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P15806

- TFE2_MOUSE

UniProt

P15806 - TFE2_MOUSE

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Protein

Transcription factor E2-alpha

Gene
Tcf3, Alf2, Me2, Tcfe2a
Organism
Mus musculus (Mouse)
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.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. sequence-specific DNA binding Source: MGI
  8. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  9. transcription coactivator activity Source: UniProtKB
  10. 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
  24. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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
Complete GO annotation...

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 – 1351Phosphoserine By similarity
Modified residuei140 – 1401Phosphoserine By similarity
Modified residuei357 – 3571Phosphoserine By 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 NEUROD2.9 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.

Miscellaneous databases

EvolutionaryTraceiP15806.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini546 – 59954bHLHAdd
BLAST

Region

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

Sequence similaritiesi

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

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. VSP_011354Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561S → N in AAK18618. 1 Publication
Sequence conflicti164 – 1641D → N in AAK18618. 1 Publication
Sequence conflicti167 – 1671L → LA in AAH18260. 1 Publication
Sequence conflicti294 – 2941P → T in BAB30842. 1 Publication
Sequence conflicti633 – 6331A → P in AAH06860. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 148 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

Similar proteinsi