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Protein

Lymphoid enhancer-binding factor 1

Gene

LEF1

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

Functioni

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.By similarity3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi299 – 36769HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • armadillo repeat domain binding Source: BHF-UCL
  • beta-catenin binding Source: UniProtKB
  • C2H2 zinc finger domain binding Source: UniProtKB
  • chromatin binding Source: GO_Central
  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA binding, bending Source: UniProtKB
  • enhancer binding Source: UniProtKB
  • estrogen receptor activity Source: UniProtKB
  • estrogen receptor binding Source: UniProtKB
  • gamma-catenin binding Source: BHF-UCL
  • histone binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  • RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: GO_Central
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: BHF-UCL
  • RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
  • sequence-specific DNA binding Source: UniProtKB
  • sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  • alpha-beta T cell differentiation Source: GO_Central
  • anatomical structure regression Source: Ensembl
  • apoptotic process involved in morphogenesis Source: GO_Central
  • apoptotic process involved in patterning of blood vessels Source: Ensembl
  • B cell proliferation Source: GO_Central
  • BMP signaling pathway Source: GO_Central
  • canonical Wnt signaling pathway Source: UniProtKB
  • cell chemotaxis Source: UniProtKB
  • cellular response to cytokine stimulus Source: BHF-UCL
  • cellular response to interleukin-4 Source: UniProtKB
  • chorio-allantoic fusion Source: GO_Central
  • dentate gyrus development Source: GO_Central
  • embryonic limb morphogenesis Source: GO_Central
  • epithelial to mesenchymal transition Source: BHF-UCL
  • eye pigmentation Source: GO_Central
  • face morphogenesis Source: GO_Central
  • forebrain neuroblast division Source: GO_Central
  • forebrain neuron differentiation Source: GO_Central
  • forebrain radial glial cell differentiation Source: GO_Central
  • formation of radial glial scaffolds Source: GO_Central
  • histone H3 acetylation Source: UniProtKB
  • histone H4 acetylation Source: UniProtKB
  • hypothalamus development Source: GO_Central
  • mammary gland development Source: GO_Central
  • muscle fiber development Source: GO_Central
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of apoptotic process in bone marrow Source: UniProtKB
  • negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  • negative regulation of cell-cell adhesion Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • negative regulation of DNA binding Source: UniProtKB
  • negative regulation of estrogen receptor binding Source: UniProtKB
  • negative regulation of interleukin-13 production Source: UniProtKB
  • negative regulation of interleukin-4 production Source: UniProtKB
  • negative regulation of interleukin-5 production Source: UniProtKB
  • negative regulation of striated muscle tissue development Source: Ensembl
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • neural crest cell migration Source: GO_Central
  • neutrophil differentiation Source: UniProtKB
  • odontoblast differentiation Source: GO_Central
  • odontogenesis of dentin-containing tooth Source: Ensembl
  • osteoblast differentiation Source: UniProtKB
  • palate development Source: BHF-UCL
  • paraxial mesoderm formation Source: GO_Central
  • patterning of blood vessels Source: GO_Central
  • positive regulation by host of viral transcription Source: UniProtKB
  • positive regulation of cell-cell adhesion Source: UniProtKB
  • positive regulation of cell cycle process Source: UniProtKB
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of cell proliferation in bone marrow Source: UniProtKB
  • positive regulation of epithelial to mesenchymal transition Source: UniProtKB
  • positive regulation of gene expression Source: AgBase
  • positive regulation of granulocyte differentiation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of cell-cell adhesion Source: Ensembl
  • regulation of striated muscle tissue development Source: GO_Central
  • sensory perception of taste Source: Ensembl
  • somitogenesis Source: GO_Central
  • sprouting angiogenesis Source: GO_Central
  • steroid hormone mediated signaling pathway Source: GOC
  • T cell receptor V(D)J recombination Source: Ensembl
  • T-helper 1 cell differentiation Source: UniProtKB
  • tongue development Source: Ensembl
  • trachea gland development Source: GO_Central
  • transcription from RNA polymerase II promoter Source: BHF-UCL
  • Wnt signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_263982. Ca2+ pathway.
REACT_264178. deactivation of the beta-catenin transactivating complex.
REACT_264242. formation of the beta-catenin:TCF transactivating complex.
REACT_264532. binding of TCF/LEF:CTNNB1 to target gene promoters.
REACT_264567. repression of WNT target genes.
SignaLinkiQ9UJU2.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:LEF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:6551. LEF1.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

