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Q9UJU2 (LEF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lymphoid enhancer-binding factor 1

Short name=LEF-1
Alternative name(s):
T cell-specific transcription factor 1-alpha
Short name=TCF1-alpha
Gene names
Name:LEF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in the Wnt signaling pathway. Activates transcription of target genes in the presence of CTNNB1 and EP300. May play a role in hair cell differentiation and follicle morphogenesis. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by LEF1 and CTNNB1. Regulates T-cell receptor alpha enhancer function. Binds DNA in a sequence-specific manner. PIAG antagonizes both Wnt-dependent and Wnt-independent activation by LEF1 By similarity. Isoform 3 lacks the CTNNB1 interaction domain and may be an antagonist for Wnt signaling. Isoform 5 transcriptionally activates the fibronectin promoter, binds to and represses transcription from the E-cadherin promoter in a CTNNB1-independent manner, and is involved in reducing cellular aggregation and increasing cell migration of pancreatic cancer cells. Isoform 1 transcriptionally activates MYC and CCND1 expression and enhances proliferation of pancreatic tumor cells. Ref.1 Ref.3 Ref.13

Subunit structure

Binds the armadillo repeat of CTNNB1 and forms a stable complex. Interacts with EP300, TLE1 and PIASG By similarity. Binds ALYREF/THOC4, MDFI and MDFIC. Interacts with NLK. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15

Subcellular location

Nucleus By similarity. Note: Found in nuclear bodies upon PIASG binding By similarity.

Tissue specificity

Detected in thymus. Not detected in normal colon, but highly expressed in colon cancer biopsies and colon cancer cell lines. Expressed in several pancreatic tumors and weakly expressed in normal pancreatic tissue. Isoforms 1 and 5 are detected in several pancreatic cell lines. Ref.3

Domain

Proline-rich and acidic regions are implicated in the activation functions of RNA polymerase II transcription factors.

Post-translational modification

Phosphorylated at Thr-155 and/or Ser-166 by NLK. Phosphorylation by NLK at these sites represses LEF1-mediated transcriptional activation of target genes of the canonical Wnt signaling pathway. Ref.15

Sequence similarities

Belongs to the TCF/LEF family.

Contains 1 HMG box DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Wnt signaling pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   LigandDNA-binding
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell proliferation

Inferred from Biological aspect of Ancestor. Source: RefGenome

BMP signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

T cell receptor V(D)J recombination

Inferred from electronic annotation. Source: Ensembl

T-helper 1 cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

Wnt signaling pathway

Inferred from direct assay PubMed 10644691. Source: BHF-UCL

alpha-beta T cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

anatomical structure regression

Inferred from electronic annotation. Source: Ensembl

apoptotic process involved in morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

apoptotic process involved in patterning of blood vessels

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 19576624. Source: UniProtKB

cell chemotaxis

Inferred from direct assay PubMed 19576624. Source: UniProtKB

cellular response to cytokine stimulus

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

cellular response to interleukin-4

Inferred from direct assay PubMed 18579517. Source: UniProtKB

chorio-allantoic fusion

Inferred from Biological aspect of Ancestor. Source: RefGenome

dentate gyrus development

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic limb morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: BHF-UCL

eye pigmentation

Inferred from Biological aspect of Ancestor. Source: RefGenome

face morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

forebrain neuroblast division

Inferred from Biological aspect of Ancestor. Source: RefGenome

forebrain neuron differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

forebrain radial glial cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

formation of radial glial scaffolds

Inferred from Biological aspect of Ancestor. Source: RefGenome

histone H3 acetylation

Inferred from mutant phenotype PubMed 20363964. Source: UniProtKB

histone H4 acetylation

Inferred from mutant phenotype PubMed 20363964. Source: UniProtKB

hypothalamus development

Inferred from Biological aspect of Ancestor. Source: RefGenome

mammary gland development

Inferred from Biological aspect of Ancestor. Source: RefGenome

muscle fiber development

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of DNA binding

Inferred from direct assay PubMed 18445004. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 20360943. Source: UniProtKB

negative regulation of apoptotic process in bone marrow

Inferred from mutant phenotype PubMed 17063141. Source: UniProtKB

negative regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 19402906. Source: UniProtKB

