CTNB1_HUMAN
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 03-AUG-2022, entry version 255.
DE RecName: Full=Catenin beta-1;
DE AltName: Full=Beta-catenin;
GN Name=CTNNB1; Synonyms=CTNNB; 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 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 [30]
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 [31]
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 [32]
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 [33]
RP INTERACTION WITH SLC9A3R1.
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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
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 [52]
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 [53]
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 [54]
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 [55]
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 [56]
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 [57]
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 [58]
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 [59]
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 [60]
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 [61]
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 [62]
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 [63]
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 [64]
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 [65]
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 [66]
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 [67]
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 [68]
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 [69]
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 [70]
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 [71]
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 [72]
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 [73]
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 [74]
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 [75]
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 [76]
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 [77]
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 [78]
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 [79]
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 [80]
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 [81]
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 [82]
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 [83]
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 [84]
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 [85]
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 [86]
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 [87]
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 [88]
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 [89]
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 [90]
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 [91]
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 [92]
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 [93]
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 [94]
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 [95]
RP VARIANT HEPATOBLASTOMA ALA-41.
RX PubMed=10398436;
RX DOI=10.1002/(sici)1098-2264(199908)25:4<399::aid-gcc14>3.0.co;2-x;
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 [96]
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 [97]
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 [98]
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 [99]
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 [100]
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 [101]
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 [102]
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).
CC {ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:17524503,
CC ECO:0000269|PubMed:18077326, ECO:0000269|PubMed:18086858,
CC ECO:0000269|PubMed:18957423, ECO:0000269|PubMed:21262353,
CC ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22647378,
CC 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 SLC9A3R1. Interacts
CC with GLIS2 and MUC1. Interacts with SLC30A9. Interacts with XIRP1.
CC Interacts 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). {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:12077367,
CC ECO:0000269|PubMed:12297051, ECO:0000269|PubMed:12370829,
CC ECO:0000269|PubMed:12408824, ECO:0000269|PubMed:12420223,
CC ECO:0000269|PubMed:12501215, ECO:0000269|PubMed:12712206,
CC ECO:0000269|PubMed:12830000, ECO:0000269|PubMed:14595118,
CC ECO:0000269|PubMed:15003504, ECO:0000269|PubMed:16424001,
CC ECO:0000269|PubMed:16858403, ECO:0000269|PubMed:17009320,
CC ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:17052462,
CC ECO:0000269|PubMed:17289029, ECO:0000269|PubMed:17524503,
CC ECO:0000269|PubMed:18077326, ECO:0000269|PubMed:18086858,
CC ECO:0000269|PubMed:18378692, ECO:0000269|PubMed:18819930,
CC ECO:0000269|PubMed:19433865, ECO:0000269|PubMed:19693690,
CC ECO:0000269|PubMed:19816403, ECO:0000269|PubMed:19996314,
CC ECO:0000269|PubMed:20026641, ECO:0000269|PubMed:20164195,
CC ECO:0000269|PubMed:21132015, ECO:0000269|PubMed:21247902,
CC ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:21623382,
CC ECO:0000269|PubMed:22056988, ECO:0000269|PubMed:22155184,
CC ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:22699938,
CC ECO:0000269|PubMed:25169422, ECO:0000269|PubMed:25183871,
CC ECO:0000269|PubMed:25266658, ECO:0000269|PubMed:25807484,
CC ECO:0000269|PubMed:28051089, ECO:0000269|PubMed:28829046,
CC ECO:0000269|PubMed:29367600, ECO:0000269|PubMed:29374064,
CC ECO:0000269|PubMed:29432739, ECO:0000269|PubMed:29739711,
CC ECO:0000269|PubMed:31073040, ECO:0000269|PubMed:7982500,
CC 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; 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=14; 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; 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; Q2LD37: KIAA1109; NbExp=2; IntAct=EBI-491549, EBI-2683809;
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; P18012: ipaC; Xeno; NbExp=4; IntAct=EBI-491549, EBI-491541;
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; 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}. Nucleus {ECO:0000269|PubMed:24342833,
CC ECO:0000269|PubMed:25183871, ECO:0000269|PubMed:28829046,
CC ECO:0000269|PubMed:29367600, ECO:0000269|PubMed:29739711}. 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:24342833}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole.
