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Q9QXN1 (LEF1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lymphoid enhancer-binding factor 1

Short name=LEF-1
Gene names
Name:Lef1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. PIASG antagonizes both Wnt-dependent and Wnt-independent activation by LEF1 By similarity.

Subunit structure

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

Subcellular location

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

Domain

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

Post-translational modification

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.

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
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
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

alpha-beta T cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

apoptosis involved in morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

canonical Wnt receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

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 Biological aspect of Ancestor. Source: RefGenome

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

hypothalamus development

Inferred from Biological aspect of Ancestor. Source: RefGenome

induction of apoptosis

Inferred from Biological aspect of Ancestor. Source: RefGenome

kidney development

Inferred from expression pattern. Source: RGD

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 apoptotic process in bone marrow

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of interleukin-13 production

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of interleukin-4 production

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of interleukin-5 production

Inferred from Biological aspect of Ancestor. Source: RefGenome

neural crest cell migration

Inferred from Biological aspect of Ancestor. Source: RefGenome

neutrophil differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

odontoblast differentiation

Inferred from mutant phenotype. Source: RGD

organ regeneration

Inferred from expression pattern. Source: RGD

osteoblast differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

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 of cell proliferation in bone marrow

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to lithium ion

Inferred from expression pattern. Source: RGD

response to organic cyclic compound

Inferred from expression pattern. Source: RGD

skin development

Inferred from expression pattern. Source: RGD

somitogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

sprouting angiogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

trachea gland development

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription factor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular functionDNA binding, bending

Inferred from sequence or structural similarity. Source: UniProtKB

armadillo repeat domain binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

beta-catenin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

chromatin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

enhancer binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

estrogen receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

gamma-catenin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

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

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397Lymphoid enhancer-binding factor 1
PRO_0000048597

Regions

DNA binding297 – 36569HMG box
Region1 – 6060CTNNB1-binding By similarity
Compositional bias6 – 116Poly-Gly
Compositional bias12 – 5039Asp/Glu-rich (acidic)
Compositional bias75 – 271197Pro-rich
Compositional bias372 – 3776Poly-Lys

Amino acid modifications

Modified residue931N6-acetyllysine By similarity
Modified residue1301Phosphoserine By similarity
Modified residue1531Phosphothreonine; by NLK By similarity
Modified residue1641Phosphoserine; by NLK By similarity
Cross-link25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9QXN1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D6BEFF805CB526EA

FASTA39744,023
        10         20         30         40         50         60 
MPQLSGGGGG GDPELCATDE MIPFKDEGDP QKEKIFAEIS HPEEEGDLAD IKSSLVNESE 

        70         80         90        100        110        120 
IIPASNGHEV VGQTQSSQEP YHDKAREHPD DGKHPDGGLY NKGPSYSSYS GYIMMPNMNS 

       130        140        150        160        170        180 
DPYMSNGSLS PPIPRTSNKV PVVQPSHAVH PLTPLITYSD EHFSPGSHPS HIPSEVNPKQ 

       190        200        210        220        230        240 
GMSRHPPAPE MPTFYPLSPG GVGQITPPLG WQGQPVYPIT GGFRQAYPSS LSGDTSMSRF 

       250        260        270        280        290        300 
SHHMIPGPPG PHTTGIPHPA IVTPQVKQEH PHTDSDLMHV KPEHEQRKEQ EPKRPHIKKP 

       310        320        330        340        350        360 
LNAFMLYMKE MRANVVAECT LKESAAINQI LGRRWHALSR EEQAKYYELA RKERQLHMQL 

       370        380        390 
YPGWSARDNY GKKKKRKREK LQESTSGTGP RMTAAYI 

« Hide

References

[1]"Cloning of the lymphoid enhancer binding factor-1 (Lef-1) cDNA from rat kidney: homology to the mouse sequence."
Kobielak K., Kobielak A., Trzeciak W.H.
Acta Biochim. Pol. 46:885-888(1999) [PubMed: 10824856] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF198533 mRNA. Translation: AAF15601.1.
IPIIPI00213373.
RefSeqNP_569113.1. NM_130429.1.
UniGeneRn.21926.

3D structure databases

ProteinModelPortalQ9QXN1.
SMRQ9QXN1. Positions 2-59, 296-371.
DisProtDP00046.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9QXN1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID161452.
KEGGrno:161452.

Organism-specific databases

CTD51176.
RGD620241. Lef1.

Phylogenomic databases

GeneTreeENSGT00390000009964.
HOVERGENHBG000419.
InParanoidQ9QXN1.

Gene expression databases

ArrayExpressQ9QXN1.
GenevestigatorQ9QXN1.
GermOnlineENSRNOG00000010121. Rattus norvegicus.

Family and domain databases

InterProIPR013558. CTNNB1-bd_N.
IPR000910. HMG_HMG1/HMG2.
IPR009071. HMG_superfamily.
[Graphical view]
Gene3DG3DSA:1.10.30.10. HMG-box. 1 hit.
KOK04492.
PfamPF08347. CTNNB1_binding. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]
SMARTSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMSSF47095. HMG-box. 1 hit.
PROSITEPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio620971.

Entry information

Entry nameLEF1_RAT
AccessionPrimary (citable) accession number: Q9QXN1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: November 16, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families