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

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein-DNA complex Source: BHF-UCL
  • transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi155 – 1551T → A: Reduced phosphorylation by NLK; when associated with A-166. 1 Publication
Mutagenesisi166 – 1661S → A: Reduced phosphorylation by NLK; when associated with A-155. 1 Publication

Organism-specific databases

PharmGKBiPA30331.

Polymorphism and mutation databases

BioMutaiLEF1.
DMDMi8928194.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 399399Lymphoid enhancer-binding factor 1PRO_0000048595Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki27 – 27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei132 – 1321Phosphoserine1 Publication
Modified residuei155 – 1551Phosphothreonine; by NLK1 Publication
Modified residuei166 – 1661Phosphoserine; by NLK1 Publication
Cross-linki269 – 269Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UJU2.
PaxDbiQ9UJU2.
PRIDEiQ9UJU2.

PTM databases

PhosphoSiteiQ9UJU2.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ9UJU2.
CleanExiHS_LEF1.
ExpressionAtlasiQ9UJU2. baseline and differential.
GenevestigatoriQ9UJU2.

Organism-specific databases

HPAiCAB019405.
HPA002087.

Interactioni

Subunit structurei

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.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352225EBI-926131,EBI-491549
IGF1RP080695EBI-926131,EBI-475981

Protein-protein interaction databases

BioGridi119354. 38 interactions.
DIPiDIP-29946N.
IntActiQ9UJU2. 17 interactions.
MINTiMINT-8329835.
STRINGi9606.ENSP00000265165.

Structurei

3D structure databases

ProteinModelPortaliQ9UJU2.
SMRiQ9UJU2. Positions 13-62, 298-373.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6262CTNNB1-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 138Poly-Gly
Compositional biasi14 – 5239Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi77 – 273197Pro-richAdd
BLAST
Compositional biasi374 – 3796Poly-Lys

Domaini

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

Sequence similaritiesi

Belongs to the TCF/LEF family.Curated
Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG299161.
GeneTreeiENSGT00390000009964.
HOGENOMiHOG000116032.
HOVERGENiHBG000419.
InParanoidiQ9UJU2.
KOiK04492.
OMAiGYSGYIM.
OrthoDBiEOG7QNVMG.
PhylomeDBiQ9UJU2.
TreeFamiTF318448.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
4.10.900.10. 1 hit.
InterProiIPR027397. Catenin_binding_dom.
IPR013558. CTNNB1-bd_N.
IPR009071. HMG_box_dom.
IPR028769. LEF1.
IPR024940. TCF/LEF.
[Graphical view]
PANTHERiPTHR10373. PTHR10373. 1 hit.
PTHR10373:SF11. PTHR10373:SF11. 1 hit.
PfamiPF08347. CTNNB1_binding. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9UJU2-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPQLSGGGGG GGGDPELCAT DEMIPFKDEG DPQKEKIFAE ISHPEEEGDL
60 70 80 90 100
ADIKSSLVNE SEIIPASNGH EVARQAQTSQ EPYHDKAREH PDDGKHPDGG
110 120 130 140 150
LYNKGPSYSS YSGYIMMPNM NNDPYMSNGS LSPPIPRTSN KVPVVQPSHA
160 170 180 190 200
VHPLTPLITY SDEHFSPGSH PSHIPSDVNS KQGMSRHPPA PDIPTFYPLS
210 220 230 240 250
PGGVGQITPP LGWQGQPVYP ITGGFRQPYP SSLSVDTSMS RFSHHMIPGP
260 270 280 290 300
PGPHTTGIPH PAIVTPQVKQ EHPHTDSDLM HVKPQHEQRK EQEPKRPHIK
310 320 330 340 350
KPLNAFMLYM KEMRANVVAE CTLKESAAIN QILGRRWHAL SREEQAKYYE
360 370 380 390
LARKERQLHM QLYPGWSARD NYGKKKKRKR EKLQESASGT GPRMTAAYI

