLLILH QAVAVILSLE 600
    QQVRERNLNP KAACLKRREE EKVSGVVGDP QLALSAAHPG LGEAHNPAGH 650
    L 651
    Length:651
    Mass (Da):67,701
    Last modified:August 16, 2004 - v2
    Checksum:i7904ABB37B8D39CB
    GO
    Isoform E47 (identifier: P15806-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         527-598: PDEDEDDLLP...LHQAVAVILS → STDEVLSLEE...LQQAVQVILG

    Note: Contains a phosphothreonine at position 528.By similarity

    Show »
    Length:648
    Mass (Da):67,417
    Checksum:i5C1B68DDBF29A93B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti156 – 1561S → N in AAK18618. (PubMed:11309385)Curated
    Sequence conflicti164 – 1641D → N in AAK18618. (PubMed:11309385)Curated
    Sequence conflicti167 – 1671L → LA in AAH18260. (PubMed:15489334)Curated
    Sequence conflicti294 – 2941P → T in BAB30842. (PubMed:16141072)Curated
    Sequence conflicti633 – 6331A → P in AAH06860. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti387 – 3871L → LQ.1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei527 – 59872PDEDE…AVILS → STDEVLSLEEKDLRDRERRM ANNARERVRVRDINEAFREL GRMCQLHLKSDKAQTKLLIL QQAVQVILG in isoform E47. 4 PublicationsVSP_011354Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF352579 mRNA. Translation: AAK18618.1.
    AK017617 mRNA. Translation: BAB30842.1.
    AK038738 mRNA. Translation: BAC30118.1.
    AK156265 mRNA. Translation: BAE33647.1.
    BC006860 mRNA. Translation: AAH06860.1.
    BC018260 mRNA. Translation: AAH18260.1.
    X17500 mRNA. Translation: CAA35541.1.
    D16631 mRNA. Translation: BAA04057.1.
    D16632 mRNA. Translation: BAA04058.1.
    D16633 mRNA. Translation: BAA04059.1.
    D16634 mRNA. Translation: BAA04060.1.
    D16635 mRNA. Translation: BAA04061.1.
    D16636 mRNA. Translation: BAA04062.1.
    D16637 mRNA. Translation: BAA04063.1.
    D16638 mRNA. Translation: BAA04064.1.
    D29919 mRNA. Translation: BAA06218.1.
    CCDSiCCDS24022.1. [P15806-2]
    CCDS48630.1. [P15806-1]
    PIRiS08410.
    RefSeqiNP_001157620.1. NM_001164148.1.
    NP_001157621.1. NM_001164149.1. [P15806-1]
    NP_001157623.1. NM_001164151.1.
    NP_035678.3. NM_011548.4. [P15806-2]
    UniGeneiMm.3406.

    Genome annotation databases

    EnsembliENSMUST00000020377; ENSMUSP00000020377; ENSMUSG00000020167.
    ENSMUST00000020379; ENSMUSP00000020379; ENSMUSG00000020167.
    ENSMUST00000105345; ENSMUSP00000100982; ENSMUSG00000020167. [P15806-2]
    ENSMUST00000105346; ENSMUSP00000100983; ENSMUSG00000020167. [P15806-1]
    GeneIDi21423.
    KEGGimmu:21423.
    UCSCiuc007gdg.2. mouse. [P15806-2]
    uc007gdi.2. mouse. [P15806-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF352579 mRNA. Translation: AAK18618.1 .
    AK017617 mRNA. Translation: BAB30842.1 .
    AK038738 mRNA. Translation: BAC30118.1 .
    AK156265 mRNA. Translation: BAE33647.1 .
    BC006860 mRNA. Translation: AAH06860.1 .
    BC018260 mRNA. Translation: AAH18260.1 .
    X17500 mRNA. Translation: CAA35541.1 .
    D16631 mRNA. Translation: BAA04057.1 .
    D16632 mRNA. Translation: BAA04058.1 .
    D16633 mRNA. Translation: BAA04059.1 .
    D16634 mRNA. Translation: BAA04060.1 .
    D16635 mRNA. Translation: BAA04061.1 .
    D16636 mRNA. Translation: BAA04062.1 .
    D16637 mRNA. Translation: BAA04063.1 .
    D16638 mRNA. Translation: BAA04064.1 .
    D29919 mRNA. Translation: BAA06218.1 .
    CCDSi CCDS24022.1. [P15806-2 ]
    CCDS48630.1. [P15806-1 ]
    PIRi S08410.
    RefSeqi NP_001157620.1. NM_001164148.1.
    NP_001157621.1. NM_001164149.1. [P15806-1 ]
    NP_001157623.1. NM_001164151.1.
    NP_035678.3. NM_011548.4. [P15806-2 ]
    UniGenei Mm.3406.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QL2 X-ray 2.50 A/C 547-606 [» ]
    ProteinModelPortali P15806.
    SMRi P15806. Positions 547-606.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204015. 99 interactions.
    DIPi DIP-30940N.
    IntActi P15806. 13 interactions.
    MINTi MINT-218641.

    PTM databases

    PhosphoSitei P15806.

