ID LEF1_HUMAN Reviewed; 399 AA. AC Q9UJU2; B4DG38; B7Z8E2; E9PDK3; Q3ZCU4; Q9HAZ0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 05-FEB-2025, entry version 217. DE RecName: Full=Lymphoid enhancer-binding factor 1 {ECO:0000312|HGNC:HGNC:6551}; DE Short=LEF-1 {ECO:0000303|PubMed:10756202}; DE AltName: Full=T cell-specific transcription factor 1-alpha; DE Short=TCF1-alpha {ECO:0000312|HGNC:HGNC:6551}; GN Name=LEF1 {ECO:0000312|HGNC:HGNC:6551}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND RP FUNCTION. RX PubMed=2010090; DOI=10.1101/gad.5.4.656; RA Waterman M.L., Fischer W.H., Jones K.A.; RT "A thymus-specific member of the HMG protein family regulates the human T RT cell receptor C alpha enhancer."; RL Genes Dev. 5:656-669(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RX PubMed=10756202; DOI=10.1093/nar/28.9.1994; RA Hovanes K., Li T.W., Waterman M.L.; RT "The human LEF-1 gene contains a promoter preferentially active in RT lymphocytes and encodes multiple isoforms derived from alternative RT splicing."; RL Nucleic Acids Res. 28:1994-2003(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), ALTERNATIVE SPLICING, RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=19653274; DOI=10.1002/ijc.24802; RA Jesse S., Koenig A., Ellenrieder V., Menke A.; RT "Lef-1 isoforms regulate different target genes and reduce cellular RT adhesion."; RL Int. J. Cancer 126:1109-1120(2010). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). RA Kobielak A., Kobielak K., Trzeciak W.H.; RT "New transcript isoform of the human LEF-1 devoid of HMG domain, derived RT from alternative splicing of exon 8."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7). RC TISSUE=Amygdala, and Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6). RC TISSUE=Skin, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP INTERACTION WITH ALYREF/THOC4. RX PubMed=9119228; DOI=10.1101/gad.11.5.640; RA Bruhn L., Munnerlyn A., Grosschedl R.; RT "ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for RT TCRalpha enhancer function."; RL Genes Dev. 11:640-653(1997). RN [10] RP INTERACTION WITH CTNNB1. RX PubMed=9488439; DOI=10.1128/mcb.18.3.1248; RA Korinek V., Barker N., Willert K., Molenaar M., Roose J., Wagenaar G., RA Markman M., Lamers W., Destree O., Clevers H.; RT "Two members of the Tcf family implicated in Wnt/b-catenin signaling during RT embryogenesis in the mouse."; RL Mol. Cell. Biol. 18:1248-1256(1998). RN [11] RP INTERACTION WITH TLE1, AND INHIBITION OF TRANSCRIPTIONAL ACTIVATION BY RP TLE1. RX PubMed=9751710; DOI=10.1073/pnas.95.20.11590; RA Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D., RA Stifani S., Paroush Z., Groner Y.; RT "Transcriptional repression by AML1 and LEF-1 is mediated by the RT TLE/Groucho corepressors."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998). RN [12] RP IDENTIFICATION (ISOFORM 3), FUNCTION, AND EXPRESSION IN COLON CANCER. RX PubMed=11326276; DOI=10.1038/ng0501-53; RA Hovanes K., Li T.W.H., Munguia J.E., Truong T., Milovanovic T., RA Lawrence Marsh J., Holcombe R.F., Waterman M.L.; RT "Beta-catenin-sensitive isoforms of lymphoid enhancer factor-1 are RT selectively expressed in colon cancer."; RL Nat. Genet. 