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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.
25-OCT-2017, entry version 218.
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] (ISOFORM 1).
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] (ISOFORM 2).
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] (ISOFORM 1).
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] (ISOFORM 1).
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 (ISOFORM 1).
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 (ISOFORM 1).
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 DEGRADATION.
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 DEGRADATION.
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]
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).
[51]
PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2.
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).
[52]
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).
[53]
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).
[54]
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).
[55]
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).
[56]
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).
[57]
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).
[58]
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).
[59]
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).
[60]
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).
[61]
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).
[62]
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).
[63]
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).
[64]
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).
[65]
INVOLVEMENT IN MRD19.
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).
[66]
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).
[67]
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).
[68]
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).
[69]
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).
[70]
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).
[71]
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).
[72]
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).
[73]
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).
[74]
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).
[75]
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).
[76]
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).
[77]
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).
[78]
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).
[79]
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).
[80]
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).
[81]
VARIANT HEPATOBLASTOMA ALA-41.
PubMed=10398436;
DOI=10.1002/(SICI)1098-2264(199908)25:4<399::AID-GCC14>3.3.CO;2-O;
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).
[82]
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).
[83]
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).
[84]
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).
[85]
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).
[86]
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).
[87]
VARIANT MRD19 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).
-!- FUNCTION: Key downstream component of the canonical Wnt signaling
pathway. 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. 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.
Involved in the regulation of cell adhesion, as component of an E-
cadherin:catenin adhesion complex. Acts as a negative regulator of
centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1
pathway of insulin internalization. Blocks anoikis of malignant
kidney and intestinal epithelial cells and promotes their
anchorage-independent growth by down-regulating DAPK2. Disrupts
