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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)DescriptionActionsGraphical viewLength
DNA bindingi299 – 367HMG boxPROSITE-ProRule annotationAdd BLAST69

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: Ensembl
  • 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
  • histone deacetylase binding Source: ParkinsonsUK-UCL
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: BHF-UCL
  • sequence-specific DNA binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: Ensembl
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: BHF-UCL
  • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding Source: GO_Central
  • transcription factor activity, sequence-specific DNA binding 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
  • beta-catenin-TCF complex assembly Source: Reactome
  • 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
  • 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
  • Wnt signaling pathway, calcium modulating pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000138795-MONOMER.
ReactomeiR-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-4086398. Ca2+ pathway.
R-HSA-4411364. Binding of TCF/LEF:CTNNB1 to target gene promoters.
R-HSA-4641265. Repression of WNT target genes.
SignaLinkiQ9UJU2.
SIGNORiQ9UJU2.

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
Proteomesi
  • UP000005640 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

  • beta-catenin-TCF complex Source: ParkinsonsUK-UCL
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi155T → A: Reduced phosphorylation by NLK; when associated with A-166. 1 Publication1
Mutagenesisi166S → A: Reduced phosphorylation by NLK; when associated with A-155. 1 Publication1

Organism-specific databases

DisGeNETi51176.
OpenTargetsiENSG00000138795.
PharmGKBiPA30331.

Chemistry databases

ChEMBLiCHEMBL3217392.

Polymorphism and mutation databases

BioMutaiLEF1.
DMDMi8928194.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000485951 – 399Lymphoid enhancer-binding factor 1Add BLAST399

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei132PhosphoserineCombined sources1
Modified residuei155Phosphothreonine; by NLK1 Publication1
Modified residuei166Phosphoserine; by NLK1 Publication1
Cross-linki269Glycyl 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

PaxDbiQ9UJU2.
PeptideAtlasiQ9UJU2.
PRIDEiQ9UJU2.
TopDownProteomicsiQ9UJU2-2. [Q9UJU2-2]

PTM databases

iPTMnetiQ9UJU2.
PhosphoSitePlusiQ9UJU2.

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

BgeeiENSG00000138795.
CleanExiHS_LEF1.
ExpressionAtlasiQ9UJU2. baseline and differential.
GenevisibleiQ9UJU2. HS.

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
CTNNB1P352226EBI-926131,EBI-491549
IGF1RP080695EBI-926131,EBI-475981

GO - Molecular functioni

  • armadillo repeat domain binding Source: BHF-UCL
  • beta-catenin binding Source: UniProtKB
  • C2H2 zinc finger domain binding Source: UniProtKB
  • estrogen receptor binding Source: UniProtKB
  • gamma-catenin binding Source: BHF-UCL
  • histone binding Source: UniProtKB
  • histone deacetylase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi119354. 38 interactors.
DIPiDIP-29946N.
IntActiQ9UJU2. 19 interactors.
MINTiMINT-8329835.
STRINGi9606.ENSP00000265165.

Structurei

3D structure databases

ProteinModelPortaliQ9UJU2.
SMRiQ9UJU2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 62CTNNB1-bindingBy similarityAdd BLAST62

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi6 – 13Poly-Gly8
Compositional biasi14 – 52Asp/Glu-rich (acidic)Add BLAST39
Compositional biasi77 – 273Pro-richAdd BLAST197
Compositional biasi374 – 379Poly-Lys6

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

eggNOGiKOG3248. Eukaryota.
ENOG41109RU. LUCA.
GeneTreeiENSGT00390000009964.
HOGENOMiHOG000116032.
HOVERGENiHBG000419.
InParanoidiQ9UJU2.
KOiK04492.
OMAiGYSGYIM.
OrthoDBiEOG091G0705.
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.
IPR024940. TCF/LEF.
[Graphical view]
PANTHERiPTHR10373. PTHR10373. 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)DescriptionActionsGraphical viewLength
Sequence conflicti146Q → R in BAH13928 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035935113G → R in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs369649181dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0070221 – 115Missing in isoform 3 and isoform 4. 1 PublicationAdd BLAST115
Alternative sequenceiVSP_0448771 – 70MPQLS…ASNGH → MA in isoform 7. 1 PublicationAdd BLAST70
Alternative sequenceiVSP_040068214 – 241Missing in isoform 5, isoform 6 and isoform 7. 3 PublicationsAdd BLAST28
Alternative sequenceiVSP_002188283 – 399KPQHE…TAAYI → CSAFLLPHPFLIPSTPSPNH HHHHLLGSLSMNRERSRSQK DLTLRSL in isoform 2 and isoform 4. 1 PublicationAdd BLAST117
Alternative sequenceiVSP_040069390 – 399TGPRMTAAYI → GKRSSFPTCKAKAATPGPLL EMEAC in isoform 6. 1 Publication10

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.3. human. [Q9UJU2-1]

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119354. 38 interactors.
DIPiDIP-29946N.
IntActiQ9UJU2. 19 interactors.
MINTiMINT-8329835.
STRINGi9606.ENSP00000265165.

Chemistry databases

ChEMBLiCHEMBL3217392.

PTM databases

iPTMnetiQ9UJU2.
PhosphoSitePlusiQ9UJU2.

Polymorphism and mutation databases

BioMutaiLEF1.
DMDMi8928194.

Proteomic databases

PaxDbiQ9UJU2.
PeptideAtlasiQ9UJU2.
PRIDEiQ9UJU2.
TopDownProteomicsiQ9UJU2-2. [Q9UJU2-2]

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.3. human. [Q9UJU2-1]

Organism-specific databases

CTDi51176.
DisGeNETi51176.
GeneCardsiLEF1.
HGNCiHGNC:6551. LEF1.
HPAiCAB019405.
HPA002087.
MIMi153245. gene.
neXtProtiNX_Q9UJU2.
OpenTargetsiENSG00000138795.
PharmGKBiPA30331.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3248. Eukaryota.
ENOG41109RU. LUCA.
GeneTreeiENSGT00390000009964.
HOGENOMiHOG000116032.
HOVERGENiHBG000419.
InParanoidiQ9UJU2.
KOiK04492.
OMAiGYSGYIM.
OrthoDBiEOG091G0705.
PhylomeDBiQ9UJU2.
TreeFamiTF318448.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000138795-MONOMER.
ReactomeiR-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-4086398. Ca2+ pathway.
R-HSA-4411364. Binding of TCF/LEF:CTNNB1 to target gene promoters.
R-HSA-4641265. Repression of WNT target genes.
SignaLinkiQ9UJU2.
SIGNORiQ9UJU2.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000138795.
CleanExiHS_LEF1.
ExpressionAtlasiQ9UJU2. baseline and differential.
GenevisibleiQ9UJU2. HS.

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.
IPR024940. TCF/LEF.
[Graphical view]
PANTHERiPTHR10373. PTHR10373. 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...

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: November 30, 2016
This is version 164 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

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 one 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.