    Proteomic databases

    MaxQBi P15806.
    PaxDbi P15806.
    PRIDEi P15806.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020377 ; ENSMUSP00000020377 ; ENSMUSG00000020167 .
    ENSMUST00000020379 ; ENSMUSP00000020379 ; ENSMUSG00000020167 .
    ENSMUST00000105345 ; ENSMUSP00000100982 ; ENSMUSG00000020167 . [P15806-2 ]
    ENSMUST00000105346 ; ENSMUSP00000100983 ; ENSMUSG00000020167 . [P15806-1 ]
    GeneIDi 21423.
    KEGGi mmu:21423.
    UCSCi uc007gdg.2. mouse. [P15806-2 ]
    uc007gdi.2. mouse. [P15806-1 ]

    Organism-specific databases

    CTDi 6929.
    MGIi MGI:98510. Tcf3.

    Phylogenomic databases

    eggNOGi NOG282899.
    GeneTreei ENSGT00510000046438.
    HOVERGENi HBG003854.
    KOi K09063.
    PhylomeDBi P15806.

    Miscellaneous databases

    ChiTaRSi TCF3. mouse.
    EvolutionaryTracei P15806.
    NextBioi 300742.
    PROi P15806.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15806.
    Bgeei P15806.
    CleanExi MM_ME2.
    MM_TCF3.
    MM_TCFE2A.
    Genevestigatori P15806.

    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 role for E12/E47 in the repression of E-cadherin expression and epithelial-mesenchymal transitions."
      Perez-Moreno M.A., Locascio A., Rodrigo I., Dhondt G., Portillo F., Nieto M.A., Cano A.
      J. Biol. Chem. 276:27424-27431(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E47).
      Strain: NIH Swiss.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS E12 AND E47).
      Strain: C57BL/6J and NOD.
      Tissue: Hypothalamus and Spleen.
    3. "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] (ISOFORMS E12 AND E47).
      Strain: FVB/N.
      Tissue: Mammary tumor and Salivary gland.
    4. "A cDNA from a mouse pancreatic beta cell encoding a putative transcription factor of the insulin gene."
      Walker M.D., Park C.W., Rosen A., Aronheim A.
      Nucleic Acids Res. 18:1159-1166(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 369-651 (ISOFORM E47).
      Tissue: Pancreas.
    5. "Identification of amino-acid polymorphism within the leucine zipper motif of mouse transcription factor A1."
      Kajimoto Y., Kawamori R., Umayahara Y., Watada H., Iwama N., Morishima T., Yamasaki Y., Kamada T.
      Gene 139:247-249(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 386-493, VARIANT GLN-387 INS.
      Tissue: Adipocyte.
    6. "Ubiquitous, but variable, expression of two alternatively spliced mRNAs encoding mouse homologues of transcription factors E47 and E12."
      Watada H., Kajimoto Y., Umayahara Y., Matsuoka T., Morishima T., Yamasaki Y., Kawamori R., Kamada T.
      Gene 153:255-259(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 485-651 (ISOFORM E12).
      Strain: C57BL/6.
    7. "Dermo-1: a novel twist-related bHLH protein expressed in the developing dermis."
      Li L., Cserjesi P., Olson E.N.
      Dev. Biol. 172:280-292(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TWIST2.
      Strain: Swiss.
      Tissue: Brain and Embryonic head.
    8. "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.
    9. "p48 subunit of mouse PTF1 binds to RBP-Jkappa/CBF-1, the intracellular mediator of Notch signalling, and is expressed in the neural tube of early stage embryos."
      Obata J., Yano M., Mimura H., Goto T., Nakayama R., Mibu Y., Oka C., Kawaichi M.
      Genes Cells 6:345-360(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTF1A.
    10. "Analysis of the DNA-binding properties of MyoD, myogenin, and E12 by fluorescence anisotropy."
      Maleki S.J., Royer C.A., Hurlburt B.K.
      Biochemistry 41:10888-10894(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    11. "Cloning and characterization of GRIPE, a novel interacting partner of the transcription factor E12 in developing mouse forebrain."
      Heng J.I.T., Tan S.-S.
      J. Biol. Chem. 277:43152-43159(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RALGAPA1.
    12. "ETO2 coordinates cellular proliferation and differentiation during erythropoiesis."
      Goardon N., Lambert J.A., Rodriguez P., Nissaire P., Herblot S., Thibault P., Dumenil D., Strouboulis J., Romeo P.-H., Hoang T.
      EMBO J. 25:357-366(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A NUCLEAR TAL-1 COMPLEX.
    13. "HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor-driven transcription."
      Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., Gradl D.
      J. Biol. Chem. 281:1755-1764(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TGFB1I1.
    14. "E protein dosage influences brain development more than family member identity."
      Ravanpay A.C., Olson J.M.
      J. Neurosci. Res. 86:1472-1481(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NEUROD2, DNA-BINDING, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
    15. "Crystal structure of E47-NeuroD1/beta2 bHLH domain-DNA complex: heterodimer selectivity and DNA recognition."
      Longo A., Guanga G.P., Rose R.B.
      Biochemistry 47:218-229(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 547-606 IN COMPLEX WITH NEUROD1 AND PROMOTER E-BOX DNA SEQUENCE, SUBUNIT.

    Entry informationi

    Entry nameiTFE2_MOUSE
    AccessioniPrimary (citable) accession number: P15806
    Secondary accession number(s): Q3U153
    , Q8CAH9, Q8VCY4, Q922S2, Q99MB8, Q9CYJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3