CC Synapse {ECO:0000250|UniProtKB:Q02248}. Cytoplasm, cytoskeleton, cilium
CC basal body {ECO:0000250|UniProtKB:Q02248}. Note=Colocalized with
CC RAPGEF2 and TJP1 at cell-cell contacts (By similarity). Cytoplasmic
CC when it is unstabilized (high level of phosphorylation) or bound to
CC CDH1. Translocates to the nucleus when it is stabilized (low level of
CC phosphorylation). Interaction with GLIS2 and MUC1 promotes nuclear
CC translocation. Interaction with EMD inhibits nuclear localization. The
CC majority of beta-catenin is localized to the cell membrane. In
CC interphase, colocalizes with CROCC between CEP250 puncta at the
CC proximal end of centrioles, and this localization is dependent on CROCC
CC and CEP250. In mitosis, when NEK2 activity increases, it localizes to
CC centrosomes at spindle poles independent of CROCC. Colocalizes with
CC CDK5 in the cell-cell contacts and plasma membrane of undifferentiated
CC and differentiated neuroblastoma cells. Interaction with FAM53B
CC promotes translocation to the nucleus (PubMed:25183871).
CC {ECO:0000250|UniProtKB:B6V8E6, 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 stabilizion 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 -!- 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="http://atlasgeneticsoncology.org/Genes/CTNNB1ID71.html";
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 ---------------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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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 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 AlphaFoldDB; P35222; -.
DR SMR; P35222; -.
DR BioGRID; 107880; 850.
DR ComplexPortal; CPX-316; beta1-catenin - LEF1 complex.
DR CORUM; P35222; -.
DR DIP; DIP-122N; -.
DR IntAct; P35222; 262.
DR MINT; P35222; -.
DR STRING; 9606.ENSP00000344456; -.
DR BindingDB; P35222; -.
DR ChEMBL; CHEMBL5866; -.
DR DrugBank; DB03904; Urea.
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 EPD; P35222; -.
DR jPOST; P35222; -.
DR MassIVE; P35222; -.
DR MaxQB; P35222; -.
DR PaxDb; P35222; -.
DR PeptideAtlas; P35222; -.
DR PRIDE; P35222; -.
DR ABCD; P35222; 7 sequenced antibodies.
DR Antibodypedia; 3432; 5066 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 CTD; 1499; -.
DR DisGeNET; 1499; -.
DR GeneCards; 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; 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; 321213at2759; -.
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 SignaLink; P35222; -.
DR SIGNOR; P35222; -.
DR BioGRID-ORCS; 1499; 97 hits in 1092 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 202 other tissues.
DR ExpressionAtlas; P35222; baseline and differential.
DR Genevisible; P35222; HS.
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:BHF-UCL.
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:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:ARUK-UCL.
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:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IPI:UniProtKB.
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:UniProtKB.
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:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:UniProtKB.
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:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
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:1904954; P:canonical Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; IC:ParkinsonsUK-UCL.
DR GO; GO:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; TAS:ARUK-UCL.
DR GO; GO:0044339; P:canonical Wnt signaling pathway involved in osteoblast differentiation; IMP:ARUK-UCL.
DR GO; GO:0061324; P:canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation; ISS:BHF-UCL.
DR GO; GO:0044334; P:canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
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:0000904; P:cell morphogenesis involved in differentiation; 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: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:0007249; P:I-kappaB kinase/NF-kappaB signaling; 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:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
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: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:1903204; P:negative regulation of oxidative stress-induced neuron death; 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:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
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:0030316; P:osteoclast differentiation; IEA:Ensembl.
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; IC:ComplexPortal.
DR GO; GO:1904798; P:positive regulation of core promoter binding; IEA:Ensembl.
DR GO; GO:2000017; P:positive regulation of determination of dorsal identity; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:ParkinsonsUK-UCL.
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; IGI:MGI.
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:0051571; P:positive regulation of histone H3-K4 methylation; ISS:ARUK-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
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: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:0051973; P:positive regulation of telomerase activity; ISS:ARUK-UCL.
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 from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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: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: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 DisProt; DP01119; -.
DR Gene3D; 1.25.10.10; -; 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; PTHR45976; 1.
DR Pfam; PF00514; Arm; 4.
DR PRINTS; PR01869; BCATNINFAMLY.
DR SMART; SM00185; ARM; 12.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 9.
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="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; unknown pathological 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 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
