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Catenin beta-1 (Beta-catenin)

 CTNB1_HUMAN             Reviewed;         781 AA.
P35222; A8K1L7; Q8NEW9; Q8NI94; Q9H391;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
12-AUG-2020, entry version 246.
RecName: Full=Catenin beta-1;
AltName: Full=Beta-catenin;
Name=CTNNB1; Synonyms=CTNNB; ORFNames=OK/SW-cl.35, PRO2286;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=7806582; DOI=10.1083/jcb.127.6.2061;
Huelsken J., Birchmeier W., Behrens J.;
"E-cadherin and APC compete for the interaction with beta-catenin and the
cytoskeleton.";
J. Cell Biol. 127:2061-2069(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W.,
Gao F., Liu M., He F.;
"Functional prediction of the coding sequences of 75 new genes deduced by
analysis of cDNA clones from human fetal liver.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-688.
NIEHS SNPs program;
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-312.
PubMed=12019147;
Kim J.-S., Crooks H., Dracheva T., Nishanian T.G., Singh B., Jen J.,
Waldman T.;
"Oncogenic beta-catenin is required for bone morphogenetic protein 4
expression in human cancer cells.";
Cancer Res. 62:2744-2748(2002).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 258-781.
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-reactive
CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[10]
IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
Butz S., Kemler R.;
"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
adhesion.";
FEBS Lett. 355:195-200(1994).
[11]
CHROMOSOMAL TRANSLOCATION WITH PLAG1.
PubMed=9020842; DOI=10.1038/ng0297-170;
Kas K., Voz M.L., Roeijer E., Astroem A.-K., Meyen E., Stenman G.,
Van de Ven W.J.M.;
"Promoter swapping between the genes for a novel zinc finger protein and
beta-catenin in pleiomorphic adenomas with t(3;8)(p21;q12)
translocations.";
Nat. Genet. 15:170-174(1997).
[12]
CHROMOSOMAL TRANSLOCATION WITH PLAG1.
PubMed=10029085;
Astroem A.-K., Voz M.L., Kas K., Roeijer E., Wedell B., Mandahl N.,
Van de Ven W., Mark J., Stenman G.;
"Conserved mechanism of PLAG1 activation in salivary gland tumors with and
without chromosome 8q12 abnormalities: identification of SII as a new
fusion partner gene.";
Cancer Res. 59:918-923(1999).
[13]
STIMULATION OF TYROSINE PHOSPHORYLATION BY EGF, AND DEPHOSPHORYLATION BY
PTPRF.
PubMed=10187801; DOI=10.1074/jbc.274.15.10173;
Mueller T., Choidas A., Reichmann E., Ullrich A.;
"Phosphorylation and free pool of beta-catenin are regulated by tyrosine
kinases and tyrosine phosphatases during epithelial cell migration.";
J. Biol. Chem. 274:10173-10183(1999).
[14]
INTERACTION WITH LEF1; APC; AXIN1; AXIN2 AND TCF7L2, PHOSPHORYLATION BY
GSK3B, AND MUTAGENESIS OF PHE-253; HIS-260; LYS-292; LYS-345; TRP-383;
ARG-386; ASN-426; LYS-435; ARG-469; HIS-470 AND LYS-508.
PubMed=10966653; DOI=10.1038/79039;
von Kries J.P., Winbeck G., Asbrand C., Schwarz-Romond T., Sochnikova N.,
Dell'Oro A., Behrens J., Birchmeier W.;
"Hot spots in beta-catenin for interactions with LEF-1, conductin and
APC.";
Nat. Struct. Biol. 7:800-807(2000).
[15]
TISSUE SPECIFICITY, AND VARIANT PTR TYR-32.
PubMed=11703283; DOI=10.1046/j.1365-2133.2001.04455.x;
Moreno-Bueno G., Gamallo C., Perez-Gallego L., Contreras F., Palacios J.;
"Beta-catenin expression in pilomatrixomas. Relationship with beta-catenin
gene mutations and comparison with beta-catenin expression in normal hair
follicles.";
Br. J. Dermatol. 145:576-581(2001).
[16]
INTERACTION WITH LEF1, AND INHIBITION BY CTNNBIP1 BINDING.
PubMed=11751639; DOI=10.1101/gad.946501;
Tutter A.V., Fryer C.J., Jones K.A.;
"Chromatin-specific regulation of LEF-1-beta-catenin transcription
activation and inhibition in vitro.";
Genes Dev. 15:3342-3354(2001).
[17]
PHOSPHORYLATION AT TYR-86 AND TYR-654, INTERACTION WITH TBP, AND
MUTAGENESIS OF TYR-654.
PubMed=11279024; DOI=10.1074/jbc.m100194200;
Piedra J., Martinez D., Castano J., Miravet S., Dunach M.,
de Herreros A.G.;
"Regulation of beta-catenin structure and activity by tyrosine
phosphorylation.";
J. Biol. Chem. 276:20436-20443(2001).
[18]
INTERACTION WITH CTNNA3.
PubMed=11590244;
Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J., Colpaert C.,
Bruyneel E., Mareel M., van Roy F.;
"AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein
mediating strong cell-cell adhesion.";
J. Cell Sci. 114:3177-3188(2001).
[19]
INTERACTION WITH SIAH1, AND UBIQUITINATION.
PubMed=11389839; DOI=10.1016/s1097-2765(01)00242-8;
Matsuzawa S., Reed J.C.;
"Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin
degradation linked to p53 responses.";
Mol. Cell 7:915-926(2001).
[20]
INTERACTION WITH SIAH1, AND UBIQUITINATION.
PubMed=11389840; DOI=10.1016/s1097-2765(01)00241-6;
Liu J., Stevens J., Rote C.A., Yost H.J., Hu Y., Neufeld K.L., White R.L.,
Matsunami N.;
"Siah-1 mediates a novel beta-catenin degradation pathway linking p53 to
the adenomatous polyposis coli protein.";
Mol. Cell 7:927-936(2001).
[21]
INVOLVEMENT IN MESOM.
PubMed=11464291; DOI=10.1038/sj.onc.1204557;
Shigemitsu K., Sekido Y., Usami N., Mori S., Sato M., Horio Y.,
Hasegawa Y., Bader S.A., Gazdar A.F., Minna J.D., Hida T., Yoshioka H.,
Imaizumi M., Ueda Y., Takahashi M., Shimokata K.;
"Genetic alteration of the beta-catenin gene (CTNNB1) in human lung cancer
and malignant mesothelioma and identification of a new 3p21.3 homozygous
deletion.";
Oncogene 20:4249-4257(2001).
[22]
INTERACTION WITH PTPRU.
PubMed=12501215; DOI=10.1021/bi026095u;
Yan H.-X., He Y.-Q., Dong H., Zhang P., Zeng J.-Z., Cao H.-F., Wu M.-C.,
Wang H.-Y.;
"Physical and functional interaction between receptor-like protein tyrosine
phosphatase PCP-2 and beta-catenin.";
Biochemistry 41:15854-15860(2002).
[23]
PHOSPHORYLATION AT SER-45, CHARACTERIZATION OF VARIANT HEPATOCELLULAR
CARCINOMA ALA-41, CHARACTERIZATION OF VARIANT DESMOID TUMOR ALA-41, AND
CHARACTERIZATION OF VARIANT HEPATOBLASTOMA ALA-41.
PubMed=12051714; DOI=10.1016/s0006-291x(02)00485-0;
Hagen T., Vidal-Puig A.;
"Characterisation of the phosphorylation of beta-catenin at the GSK-3
priming site Ser45.";
Biochem. Biophys. Res. Commun. 294:324-328(2002).
[24]
INTERACTION WITH CXADR.
PubMed=12297051; DOI=10.1016/s0092-8674(02)00912-1;
Walters R.W., Freimuth P., Moninger T.O., Ganske I., Zabner J., Welsh M.J.;
"Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing
virus escape.";
Cell 110:789-799(2002).
[25]
PHOSPHORYLATION AT SER-23 AND SER-29 BY GSK3B, PHOSPHORYLATION AT THR-41,
MUTAGENESIS OF SER-29, CHARACTERIZATION OF VARIANTS HEPATOCELLULAR
CARCINOMA ARG-23; ALA-37 AND ALA-41, CHARACTERIZATION OF VARIANT PTR
TYR-33, CHARACTERIZATION OF VARIANT MDB ALA-37, CHARACTERIZATION OF VARIANT
DESMOID TUMOR ALA-41, AND CHARACTERIZATION OF VARIANT HEPATOBLASTOMA
ALA-41.
PubMed=12027456; DOI=10.1006/excr.2002.5520;
van Noort M., van de Wetering M., Clevers H.;
"Identification of two novel regulated serines in the N-terminus of beta-
catenin.";
Exp. Cell Res. 276:264-272(2002).
[26]
WNT SIGNALING MODULATES PHOSPHORYLATION.
PubMed=11834740; DOI=10.1074/jbc.m111635200;
van Noort M., Meeldijk J., van der Zee R., Destree O., Clevers H.;
"Wnt signaling controls the phosphorylation status of beta-catenin.";
J. Biol. Chem. 277:17901-17905(2002).
[27]
PHOSPHORYLATION, AND INTERACTION OF PHOSPHORYLATED CTNNB1 WITH BTRC.
PubMed=12077367;
Sadot E., Conacci-Sorrell M., Zhurinsky J., Shnizer D., Lando Z.,
Zharhary D., Kam Z., Ben-Ze'ev A., Geiger B.;
"Regulation of S33/S37 phosphorylated beta-catenin in normal and
transformed cells.";
J. Cell Sci. 115:2771-2780(2002).
[28]
INTERACTION WITH PTPRJ.
PubMed=12370829; DOI=10.1038/sj.onc.1205858;
Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.;
"The transmembrane receptor protein tyrosine phosphatase DEP1 interacts
with p120(ctn).";
Oncogene 21:7067-7076(2002).
[29]
INTERACTION WITH PCDH11Y.
PubMed=12420223; DOI=10.1038/sj.onc.1205991;
Chen M.-W., Vacherot F., De La Taille A., Gil-Diez-De-Medina S., Shen R.,
Friedman R.A., Burchardt M., Chopin D.K., Buttyan R.;
"The emergence of protocadherin-PC expression during the acquisition of
apoptosis-resistance by prostate cancer cells.";
Oncogene 21:7861-7871(2002).
[30]
INTERACTION WITH SLC9A3R1.
PubMed=12830000; DOI=10.1053/jhep.2003.50270;
Shibata T., Chuma M., Kokubu A., Sakamoto M., Hirohashi S.;
"EBP50, a beta-catenin-associating protein, enhances Wnt signaling and is
over-expressed in hepatocellular carcinoma.";
Hepatology 38:178-186(2003).
[31]
REVIEW.
PubMed=10679188; DOI=10.1006/bbrc.1999.1860;
Kikuchi A.;
"Regulation of beta-catenin signaling in the Wnt pathway.";
Biochem. Biophys. Res. Commun. 268:243-248(2000).
[32]
PHOSPHORYLATION AT TYR-142 BY FYN.
PubMed=12640114; DOI=10.1128/mcb.23.7.2287-2297.2003;
Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N.,
Garcia de Herreros A., Dunach M.;
"p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin
Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction.";
Mol. Cell. Biol. 23:2287-2297(2003).
[33]
INTERACTION WITH CBY1.
PubMed=12712206; DOI=10.1038/nature01570;
Takemaru K., Yamaguchi S., Lee Y.S., Zhang Y., Carthew R.W., Moon R.T.;
"Chibby, a nuclear beta-catenin-associated antagonist of the Wnt/Wingless
pathway.";
Nature 422:905-909(2003).
[34]
INTERACTION WITH AJAP1.
TISSUE=Brain;
PubMed=14595118; DOI=10.1091/mbc.e03-05-0281;
Bharti S., Handrow-Metzmacher H., Zickenheiner S., Zeitvogel A.,
Baumann R., Starzinski-Powitz A.;
"Novel membrane protein shrew-1 targets to cadherin-mediated junctions in
polarized epithelial cells.";
Mol. Biol. Cell 15:397-406(2004).
[35]
INTERACTION WITH CBY1, AND SUBCELLULAR LOCATION.
PubMed=16424001; DOI=10.1158/0008-5472.can-05-3124;
Jung Y., Bang S., Choi K., Kim E., Kim Y., Kim J., Park J., Koo H.,
Moon R.T., Song K., Lee I.;
"TC1 (C8orf4) enhances the Wnt/beta-catenin pathway by relieving
antagonistic activity of Chibby.";
Cancer Res. 66:723-728(2006).
[36]
SUBCELLULAR LOCATION, AND INTERACTION WITH NANOS1.
PubMed=17047063; DOI=10.1158/0008-5472.can-05-3096;
Strumane K., Bonnomet A., Stove C., Vandenbroucke R., Nawrocki-Raby B.,
Bruyneel E., Mareel M., Birembaut P., Berx G., van Roy F.;
"E-cadherin regulates human Nanos1, which interacts with p120ctn and
induces tumor cell migration and invasion.";
Cancer Res. 66:10007-10015(2006).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[38]
SUBCELLULAR LOCATION, AND INTERACTION WITH EMD.
PubMed=16858403; DOI=10.1038/sj.emboj.7601230;
Markiewicz E., Tilgner K., Barker N., van de Wetering M., Clevers H.,
Dorobek M., Hausmanowa-Petrusewicz I., Ramaekers F.C.S., Broers J.L.V.,
Blankesteijn W.M., Salpingidou G., Wilson R.G., Ellis J.A., Hutchison C.J.;
"The inner nuclear membrane protein emerin regulates beta-catenin activity
by restricting its accumulation in the nucleus.";
EMBO J. 25:3275-3285(2006).