negative regulation of cell-cell adhesion

Inferred from direct assay Ref.3. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 20360943. Source: UniProtKB

negative regulation of estrogen receptor binding

Inferred from direct assay PubMed 18794125. Source: UniProtKB

negative regulation of interleukin-13 production

Inferred from direct assay PubMed 18445004. Source: UniProtKB

negative regulation of interleukin-4 production

Inferred from direct assay PubMed 18445004. Source: UniProtKB

negative regulation of interleukin-5 production

Inferred from direct assay PubMed 18445004. Source: UniProtKB

negative regulation of striated muscle tissue development

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18794125Ref.3. Source: UniProtKB

neural crest cell migration

Inferred from Biological aspect of Ancestor. Source: RefGenome

neutrophil differentiation

Inferred from mutant phenotype PubMed 17063141. Source: UniProtKB

odontoblast differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from expression pattern PubMed 20128911. Source: UniProtKB

palate development

Inferred from sequence or structural similarity. Source: BHF-UCL

paraxial mesoderm formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

patterning of blood vessels

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation by host of viral transcription

Inferred from direct assay PubMed 7657162. Source: UniProtKB

positive regulation of cell cycle process

Inferred from direct assay Ref.3. Source: UniProtKB

positive regulation of cell growth

Inferred from mutant phenotype PubMed 20360943. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay Ref.3. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 19351848Ref.3. Source: UniProtKB

positive regulation of cell proliferation in bone marrow

Inferred from mutant phenotype PubMed 17063141. Source: UniProtKB

positive regulation of cell-cell adhesion

Inferred from direct assay Ref.3. Source: UniProtKB

positive regulation of epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 20018240. Source: UniProtKB

positive regulation of gene expression

Inferred from direct assay PubMed 16344550. Source: AgBase

positive regulation of granulocyte differentiation

Inferred from direct assay PubMed 19620402. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 11751639. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 17063141PubMed 19620402PubMed 20128911PubMed 7657162Ref.3. Source: UniProtKB

regulation of cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of striated muscle tissue development

Inferred from Biological aspect of Ancestor. Source: RefGenome

sensory perception of taste

Inferred from electronic annotation. Source: Ensembl

somitogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

sprouting angiogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

steroid hormone mediated signaling pathway

Inferred from direct assay PubMed 18794125. Source: GOC

tongue development

Inferred from electronic annotation. Source: Ensembl

trachea gland development

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 23001182. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 19402906. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17063141PubMed 18579517. Source: UniProtKB

protein-DNA complex

Inferred from direct assay PubMed 10825188. Source: BHF-UCL

transcription factor complex

Inferred from direct assay PubMed 11751639PubMed 23001182. Source: BHF-UCL

   Molecular_functionC2H2 zinc finger domain binding

Inferred from physical interaction PubMed 18445004. Source: UniProtKB

DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

DNA binding, bending

Inferred from sequence or structural similarity. Source: UniProtKB

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

RNA polymerase II regulatory region sequence-specific DNA binding

Inferred from direct assay PubMed 23001182. Source: BHF-UCL

RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

armadillo repeat domain binding

Inferred from physical interaction PubMed 12408825. Source: BHF-UCL

beta-catenin binding

Inferred from physical interaction PubMed 20360943. Source: UniProtKB

chromatin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from mutant phenotype PubMed 20360943. Source: UniProtKB

enhancer binding

Inferred from direct assay PubMed 7657162. Source: UniProtKB

estrogen receptor activity

Inferred from direct assay PubMed 18794125. Source: UniProtKB

estrogen receptor binding

Inferred from direct assay PubMed 18794125. Source: UniProtKB

gamma-catenin binding

Inferred from physical interaction PubMed 14661054. Source: BHF-UCL

histone binding

Inferred from physical interaction PubMed 20363964. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.14PubMed 19460168Ref.11. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 9308964. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 11751639. Source: BHF-UCL

transcription regulatory region DNA binding

Inferred from direct assay PubMed 17063141PubMed 18579517PubMed 19351848PubMed 20128911PubMed 20363964Ref.3. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTNNB1P352225EBI-926131,EBI-491549
IGF1RP080695EBI-926131,EBI-475981

Alternative products

This entry describes 7 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9UJU2-1)

