LEF1_MOUSE
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 03-AUG-2022, entry version 207.
DE RecName: Full=Lymphoid enhancer-binding factor 1;
DE Short=LEF-1;
GN Name=Lef1; Synonyms=Lef-1;
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 TISSUE SPECIFICITY.
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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). May play a role in hair cell
CC 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}.
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 {ECO:0000250, ECO:0000269|PubMed:10966653, ECO:0000269|PubMed:11731474,
CC ECO:0000269|PubMed:12446687}.
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. Note=Found in nuclear bodies upon PIASG
CC 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: Detected throughout the basal layer, in ectodermal
CC placodes and the underlying dermal condensates in embryonic skin, and
CC in epithelium and mesenchyme from early hair germs. At birth expression
CC decreases in the basal level of the epidermis and increases in hair
CC bulbs, in particular in matrix and precortex. At day 6-9 expression is
CC concentrated in follicle bulbs and in the hair shaft in a concentric
CC ring of hair-keratin-expressing cells derived from the precortex.
CC Detected in dermal papilla throughout the hair cycle, and in a subset
CC of cells emanating from the bulge to form the secondary hair germ.
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. Phosphorylation
CC by NLK at these sites represses LEF1-mediated transcriptional
CC activation of target genes of the canonical Wnt signaling pathway (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
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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; P27782; -.
DR PeptideAtlas; P27782; -.
DR PRIDE; P27782; -.
DR ProteomicsDB; 290018; -. [P27782-1]
DR ProteomicsDB; 290019; -. [P27782-2]
DR Antibodypedia; 912; 810 antibodies from 45 providers.
DR DNASU; 16842; -.
DR Ensembl; ENSMUST00000029611; ENSMUSP00000029611; ENSMUSG00000027985. [P27782-1]
DR GeneID; 16842; -.
DR KEGG; mmu:16842; -.
DR UCSC; uc008rjf.2; mouse. [P27782-1]
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; 807716at2759; -.
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 78 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 243 other tissues.
DR ExpressionAtlas; P27782; baseline and differential.
DR Genevisible; P27782; MM.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
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: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:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IMP:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; ISO: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:0022408; P:negative regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISO: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:0045892; P:negative regulation of transcription, DNA-templated; 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; IC:ComplexPortal.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; ISO:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IMP: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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:MGI.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:MGI.
DR GO; GO:0050767; P:regulation of neurogenesis; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
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 DisProt; DP00767; -.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 4.10.900.10; -; 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; IPR028769; LEF1.
DR InterPro; IPR024940; TCF/LEF.
DR PANTHER; PTHR10373; PTHR10373; 1.
DR PANTHER; PTHR10373:SF11; PTHR10373:SF11; 1.
DR Pfam; PF08347; CTNNB1_binding; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
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