[39]
INTERACTION WITH MUC1, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=17524503; DOI=10.1016/j.bbamcr.2007.04.009;
Lillehoj E.P., Lu W., Kiser T., Goldblum S.E., Kim K.C.;
"MUC1 inhibits cell proliferation by a beta-catenin-dependent mechanism.";
Biochim. Biophys. Acta 1773:1028-1038(2007).
[40]
INTERACTION WITH GLIS2, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=17289029; DOI=10.1016/j.febslet.2007.01.058;
Kim Y.-S., Kang H.S., Jetten A.M.;
"The Kruppel-like zinc finger protein Glis2 functions as a negative
modulator of the Wnt/beta-catenin signaling pathway.";
FEBS Lett. 581:858-864(2007).
[41]
PHOSPHORYLATION AT SER-191 AND SER-246, INTERACTION WITH CDK5, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=17009320; DOI=10.1002/jcb.21041;
Munoz J.P., Huichalaf C.H., Orellana D., Maccioni R.B.;
"cdk5 modulates beta- and delta-catenin/Pin1 interactions in neuronal
cells.";
J. Cell. Biochem. 100:738-749(2007).
[42]
INTERACTION WITH FHIT, IDENTIFICATION IN A COMPLEX WITH LEF1, AND FUNCTION.
PubMed=18077326; DOI=10.1073/pnas.0703664105;
Weiske J., Albring K.F., Huber O.;
"The tumor suppressor Fhit acts as a repressor of beta-catenin
transcriptional activity.";
Proc. Natl. Acad. Sci. U.S.A. 104:20344-20349(2007).
[43]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH NEK2.
PubMed=18086858; DOI=10.1101/gad.1596308;
Bahmanyar S., Kaplan D.D., Deluca J.G., Giddings T.H. Jr., O'Toole E.T.,
Winey M., Salmon E.D., Casey P.J., Nelson W.J., Barth A.I.;
"beta-Catenin is a Nek2 substrate involved in centrosome separation.";
Genes Dev. 22:91-105(2008).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-556 AND SER-675, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[45]
INTERACTION WITH SOX7.
PubMed=18819930; DOI=10.1158/1541-7786.mcr-07-2175;
Guo L., Zhong D., Lau S., Liu X., Dong X.Y., Sun X., Yang V.W.,
Vertino P.M., Moreno C.S., Varma V., Dong J.T., Zhou W.;
"Sox7 Is an independent checkpoint for beta-catenin function in prostate
and colon epithelial cells.";
Mol. Cancer Res. 6:1421-1430(2008).
[46]
INTERACTION WITH CHD8.
PubMed=18378692; DOI=10.1128/mcb.00322-08;
Thompson B.A., Tremblay V., Lin G., Bochar D.A.;
"CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-
catenin target genes.";
Mol. Cell. Biol. 28:3894-3904(2008).
[47]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[48]
INTERACTION WITH TCF7L2 AND TNIK.
PubMed=19816403; DOI=10.1038/emboj.2009.285;
Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S.,
Heck A.J., Clevers H.;
"The kinase TNIK is an essential activator of Wnt target genes.";
EMBO J. 28:3329-3340(2009).
[49]
FUNCTION.
PubMed=18957423; DOI=10.1074/jbc.m805612200;
Li H., Ray G., Yoo B.H., Erdogan M., Rosen K.V.;
"Down-regulation of death-associated protein kinase-2 is required for beta-
catenin-induced anoikis resistance of malignant epithelial cells.";
J. Biol. Chem. 284:2012-2022(2009).
[50]
INTERACTION WITH RUVBL2; APPL2; APPL1; HDAC1 AND HDAC2.
PubMed=19433865; DOI=10.1074/jbc.m109.007237;
Rashid S., Pilecka I., Torun A., Olchowik M., Bielinska B., Miaczynska M.;
"Endosomal adaptor proteins APPL1 and APPL2 are novel activators of beta-
catenin/TCF-mediated transcription.";
J. Biol. Chem. 284:18115-18128(2009).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[52]
PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2, AND UBIQUITINATION.
PubMed=20307497; DOI=10.1016/j.bbrc.2010.03.099;
Kim E.-A., Kim J.E., Sung K.S., Choi D.W., Lee B.J., Choi C.Y.;
"Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-catenin for
phosphorylation and proteasomal degradation.";
Biochem. Biophys. Res. Commun. 394:966-971(2010).
[53]
INTERACTION WITH SESTD1.
PubMed=20164195; DOI=10.1074/jbc.m109.068304;
Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C.;
"The phospholipid-binding protein SESTD1 is a novel regulator of the
transient receptor potential channels TRPC4 and TRPC5.";
J. Biol. Chem. 285:12426-12434(2010).
[54]
INTERACTION WITH TRPC4.
PubMed=19996314; DOI=10.1074/jbc.m109.060301;
Graziani A., Poteser M., Heupel W.M., Schleifer H., Krenn M.,
Drenckhahn D., Romanin C., Baumgartner W., Groschner K.;
"Cell-cell contact formation governs Ca2+ signaling by TRPC4 in the
vascular endothelium: evidence for a regulatory TRPC4-beta-catenin
interaction.";
J. Biol. Chem. 285:4213-4223(2010).
[55]
INTERACTION WITH CDK5.
PubMed=19693690; DOI=10.1007/s11033-009-9752-7;
Li Q., Liu X., Zhang M., Ye G., Qiao Q., Ling Y., Wu Y., Zhang Y., Yu L.;
"Characterization of a novel human CDK5 splicing variant that inhibits
Wnt/beta-catenin signaling.";
Mol. Biol. Rep. 37:2415-2421(2010).
[56]
PHOSPHORYLATION AT TYR-64; TYR-142; TYR-331 AND TYR-333, INTERACTION WITH
PTK6, AND MUTAGENESIS OF TYR-64.
PubMed=20026641; DOI=10.1242/jcs.053264;
Palka-Hamblin H.L., Gierut J.J., Bie W., Brauer P.M., Zheng Y., Asara J.M.,
Tyner A.L.;
"Identification of beta-catenin as a target of the intracellular tyrosine
kinase PTK6.";
J. Cell Sci. 123:236-245(2010).
[57]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[58]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[59]
FUNCTION IN INSULIN INTERNALIZATION, SUBCELLULAR LOCATION, INTERACTION WITH
CDK2, AND PHOSPHORYLATION BY CDK2.
PubMed=21262353; DOI=10.1016/j.cellsig.2011.01.019;
Fiset A., Xu E., Bergeron S., Marette A., Pelletier G., Siminovitch K.A.,
Olivier M., Beauchemin N., Faure R.L.;
"Compartmentalized CDK2 is connected with SHP-1 and beta-catenin and
regulates insulin internalization.";
Cell. Signal. 23:911-919(2011).
[60]
INTERACTION WITH PKT7.
PubMed=21132015; DOI=10.1038/embor.2010.185;
Puppo F., Thome V., Lhoumeau A.-C., Cibois M., Gangar A., Lembo F.,
Belotti E., Marchetto S., Lecine P., Prebet T., Sebbagh M., Shin W.-S.,
Lee S.-T., Kodjabachian L., Borg J.-P.;
"Protein tyrosine kinase 7 has a conserved role in Wnt/beta-catenin
canonical signalling.";
EMBO Rep. 12:43-49(2011).
[61]
INTERACTION WITH NDRG2.
PubMed=21247902; DOI=10.1074/jbc.m110.170803;
Hwang J., Kim Y., Kang H.B., Jaroszewski L., Deacon A.M., Lee H.,
Choi W.C., Kim K.J., Kim C.H., Kang B.S., Lee J.O., Oh T.K., Kim J.W.,
Wilson I.A., Kim M.H.;
"Crystal structure of the human N-Myc downstream-regulated gene 2 protein
provides insight into its role as a tumor suppressor.";
J. Biol. Chem. 286:12450-12460(2011).
[62]
INTERACTION WITH AHI1.
PubMed=21623382; DOI=10.1038/nm.2380;
Lancaster M.A., Gopal D.J., Kim J., Saleem S.N., Silhavy J.L., Louie C.M.,
Thacker B.E., Williams Y., Zaki M.S., Gleeson J.G.;
"Defective Wnt-dependent cerebellar midline fusion in a mouse model of
Joubert syndrome.";
Nat. Med. 17:726-731(2011).
[63]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-552, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[64]
IDENTIFICATION IN A COMPLEX WITH HINT1 AND MITF, AND FUNCTION.
PubMed=22647378; DOI=10.4161/cc.20765;
Genovese G., Ghosh P., Li H., Rettino A., Sioletic S., Cittadini A.,
Sgambato A.;
"The tumor suppressor HINT1 regulates MITF and beta-catenin transcriptional
activity in melanoma cells.";
Cell Cycle 11:2206-2215(2012).
[65]
FUNCTION, INTERACTION WITH FERMT2, IDENTIFICATION IN A COMPLEX WITH FERMT2
AND TCF7L2, AND SUBCELLULAR LOCATION.
PubMed=22699938; DOI=10.1038/embor.2012.88;
Yu Y., Wu J., Wang Y., Zhao T., Ma B., Liu Y., Fang W., Zhu W.G., Zhang H.;
"Kindlin 2 forms a transcriptional complex with beta-catenin and TCF4 to
enhance Wnt signalling.";
EMBO Rep. 13:750-758(2012).
[66]
FUNCTION, AND INTERACTION WITH PML.
PubMed=22155184; DOI=10.1053/j.gastro.2011.11.041;
Satow R., Shitashige M., Jigami T., Fukami K., Honda K., Kitabayashi I.,
Yamada T.;
"Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor
function in colorectal cancer cells.";
Gastroenterology 142:572-581(2012).
[67]
INVOLVEMENT IN NEDSDV.
PubMed=23033978; DOI=10.1056/nejmoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
[68]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[69]
SUBCELLULAR LOCATION, AND INTERACTION WITH FAM53B.
PubMed=25183871; DOI=10.1242/dev.108415;
Kizil C., Kuechler B., Yan J.J., Oezhan G., Moro E., Argenton F., Brand M.,
Weidinger G., Antos C.L.;
"Simplet/Fam53b is required for Wnt signal transduction by regulating beta-
catenin nuclear localization.";
Development 141:3529-3539(2014).
[70]
GLYCOSYLATION AT SER-23, AND SUBCELLULAR LOCATION.
PubMed=24342833; DOI=10.1016/j.yexcr.2013.11.021;
Ha J.R., Hao L., Venkateswaran G., Huang Y.H., Garcia E., Persad S.;
"beta-catenin is O-GlcNAc glycosylated at Serine 23: implications for beta-
catenin's subcellular localization and transactivator function.";
Exp. Cell Res. 321:153-166(2014).
[71]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-552, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[72]
INTERACTION WITH RNF220.
PubMed=25266658; DOI=10.1128/mcb.00731-14;
Ma P., Yang X., Kong Q., Li C., Yang S., Li Y., Mao B.;
"The ubiquitin ligase RNF220 enhances canonical Wnt signaling through USP7-
mediated deubiquitination of beta-catenin.";
Mol. Cell. Biol. 34:4355-4366(2014).
[73]
ACETYLATION AT LYS-49, AND DEACETYLATION.
PubMed=24824780; DOI=10.1002/ijc.28967;
Pangon L., Mladenova D., Watkins L., Van Kralingen C., Currey N.,
Al-Sohaily S., Lecine P., Borg J.P., Kohonen-Corish M.R.;
"MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in
the cytoplasm.";
Int. J. Cancer 136:55-64(2015).
[74]
INTERACTION WITH JPT1, AND PHOSPHORYLATION AT SER-33.
PubMed=25169422; DOI=10.1002/jcb.24956;
Varisli L., Ozturk B.E., Akyuz G.K., Korkmaz K.S.;
"HN1 negatively influences the beta-catenin/E-cadherin interaction, and
contributes to migration in prostate cells.";
J. Cell. Biochem. 116:170-178(2015).
[75]
INTERACTION WITH CTNND2.
PubMed=25807484; DOI=10.1038/nature14186;
Turner T.N., Sharma K., Oh E.C., Liu Y.P., Collins R.L., Sosa M.X.,
Auer D.R., Brand H., Sanders S.J., Moreno-De-Luca D., Pihur V., Plona T.,
Pike K., Soppet D.R., Smith M.W., Cheung S.W., Martin C.L., State M.W.,
Talkowski M.E., Cook E., Huganir R., Katsanis N., Chakravarti A.;
"Loss of delta-catenin function in severe autism.";
Nature 520:51-56(2015).
[76]
INTERACTION WITH GID8; AXIN1 AND TCF7L2, AND SUBCELLULAR LOCATION.
PubMed=28829046; DOI=10.1038/cr.2017.107;
Lu Y., Xie S., Zhang W., Zhang C., Gao C., Sun Q., Cai Y., Xu Z., Xiao M.,
Xu Y., Huang X., Wu X., Liu W., Wang F., Kang Y., Zhou T.;
"Twa1/Gid8 is a beta-catenin nuclear retention factor in Wnt signaling and
colorectal tumorigenesis.";
Cell Res. 27:1422-1440(2017).
[77]
IDENTIFICATION IN A CADHERIN/CATENIN ADHESION COMPLEX.
PubMed=28051089; DOI=10.1038/mi.2016.120;
Caldwell J.M., Collins M.H., Kemme K.A., Sherrill J.D., Wen T., Rochman M.,
Stucke E.M., Amin L., Tai H., Putnam P.E., Jimenez-Dalmaroni M.J.,
Wormald M.R., Porollo A., Abonia J.P., Rothenberg M.E.;
"Cadherin 26 is an alpha integrin-binding epithelial receptor regulated
during allergic inflammation.";
Mucosal Immunol. 10:1190-1201(2017).
[78]
INTERACTION WITH TCF7L2/TCF4 AND HERPES VIRUS 8 PROTEIN VPK (MICROBIAL
INFECTION).
PubMed=29432739; DOI=10.1016/j.bbrc.2018.02.089;
Cha S., Kang M.S., Seo T.;
"KSHV vPK inhibits Wnt signaling via preventing interactions between beta-
catenin and TCF4.";
Biochem. Biophys. Res. Commun. 497:381-387(2018).
[79]
SUBCELLULAR LOCATION, INTERACTION WITH TMEM170B, AND TISSUE SPECIFICITY.
PubMed=29367600; DOI=10.1038/s41419-017-0128-y;
Li M., Han Y., Zhou H., Li X., Lin C., Zhang E., Chi X., Hu J., Xu H.;
"Transmembrane protein 170B is a novel breast tumorigenesis suppressor gene
that inhibits the Wnt/beta-catenin pathway.";
Cell Death Dis. 9:91-91(2018).
[80]
INVOLVEMENT IN EVR7, AND VARIANT EVR7 CYS-710.
PubMed=28575650; DOI=10.1016/j.ajhg.2017.05.001;
Panagiotou E.S., Sanjurjo Soriano C., Poulter J.A., Lord E.C., Dzulova D.,
Kondo H., Hiyoshi A., Chung B.H., Chu Y.W., Lai C.H.Y., Tafoya M.E.,
Karjosukarso D., Collin R.W.J., Topping J., Downey L.M., Ali M.,
Inglehearn C.F., Toomes C.;
"Defects in the cell signaling mediator beta-catenin cause the retinal
vascular condition FEVR.";
Am. J. Hum. Genet. 100:960-968(2017).
[81]
INTERACTION WITH IRF2BPL, AND VARIANT TYR-33.
PubMed=29374064; DOI=10.1158/0008-5472.can-17-2403;
Higashimori A., Dong Y., Zhang Y., Kang W., Nakatsu G., Ng S.S.M.,
Arakawa T., Sung J.J.Y., Chan F.K.L., Yu J.;
"Forkhead Box F2 Suppresses Gastric Cancer through a Novel FOXF2-IRF2BPL-
beta-Catenin Signaling Axis.";
Cancer Res. 78:1643-1656(2018).
[82]
INTERACTION WITH SOX30 AND TCF7L2, AND SUBCELLULAR LOCATION.
PubMed=29739711; DOI=10.1016/j.ebiom.2018.04.026;
Han F., Liu W.B., Shi X.Y., Yang J.T., Zhang X., Li Z.M., Jiang X., Yin L.,
Li J.J., Huang C.S., Cao J., Liu J.Y.;
"SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling via
Transcriptional and Posttranslational Regulation of beta-Catenin in Lung
Cancer.";
EBioMedicine 31:253-266(2018).
[83]
INTERACTION WITH LMBR1L.
PubMed=31073040; DOI=10.1126/science.aau0812;
Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J.,
Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M.,
Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y.,
Beutler B.;
"LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling.";
Science 364:0-0(2019).
[84]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 133-664.
PubMed=11136974; DOI=10.1016/s0092-8674(00)00192-6;
Graham T.A., Weaver C., Mao F., Kimelman D., Xu W.;
"Crystal structure of a beta-catenin/Tcf complex.";
Cell 103:885-896(2000).
[85]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-664 IN COMPLEX WITH TCF7L2,
AND MUTAGENESIS OF LYS-312 AND LYS-435.
PubMed=11713475; DOI=10.1038/nsb718;
Graham T.A., Ferkey D.M., Mao F., Kimelman D., Xu W.;
"Tcf4 can specifically recognize beta-catenin using alternative
conformations.";
Nat. Struct. Biol. 8:1048-1052(2001).
[86]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-668 IN COMPLEX WITH TCF7L2.
PubMed=11713476; DOI=10.1038/nsb720;
Poy F., Lepourcelet M., Shivdasani R.A., Eck M.J.;
"Structure of a human Tcf4-beta-catenin complex.";
Nat. Struct. Biol. 8:1053-1057(2001).
[87]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-664 IN COMPLEX WITH CTNNBIP1,
AND MUTAGENESIS OF PHE-660 AND ARG-661.
PubMed=12408824; DOI=10.1016/s1097-2765(02)00637-8;
Graham T.A., Clements W.K., Kimelman D., Xu W.;
"The crystal structure of the beta-catenin/ICAT complex reveals the
inhibitory mechanism of ICAT.";
Mol. Cell 10:563-571(2002).
[88]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-136 IN COMPLEX WITH BCL9 AND
TCF7L2, INTERACTION WITH BCL9; BCL9L CDH3 AND TCF7L2, AND MUTAGENESIS OF
TYR-142; LEU-156; LEU-159 AND LEU-178.
PubMed=17052462; DOI=10.1016/j.molcel.2006.09.001;
Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.;
"Crystal structure of a beta-catenin/BCL9/Tcf4 complex.";
Mol. Cell 24:293-300(2006).
[89]
VARIANTS COLORECTAL CANCER TYR-33 AND SER-45 DEL.
PubMed=9065402; DOI=10.1126/science.275.5307.1787;
Morin P.J., Sparks A.B., Korinek V., Barker N., Clevers H., Vogelstein B.,
Kinzler K.W.;
"Activation of beta-catenin-Tcf signaling in colon cancer by mutations in
beta-catenin or APC.";
Science 275:1787-1790(1997).
[90]
VARIANTS HEPATOBLASTOMA TYR-32; VAL-34; CYS-37 AND ALA-41.
PubMed=9927029;
Koch A., Denkhaus D., Albrecht S., Leuschner I., von Schweinitz D.,
Pietsch T.;
"Childhood hepatoblastomas frequently carry a mutated degradation targeting
box of the beta-catenin gene.";
Cancer Res. 59:269-273(1999).
[91]
VARIANT HEPATOBLASTOMA ALA-41.
PubMed=10398436;
DOI=10.1002/(sici)1098-2264(199908)25:4<399::aid-gcc14>3.0.co;2-x;
Blaeker H., Hofmann W.J., Rieker R.J., Penzel R., Graf M., Otto H.F.;
"Beta-catenin accumulation and mutation of the CTNNB1 gene in
hepatoblastoma.";
Genes Chromosomes Cancer 25:399-402(1999).
[92]
VARIANTS OVARIAN CANCER CYS-37; ILE-41 AND ALA-41.
PubMed=10391090; DOI=10.1111/j.1349-7006.1999.tb00777.x;
Sagae S., Kobayashi K., Nishioka Y., Sugimura M., Ishioka S., Nagata M.,
Terasawa K., Tokino T., Kudo R.;
"Mutational analysis of beta-catenin gene in Japanese ovarian carcinomas:
frequent mutations in endometrioid carcinomas.";
Jpn. J. Cancer Res. 90:510-515(1999).
[93]
VARIANT DESMOID TUMOR ALA-41.
PubMed=10655994; DOI=10.1136/jcp.52.9.695;
Shitoh K., Konishi F., Iijima T., Ohdaira T., Sakai K., Kanazawa K.,
Miyaki M.;
"A novel case of a sporadic desmoid tumour with mutation of the beta
catenin gene.";
J. Clin. Pathol. 52:695-696(1999).
[94]
VARIANTS PTR GLY-32; TYR-32; PHE-33; TYR-33; GLU-34; CYS-37; PHE-37 AND
ILE-41.
PubMed=10192393; DOI=10.1038/7747;
Chan E.F., Gat U., McNiff J.M., Fuchs E.;
"A common human skin tumour is caused by activating mutations in beta-
catenin.";
Nat. Genet. 21:410-413(1999).
[95]
VARIANTS HEPATOCELLULAR CARCINOMA ARG-23; 25-TRP--SER-33 DEL; ALA-32;
GLY-32; TYR-32; LEU-33; PHE-33; ARG-34; SER-35; ALA-37; 37-SER-GLY-38
DELINS TRP; TYR-37; ALA-41; ILE-41; PHE-45 AND PRO-45.
PubMed=10435629; DOI=10.1038/sj.onc.1202800;
Legoix P., Bluteau O., Bayer J., Perret C., Balabaud C., Belghiti J.,
Franco D., Thomas G., Laurent-Puig P., Zucman-Rossi J.;
"Beta-catenin mutations in hepatocellular carcinoma correlate with a low
rate of loss of heterozygosity.";
Oncogene 18:4044-4046(1999).
[96]
VARIANTS MDB PHE-33 AND ALA-37.
PubMed=10666372; DOI=10.1016/s0002-9440(10)64747-5;
Huang H., Mahler-Araujo B.M., Sankila A., Chimelli L., Yonekawa Y.,
Kleihues P., Ohgaki H.;
"APC mutations in sporadic medulloblastomas.";
Am. J. Pathol. 156:433-437(2000).
[97]
VARIANT NEDSDV PRO-388.
PubMed=25326669; DOI=10.1007/s00439-014-1498-1;
Kuechler A., Willemsen M.H., Albrecht B., Bacino C.A., Bartholomew D.W.,
van Bokhoven H., van den Boogaard M.J., Bramswig N., Buettner C.,
Cremer K., Czeschik J.C., Engels H., van Gassen K., Graf E., van Haelst M.,
He W., Hogue J.S., Kempers M., Koolen D., Monroe G., de Munnik S.,
Pastore M., Reis A., Reuter M.S., Tegay D.H., Veltman J., Visser G.,
van Hasselt P., Smeets E.E., Vissers L., Wieland T., Wissink W., Yntema H.,
Zink A.M., Strom T.M., Luedecke H.J., Kleefstra T., Wieczorek D.;
"De novo mutations in beta-catenin (CTNNB1) appear to be a frequent cause
of intellectual disability: expanding the mutational and clinical
spectrum.";
Hum. Genet. 134:97-109(2015).
[98]
VARIANT NEDSDV 558-GLN--LEU-781 DEL.
PubMed=28514307; DOI=10.1097/md.0000000000006914;
Li N., Xu Y., Li G., Yu T., Yao R.E., Wang X., Wang J.;
"Exome sequencing identifies a de novo mutation of CTNNB1 gene in a patient
mainly presented with retinal detachment, lens and vitreous opacities,
microcephaly, and developmental delay: Case report and literature review.";
Medicine (Baltimore) 96:E6914-E6914(2017).
-!- FUNCTION: Key downstream component of the canonical Wnt signaling
pathway (PubMed:17524503, PubMed:18077326, PubMed:18086858,
PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378,
PubMed:22699938). In the absence of Wnt, forms a complex with AXIN1,
AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-
terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and
its subsequent degradation by the proteasome (PubMed:17524503,
PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353,
PubMed:22155184, PubMed:22647378, PubMed:22699938). In the presence of
Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus,
where it acts as a coactivator for transcription factors of the TCF/LEF
family, leading to activate Wnt responsive genes (PubMed:17524503,
PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353,
PubMed:22155184, PubMed:22647378, PubMed:22699938). Involved in the
regulation of cell adhesion, as component of an E-cadherin:catenin
adhesion complex (By similarity). Acts as a negative regulator of
centrosome cohesion (PubMed:18086858). Involved in the
CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization
(PubMed:21262353). Blocks anoikis of malignant kidney and intestinal
epithelial cells and promotes their anchorage-independent growth by
down-regulating DAPK2 (PubMed:18957423). Disrupts PML function and PML-
NB formation by inhibiting RANBP2-mediated sumoylation of PML
(PubMed:22155184). Promotes neurogenesis by maintaining sympathetic
neuroblasts within the cell cycle (By similarity). Involved in
chondrocyte differentiation via interaction with SOX9: SOX9-binding
competes with the binding sites of TCF/LEF within CTNNB1, thereby
inhibiting the Wnt signaling (By similarity).
{ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:17524503,
ECO:0000269|PubMed:18077326, ECO:0000269|PubMed:18086858,
ECO:0000269|PubMed:18957423, ECO:0000269|PubMed:21262353,
ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22647378,
ECO:0000269|PubMed:22699938}.
-!- SUBUNIT: Two separate complex-associated pools are found in the
cytoplasm. The majority is present as component of an E-
cadherin:catenin adhesion complex composed of at least E-cadherin/CDH1
and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex
is located to adherens junctions. The stable association of CTNNA1 is
controversial as CTNNA1 was shown not to bind to F-actin when assembled
in the complex. Alternatively, the CTNNA1-containing complex may be
linked to F-actin by other proteins such as LIMA1. Another cytoplasmic
pool is part of a large complex containing AXIN1, AXIN2, APC, CSNK1A1
and GSK3B that promotes phosphorylation on N-terminal Ser and Thr
residues and ubiquitination of CTNNB1 via BTRC and its subsequent
degradation by the proteasome. Wnt-dependent activation of DVL
antagonizes the action of GSK3B. When GSK3B activity is inhibited the
complex dissociates, CTNNB1 is dephosphorylated and is no longer
targeted for destruction. The stabilized protein translocates to the
nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9, BCL9L and
possibly also RUVBL1 and CHD8. Binds CTNNBIP and EP300. CTNNB1 forms a
ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1
binding. Interacts with TAX1BP3 (via the PDZ domain); this interaction
inhibits the transcriptional activity of CTNNB1. Interacts with AJAP1,
BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1. Interacts
with GLIS2 and MUC1. Interacts with SLC30A9. Interacts with XIRP1.