Also known as: A;

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.
Note: Produced by alternative promoter usage.
Isoform 2 (identifier: Q9UJU2-2)

Also known as: B; 8A;

The sequence of this isoform differs from the canonical sequence as follows:
     283-399: KPQHEQRKEQ...TGPRMTAAYI → CSAFLLPHPF...SQKDLTLRSL
Note: Produced by alternative splicing of isoform 1. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 3 (identifier: Q9UJU2-3)

Also known as: LEF-1-DN;

The sequence of this isoform differs from the canonical sequence as follows:
     1-115: Missing.
Note: Produced by alternative promoter usage. Acts as dominant negative mutant.
Isoform 4 (identifier: Q9UJU2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-115: Missing.
     283-399: KPQHEQRKEQ...TGPRMTAAYI → CSAFLLPHPF...SQKDLTLRSL
Note: Produced by alternative splicing of isoform 3.
Isoform 5 (identifier: Q9UJU2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     214-241: Missing.
Note: Produced by alternative splicing of isoform 1.
Isoform 6 (identifier: Q9UJU2-6)

The sequence of this isoform differs from the canonical sequence as follows:
     214-241: Missing.
     390-399: TGPRMTAAYI → GKRSSFPTCKAKAATPGPLLEMEAC
Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.
Isoform 7 (identifier: Q9UJU2-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: MPQLSGGGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLADIKSSLVNESEIIPASNGH → MA
     214-241: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399Lymphoid enhancer-binding factor 1
PRO_0000048595

Regions

DNA binding299 – 36769HMG box
Region1 – 6262CTNNB1-binding By similarity
Compositional bias6 – 138Poly-Gly
Compositional bias14 – 5239Asp/Glu-rich (acidic)
Compositional bias77 – 273197Pro-rich
Compositional bias374 – 3796Poly-Lys

Amino acid modifications

Modified residue1321Phosphoserine Ref.17
Modified residue1551Phosphothreonine; by NLK Probable
Modified residue1661Phosphoserine; by NLK Probable
Cross-link27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link269Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 115115Missing in isoform 3 and isoform 4.
VSP_007022
Alternative sequence1 – 7070MPQLS…ASNGH → MA in isoform 7.
VSP_044877
Alternative sequence214 – 24128Missing in isoform 5, isoform 6 and isoform 7.
VSP_040068
Alternative sequence283 – 399117KPQHE…TAAYI → CSAFLLPHPFLIPSTPSPNH HHHHLLGSLSMNRERSRSQK DLTLRSL in isoform 2 and isoform 4.
VSP_002188
Alternative sequence390 – 39910TGPRMTAAYI → GKRSSFPTCKAKAATPGPLL EMEAC in isoform 6.
VSP_040069
Natural variant1131G → R in a colorectal cancer sample; somatic mutation. Ref.18
VAR_035935

Experimental info

Mutagenesis1551T → A: Reduced phosphorylation by NLK; when associated with A-166. Ref.15
Mutagenesis1661S → A: Reduced phosphorylation by NLK; when associated with A-155. Ref.15
Sequence conflict1461Q → R in BAH13928. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D480D440698EEFE3

FASTA39944,201
        10         20         30         40         50         60 
MPQLSGGGGG GGGDPELCAT DEMIPFKDEG DPQKEKIFAE ISHPEEEGDL ADIKSSLVNE 

        70         80         90        100        110        120 
SEIIPASNGH EVARQAQTSQ EPYHDKAREH PDDGKHPDGG LYNKGPSYSS YSGYIMMPNM 

       130        140        150        160        170        180 
NNDPYMSNGS LSPPIPRTSN KVPVVQPSHA VHPLTPLITY SDEHFSPGSH PSHIPSDVNS 

       190        200        210        220        230        240 
KQGMSRHPPA PDIPTFYPLS PGGVGQITPP LGWQGQPVYP ITGGFRQPYP SSLSVDTSMS 

       250        260        270        280        290        300 
RFSHHMIPGP PGPHTTGIPH PAIVTPQVKQ EHPHTDSDLM HVKPQHEQRK EQEPKRPHIK 

       310        320        330        340        350        360 
KPLNAFMLYM KEMRANVVAE CTLKESAAIN QILGRRWHAL SREEQAKYYE LARKERQLHM 

       370        380        390 
QLYPGWSARD NYGKKKKRKR EKLQESASGT GPRMTAAYI 

« Hide

Isoform 2 (B) (8A) [UniParc].

