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Protein

Lymphoid enhancer-binding factor 1

Gene

Lef1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. PIASG antagonizes both Wnt-dependent and Wnt-independent activation by LEF1 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi297 – 36569HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lymphoid enhancer-binding factor 1
Short name:
LEF-1
Gene namesi
Name:Lef1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620241. Lef1.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

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

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • nucleoplasm Source: Reactome
  • nucleus Source: RGD
  • transcription factor complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Lymphoid enhancer-binding factor 1PRO_0000048597Add
BLAST

Amino acid modifications

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

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).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9QXN1.

PTM databases

iPTMnetiQ9QXN1.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi250906. 1 interaction.
IntActiQ9QXN1. 1 interaction.
MINTiMINT-8388232.
STRINGi10116.ENSRNOP00000013694.

Structurei

3D structure databases

DisProtiDP00046.
ProteinModelPortaliQ9QXN1.
SMRiQ9QXN1. Positions 2-59, 296-371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6060CTNNB1-bindingBy similarityAdd
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.Curated
Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3248. Eukaryota.
ENOG41109RU. LUCA.
HOGENOMiHOG000116032.
HOVERGENiHBG000419.
InParanoidiQ9QXN1.
KOiK04492.
PhylomeDBiQ9QXN1.

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]

Sequencei

Sequence statusi: Complete.

Q9QXN1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQLSGGGGG GDPELCATDE MIPFKDEGDP QKEKIFAEIS HPEEEGDLAD
60 70 80 90 100
IKSSLVNESE IIPASNGHEV VGQTQSSQEP YHDKAREHPD DGKHPDGGLY
110 120 130 140 150
NKGPSYSSYS GYIMMPNMNS DPYMSNGSLS PPIPRTSNKV PVVQPSHAVH
160 170 180 190 200
PLTPLITYSD EHFSPGSHPS HIPSEVNPKQ GMSRHPPAPE MPTFYPLSPG
210 220 230 240 250
GVGQITPPLG WQGQPVYPIT GGFRQAYPSS LSGDTSMSRF SHHMIPGPPG
260 270 280 290 300
PHTTGIPHPA IVTPQVKQEH PHTDSDLMHV KPEHEQRKEQ EPKRPHIKKP
310 320 330 340 350
LNAFMLYMKE MRANVVAECT LKESAAINQI LGRRWHALSR EEQAKYYELA
360 370 380 390
RKERQLHMQL YPGWSARDNY GKKKKRKREK LQESTSGTGP RMTAAYI
Length:397
Mass (Da):44,023
Last modified:May 1, 2000 - v1
Checksum:iD6BEFF805CB526EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF198533 mRNA. Translation: AAF15601.1.
RefSeqiNP_569113.1. NM_130429.1.
UniGeneiRn.228611.

Genome annotation databases

GeneIDi161452.
KEGGirno:161452.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF198533 mRNA. Translation: AAF15601.1.
RefSeqiNP_569113.1. NM_130429.1.
UniGeneiRn.228611.

3D structure databases

DisProtiDP00046.
ProteinModelPortaliQ9QXN1.
SMRiQ9QXN1. Positions 2-59, 296-371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250906. 1 interaction.
IntActiQ9QXN1. 1 interaction.
MINTiMINT-8388232.
STRINGi10116.ENSRNOP00000013694.

PTM databases

iPTMnetiQ9QXN1.

Proteomic databases

PaxDbiQ9QXN1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi161452.
KEGGirno:161452.

Organism-specific databases

CTDi51176.
RGDi620241. Lef1.

Phylogenomic databases

eggNOGiKOG3248. Eukaryota.
ENOG41109RU. LUCA.
HOGENOMiHOG000116032.
HOVERGENiHBG000419.
InParanoidiQ9QXN1.
KOiK04492.
PhylomeDBiQ9QXN1.

Miscellaneous databases

PROiQ9QXN1.

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...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiLEF1_RAT
AccessioniPrimary (citable) accession number: Q9QXN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 127 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

Complete proteome, Reference proteome

Documents

  1. 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.