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P27782

- LEF1_MOUSE

UniProt

P27782 - LEF1_MOUSE

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Protein

Lymphoid enhancer-binding factor 1

Gene
Lef1, Lef-1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 By similarity. Regulates T-cell receptor alpha enhancer function. Binds DNA in a sequence-specific manner. PIASG antagonizes both Wnt-dependent and Wnt-independent activation by LEF1.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi297 – 36569HMG boxAdd
BLAST

GO - Molecular functioni

  1. armadillo repeat domain binding Source: RefGenome
  2. beta-catenin binding Source: RefGenome
  3. chromatin binding Source: MGI
  4. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: Ensembl
  5. DNA binding Source: UniProtKB
  6. DNA binding, bending Source: UniProtKB
  7. enhancer binding Source: RefGenome
  8. estrogen receptor activity Source: Ensembl
  9. estrogen receptor binding Source: RefGenome
  10. gamma-catenin binding Source: RefGenome
  11. protein binding Source: UniProtKB
  12. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: MGI
  13. RNA polymerase II regulatory region sequence-specific DNA binding Source: Ensembl
  14. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  15. sequence-specific DNA binding Source: MGI
  16. sequence-specific DNA binding transcription factor activity Source: MGI
  17. transcription factor binding Source: MGI
  18. transcription regulatory region DNA binding Source: MGI

GO - Biological processi

  1. alpha-beta T cell differentiation Source: MGI
  2. anatomical structure regression Source: MGI
  3. apoptotic process involved in morphogenesis Source: MGI
  4. apoptotic process involved in patterning of blood vessels Source: MGI
  5. B cell proliferation Source: MGI
  6. BMP signaling pathway Source: MGI
  7. canonical Wnt signaling pathway Source: RefGenome
  8. cell chemotaxis Source: Ensembl
  9. cell development Source: MGI
  10. cellular response to interleukin-4 Source: Ensembl
  11. chorio-allantoic fusion Source: MGI
  12. dentate gyrus development Source: MGI
  13. embryonic limb morphogenesis Source: MGI
  14. epithelial to mesenchymal transition Source: BHF-UCL
  15. eye pigmentation Source: RefGenome
  16. face morphogenesis Source: MGI
  17. forebrain neuroblast division Source: MGI
  18. forebrain neuron differentiation Source: RefGenome
  19. forebrain radial glial cell differentiation Source: MGI
  20. formation of radial glial scaffolds Source: MGI
  21. hippocampus development Source: MGI
  22. histone H3 acetylation Source: Ensembl
  23. histone H4 acetylation Source: Ensembl
  24. hypothalamus development Source: RefGenome
  25. mammary gland development Source: MGI
  26. muscle fiber development Source: RefGenome
  27. negative regulation of apoptotic process in bone marrow Source: RefGenome
  28. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  29. negative regulation of cell-cell adhesion Source: Ensembl
  30. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RefGenome
  31. negative regulation of DNA binding Source: Ensembl
  32. negative regulation of estrogen receptor binding Source: Ensembl
  33. negative regulation of interleukin-13 production Source: RefGenome
  34. negative regulation of interleukin-4 production Source: RefGenome
  35. negative regulation of interleukin-5 production Source: RefGenome
  36. negative regulation of striated muscle tissue development Source: MGI
  37. negative regulation of transcription, DNA-templated Source: MGI
  38. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  39. neural crest cell migration Source: RefGenome
  40. neutrophil differentiation Source: RefGenome
  41. odontoblast differentiation Source: RefGenome
  42. odontogenesis of dentin-containing tooth Source: MGI
  43. osteoblast differentiation Source: RefGenome
  44. palate development Source: BHF-UCL
  45. paraxial mesoderm formation Source: MGI
  46. patterning of blood vessels Source: MGI
  47. positive regulation by host of viral transcription Source: Ensembl
  48. positive regulation of cell-cell adhesion Source: Ensembl
  49. positive regulation of cell cycle process Source: Ensembl
  50. positive regulation of cell growth Source: Ensembl
  51. positive regulation of cell migration Source: Ensembl
  52. positive regulation of cell proliferation in bone marrow Source: RefGenome
  53. positive regulation of epithelial to mesenchymal transition Source: Ensembl
  54. positive regulation of granulocyte differentiation Source: Ensembl
  55. positive regulation of transcription, DNA-templated Source: MGI
  56. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  57. regulation of cell-cell adhesion Source: MGI
  58. regulation of transcription from RNA polymerase II promoter Source: MGI
  59. regulation of Wnt signaling pathway Source: MGI
  60. sensory perception of taste Source: MGI
  61. somitogenesis Source: MGI
  62. sprouting angiogenesis Source: MGI
  63. T cell receptor V(D)J recombination Source: MGI
  64. T-helper 1 cell differentiation Source: UniProtKB
  65. tongue development Source: MGI
  66. trachea gland development Source: MGI
  67. vasculature development Source: MGI
  68. Wnt signaling pathway Source: MGI
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_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_219771. deactivation of the beta-catenin transactivating complex.
REACT_221970. Ca2+ pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Lymphoid enhancer-binding factor 1
Short name:
LEF-1
Gene namesi
Name:Lef1
Synonyms:Lef-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:96770. Lef1.

