ID CTNB1_HUMAN Reviewed; 781 AA. AC P35222; A8K1L7; Q8NEW9; Q8NI94; Q9H391; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 27-MAR-2024, entry version 264. DE RecName: Full=Catenin beta-1 {ECO:0000312|HGNC:HGNC:2514}; DE AltName: Full=Beta-catenin {ECO:0000303|PubMed:7806582}; GN Name=CTNNB1 {ECO:0000312|HGNC:HGNC:2514}; Synonyms=CTNNB; GN ORFNames=OK/SW-cl.35, PRO2286; 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]. RC TISSUE=Placenta; RX PubMed=7806582; DOI=10.1083/jcb.127.6.2061; RA Huelsken J., Birchmeier W., Behrens J.; RT "E-cadherin and APC compete for the interaction with beta-catenin and the RT cytoskeleton."; RL J. Cell Biol. 127:2061-2069(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W., RA Gao F., Liu M., He F.; RT "Functional prediction of the coding sequences of 75 new genes deduced by RT analysis of cDNA clones from human fetal liver."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-688. RG NIEHS SNPs program; RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Hippocampus; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-312. RX PubMed=12019147; RA Kim J.-S., Crooks H., Dracheva T., Nishanian T.G., Singh B., Jen J., RA Waldman T.; RT "Oncogenic beta-catenin is required for bone morphogenetic protein 4 RT expression in human cancer cells."; RL Cancer Res. 62:2744-2748(2002). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 258-781. RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor-reactive RT CTL generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [10] RP IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX. RX PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9; RA Butz S., Kemler R.; RT "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell RT adhesion."; RL FEBS Lett. 355:195-200(1994). RN [11] RP CHROMOSOMAL TRANSLOCATION WITH PLAG1. RX PubMed=9020842; DOI=10.1038/ng0297-170; RA Kas K., Voz M.L., Roeijer E., Astroem A.-K., Meyen E., Stenman G., RA Van de Ven W.J.M.; RT "Promoter swapping between the genes for a novel zinc finger protein and RT beta-catenin in pleiomorphic adenomas with t(3;8)(p21;q12) RT translocations."; RL Nat. Genet. 15:170-174(1997). RN [12] RP CHROMOSOMAL TRANSLOCATION WITH PLAG1. RX PubMed=10029085; RA Astroem A.-K., Voz M.L., Kas K., Roeijer E., Wedell B., Mandahl N., RA Van de Ven W., Mark J., Stenman G.; RT "Conserved mechanism of PLAG1 activation in salivary gland tumors with and RT without chromosome 8q12 abnormalities: identification of SII as a new RT fusion partner gene."; RL Cancer Res. 59:918-923(1999). RN [13] RP STIMULATION OF TYROSINE PHOSPHORYLATION BY EGF, AND DEPHOSPHORYLATION BY RP PTPRF. RX PubMed=10187801; DOI=10.1074/jbc.274.15.10173; RA Mueller T., Choidas A., Reichmann E., Ullrich A.; RT "Phosphorylation and free pool of beta-catenin are regulated by tyrosine RT kinases and tyrosine phosphatases during epithelial cell migration."; RL J. Biol. Chem. 274:10173-10183(1999). RN [14] RP SUBCELLULAR LOCATION. RX PubMed=10725230; DOI=10.1242/jcs.113.8.1481; RA Mariner D.J., Wang J., Reynolds A.B.; RT "ARVCF localizes to the nucleus and adherens junction and is mutually RT exclusive with p120(ctn) in E-cadherin complexes."; RL J. Cell Sci. 113:1481-1490(2000). RN [15] RP INTERACTION WITH LEF1; APC; AXIN1; AXIN2 AND TCF7L2, PHOSPHORYLATION BY RP GSK3B, AND MUTAGENESIS OF PHE-253; HIS-260; LYS-292; LYS-345; TRP-383; RP ARG-386; ASN-426; LYS-435; ARG-469; HIS-470 AND LYS-508. 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 [16] RP TISSUE SPECIFICITY, AND VARIANT PTR TYR-32. RX PubMed=11703283; DOI=10.1046/j.1365-2133.2001.04455.x; RA Moreno-Bueno G., Gamallo C., Perez-Gallego L., Contreras F., Palacios J.; RT "Beta-catenin expression in pilomatrixomas. Relationship with beta-catenin RT gene mutations and comparison with beta-catenin expression in normal hair RT follicles."; RL Br. J. Dermatol. 145:576-581(2001). RN [17] RP INTERACTION WITH LEF1, AND INHIBITION BY CTNNBIP1 BINDING. RX PubMed=11751639; DOI=10.1101/gad.946501; RA Tutter A.V., Fryer C.J., Jones K.A.; RT "Chromatin-specific regulation of LEF-1-beta-catenin transcription RT activation and inhibition in vitro."; RL Genes Dev. 15:3342-3354(2001). RN [18] RP RETRACTED PAPER. RX PubMed=11279024; DOI=10.1074/jbc.m100194200; RA Piedra J., Martinez D., Castano J., Miravet S., Dunach M., RA de Herreros A.G.; RT "Regulation of beta-catenin structure and activity by tyrosine RT phosphorylation."; RL J. Biol. Chem. 276:20436-20443(2001). RN [19] RP INTERACTION WITH SPN/CD43 CYTOPLASMIC TAIL. RX PubMed=15003504; DOI=10.1016/j.bbrc.2004.02.011; RA Andersson C.X., Fernandez-Rodriguez J., Laos S., Sikut R., Sikut A., RA Baeckstroem D., Hansson G.C.; RT "CD43 has a functional NLS, interacts with beta-catenin, and affects gene RT expression."; RL Biochem. Biophys. Res. Commun. 316:12-17(2004). RN [20] RP RETRACTION NOTICE OF PUBMED:11279024. RX PubMed=27226643; DOI=10.1074/jbc.a116.100194; RA Piedra J., Martinez D., Castano J., Miravet S., Dunach M., RA de Herreros A.G.; RL J. Biol. Chem. 291:11463-11463(2016). RN [21] RP INTERACTION WITH CTNNA3. RX PubMed=11590244; DOI=10.1242/jcs.114.17.3177; RA Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J., Colpaert C., RA Bruyneel E., Mareel M., van Roy F.; RT "AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein RT mediating strong cell-cell adhesion."; RL J. Cell Sci. 114:3177-3188(2001). RN [22] RP INTERACTION WITH SIAH1, AND UBIQUITINATION. RX PubMed=11389839; DOI=10.1016/s1097-2765(01)00242-8; RA Matsuzawa S., Reed J.C.; RT "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin RT degradation linked to p53 responses."; RL Mol. Cell 7:915-926(2001). RN [23] RP INTERACTION WITH SIAH1, AND UBIQUITINATION. RX PubMed=11389840; DOI=10.1016/s1097-2765(01)00241-6; RA Liu J., Stevens J., Rote C.A., Yost H.J., Hu Y., Neufeld K.L., White R.L., RA Matsunami N.; RT "Siah-1 mediates a novel beta-catenin degradation pathway linking p53 to RT the adenomatous polyposis coli protein."; RL Mol. Cell 7:927-936(2001). RN [24] RP INVOLVEMENT IN MESOM. RX PubMed=11464291; DOI=10.1038/sj.onc.1204557; RA Shigemitsu K., Sekido Y., Usami N., Mori S., Sato M., Horio Y., RA Hasegawa Y., Bader S.A., Gazdar A.F., Minna J.D., Hida T., Yoshioka H., RA Imaizumi M., Ueda Y., Takahashi M., Shimokata K.; RT "Genetic alteration of the beta-catenin gene (CTNNB1) in human lung cancer RT and malignant mesothelioma and identification of a new 3p21.3 homozygous RT deletion."; RL Oncogene 20:4249-4257(2001). RN [25] RP INTERACTION WITH PTPRU. RX PubMed=12501215; DOI=10.1021/bi026095u; RA Yan H.-X., He Y.-Q., Dong H., Zhang P., Zeng J.-Z., Cao H.-F., Wu M.-C., RA Wang H.-Y.; RT "Physical and functional interaction between receptor-like protein tyrosine RT phosphatase PCP-2 and beta-catenin."; RL Biochemistry 41:15854-15860(2002). RN [26] RP PHOSPHORYLATION AT SER-45, CHARACTERIZATION OF VARIANT HEPATOCELLULAR RP CARCINOMA ALA-41, CHARACTERIZATION OF VARIANT DESMOID TUMOR ALA-41, AND RP CHARACTERIZATION OF VARIANT HEPATOBLASTOMA ALA-41. RX PubMed=12051714; DOI=10.1016/s0006-291x(02)00485-0; RA Hagen T., Vidal-Puig A.; RT "Characterisation of the phosphorylation of beta-catenin at the GSK-3 RT priming site Ser45."; RL Biochem. Biophys. Res. Commun. 294:324-328(2002). RN [27] RP INTERACTION WITH CXADR. RX PubMed=12297051; DOI=10.1016/s0092-8674(02)00912-1; RA Walters R.W., Freimuth P., Moninger T.O., Ganske I., Zabner J., Welsh M.J.; RT "Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing RT virus escape."; RL Cell 110:789-799(2002). RN [28] RP PHOSPHORYLATION AT SER-23 AND SER-29 BY GSK3B, PHOSPHORYLATION AT THR-41, RP MUTAGENESIS OF SER-29, CHARACTERIZATION OF VARIANTS HEPATOCELLULAR RP CARCINOMA ARG-23; ALA-37 AND ALA-41, CHARACTERIZATION OF VARIANT PTR RP TYR-33, CHARACTERIZATION OF VARIANT MDB ALA-37, CHARACTERIZATION OF VARIANT RP DESMOID TUMOR ALA-41, AND CHARACTERIZATION OF VARIANT HEPATOBLASTOMA RP ALA-41. RX PubMed=12027456; DOI=10.1006/excr.2002.5520; RA van Noort M., van de Wetering M., Clevers H.; RT "Identification of two novel regulated serines in the N-terminus of beta- RT catenin."; RL Exp. Cell Res. 276:264-272(2002). RN [29] RP INTERACTION WITH CDH1 AND PKP2, AND SUBCELLULAR LOCATION. RX PubMed=11790773; DOI=10.1074/jbc.m108765200; RA Chen X., Bonne S., Hatzfeld M., van Roy F., Green K.J.; RT "Protein binding and functional characterization of plakophilin 2. Evidence RT for its diverse roles in desmosomes and beta -catenin signaling."; RL J. Biol. Chem. 277:10512-10522(2002). RN [30] RP WNT SIGNALING MODULATES PHOSPHORYLATION. RX PubMed=11834740; DOI=10.1074/jbc.m111635200; RA van Noort M., Meeldijk J., van der Zee R., Destree O., Clevers H.; RT "Wnt signaling controls the phosphorylation status of beta-catenin."; RL J. Biol. Chem. 277:17901-17905(2002). RN [31] RP PHOSPHORYLATION, AND INTERACTION OF PHOSPHORYLATED CTNNB1 WITH BTRC. RX PubMed=12077367; DOI=10.1242/jcs.115.13.2771; RA Sadot E., Conacci-Sorrell M., Zhurinsky J., Shnizer D., Lando Z., RA Zharhary D., Kam Z., Ben-Ze'ev A., Geiger B.; RT "Regulation of S33/S37 phosphorylated beta-catenin in normal and RT transformed cells."; RL J. Cell Sci. 115:2771-2780(2002). RN [32] RP INTERACTION WITH PTPRJ. RX PubMed=12370829; DOI=10.1038/sj.onc.1205858; RA Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.; RT "The transmembrane receptor protein tyrosine phosphatase DEP1 interacts RT with p120(ctn)."; RL Oncogene 21:7067-7076(2002). RN [33] RP INTERACTION WITH PCDH11Y. RX PubMed=12420223; DOI=10.1038/sj.onc.1205991; RA Chen M.-W., Vacherot F., De La Taille A., Gil-Diez-De-Medina S., Shen R., RA Friedman R.A., Burchardt M., Chopin D.K., Buttyan R.; RT "The emergence of protocadherin-PC expression during the acquisition of RT apoptosis-resistance by prostate cancer cells."; RL Oncogene 21:7861-7871(2002). RN [34] RP INTERACTION WITH NHERF1. RX PubMed=12830000; DOI=10.1053/jhep.2003.50270; RA Shibata T., Chuma M., Kokubu A., Sakamoto M., Hirohashi S.; RT "EBP50, a beta-catenin-associating protein, enhances Wnt signaling and is RT over-expressed in hepatocellular carcinoma."; RL Hepatology 38:178-186(2003). RN [35] RP REVIEW. RX PubMed=10679188; DOI=10.1006/bbrc.1999.1860; RA Kikuchi A.; RT "Regulation of beta-catenin signaling in the Wnt pathway."; RL Biochem. Biophys. Res. Commun. 268:243-248(2000). RN [36] RP PHOSPHORYLATION AT TYR-142 BY FYN. RX PubMed=12640114; DOI=10.1128/mcb.23.7.2287-2297.2003; RA Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N., RA Garcia de Herreros A., Dunach M.; RT "p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin RT Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction."; RL Mol. Cell. Biol. 23:2287-2297(2003). RN [37] RP INTERACTION WITH CBY1. RX PubMed=12712206; DOI=10.1038/nature01570; RA Takemaru K., Yamaguchi S., Lee Y.S., Zhang Y., Carthew R.W., Moon R.T.; RT "Chibby, a nuclear beta-catenin-associated antagonist of the Wnt/Wingless RT pathway."; RL Nature 422:905-909(2003). RN [38] RP INTERACTION WITH AJAP1. RC TISSUE=Brain; RX PubMed=14595118; DOI=10.1091/mbc.e03-05-0281; RA Bharti S., Handrow-Metzmacher H., Zickenheiner S., Zeitvogel A., RA Baumann R., Starzinski-Powitz A.; RT "Novel membrane protein shrew-1 targets to cadherin-mediated junctions in RT polarized epithelial cells."; RL Mol. Biol. Cell 15:397-406(2004). RN [39] RP INTERACTION WITH CBY1, AND SUBCELLULAR LOCATION. RX PubMed=16424001; DOI=10.1158/0008-5472.can-05-3124; RA Jung Y., Bang S., Choi K., Kim E., Kim Y., Kim J., Park J., Koo H., RA Moon R.T., Song K., Lee I.; RT "TC1 (C8orf4) enhances the Wnt/beta-catenin pathway by relieving RT antagonistic activity of Chibby."; RL Cancer Res. 66:723-728(2006). RN [40] RP SUBCELLULAR LOCATION, AND INTERACTION WITH NANOS1. RX PubMed=17047063; DOI=10.1158/0008-5472.can-05-3096; RA Strumane K., Bonnomet A., Stove C., Vandenbroucke R., Nawrocki-Raby B., RA Bruyneel E., Mareel M., Birembaut P., Berx G., van Roy F.; RT "E-cadherin regulates human Nanos1, which interacts with p120ctn and RT induces tumor cell migration and invasion."; RL Cancer Res. 66:10007-10015(2006). RN [41] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [42] RP SUBCELLULAR LOCATION, AND INTERACTION WITH EMD. RX PubMed=16858403; DOI=10.1038/sj.emboj.7601230; RA Markiewicz E., Tilgner K., Barker N., van de Wetering M., Clevers H., RA Dorobek M., Hausmanowa-Petrusewicz I., Ramaekers F.C.S., Broers J.L.V., RA Blankesteijn W.M., Salpingidou G., Wilson R.G., Ellis J.A., Hutchison C.J.; RT "The inner nuclear membrane protein emerin regulates beta-catenin activity RT by restricting its accumulation in the nucleus."; RL EMBO J. 25:3275-3285(2006). RN [43] RP INTERACTION WITH MUC1, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=17524503; DOI=10.1016/j.bbamcr.2007.04.009; RA Lillehoj E.P., Lu W., Kiser T., Goldblum S.E., Kim K.C.; RT "MUC1 inhibits cell proliferation by a beta-catenin-dependent mechanism."; RL Biochim. Biophys. Acta 1773:1028-1038(2007). RN [44] RP INTERACTION WITH GLIS2, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=17289029; DOI=10.1016/j.febslet.2007.01.058; RA Kim Y.