Checksum: 3632325D440CA5DD
Show »

FASTA32935,672
Isoform 3 (LEF-1-DN) [UniParc].

Checksum: 22320A1A195401ED
Show »

FASTA28431,919
Isoform 4 [UniParc].

Checksum: DDBF9358A5E8944C
Show »

FASTA21423,390
Isoform 5 [UniParc].

Checksum: F929C8679F4EC1A3
Show »

FASTA37141,162
Isoform 6 [UniParc].

Checksum: 918B4201D718A485
Show »

FASTA38642,676
Isoform 7 [UniParc].

Checksum: 38F7331074A62A79
Show »

FASTA30334,103

References

« Hide 'large scale' references
[1]"A thymus-specific member of the HMG protein family regulates the human T cell receptor C alpha enhancer."
Waterman M.L., Fischer W.H., Jones K.A.
Genes Dev. 5:656-669(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION.
[2]"The human LEF-1 gene contains a promoter preferentially active in lymphocytes and encodes multiple isoforms derived from alternative splicing."
Hovanes K., Li T.W., Waterman M.L.
Nucleic Acids Res. 28:1994-2003(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[3]"Lef-1 isoforms regulate different target genes and reduce cellular adhesion."
Jesse S., Koenig A., Ellenrieder V., Menke A.
Int. J. Cancer 126:1109-1120(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), ALTERNATIVE SPLICING, FUNCTION, TISSUE SPECIFICITY.
[4]"New transcript isoform of the human LEF-1 devoid of HMG domain, derived from alternative splicing of exon 8."
Kobielak A., Kobielak K., Trzeciak W.H.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7).
Tissue: Amygdala and Thymus.
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 1 AND 6).
Tissue: Skin and Testis.
[9]"ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for TCRalpha enhancer function."
Bruhn L., Munnerlyn A., Grosschedl R.
Genes Dev. 11:640-653(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALYREF/THOC4.
[10]"Two members of the Tcf family implicated in Wnt/b-catenin signaling during embryogenesis in the mouse."
Korinek V., Barker N., Willert K., Molenaar M., Roose J., Wagenaar G., Markman M., Lamers W., Destree O., Clevers H.
Mol. Cell. Biol. 18:1248-1256(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTNNB1.
[11]"Transcriptional repression by AML1 and LEF-1 is mediated by the TLE/Groucho corepressors."
Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D., Stifani S., Paroush Z., Groner Y.
Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TLE1, INHIBITION OF TRANSCRIPTIONAL ACTIVATION BY TLE1.
[12]"Beta-catenin-sensitive isoforms of lymphoid enhancer factor-1 are selectively expressed in colon cancer."
Hovanes K., Li T.W.H., Munguia J.E., Truong T., Milovanovic T., Lawrence Marsh J., Holcombe R.F., Waterman M.L.
Nat. Genet. 28:53-57(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION (ISOFORM 3), EXPRESSION IN COLON CANCER.
[13]"All Tcf HMG box transcription factors interact with Groucho-related co-repressors."
Brantjes H., Roose J., van De Wetering M., Clevers H.
Nucleic Acids Res. 29:1410-1419(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTIONAL INTERACTION WITH TLE1; TLE2; TLE3 AND TLE4.
[14]"I-mfa domain proteins interact with Axin and affect its regulation of the Wnt and c-Jun N-terminal kinase signaling pathways."
Kusano S., Raab-Traub N.
Mol. Cell. Biol. 22:6393-6405(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MDFI AND MDFIC.
[15]"Regulation of lymphoid enhancer factor 1/T-cell factor by mitogen-activated protein kinase-related Nemo-like kinase-dependent phosphorylation in Wnt/beta-catenin signaling."
Ishitani T., Ninomiya-Tsuji J., Matsumoto K.
Mol. Cell. Biol. 23:1379-1389(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NLK, PHOSPHORYLATION AT THR-155 AND/OR SER-166 BY NLK, MUTAGENESIS OF THR-155 AND SER-166.
[16]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[17]"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-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-113.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF288571 mRNA. Translation: AAG01022.1.
AF198532 mRNA. Translation: AAF13268.1.
AF294627 mRNA. Translation: AAG26886.1.
AK294395 mRNA. Translation: BAG57649.1.
AK303272 mRNA. Translation: BAH13928.1.
AC092539 Genomic DNA. No translation available.
AC097067 Genomic DNA. No translation available.
AC118062 Genomic DNA. No translation available.
AC123576 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX06223.1.
CH471057 Genomic DNA. Translation: EAX06225.1.
BC040559 mRNA. Translation: AAH40559.1.
BC050632 mRNA. Translation: AAH50632.1.
CCDSCCDS3679.1. [Q9UJU2-1]
CCDS47122.1. [Q9UJU2-6]
CCDS47123.1. [Q9UJU2-5]
CCDS54791.1. [Q9UJU2-7]
PIRA39625.
RefSeqNP_001124185.1. NM_001130713.2. [Q9UJU2-5]
NP_001124186.1. NM_001130714.2. [Q9UJU2-6]
NP_001159591.1. NM_001166119.1. [Q9UJU2-7]
NP_057353.1. NM_016269.4. [Q9UJU2-1]
UniGeneHs.743478.