Interacts directly with AXIN1; the interaction is regulated by CDK2
phosphorylation of AXIN1. Interacts with SCRIB. Interacts with RAPGEF2.
Interacts with PTPRU (via the cytoplasmic juxtamembrane domain).
Interacts with EMD. Interacts with TNIK and TCF7L2. Interacts with
SESTD1 and TRPC4. Interacts with CAV1. Interacts with TRPV4. The TRPV4
and CTNNB1 complex can interact with CDH1. Interacts with VCL.
Interacts with PTPRJ. Interacts with PKT7 and CDK2. Interacts with FAT1
(via the cytoplasmic domain). Interacts with NANOS1 and NDRG2.
Interacts with isoform 1 of NEK2. Interacts with both isoform 1 and
isoform 2 of CDK5. Interacts with PTK6. Interacts with SOX7; this
interaction may lead to proteasomal degradation of active CTNNB1 and
thus inhibition of Wnt/beta-catenin-stimulated transcription.
Identified in a complex with HINT1 and MITF. Interacts with FHIT. The
CTNNB1 and TCF7L2/TCF4 complex interacts with PML (isoform PML-4).
Interacts with FERMT2. Identified in a complex with TCF7L2/TCF4 and
FERMT2 (PubMed:29739711, PubMed:22699938). Interacts with RORA. May
interact with P-cadherin/CDH3. Interacts with RNF220 (PubMed:25266658).
Interacts with CTNND2 (PubMed:25807484). Interacts (via the C-terminal
region) with CBY1 (PubMed:12712206, PubMed:16424001). The complex
composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the
interaction requires the inactive form of GSK3B (phosphorylated at
'Ser-9') (PubMed:25169422). Interacts with DLG5 (By similarity).
Interacts with FAM53B; promoting translocation to the nucleus
(PubMed:25183871). Interacts with TMEM170B (PubMed:29367600). Interacts
with AHI1 (PubMed:21623382). Interacts with GID8 (PubMed:28829046).
Component of an cadherin:catenin adhesion complex composed of at least
of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120
catenin/CTNND1 (PubMed:28051089). Forms a complex comprising APPL1,
RUVBL2, APPL2, HDAC1 and HDAC2 (PubMed:19433865). Interacts with
IRF2BPL; mediates the ubiquitination and degradation of CTNNB1
(PubMed:29374064). Interacts with AMFR (By similarity). Interacts with
LMBR1L (PubMed:31073040). Interacts with SOX30; prevents interaction of
CTNNB1 with TCF7L2/TCF4 and leads to inhibition of Wnt signaling
(PubMed:29739711). Interacts with SOX9; inhibiting CTNNB1 activity by
competing with the binding sites of TCF/LEF within CTNNB1, thereby
inhibiting the Wnt signaling (By similarity).
{ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:10966653,
ECO:0000269|PubMed:11279024, ECO:0000269|PubMed:11389839,
ECO:0000269|PubMed:11389840, ECO:0000269|PubMed:11590244,
ECO:0000269|PubMed:11713475, ECO:0000269|PubMed:11713476,
ECO:0000269|PubMed:11751639, ECO:0000269|PubMed:12077367,
ECO:0000269|PubMed:12297051, ECO:0000269|PubMed:12370829,
ECO:0000269|PubMed:12408824, ECO:0000269|PubMed:12420223,
ECO:0000269|PubMed:12501215, ECO:0000269|PubMed:12712206,
ECO:0000269|PubMed:12830000, ECO:0000269|PubMed:14595118,
ECO:0000269|PubMed:16424001, ECO:0000269|PubMed:16858403,
ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:17047063,
ECO:0000269|PubMed:17052462, ECO:0000269|PubMed:17289029,
ECO:0000269|PubMed:17524503, ECO:0000269|PubMed:18077326,
ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18378692,
ECO:0000269|PubMed:18819930, ECO:0000269|PubMed:19433865,
ECO:0000269|PubMed:19693690, ECO:0000269|PubMed:19816403,
ECO:0000269|PubMed:19996314, ECO:0000269|PubMed:20026641,
ECO:0000269|PubMed:20164195, ECO:0000269|PubMed:21132015,
ECO:0000269|PubMed:21247902, ECO:0000269|PubMed:21262353,
ECO:0000269|PubMed:21623382, ECO:0000269|PubMed:22155184,
ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:22699938,
ECO:0000269|PubMed:25169422, ECO:0000269|PubMed:25183871,
ECO:0000269|PubMed:25266658, ECO:0000269|PubMed:25807484,
ECO:0000269|PubMed:28051089, ECO:0000269|PubMed:28829046,
ECO:0000269|PubMed:29367600, ECO:0000269|PubMed:29374064,
ECO:0000269|PubMed:29432739, ECO:0000269|PubMed:29739711,
ECO:0000269|PubMed:31073040, ECO:0000269|PubMed:7982500,
ECO:0000305|PubMed:31073040}.
-!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8 protein
vPK; this interaction inhibits the Wnt signaling pathway.
{ECO:0000269|PubMed:29432739}.
-!- INTERACTION:
P35222; P00519: ABL1; NbExp=2; IntAct=EBI-491549, EBI-375543;
P35222; O43707: ACTN4; NbExp=7; IntAct=EBI-491549, EBI-351526;
P35222; Q5JTC6: AMER1; NbExp=9; IntAct=EBI-491549, EBI-6169747;
P35222; P25054: APC; NbExp=19; IntAct=EBI-491549, EBI-727707;
P35222; P10275: AR; NbExp=11; IntAct=EBI-491549, EBI-608057;
P35222; O15169: AXIN1; NbExp=44; IntAct=EBI-491549, EBI-710484;
P35222; Q9Y2T1: AXIN2; NbExp=2; IntAct=EBI-491549, EBI-4400025;
P35222; O00512: BCL9; NbExp=2; IntAct=EBI-491549, EBI-533127;
P35222; A1Z199: BCR/ABL fusion; NbExp=2; IntAct=EBI-491549, EBI-7286259;
P35222; Q9Y297: BTRC; NbExp=8; IntAct=EBI-491549, EBI-307461;
P35222; Q6P1J9: CDC73; NbExp=10; IntAct=EBI-491549, EBI-930143;
P35222; P12830: CDH1; NbExp=14; IntAct=EBI-491549, EBI-727477;
P35222; P19022: CDH2; NbExp=8; IntAct=EBI-491549, EBI-2256711;
P35222; P33151: CDH5; NbExp=7; IntAct=EBI-491549, EBI-2903122;
P35222; Q92793: CREBBP; NbExp=2; IntAct=EBI-491549, EBI-81215;
P35222; P35221: CTNNA1; NbExp=3; IntAct=EBI-491549, EBI-701918;
P35222; Q9UI47: CTNNA3; NbExp=2; IntAct=EBI-491549, EBI-3937546;
P35222; Q9UI47-1: CTNNA3; NbExp=4; IntAct=EBI-491549, EBI-21980640;
P35222; Q9NSA3: CTNNBIP1; NbExp=12; IntAct=EBI-491549, EBI-747082;
P35222; Q9NYF0: DACT1; NbExp=3; IntAct=EBI-491549, EBI-3951744;
P35222; P26358: DNMT1; NbExp=8; IntAct=EBI-491549, EBI-719459;
P35222; P18146: EGR1; NbExp=7; IntAct=EBI-491549, EBI-2834611;
P35222; P50402: EMD; NbExp=3; IntAct=EBI-491549, EBI-489887;
P35222; P29317: EPHA2; NbExp=2; IntAct=EBI-491549, EBI-702104;
P35222; Q9UKB1: FBXW11; NbExp=4; IntAct=EBI-491549, EBI-355189;
P35222; Q96AC1: FERMT2; NbExp=13; IntAct=EBI-491549, EBI-4399465;
P35222; P11362: FGFR1; NbExp=2; IntAct=EBI-491549, EBI-1028277;
P35222; P49789: FHIT; NbExp=4; IntAct=EBI-491549, EBI-741760;
P35222; P17948: FLT1; NbExp=2; IntAct=EBI-491549, EBI-1026718;
P35222; Q08050: FOXM1; NbExp=16; IntAct=EBI-491549, EBI-866480;
P35222; Q9BZE0: GLIS2; NbExp=6; IntAct=EBI-491549, EBI-7251368;
P35222; P49841: GSK3B; NbExp=19; IntAct=EBI-491549, EBI-373586;
P35222; Q9UBN7: HDAC6; NbExp=4; IntAct=EBI-491549, EBI-301697;
P35222; Q16665: HIF1A; NbExp=4; IntAct=EBI-491549, EBI-447269;
P35222; P42858: HTT; NbExp=5; IntAct=EBI-491549, EBI-466029;
P35222; P08069: IGF1R; NbExp=3; IntAct=EBI-491549, EBI-475981;
P35222; P46940: IQGAP1; NbExp=3; IntAct=EBI-491549, EBI-297509;
P35222; O75564: JRK; NbExp=3; IntAct=EBI-491549, EBI-8607681;
P35222; P14923: JUP; NbExp=3; IntAct=EBI-491549, EBI-702484;
P35222; Q14678: KANK1; NbExp=2; IntAct=EBI-491549, EBI-2556221;
P35222; Q2LD37: KIAA1109; NbExp=2; IntAct=EBI-491549, EBI-2683809;
P35222; Q9UJU2: LEF1; NbExp=10; IntAct=EBI-491549, EBI-926131;
P35222; Q8WVC0: LEO1; NbExp=2; IntAct=EBI-491549, EBI-932432;
P35222; Q9GZQ8: MAP1LC3B; NbExp=5; IntAct=EBI-491549, EBI-373144;
P35222; P55197: MLLT10; NbExp=4; IntAct=EBI-491549, EBI-1104952;
P35222; Q92597: NDRG1; NbExp=3; IntAct=EBI-491549, EBI-716486;
P35222; P19838: NFKB1; NbExp=3; IntAct=EBI-491549, EBI-300010;
P35222; P29474: NOS3; NbExp=4; IntAct=EBI-491549, EBI-1391623;
P35222; O00482-1: NR5A2; NbExp=5; IntAct=EBI-491549, EBI-15960777;
P35222; P49757: NUMB; NbExp=2; IntAct=EBI-491549, EBI-915016;
P35222; P49757-3: NUMB; NbExp=3; IntAct=EBI-491549, EBI-10692196;
P35222; Q8TEW0: PARD3; NbExp=2; IntAct=EBI-491549, EBI-81968;
P35222; P16284: PECAM1; NbExp=3; IntAct=EBI-491549, EBI-716404;
P35222; Q99697: PITX2; NbExp=2; IntAct=EBI-491549, EBI-1175211;
P35222; P14618: PKM; NbExp=4; IntAct=EBI-491549, EBI-353408;
P35222; P14618-1: PKM; NbExp=3; IntAct=EBI-491549, EBI-4304679;
P35222; Q03431: PTH1R; NbExp=4; IntAct=EBI-491549, EBI-2860297;
P35222; Q13308: PTK7; NbExp=5; IntAct=EBI-491549, EBI-2803245;
P35222; P08575: PTPRC; NbExp=2; IntAct=EBI-491549, EBI-1341;
P35222; P23470: PTPRG; NbExp=2; IntAct=EBI-491549, EBI-2258115;
P35222; Q12913: PTPRJ; NbExp=2; IntAct=EBI-491549, EBI-2264500;
P35222; P49023: PXN; NbExp=4; IntAct=EBI-491549, EBI-702209;
P35222; Q04206: RELA; NbExp=3; IntAct=EBI-491549, EBI-73886;
P35222; Q13761: RUNX3; NbExp=12; IntAct=EBI-491549, EBI-925990;
P35222; Q9Y265: RUVBL1; NbExp=3; IntAct=EBI-491549, EBI-353675;
P35222; Q01826: SATB1; NbExp=9; IntAct=EBI-491549, EBI-743747;
P35222; P63208: SKP1; NbExp=3; IntAct=EBI-491549, EBI-307486;
P35222; Q9H6I2: SOX17; NbExp=2; IntAct=EBI-491549, EBI-9106753;
P35222; P12931: SRC; NbExp=2; IntAct=EBI-491549, EBI-621482;
P35222; P15884: TCF4; NbExp=22; IntAct=EBI-491549, EBI-533224;
P35222; P36402: TCF7; NbExp=4; IntAct=EBI-491549, EBI-2119465;
P35222; Q9NQB0: TCF7L2; NbExp=27; IntAct=EBI-491549, EBI-924724;
P35222; O14746: TERT; NbExp=2; IntAct=EBI-491549, EBI-1772203;
P35222; Q9UKE5: TNIK; NbExp=3; IntAct=EBI-491549, EBI-1051794;
P35222; P11388: TOP2A; NbExp=5; IntAct=EBI-491549, EBI-539628;
P35222; Q13625: TP53BP2; NbExp=5; IntAct=EBI-491549, EBI-77642;
P35222; O95071: UBR5; NbExp=6; IntAct=EBI-491549, EBI-358329;
P35222; Q9GZV5: WWTR1; NbExp=4; IntAct=EBI-491549, EBI-747743;
P35222; P46937: YAP1; NbExp=13; IntAct=EBI-491549, EBI-1044059;
P35222; P46937-3: YAP1; NbExp=2; IntAct=EBI-491549, EBI-6558686;
P35222; O35625: Axin1; Xeno; NbExp=4; IntAct=EBI-491549, EBI-2365912;
P35222; Q9YGY0: axin1; Xeno; NbExp=2; IntAct=EBI-491549, EBI-1037449;
P35222; P33724: CAV1; Xeno; NbExp=5; IntAct=EBI-491549, EBI-79998;
P35222; P26231: Ctnna1; Xeno; NbExp=2; IntAct=EBI-491549, EBI-647895;
P35222; P18012: ipaC; Xeno; NbExp=4; IntAct=EBI-491549, EBI-491541;
P35222; P27782: Lef1; Xeno; NbExp=2; IntAct=EBI-491549, EBI-984464;
P35222; Q9JHQ5: Lztfl1; Xeno; NbExp=2; IntAct=EBI-491549, EBI-6142879;
P35222; Q01887: Ryk; Xeno; NbExp=2; IntAct=EBI-491549, EBI-16110594;
P35222; Q9DBG9: Tax1bp3; Xeno; NbExp=3; IntAct=EBI-491549, EBI-1161647;
P35222; Q9EPK5: Wwtr1; Xeno; NbExp=2; IntAct=EBI-491549, EBI-1211920;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25183871,
ECO:0000269|PubMed:29739711}. Nucleus {ECO:0000269|PubMed:24342833,
ECO:0000269|PubMed:25183871, ECO:0000269|PubMed:28829046,
ECO:0000269|PubMed:29367600, ECO:0000269|PubMed:29739711}. Cytoplasm,
cytoskeleton {ECO:0000250|UniProtKB:B6V8E6}. Cell junction, adherens
junction {ECO:0000250|UniProtKB:Q02248}. Cell junction
{ECO:0000250|UniProtKB:B6V8E6}. Cell membrane
{ECO:0000269|PubMed:24342833}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole.
Cell junction, synapse {ECO:0000250|UniProtKB:Q02248}. Cytoplasm,
cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q02248}.
Note=Colocalized with RAPGEF2 and TJP1 at cell-cell contacts (By
similarity). Cytoplasmic when it is unstabilized (high level of
phosphorylation) or bound to CDH1. Translocates to the nucleus when it
is stabilized (low level of phosphorylation). Interaction with GLIS2
and MUC1 promotes nuclear translocation. Interaction with EMD inhibits
nuclear localization. The majority of beta-catenin is localized to the
cell membrane. In interphase, colocalizes with CROCC between CEP250
puncta at the proximal end of centrioles, and this localization is
dependent on CROCC and CEP250. In mitosis, when NEK2 activity
increases, it localizes to centrosomes at spindle poles independent of
CROCC. Colocalizes with CDK5 in the cell-cell contacts and plasma
membrane of undifferentiated and differentiated neuroblastoma cells.
Interaction with FAM53B promotes translocation to the nucleus
(PubMed:25183871). {ECO:0000250|UniProtKB:B6V8E6,
ECO:0000269|PubMed:25183871}.
-!- TISSUE SPECIFICITY: Expressed in several hair follicle cell types:
basal and peripheral matrix cells, and cells of the outer and inner
root sheaths. Expressed in colon. Present in cortical neurons (at
protein level). Expressed in breast cancer tissues (at protein level)
(PubMed:29367600). {ECO:0000269|PubMed:11703283,
ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:17289029,
ECO:0000269|PubMed:29367600}.
-!- PTM: Phosphorylation at Ser-552 by AMPK promotes stabilizion of the
protein, enhancing TCF/LEF-mediated transcription (By similarity).
Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by
another kinase. Phosphorylation proceeds then from Thr-41 to Ser-37 and
Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine
phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and
enhances TBP binding. Phosphorylated on Ser-33 and Ser-37 by HIPK2 and
GSK3B, this phosphorylation triggers proteasomal degradation
(PubMed:25169422). Phosphorylation on Ser-191 and Ser-246 by CDK5.
Phosphorylation by CDK2 regulates insulin internalization.
Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or Tyr-333 with
the predominant site at Tyr-64 is not essential for inhibition of
transcriptional activity. {ECO:0000250, ECO:0000269|PubMed:10966653,
ECO:0000269|PubMed:11279024, ECO:0000269|PubMed:12027456,
ECO:0000269|PubMed:12051714, ECO:0000269|PubMed:12077367,
ECO:0000269|PubMed:12640114, ECO:0000269|PubMed:17009320,
ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:20026641,
ECO:0000269|PubMed:20307497, ECO:0000269|PubMed:21262353,
ECO:0000269|PubMed:25169422}.
-!- PTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when
phosphorylated by GSK3B, leading to its degradation (PubMed:12077367).
Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1,
SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent
proteasomal degradation (PubMed:11389839, PubMed:11389840,
PubMed:20307497). Ubiquitinated and degraded following interaction with
SOX9 (By similarity). {ECO:0000250|UniProtKB:Q02248,
ECO:0000269|PubMed:11389839, ECO:0000269|PubMed:11389840,
ECO:0000269|PubMed:12077367, ECO:0000269|PubMed:20307497}.
-!- PTM: S-nitrosylation at Cys-619 within adherens junctions promotes
VEGF-induced, NO-dependent endothelial cell permeability by disrupting
interaction with E-cadherin, thus mediating disassembly adherens
junctions. {ECO:0000250|UniProtKB:Q02248}.
-!- PTM: O-glycosylation at Ser-23 decreases nuclear localization and
transcriptional activity, and increases localization to the plasma
membrane and interaction with E-cadherin CDH1.
{ECO:0000269|PubMed:24342833}.
-!- PTM: Deacetylated at Lys-49 by SIRT1. {ECO:0000269|PubMed:24824780}.
-!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease
characterized by malignant lesions arising from the inner wall of the
large intestine (the colon) and the rectum. Genetic alterations are
often associated with progression from premalignant lesion (adenoma) to
invasive adenocarcinoma. Risk factors for cancer of the colon and
rectum include colon polyps, long-standing ulcerative colitis, and
genetic family history. {ECO:0000269|PubMed:9065402}. Note=The gene
represented in this entry may be involved in disease pathogenesis.
-!- DISEASE: Note=Activating mutations in CTNNB1 have oncogenic activity
resulting in tumor development. Somatic mutations are found in various
tumor types, including colon cancers, ovarian and prostate carcinomas,
hepatoblastoma (HB), hepatocellular carcinoma (HCC). HBs are malignant
embryonal tumors mainly affecting young children in the first three
years of life.
-!- DISEASE: Pilomatrixoma (PTR) [MIM:132600]: Common benign skin tumor.
{ECO:0000269|PubMed:10192393, ECO:0000269|PubMed:11703283,
ECO:0000269|PubMed:12027456}. Note=The gene represented in this entry
is involved in disease pathogenesis.
-!- DISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive
embryonal tumor of the cerebellum with a preferential manifestation in
children. {ECO:0000269|PubMed:10666372, ECO:0000269|PubMed:12027456}.
Note=The gene represented in this entry may be involved in disease
pathogenesis.
-!- DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer
defines malignancies originating from ovarian tissue. Although many
histologic types of ovarian tumors have been described, epithelial
ovarian carcinoma is the most common form. Ovarian cancers are often
asymptomatic and the recognized signs and symptoms, even of late-stage
disease, are vague. Consequently, most patients are diagnosed with
advanced disease. {ECO:0000269|PubMed:10391090}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- DISEASE: Note=A chromosomal aberration involving CTNNB1 is found in
salivary gland pleiomorphic adenomas, the most common benign epithelial
tumors of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1.
-!- DISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive
neoplasm of the serosal lining of the chest. It appears as broad sheets
of cells, with some regions containing spindle-shaped, sarcoma-like
cells and other regions showing adenomatous patterns. Pleural
mesotheliomas have been linked to exposure to asbestos.
{ECO:0000269|PubMed:11464291}. Note=The gene represented in this entry
may be involved in disease pathogenesis.
-!- DISEASE: Neurodevelopmental disorder with spastic diplegia and visual
defects (NEDSDV) [MIM:615075]: An autosomal dominant disorder
characterized by global developmental delay, severe intellectual
disability with absent or very limited speech, microcephaly,
spasticity, and visual abnormalities. {ECO:0000269|PubMed:23033978,
ECO:0000269|PubMed:25326669, ECO:0000269|PubMed:28514307}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Vitreoretinopathy, exudative 7 (EVR7) [MIM:617572]: A form of
exudative vitreoretinopathy, a disorder of the retinal vasculature
characterized by an abrupt cessation of growth of peripheral
capillaries, leading to an avascular peripheral retina. This may lead
to compensatory retinal neovascularization, which is thought to be
induced by hypoxia from the initial avascular insult. New vessels are
prone to leakage and rupture causing exudates and bleeding, followed by
scarring, retinal detachment and blindness. Clinical features can be
highly variable, even within the same family. Patients with mild forms
of the disease are asymptomatic, and their only disease related
abnormality is an arc of avascular retina in the extreme temporal
periphery. {ECO:0000269|PubMed:28575650}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG35511.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=BAB93475.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CTNNB1ID71.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ctnnb1/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Beta-catenin entry;
URL="https://en.wikipedia.org/wiki/Beta-catenin";
---------------------------------------------------------------------------
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EMBL; X87838; CAA61107.1; -; mRNA.
EMBL; Z19054; CAA79497.1; -; mRNA.
EMBL; AF130085; AAG35511.1; ALT_SEQ; mRNA.
EMBL; AY463360; AAR18817.1; -; Genomic_DNA.
EMBL; AK289932; BAF82621.1; -; mRNA.
EMBL; AC104307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64625.1; -; Genomic_DNA.
EMBL; BC058926; AAH58926.1; -; mRNA.
EMBL; AY081165; AAL89457.1; -; Genomic_DNA.
EMBL; AB062292; BAB93475.1; ALT_INIT; mRNA.
CCDS; CCDS2694.1; -.
PIR; A38973; A38973.
RefSeq; NP_001091679.1; NM_001098209.1.
RefSeq; NP_001091680.1; NM_001098210.1.
RefSeq; NP_001895.1; NM_001904.3.
RefSeq; XP_005264943.1; XM_005264886.2.
RefSeq; XP_016861227.1; XM_017005738.1.
PDB; 1G3J; X-ray; 2.10 A; A/C=133-664.
PDB; 1JDH; X-ray; 1.90 A; A=135-663.
PDB; 1JPW; X-ray; 2.50 A; A/B/C=131-670.
PDB; 1LUJ; X-ray; 2.50 A; A=150-663.
PDB; 1P22; X-ray; 2.95 A; C=19-44.
PDB; 1QZ7; X-ray; 2.20 A; A=133-665.
PDB; 1T08; X-ray; 2.10 A; A=146-664.
PDB; 1TH1; X-ray; 2.50 A; A/B=133-664.
PDB; 2G57; NMR; -; A=19-44.
PDB; 2GL7; X-ray; 2.60 A; A/D=138-686.
PDB; 2Z6H; X-ray; 2.20 A; A=138-781.
PDB; 3DIW; X-ray; 2.10 A; C/D=772-781.
PDB; 3FQN; X-ray; 1.65 A; C=30-39.
PDB; 3FQR; X-ray; 1.70 A; C=30-39.
PDB; 3SL9; X-ray; 2.20 A; A/B/E/G=141-305.
PDB; 3SLA; X-ray; 2.50 A; A/B/C/D/E=141-306.
PDB; 3TX7; X-ray; 2.76 A; A=138-663.
PDB; 4DJS; X-ray; 3.03 A; A=148-665.
PDB; 6M90; X-ray; 2.05 A; C=17-48.
PDB; 6M91; X-ray; 2.40 A; C=17-48.
PDB; 6M92; X-ray; 2.35 A; C=17-48.
PDB; 6M93; X-ray; 2.50 A; C=17-48.
PDB; 6M94; X-ray; 2.70 A; C=17-48.
PDB; 6O9B; X-ray; 2.20 A; C=41-49.
PDB; 6O9C; X-ray; 2.45 A; C=41-49.
PDB; 6WNX; X-ray; 2.50 A; C/F/I=31-39.
PDBsum; 1G3J; -.
PDBsum; 1JDH; -.
PDBsum; 1JPW; -.
PDBsum; 1LUJ; -.
PDBsum; 1P22; -.
PDBsum; 1QZ7; -.
PDBsum; 1T08; -.
PDBsum; 1TH1; -.
PDBsum; 2G57; -.
PDBsum; 2GL7; -.
PDBsum; 2Z6H; -.
PDBsum; 3DIW; -.
PDBsum; 3FQN; -.
PDBsum; 3FQR; -.
PDBsum; 3SL9; -.
PDBsum; 3SLA; -.
PDBsum; 3TX7; -.
PDBsum; 4DJS; -.
PDBsum; 6M90; -.
PDBsum; 6M91; -.
PDBsum; 6M92; -.
PDBsum; 6M93; -.
PDBsum; 6M94; -.
PDBsum; 6O9B; -.
PDBsum; 6O9C; -.
PDBsum; 6WNX; -.
SMR; P35222; -.
BioGRID; 107880; 705.
ComplexPortal; CPX-316; beta1-catenin - LEF1 complex.
CORUM; P35222; -.
DIP; DIP-122N; -.
IntAct; P35222; 233.
MINT; P35222; -.
STRING; 9606.ENSP00000344456; -.
BindingDB; P35222; -.
ChEMBL; CHEMBL5866; -.
DrugBank; DB03904; Urea.
GlyGen; P35222; 1 site.
iPTMnet; P35222; -.
MetOSite; P35222; -.
PhosphoSitePlus; P35222; -.
SwissPalm; P35222; -.
BioMuta; CTNNB1; -.
DMDM; 461854; -.
CPTAC; CPTAC-1745; -.
EPD; P35222; -.
jPOST; P35222; -.
MassIVE; P35222; -.
MaxQB; P35222; -.
PaxDb; P35222; -.
PeptideAtlas; P35222; -.
PRIDE; P35222; -.
ABCD; P35222; 2 sequenced antibodies.
Antibodypedia; 3432; 4773 antibodies.
DNASU; 1499; -.
Ensembl; ENST00000349496; ENSP00000344456; ENSG00000168036.
Ensembl; ENST00000396183; ENSP00000379486; ENSG00000168036.
Ensembl; ENST00000396185; ENSP00000379488; ENSG00000168036.
Ensembl; ENST00000405570; ENSP00000385604; ENSG00000168036.
Ensembl; ENST00000431914; ENSP00000412219; ENSG00000168036.
Ensembl; ENST00000433400; ENSP00000387455; ENSG00000168036.
Ensembl; ENST00000441708; ENSP00000401599; ENSG00000168036.
Ensembl; ENST00000450969; ENSP00000409302; ENSG00000168036.
Ensembl; ENST00000642248; ENSP00000495244; ENSG00000168036.
Ensembl; ENST00000642315; ENSP00000495076; ENSG00000168036.
Ensembl; ENST00000642426; ENSP00000495719; ENSG00000168036.
Ensembl; ENST00000642992; ENSP00000496385; ENSG00000168036.
Ensembl; ENST00000643031; ENSP00000495450; ENSG00000168036.
Ensembl; ENST00000643297; ENSP00000494677; ENSG00000168036.
Ensembl; ENST00000643541; ENSP00000494411; ENSG00000168036.
Ensembl; ENST00000643977; ENSP00000494053; ENSG00000168036.
Ensembl; ENST00000643992; ENSP00000493610; ENSG00000168036.
Ensembl; ENST00000644867; ENSP00000495992; ENSG00000168036.
Ensembl; ENST00000645210; ENSP00000496180; ENSG00000168036.
Ensembl; ENST00000645320; ENSP00000495360; ENSG00000168036.
Ensembl; ENST00000645982; ENSP00000494845; ENSG00000168036.
Ensembl; ENST00000646369; ENSP00000494914; ENSG00000168036.
Ensembl; ENST00000646725; ENSP00000496021; ENSG00000168036.
Ensembl; ENST00000647390; ENSP00000493533; ENSG00000168036.
GeneID; 1499; -.
KEGG; hsa:1499; -.
UCSC; uc003ckp.3; human.
CTD; 1499; -.
DisGeNET; 1499; -.
EuPathDB; HostDB:ENSG00000168036.16; -.
GeneCards; CTNNB1; -.
HGNC; HGNC:2514; CTNNB1.
HPA; ENSG00000168036; Low tissue specificity.
MalaCards; CTNNB1; -.
MIM; 114500; phenotype.
MIM; 116806; gene.
MIM; 132600; phenotype.
MIM; 155255; phenotype.
MIM; 156240; phenotype.
MIM; 167000; phenotype.
MIM; 181030; phenotype.
MIM; 615075; phenotype.
MIM; 617572; phenotype.
neXtProt; NX_P35222; -.
OpenTargets; ENSG00000168036; -.
Orphanet; 210159; Adult hepatocellular carcinoma.
Orphanet; 54595; Craniopharyngioma.
Orphanet; 873; Desmoid tumor.
Orphanet; 891; Familial exudative vitreoretinopathy.
Orphanet; 85142; NON RARE IN EUROPE: Aldosterone-producing adenoma.
Orphanet; 33402; Pediatric hepatocellular carcinoma.
Orphanet; 91414; Pilomatrixoma.
Orphanet; 404473; Severe intellectual disability-progressive spastic diplegia syndrome.
PharmGKB; PA27013; -.
eggNOG; KOG4203; Eukaryota.
GeneTree; ENSGT00940000155471; -.
InParanoid; P35222; -.
KO; K02105; -.
OMA; MAWNEXP; -.
OrthoDB; 321213at2759; -.
PhylomeDB; P35222; -.
TreeFam; TF317997; -.
PathwayCommons; P35222; -.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-418990; Adherens junctions interactions.
Reactome; R-HSA-4411364; Binding of TCF/LEF:CTNNB1 to target gene promoters.
Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-HSA-525793; Myogenesis.
Reactome; R-HSA-5339716; Misspliced GSK3beta mutants stabilize beta-catenin.
Reactome; R-HSA-5358747; S33 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358749; S37 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358751; S45 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358752; T41 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
Reactome; R-HSA-8876493; InlA-mediated entry of Listeria monocytogenes into host cells.
Reactome; R-HSA-8951430; RUNX3 regulates WNT signaling.
SignaLink; P35222; -.
SIGNOR; P35222; -.
BioGRID-ORCS; 1499; 89 hits in 885 CRISPR screens.
ChiTaRS; CTNNB1; human.
EvolutionaryTrace; P35222; -.
GeneWiki; Beta-catenin; -.
GenomeRNAi; 1499; -.
Pharos; P35222; Tchem.
PRO; PR:P35222; -.
Proteomes; UP000005640; Chromosome 3.
RNAct; P35222; protein.
Bgee; ENSG00000168036; Expressed in adrenal tissue and 251 other tissues.
ExpressionAtlas; P35222; baseline and differential.
Genevisible; P35222; HS.
GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0030877; C:beta-catenin destruction complex; IDA:BHF-UCL.
GO; GO:1990907; C:beta-catenin-TCF complex; IDA:FlyBase.
GO; GO:0070369; C:beta-catenin-TCF7L2 complex; IDA:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
GO; GO:0016342; C:catenin complex; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IDA:BHF-UCL.
GO; GO:0030054; C:cell junction; IDA:BHF-UCL.
GO; GO:0071944; C:cell periphery; IDA:BHF-UCL.
GO; GO:0005911; C:cell-cell junction; IDA:BHF-UCL.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
GO; GO:0016600; C:flotillin complex; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0016328; C:lateral plasma membrane; IDA:ARUK-UCL.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0031528; C:microvillus membrane; IEA:Ensembl.
GO; GO:0005719; C:nuclear euchromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0099092; C:postsynaptic density, intracellular component; IEA:Ensembl.
GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IEA:Ensembl.
GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
GO; GO:0032991; C:protein-containing complex; IDA:MGI.
GO; GO:0032993; C:protein-DNA complex; IDA:BHF-UCL.
GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IEA:Ensembl.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
GO; GO:1990909; C:Wnt signalosome; NAS:ParkinsonsUK-UCL.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0045294; F:alpha-catenin binding; IPI:BHF-UCL.
GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
GO; GO:0045296; F:cadherin binding; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:ParkinsonsUK-UCL.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IPI:BHF-UCL.
GO; GO:0070411; F:I-SMAD binding; IPI:BHF-UCL.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0019900; F:kinase binding; IPI:BHF-UCL.
GO; GO:0035257; F:nuclear hormone receptor binding; IPI:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; IEA:Ensembl.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IDA:UniProtKB.
GO; GO:0046332; F:SMAD binding; IPI:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0034333; P:adherens junction assembly; IMP:BHF-UCL.
GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl.
GO; GO:0036520; P:astrocyte-dopaminergic neuron signaling; IEA:Ensembl.
GO; GO:1904886; P:beta-catenin destruction complex disassembly; TAS:Reactome.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0045453; P:bone resorption; IEA:Ensembl.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IC:BHF-UCL.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
GO; GO:1904954; P:canonical Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; IC:ParkinsonsUK-UCL.
GO; GO:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; TAS:ARUK-UCL.
GO; GO:0061324; P:canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation; ISS:BHF-UCL.
GO; GO:0044334; P:canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0007155; P:cell adhesion; IMP:BHF-UCL.
GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
GO; GO:0048469; P:cell maturation; IEA:Ensembl.
GO; GO:0000904; P:cell morphogenesis involved in differentiation; IEA:Ensembl.
GO; GO:0098609; P:cell-cell adhesion; IMP:BHF-UCL.
GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL.
GO; GO:0071681; P:cellular response to indole-3-methanol; IDA:UniProtKB.
GO; GO:0022009; P:central nervous system vasculogenesis; IEA:Ensembl.
GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; IEA:Ensembl.
GO; GO:0061550; P:cranial ganglion development; IEA:Ensembl.
GO; GO:1904888; P:cranial skeletal system development; IEA:Ensembl.
GO; GO:1990791; P:dorsal root ganglion development; IEA:Ensembl.
GO; GO:0009950; P:dorsal/ventral axis specification; IEA:Ensembl.
GO; GO:0007398; P:ectoderm development; IEA:Ensembl.
GO; GO:0000578; P:embryonic axis specification; IEA:Ensembl.
GO; GO:1990403; P:embryonic brain development; IEA:Ensembl.
GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl.
GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
GO; GO:0035050; P:embryonic heart tube development; IEA:Ensembl.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
GO; GO:0036023; P:embryonic skeletal limb joint morphogenesis; ISS:BHF-UCL.
GO; GO:0001711; P:endodermal cell fate commitment; IEA:Ensembl.
GO; GO:0061154; P:endothelial tube morphogenesis; IMP:BHF-UCL.
GO; GO:0035635; P:entry of bacterium into host cell; TAS:Reactome.
GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IEA:Ensembl.
GO; GO:0001837; P:epithelial to mesenchymal transition; TAS:HGNC-UCL.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
GO; GO:0061198; P:fungiform papilla formation; IEA:Ensembl.
GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
GO; GO:0035112; P:genitalia morphogenesis; IEA:Ensembl.
GO; GO:0007403; P:glial cell fate determination; IEA:Ensembl.
GO; GO:0035315; P:hair cell differentiation; TAS:BHF-UCL.
GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
GO; GO:0060789; P:hair follicle placode formation; IEA:Ensembl.
GO; GO:0030902; P:hindbrain development; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl.
GO; GO:0002089; P:lens morphogenesis in camera-type eye; IEA:Ensembl.
GO; GO:0060479; P:lung cell differentiation; IEA:Ensembl.
GO; GO:0060492; P:lung induction; IEA:Ensembl.
GO; GO:0060484; P:lung-associated mesenchyme development; IEA:Ensembl.
GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IEA:Ensembl.
GO; GO:0003338; P:metanephros morphogenesis; IEA:Ensembl.
GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; ISS:ParkinsonsUK-UCL.
GO; GO:0016525; P:negative regulation of angiogenesis; ISS:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; IEA:Ensembl.
GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; ISS:UniProtKB.
GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IEA:Ensembl.
GO; GO:0033234; P:negative regulation of protein sumoylation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0072079; P:nephron tubule formation; IEA:Ensembl.
GO; GO:0001840; P:neural plate development; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:1990138; P:neuron projection extension; IMP:UniProtKB.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0048599; P:oocyte development; IEA:Ensembl.
GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
GO; GO:0060066; P:oviduct development; IEA:Ensembl.
GO; GO:0031016; P:pancreas development; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:1904501; P:positive regulation of chromatin-mediated maintenance of transcription; IEA:Ensembl.
GO; GO:1904798; P:positive regulation of core promoter binding; IDA:BHF-UCL.
GO; GO:2000017; P:positive regulation of determination of dorsal identity; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:ParkinsonsUK-UCL.
GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IC:BHF-UCL.
GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IEA:Ensembl.
GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IGI:MGI.
GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; IMP:BHF-UCL.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IC:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:ParkinsonsUK-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IEA:Ensembl.
GO; GO:0051973; P:positive regulation of telomerase activity; IEA:Ensembl.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0034394; P:protein localization to cell surface; IMP:BHF-UCL.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
GO; GO:0045765; P:regulation of angiogenesis; TAS:BHF-UCL.
GO; GO:0090279; P:regulation of calcium ion import; IDA:BHF-UCL.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0030997; P:regulation of centriole-centriole cohesion; IDA:UniProtKB.
GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; IMP:BHF-UCL.
GO; GO:1904793; P:regulation of euchromatin binding; IEA:Ensembl.
GO; GO:0048145; P:regulation of fibroblast proliferation; TAS:BHF-UCL.
GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
GO; GO:0072182; P:regulation of nephron tubule epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0050767; P:regulation of neurogenesis; TAS:ParkinsonsUK-UCL.
GO; GO:2000008; P:regulation of protein localization to cell surface; IDA:BHF-UCL.
GO; GO:0003266; P:regulation of secondary heart field cardioblast proliferation; IEA:Ensembl.
GO; GO:0048660; P:regulation of smooth muscle cell proliferation; IMP:BHF-UCL.
GO; GO:0042129; P:regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0051884; P:regulation of timing of anagen; IEA:Ensembl.
GO; GO:0072053; P:renal inner medulla development; IEA:Ensembl.
GO; GO:0072054; P:renal outer medulla development; IEA:Ensembl.
GO; GO:0072033; P:renal vesicle formation; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEP:UniProtKB.
GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL.
GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl.
GO; GO:0019827; P:stem cell population maintenance; TAS:BHF-UCL.
GO; GO:0061549; P:sympathetic ganglion development; ISS:UniProtKB.