Subcellular locationi

Nucleus
Note: Found in nuclear bodies upon PIASG binding.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleus Source: UniProtKB
  3. protein-DNA complex Source: Ensembl
  4. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191D → A: Strongly diminishes CTNNB1 binding and transactivation. Prevents nuclear translocation of CTNNB1. 1 Publication
Mutagenesisi20 – 201E → A: Prevents nuclear translocation of CTNNB1. 1 Publication
Mutagenesisi24 – 241F → A: Strongly diminishes CTNNB1 binding and transactivation. Prevents nuclear translocation of CTNNB1. 1 Publication
Mutagenesisi26 – 261D → A: Prevents nuclear translocation of CTNNB1. 1 Publication
Mutagenesisi27 – 271E → A: Prevents nuclear translocation of CTNNB1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Lymphoid enhancer-binding factor 1PRO_0000048596Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki25 – 25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei130 – 1301Phosphoserine By similarity
Modified residuei153 – 1531Phosphothreonine; by NLK By similarity
Modified residuei164 – 1641Phosphoserine; by NLK By similarity
Cross-linki267 – 267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Phosphorylated at Thr-153 and/or Ser-164 by NLK. Phosphorylation by NLK at these sites represses LEF1-mediated transcriptional activation of target genes of the canonical Wnt signaling pathway By similarity.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP27782.

PTM databases

PhosphoSiteiP27782.

Expressioni

Tissue specificityi

Lymphocytes. Found in distinct epithelial cell compartments of the skin and is abundant in the hair-producing progenitors of the follicle.1 Publication

Developmental stagei

Detected throughout the basal layer, in ectodermal placodes and the underlying dermal condensates in embryonic skin, and in epithelium and mesenchyme from early hair germs. At birth expression decreases in the basal level of the epidermis and increases in hair bulbs, in particular in matrix and precortex. At day 6-9 expression is concentrated in follicle bulbs and in the hair shaft in a concentric ring of hair-keratin-expressing cells derived from the precortex. Detected in dermal papilla throughout the hair cycle, and in a subset of cells emanating from the bulge to form the secondary hair germ.

Gene expression databases

ArrayExpressiP27782.
BgeeiP27782.
CleanExiMM_LEF1.
GenevestigatoriP27782.

Interactioni

Subunit structurei

Binds the armadillo repeat of CTNNB1 and forms a stable complex. Binds TLE1, ALYREF/THOC4, MDFI and MDFIC By similarity. Interacts with NLK By similarity. Interacts with EP300 and PIASG.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ctnnb1Q022486EBI-984464,EBI-397872
JRKO755643EBI-984464,EBI-8607681From a different organism.