3D structure databases

ProteinModelPortalQ9UJU2.
SMRQ9UJU2. Positions 13-62, 298-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119354. 34 interactions.
DIPDIP-29946N.
IntActQ9UJU2. 8 interactions.
MINTMINT-8329835.
STRING9606.ENSP00000265165.

PTM databases

PhosphoSiteQ9UJU2.

Polymorphism databases

DMDM8928194.

Proteomic databases

MaxQBQ9UJU2.
PaxDbQ9UJU2.
PRIDEQ9UJU2.

Protocols and materials databases

DNASU51176.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265165; ENSP00000265165; ENSG00000138795. [Q9UJU2-1]
ENST00000379951; ENSP00000369284; ENSG00000138795. [Q9UJU2-6]
ENST00000438313; ENSP00000406176; ENSG00000138795. [Q9UJU2-5]
ENST00000506680; ENSP00000422334; ENSG00000138795. [Q9UJU2-2]
ENST00000510624; ENSP00000422840; ENSG00000138795. [Q9UJU2-7]
GeneID51176.
KEGGhsa:51176.
UCSCuc003hyt.2. human. [Q9UJU2-1]
uc003hyu.2. human. [Q9UJU2-5]
uc003hyv.2. human. [Q9UJU2-6]

Organism-specific databases

CTD51176.
GeneCardsGC04M108968.
HGNCHGNC:6551. LEF1.
HPACAB019405.
HPA002087.
MIM153245. gene.
neXtProtNX_Q9UJU2.
PharmGKBPA30331.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG299161.
HOGENOMHOG000116032.
HOVERGENHBG000419.
InParanoidQ9UJU2.
KOK04492.
OMAGYSGYIM.
OrthoDBEOG7QNVMG.
PhylomeDBQ9UJU2.
TreeFamTF318448.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ9UJU2.

Gene expression databases

ArrayExpressQ9UJU2.
BgeeQ9UJU2.
CleanExHS_LEF1.
GenevestigatorQ9UJU2.

Family and domain databases

Gene3D1.10.30.10. 1 hit.
4.10.900.10. 1 hit.
InterProIPR027397. Catenin_binding_dom.
IPR013558. CTNNB1-bd_N.
IPR009071. HMG_box_dom.
IPR028769. LEF1.
IPR024940. TCF/LEF.
[Graphical view]
PANTHERPTHR10373. PTHR10373. 1 hit.
PTHR10373:SF11. PTHR10373:SF11. 1 hit.
PfamPF08347. CTNNB1_binding. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]
SMARTSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMSSF47095. SSF47095. 1 hit.
PROSITEPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLEF1. human.
GeneWikiLymphoid_enhancer-binding_factor_1.
GenomeRNAi51176.
NextBio54133.
PROQ9UJU2.
SOURCESearch...

Entry information

Entry nameLEF1_HUMAN
AccessionPrimary (citable) accession number: Q9UJU2
Secondary accession number(s): B4DG38 expand/collapse secondary AC list , B7Z8E2, E9PDK3, Q3ZCU4, Q9HAZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM