ID LEF1_MOUSE Reviewed; 397 AA. AC P27782; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 27-MAR-2024, entry version 216. DE RecName: Full=Lymphoid enhancer-binding factor 1 {ECO:0000312|MGI:MGI:96770}; DE Short=LEF-1 {ECO:0000303|PubMed:1827423}; GN Name=Lef1 {ECO:0000312|MGI:MGI:96770}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6 X DBA; RX PubMed=1827423; DOI=10.1101/gad.5.5.880; RA Travis A., Amsterdam A., Belanger C., Grosschedl R.; RT "LEF-1, a gene encoding a lymphoid-specific protein with an HMG domain, RT regulates T-cell receptor alpha enhancer function."; RL Genes Dev. 5:880-894(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; RX PubMed=8415007; DOI=10.1093/nar/21.18.4403; RA Fujimoto S., Morita K., Kanaitsuka T., Germeraad W.T., Mazda O., RA Katsura Y.; RT "Nucleotide sequence of a cDNA encoding an alternative form of LEF-1."; RL Nucleic Acids Res. 21:4403-4403(1993). RN [3] RP DEVELOPMENTAL STAGE. RX PubMed=8898217; DOI=10.1242/dev.122.10.3035; RA Chen Y., Bei M., Woo I., Satokata I., Maas R.; RT "Msx1 controls inductive signaling in mammalian tooth morphogenesis."; RL Development 122:3035-3044(1996). RN [4] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=10498690; DOI=10.1242/dev.126.20.4557; RA DasGupta R., Fuchs E.; RT "Multiple roles for activated LEF/TCF transcription complexes during hair RT follicle development and differentiation."; RL Development 126:4557-4568(1999). RN [5] RP INTERACTION WITH CTNNB1, AND MUTAGENESIS OF ASP-19; GLU-20; PHE-24; ASP-26 RP AND GLU-27. RX PubMed=10966653; DOI=10.1038/79039; RA von Kries J.P., Winbeck G., Asbrand C., Schwarz-Romond T., Sochnikova N., RA Dell'Oro A., Behrens J., Birchmeier W.; RT "Hot spots in beta-catenin for interactions with LEF-1, conductin and RT APC."; RL Nat. Struct. Biol. 7:800-807(2000). RN [6] RP FUNCTION IN HAIR DEVELOPMENT. RX PubMed=11445543; DOI=10.1101/gad.891401; RA Merrill B.J., Gat U., DasGupta R., Fuchs E.; RT "Tcf3 and Lef1 regulate lineage differentiation of multipotent stem cells RT in skin."; RL Genes Dev. 15:1688-1705(2001). RN [7] RP FUNCTION, INTERACTION WITH PIASG, LOCATION IN NUCLEAR BODIES, AND RP SUMOYLATION. RX PubMed=11731474; DOI=10.1101/gad.944801; RA Sachdev S., Bruhn L., Sieber H., Pichler A., Melchior F., Grosschedl R.; RT "PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity RT by sequestration into nuclear bodies."; RL Genes Dev. 15:3088-3103(2001). RN [8] RP FUNCTION, AND INTERACTION WITH EP300. RX PubMed=12446687; DOI=10.1074/jbc.m210081200; RA Hecht A., Stemmler M.P.; RT "Identification of a promoter-specific transcriptional activation domain at RT the C-terminus of the Wnt effector protein T-cell factor 4."; RL J. Biol. Chem. 278:3776-3785(2003). RN [9] RP TISSUE SPECIFICITY. RX PubMed=17218525; DOI=10.1126/science.1135344; RA Melichar H.J., Narayan K., Der S.D., Hiraoka Y., Gardiol N., Jeannet G., RA Held W., Chambers C.A., Kang J.; RT "Regulation of gammadelta versus alphabeta T lymphocyte differentiation by RT the transcription factor SOX13."; RL Science 315:230-233(2007). RN [10] RP INTERACTION WITH DAZAP2. RX PubMed=19304756; DOI=10.1093/nar/gkp179; RA Lukas J., Mazna P., Valenta T., Doubravska L., Pospichalova V., RA Vojtechova M., Fafilek B., Ivanek R., Plachy J., Novak J., Korinek V.; RT "Dazap2 modulates transcription driven by the Wnt effector TCF-4."; RL Nucleic Acids Res. 37:3007-3020(2009). RN [11] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=23562159; DOI=10.1016/j.immuni.2013.01.010; RG Immunological Genome Project Consortium; RA Malhotra N., Narayan K., Cho O.H., Sylvia K.E., Yin C., Melichar H., RA Rashighi M., Lefebvre V., Harris J.E., Berg L.J., Kang J.; RT "A network of high-mobility group box transcription factors programs innate RT interleukin-17 production."; RL Immunity 38:681-693(2013). RN [12] RP DEVELOPMENTAL STAGE. RX PubMed=27713059; DOI=10.1016/j.ydbio.2016.10.001; RA Jia S., Kwon H.E., Lan Y., Zhou J., Liu H., Jiang R.; RT "Bmp4-Msx1 signaling and Osr2 control tooth organogenesis through RT antagonistic regulation of secreted Wnt antagonists."; RL Dev. Biol. 420:110-119(2016). RN [13] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=29148101; DOI=10.1111/eos.12390; RA Feng X.Y., Wu X.S., Wang J.S., Zhang C.M., Wang S.L.; RT "Homeobox protein MSX-1 inhibits expression of bone morphogenetic protein RT 2, bone morphogenetic protein 4, and lymphoid enhancer-binding factor 1 via RT Wnt/beta-catenin signaling to prevent differentiation of dental mesenchymal RT cells during the late bell stage."; RL Eur. J. Oral Sci. 126:1-12(2018). RN [14] RP STRUCTURE BY NMR OF 296-380. RX PubMed=7651541; DOI=10.1038/376791a0; RA Love J.J., Li X., Case D.A., Glese K., Grosschedl P., Wright P.E.; RT "Structural basis for DNA bending by the architectural transcription factor RT LEF-1."; RL Nature 376:791-795(1995). RN [15] RP STRUCTURE BY NMR OF 296-380. RA Li X., Love J.J., Case D.A., Wright P.E.; RT "High resolution NMR structure of the LEF-1 HMG domain complexed with its RT cognate DNA."; RL Submitted (OCT-1998) to the PDB data bank. CC -!- FUNCTION: Transcription factor that binds DNA in a sequence-specific CC manner (By similarity). Participates in the Wnt signaling pathway CC (PubMed:11445543). Activates transcription of target genes in the CC presence of CTNNB1 and EP300 (PubMed:12446687). PIASG antagonizes both CC Wnt-dependent and Wnt-independent activation by LEF1 (PubMed:11731474). CC TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by LEF1 and CC CTNNB1 (By similarity). Regulates T-cell receptor alpha enhancer CC function (By similarity). Required for IL17A expressing gamma-delta T- CC cell maturation and development, via binding to regulator loci of BLK CC to modulate expression (PubMed:23562159). Acts as a positive regulator CC of odontoblast differentiation during mesenchymal tooth germ formation, CC expression is repressed during the bell stage by MSX1-mediated CC inhibition of CTNNB1 signaling (PubMed:29148101). May play a role in CC hair cell differentiation and follicle morphogenesis (PubMed:11445543). CC {ECO:0000250|UniProtKB:Q9UJU2, ECO:0000269|PubMed:11445543, CC ECO:0000269|PubMed:11731474, ECO:0000269|PubMed:12446687, CC ECO:0000269|PubMed:23562159, ECO:0000269|PubMed:29148101}. CC -!- SUBUNIT: Binds the armadillo repeat of CTNNB1 and forms a stable CC complex. Binds TLE1, ALYREF/THOC4, MDFI and MDFIC (By similarity). CC Interacts with NLK (By similarity). Interacts with EP300 and PIASG. CC Interacts with DAZAP2 (PubMed:19304756). {ECO:0000250|UniProtKB:Q9UJU2, CC ECO:0000269|PubMed:10966653, ECO:0000269|PubMed:11731474, CC ECO:0000269|PubMed:12446687, ECO:0000269|PubMed:19304756}. CC -!- INTERACTION: CC P27782; Q02248: Ctnnb1; NbExp=6; IntAct=EBI-984464, EBI-397872; CC P27782; P30681: Hmgb2; NbExp=2; IntAct=EBI-984464, EBI-6910056; CC P27782; P35222: CTNNB1; Xeno; NbExp=2; IntAct=EBI-984464, EBI-491549; CC P27782; O75564: JRK; Xeno; NbExp=3; IntAct=EBI-984464, EBI-8607681; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10498690}. Note=Found CC in nuclear bodies upon PIASG binding. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P27782-1; Sequence=Displayed; CC Name=2; Synonyms=LEF-1S; CC IsoId=P27782-2; Sequence=VSP_006983; CC -!- TISSUE SPECIFICITY: Expressed in Vgamma1.1 and Vgamma2 gamma-delta T- CC cells, however not expressed in gamma-delta thymocytes fated for Il17a CC expression (at protein level) (PubMed:17218525, PubMed:23562159). CC Expressed in alpha-beta T-cell lineages (PubMed:17218525). Expressed in CC the thymus (PubMed:1827423). Found in distinct epithelial cell CC compartments of the skin and is abundant in the hair-producing CC progenitors of the follicle (PubMed:10498690). CC {ECO:0000269|PubMed:10498690, ECO:0000269|PubMed:17218525, CC ECO:0000269|PubMed:1827423, ECO:0000269|PubMed:23562159}. CC -!- DEVELOPMENTAL STAGE: Expressed in the lower molar mesenchyme at 13.5 CC dpc and 14.5 dpc (PubMed:8898217). Expressed in the distal tooth bud CC epithelium and condensing tooth mesenchyme surrounding the tooth bud CC during the bud stage of mandibular molar tooth development at 13.5 dpc CC (PubMed:27713059). Expressed in bell stage dental mesenchymal cells at CC 17.5 dpc (at protein level) (PubMed:29148101). Detected throughout the CC basal layer, in ectodermal placodes and the underlying dermal CC condensates in embryonic skin, and in epithelium and mesenchyme from CC early hair germs at 16.5 dpc (at protein level) (PubMed:10498690). At CC birth expression decreases in the basal level of the epidermis and CC increases in hair bulbs, in particular in matrix and precortex CC (PubMed:10498690). At day 6-9 expression is concentrated in follicle CC bulbs and in the hair shaft in a concentric ring of hair-keratin- CC expressing cells derived from the precortex (PubMed:10498690). Detected CC in dermal papilla throughout the hair cycle, and in a subset of cells CC emanating from the bulge to form the secondary hair germ CC (PubMed:10498690). {ECO:0000269|PubMed:10498690, CC ECO:0000269|PubMed:27713059, ECO:0000269|PubMed:29148101, CC ECO:0000269|PubMed:8898217}. CC -!- DOMAIN: Proline-rich and acidic regions are implicated in the CC activation functions of RNA polymerase II transcription factors. CC -!- PTM: Phosphorylated at Thr-153 and/or Ser-164 by NLK (By similarity). CC Phosphorylation by NLK at these sites represses LEF1-mediated CC transcriptional activation of target genes of the canonical Wnt CC signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q9UJU2}. CC -!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X58636; CAA41493.1; -; mRNA. DR EMBL; D16503; BAA03954.1; -; mRNA. DR CCDS; CCDS17842.1; -. [P27782-1] DR PIR; A39565; A39565. DR RefSeq; NP_034833.2; NM_010703.4. [P27782-1] DR PDB; 2LEF; NMR; -; A=296-380. DR PDB; 3OUW; X-ray; 2.91 A; B=1-63. DR PDB; 3OUX; X-ray; 2.40 A; B=1-63. DR PDBsum; 2LEF; -. DR PDBsum; 3OUW; -. DR PDBsum; 3OUX; -. DR AlphaFoldDB; P27782; -. DR BMRB; P27782; -. DR SMR; P27782; -. DR BioGRID; 201137; 17. DR ComplexPortal; CPX-318; beta1-catenin - LEF1 complex. DR CORUM; P27782; -. DR DIP; DIP-35132N; -. DR ELM; P27782; -. DR IntAct; P27782; 9. DR MINT; P27782; -. DR STRING; 10090.ENSMUSP00000029611; -. DR iPTMnet; P27782; -. DR PhosphoSitePlus; P27782; -. DR EPD; P27782; -. DR MaxQB; P27782; -. DR PaxDb; 10090-ENSMUSP00000029611; -. DR PeptideAtlas; P27782; -. DR ProteomicsDB; 290018; -. [P27782-1] DR ProteomicsDB; 290019; -. [P27782-2] DR Antibodypedia; 912; 931 antibodies from 45 providers. DR DNASU; 16842; -. DR Ensembl; ENSMUST00000029611.14; ENSMUSP00000029611.8; ENSMUSG00000027985.15. [P27782-1] DR GeneID; 16842; -. DR KEGG; mmu:16842; -. DR UCSC; uc008rjf.2; mouse. [P27782-1] DR AGR; MGI:96770; -. DR CTD; 51176; -. DR MGI; MGI:96770; Lef1. DR VEuPathDB; HostDB:ENSMUSG00000027985; -. DR eggNOG; KOG3248; Eukaryota. DR GeneTree; ENSGT00940000159660; -. DR InParanoid; P27782; -. DR OMA; NFSTCKA; -. DR OrthoDB; 5351131at2759; -. DR PhylomeDB; P27782; -. DR TreeFam; TF318448; -. DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex. DR Reactome; R-MMU-4086398; Ca2+ pathway. DR Reactome; R-MMU-4641265; Repression of WNT target genes. DR Reactome; R-MMU-8853884; Transcriptional Regulation by VENTX. DR Reactome; R-MMU-8951430; RUNX3 regulates WNT signaling. DR BioGRID-ORCS; 16842; 3 hits in 83 CRISPR screens. DR ChiTaRS; Lef1; mouse. DR EvolutionaryTrace; P27782; -. DR PRO; PR:P27782; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; P27782; Protein. DR Bgee; ENSMUSG00000027985; Expressed in embryonic post-anal tail and 246 other cell types or tissues. DR ExpressionAtlas; P27782; baseline and differential. DR GO; GO:1990907; C:beta-catenin-TCF complex; IDA:ParkinsonsUK-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:CAFA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0070016; F:armadillo repeat domain binding; ISO:MGI. DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI. DR GO; GO:0070742; F:C2H2 zinc finger domain binding; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0008301; F:DNA binding, bending; IDA:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IGI:MGI. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IMP:MGI. DR GO; GO:0045295; F:gamma-catenin binding; ISO:MGI. DR GO; GO:0042393; F:histone binding; ISO:MGI. DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI. DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI. DR GO; GO:0003676; F:nucleic acid binding; EXP:DisProt. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI. DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI. DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:MGI. DR GO; GO:0046632; P:alpha-beta T cell differentiation; IGI:MGI. DR GO; GO:0060033; P:anatomical structure regression; IMP:MGI. DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IMP:MGI. DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; IMP:MGI. DR GO; GO:0042100; P:B cell proliferation; IMP:MGI. DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI. DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:ComplexPortal. DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI. DR GO; GO:0048468; P:cell development; IGI:MGI. DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI. DR GO; GO:0071353; P:cellular response to interleukin-4; ISO:MGI. DR GO; GO:0060710; P:chorio-allantoic fusion; IGI:MGI. DR GO; GO:0021542; P:dentate gyrus development; IMP:MGI. DR GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI. DR GO; GO:1904019; P:epithelial cell apoptotic process; IMP:MGI. DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:BHF-UCL. DR GO; GO:0060325; P:face morphogenesis; IGI:MGI. DR GO; GO:0021873; P:forebrain neuroblast division; IGI:MGI. DR GO; GO:0021861; P:forebrain radial glial cell differentiation; IGI:MGI. DR GO; GO:0021943; P:formation of radial glial scaffolds; IGI:MGI. DR GO; GO:0021766; P:hippocampus development; IMP:MGI. DR GO; GO:0030879; P:mammary gland development; IMP:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0071866; P:negative regulation of apoptotic process in bone marrow cell; ISO:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0032696; P:negative regulation of interleukin-13 production; ISO:MGI. DR GO; GO:0032713; P:negative regulation of interleukin-4 production; ISO:MGI. DR GO; GO:0032714; P:negative regulation of interleukin-5 production; ISO:MGI. DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; IDA:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0030223; P:neutrophil differentiation; ISO:MGI. DR GO; GO:0071895; P:odontoblast differentiation; ISO:MGI. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0048341; P:paraxial mesoderm formation; IGI:MGI. DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI. DR GO; GO:0090068; P:positive regulation of cell cycle process; ISO:MGI. DR GO; GO:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI. DR GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; ISO:MGI. DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IMP:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI. DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:0030854; P:positive regulation of granulocyte differentiation; ISO:MGI. DR GO; GO:1901331; P:positive regulation of odontoblast differentiation; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:MGI. DR GO; GO:0071168; P:protein localization to chromatin; ISO:MGI. DR GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0050767; P:regulation of neurogenesis; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IGI:MGI. DR GO; GO:0062009; P:secondary palate development; IMP:BHF-UCL. DR GO; GO:0050909; P:sensory perception of taste; IMP:MGI. DR GO; GO:0001756; P:somitogenesis; IMP:MGI. DR GO; GO:0002040; P:sprouting angiogenesis; IMP:MGI. DR GO; GO:0033153; P:T cell receptor V(D)J recombination; IGI:MGI. DR GO; GO:0045063; P:T-helper 1 cell differentiation; IDA:UniProtKB. DR GO; GO:0043586; P:tongue development; IMP:MGI. DR GO; GO:0061153; P:trachea gland development; IMP:MGI. DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI. DR GO; GO:0001944; P:vasculature development; IMP:MGI. DR CDD; cd21996; HMG-box_TCF7-like; 1. DR DisProt; DP00767; -. DR Gene3D; 1.10.30.10; High mobility group box domain; 1. DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1. DR IDEAL; IID50006; -. DR InterPro; IPR027397; Catenin-bd_sf. DR InterPro; IPR013558; CTNNB1-bd_N. DR InterPro; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. DR InterPro; IPR024940; TCF/LEF. DR PANTHER; PTHR10373:SF11; LYMPHOID ENHANCER-BINDING FACTOR 1; 1. DR PANTHER; PTHR10373; TRANSCRIPTION FACTOR 7 FAMILY MEMBER; 1. DR Pfam; PF08347; CTNNB1_binding; 1. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR SUPFAM; SSF47095; HMG-box; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. DR Genevisible; P27782; MM. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; DNA-binding; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation; Ubl conjugation; KW Wnt signaling pathway. FT CHAIN 1..397 FT /note="Lymphoid enhancer-binding factor 1" FT /id="PRO_0000048596" FT DNA_BIND 297..365 FT /note="HMG box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT REGION 1..60 FT /note="CTNNB1-binding" FT REGION 59..102 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 164..191 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 266..296 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 367..397 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 79..97 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 269..296 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 130 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UJU2" FT MOD_RES 153 FT /note="Phosphothreonine; by NLK" FT /evidence="ECO:0000250|UniProtKB:Q9UJU2" FT MOD_RES 164 FT /note="Phosphoserine; by NLK" FT /evidence="ECO:0000250|UniProtKB:Q9UJU2" FT CROSSLNK 25 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT CROSSLNK 267 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT VAR_SEQ 1..113 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8415007" FT /id="VSP_006983" FT MUTAGEN 19 FT /note="D->A: Strongly diminishes CTNNB1 binding and FT transactivation. Prevents nuclear translocation of CTNNB1." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 20 FT /note="E->A: Prevents nuclear translocation of CTNNB1." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 24 FT /note="F->A: Strongly diminishes CTNNB1 binding and FT transactivation. Prevents nuclear translocation of CTNNB1." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 26 FT /note="D->A: Prevents nuclear translocation of CTNNB1." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 27 FT /note="E->A: Prevents nuclear translocation of CTNNB1." FT /evidence="ECO:0000269|PubMed:10966653" FT TURN 13..16 FT /evidence="ECO:0007829|PDB:3OUX" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:3OUX" FT HELIX 48..58 FT /evidence="ECO:0007829|PDB:3OUX" FT HELIX 303..318 FT /evidence="ECO:0007829|PDB:2LEF" FT HELIX 324..335 FT /evidence="ECO:0007829|PDB:2LEF" FT HELIX 340..360 FT /evidence="ECO:0007829|PDB:2LEF" FT TURN 370..372 FT /evidence="ECO:0007829|PDB:2LEF" SQ SEQUENCE 397 AA; 44059 MW; 0CA01B6C528FD7FA CRC64; MPQLSGGGGG GDPELCATDE MIPFKDEGDP QKEKIFAEIS HPEEEGDLAD IKSSLVNESE IIPASNGHEV VRQAPSSQEP YHDKAREHPD EGKHPDGGLY NKGPSYSSYS GYIMMPNMNS DPYMSNGSLS PPIPRTSNKV PVVQPSHAVH PLTPLITYSD EHFSPGSHPS HIPSDVNSKQ GMSRHPPAPE IPTFYPLSPG GVGQITPPIG WQGQPVYPIT GGFRQPYPSS LSGDTSMSRF SHHMIPGPPG PHTTGIPHPA IVTPQVKQEH PHTDSDLMHV KPQHEQRKEQ EPKRPHIKKP LNAFMLYMKE MRANVVAECT LKESAAINQI LGRRWHALSR EEQAKYYELA RKERQLHMQL YPGWSARDNY GKKKKRKREK LQESTSGTGP RMTAAYI //