GO; GO:0050808; P:synapse organization; IEA:Ensembl.
GO; GO:0097091; P:synaptic vesicle clustering; IEA:Ensembl.
GO; GO:0048489; P:synaptic vesicle transport; IEA:Ensembl.
GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
GO; GO:0060440; P:trachea formation; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
DisProt; DP01119; -.
Gene3D; 1.25.10.10; -; 1.
IDEAL; IID00039; -.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000225; Armadillo.
InterPro; IPR013284; Beta-catenin.
PANTHER; PTHR45976; PTHR45976; 1.
Pfam; PF00514; Arm; 4.
PRINTS; PR01869; BCATNINFAMLY.
SMART; SM00185; ARM; 12.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50176; ARM_REPEAT; 9.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Chromosomal rearrangement; Cytoplasm;
Cytoskeleton; Disease mutation; Glycoprotein; Host-virus interaction;
Membrane; Mental retardation; Neurogenesis; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; S-nitrosylation; Synapse;
Transcription; Transcription regulation; Ubl conjugation;
Wnt signaling pathway.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000244|PubMed:22814378"
CHAIN 2..781
/note="Catenin beta-1"
/id="PRO_0000064271"
REPEAT 151..191
/note="ARM 1"
REPEAT 193..234
/note="ARM 2"
REPEAT 235..276
/note="ARM 3"
REPEAT 277..318
/note="ARM 4"
REPEAT 319..360
/note="ARM 5"
REPEAT 361..389
/note="ARM 6"
REPEAT 400..441
/note="ARM 7"
REPEAT 442..484
/note="ARM 8"
REPEAT 489..530
/note="ARM 9"
REPEAT 531..571
/note="ARM 10"
REPEAT 594..636
/note="ARM 11"
REPEAT 637..666
/note="ARM 12"
REGION 2..23
/note="Interaction with VCL"
/evidence="ECO:0000250"
REGION 156..178
/note="Interaction with BCL9"
/evidence="ECO:0000269|PubMed:17052462"
REGION 772..781
/note="Interaction with SCRIB"
/evidence="ECO:0000250"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000244|PubMed:22814378"
MOD_RES 23
/note="Phosphoserine; by GSK3-beta; alternate"
/evidence="ECO:0000269|PubMed:12027456"
MOD_RES 29
/note="Phosphoserine; by GSK3-beta"
/evidence="ECO:0000269|PubMed:12027456"
MOD_RES 33
/note="Phosphoserine; by GSK3-beta and HIPK2"
/evidence="ECO:0000269|PubMed:20307497,
ECO:0000269|PubMed:25169422"
MOD_RES 37
/note="Phosphoserine; by GSK3-beta and HIPK2"
/evidence="ECO:0000269|PubMed:20307497"
MOD_RES 41
/note="Phosphothreonine; by GSK3-beta"
/evidence="ECO:0000269|PubMed:12027456"
MOD_RES 45
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:12051714"
MOD_RES 49
/note="N6-acetyllysine"
/evidence="ECO:0000269|PubMed:24824780"
MOD_RES 64
/note="Phosphotyrosine; by PTK6"
/evidence="ECO:0000269|PubMed:20026641"
MOD_RES 86
/note="Phosphotyrosine; by CSK"
/evidence="ECO:0000269|PubMed:11279024"
MOD_RES 142
/note="Phosphotyrosine; by FYN and PTK6"
/evidence="ECO:0000269|PubMed:12640114,
ECO:0000269|PubMed:20026641"
MOD_RES 191
/note="Phosphoserine; by CDK5"
/evidence="ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569, ECO:0000269|PubMed:17009320"
MOD_RES 246
/note="Phosphoserine; by CDK5"
/evidence="ECO:0000269|PubMed:17009320"
MOD_RES 331
/note="Phosphotyrosine; by PTK6"
/evidence="ECO:0000269|PubMed:20026641"
MOD_RES 333
/note="Phosphotyrosine; by PTK6"
/evidence="ECO:0000305|PubMed:20026641"
MOD_RES 552
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569"
MOD_RES 556
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18220336"
MOD_RES 619
/note="S-nitrosocysteine"
/evidence="ECO:0000250|UniProtKB:Q02248"
MOD_RES 654
/note="Phosphotyrosine; by CSK"
/evidence="ECO:0000269|PubMed:11279024"
MOD_RES 675
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336, ECO:0000244|PubMed:20068231"
CARBOHYD 23
/note="O-linked (GlcNAc) serine; alternate"
/evidence="ECO:0000269|PubMed:24342833"
VARIANT 23
/note="S -> R (in hepatocellular carcinoma; no effect;
dbSNP:rs1413975856)"
/evidence="ECO:0000269|PubMed:10435629,
ECO:0000269|PubMed:12027456"
/id="VAR_017612"
VARIANT 25..33
/note="Missing (in hepatocellular carcinoma)"
/evidence="ECO:0000269|PubMed:10435629"
/id="VAR_017613"
VARIANT 32
/note="D -> A (in hepatocellular carcinoma;
dbSNP:rs121913396)"
/evidence="ECO:0000269|PubMed:10435629"
/id="VAR_017614"
VARIANT 32
/note="D -> G (in PTR and hepatocellular carcinoma;
dbSNP:rs121913396)"
/evidence="ECO:0000269|PubMed:10192393,
ECO:0000269|PubMed:10435629"
/id="VAR_017615"
VARIANT 32
/note="D -> Y (in PTR, hepatoblastoma and hepatocellular
carcinoma; dbSNP:rs28931588)"
/evidence="ECO:0000269|PubMed:10192393,
ECO:0000269|PubMed:10435629, ECO:0000269|PubMed:11703283,
ECO:0000269|PubMed:9927029"
/id="VAR_017616"
VARIANT 33
/note="S -> F (in PTR, MDB and hepatocellular carcinoma;
dbSNP:rs121913400)"
/evidence="ECO:0000269|PubMed:10192393,
ECO:0000269|PubMed:10435629, ECO:0000269|PubMed:10666372"
/id="VAR_017617"
VARIANT 33
/note="S -> L (in hepatocellular carcinoma)"
/evidence="ECO:0000269|PubMed:10435629"
/id="VAR_017618"
VARIANT 33
/note="S -> Y (in colorectal cancer and PTR; constitutively
active Wnt signaling pathway; enhances transactivation of
target genes; dbSNP:rs121913400)"
/evidence="ECO:0000269|PubMed:10192393,
ECO:0000269|PubMed:12027456, ECO:0000269|PubMed:29374064,
ECO:0000269|PubMed:9065402"
/id="VAR_017619"
VARIANT 34
/note="G -> E (in PTR; dbSNP:rs28931589)"
/evidence="ECO:0000269|PubMed:10192393"
/id="VAR_017620"
VARIANT 34
/note="G -> R (in hepatocellular carcinoma;
dbSNP:rs121913399)"
/evidence="ECO:0000269|PubMed:10435629"
/id="VAR_017621"
VARIANT 34
/note="G -> V (in hepatoblastoma; dbSNP:rs28931589)"
/evidence="ECO:0000269|PubMed:9927029"
/id="VAR_017622"
VARIANT 35
/note="I -> S (in hepatocellular carcinoma)"
/evidence="ECO:0000269|PubMed:10435629"
/id="VAR_017623"
VARIANT 37..38
/note="SG -> W (in hepatocellular carcinoma)"
/evidence="ECO:0000269|PubMed:10435629"
/id="VAR_017628"
VARIANT 37
/note="S -> A (in MDB and hepatocellular carcinoma;
enhances transactivation of target genes;
dbSNP:rs121913228)"
/evidence="ECO:0000269|PubMed:10435629,
ECO:0000269|PubMed:10666372, ECO:0000269|PubMed:12027456"
/id="VAR_017624"
VARIANT 37
/note="S -> C (in PTR, hepatoblastoma and ovarian cancer;
dbSNP:rs121913403)"
/evidence="ECO:0000269|PubMed:10192393,
ECO:0000269|PubMed:10391090, ECO:0000269|PubMed:9927029"
/id="VAR_017625"
VARIANT 37
/note="S -> F (in PTR; dbSNP:rs121913403)"
/evidence="ECO:0000269|PubMed:10192393"
/id="VAR_017626"
VARIANT 37
/note="S -> Y (in hepatocellular carcinoma;
dbSNP:rs121913403)"
/evidence="ECO:0000269|PubMed:10435629"
/id="VAR_017627"
VARIANT 41
/note="T -> A (in hepatoblastoma and hepatocellular
carcinoma; also in a desmoid tumor; strongly reduces
phosphorylation and degradation; abolishes phosphorylation
on Ser-33 and Ser-37 and enhances transactivation of target
genes; dbSNP:rs121913412)"
/evidence="ECO:0000269|PubMed:10391090,
ECO:0000269|PubMed:10398436, ECO:0000269|PubMed:10435629,
ECO:0000269|PubMed:10655994, ECO:0000269|PubMed:12027456,
ECO:0000269|PubMed:12051714, ECO:0000269|PubMed:9927029"
/id="VAR_017629"
VARIANT 41
/note="T -> I (in PTR, hepatocellular carcinoma and ovarian
cancer; dbSNP:rs121913413)"
/evidence="ECO:0000269|PubMed:10192393,
ECO:0000269|PubMed:10391090, ECO:0000269|PubMed:10435629"
/id="VAR_017630"
VARIANT 45
/note="S -> F (in hepatocellular carcinoma;
dbSNP:rs121913409)"
/evidence="ECO:0000269|PubMed:10435629"
/id="VAR_017631"
VARIANT 45
/note="S -> P (in hepatocellular carcinoma;
dbSNP:rs121913407)"
/evidence="ECO:0000269|PubMed:10435629"
/id="VAR_017632"
VARIANT 45
/note="Missing (in colorectal cancer)"
/evidence="ECO:0000269|PubMed:9065402"
/id="VAR_055430"
VARIANT 388
/note="L -> P (in NEDSDV)"
/evidence="ECO:0000269|PubMed:25326669"
/id="VAR_072282"
VARIANT 558..781
/note="Missing (in NEDSDV; the patient also manifest
features of exudative vitreoretinopathy)"
/evidence="ECO:0000269|PubMed:28514307"
/id="VAR_079199"
VARIANT 688
/note="M -> V (in dbSNP:rs4135384)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_018954"
VARIANT 710
/note="R -> C (in EVR7; unknown pathological significance;
dbSNP:rs748653573)"
/evidence="ECO:0000269|PubMed:28575650"
/id="VAR_079200"
MUTAGEN 29
/note="S->F: No effect."
/evidence="ECO:0000269|PubMed:12027456"
MUTAGEN 64
/note="Y->F: Abolishes phosphorylation by PTK6."
/evidence="ECO:0000269|PubMed:20026641"
MUTAGEN 142
/note="Y->E: No effect on interaction with BCL9 and BCL9L."
/evidence="ECO:0000269|PubMed:17052462"
MUTAGEN 156
/note="L->A: Abolishes interaction with BCL9 but no effect
on interaction with CDH3; when associated with A-159."
/evidence="ECO:0000269|PubMed:17052462"
MUTAGEN 159
/note="L->A: No effect on interaction with BCL9 and CDH3.
Abolishes interaction with BCL9 but no effect on
interaction with CDH3; when associated with A-156."
/evidence="ECO:0000269|PubMed:17052462"
MUTAGEN 178
/note="L->A: No effect on interaction with BCL9 and CDH3."
/evidence="ECO:0000269|PubMed:17052462"
MUTAGEN 253
/note="F->A: Abolishes or strongly reduces AXIN2 binding."
/evidence="ECO:0000269|PubMed:10966653"
MUTAGEN 260
/note="H->A: Abolishes or strongly reduces AXIN1 and AXIN2
binding. Strongly reduces phosphorylation and degradation;
when associated with A-386 and A-383."
/evidence="ECO:0000269|PubMed:10966653"
MUTAGEN 292
/note="K->A: Abolishes or strongly reduces AXIN1 and AXIN2
binding."
/evidence="ECO:0000269|PubMed:10966653"
MUTAGEN 312
/note="K->E: Abolishes TCF7L2 binding."
/evidence="ECO:0000269|PubMed:11713475"
MUTAGEN 345
/note="K->A: Abolishes APC binding."
/evidence="ECO:0000269|PubMed:10966653"
MUTAGEN 383
/note="W->A: Abolishes APC binding. Strongly reduces
phosphorylation and degradation; when associated with A-260
and A-386."
/evidence="ECO:0000269|PubMed:10966653"
MUTAGEN 386
/note="R->A: Strongly reduces APC binding. Strongly reduces
phosphorylation and degradation; when associated with A-260
and A-383."
/evidence="ECO:0000269|PubMed:10966653"
MUTAGEN 426
/note="N->A: Abolishes TCF7L2 and LEF1 binding."
/evidence="ECO:0000269|PubMed:10966653"
MUTAGEN 435
/note="K->A: Strongly reduces or abolishes LEF1 binding."
/evidence="ECO:0000269|PubMed:10966653,
ECO:0000269|PubMed:11713475"
MUTAGEN 435
/note="K->E: Abolishes TCF7L2 binding."
/evidence="ECO:0000269|PubMed:10966653,
ECO:0000269|PubMed:11713475"
MUTAGEN 469
/note="R->A: Abolishes TCF7L2 binding, and strongly reduces
or abolishes LEF1 binding."
/evidence="ECO:0000269|PubMed:10966653"
MUTAGEN 470
/note="H->A: Abolishes TCF7L2 binding, and strongly reduces
or abolishes LEF1 binding."