28:53-57(2001). RN [13] RP FUNCTIONAL INTERACTION WITH TLE1; TLE2; TLE3 AND TLE4. RX PubMed=11266540; DOI=10.1093/nar/29.7.1410; RA Brantjes H., Roose J., van De Wetering M., Clevers H.; RT "All Tcf HMG box transcription factors interact with Groucho-related co- RT repressors."; RL Nucleic Acids Res. 29:1410-1419(2001). RN [14] RP INTERACTION WITH MDFI AND MDFIC. RX PubMed=12192039; DOI=10.1128/mcb.22.18.6393-6405.2002; RA Kusano S., Raab-Traub N.; RT "I-mfa domain proteins interact with Axin and affect its regulation of the RT Wnt and c-Jun N-terminal kinase signaling pathways."; RL Mol. Cell. Biol. 22:6393-6405(2002). RN [15] RP INTERACTION WITH NLK, PHOSPHORYLATION AT THR-155 AND/OR SER-166 BY NLK, AND RP MUTAGENESIS OF THR-155 AND SER-166. RX PubMed=12556497; DOI=10.1128/mcb.23.4.1379-1389.2003; RA Ishitani T., Ninomiya-Tsuji J., Matsumoto K.; RT "Regulation of lymphoid enhancer factor 1/T-cell factor by mitogen- RT activated protein kinase-related Nemo-like kinase-dependent phosphorylation RT in Wnt/beta-catenin signaling."; RL Mol. Cell. Biol. 23:1379-1389(2003). RN [16] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [19] RP VARIANT [LARGE SCALE ANALYSIS] ARG-113. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Transcription factor that binds DNA in a sequence-specific CC manner (PubMed:2010090). Participates in the Wnt signaling pathway (By CC similarity). Activates transcription of target genes in the presence of CC CTNNB1 and EP300 (By similarity). PIAG antagonizes both Wnt-dependent CC and Wnt-independent activation by LEF1 (By similarity). TLE1, TLE2, CC TLE3 and TLE4 repress transactivation mediated by LEF1 and CTNNB1 CC (PubMed:11266540). Regulates T-cell receptor alpha enhancer function CC (PubMed:19653274). Required for IL17A expressing gamma-delta T-cell CC maturation and development, via binding to regulator loci of BLK to CC modulate expression (By similarity). Acts as a positive regulator of CC odontoblast differentiation during mesenchymal tooth germ formation, CC expression is repressed during the bell stage by MSX1-mediated CC inhibition of CTNNB1 signaling (By similarity). May play a role in hair CC cell differentiation and follicle morphogenesis (By similarity). CC {ECO:0000250|UniProtKB:P27782, ECO:0000269|PubMed:11266540, CC ECO:0000269|PubMed:19653274, ECO:0000269|PubMed:2010090}. CC -!- FUNCTION: [Isoform 1]: Transcriptionally activates MYC and CCND1 CC expression and enhances proliferation of pancreatic tumor cells. CC {ECO:0000269|PubMed:19653274}. CC -!- FUNCTION: [Isoform 3]: Lacks the CTNNB1 interaction domain and may CC therefore be an antagonist for Wnt signaling. CC {ECO:0000269|PubMed:11326276}. CC -!- FUNCTION: [Isoform 5]: Transcriptionally activates the fibronectin CC promoter, binds to and represses transcription from the E-cadherin CC promoter in a CTNNB1-independent manner, and is involved in reducing CC cellular aggregation and increasing cell migration of pancreatic cancer CC cells. {ECO:0000269|PubMed:19653274}. CC -!- SUBUNIT: Binds the armadillo repeat of CTNNB1 and forms a stable CC complex. Interacts with EP300, TLE1 and PIASG (By similarity). Binds CC ALYREF/THOC4, MDFI and MDFIC. Interacts with NLK. Interacts with DAZAP2 CC (PubMed:19304756). {ECO:0000250|UniProtKB:P27782, CC ECO:0000269|PubMed:12192039, ECO:0000269|PubMed:12556497, CC ECO:0000269|PubMed:19304756, ECO:0000269|PubMed:9119228, CC ECO:0000269|PubMed:9488439, ECO:0000269|PubMed:9751710}. CC -!- INTERACTION: CC Q9UJU2; P35222: CTNNB1; NbExp=10; IntAct=EBI-926131, EBI-491549; CC Q9UJU2; P49789: FHIT; NbExp=2; IntAct=EBI-926131, EBI-741760; CC Q9UJU2; P08069: IGF1R; NbExp=5; IntAct=EBI-926131, EBI-475981; CC Q9UJU2; Q16236: NFE2L2; NbExp=3; IntAct=EBI-926131, EBI-2007911; CC Q9UJU2; Q96LA8: PRMT6; NbExp=3; IntAct=EBI-926131, EBI-912440; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. CC Note=Found in nuclear bodies upon PIASG binding. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=7; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=A; CC IsoId=Q9UJU2-1; Sequence=Displayed; CC Name=2; Synonyms=B, 8A; CC IsoId=Q9UJU2-2; Sequence=VSP_002188; CC Name=3; Synonyms=LEF-1-DN; CC IsoId=Q9UJU2-3; Sequence=VSP_007022; CC Name=4; CC IsoId=Q9UJU2-4; Sequence=VSP_007022, VSP_002188; CC Name=5; CC IsoId=Q9UJU2-5; Sequence=VSP_040068; CC Name=6; CC IsoId=Q9UJU2-6; Sequence=VSP_040068, VSP_040069; CC Name=7; CC IsoId=Q9UJU2-7; Sequence=VSP_044877, VSP_040068; CC -!- TISSUE SPECIFICITY: Detected in thymus. Not detected in normal colon, CC but highly expressed in colon cancer biopsies and colon cancer cell CC lines. Expressed in several pancreatic tumors and weakly expressed in CC normal pancreatic tissue. Isoforms 1 and 5 are detected in several CC pancreatic cell lines. {ECO:0000269|PubMed:19653274}. 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-155 and/or Ser-166 by NLK. Phosphorylation CC by NLK at these sites represses LEF1-mediated transcriptional CC activation of target genes of the canonical Wnt signaling pathway. CC {ECO:0000269|PubMed:12556497}. CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform CC 1. May be produced at very low levels due to a premature stop codon in CC the mRNA, leading to nonsense-mediated mRNA decay. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage. CC Acts as a dominant negative mutant. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform CC 3. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. 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; AF288571; AAG01022.1; -; mRNA. DR EMBL; AF198532; AAF13268.1; -; mRNA. DR EMBL; AF294627; AAG26886.1; -; mRNA. DR EMBL; AK294395; BAG57649.1; -; mRNA. DR EMBL; AK303272; BAH13928.1; -; mRNA. DR EMBL; AC092539; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC097067; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC118062; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC123576; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471057; EAX06223.1; -; Genomic_DNA. DR EMBL; CH471057; EAX06225.1; -; Genomic_DNA. DR EMBL; BC040559; AAH40559.1; -; mRNA. DR EMBL; BC050632; AAH50632.1; -; mRNA. DR CCDS; CCDS3679.1; -. [Q9UJU2-1] DR CCDS; CCDS47122.1; -. [Q9UJU2-6] DR CCDS; CCDS47123.1; -. [Q9UJU2-5] DR CCDS; CCDS54791.1; -. [Q9UJU2-7] DR PIR; A39625; A39625. DR RefSeq; NP_001124185.1; NM_001130713.2. [Q9UJU2-5] DR RefSeq; NP_001124186.1; NM_001130714.2. [Q9UJU2-6] DR RefSeq; NP_001159591.1; NM_001166119.1. [Q9UJU2-7] DR RefSeq; NP_057353.1; NM_016269.4. [Q9UJU2-1] DR AlphaFoldDB; Q9UJU2; -. DR BMRB; Q9UJU2; -. DR SMR; Q9UJU2; -. DR BioGRID; 119354; 58. DR ComplexPortal; CPX-316; beta1-catenin - LEF1 complex. DR CORUM; Q9UJU2; -. DR DIP; DIP-29946N; -. DR IntAct; Q9UJU2; 27. DR MINT; Q9UJU2; -. DR STRING; 9606.ENSP00000265165; -. DR ChEMBL; CHEMBL3217392; -. DR DrugBank; DB00903; Etacrynic acid. DR GlyConnect; 2055; 1 N-Linked glycan (1 site). DR GlyCosmos; Q9UJU2; 1 site, 2 glycans. DR GlyGen; Q9UJU2; 1 site, 2 N-linked glycans (1 site). DR iPTMnet; Q9UJU2; -. DR PhosphoSitePlus; Q9UJU2; -. DR BioMuta; LEF1; -. DR DMDM; 8928194; -. DR jPOST; Q9UJU2; -. DR MassIVE; Q9UJU2; -. DR PaxDb; 9606-ENSP00000265165; -. DR PeptideAtlas; Q9UJU2; -. DR ProteomicsDB; 19686; -. DR ProteomicsDB; 84650; -. [Q9UJU2-1] DR ProteomicsDB; 84651; -. [Q9UJU2-2] DR ProteomicsDB; 84652; -. [Q9UJU2-3] DR ProteomicsDB; 84653; -. [Q9UJU2-4] DR ProteomicsDB; 84654; -. [Q9UJU2-5] DR ProteomicsDB; 84655; -. [Q9UJU2-6] DR Pumba; Q9UJU2; -. DR TopDownProteomics; Q9UJU2-2; -. [Q9UJU2-2] DR Antibodypedia; 912; 1017 antibodies from 46 providers. DR DNASU; 51176; -. DR Ensembl; ENST00000265165.6; ENSP00000265165.1; ENSG00000138795.10. [Q9UJU2-1] DR Ensembl; ENST00000379951.6; ENSP00000369284.2; ENSG00000138795.10. [Q9UJU2-6] DR Ensembl; ENST00000438313.6; ENSP00000406176.2; ENSG00000138795.10. [Q9UJU2-5] DR Ensembl; ENST00000506680.5; ENSP00000422334.1; ENSG00000138795.10. [Q9UJU2-2] DR Ensembl; ENST00000510624.5; ENSP00000422840.1; ENSG00000138795.10. [Q9UJU2-7] DR GeneID; 51176; -. DR KEGG; hsa:51176; -. DR MANE-Select; ENST00000265165.6; ENSP00000265165.1; NM_016269.5; NP_057353.1. DR UCSC; uc003hyt.3; human. [Q9UJU2-1] DR AGR; HGNC:6551; -. DR CTD; 51176; -. DR DisGeNET; 51176; -. DR GeneCards; LEF1; -. DR HGNC; HGNC:6551; LEF1. DR HPA; ENSG00000138795; Tissue enriched (lymphoid). DR MalaCards; LEF1; -. DR MIM; 153245; gene. DR neXtProt; NX_Q9UJU2; -. DR OpenTargets; ENSG00000138795; -. DR PharmGKB; PA30331; -. DR VEuPathDB; HostDB:ENSG00000138795; -. DR eggNOG; KOG3248; Eukaryota. DR GeneTree; ENSGT00940000159660; -. DR HOGENOM; CLU_013229_5_0_1; -. DR InParanoid; Q9UJU2; -. DR OMA; NFSTCKA; -. DR OrthoDB; 2307332at2759; -. DR PhylomeDB; Q9UJU2; -. DR TreeFam; TF318448; -. DR PathwayCommons; Q9UJU2; -. DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex. DR Reactome; R-HSA-4086398; Ca2+ pathway. DR Reactome; R-HSA-4411364; Binding of TCF/LEF:CTNNB1 to target gene promoters. DR Reactome; R-HSA-4641265; Repression of WNT target genes. DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX. DR Reactome; R-HSA-8951430; RUNX3 regulates WNT signaling. DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis. DR Reactome; R-HSA-9733709; Cardiogenesis. DR Reactome; R-HSA-9754189; Germ layer formation at gastrulation. DR Reactome; R-HSA-9793380; Formation of paraxial mesoderm. DR Reactome; R-HSA-9796292; Formation of axial mesoderm. DR Reactome; R-HSA-9824272; Somitogenesis. DR Reactome; R-HSA-9824585; Regulation of MITF-M-dependent genes involved in pigmentation. DR Reactome; R-HSA-9825892; Regulation of MITF-M-dependent genes involved in cell cycle and proliferation. DR Reactome; R-HSA-9856649; Transcriptional and post-translational regulation of MITF-M expression and activity. DR SignaLink; Q9UJU2; -. DR SIGNOR; Q9UJU2; -. DR BioGRID-ORCS; 51176; 13 hits in 1180 CRISPR screens. DR ChiTaRS; LEF1; human. DR GeneWiki; Lymphoid_enhancer-binding_factor_1; -. DR GenomeRNAi; 51176; -. DR Pharos; Q9UJU2; Tchem. DR PRO; PR:Q9UJU2; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q9UJU2; protein. DR Bgee; ENSG00000138795; Expressed in thymus and 180 other cell types or tissues. DR ExpressionAtlas; Q9UJU2; baseline and differential. DR GO; GO:1990907; C:beta-catenin-TCF complex; IPI:ParkinsonsUK-UCL. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032993; C:protein-DNA complex; IDA:BHF-UCL. DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL. DR GO; GO:0070016; F:armadillo repeat domain binding; IPI:BHF-UCL. DR GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL. DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0008301; F:DNA binding, bending; ISS:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:BHF-UCL. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:GO_Central. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl. DR GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL. DR GO; GO:0042826; F:histone deacetylase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0030331; F:nuclear estrogen receptor binding; IDA:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB. DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:GO_Central. DR GO; GO:0060033; P:anatomical structure regression; IEA:Ensembl. DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IEA:Ensembl. DR GO; GO:0042100; P:B cell proliferation; IEA:Ensembl. DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl. DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL. DR GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB. DR GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:BHF-UCL. DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:UniProtKB. DR GO; GO:0060710; P:chorio-allantoic fusion; IEA:Ensembl. DR GO; GO:0021542; P:dentate gyrus development; IEA:Ensembl. DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl. DR GO; GO:1904019; P:epithelial cell apoptotic process; IEA:Ensembl. DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:BHF-UCL. DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl. DR GO; GO:0021873; P:forebrain neuroblast division; IEA:Ensembl. DR GO; GO:0021861; P:forebrain radial glial cell differentiation; IEA:Ensembl. DR GO; GO:0021943; P:formation of radial glial scaffolds; IEA:Ensembl. DR GO; GO:0030879; P:mammary gland development; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0071866; P:negative regulation of apoptotic process in bone marrow cell; IMP:UniProtKB. DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0032696; P:negative regulation of interleukin-13 production; IDA:UniProtKB. DR GO; GO:0032713; P:negative regulation of interleukin-4 production; IDA:UniProtKB. DR GO; GO:0032714; P:negative regulation of interleukin-5 production; IDA:UniProtKB. DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0030223; P:neutrophil differentiation; IMP:UniProtKB. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; IEP:UniProtKB. DR GO; GO:0048341; P:paraxial mesoderm formation; IEA:Ensembl. DR GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB. DR GO; GO:0090068; P:positive regulation of cell cycle process; IDA:UniProtKB. DR GO; GO:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB. DR GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; IMP:UniProtKB. DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB. DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase. DR GO; GO:0030854; P:positive regulation of granulocyte differentiation; IDA:UniProtKB. DR GO; GO:1901331; P:positive regulation of odontoblast differentiation; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0071168; P:protein localization to chromatin; IMP:UniProtKB. DR GO; GO:0050767; P:regulation of neurogenesis; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0062009; P:secondary palate development; ISS:BHF-UCL. DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl. DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl. DR GO; GO:0002040; P:sprouting angiogenesis; IEA:Ensembl. DR GO; GO:0033153; P:T cell receptor V(D)J recombination; IEA:Ensembl. DR GO; GO:0045063; P:T-helper 1 cell differentiation; ISS:UniProtKB. DR GO; GO:0043586; P:tongue development; IEA:Ensembl. DR GO; GO:0061153; P:trachea gland development; IEA:Ensembl. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl. DR CDD; cd21996; HMG-box_TCF7-like; 1. DR FunFam; 4.10.900.10:FF:000004; lymphoid enhancer-binding factor 1 isoform X2; 1. DR FunFam; 1.10.30.10:FF:000001; transcription factor 7 isoform X2; 1. 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 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. PE 1: Evidence at protein level; KW Activator; Alternative promoter usage; Alternative splicing; KW Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; KW Transcription; Transcription regulation; Ubl conjugation; KW Wnt signaling pathway. FT CHAIN 1..399 FT /note="Lymphoid enhancer-binding factor 1" FT /id="PRO_0000048595" FT DNA_BIND 299..367 FT /note="HMG box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT REGION 1..104 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1..62 FT /note="CTNNB1-binding" FT /evidence="ECO:0000250" FT REGION 166..192 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 268..298 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 369..399 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 24..45 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 82..98 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 132 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 155 FT /note="Phosphothreonine; by NLK" FT /evidence="ECO:0000305|PubMed:12556497" FT MOD_RES 166 FT /note="Phosphoserine; by NLK" FT /evidence="ECO:0000305|PubMed:12556497" FT CROSSLNK 27 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250" FT CROSSLNK 269 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250" FT VAR_SEQ 1..115 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_007022" FT VAR_SEQ 1..70 FT /note="MPQLSGGGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLAD FT IKSSLVNESEIIPASNGH -> MA (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044877" FT VAR_SEQ 214..241 FT /note="Missing (in isoform 5, isoform 6 and isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:19653274" FT /id="VSP_040068" FT VAR_SEQ 283..399 FT /note="KPQHEQRKEQEPKRPHIKKPLNAFMLYMKEMRANVVAECTLKESAAINQILG FT RRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKREKLQESASGTGPR FT MTAAYI -> CSAFLLPHPFLIPSTPSPNHHHHHLLGSLSMNRERSRSQKDLTLRSL FT (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_002188" FT VAR_SEQ 390..399 FT /note="TGPRMTAAYI -> GKRSSFPTCKAKAATPGPLLEMEAC (in isoform FT 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040069" FT VARIANT 113 FT /note="G -> R (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs369649181)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035935" FT MUTAGEN 155 FT /note="T->A: Reduced phosphorylation by NLK; when FT associated with A-166." FT /evidence="ECO:0000269|PubMed:12556497" FT MUTAGEN 166 FT /note="S->A: Reduced phosphorylation by NLK; when FT associated with A-155." FT /evidence="ECO:0000269|PubMed:12556497" FT CONFLICT 146 FT /note="Q -> R (in Ref. 5; BAH13928)" FT /evidence="ECO:0000305" SQ SEQUENCE 399 AA; 44201 MW; D480D440698EEFE3 CRC64; MPQLSGGGGG GGGDPELCAT DEMIPFKDEG DPQKEKIFAE ISHPEEEGDL ADIKSSLVNE SEIIPASNGH EVARQAQTSQ EPYHDKAREH PDDGKHPDGG LYNKGPSYSS YSGYIMMPNM NNDPYMSNGS LSPPIPRTSN KVPVVQPSHA VHPLTPLITY SDEHFSPGSH PSHIPSDVNS KQGMSRHPPA PDIPTFYPLS PGGVGQITPP LGWQGQPVYP ITGGFRQPYP SSLSVDTSMS RFSHHMIPGP PGPHTTGIPH PAIVTPQVKQ EHPHTDSDLM HVKPQHEQRK EQEPKRPHIK KPLNAFMLYM KEMRANVVAE CTLKESAAIN QILGRRWHAL SREEQAKYYE LARKERQLHM QLYPGWSARD NYGKKKKRKR EKLQESASGT GPRMTAAYI //