PML function and PML-NB formation by inhibiting RANBP2-mediated
sumoylation of PML (PubMed:17524503, PubMed:18077326,
PubMed:18086858, PubMed:18957423, PubMed:21262353,
PubMed:22647378, PubMed:22699938, PubMed:22155184). Promotes
neurogenesis by maintaining sympathetic neuroblasts within the
cell cycle (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. 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). {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: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: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:7982500}.
-!- INTERACTION:
P00519:ABL1; NbExp=2; IntAct=EBI-491549, EBI-375543;
O43707:ACTN4; NbExp=7; IntAct=EBI-491549, EBI-351526;
Q5JTC6:AMER1; NbExp=9; IntAct=EBI-491549, EBI-6169747;
P25054:APC; NbExp=17; IntAct=EBI-491549, EBI-727707;
P10275:AR; NbExp=11; IntAct=EBI-491549, EBI-608057;
O15169:AXIN1; NbExp=44; IntAct=EBI-491549, EBI-710484;
O35625:Axin1 (xeno); NbExp=4; IntAct=EBI-491549, EBI-2365912;
Q9YGY0:axin1 (xeno); NbExp=2; IntAct=EBI-491549, EBI-1037449;
Q9Y2T1:AXIN2; NbExp=2; IntAct=EBI-491549, EBI-4400025;
O00512:BCL9; NbExp=2; IntAct=EBI-491549, EBI-533127;
A1Z199:BCR/ABL fusion; NbExp=2; IntAct=EBI-491549, EBI-7286259;
Q9Y297:BTRC; NbExp=8; IntAct=EBI-491549, EBI-307461;
P33724:CAV1 (xeno); NbExp=5; IntAct=EBI-491549, EBI-79998;
Q6P1J9:CDC73; NbExp=9; IntAct=EBI-491549, EBI-930143;
P12830:CDH1; NbExp=14; IntAct=EBI-491549, EBI-727477;
P19022:CDH2; NbExp=8; IntAct=EBI-491549, EBI-2256711;
P33151:CDH5; NbExp=6; IntAct=EBI-491549, EBI-2903122;
Q92793:CREBBP; NbExp=2; IntAct=EBI-491549, EBI-81215;
P35221:CTNNA1; NbExp=3; IntAct=EBI-491549, EBI-701918;
P26231:Ctnna1 (xeno); NbExp=2; IntAct=EBI-491549, EBI-647895;
Q9NSA3:CTNNBIP1; NbExp=10; IntAct=EBI-491549, EBI-747082;
Q9NYF0:DACT1; NbExp=3; IntAct=EBI-491549, EBI-3951744;
P18146:EGR1; NbExp=7; IntAct=EBI-491549, EBI-2834611;
P50402:EMD; NbExp=3; IntAct=EBI-491549, EBI-489887;
P29317:EPHA2; NbExp=2; IntAct=EBI-491549, EBI-702104;
Q9UKB1:FBXW11; NbExp=4; IntAct=EBI-491549, EBI-355189;
Q96AC1:FERMT2; NbExp=13; IntAct=EBI-491549, EBI-4399465;
P11362:FGFR1; NbExp=2; IntAct=EBI-491549, EBI-1028277;
P49789:FHIT; NbExp=4; IntAct=EBI-491549, EBI-741760;
P17948:FLT1; NbExp=2; IntAct=EBI-491549, EBI-1026718;
Q08050:FOXM1; NbExp=16; IntAct=EBI-491549, EBI-866480;
Q9BZE0:GLIS2; NbExp=6; IntAct=EBI-491549, EBI-7251368;
P49841:GSK3B; NbExp=16; IntAct=EBI-491549, EBI-373586;
P42858:HTT; NbExp=5; IntAct=EBI-491549, EBI-466029;
P08069:IGF1R; NbExp=3; IntAct=EBI-491549, EBI-475981;
P18012:ipaC (xeno); NbExp=4; IntAct=EBI-491563, EBI-491541;
P46940:IQGAP1; NbExp=3; IntAct=EBI-491549, EBI-297509;
O75564:JRK; NbExp=3; IntAct=EBI-491549, EBI-8607681;
P14923:JUP; NbExp=3; IntAct=EBI-491549, EBI-702484;
Q14678:KANK1; NbExp=2; IntAct=EBI-491549, EBI-2556221;
Q2LD37:KIAA1109; NbExp=2; IntAct=EBI-491549, EBI-2683809;
Q9UJU2:LEF1; NbExp=9; IntAct=EBI-491549, EBI-926131;
P27782:Lef1 (xeno); NbExp=2; IntAct=EBI-491549, EBI-984464;
Q8WVC0:LEO1; NbExp=2; IntAct=EBI-491549, EBI-932432;
Q9JHQ5:Lztfl1 (xeno); NbExp=2; IntAct=EBI-491549, EBI-6142879;
Q9GZQ8:MAP1LC3B; NbExp=5; IntAct=EBI-491549, EBI-373144;
P55197:MLLT10; NbExp=4; IntAct=EBI-491549, EBI-1104952;
P19838:NFKB1; NbExp=3; IntAct=EBI-491549, EBI-300010;
P29474:NOS3; NbExp=4; IntAct=EBI-491549, EBI-1391623;
O00482-1:NR5A2; NbExp=5; IntAct=EBI-491549, EBI-15960777;
P49757:NUMB; NbExp=2; IntAct=EBI-491549, EBI-915016;
P49757-3:NUMB; NbExp=3; IntAct=EBI-491549, EBI-10692196;
Q8TEW0:PARD3; NbExp=2; IntAct=EBI-491549, EBI-81968;
P16284:PECAM1; NbExp=3; IntAct=EBI-491549, EBI-716404;
Q99697:PITX2; NbExp=2; IntAct=EBI-491549, EBI-1175211;
P14618:PKM; NbExp=4; IntAct=EBI-491549, EBI-353408;
P14618-1:PKM; NbExp=3; IntAct=EBI-491549, EBI-4304679;
P49768:PSEN1; NbExp=2; IntAct=EBI-491549, EBI-297277;
Q03431:PTH1R; NbExp=4; IntAct=EBI-491549, EBI-2860297;
Q13308:PTK7; NbExp=5; IntAct=EBI-491549, EBI-2803245;
P08575:PTPRC; NbExp=2; IntAct=EBI-491549, EBI-1341;
P23470:PTPRG; NbExp=2; IntAct=EBI-491549, EBI-2258115;
Q12913:PTPRJ; NbExp=2; IntAct=EBI-491549, EBI-2264500;
P49023:PXN; NbExp=4; IntAct=EBI-491549, EBI-702209;
Q04206:RELA; NbExp=3; IntAct=EBI-491549, EBI-73886;
Q13761:RUNX3; NbExp=12; IntAct=EBI-491549, EBI-925990;
Q9Y265:RUVBL1; NbExp=3; IntAct=EBI-491549, EBI-353675;
Q01887:Ryk (xeno); NbExp=2; IntAct=EBI-491549, EBI-16110594;
Q01826:SATB1; NbExp=9; IntAct=EBI-491549, EBI-743747;
P63208:SKP1; NbExp=3; IntAct=EBI-491549, EBI-307486;
Q9H6I2:SOX17; NbExp=2; IntAct=EBI-491549, EBI-9106753;
P12931:SRC; NbExp=2; IntAct=EBI-491549, EBI-621482;
P15884:TCF4; NbExp=21; IntAct=EBI-491549, EBI-533224;
P36402:TCF7; NbExp=4; IntAct=EBI-491549, EBI-2119465;
Q9NQB0:TCF7L2; NbExp=34; IntAct=EBI-491549, EBI-924724;
O14746:TERT; NbExp=2; IntAct=EBI-491549, EBI-1772203;
Q9UKE5:TNIK; NbExp=3; IntAct=EBI-491549, EBI-1051794;
P11388:TOP2A; NbExp=5; IntAct=EBI-491549, EBI-539628;
Q13625:TP53BP2; NbExp=5; IntAct=EBI-491549, EBI-77642;
O95071:UBR5; NbExp=6; IntAct=EBI-491549, EBI-358329;
Q9GZV5:WWTR1; NbExp=4; IntAct=EBI-491549, EBI-747743;
Q9EPK5:Wwtr1 (xeno); NbExp=2; IntAct=EBI-491549, EBI-1211920;
P46937:YAP1; NbExp=13; IntAct=EBI-491549, EBI-1044059;
P46937-3:YAP1; NbExp=2; IntAct=EBI-491549, EBI-6558686;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25183871}.
Nucleus {ECO:0000269|PubMed:24342833,
ECO:0000269|PubMed:25183871}. 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}. 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P35222-1; Sequence=Displayed;
Name=2;
IsoId=P35222-2; Sequence=VSP_006984, VSP_006985, VSP_006986;
Note=No experimental confirmation available.;
-!- 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). {ECO:0000269|PubMed:11703283,
ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:17289029}.
-!- 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. Ubiquitinated
by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1,
CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent
proteasomal degradation (By similarity). {ECO:0000250}.
-!- 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: Mental retardation, autosomal dominant 19 (MRD19)
[MIM:615075]: A disorder characterized by significantly below
average general intellectual functioning associated with
impairments in adaptive behavior and manifested during the
developmental period. MRD19 features include severe intellectual
disability with absent or very limited speech, microcephaly, and
spasticity which severely impaired the ability to walk.
{ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:25326669}.
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=BAB93475.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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; -; 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; -. [P35222-1]
PIR; A38973; A38973.
RefSeq; NP_001091679.1; NM_001098209.1. [P35222-1]
RefSeq; NP_001091680.1; NM_001098210.1. [P35222-1]
RefSeq; NP_001895.1; NM_001904.3. [P35222-1]
RefSeq; XP_005264943.1; XM_005264886.2. [P35222-1]
RefSeq; XP_016861227.1; XM_017005738.1. [P35222-1]
UniGene; Hs.476018; -.
UniGene; Hs.712929; -.
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.
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; -.
ProteinModelPortal; P35222; -.
SMR; P35222; -.
BioGrid; 107880; 320.
CORUM; P35222; -.
DIP; DIP-122N; -.
IntAct; P35222; 215.
MINT; MINT-105089; -.
STRING; 9606.ENSP00000344456; -.
BindingDB; P35222; -.
ChEMBL; CHEMBL5866; -.
DrugBank; DB03904; Urea.
iPTMnet; P35222; -.
PhosphoSitePlus; P35222; -.
SwissPalm; P35222; -.
BioMuta; CTNNB1; -.
DMDM; 461854; -.
EPD; P35222; -.
MaxQB; P35222; -.
PaxDb; P35222; -.
PeptideAtlas; P35222; -.
PRIDE; P35222; -.
DNASU; 1499; -.