Protein-protein interaction databases

BioGridi201137. 13 interactions.
DIPiDIP-35132N.
IntActiP27782. 6 interactions.
MINTiMINT-8177749.

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni13 – 164
Beta strandi32 – 343
Helixi48 – 5811
Helixi303 – 31816
Helixi324 – 33512
Helixi340 – 36021
Turni370 – 3723

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LEFNMR-A296-380[»]
3OUWX-ray2.91B1-63[»]
3OUXX-ray2.40B1-63[»]
ProteinModelPortaliP27782.
SMRiP27782. Positions 11-60, 296-371.

Miscellaneous databases

EvolutionaryTraceiP27782.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6060CTNNB1-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 116Poly-Gly
Compositional biasi12 – 5039Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi75 – 271197Pro-richAdd
BLAST
Compositional biasi372 – 3776Poly-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.

Phylogenomic databases

eggNOGiNOG299161.
HOGENOMiHOG000116032.
HOVERGENiHBG000419.
InParanoidiP27782.
KOiK04492.
OMAiGYSGYIM.
OrthoDBiEOG7QNVMG.
PhylomeDBiP27782.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P27782-1) [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

MPQLSGGGGG GDPELCATDE MIPFKDEGDP QKEKIFAEIS HPEEEGDLAD    50
IKSSLVNESE IIPASNGHEV VRQAPSSQEP YHDKAREHPD EGKHPDGGLY 100
NKGPSYSSYS GYIMMPNMNS DPYMSNGSLS PPIPRTSNKV PVVQPSHAVH 150
PLTPLITYSD EHFSPGSHPS HIPSDVNSKQ GMSRHPPAPE IPTFYPLSPG 200
GVGQITPPIG WQGQPVYPIT GGFRQPYPSS LSGDTSMSRF SHHMIPGPPG 250
PHTTGIPHPA IVTPQVKQEH PHTDSDLMHV KPQHEQRKEQ EPKRPHIKKP 300
LNAFMLYMKE MRANVVAECT LKESAAINQI LGRRWHALSR EEQAKYYELA 350
RKERQLHMQL YPGWSARDNY GKKKKRKREK LQESTSGTGP RMTAAYI 397
Length:397
Mass (Da):44,059
Last modified:August 1, 1992 - v1
Checksum:i0CA01B6C528FD7FA
GO
Isoform 2 (identifier: P27782-2) [UniParc]FASTAAdd to Basket

Also known as: LEF-1S

The sequence of this isoform differs from the canonical sequence as follows:
     1-113: Missing.

Show »
Length:284
Mass (Da):31,894
Checksum:i86E7EBEA4B85F890
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 113113Missing in isoform 2. VSP_006983Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58636 mRNA. Translation: CAA41493.1.
D16503 mRNA. Translation: BAA03954.1.
CCDSiCCDS17842.1. [P27782-1]
PIRiA39565.
RefSeqiNP_034833.2. NM_010703.4. [P27782-1]
UniGeneiMm.255219.

Genome annotation databases

EnsembliENSMUST00000029611; ENSMUSP00000029611; ENSMUSG00000027985. [P27782-1]
GeneIDi16842.
KEGGimmu:16842.
UCSCiuc008rjf.1. mouse. [P27782-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58636 mRNA. Translation: CAA41493.1 .
D16503 mRNA. Translation: BAA03954.1 .
CCDSi CCDS17842.1. [P27782-1 ]
PIRi A39565.
RefSeqi NP_034833.2. NM_010703.4. [P27782-1 ]
UniGenei Mm.255219.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LEF NMR - A 296-380 [» ]
3OUW X-ray 2.91 B 1-63 [» ]
3OUX X-ray 2.40 B 1-63 [» ]
ProteinModelPortali P27782.
SMRi P27782. Positions 11-60, 296-371.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201137. 13 interactions.
DIPi DIP-35132N.
IntActi P27782. 6 interactions.
MINTi MINT-8177749.

PTM databases

PhosphoSitei P27782.

Proteomic databases

PRIDEi P27782.

Protocols and materials databases

DNASUi 16842.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029611 ; ENSMUSP00000029611 ; ENSMUSG00000027985 . [P27782-1 ]
GeneIDi 16842.
KEGGi mmu:16842.
UCSCi uc008rjf.1. mouse. [P27782-1 ]

Organism-specific databases

CTDi 51176.
MGIi MGI:96770. Lef1.

Phylogenomic databases

eggNOGi NOG299161.
HOGENOMi HOG000116032.
HOVERGENi HBG000419.
InParanoidi P27782.
KOi K04492.
OMAi GYSGYIM.
OrthoDBi EOG7QNVMG.
PhylomeDBi P27782.
TreeFami TF318448.

Enzyme and pathway databases

Reactomei REACT_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_219771. deactivation of the beta-catenin transactivating complex.
REACT_221970. Ca2+ pathway.

Miscellaneous databases

ChiTaRSi LEF1. mouse.
EvolutionaryTracei P27782.
NextBioi 290768.
PROi P27782.
SOURCEi Search...

Gene expression databases

ArrayExpressi P27782.
Bgeei P27782.
CleanExi MM_LEF1.
Genevestigatori P27782.

Family and domain databases

Gene3Di 1.10.30.10. 1 hit.
4.10.900.10. 1 hit.
InterProi IPR027397. Catenin_binding_dom.
IPR013558. CTNNB1-bd_N.
IPR009071. HMG_box_dom.
IPR024940. TCF/LEF.
[Graphical view ]
PANTHERi PTHR10373. PTHR10373. 1 hit.
Pfami PF08347. CTNNB1_binding. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view ]
SMARTi SM00398. HMG. 1 hit.
[Graphical view ]
SUPFAMi SSF47095. SSF47095. 1 hit.
PROSITEi PS50118. HMG_BOX_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "LEF-1, a gene encoding a lymphoid-specific protein with an HMG domain, regulates T-cell receptor alpha enhancer function."
    Travis A., Amsterdam A., Belanger C., Grosschedl R.
    Genes Dev. 5:880-894(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6 X DBA.
  2. "Nucleotide sequence of a cDNA encoding an alternative form of LEF-1."
    Fujimoto S., Morita K., Kanaitsuka T., Germeraad W.T., Mazda O., Katsura Y.
    Nucleic Acids Res. 21:4403-4403(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/6.
  3. "Multiple roles for activated LEF/TCF transcription complexes during hair follicle development and differentiation."
    DasGupta R., Fuchs E.
    Development 126:4557-4568(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. Cited for: INTERACTION WITH CTNNB1, MUTAGENESIS OF ASP-19; GLU-20; PHE-24; ASP-26 AND GLU-27.
  5. "Tcf3 and Lef1 regulate lineage differentiation of multipotent stem cells in skin."
    Merrill B.J., Gat U., DasGupta R., Fuchs E.
    Genes Dev. 15:1688-1705(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HAIR DEVELOPMENT.
  6. "PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies."
    Sachdev S., Bruhn L., Sieber H., Pichler A., Melchior F., Grosschedl R.
    Genes Dev. 15:3088-3103(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, INTERACTION WITH PIASG, LOCATION IN NUCLEAR BODIES.
  7. "Identification of a promoter-specific transcriptional activation domain at the C-terminus of the Wnt effector protein T-cell factor 4."
    Hecht A., Stemmler M.P.
    J. Biol. Chem. 278:3776-3785(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EP300.
  8. "Structural basis for DNA bending by the architectural transcription factor LEF-1."
    Love J.J., Li X., Case D.A., Glese K., Grosschedl P., Wright P.E.
    Nature 376:791-795(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 296-380.
  9. "High resolution NMR structure of the LEF-1 HMG domain complexed with its cognate DNA."
    Li X., Love J.J., Case D.A., Wright P.E.
    Submitted (OCT-1998) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 296-380.

Entry informationi

Entry nameiLEF1_MOUSE
AccessioniPrimary (citable) accession number: P27782
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: September 3, 2014
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

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

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