Note: Produced by alternative promoter usage.

Length:399
Mass (Da):44,201
Last modified:May 1, 2000 - v1
Checksum:iD480D440698EEFE3
GO
Isoform 2 (identifier: Q9UJU2-2) [UniParc]FASTAAdd to basket

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.

Show »
Length:329
Mass (Da):35,672
Checksum:i3632325D440CA5DD
GO
Isoform 3 (identifier: Q9UJU2-3) [UniParc]FASTAAdd to basket

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.

Show »
Length:284
Mass (Da):31,919
Checksum:i22320A1A195401ED
GO
Isoform 4 (identifier: Q9UJU2-4) [UniParc]FASTAAdd to basket

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.

Show »
Length:214
Mass (Da):23,390
Checksum:iDDBF9358A5E8944C
GO
Isoform 5 (identifier: Q9UJU2-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     214-241: Missing.

Note: Produced by alternative splicing of isoform 1.

Show »
Length:371
Mass (Da):41,162
Checksum:iF929C8679F4EC1A3
GO
Isoform 6 (identifier: Q9UJU2-6) [UniParc]FASTAAdd to basket

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.

Show »
Length:386
Mass (Da):42,676
Checksum:i918B4201D718A485
GO
Isoform 7 (identifier: Q9UJU2-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: MPQLSGGGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLADIKSSLVNESEIIPASNGH → MA
     214-241: Missing.

Note: No experimental confirmation available.

Show »
Length:303
Mass (Da):34,103
Checksum:i38F7331074A62A79
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461Q → R in BAH13928 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti113 – 1131G → R in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035935

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 115115Missing in isoform 3 and isoform 4. 1 PublicationVSP_007022Add
BLAST
Alternative sequencei1 – 7070MPQLS…ASNGH → MA in isoform 7. 1 PublicationVSP_044877Add
BLAST
Alternative sequencei214 – 24128Missing in isoform 5, isoform 6 and isoform 7. 3 PublicationsVSP_040068Add
BLAST
Alternative sequencei283 – 399117KPQHE…TAAYI → CSAFLLPHPFLIPSTPSPNH HHHHLLGSLSMNRERSRSQK DLTLRSL in isoform 2 and isoform 4. 1 PublicationVSP_002188Add
BLAST
Alternative sequencei390 – 39910TGPRMTAAYI → GKRSSFPTCKAKAATPGPLL EMEAC in isoform 6. 1 PublicationVSP_040069

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3679.1. [Q9UJU2-1]
CCDS47122.1. [Q9UJU2-6]
CCDS47123.1. [Q9UJU2-5]
CCDS54791.1. [Q9UJU2-7]
PIRiA39625.
RefSeqiNP_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]
UniGeneiHs.743478.

Genome annotation databases

EnsembliENST00000265165; ENSP00000265165; ENSG00000138795. [Q9UJU2-1]
ENST00000379951; ENSP00000369284; ENSG00000138795. [Q9UJU2-6]
ENST00000438313; ENSP00000406176; ENSG00000138795. [Q9UJU2-5]
ENST00000506680; ENSP00000422334; ENSG00000138795. [Q9UJU2-2]
ENST00000510624; ENSP00000422840; ENSG00000138795. [Q9UJU2-7]
GeneIDi51176.
KEGGihsa:51176.
UCSCiuc003hyt.2. human. [Q9UJU2-1]
uc003hyu.2. human. [Q9UJU2-5]
uc003hyv.2. human. [Q9UJU2-6]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3679.1. [Q9UJU2-1]
CCDS47122.1. [Q9UJU2-6]
CCDS47123.1. [Q9UJU2-5]
CCDS54791.1. [Q9UJU2-7]
PIRiA39625.
RefSeqiNP_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]
UniGeneiHs.743478.