/evidence="ECO:0000269|PubMed:10966653"
MUTAGEN 508
/note="K->A: Abolishes TCF7L2 and LEF1 binding."
/evidence="ECO:0000269|PubMed:10966653"
MUTAGEN 654
/note="Y->E: Enhances TBP binding and transactivation of
target genes."
/evidence="ECO:0000269|PubMed:11279024"
MUTAGEN 654
/note="Y->F: Abolishes increase of TBP binding after
phosphorylation by CSK."
/evidence="ECO:0000269|PubMed:11279024"
MUTAGEN 660
/note="F->A: Abolishes CTNNBIP1 binding; when associated
with A-661."
/evidence="ECO:0000269|PubMed:12408824"
MUTAGEN 661
/note="R->A: Abolishes CTNNBIP1 binding; when associated
with A-660."
/evidence="ECO:0000269|PubMed:12408824"
HELIX 135..150
/evidence="ECO:0000244|PDB:1G3J"
HELIX 152..160
/evidence="ECO:0000244|PDB:1JDH"
HELIX 165..179
/evidence="ECO:0000244|PDB:1JDH"
HELIX 182..189
/evidence="ECO:0000244|PDB:1JDH"
HELIX 192..204
/evidence="ECO:0000244|PDB:1JDH"
HELIX 208..221
/evidence="ECO:0000244|PDB:1JDH"
HELIX 225..233
/evidence="ECO:0000244|PDB:1JDH"
HELIX 236..243
/evidence="ECO:0000244|PDB:1JDH"
HELIX 249..265
/evidence="ECO:0000244|PDB:1JDH"
HELIX 269..276
/evidence="ECO:0000244|PDB:1JDH"
HELIX 278..284
/evidence="ECO:0000244|PDB:1JDH"
HELIX 285..287
/evidence="ECO:0000244|PDB:1JDH"
HELIX 291..305
/evidence="ECO:0000244|PDB:1JDH"
HELIX 309..317
/evidence="ECO:0000244|PDB:1JDH"
HELIX 320..330
/evidence="ECO:0000244|PDB:1JDH"
HELIX 334..347
/evidence="ECO:0000244|PDB:1JDH"
HELIX 353..359
/evidence="ECO:0000244|PDB:1JDH"
HELIX 362..367
/evidence="ECO:0000244|PDB:1JDH"
TURN 368..371
/evidence="ECO:0000244|PDB:1JDH"
HELIX 375..389
/evidence="ECO:0000244|PDB:1JDH"
HELIX 399..408
/evidence="ECO:0000244|PDB:1JDH"
HELIX 414..427
/evidence="ECO:0000244|PDB:1JDH"
TURN 428..430
/evidence="ECO:0000244|PDB:1JDH"
HELIX 432..440
/evidence="ECO:0000244|PDB:1JDH"
HELIX 443..454
/evidence="ECO:0000244|PDB:1JDH"
HELIX 458..471
/evidence="ECO:0000244|PDB:1JDH"
STRAND 473..475
/evidence="ECO:0000244|PDB:1JDH"
HELIX 478..487
/evidence="ECO:0000244|PDB:1JDH"
HELIX 491..496
/evidence="ECO:0000244|PDB:1JDH"
STRAND 499..501
/evidence="ECO:0000244|PDB:4DJS"
HELIX 504..517
/evidence="ECO:0000244|PDB:1JDH"
HELIX 521..523
/evidence="ECO:0000244|PDB:1JDH"
HELIX 524..529
/evidence="ECO:0000244|PDB:1JDH"
HELIX 532..547
/evidence="ECO:0000244|PDB:1JDH"
STRAND 550..552
/evidence="ECO:0000244|PDB:1QZ7"
STRAND 554..557
/evidence="ECO:0000244|PDB:1QZ7"
STRAND 561..563
/evidence="ECO:0000244|PDB:1T08"
HELIX 566..580
/evidence="ECO:0000244|PDB:1JDH"
HELIX 584..592
/evidence="ECO:0000244|PDB:1JDH"
HELIX 596..601
/evidence="ECO:0000244|PDB:1JDH"
HELIX 602..604
/evidence="ECO:0000244|PDB:1JDH"
HELIX 608..621
/evidence="ECO:0000244|PDB:1JDH"
HELIX 625..633
/evidence="ECO:0000244|PDB:1JDH"
HELIX 637..642
/evidence="ECO:0000244|PDB:1JDH"
HELIX 643..645
/evidence="ECO:0000244|PDB:1JDH"
HELIX 649..662
/evidence="ECO:0000244|PDB:1JDH"
TURN 663..665
/evidence="ECO:0000244|PDB:2Z6H"
HELIX 668..682
/evidence="ECO:0000244|PDB:2Z6H"
HELIX 688..690
/evidence="ECO:0000244|PDB:2Z6H"
STRAND 778..780
/evidence="ECO:0000244|PDB:3DIW"
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


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U1021h CLIA Beta-catenin,Catenin beta-1,CTNNB,CTNNB1,Homo sapiens,Human,OK_SW-cl.35,PRO2286 96T
bs-2063P Peptides: p- Beta catenin(p-beta Catenin(phosphor-Y142)) Protein Length:12-25 amino acids. 200ug lyophilized
20-321-175182 BETA-CATENIN - MONOCLONAL ANTIBODY TO HUMAN BETA-CATENIN; Beta-catenin Monoclonal 0.1 mg
20-272-191813 beta Catenin - Mouse monoclonal [BDI920] to beta Catenin; Beta-catenin Monoclonal 0.05 mg
20-272-191814 beta Catenin - Mouse monoclonal [BDI710] to beta Catenin; Beta-catenin Monoclonal 0.05 mg
20-272-190467 beta Catenin ( Cy3 ) - Mouse monoclonal [15B8] to beta Catenin ( Cy3 ); Beta-catenin Monoclonal 0.1 ml
E1021r ELISA kit Beta-catenin,Catenin beta-1,Catnb,Ctnnb1,Rat,Rattus norvegicus 96T
E1021m ELISA Beta-catenin,Catenin beta-1,Catnb,Ctnnb1,Mouse,Mus musculus 96T
E1021r ELISA Beta-catenin,Catenin beta-1,Catnb,Ctnnb1,Rat,Rattus norvegicus 96T
E1021m ELISA kit Beta-catenin,Catenin beta-1,Catnb,Ctnnb1,Mouse,Mus musculus 96T
U1021m CLIA Beta-catenin,Catenin beta-1,Catnb,Ctnnb1,Mouse,Mus musculus 96T
U1021r CLIA Beta-catenin,Catenin beta-1,Catnb,Ctnnb1,Rat,Rattus norvegicus 96T
U1021b CLIA Beta-catenin,Bos taurus,Bovine,Catenin beta-1,CTNNB1 96T
E1021b ELISA Beta-catenin,Bos taurus,Bovine,Catenin beta-1,CTNNB1 96T
E1021b ELISA kit Beta-catenin,Bos taurus,Bovine,Catenin beta-1,CTNNB1 96T
18-785-210043 beta-Catenin (Phospho-Ser33) - Beta-catenin Polyclonal 0.1 mg
18-785-210044 beta-Catenin (Phospho-Ser37) - Beta-catenin Polyclonal 0.1 mg
18-785-210041 beta-Catenin (Phospho-Thr41_Ser45) - Beta-catenin Polyclonal 0.05 mg
18-785-210041 beta-Catenin (Phospho-Thr41_Ser45) - Beta-catenin Polyclonal 0.1 mg
18-785-210044 beta-Catenin (Phospho-Ser37) - Beta-catenin Polyclonal 0.05 mg
18-785-210043 beta-Catenin (Phospho-Ser33) - Beta-catenin Polyclonal 0.05 mg
Pathways :
WP566: canonical wnt - zebrafish
WP215: noncanonical wnt pathway
WP249: Beta Oxidation of Unsaturated Fatty Acids
WP763: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1045: TGF-beta Receptor Signaling Pathway
WP1835: Interferon alpha/beta signaling
WP433: tRNA Synthetases
WP126: Fatty Acid Beta Oxidation 1
WP471: Beta Oxidation of Unsaturated Fatty Acids
WP1367: TGF-beta Receptor Signaling Pathway
WP262: EBV LMP1 signaling
WP825: Fatty Acid Beta Oxidation
WP1058: Senescence and Autophagy
WP1904: RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways
WP930: TGF Beta Signaling Pathway
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1982: SREBP signalling
WP499: Fatty Acid Beta Oxidation 3
WP1434: Osteopontin Signaling
WP32: Translation Factors
WP1566: Citrate cycle (TCA cycle)
WP368: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP989: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1164: TGF Beta Signaling Pathway
WP210: Cytoplasmic Ribosomal Proteins

Related Genes :
[CTNNB1 CTNNB OK/SW-cl.35 PRO2286] Catenin beta-1 (Beta-catenin)
[Ctnnb1 Catnb] Catenin beta-1 (Beta-catenin)
[Ctnnb1 Catnb] Catenin beta-1 (Beta-catenin)
[CTNNB1] Catenin beta-1 (Beta-catenin)
[CTNNB1] Catenin beta-1 (Beta-catenin)
[hmp-2 K05C4.6] Beta-catenin-like protein hmp-2 (Protein humpback-2)
[Ctnna1 Catna1] Catenin alpha-1 (102 kDa cadherin-associated protein) (Alpha E-catenin) (CAP102)
[CTNNA1] Catenin alpha-1 (Alpha E-catenin) (Cadherin-associated protein) (Renal carcinoma antigen NY-REN-13)
[CTNND1 KIAA0384] Catenin delta-1 (Cadherin-associated Src substrate) (CAS) (p120 catenin) (p120(ctn)) (p120(cas))
[Arhgap32 Grit Kiaa0712 Rics] Rho GTPase-activating protein 32 (Brain-specific Rho GTPase-activating protein) (GAB-associated Cdc42/Rac GTPase-activating protein) (GC-GAP) (Rho-type GTPase-activating protein 32) (Rho/Cdc42/Rac GTPase-activating protein RICS) (RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling) (p200RhoGAP) (p250GAP)
[DACT3 RRR1] Dapper homolog 3 (Antagonist of beta-catenin Dapper homolog 3) (Arginine-rich region 1 protein) (Dapper antagonist of catenin 3)
[CTNNA2 CAPR] Catenin alpha-2 (Alpha N-catenin) (Alpha-catenin-related protein)
[CTNND2 NPRAP] Catenin delta-2 (Delta-catenin) (GT24) (Neural plakophilin-related ARM-repeat protein) (NPRAP) (Neurojungin)
[] Testis cDNA clone: QtsA-17763, similar to human catenin (cadherin-associated protein), beta 1, 88kDa(CTNNB1)
[DACT1 DPR1 HNG3] Dapper homolog 1 (hDPR1) (Dapper antagonist of catenin 1) (Hepatocellular carcinoma novel gene 3 protein)
[Dact1 Thyex3] Dapper homolog 1 (Dapper antagonist of catenin 1) (Frodo homolog) (MDpr1) (Thymus-expressed novel gene 3 protein)
[Ctnna1 Catna1 rCG_49560] Catenin (Cadherin associated protein), alpha 1 (Catenin (Cadherin-associated protein), alpha 1, isoform CRA_b) (Catenin alpha 1)
[Dact2 Dpr2 Frd2] Dapper homolog 2 (mDpr2) (Dapper antagonist of catenin 2)
[JUP CTNNG DP3] Junction plakoglobin (Catenin gamma) (Desmoplakin III) (Desmoplakin-3)
[Ctnnd2 Catnd2 Nprap] Catenin delta-2 (Neural plakophilin-related ARM-repeat protein) (NPRAP) (Neurojungin)
[Ctnnd2] Catenin delta-2 (Fragment)
[ctnnA vcl vinA DDB_G0285939] Probable vinculin (Ddalpha-catenin)
[Ctnna1] Catenin alpha 1
[hmp-2 CELE_K05C4.6 K05C4.6] Beta-catenin-like protein hmp-2
[Dact3] Dapper homolog 3 (Dapper antagonist of catenin 3)
[MUC1 PUM] Mucin-1 (MUC-1) (Breast carcinoma-associated antigen DF3) (Cancer antigen 15-3) (CA 15-3) (Carcinoma-associated mucin) (Episialin) (H23AG) (Krebs von den Lungen-6) (KL-6) (PEMT) (Peanut-reactive urinary mucin) (PUM) (Polymorphic epithelial mucin) (PEM) (Tumor-associated epithelial membrane antigen) (EMA) (Tumor-associated mucin) (CD antigen CD227) [Cleaved into: Mucin-1 subunit alpha (MUC1-NT) (MUC1-alpha); Mucin-1 subunit beta (MUC1-beta) (MUC1-CT)]
[Muc1 Muc-1] Mucin-1 (MUC-1) (Episialin) (CD antigen CD227) [Cleaved into: Mucin-1 subunit alpha (MUC1-NT) (MUC1-alpha); Mucin-1 subunit beta (MUC1-beta) (MUC1-CT)]
[MUC1] Mucin-1 (MUC-1) (CD antigen CD227) [Cleaved into: Mucin-1 subunit alpha (MUC1-NT) (MUC1-alpha); Mucin-1 subunit beta (MUC1-beta) (MUC1-CT)]
[PPP2R1B] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (PP2A subunit A isoform PR65-beta) (PP2A subunit A isoform R1-beta)
[GSK3B] Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1)

Bibliography :
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