-S., Kang H.S., Jetten A.M.; RT "The Kruppel-like zinc finger protein Glis2 functions as a negative RT modulator of the Wnt/beta-catenin signaling pathway."; RL FEBS Lett. 581:858-864(2007). RN [45] RP PHOSPHORYLATION AT SER-191 AND SER-246, INTERACTION WITH CDK5, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=17009320; DOI=10.1002/jcb.21041; RA Munoz J.P., Huichalaf C.H., Orellana D., Maccioni R.B.; RT "cdk5 modulates beta- and delta-catenin/Pin1 interactions in neuronal RT cells."; RL J. Cell. Biochem. 100:738-749(2007). RN [46] RP INTERACTION WITH FHIT, IDENTIFICATION IN A COMPLEX WITH LEF1, AND FUNCTION. RX PubMed=18077326; DOI=10.1073/pnas.0703664105; RA Weiske J., Albring K.F., Huber O.; RT "The tumor suppressor Fhit acts as a repressor of beta-catenin RT transcriptional activity."; RL Proc. Natl. Acad. Sci. U.S.A. 104:20344-20349(2007). RN [47] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH NEK2. RX PubMed=18086858; DOI=10.1101/gad.1596308; RA Bahmanyar S., Kaplan D.D., Deluca J.G., Giddings T.H. Jr., O'Toole E.T., RA Winey M., Salmon E.D., Casey P.J., Nelson W.J., Barth A.I.; RT "beta-Catenin is a Nek2 substrate involved in centrosome separation."; RL Genes Dev. 22:91-105(2008). RN [48] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-556 AND SER-675, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [49] RP INTERACTION WITH SOX7. RX PubMed=18819930; DOI=10.1158/1541-7786.mcr-07-2175; RA Guo L., Zhong D., Lau S., Liu X., Dong X.Y., Sun X., Yang V.W., RA Vertino P.M., Moreno C.S., Varma V., Dong J.T., Zhou W.; RT "Sox7 Is an independent checkpoint for beta-catenin function in prostate RT and colon epithelial cells."; RL Mol. Cancer Res. 6:1421-1430(2008). RN [50] RP INTERACTION WITH CHD8. RX PubMed=18378692; DOI=10.1128/mcb.00322-08; RA Thompson B.A., Tremblay V., Lin G., Bochar D.A.; RT "CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta- RT catenin target genes."; RL Mol. Cell. Biol. 28:3894-3904(2008). RN [51] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [52] RP INTERACTION WITH TCF7L2 AND TNIK. RX PubMed=19816403; DOI=10.1038/emboj.2009.285; RA Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., RA Heck A.J., Clevers H.; RT "The kinase TNIK is an essential activator of Wnt target genes."; RL EMBO J. 28:3329-3340(2009). RN [53] RP FUNCTION. RX PubMed=18957423; DOI=10.1074/jbc.m805612200; RA Li H., Ray G., Yoo B.H., Erdogan M., Rosen K.V.; RT "Down-regulation of death-associated protein kinase-2 is required for beta- RT catenin-induced anoikis resistance of malignant epithelial cells."; RL J. Biol. Chem. 284:2012-2022(2009). RN [54] RP INTERACTION WITH RUVBL2; APPL2; APPL1; HDAC1 AND HDAC2. RX PubMed=19433865; DOI=10.1074/jbc.m109.007237; RA Rashid S., Pilecka I., Torun A., Olchowik M., Bielinska B., Miaczynska M.; RT "Endosomal adaptor proteins APPL1 and APPL2 are novel activators of beta- RT catenin/TCF-mediated transcription."; RL J. Biol. Chem. 284:18115-18128(2009). RN [55] RP IDENTIFICATION BY 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 [56] RP PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2, AND UBIQUITINATION. RX PubMed=20307497; DOI=10.1016/j.bbrc.2010.03.099; RA Kim E.-A., Kim J.E., Sung K.S., Choi D.W., Lee B.J., Choi C.Y.; RT "Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-catenin for RT phosphorylation and proteasomal degradation."; RL Biochem. Biophys. Res. Commun. 394:966-971(2010). RN [57] RP INTERACTION WITH SESTD1. RX PubMed=20164195; DOI=10.1074/jbc.m109.068304; RA Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C.; RT "The phospholipid-binding protein SESTD1 is a novel regulator of the RT transient receptor potential channels TRPC4 and TRPC5."; RL J. Biol. Chem. 285:12426-12434(2010). RN [58] RP INTERACTION WITH TRPC4. RX PubMed=19996314; DOI=10.1074/jbc.m109.060301; RA Graziani A., Poteser M., Heupel W.M., Schleifer H., Krenn M., RA Drenckhahn D., Romanin C., Baumgartner W., Groschner K.; RT "Cell-cell contact formation governs Ca2+ signaling by TRPC4 in the RT vascular endothelium: evidence for a regulatory TRPC4-beta-catenin RT interaction."; RL J. Biol. Chem. 285:4213-4223(2010). RN [59] RP INTERACTION WITH CDK5. RX PubMed=19693690; DOI=10.1007/s11033-009-9752-7; RA Li Q., Liu X., Zhang M., Ye G., Qiao Q., Ling Y., Wu Y., Zhang Y., Yu L.; RT "Characterization of a novel human CDK5 splicing variant that inhibits RT Wnt/beta-catenin signaling."; RL Mol. Biol. Rep. 37:2415-2421(2010). RN [60] RP PHOSPHORYLATION AT TYR-64; TYR-142; TYR-331 AND TYR-333, INTERACTION WITH RP PTK6, AND MUTAGENESIS OF TYR-64. RX PubMed=20026641; DOI=10.1242/jcs.053264; RA Palka-Hamblin H.L., Gierut J.J., Bie W., Brauer P.M., Zheng Y., Asara J.M., RA Tyner A.L.; RT "Identification of beta-catenin as a target of the intracellular tyrosine RT kinase PTK6."; RL J. Cell Sci. 123:236-245(2010). RN [61] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [62] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [63] RP FUNCTION IN INSULIN INTERNALIZATION, SUBCELLULAR LOCATION, INTERACTION WITH RP CDK2, AND PHOSPHORYLATION BY CDK2. RX PubMed=21262353; DOI=10.1016/j.cellsig.2011.01.019; RA Fiset A., Xu E., Bergeron S., Marette A., Pelletier G., Siminovitch K.A., RA Olivier M., Beauchemin N., Faure R.L.; RT "Compartmentalized CDK2 is connected with SHP-1 and beta-catenin and RT regulates insulin internalization."; RL Cell. Signal. 23:911-919(2011). RN [64] RP INTERACTION WITH PKT7. RX PubMed=21132015; DOI=10.1038/embor.2010.185; RA Puppo F., Thome V., Lhoumeau A.-C., Cibois M., Gangar A., Lembo F., RA Belotti E., Marchetto S., Lecine P., Prebet T., Sebbagh M., Shin W.-S., RA Lee S.-T., Kodjabachian L., Borg J.-P.; RT "Protein tyrosine kinase 7 has a conserved role in Wnt/beta-catenin RT canonical signalling."; RL EMBO Rep. 12:43-49(2011). RN [65] RP INTERACTION WITH NDRG2. RX PubMed=21247902; DOI=10.1074/jbc.m110.170803; RA Hwang J., Kim Y., Kang H.B., Jaroszewski L., Deacon A.M., Lee H., RA Choi W.C., Kim K.J., Kim C.H., Kang B.S., Lee J.O., Oh T.K., Kim J.W., RA Wilson I.A., Kim M.H.; RT "Crystal structure of the human N-Myc downstream-regulated gene 2 protein RT provides insight into its role as a tumor suppressor."; RL J. Biol. Chem. 286:12450-12460(2011). RN [66] RP INTERACTION WITH PKM ISOFORM M2, PHOSPHORYLATION AT TYR-333, AND RP MUTAGENESIS OF TYR-333. RX PubMed=22056988; DOI=10.1038/nature10598; RA Yang W., Xia Y., Ji H., Zheng Y., Liang J., Huang W., Gao X., Aldape K., RA Lu Z.; RT "Nuclear PKM2 regulates beta-catenin transactivation upon EGFR RT activation."; RL Nature 480:118-122(2011). RN [67] RP INTERACTION WITH AHI1. RX PubMed=21623382; DOI=10.1038/nm.2380; RA Lancaster M.A., Gopal D.J., Kim J., Saleem S.N., Silhavy J.L., Louie C.M., RA Thacker B.E., Williams Y., Zaki M.S., Gleeson J.G.; RT "Defective Wnt-dependent cerebellar midline fusion in a mouse model of RT Joubert syndrome."; RL Nat. Med. 17:726-731(2011). RN [68] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-552, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [69] RP IDENTIFICATION IN A COMPLEX WITH HINT1 AND MITF, AND FUNCTION. RX PubMed=22647378; DOI=10.4161/cc.20765; RA Genovese G., Ghosh P., Li H., Rettino A., Sioletic S., Cittadini A., RA Sgambato A.; RT "The tumor suppressor HINT1 regulates MITF and beta-catenin transcriptional RT activity in melanoma cells."; RL Cell Cycle 11:2206-2215(2012). RN [70] RP FUNCTION, INTERACTION WITH FERMT2, IDENTIFICATION IN A COMPLEX WITH FERMT2 RP AND TCF7L2, AND SUBCELLULAR LOCATION. RX PubMed=22699938; DOI=10.1038/embor.2012.88; RA Yu Y., Wu J., Wang Y., Zhao T., Ma B., Liu Y., Fang W., Zhu W.G., Zhang H.; RT "Kindlin 2 forms a transcriptional complex with beta-catenin and TCF4 to RT enhance Wnt signalling."; RL EMBO Rep. 13:750-758(2012). RN [71] RP FUNCTION, AND INTERACTION WITH PML. RX PubMed=22155184; DOI=10.1053/j.gastro.2011.11.041; RA Satow R., Shitashige M., Jigami T., Fukami K., Honda K., Kitabayashi I., RA Yamada T.; RT "Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor RT function in colorectal cancer cells."; RL Gastroenterology 142:572-581(2012). RN [72] RP INVOLVEMENT IN NEDSDV. RX PubMed=23033978; DOI=10.1056/nejmoa1206524; RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., RA Veltman J.A., Vissers L.E.; RT "Diagnostic exome sequencing in persons with severe intellectual RT disability."; RL N. Engl. J. Med. 367:1921-1929(2012). RN [73] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [74] RP SUBCELLULAR LOCATION, AND INTERACTION WITH FAM53B. RX PubMed=25183871; DOI=10.1242/dev.108415; RA Kizil C., Kuechler B., Yan J.J., Oezhan G., Moro E., Argenton F., Brand M., RA Weidinger G., Antos C.L.; RT "Simplet/Fam53b is required for Wnt signal transduction by regulating beta- RT catenin nuclear localization."; RL Development 141:3529-3539(2014). RN [75] RP GLYCOSYLATION AT SER-23, AND SUBCELLULAR LOCATION. RX PubMed=24342833; DOI=10.1016/j.yexcr.2013.11.021; RA Ha J.R., Hao L., Venkateswaran G., Huang Y.H., Garcia E., Persad S.; RT "beta-catenin is O-GlcNAc glycosylated at Serine 23: implications for beta- RT catenin's subcellular localization and transactivator function."; RL Exp. Cell Res. 321:153-166(2014). RN [76] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-552, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [77] RP INTERACTION WITH RNF220. RX PubMed=25266658; DOI=10.1128/mcb.00731-14; RA Ma P., Yang X., Kong Q., Li C., Yang S., Li Y., Mao B.; RT "The ubiquitin ligase RNF220 enhances canonical Wnt signaling through USP7- RT mediated deubiquitination of beta-catenin."; RL Mol. Cell. Biol. 34:4355-4366(2014). RN [78] RP ACETYLATION AT LYS-49, AND DEACETYLATION. RX PubMed=24824780; DOI=10.1002/ijc.28967; RA Pangon L., Mladenova D., Watkins L., Van Kralingen C., Currey N., RA Al-Sohaily S., Lecine P., Borg J.P., Kohonen-Corish M.R.; RT "MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in RT the cytoplasm."; RL Int. J. Cancer 136:55-64(2015). RN [79] RP INTERACTION WITH JPT1, AND PHOSPHORYLATION AT SER-33. RX PubMed=25169422; DOI=10.1002/jcb.24956; RA Varisli L., Ozturk B.E., Akyuz G.K., Korkmaz K.S.; RT "HN1 negatively influences the beta-catenin/E-cadherin interaction, and RT contributes to migration in prostate cells."; RL J. Cell. Biochem. 116:170-178(2015). RN [80] RP INTERACTION WITH CTNND2. RX PubMed=25807484; DOI=10.1038/nature14186; RA Turner T.N., Sharma K., Oh E.C., Liu Y.P., Collins R.L., Sosa M.X., RA Auer D.R., Brand H., Sanders S.J., Moreno-De-Luca D., Pihur V., Plona T., RA Pike K., Soppet D.R., Smith M.W., Cheung S.W., Martin C.L., State M.W., RA Talkowski M.E., Cook E., Huganir R., Katsanis N., Chakravarti A.; RT "Loss of delta-catenin function in severe autism."; RL Nature 520:51-56(2015). RN [81] RP INTERACTION WITH GID8; AXIN1 AND TCF7L2, AND SUBCELLULAR LOCATION. RX PubMed=28829046; DOI=10.1038/cr.2017.107; RA Lu Y., Xie S., Zhang W., Zhang C., Gao C., Sun Q., Cai Y., Xu Z., Xiao M., RA Xu Y., Huang X., Wu X., Liu W., Wang F., Kang Y., Zhou T.; RT "Twa1/Gid8 is a beta-catenin nuclear retention factor in Wnt signaling and RT colorectal tumorigenesis."; RL Cell Res. 27:1422-1440(2017). RN [82] RP IDENTIFICATION IN A CADHERIN/CATENIN ADHESION COMPLEX. RX PubMed=28051089; DOI=10.1038/mi.2016.120; RA Caldwell J.M., Collins M.H., Kemme K.A., Sherrill J.D., Wen T., Rochman M., RA Stucke E.M., Amin L., Tai H., Putnam P.E., Jimenez-Dalmaroni M.J., RA Wormald M.R., Porollo A., Abonia J.P., Rothenberg M.E.; RT "Cadherin 26 is an alpha integrin-binding epithelial receptor regulated RT during allergic inflammation."; RL Mucosal Immunol. 10:1190-1201(2017). RN [83] RP INTERACTION WITH TCF7L2/TCF4 AND HERPES VIRUS 8 PROTEIN VPK (MICROBIAL RP INFECTION). RX PubMed=29432739; DOI=10.1016/j.bbrc.2018.02.089; RA Cha S., Kang M.S., Seo T.; RT "KSHV vPK inhibits Wnt signaling via preventing interactions between beta- RT catenin and TCF4."; RL Biochem. Biophys. Res. Commun. 497:381-387(2018). RN [84] RP SUBCELLULAR LOCATION, INTERACTION WITH TMEM170B, AND TISSUE SPECIFICITY. RX PubMed=29367600; DOI=10.1038/s41419-017-0128-y; RA Li M., Han Y., Zhou H., Li X., Lin C., Zhang E., Chi X., Hu J., Xu H.; RT "Transmembrane protein 170B is a novel breast tumorigenesis suppressor gene RT that inhibits the Wnt/beta-catenin pathway."; RL Cell Death Dis. 9:91-91(2018). RN [85] RP INVOLVEMENT IN EVR7, AND VARIANT EVR7 CYS-710. RX PubMed=28575650; DOI=10.1016/j.ajhg.2017.05.001; RA Panagiotou E.S., Sanjurjo Soriano C., Poulter J.A., Lord E.C., Dzulova D., RA Kondo H., Hiyoshi A., Chung B.H., Chu Y.W., Lai C.H.Y., Tafoya M.E., RA Karjosukarso D., Collin R.W.J., Topping J., Downey L.M., Ali M., RA Inglehearn C.F., Toomes C.; RT "Defects in the cell signaling mediator beta-catenin cause the retinal RT vascular condition FEVR."; RL Am. J. Hum. Genet. 100:960-968(2017). RN [86] RP INTERACTION WITH IRF2BPL, AND VARIANT TYR-33. RX PubMed=29374064; DOI=10.1158/0008-5472.can-17-2403; RA Higashimori A., Dong Y., Zhang Y., Kang W., Nakatsu G., Ng S.S.M., RA Arakawa T., Sung J.J.Y., Chan F.K.L., Yu J.; RT "Forkhead Box F2 Suppresses Gastric Cancer through a Novel FOXF2-IRF2BPL- RT beta-Catenin Signaling Axis."; RL Cancer Res. 78:1643-1656(2018). RN [87] RP INTERACTION WITH SOX30 AND TCF7L2, AND SUBCELLULAR LOCATION. RX PubMed=29739711; DOI=10.1016/j.ebiom.2018.04.026; RA Han F., Liu W.B., Shi X.Y., Yang J.T., Zhang X., Li Z.M., Jiang X., Yin L., RA Li J.J., Huang C.S., Cao J., Liu J.Y.; RT "SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling via RT Transcriptional and Posttranslational Regulation of beta-Catenin in Lung RT Cancer."; RL EBioMedicine 31:253-266(2018). RN [88] RP INTERACTION WITH FLYWCH1. RX PubMed=30097457; DOI=10.1158/1541-7786.mcr-18-0262; RA Muhammad B.A., Almozyan S., Babaei-Jadidi R., Onyido E.K., Saadeddin A., RA Kashfi S.H., Spencer-Dene B., Ilyas M., Lourdusamy A., Behrens A., RA Nateri A.S.; RT "FLYWCH1, a Novel Suppressor of Nuclear beta-Catenin, Regulates Migration RT and Morphology in Colorectal Cancer."; RL Mol. Cancer Res. 16:1977-1990(2018). RN [89] RP INTERACTION WITH LMBR1L. RX PubMed=31073040; DOI=10.1126/science.aau0812; RA Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J., RA Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M., RA Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y., RA Beutler B.; RT "LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling."; RL Science 364:0-0(2019). RN [90] RP PHOSPHORYLATION AT THR-556 (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION. RX PubMed=31801859; DOI=10.1128/jvi.01847-19; RA You H., Lin Y., Lin F., Yang M., Li J., Zhang R., Huang Z., Shen Q., RA Tang R., Zheng C.; RT "beta-Catenin Is Required for the cGAS/STING Signaling Pathway but RT Antagonized by the Herpes Simplex Virus 1 US3 Protein."; RL J. Virol. 94:0-0(2020). RN [91] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 133-664. RX PubMed=11136974; DOI=10.1016/s0092-8674(00)00192-6; RA Graham T.A., Weaver C., Mao F., Kimelman D., Xu W.; RT "Crystal structure of a beta-catenin/Tcf complex."; RL Cell 103:885-896(2000). RN [92] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-664 IN COMPLEX WITH TCF7L2, RP AND MUTAGENESIS OF LYS-312 AND LYS-435. RX PubMed=11713475; DOI=10.1038/nsb718; RA Graham T.A., Ferkey D.M., Mao F., Kimelman D., Xu W.; RT "Tcf4 can specifically recognize beta-catenin using alternative RT conformations."; RL Nat. Struct. Biol. 8:1048-1052(2001). RN [93] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-668 IN COMPLEX WITH TCF7L2. RX PubMed=11713476; DOI=10.1038/nsb720; RA Poy F., Lepourcelet M., Shivdasani R.A., Eck M.J.; RT "Structure of a human Tcf4-beta-catenin complex."; RL Nat. Struct. Biol. 8:1053-1057(2001). RN [94] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-664 IN COMPLEX WITH CTNNBIP1, RP AND MUTAGENESIS OF PHE-660 AND ARG-661. RX PubMed=12408824; DOI=10.1016/s1097-2765(02)00637-8; RA Graham T.A., Clements W.K., Kimelman D., Xu W.; RT "The crystal structure of the beta-catenin/ICAT complex reveals the RT inhibitory mechanism of ICAT."; RL Mol. Cell 10:563-571(2002). RN [95] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-136 IN COMPLEX WITH BCL9 AND RP TCF7L2, INTERACTION WITH BCL9; BCL9L CDH3 AND TCF7L2, AND MUTAGENESIS OF RP TYR-142; LEU-156; LEU-159 AND LEU-178. RX PubMed=17052462; DOI=10.1016/j.molcel.2006.09.001; RA Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.; RT "Crystal structure of a beta-catenin/BCL9/Tcf4 complex."; RL Mol. Cell 24:293-300(2006). RN [96] RP VARIANTS COLORECTAL CANCER TYR-33 AND SER-45 DEL. RX PubMed=9065402; DOI=10.1126/science.275.5307.1787; RA Morin P.J., Sparks A.B., Korinek V., Barker N., Clevers H., Vogelstein B., RA Kinzler K.W.; RT "Activation of beta-catenin-Tcf signaling in colon cancer by mutations in RT beta-catenin or APC."; RL Science 275:1787-1790(1997). RN [97] RP VARIANTS HEPATOBLASTOMA TYR-32; VAL-34; CYS-37 AND ALA-41. RX PubMed=9927029; RA Koch A., Denkhaus D., Albrecht S., Leuschner I., von Schweinitz D., RA Pietsch T.; RT "Childhood hepatoblastomas frequently carry a mutated degradation targeting RT box of the beta-catenin gene."; RL Cancer Res. 59:269-273(1999). RN [98] RP VARIANT HEPATOBLASTOMA ALA-41. RX PubMed=10398436; RX DOI=10.1002/(sici)1098-2264(199908)25:4<399::aid-gcc14>3.3.co;2-o; RA Blaeker H., Hofmann W.J., Rieker R.J., Penzel R., Graf M., Otto H.F.; RT "Beta-catenin accumulation and mutation of the CTNNB1 gene in RT hepatoblastoma."; RL Genes Chromosomes Cancer 25:399-402(1999). RN [99] RP VARIANTS OVARIAN CANCER CYS-37; ILE-41 AND ALA-41. RX PubMed=10391090; DOI=10.1111/j.1349-7006.1999.tb00777.x; RA Sagae S., Kobayashi K., Nishioka Y., Sugimura M., Ishioka S., Nagata M., RA Terasawa K., Tokino T., Kudo R.; RT "Mutational analysis of beta-catenin gene in Japanese ovarian carcinomas: RT frequent mutations in endometrioid carcinomas."; RL Jpn. J. Cancer Res. 90:510-515(1999). RN [100] RP VARIANT DESMOID TUMOR ALA-41. RX PubMed=10655994; DOI=10.1136/jcp.52.9.695; RA Shitoh K., Konishi F., Iijima T., Ohdaira T., Sakai K., Kanazawa K., RA Miyaki M.; RT "A novel case of a sporadic desmoid tumour with mutation of the beta RT catenin gene."; RL J. Clin. Pathol. 52:695-696(1999). RN [101] RP VARIANTS PTR GLY-32; TYR-32; PHE-33; TYR-33; GLU-34; CYS-37; PHE-37 AND RP ILE-41. RX PubMed=10192393; DOI=10.1038/7747; RA Chan E.F., Gat U., McNiff J.M., Fuchs E.; RT "A common human skin tumour is caused by activating mutations in beta- RT catenin."; RL Nat. Genet. 21:410-413(1999). RN [102] RP VARIANTS HEPATOCELLULAR CARCINOMA ARG-23; 25-TRP--SER-33 DEL; ALA-32; RP GLY-32; TYR-32; LEU-33; PHE-33; ARG-34; SER-35; ALA-37; 37-SER-GLY-38 RP DELINS TRP; TYR-37; ALA-41; ILE-41; PHE-45 AND PRO-45. RX PubMed=10435629; DOI=10.1038/sj.onc.1202800; RA Legoix P., Bluteau O., Bayer J., Perret C., Balabaud C., Belghiti J., RA Franco D., Thomas G., Laurent-Puig P., Zucman-Rossi J.; RT "Beta-catenin mutations in hepatocellular carcinoma correlate with a low RT rate of loss of heterozygosity."; RL Oncogene 18:4044-4046(1999). RN [103] RP VARIANTS MDB PHE-33 AND ALA-37. RX PubMed=10666372; DOI=10.1016/s0002-9440(10)64747-5; RA Huang H., Mahler-Araujo B.M., Sankila A., Chimelli L., Yonekawa Y., RA Kleihues P., Ohgaki H.; RT "APC mutations in sporadic medulloblastomas."; RL Am. J. Pathol. 156:433-437(2000). RN [104] RP VARIANT NEDSDV PRO-388. RX PubMed=25326669; DOI=10.1007/s00439-014-1498-1; RA Kuechler A., Willemsen M.H., Albrecht B., Bacino C.A., Bartholomew D.W., RA van Bokhoven H., van den Boogaard M.J., Bramswig N., Buettner C., RA Cremer K., Czeschik J.C., Engels H., van Gassen K., Graf E., van Haelst M., RA He W., Hogue J.S., Kempers M., Koolen D., Monroe G., de Munnik S., RA Pastore M., Reis A., Reuter M.S., Tegay D.H., Veltman J., Visser G., RA van Hasselt P., Smeets E.E., Vissers L., Wieland T., Wissink W., Yntema H., RA Zink A.M., Strom T.M., Luedecke H.J., Kleefstra T., Wieczorek D.; RT "De novo mutations in beta-catenin (CTNNB1) appear to be a frequent cause RT of intellectual disability: expanding the mutational and clinical RT spectrum."; RL Hum. Genet. 134:97-109(2015). RN [105] RP VARIANT NEDSDV 558-GLN--LEU-781 DEL. RX PubMed=28514307; DOI=10.1097/md.0000000000006914; RA Li N., Xu Y., Li G., Yu T., Yao R.E., Wang X., Wang J.; RT "Exome sequencing identifies a de novo mutation of CTNNB1 gene in a patient RT mainly presented with retinal detachment, lens and vitreous opacities, RT microcephaly, and developmental delay: Case report and literature review."; RL Medicine (Baltimore) 96:E6914-E6914(2017). CC -!- FUNCTION: Key downstream component of the canonical Wnt signaling CC pathway (PubMed:17524503, PubMed:18077326, PubMed:18086858, CC PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, CC PubMed:22699938). In the absence of Wnt, forms a complex with AXIN1, CC AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N- CC terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and CC its subsequent degradation by the proteasome (PubMed:17524503, CC PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, CC PubMed:22155184, PubMed:22647378, PubMed:22699938). In the presence of CC Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, CC where it acts as a coactivator for transcription factors of the TCF/LEF CC family, leading to activate Wnt responsive genes (PubMed:17524503, CC PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, CC PubMed:22155184, PubMed:22647378, PubMed:22699938). Involved in the CC regulation of cell adhesion, as component of an E-cadherin:catenin CC adhesion complex (By similarity). Acts as a negative regulator of CC centrosome cohesion (PubMed:18086858). Involved in the CC CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization CC (PubMed:21262353). Blocks anoikis of malignant kidney and intestinal CC epithelial cells and promotes their anchorage-independent growth by CC down-regulating DAPK2 (PubMed:18957423). Disrupts PML function and PML- CC NB formation by inhibiting RANBP2-mediated sumoylation of PML CC (PubMed:22155184). Promotes neurogenesis by maintaining sympathetic CC neuroblasts within the cell cycle (By similarity). Involved in CC chondrocyte differentiation via interaction with SOX9: SOX9-binding CC competes with the binding sites of TCF/LEF within CTNNB1, thereby CC inhibiting the Wnt signaling (By similarity). Acts as a positive CC regulator of odontoblast differentiation during mesenchymal tooth germ CC formation, via promoting the transcription of differentiation factors CC such as LEF1, BMP2 and BMP4 (By similarity). Activity is repressed in a CC MSX1-mediated manner at the bell stage of mesenchymal tooth germ CC formation which prevents premature differentiation of odontoblasts (By CC similarity). {ECO:0000250|UniProtKB:Q02248, CC ECO:0000269|PubMed:17524503, ECO:0000269|PubMed:18077326, CC ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18957423, CC ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:22155184, CC ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:22699938}. CC -!- SUBUNIT: Two separate complex-associated pools are found in the CC cytoplasm. The majority is present as component of an E- CC cadherin:catenin adhesion complex composed of at least E-cadherin/CDH1 CC and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex CC is located to adherens junctions. The stable association of CTNNA1 is CC controversial as CTNNA1 was shown not to bind to F-actin when assembled CC in the complex. Alternatively, the CTNNA1-containing complex may be CC linked to F-actin by other proteins such as LIMA1. Another cytoplasmic CC pool is part of a large complex containing AXIN1, AXIN2, APC, CSNK1A1 CC and GSK3B that promotes phosphorylation on N-terminal Ser and Thr CC residues and ubiquitination of CTNNB1 via BTRC and its subsequent CC degradation by the proteasome. Wnt-dependent activation of DVL CC antagonizes the action of GSK3B. When GSK3B activity is inhibited the CC complex dissociates, CTNNB1 is dephosphorylated and is no longer CC targeted for destruction. The stabilized protein translocates to the CC nucleus, where it binds TCF/LEF-1 family members, BCL9, BCL9L and CC possibly also RUVBL1 and CHD8. Binds CTNNBIP and EP300. CTNNB1 forms a CC ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 CC binding. Interacts with TAX1BP3 (via the PDZ domain); this interaction CC inhibits the transcriptional activity of CTNNB1. Interacts with AJAP1, CC BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds NHERF1. Interacts with CC GLIS2 and MUC1. Interacts with SLC30A9. Interacts with XIRP1. Interacts CC directly with AXIN1; the interaction is regulated by CDK2 CC phosphorylation of AXIN1. Interacts with SCRIB. Interacts with RAPGEF2. CC Interacts with PTPRU (via the cytoplasmic juxtamembrane domain). CC Interacts with EMD. Interacts with TNIK and TCF7L2. Interacts with CC SESTD1 and TRPC4. Interacts with CAV1. Interacts with TRPV4. The TRPV4 CC and CTNNB1 complex can interact with CDH1. Interacts with VCL. CC Interacts with PTPRJ. Interacts with PKT7 and CDK2. Interacts with FAT1 CC (via the cytoplasmic domain). Interacts with NANOS1 and NDRG2. CC Interacts with isoform 1 of NEK2. Interacts with both isoform 1 and CC isoform 2 of CDK5. Interacts with PTK6. Interacts with SOX7; this CC interaction may lead to proteasomal degradation of active CTNNB1 and CC thus inhibition of Wnt/beta-catenin-stimulated transcription. CC Identified in a complex with HINT1 and MITF. Interacts with FHIT. The CC CTNNB1 and TCF7L2/TCF4 complex interacts with PML (isoform PML-4). CC Interacts with FERMT2. Identified in a complex with TCF7L2/TCF4 and CC FERMT2 (PubMed:29739711, PubMed:22699938). Interacts with RORA. May CC interact with P-cadherin/CDH3. Interacts with RNF220 (PubMed:25266658). CC Interacts with CTNND2 (PubMed:25807484). Interacts (via the C-terminal CC region) with CBY1 (PubMed:12712206, PubMed:16424001). The complex CC composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the CC interaction requires the inactive form of GSK3B (phosphorylated at CC 'Ser-9') (PubMed:25169422). Interacts with DLG5 (By similarity). CC Interacts with FAM53B; promoting translocation to the nucleus CC (PubMed:25183871). Interacts with TMEM170B (PubMed:29367600). Interacts CC with AHI1 (PubMed:21623382). Interacts with GID8 (PubMed:28829046). CC Component of an cadherin:catenin adhesion complex composed of at least CC of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 CC catenin/CTNND1 (PubMed:28051089). Forms a complex comprising APPL1, CC RUVBL2, APPL2, HDAC1 and HDAC2 (PubMed:19433865). Interacts with CC IRF2BPL; mediates the ubiquitination and degradation of CTNNB1 CC (PubMed:29374064). Interacts with AMFR (By similarity). Interacts with CC LMBR1L (PubMed:31073040). Interacts with SOX30; prevents interaction of CC CTNNB1 with TCF7L2/TCF4 and leads to inhibition of Wnt signaling CC (PubMed:29739711). Interacts with SOX9; inhibiting CTNNB1 activity by CC competing with the binding sites of TCF/LEF within CTNNB1, thereby CC inhibiting the Wnt signaling (By similarity). Interacts with SPN/CD43 CC cytoplasmic tail (PubMed:15003504). Interacts (when phosphorylated at CC Tyr-333) with isoform M2 of PKM (PKM2); promoting transcription CC activation (PubMed:22056988). Interacts with PKP2 (via HEAD domain) CC (PubMed:11790773). Interacts with CDH1 (PubMed:11790773). Interacts CC (when unphosphorylated) with FLYWCH1, perhaps preventing interaction of CC CTNNB1 with TCF4, and thereby regulating transcription activation; CC phosphorylation of CTNNB1 may inhibit the interaction CC (PubMed:30097457). Interacts (via the central armadillo domains) with CC probable transcriptional regulator ADNP (via N-terminal region); CC interaction is direct and stabilizes CTNNB1 by modulating its CC phosphorylation by glycogen synthase kinase-3 beta GSK3B (By CC similarity). {ECO:0000250|UniProtKB:Q02248, CC ECO:0000269|PubMed:10966653, ECO:0000269|PubMed:11389839, CC ECO:0000269|PubMed:11389840, ECO:0000269|PubMed:11590244, CC ECO:0000269|PubMed:11713475, ECO:0000269|PubMed:11713476, CC ECO:0000269|PubMed:11751639, ECO:0000269|PubMed:11790773, CC ECO:0000269|PubMed:12077367, ECO:0000269|PubMed:12297051, CC ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:12408824, CC ECO:0000269|PubMed:12420223, ECO:0000269|PubMed:12501215, CC ECO:0000269|PubMed:12712206, ECO:0000269|PubMed:12830000, CC ECO:0000269|PubMed:14595118, ECO:0000269|PubMed:15003504, CC ECO:0000269|PubMed:16424001, ECO:0000269|PubMed:16858403, CC ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:17047063, CC ECO:0000269|PubMed:17052462, ECO:0000269|PubMed:17289029, CC ECO:0000269|PubMed:17524503, ECO:0000269|PubMed:18077326, CC ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18378692, CC ECO:0000269|PubMed:18819930, ECO:0000269|PubMed:19433865, CC ECO:0000269|PubMed:19693690, ECO:0000269|PubMed:19816403, CC ECO:0000269|PubMed:19996314, ECO:0000269|PubMed:20026641, CC ECO:0000269|PubMed:20164195, ECO:0000269|PubMed:21132015, CC ECO:0000269|PubMed:21247902, ECO:0000269|PubMed:21262353, CC ECO:0000269|PubMed:21623382, ECO:0000269|PubMed:22056988, CC ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22647378, CC ECO:0000269|PubMed:22699938, ECO:0000269|PubMed:25169422, CC ECO:0000269|PubMed:25183871, ECO:0000269|PubMed:25266658, CC ECO:0000269|PubMed:25807484, ECO:0000269|PubMed:28051089, CC ECO:0000269|PubMed:28829046, ECO:0000269|PubMed:29367600, CC ECO:0000269|PubMed:29374064, ECO:0000269|PubMed:29432739, CC ECO:0000269|PubMed:29739711, ECO:0000269|PubMed:31073040, CC ECO:0000269|PubMed:7982500, ECO:0000305|PubMed:31073040}. CC -!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8 protein CC vPK; this interaction inhibits the Wnt signaling pathway. CC {ECO:0000269|PubMed:29432739}. CC -!- INTERACTION: CC P35222; P01023: A2M; NbExp=3; IntAct=EBI-491549, EBI-640741; CC P35222; P00519: ABL1; NbExp=2; IntAct=EBI-491549, EBI-375543; CC P35222; O43707: ACTN4; NbExp=7; IntAct=EBI-491549, EBI-351526; CC P35222; Q5JTC6: AMER1; NbExp=9; IntAct=EBI-491549, EBI-6169747; CC P35222; P25054: APC; NbExp=19; IntAct=EBI-491549, EBI-727707; CC P35222; P10275: AR; NbExp=11; IntAct=EBI-491549, EBI-608057; CC P35222; O15169: AXIN1; NbExp=44; IntAct=EBI-491549, EBI-710484; CC P35222; Q9Y2T1: AXIN2; NbExp=2; IntAct=EBI-491549, EBI-4400025; CC P35222; O00512: BCL9; NbExp=5; IntAct=EBI-491549, EBI-533127; CC P35222; A1Z199: BCR/ABL fusion; NbExp=2; IntAct=EBI-491549, EBI-7286259; CC P35222; P23560-2: BDNF; NbExp=3; IntAct=EBI-491549, EBI-12275524; CC P35222; Q2LD37: BLTP1; NbExp=2; IntAct=EBI-491549, EBI-2683809; CC P35222; Q9Y297: BTRC; NbExp=8; IntAct=EBI-491549, EBI-307461; CC P35222; P55212: CASP6; NbExp=3; IntAct=EBI-491549, EBI-718729; CC P35222; P35520: CBS; NbExp=3; IntAct=EBI-491549, EBI-740135; CC P35222; Q6P1J9: CDC73; NbExp=10; IntAct=EBI-491549, EBI-930143; CC P35222; P12830: CDH1; NbExp=17; IntAct=EBI-491549, EBI-727477; CC P35222; P19022: CDH2; NbExp=8; IntAct=EBI-491549, EBI-2256711; CC P35222; P33151: CDH5; NbExp=7; IntAct=EBI-491549, EBI-2903122; CC P35222; Q92793: CREBBP; NbExp=2; IntAct=EBI-491549, EBI-81215; CC P35222; P02511: CRYAB; NbExp=6; IntAct=EBI-491549, EBI-739060; CC P35222; P35221: CTNNA1; NbExp=5; IntAct=EBI-491549, EBI-701918; CC P35222; Q9UI47-1: CTNNA3; NbExp=4; IntAct=EBI-491549, EBI-21980640; CC P35222; Q9NSA3: CTNNBIP1; NbExp=14; IntAct=EBI-491549, EBI-747082; CC P35222; Q9NYF0: DACT1; NbExp=3; IntAct=EBI-491549, EBI-3951744; CC P35222; G5E9A7: DMWD; NbExp=3; IntAct=EBI-491549, EBI-10976677; CC P35222; P26358: DNMT1; NbExp=8; IntAct=EBI-491549, EBI-719459; CC P35222; P18146: EGR1; NbExp=7; IntAct=EBI-491549, EBI-2834611; CC P35222; P50402: EMD; NbExp=3; IntAct=EBI-491549, EBI-489887; CC P35222; P29317: EPHA2; NbExp=2; IntAct=EBI-491549, EBI-702104; CC P35222; Q9UKB1: FBXW11; NbExp=4; IntAct=EBI-491549, EBI-355189; CC P35222; Q96AC1: FERMT2; NbExp=13; IntAct=EBI-491549, EBI-4399465; CC P35222; Q92915-2: FGF14; NbExp=3; IntAct=EBI-491549, EBI-12836320; CC P35222; P11362: FGFR1; NbExp=3; IntAct=EBI-491549, EBI-1028277; CC P35222; P49789: FHIT; NbExp=4; IntAct=EBI-491549, EBI-741760; CC P35222; Q08050: FOXM1; NbExp=16; IntAct=EBI-491549, EBI-866480; CC P35222; P04406: GAPDH; NbExp=3; IntAct=EBI-491549, EBI-354056; CC P35222; P14136: GFAP; NbExp=3; IntAct=EBI-491549, EBI-744302; CC P35222; Q9BZE0: GLIS2; NbExp=6; IntAct=EBI-491549, EBI-7251368; CC P35222; P49841: GSK3B; NbExp=19; IntAct=EBI-491549, EBI-373586; CC P35222; Q9UBN7: HDAC6; NbExp=4; IntAct=EBI-491549, EBI-301697; CC P35222; Q16665: HIF1A; NbExp=4; IntAct=EBI-491549, EBI-447269; CC P35222; O00291: HIP1; NbExp=3; IntAct=EBI-491549, EBI-473886; CC P35222; P07900: HSP90AA1; NbExp=3; IntAct=EBI-491549, EBI-296047; CC P35222; P42858: HTT; NbExp=14; IntAct=EBI-491549, EBI-466029; CC P35222; P08069: IGF1R; NbExp=3; IntAct=EBI-491549, EBI-475981; CC P35222; P46940: IQGAP1; NbExp=3; IntAct=EBI-491549, EBI-297509; CC P35222; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-491549, EBI-1055254; CC P35222; O75564: JRK; NbExp=3; IntAct=EBI-491549, EBI-8607681; CC P35222; Q14678: KANK1; NbExp=2; IntAct=EBI-491549, EBI-2556221; CC P35222; P13473-2: LAMP2; NbExp=3; IntAct=EBI-491549, EBI-21591415; CC P35222; Q9UJU2: LEF1; NbExp=10; IntAct=EBI-491549, EBI-926131; CC P35222; Q8WVC0: LEO1; NbExp=2; IntAct=EBI-491549, EBI-932432; CC P35222; Q14114-3: LRP8; NbExp=3; IntAct=EBI-491549, EBI-25832196; CC P35222; Q9GZQ8: MAP1LC3B; NbExp=5; IntAct=EBI-491549, EBI-373144; CC P35222; P51608: MECP2; NbExp=3; IntAct=EBI-491549, EBI-1189067; CC P35222; P55197: MLLT10; NbExp=4; IntAct=EBI-491549, EBI-1104952; CC P35222; Q92597: NDRG1; NbExp=3; IntAct=EBI-491549, EBI-716486; CC P35222; P19404: NDUFV2; NbExp=3; IntAct=EBI-491549, EBI-713665; CC P35222; P19838: NFKB1; NbExp=3; IntAct=EBI-491549, EBI-300010; CC P35222; P29474: NOS3; NbExp=4; IntAct=EBI-491549, EBI-1391623; CC P35222; O00482-1: NR5A2; NbExp=5; IntAct=EBI-491549, EBI-15960777; CC P35222; P49757: NUMB; NbExp=2; IntAct=EBI-491549, EBI-915016; CC P35222; P49757-3: NUMB; NbExp=3; IntAct=EBI-491549, EBI-10692196; CC P35222; P14618: PKM; NbExp=4; IntAct=EBI-491549, EBI-353408; CC P35222; P14618-1: PKM; NbExp=3; IntAct=EBI-491549, EBI-4304679; CC P35222; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-491549, EBI-5280197; CC P35222; Q03431: PTH1R; NbExp=4; IntAct=EBI-491549, EBI-2860297; CC P35222; Q13308: PTK7; NbExp=5; IntAct=EBI-491549, EBI-2803245; CC P35222; P08575: PTPRC; NbExp=2; IntAct=EBI-491549, EBI-1341; CC P35222; P23470: PTPRG; NbExp=2; IntAct=EBI-491549, EBI-2258115; CC P35222; Q12913: PTPRJ; NbExp=2; IntAct=EBI-491549, EBI-2264500; CC P35222; P49023: PXN; NbExp=4; IntAct=EBI-491549, EBI-702209; CC P35222; P62826: RAN; NbExp=3; IntAct=EBI-491549, EBI-286642; CC P35222; Q04206: RELA; NbExp=3; IntAct=EBI-491549, EBI-73886; CC P35222; Q13761: RUNX3; NbExp=12; IntAct=EBI-491549, EBI-925990; CC P35222; Q9Y265: RUVBL1; NbExp=3; IntAct=EBI-491549, EBI-353675; CC P35222; Q01826: SATB1; NbExp=9; IntAct=EBI-491549, EBI-743747; CC P35222; Q9H6I2: SOX17; NbExp=2; IntAct=EBI-491549, EBI-9106753; CC P35222; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-491549, EBI-5235340; CC P35222; P12931: SRC; NbExp=2; IntAct=EBI-491549, EBI-621482; CC P35222; P15884: TCF4; NbExp=22; IntAct=EBI-491549, EBI-533224; CC P35222; P36402: TCF7; NbExp=4; IntAct=EBI-491549, EBI-2119465; CC P35222; Q9NQB0: TCF7L2; NbExp=27; IntAct=EBI-491549, EBI-924724; CC P35222; O14746: TERT; NbExp=2; IntAct=EBI-491549, EBI-1772203; CC P35222; Q9UKE5: TNIK; NbExp=3; IntAct=EBI-491549, EBI-1051794; CC P35222; P11388: TOP2A; NbExp=5; IntAct=EBI-491549, EBI-539628; CC P35222; O14656-2: TOR1A; NbExp=3; IntAct=EBI-491549, EBI-25847109; CC P35222; Q13625: TP53BP2; NbExp=5; IntAct=EBI-491549, EBI-77642; CC P35222; O95071: UBR5; NbExp=6; IntAct=EBI-491549, EBI-358329; CC P35222; Q9GZV5: WWTR1; NbExp=4; IntAct=EBI-491549, EBI-747743; CC P35222; P46937: YAP1; NbExp=13; IntAct=EBI-491549, EBI-1044059; CC P35222; P46937-3: YAP1; NbExp=2; IntAct=EBI-491549, EBI-6558686; CC P35222; O35625: Axin1; Xeno; NbExp=4; IntAct=EBI-491549, EBI-2365912; CC P35222; Q9YGY0: axin1; Xeno; NbExp=2; IntAct=EBI-491549, EBI-1037449; CC P35222; Q67FY2: Bcl9l; Xeno; NbExp=2; IntAct=EBI-491549, EBI-5234367; CC P35222; P33724: CAV1; Xeno; NbExp=5; IntAct=EBI-491549, EBI-79998; CC P35222; P26231: Ctnna1; Xeno; NbExp=2; IntAct=EBI-491549, EBI-647895; CC P35222; P27782: Lef1; Xeno; NbExp=2; IntAct=EBI-491549, EBI-984464; CC P35222; Q01887: Ryk; Xeno; NbExp=2; IntAct=EBI-491549, EBI-16110594; CC P35222; P18012: sctB; Xeno; NbExp=4; IntAct=EBI-491549, EBI-491541; CC P35222; P40645: Sox6; Xeno; NbExp=2; IntAct=EBI-491549, EBI-3505685; CC P35222; Q9DBG9: Tax1bp3; Xeno; NbExp=3; IntAct=EBI-491549, EBI-1161647; CC P35222; Q9EPK5: Wwtr1; Xeno; NbExp=2; IntAct=EBI-491549, EBI-1211920; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25183871, CC ECO:0000269|PubMed:29739711, ECO:0000269|PubMed:31801859}. Nucleus CC {ECO:0000269|PubMed:24342833, ECO:0000269|PubMed:25183871, CC ECO:0000269|PubMed:28829046, ECO:0000269|PubMed:29367600, CC ECO:0000269|PubMed:29739711, ECO:0000269|PubMed:31801859}. Cytoplasm, CC cytoskeleton {ECO:0000250|UniProtKB:B6V8E6}. Cell junction, adherens CC junction {ECO:0000269|PubMed:10725230}. Cell junction CC {ECO:0000250|UniProtKB:B6V8E6}. Cell membrane CC {ECO:0000269|PubMed:11790773, ECO:0000269|PubMed:24342833}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, CC cytoskeleton, spindle pole. Synapse {ECO:0000250|UniProtKB:Q02248}. CC Cytoplasm, cytoskeleton, cilium basal body CC {ECO:0000250|UniProtKB:Q02248}. Note=Colocalized with RAPGEF2 and TJP1 CC at cell-cell contacts (By similarity). Cytoplasmic when it is un-stable CC (highly phosphorylated) or bound to CDH1. Translocates to the nucleus CC when it is stabilized (low level of phosphorylation). Interaction with CC GLIS2 and MUC1 promotes nuclear translocation. Interaction with EMD CC inhibits nuclear localization. The majority of beta-catenin is CC localized to the cell membrane. In interphase, colocalizes with CROCC CC between CEP250 puncta at the proximal end of centrioles, and this CC localization is dependent on CROCC and CEP250. In mitosis, when NEK2 CC activity increases, it localizes to centrosomes at spindle poles CC independent of CROCC. Colocalizes with CDK5 in the cell-cell contacts CC and plasma membrane of undifferentiated and differentiated CC neuroblastoma cells. Interaction with FAM53B promotes translocation to CC the nucleus (PubMed:25183871). {ECO:0000250|UniProtKB:B6V8E6, CC ECO:0000269|PubMed:25183871}. CC -!- TISSUE SPECIFICITY: Expressed in several hair follicle cell types: CC basal and peripheral matrix cells, and cells of the outer and inner CC root sheaths. Expressed in colon. Present in cortical neurons (at CC protein level). Expressed in breast cancer tissues (at protein level) CC (PubMed:29367600). {ECO:0000269|PubMed:11703283, CC ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:17289029, CC ECO:0000269|PubMed:29367600}. CC -!- PTM: Phosphorylation at Ser-552 by AMPK promotes stabilization of the CC protein, enhancing TCF/LEF-mediated transcription (By similarity). CC Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by CC another kinase (PubMed:10966653, PubMed:12051714, PubMed:12027456). CC Phosphorylation proceeds then from Thr-41 to Ser-37 and Ser-33 CC (PubMed:12077367, PubMed:25169422). Phosphorylated by NEK2 CC (PubMed:18086858). EGF stimulates tyrosine phosphorylation CC (PubMed:10187801). Phosphorylated on Ser-33 and Ser-37 by HIPK2 and CC GSK3B, this phosphorylation triggers proteasomal degradation CC (PubMed:20307497). Phosphorylation on Ser-191 and Ser-246 by CDK5 CC (PubMed:17009320). Phosphorylation by CDK2 regulates insulin CC internalization (PubMed:21262353). Phosphorylation by PTK6 at Tyr-64, CC Tyr-142, Tyr-331 and/or Tyr-333 with the predominant site at Tyr-64 is CC not essential for inhibition of transcriptional activity CC (PubMed:20026641). Phosphorylation by SRC at Tyr-333 promotes CC interaction with isoform M2 of PKM (PKM2); promoting transcription CC activation (PubMed:22056988). {ECO:0000250|UniProtKB:Q02248, CC ECO:0000269|PubMed:10187801, ECO:0000269|PubMed:10966653, CC ECO:0000269|PubMed:12027456, ECO:0000269|PubMed:12051714, CC ECO:0000269|PubMed:12077367, ECO:0000269|PubMed:17009320, CC ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:20026641, CC ECO:0000269|PubMed:20307497, ECO:0000269|PubMed:21262353, CC ECO:0000269|PubMed:22056988, ECO:0000269|PubMed:25169422}. CC -!- PTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when CC phosphorylated by GSK3B, leading to its degradation (PubMed:12077367). CC Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, CC SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent CC proteasomal degradation (PubMed:11389839, PubMed:11389840, CC PubMed:20307497). Ubiquitinated and degraded following interaction with CC SOX9 (By similarity). {ECO:0000250|UniProtKB:Q02248, CC ECO:0000269|PubMed:11389839, ECO:0000269|PubMed:11389840, CC ECO:0000269|PubMed:12077367, ECO:0000269|PubMed:20307497}. CC -!- PTM: S-nitrosylation at Cys-619 within adherens junctions promotes CC VEGF-induced, NO-dependent endothelial cell permeability by disrupting CC interaction with E-cadherin, thus mediating disassembly adherens CC junctions. {ECO:0000250|UniProtKB:Q02248}. CC -!- PTM: O-glycosylation at Ser-23 decreases nuclear localization and CC transcriptional activity, and increases localization to the plasma CC membrane and interaction with E-cadherin CDH1. CC {ECO:0000269|PubMed:24342833}. CC -!- PTM: Deacetylated at Lys-49 by SIRT1. {ECO:0000269|PubMed:24824780}. CC -!- PTM: Phosphorylated at Thr-556 by herpes virus 1/HHV-1 leading to CC CTNNB1 inhibition. {ECO:0000269|PubMed:24824780}. CC -!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease CC characterized by malignant lesions arising from the inner wall of the CC large intestine (the colon) and the rectum. Genetic alterations are CC often associated with progression from premalignant lesion (adenoma) to CC invasive adenocarcinoma. Risk factors for cancer of the colon and CC rectum include colon polyps, long-standing ulcerative colitis, and CC genetic family history. {ECO:0000269|PubMed:9065402}. Note=The gene CC represented in this entry may be involved in disease pathogenesis. CC -!- DISEASE: Note=Activating mutations in CTNNB1 have oncogenic activity CC resulting in tumor development. Somatic mutations are found in various CC tumor types, including colon cancers, ovarian and prostate carcinomas, CC hepatoblastoma (HB), hepatocellular carcinoma (HCC). HBs are malignant CC embryonal tumors mainly affecting young children in the first three CC years of life. CC -!- DISEASE: Pilomatrixoma (PTR) [MIM:132600]: Common benign skin tumor. CC {ECO:0000269|PubMed:10192393, ECO:0000269|PubMed:11703283, CC ECO:0000269|PubMed:12027456}. Note=The gene represented in this entry CC is involved in disease pathogenesis. CC -!- DISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive CC embryonal tumor of the cerebellum with a preferential manifestation in CC children. {ECO:0000269|PubMed:10666372, ECO:0000269|PubMed:12027456}. CC Note=The gene represented in this entry may be involved in disease CC pathogenesis. CC -!- DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer CC defines malignancies originating from ovarian tissue. Although many CC histologic types of ovarian tumors have been described, epithelial CC ovarian carcinoma is the most common form. Ovarian cancers are often CC asymptomatic and the recognized signs and symptoms, even of late-stage CC disease, are vague. Consequently, most patients are diagnosed with CC advanced disease. {ECO:0000269|PubMed:10391090}. Note=Disease CC susceptibility is associated with variants affecting the gene CC represented in this entry. CC -!- DISEASE: Note=A chromosomal aberration involving CTNNB1 is found in CC salivary gland pleiomorphic adenomas, the most common benign epithelial CC tumors of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1. CC -!- DISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive CC neoplasm of the serosal lining of the chest. It appears as broad sheets CC of cells, with some regions containing spindle-shaped, sarcoma-like CC cells and other regions showing adenomatous patterns. Pleural CC mesotheliomas have been linked to exposure to asbestos. CC {ECO:0000269|PubMed:11464291}. Note=The gene represented in this entry CC may be involved in disease pathogenesis. CC -!- DISEASE: Neurodevelopmental disorder with spastic diplegia and visual CC defects (NEDSDV) [MIM:615075]: An autosomal dominant disorder CC characterized by global developmental delay, severe intellectual CC disability with absent or very limited speech, microcephaly, CC spasticity, and visual abnormalities. {ECO:0000269|PubMed:23033978, CC ECO:0000269|PubMed:25326669, ECO:0000269|PubMed:28514307}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Vitreoretinopathy, exudative 7 (EVR7) [MIM:617572]: A form of CC exudative vitreoretinopathy, a disorder of the retinal vasculature CC characterized by an abrupt cessation of growth of peripheral CC capillaries, leading to an avascular peripheral retina. This may lead CC to compensatory retinal neovascularization, which is thought to be CC induced by hypoxia from the initial avascular insult. New vessels are CC prone to leakage and rupture causing exudates and bleeding, followed by CC scarring, retinal detachment and blindness. Clinical features can be CC highly variable, even within the same family. Patients with mild forms CC of the disease are asymptomatic, and their only disease related CC abnormality is an arc of avascular retina in the extreme temporal CC periphery. {ECO:0000269|PubMed:28575650}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}. CC -!- CAUTION: A paper showing an interaction with TBP and phosphorylation at CC Tyr-86 and Tyr-654 has been retracted due to panel duplication in CC several figures. {ECO:0000269|PubMed:11279024, CC ECO:0000305|PubMed:27226643}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG35511.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC Sequence=BAB93475.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/71/CTNNB1"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ctnnb1/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Beta-catenin entry; CC URL="https://en.wikipedia.org/wiki/Beta-catenin"; 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; X87838; CAA61107.1; -; mRNA. DR EMBL; Z19054; CAA79497.1; -; mRNA. DR EMBL; AF130085; AAG35511.1; ALT_SEQ; mRNA. DR EMBL; AY463360; AAR18817.1; -; Genomic_DNA. DR EMBL; AK289932; BAF82621.1; -; mRNA. DR EMBL; AC104307; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64625.1; -; Genomic_DNA. DR EMBL; BC058926; AAH58926.1; -; mRNA. DR EMBL; AY081165; AAL89457.1; -; Genomic_DNA. DR EMBL; AB062292; BAB93475.1; ALT_INIT; mRNA. DR CCDS; CCDS2694.1; -. DR PIR; A38973; A38973. DR RefSeq; NP_001091679.1; NM_001098209.1. DR RefSeq; NP_001091680.1; NM_001098210.1. DR RefSeq; NP_001895.1; NM_001904.3. DR RefSeq; XP_005264943.1; XM_005264886.2. DR RefSeq; XP_016861227.1; XM_017005738.1. DR PDB; 1G3J; X-ray; 2.10 A; A/C=133-664. DR PDB; 1JDH; X-ray; 1.90 A; A=135-663. DR PDB; 1JPW; X-ray; 2.50 A; A/B/C=131-670. DR PDB; 1LUJ; X-ray; 2.50 A; A=150-663. DR PDB; 1P22; X-ray; 2.95 A; C=19-44. DR PDB; 1QZ7; X-ray; 2.20 A; A=133-665. DR PDB; 1T08; X-ray; 2.10 A; A=146-664. DR PDB; 1TH1; X-ray; 2.50 A; A/B=133-664. DR PDB; 2G57; NMR; -; A=19-44. DR PDB; 2GL7; X-ray; 2.60 A; A/D=138-686. DR PDB; 2Z6H; X-ray; 2.20 A; A=138-781. DR PDB; 3DIW; X-ray; 2.10 A; C/D=772-781. DR PDB; 3FQN; X-ray; 1.65 A; C=30-39. DR PDB; 3FQR; X-ray; 1.70 A; C=30-39. DR PDB; 3SL9; X-ray; 2.20 A; A/B/E/G=141-305. DR PDB; 3SLA; X-ray; 2.50 A; A/B/C/D/E=141-306. DR PDB; 3TX7; X-ray; 2.76 A; A=138-663. DR PDB; 4DJS; X-ray; 3.03 A; A=148-665. DR PDB; 6M90; X-ray; 2.05 A; C=17-48. DR PDB; 6M91; X-ray; 2.40 A; C=17-48. DR PDB; 6M92; X-ray; 2.35 A; C=17-48. DR PDB; 6M93; X-ray; 2.50 A; C=17-48. DR PDB; 6M94; X-ray; 2.70 A; C=17-48. DR PDB; 6O9B; X-ray; 2.20 A; C=41-49. DR PDB; 6O9C; X-ray; 2.45 A; C=41-49. DR PDB; 6WLX; X-ray; 2.20 A; B=671-677. DR PDB; 6WNX; X-ray; 2.50 A; C/F/I=31-39. DR PDB; 7AFW; X-ray; 1.81 A; A=141-305. DR PDB; 7AR4; X-ray; 2.60 A; AAA=134-665. DR PDB; 7UWI; X-ray; 2.32 A; A=143-663. DR PDB; 7UWO; X-ray; 2.75 A; A=134-665. DR PDB; 8EI9; X-ray; 3.90 A; A=134-665. DR PDB; 8EIA; X-ray; 3.60 A; A=134-665. DR PDB; 8EIB; X-ray; 3.76 A; A=134-665. DR PDB; 8EIC; X-ray; 2.62 A; A=134-665. DR PDBsum; 1G3J; -. DR PDBsum; 1JDH; -. DR PDBsum; 1JPW; -. DR PDBsum; 1LUJ; -. DR PDBsum; 1P22; -. DR PDBsum; 1QZ7; -. DR PDBsum; 1T08; -. DR PDBsum; 1TH1; -. DR PDBsum; 2G57; -. DR PDBsum; 2GL7; -. DR PDBsum; 2Z6H; -. DR PDBsum; 3DIW; -. DR PDBsum; 3FQN; -. DR PDBsum; 3FQR; -. DR PDBsum; 3SL9; -. DR PDBsum; 3SLA; -. DR PDBsum; 3TX7; -. DR PDBsum; 4DJS; -. DR PDBsum; 6M90; -. DR PDBsum; 6M91; -. DR PDBsum; 6M92; -. DR PDBsum; 6M93; -. DR PDBsum; 6M94; -. DR PDBsum; 6O9B; -. DR PDBsum; 6O9C; -. DR PDBsum; 6WLX; -. DR PDBsum; 6WNX; -. DR PDBsum; 7AFW; -. DR PDBsum; 7AR4; -. DR PDBsum; 7UWI; -. DR PDBsum; 7UWO; -. DR PDBsum; 8EI9; -. DR PDBsum; 8EIA; -. DR PDBsum; 8EIB; -. DR PDBsum; 8EIC; -. DR AlphaFoldDB; P35222; -. DR SMR; P35222; -. DR BioGRID; 107880; 919. DR ComplexPortal; CPX-316; beta1-catenin - LEF1 complex. DR CORUM; P35222; -. DR DIP; DIP-122N; -. DR IntAct; P35222; 278. DR MINT; P35222; -. DR STRING; 9606.ENSP00000495360; -. DR BindingDB; P35222; -. DR ChEMBL; CHEMBL5866; -. DR DrugBank; DB03904; Urea. DR GlyCosmos; P35222; 4 sites, 1 glycan. DR GlyGen; P35222; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P35222; -. DR MetOSite; P35222; -. DR PhosphoSitePlus; P35222; -. DR SwissPalm; P35222; -. DR BioMuta; CTNNB1; -. DR DMDM; 461854; -. DR CPTAC; CPTAC-1745; -. DR CPTAC; non-CPTAC-3265; -. DR CPTAC; non-CPTAC-3266; -. DR CPTAC; non-CPTAC-5365; -. DR CPTAC; non-CPTAC-5715; -. DR CPTAC; non-CPTAC-5716; -. DR EPD; P35222; -. DR jPOST; P35222; -. DR MassIVE; P35222; -. DR MaxQB; P35222; -. DR PaxDb; 9606-ENSP00000344456; -. DR PeptideAtlas; P35222; -. DR PRIDE; P35222; -. DR Pumba; P35222; -. DR ABCD; P35222; 7 sequenced antibodies. DR Antibodypedia; 3432; 5983 antibodies from 57 providers. DR DNASU; 1499; -. DR Ensembl; ENST00000349496.11; ENSP00000344456.5; ENSG00000168036.18. DR Ensembl; ENST00000396183.7; ENSP00000379486.3; ENSG00000168036.18. DR Ensembl; ENST00000396185.8; ENSP00000379488.3; ENSG00000168036.18. DR Ensembl; ENST00000405570.6; ENSP00000385604.1; ENSG00000168036.18. DR Ensembl; ENST00000431914.6; ENSP00000412219.2; ENSG00000168036.18. DR Ensembl; ENST00000433400.6; ENSP00000387455.2; ENSG00000168036.18. DR Ensembl; ENST00000441708.2; ENSP00000401599.2; ENSG00000168036.18. DR Ensembl; ENST00000450969.6; ENSP00000409302.2; ENSG00000168036.18. DR Ensembl; ENST00000642248.1; ENSP00000495244.1; ENSG00000168036.18. DR Ensembl; ENST00000642315.1; ENSP00000495076.1; ENSG00000168036.18. DR Ensembl; ENST00000642426.1; ENSP00000495719.1; ENSG00000168036.18. DR Ensembl; ENST00000642992.1; ENSP00000496385.1; ENSG00000168036.18. DR Ensembl; ENST00000643031.1; ENSP00000495450.1; ENSG00000168036.18. DR Ensembl; ENST00000643297.1; ENSP00000494677.1; ENSG00000168036.18. DR Ensembl; ENST00000643541.1; ENSP00000494411.1; ENSG00000168036.18. DR Ensembl; ENST00000643977.1; ENSP00000494053.1; ENSG00000168036.18. DR Ensembl; ENST00000643992.1; ENSP00000493610.1; ENSG00000168036.18. DR Ensembl; ENST00000644867.1; ENSP00000495992.1; ENSG00000168036.18. DR Ensembl; ENST00000645210.1; ENSP00000496180.1; ENSG00000168036.18. DR Ensembl; ENST00000645320.1; ENSP00000495360.1; ENSG00000168036.18. DR Ensembl; ENST00000645982.1; ENSP00000494845.1; ENSG00000168036.18. DR Ensembl; ENST00000646369.1; ENSP00000494914.1; ENSG00000168036.18. DR Ensembl; ENST00000646725.1; ENSP00000496021.1; ENSG00000168036.18. DR Ensembl; ENST00000647390.1; ENSP00000493533.1; ENSG00000168036.18. DR GeneID; 1499; -. DR KEGG; hsa:1499; -. DR MANE-Select; ENST00000349496.11; ENSP00000344456.5; NM_001904.4; NP_001895.1. DR UCSC; uc003ckp.3; human. DR AGR; HGNC:2514; -. DR CTD; 1499; -. DR DisGeNET; 1499; -. DR GeneCards; CTNNB1; -. DR GeneReviews; CTNNB1; -. DR HGNC; HGNC:2514; CTNNB1. DR HPA; ENSG00000168036; Low tissue specificity. DR MalaCards; CTNNB1; -. DR MIM; 114500; phenotype. DR MIM; 116806; gene. DR MIM; 132600; phenotype. DR MIM; 155255; phenotype. DR MIM; 156240; phenotype. DR MIM; 167000; phenotype. DR MIM; 181030; phenotype. DR MIM; 615075; phenotype. DR MIM; 617572; phenotype. DR neXtProt; NX_P35222; -. DR OpenTargets; ENSG00000168036; -. DR Orphanet; 1501; Adrenocortical carcinoma. DR Orphanet; 210159; Adult hepatocellular carcinoma. DR Orphanet; 54595; Craniopharyngioma. DR Orphanet; 873; Desmoid tumor. DR Orphanet; 891; Familial exudative vitreoretinopathy. DR Orphanet; 569248; Microcystic stromal tumor. DR Orphanet; 85142; NON RARE IN EUROPE: Aldosterone-producing adenoma. DR Orphanet; 33402; Pediatric hepatocellular carcinoma. DR Orphanet; 91414; Pilomatrixoma. DR Orphanet; 404473; Severe intellectual disability-progressive spastic diplegia syndrome. DR PharmGKB; PA27013; -. DR VEuPathDB; HostDB:ENSG00000168036; -. DR eggNOG; KOG4203; Eukaryota. DR GeneTree; ENSGT00940000155471; -. DR InParanoid; P35222; -. DR OMA; YPKLVYT; -. DR OrthoDB; 50711at2759; -. DR PhylomeDB; P35222; -. DR TreeFam; TF317997; -. DR PathwayCommons; P35222; -. DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade. DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT. DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-HSA-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production. DR Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins. DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex. DR Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1). DR Reactome; R-HSA-4086398; Ca2+ pathway. DR Reactome; R-HSA-418990; Adherens junctions interactions. DR Reactome; R-HSA-4411364; Binding of TCF/LEF:CTNNB1 to target gene promoters. DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane. DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-HSA-525793; Myogenesis. DR Reactome; R-HSA-5339716; Signaling by GSK3beta mutants. DR Reactome; R-HSA-5358747; CTNNB1 S33 mutants aren't phosphorylated. DR Reactome; R-HSA-5358749; CTNNB1 S37 mutants aren't phosphorylated. DR Reactome; R-HSA-5358751; CTNNB1 S45 mutants aren't phosphorylated. DR Reactome; R-HSA-5358752; CTNNB1 T41 mutants aren't phosphorylated. DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs. DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX. DR Reactome; R-HSA-8876493; InlA-mediated entry of Listeria monocytogenes into host cells. DR Reactome; R-HSA-8951430; RUNX3 regulates WNT signaling. DR Reactome; R-HSA-9733709; Cardiogenesis. DR Reactome; R-HSA-9754189; Germ layer formation at gastrulation. DR Reactome; R-HSA-9762292; Regulation of CDH11 function. DR Reactome; R-HSA-9764302; Regulation of CDH19 Expression and Function. DR Reactome; R-HSA-9793380; Formation of paraxial mesoderm. DR Reactome; R-HSA-9796292; Formation of axial mesoderm. DR Reactome; R-HSA-9823730; Formation of definitive endoderm. DR Reactome; R-HSA-9824272; Somitogenesis. DR Reactome; R-HSA-9833576; CDH11 homotypic and heterotypic interactions. DR SignaLink; P35222; -. DR SIGNOR; P35222; -. DR BioGRID-ORCS; 1499; 103 hits in 1178 CRISPR screens. DR ChiTaRS; CTNNB1; human. DR EvolutionaryTrace; P35222; -. DR GeneWiki; Beta-catenin; -. DR GenomeRNAi; 1499; -. DR Pharos; P35222; Tchem. DR PRO; PR:P35222; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P35222; Protein. DR Bgee; ENSG00000168036; Expressed in adrenal tissue and 204 other cell types or tissues. DR ExpressionAtlas; P35222; baseline and differential. DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB. DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl. DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0030877; C:beta-catenin destruction complex; IDA:BHF-UCL. DR GO; GO:1990711; C:beta-catenin-ICAT complex; IEA:Ensembl. DR GO; GO:1990907; C:beta-catenin-TCF complex; IDA:FlyBase. DR GO; GO:0070369; C:beta-catenin-TCF7L2 complex; IDA:UniProtKB. DR GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl. DR GO; GO:0016342; C:catenin complex; IDA:UniProtKB. DR GO; GO:0005938; C:cell cortex; IDA:BHF-UCL. DR GO; GO:0030054; C:cell junction; IDA:BHF-UCL. DR GO; GO:0071944; C:cell periphery; IDA:BHF-UCL. DR GO; GO:0005911; C:cell-cell junction; IDA:MGI. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0000791; C:euchromatin; IDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005916; C:fascia adherens; IEA:Ensembl. DR GO; GO:0016600; C:flotillin complex; IEA:Ensembl. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl. DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0031528; C:microvillus membrane; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0099092; C:postsynaptic density, intracellular component; IEA:Ensembl. DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl. DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IEA:Ensembl. DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0032993; C:protein-DNA complex; IDA:BHF-UCL. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IEA:Ensembl. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; ISS:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL. DR GO; GO:1990909; C:Wnt signalosome; NAS:ParkinsonsUK-UCL. DR GO; GO:0030018; C:Z disc; IEA:Ensembl. DR GO; GO:0045294; F:alpha-catenin binding; IPI:BHF-UCL. DR GO; GO:0045296; F:cadherin binding; IPI:BHF-UCL. DR GO; GO:0003682; F:chromatin binding; ISS:ParkinsonsUK-UCL. DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL. DR GO; GO:1990226; F:histone methyltransferase binding; ISS:ARUK-UCL. DR GO; GO:0070411; F:I-SMAD binding; IPI:BHF-UCL. DR GO; GO:0019900; F:kinase binding; IPI:BHF-UCL. DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:BHF-UCL. DR GO; GO:0016922; F:nuclear receptor binding; IPI:BHF-UCL. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IPI:ARUK-UCL. DR GO; GO:0046332; F:SMAD binding; IPI:BHF-UCL. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0001221; F:transcription coregulator binding; ISS:ARUK-UCL. DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL. DR GO; GO:0031625; F:ubiquitin protein ligase binding; EXP:DisProt. DR GO; GO:0090425; P:acinar cell differentiation; IEA:Ensembl. DR GO; GO:0034333; P:adherens junction assembly; IMP:BHF-UCL. DR GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl. DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0036520; P:astrocyte-dopaminergic neuron signaling; IEA:Ensembl. DR GO; GO:0045453; P:bone resorption; IEA:Ensembl. DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:BHF-UCL. DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0044338; P:canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IMP:BHF-UCL. DR GO; GO:0001708; P:cell fate specification; IEA:Ensembl. DR GO; GO:0048469; P:cell maturation; IEA:Ensembl. DR GO; GO:0098609; P:cell-cell adhesion; IMP:BHF-UCL. DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL. DR GO; GO:0071681; P:cellular response to indole-3-methanol; IDA:UniProtKB. DR GO; GO:0022009; P:central nervous system vasculogenesis; IEA:Ensembl. DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl. DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl. DR GO; GO:0061550; P:cranial ganglion development; IEA:Ensembl. DR GO; GO:1904888; P:cranial skeletal system development; IEA:Ensembl. DR GO; GO:0035995; P:detection of muscle stretch; TAS:BHF-UCL. DR GO; GO:1990791; P:dorsal root ganglion development; IEA:Ensembl. DR GO; GO:0009950; P:dorsal/ventral axis specification; IEA:Ensembl. DR GO; GO:0007398; P:ectoderm development; IEA:Ensembl. DR GO; GO:0000578; P:embryonic axis specification; IEA:Ensembl. DR GO; GO:1990403; P:embryonic brain development; IEA:Ensembl. DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl. DR GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl. DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl. DR GO; GO:0035050; P:embryonic heart tube development; IEA:Ensembl. DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl. DR GO; GO:0036023; P:embryonic skeletal limb joint morphogenesis; ISS:BHF-UCL. DR GO; GO:0001711; P:endodermal cell fate commitment; IEA:Ensembl. DR GO; GO:0061154; P:endothelial tube morphogenesis; IMP:BHF-UCL. DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IEA:Ensembl. DR GO; GO:0060767; P:epithelial cell proliferation involved in prostate gland development; IEA:Ensembl. DR GO; GO:0001837; P:epithelial to mesenchymal transition; TAS:HGNC-UCL. DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl. DR GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl. DR GO; GO:1990963; P:establishment of blood-retinal barrier; IEA:Ensembl. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0061198; P:fungiform papilla formation; IEA:Ensembl. DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl. DR GO; GO:0035112; P:genitalia morphogenesis; IEA:Ensembl. DR GO; GO:0007403; P:glial cell fate determination; IEA:Ensembl. DR GO; GO:0035315; P:hair cell differentiation; TAS:BHF-UCL. DR GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl. DR GO; GO:0060789; P:hair follicle placode formation; IEA:Ensembl. DR GO; GO:0030902; P:hindbrain development; IEA:Ensembl. DR GO; GO:0021854; P:hypothalamus development; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl. DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IEA:Ensembl. DR GO; GO:0060487; P:lung epithelial cell differentiation; IEA:Ensembl. DR GO; GO:0060492; P:lung induction; IEA:Ensembl. DR GO; GO:0060484; P:lung-associated mesenchyme development; IEA:Ensembl. DR GO; GO:0030539; P:male genitalia development; IEA:Ensembl. DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl. DR GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IEA:Ensembl. DR GO; GO:0072497; P:mesenchymal stem cell differentiation; IMP:ARUK-UCL. DR GO; GO:0003338; P:metanephros morphogenesis; IEA:Ensembl. DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; ISS:ParkinsonsUK-UCL. DR GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl. DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:BHF-UCL. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; IEA:Ensembl. DR GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; ISS:UniProtKB. DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IEA:Ensembl. DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl. DR GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0033234; P:negative regulation of protein sumoylation; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0072079; P:nephron tubule formation; IEA:Ensembl. DR GO; GO:0001840; P:neural plate development; IEA:Ensembl. DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl. DR GO; GO:0048664; P:neuron fate determination; IEA:Ensembl. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:1990138; P:neuron projection extension; IMP:UniProtKB. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl. DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl. DR GO; GO:0048599; P:oocyte development; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; IMP:ARUK-UCL. DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl. DR GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL. DR GO; GO:0060066; P:oviduct development; IEA:Ensembl. DR GO; GO:0031016; P:pancreas development; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0061047; P:positive regulation of branching involved in lung morphogenesis; IEA:Ensembl. DR GO; GO:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:BHF-UCL. DR GO; GO:2000017; P:positive regulation of determination of dorsal identity; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IEA:Ensembl. DR GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl. DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL. DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; IMP:BHF-UCL. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl. DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl. DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IEA:Ensembl. DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:UniProtKB. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:ParkinsonsUK-UCL. DR GO; GO:1901331; P:positive regulation of odontoblast differentiation; IEA:Ensembl. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl. DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IEA:Ensembl. DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISS:ARUK-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:Ensembl. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0034394; P:protein localization to cell surface; IMP:BHF-UCL. DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB. DR GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl. DR GO; GO:0045765; P:regulation of angiogenesis; TAS:BHF-UCL. DR GO; GO:0090279; P:regulation of calcium ion import; IDA:BHF-UCL. DR GO; GO:0030997; P:regulation of centriole-centriole cohesion; IDA:UniProtKB. DR GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; IMP:BHF-UCL. DR GO; GO:0048145; P:regulation of fibroblast proliferation; TAS:BHF-UCL. DR GO; GO:0031641; P:regulation of myelination; IEA:Ensembl. DR GO; GO:0072182; P:regulation of nephron tubule epithelial cell differentiation; ISS:UniProtKB. DR GO; GO:0050767; P:regulation of neurogenesis; TAS:ParkinsonsUK-UCL. DR GO; GO:2000008; P:regulation of protein localization to cell surface; IDA:BHF-UCL. DR GO; GO:0031396; P:regulation of protein ubiquitination; IMP:DisProt. DR GO; GO:0003266; P:regulation of secondary heart field cardioblast proliferation; IEA:Ensembl. DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; IMP:BHF-UCL. DR GO; GO:0051963; P:regulation of synapse assembly; IEA:Ensembl. DR GO; GO:0042129; P:regulation of T cell proliferation; IEA:Ensembl. DR GO; GO:0051884; P:regulation of timing of anagen; IEA:Ensembl. DR GO; GO:0072053; P:renal inner medulla development; IEA:Ensembl. DR GO; GO:0072054; P:renal outer medulla development; IEA:Ensembl. DR GO; GO:0072033; P:renal vesicle formation; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:UniProtKB. DR GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl. DR GO; GO:0019827; P:stem cell population maintenance; TAS:BHF-UCL. DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl. DR GO; GO:0061549; P:sympathetic ganglion development; ISS:UniProtKB. DR GO; GO:0050808; P:synapse organization; IEA:Ensembl. DR GO; GO:0097091; P:synaptic vesicle clustering; IEA:Ensembl. DR GO; GO:0048489; P:synaptic vesicle transport; IEA:Ensembl. DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl. DR GO; GO:0048538; P:thymus development; IEA:Ensembl. DR GO; GO:0060440; P:trachea formation; IEA:Ensembl. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl. DR CDD; cd21724; CTNNAbd_CTNNB1; 1. DR DisProt; DP01119; -. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR IDEAL; IID00039; -. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000225; Armadillo. DR InterPro; IPR013284; Beta-catenin. DR PANTHER; PTHR45976; ARMADILLO SEGMENT POLARITY PROTEIN; 1. DR PANTHER; PTHR45976:SF4; CATENIN BETA-1; 1. DR Pfam; PF00514; Arm; 4. DR PRINTS; PR01869; BCATNINFAMLY. DR SMART; SM00185; ARM; 12. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50176; ARM_REPEAT; 9. DR Genevisible; P35222; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Cell adhesion; Cell junction; KW Cell membrane; Cell projection; Chromosomal rearrangement; Cytoplasm; KW Cytoskeleton; Disease variant; Glycoprotein; Host-virus interaction; KW Intellectual disability; Membrane; Neurogenesis; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; S-nitrosylation; Synapse; Transcription; KW Transcription regulation; Ubl conjugation; Wnt signaling pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..781 FT /note="Catenin beta-1" FT /id="PRO_0000064271" FT REPEAT 151..191 FT /note="ARM 1" FT REPEAT 193..234 FT /note="ARM 2" FT REPEAT 235..276 FT /note="ARM 3" FT REPEAT 277..318 FT /note="ARM 4" FT REPEAT 319..360 FT /note="ARM 5" FT REPEAT 361..389 FT /note="ARM 6" FT REPEAT 400..441 FT /note="ARM 7" FT REPEAT 442..484 FT /note="ARM 8" FT REPEAT 489..530 FT /note="ARM 9" FT REPEAT 531..571 FT /note="ARM 10" FT REPEAT 594..636 FT /note="ARM 11" FT REPEAT 637..666 FT /note="ARM 12" FT REGION 2..23 FT /note="Interaction with VCL" FT /evidence="ECO:0000250" FT REGION 34..57 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 156..178 FT /note="Interaction with BCL9" FT /evidence="ECO:0000269|PubMed:17052462" FT REGION 705..781 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 772..781 FT /note="Interaction with SCRIB" FT /evidence="ECO:0000250" FT COMPBIAS 34..48 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 23 FT /note="Phosphoserine; by GSK3-beta; alternate" FT /evidence="ECO:0000269|PubMed:12027456" FT MOD_RES 29 FT /note="Phosphoserine; by GSK3-beta" FT /evidence="ECO:0000269|PubMed:12027456" FT MOD_RES 33 FT /note="Phosphoserine; by GSK3-beta and HIPK2" FT /evidence="ECO:0000269|PubMed:20307497, FT ECO:0000269|PubMed:25169422" FT MOD_RES 37 FT /note="Phosphoserine; by GSK3-beta and HIPK2" FT /evidence="ECO:0000269|PubMed:20307497" FT MOD_RES 41 FT /note="Phosphothreonine; by GSK3-beta" FT /evidence="ECO:0000269|PubMed:12027456" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12051714" FT MOD_RES 49 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:24824780" FT MOD_RES 64 FT /note="Phosphotyrosine; by PTK6" FT /evidence="ECO:0000269|PubMed:20026641" FT MOD_RES 142 FT /note="Phosphotyrosine; by FYN and PTK6" FT /evidence="ECO:0000269|PubMed:12640114, FT ECO:0000269|PubMed:20026641" FT MOD_RES 191 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000269|PubMed:17009320, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 246 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000269|PubMed:17009320" FT MOD_RES 331 FT /note="Phosphotyrosine; by PTK6" FT /evidence="ECO:0000269|PubMed:20026641" FT MOD_RES 333 FT /note="Phosphotyrosine; by SRC and PTK6" FT /evidence="ECO:0000269|PubMed:22056988, FT ECO:0000305|PubMed:20026641" FT MOD_RES 552 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 556 FT /note="(Microbial infection) Phosphothreonine" FT /evidence="ECO:0000269|PubMed:31801859" FT MOD_RES 556 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18220336" FT MOD_RES 619 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:Q02248" FT MOD_RES 675 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231" FT CARBOHYD 23 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000269|PubMed:24342833" FT VARIANT 23 FT /note="S -> R (in hepatocellular carcinoma; no effect; FT dbSNP:rs1413975856)" FT /evidence="ECO:0000269|PubMed:10435629, FT ECO:0000269|PubMed:12027456" FT /id="VAR_017612" FT VARIANT 25..33 FT /note="Missing (in hepatocellular carcinoma)" FT /evidence="ECO:0000269|PubMed:10435629" FT /id="VAR_017613" FT VARIANT 32 FT /note="D -> A (in hepatocellular carcinoma; FT dbSNP:rs121913396)" FT /evidence="ECO:0000269|PubMed:10435629" FT /id="VAR_017614" FT VARIANT 32 FT /note="D -> G (in PTR and hepatocellular carcinoma; FT dbSNP:rs121913396)" FT /evidence="ECO:0000269|PubMed:10192393, FT ECO:0000269|PubMed:10435629" FT /id="VAR_017615" FT VARIANT 32 FT /note="D -> Y (in PTR, hepatoblastoma and hepatocellular FT carcinoma; dbSNP:rs28931588)" FT /evidence="ECO:0000269|PubMed:10192393, FT ECO:0000269|PubMed:10435629, ECO:0000269|PubMed:11703283, FT ECO:0000269|PubMed:9927029" FT /id="VAR_017616" FT VARIANT 33 FT /note="S -> F (in PTR, MDB and hepatocellular carcinoma; FT dbSNP:rs121913400)" FT /evidence="ECO:0000269|PubMed:10192393, FT ECO:0000269|PubMed:10435629, ECO:0000269|PubMed:10666372" FT /id="VAR_017617" FT VARIANT 33 FT /note="S -> L (in hepatocellular carcinoma)" FT /evidence="ECO:0000269|PubMed:10435629" FT /id="VAR_017618" FT VARIANT 33 FT /note="S -> Y (in colorectal cancer and PTR; constitutively FT active Wnt signaling pathway; enhances transactivation of FT target genes; dbSNP:rs121913400)" FT /evidence="ECO:0000269|PubMed:10192393, FT ECO:0000269|PubMed:12027456, ECO:0000269|PubMed:29374064, FT ECO:0000269|PubMed:9065402" FT /id="VAR_017619" FT VARIANT 34 FT /note="G -> E (in PTR; dbSNP:rs28931589)" FT /evidence="ECO:0000269|PubMed:10192393" FT /id="VAR_017620" FT VARIANT 34 FT /note="G -> R (in hepatocellular carcinoma; FT dbSNP:rs121913399)" FT /evidence="ECO:0000269|PubMed:10435629" FT /id="VAR_017621" FT VARIANT 34 FT /note="G -> V (in hepatoblastoma; dbSNP:rs28931589)" FT /evidence="ECO:0000269|PubMed:9927029" FT /id="VAR_017622" FT VARIANT 35 FT /note="I -> S (in hepatocellular carcinoma)" FT /evidence="ECO:0000269|PubMed:10435629" FT /id="VAR_017623" FT VARIANT 37..38 FT /note="SG -> W (in hepatocellular carcinoma)" FT /evidence="ECO:0000269|PubMed:10435629" FT /id="VAR_017628" FT VARIANT 37 FT /note="S -> A (in MDB and hepatocellular carcinoma; FT enhances transactivation of target genes; FT dbSNP:rs121913228)" FT /evidence="ECO:0000269|PubMed:10435629, FT ECO:0000269|PubMed:10666372, ECO:0000269|PubMed:12027456" FT /id="VAR_017624" FT VARIANT 37 FT /note="S -> C (in PTR, hepatoblastoma and ovarian cancer; FT dbSNP:rs121913403)" FT /evidence="ECO:0000269|PubMed:10192393, FT ECO:0000269|PubMed:10391090, ECO:0000269|PubMed:9927029" FT /id="VAR_017625" FT VARIANT 37 FT /note="S -> F (in PTR; dbSNP:rs121913403)" FT /evidence="ECO:0000269|PubMed:10192393" FT /id="VAR_017626" FT VARIANT 37 FT /note="S -> Y (in hepatocellular carcinoma; FT dbSNP:rs121913403)" FT /evidence="ECO:0000269|PubMed:10435629" FT /id="VAR_017627" FT VARIANT 41 FT /note="T -> A (in hepatoblastoma and hepatocellular FT carcinoma; also in a desmoid tumor; strongly reduces FT phosphorylation and degradation; abolishes phosphorylation FT on Ser-33 and Ser-37 and enhances transactivation of target FT genes; dbSNP:rs121913412)" FT /evidence="ECO:0000269|PubMed:10391090, FT ECO:0000269|PubMed:10398436, ECO:0000269|PubMed:10435629, FT ECO:0000269|PubMed:10655994, ECO:0000269|PubMed:12027456, FT ECO:0000269|PubMed:12051714, ECO:0000269|PubMed:9927029" FT /id="VAR_017629" FT VARIANT 41 FT /note="T -> I (in PTR, hepatocellular carcinoma and ovarian FT cancer; dbSNP:rs121913413)" FT /evidence="ECO:0000269|PubMed:10192393, FT ECO:0000269|PubMed:10391090, ECO:0000269|PubMed:10435629" FT /id="VAR_017630" FT VARIANT 45 FT /note="S -> F (in hepatocellular carcinoma; FT dbSNP:rs121913409)" FT /evidence="ECO:0000269|PubMed:10435629" FT /id="VAR_017631" FT VARIANT 45 FT /note="S -> P (in hepatocellular carcinoma; FT dbSNP:rs121913407)" FT /evidence="ECO:0000269|PubMed:10435629" FT /id="VAR_017632" FT VARIANT 45 FT /note="Missing (in colorectal cancer)" FT /evidence="ECO:0000269|PubMed:9065402" FT /id="VAR_055430" FT VARIANT 388 FT /note="L -> P (in NEDSDV)" FT /evidence="ECO:0000269|PubMed:25326669" FT /id="VAR_072282" FT VARIANT 558..781 FT /note="Missing (in NEDSDV; the patient also manifest FT features of exudative vitreoretinopathy)" FT /evidence="ECO:0000269|PubMed:28514307" FT /id="VAR_079199" FT VARIANT 688 FT /note="M -> V (in dbSNP:rs4135384)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_018954" FT VARIANT 710 FT /note="R -> C (in EVR7; uncertain significance; FT dbSNP:rs748653573)" FT /evidence="ECO:0000269|PubMed:28575650" FT /id="VAR_079200" FT MUTAGEN 29 FT /note="S->F: No effect." FT /evidence="ECO:0000269|PubMed:12027456" FT MUTAGEN 64 FT /note="Y->F: Abolishes phosphorylation by PTK6." FT /evidence="ECO:0000269|PubMed:20026641" FT MUTAGEN 142 FT /note="Y->E: No effect on interaction with BCL9 and BCL9L." FT /evidence="ECO:0000269|PubMed:17052462" FT MUTAGEN 156 FT /note="L->A: Abolishes interaction with BCL9 but no effect FT on interaction with CDH3; when associated with A-159." FT /evidence="ECO:0000269|PubMed:17052462" FT MUTAGEN 159 FT /note="L->A: No effect on interaction with BCL9 and CDH3. FT Abolishes interaction with BCL9 but no effect on FT interaction with CDH3; when associated with A-156." FT /evidence="ECO:0000269|PubMed:17052462" FT MUTAGEN 178 FT /note="L->A: No effect on interaction with BCL9 and CDH3." FT /evidence="ECO:0000269|PubMed:17052462" FT MUTAGEN 253 FT /note="F->A: Abolishes or strongly reduces AXIN2 binding." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 260 FT /note="H->A: Abolishes or strongly reduces AXIN1 and AXIN2 FT binding. Strongly reduces phosphorylation and degradation; FT when associated with A-386 and A-383." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 292 FT /note="K->A: Abolishes or strongly reduces AXIN1 and AXIN2 FT binding." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 312 FT /note="K->E: Abolishes TCF7L2 binding." FT /evidence="ECO:0000269|PubMed:11713475" FT MUTAGEN 333 FT /note="Y->F: Abolished phosphorylation by SRC and FT interaction with isoform M2 of PKM (PKM2)." FT /evidence="ECO:0000269|PubMed:22056988" FT MUTAGEN 345 FT /note="K->A: Abolishes APC binding." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 383 FT /note="W->A: Abolishes APC binding. Strongly reduces FT phosphorylation and degradation; when associated with A-260 FT and A-386." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 386 FT /note="R->A: Strongly reduces APC binding. Strongly reduces FT phosphorylation and degradation; when associated with A-260 FT and A-383." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 426 FT /note="N->A: Abolishes TCF7L2 and LEF1 binding." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 435 FT /note="K->A: Strongly reduces or abolishes LEF1 binding." FT /evidence="ECO:0000269|PubMed:10966653, FT ECO:0000269|PubMed:11713475" FT MUTAGEN 435 FT /note="K->E: Abolishes TCF7L2 binding." FT /evidence="ECO:0000269|PubMed:10966653, FT ECO:0000269|PubMed:11713475" FT MUTAGEN 469 FT /note="R->A: Abolishes TCF7L2 binding, and strongly reduces FT or abolishes LEF1 binding." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 470 FT /note="H->A: Abolishes TCF7L2 binding, and strongly reduces FT or abolishes LEF1 binding." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 508 FT /note="K->A: Abolishes TCF7L2 and LEF1 binding." FT /evidence="ECO:0000269|PubMed:10966653" FT MUTAGEN 660 FT /note="F->A: Abolishes CTNNBIP1 binding; when associated FT with A-661." FT /evidence="ECO:0000269|PubMed:12408824" FT MUTAGEN 661 FT /note="R->A: Abolishes CTNNBIP1 binding; when associated FT with A-660." FT /evidence="ECO:0000269|PubMed:12408824" FT HELIX 145..160 FT /evidence="ECO:0007829|PDB:7AFW" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:7UWO" FT HELIX 165..179 FT /evidence="ECO:0007829|PDB:7AFW" FT HELIX 182..189 FT /evidence="ECO:0007829|PDB:7AFW" FT HELIX 192..204 FT /evidence="ECO:0007829|PDB:7AFW" FT HELIX 208..221 FT /evidence="ECO:0007829|PDB:7AFW" FT HELIX 225..233 FT /evidence="ECO:0007829|PDB:7AFW" FT HELIX 236..243 FT /evidence="ECO:0007829|PDB:7AFW" FT HELIX 249..265 FT /evidence="ECO:0007829|PDB:7AFW" FT HELIX 269..275 FT /evidence="ECO:0007829|PDB:7AFW" FT HELIX 278..284 FT /evidence="ECO:0007829|PDB:7AFW" FT HELIX 285..287 FT /evidence="ECO:0007829|PDB:7AFW" FT HELIX 291..303 FT /evidence="ECO:0007829|PDB:7AFW" FT HELIX 309..317 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 320..330 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 334..347 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 353..359 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 362..367 FT /evidence="ECO:0007829|PDB:1JDH" FT TURN 368..371 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 375..389 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 399..408 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 414..427 FT /evidence="ECO:0007829|PDB:1JDH" FT TURN 428..430 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 432..440 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 443..454 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 458..471 FT /evidence="ECO:0007829|PDB:1JDH" FT STRAND 473..475 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 478..487 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 491..496 FT /evidence="ECO:0007829|PDB:1JDH" FT STRAND 499..501 FT /evidence="ECO:0007829|PDB:4DJS" FT HELIX 504..517 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 521..523 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 524..529 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 532..547 FT /evidence="ECO:0007829|PDB:1JDH" FT STRAND 550..552 FT /evidence="ECO:0007829|PDB:1QZ7" FT STRAND 554..557 FT /evidence="ECO:0007829|PDB:1QZ7" FT STRAND 561..563 FT /evidence="ECO:0007829|PDB:1T08" FT HELIX 566..580 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 584..592 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 596..601 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 602..604 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 608..621 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 625..633 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 637..642 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 643..645 FT /evidence="ECO:0007829|PDB:1JDH" FT HELIX 649..662 FT /evidence="ECO:0007829|PDB:1JDH" FT TURN 663..665 FT /evidence="ECO:0007829|PDB:2Z6H" FT HELIX 668..682 FT /evidence="ECO:0007829|PDB:2Z6H" FT HELIX 688..690 FT /evidence="ECO:0007829|PDB:2Z6H" FT STRAND 778..780 FT /evidence="ECO:0007829|PDB:3DIW" SQ SEQUENCE 781 AA; 85497 MW; CB78F165A3EEF86E CRC64; MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTS QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDAAHPT NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC SSNKPAIVEA GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL VRAHQDTQRR TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI GAQGEPLGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L //