3D structure databases

ProteinModelPortaliQ9UJU2.
SMRiQ9UJU2. Positions 13-62, 298-373.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119354. 38 interactions.
DIPiDIP-29946N.
IntActiQ9UJU2. 17 interactions.
MINTiMINT-8329835.
STRINGi9606.ENSP00000265165.

Chemistry

ChEMBLiCHEMBL3217392.

PTM databases

PhosphoSiteiQ9UJU2.

Polymorphism and mutation databases

BioMutaiLEF1.
DMDMi8928194.

Proteomic databases

MaxQBiQ9UJU2.
PaxDbiQ9UJU2.
PRIDEiQ9UJU2.

Protocols and materials databases

DNASUi51176.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265165; ENSP00000265165; ENSG00000138795. [Q9UJU2-1]
ENST00000379951; ENSP00000369284; ENSG00000138795. [Q9UJU2-6]
ENST00000438313; ENSP00000406176; ENSG00000138795. [Q9UJU2-5]
ENST00000506680; ENSP00000422334; ENSG00000138795. [Q9UJU2-2]
ENST00000510624; ENSP00000422840; ENSG00000138795. [Q9UJU2-7]
GeneIDi51176.
KEGGihsa:51176.
UCSCiuc003hyt.2. human. [Q9UJU2-1]
uc003hyu.2. human. [Q9UJU2-5]
uc003hyv.2. human. [Q9UJU2-6]

Organism-specific databases

CTDi51176.
GeneCardsiGC04M108968.
HGNCiHGNC:6551. LEF1.
HPAiCAB019405.
HPA002087.
MIMi153245. gene.
neXtProtiNX_Q9UJU2.
PharmGKBiPA30331.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG299161.
GeneTreeiENSGT00390000009964.
HOGENOMiHOG000116032.
HOVERGENiHBG000419.
InParanoidiQ9UJU2.
KOiK04492.
OMAiGYSGYIM.
OrthoDBiEOG7QNVMG.
PhylomeDBiQ9UJU2.
TreeFamiTF318448.

Enzyme and pathway databases

ReactomeiREACT_263982. Ca2+ pathway.
REACT_264178. deactivation of the beta-catenin transactivating complex.
REACT_264242. formation of the beta-catenin:TCF transactivating complex.
REACT_264532. binding of TCF/LEF:CTNNB1 to target gene promoters.
REACT_264567. repression of WNT target genes.
SignaLinkiQ9UJU2.

Miscellaneous databases

ChiTaRSiLEF1. human.
GeneWikiiLymphoid_enhancer-binding_factor_1.
GenomeRNAii51176.
NextBioi54133.
PROiQ9UJU2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJU2.
CleanExiHS_LEF1.
ExpressionAtlasiQ9UJU2. baseline and differential.
GenevestigatoriQ9UJU2.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
4.10.900.10. 1 hit.
InterProiIPR027397. Catenin_binding_dom.
IPR013558. CTNNB1-bd_N.
IPR009071. HMG_box_dom.
IPR028769. LEF1.
IPR024940. TCF/LEF.
[Graphical view]
PANTHERiPTHR10373. PTHR10373. 1 hit.
PTHR10373:SF11. PTHR10373:SF11. 1 hit.
PfamiPF08347. CTNNB1_binding. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-113.

Entry informationi

Entry nameiLEF1_HUMAN
AccessioniPrimary (citable) accession number: Q9UJU2
Secondary accession number(s): B4DG38
, B7Z8E2, E9PDK3, Q3ZCU4, Q9HAZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 147 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.