Ensembl; ENST00000349496; ENSP00000344456; ENSG00000168036. [P35222-1]
Ensembl; ENST00000396183; ENSP00000379486; ENSG00000168036. [P35222-1]
Ensembl; ENST00000396185; ENSP00000379488; ENSG00000168036. [P35222-1]
Ensembl; ENST00000405570; ENSP00000385604; ENSG00000168036. [P35222-1]
GeneID; 1499; -.
KEGG; hsa:1499; -.
UCSC; uc003ckp.3; human. [P35222-1]
CTD; 1499; -.
DisGeNET; 1499; -.
EuPathDB; HostDB:ENSG00000168036.16; -.
GeneCards; CTNNB1; -.
H-InvDB; HIX0163439; -.
H-InvDB; HIX0163473; -.
HGNC; HGNC:2514; CTNNB1.
HPA; CAB000108; -.
HPA; CAB001950; -.
HPA; HPA029159; -.
HPA; HPA029160; -.
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.
neXtProt; NX_P35222; -.
OpenTargets; ENSG00000168036; -.
Orphanet; 85142; Aldosterone-producing adenoma.
Orphanet; 54595; Craniopharyngioma.
Orphanet; 873; Desmoid tumor.
Orphanet; 91414; Pilomatrixoma.
Orphanet; 404473; Severe intellectual disability-progressive spastic diplegia syndrome.
PharmGKB; PA27013; -.
eggNOG; KOG4203; Eukaryota.
eggNOG; COG0035; LUCA.
GeneTree; ENSGT00730000110821; -.
HOGENOM; HOG000230958; -.
HOVERGEN; HBG000919; -.
InParanoid; P35222; -.
KO; K02105; -.
OMA; WEQGFNQ; -.
OrthoDB; EOG091G03A5; -.
PhylomeDB; P35222; -.
TreeFam; TF317997; -.
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-375170; CDO in myogenesis.
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-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-8876493; InlA-mediated entry of Listeria monocytogenes into host cells.
Reactome; R-HSA-8951430; RUNX3 regulates WNT signaling.
SignaLink; P35222; -.
SIGNOR; P35222; -.
ChiTaRS; CTNNB1; human.
EvolutionaryTrace; P35222; -.
GeneWiki; Beta-catenin; -.
GenomeRNAi; 1499; -.
PMAP-CutDB; P35222; -.
PRO; PR:P35222; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000168036; -.
CleanEx; HS_CTNNB1; -.
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; IPI:FlyBase.
GO; GO:0070369; C:beta-catenin-TCF7L2 complex; IDA:BHF-UCL.
GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
GO; GO:0016342; C:catenin complex; IDA:BHF-UCL.
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:0005913; C:cell-cell adherens junction; IDA:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
GO; GO:0016600; C:flotillin complex; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
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:0043234; C:protein complex; IDA:MGI.
GO; GO:0032993; C:protein-DNA complex; IDA:UniProtKB.
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 factor 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:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; 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:0046982; F:protein heterodimerization activity; IEA:Ensembl.
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:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0004871; F:signal transducer activity; NAS:ProtInc.
GO; GO:0046332; F:SMAD binding; IPI:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
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: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; IMP:BHF-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:0035411; P:catenin import into nucleus; TAS:Reactome.
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.
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:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0060548; P:negative regulation of cell death; TAS:ARUK-UCL.
GO; GO:0008285; P:negative regulation of cell 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 from RNA polymerase II promoter; 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: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:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:ParkinsonsUK-UCL.
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 from RNA polymerase II promoter; 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; TAS:Reactome.
GO; GO:0034394; P:protein localization to cell surface; IMP:BHF-UCL.
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: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: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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000225; Armadillo.
InterPro; IPR013284; Beta-catenin.
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; Alternative splicing;
Cell adhesion; Cell junction; Cell membrane;
Chromosomal rearrangement; Complete proteome; Cytoplasm; Cytoskeleton;
Disease mutation; Glycoprotein; Membrane; Mental retardation;
Neurogenesis; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; S-nitrosylation; Synapse; Transcription;
Transcription regulation; Ubl conjugation; Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 781 Catenin beta-1.
/FTId=PRO_0000064271.
REPEAT 151 191 ARM 1.
REPEAT 193 234 ARM 2.
REPEAT 235 276 ARM 3.
REPEAT 277 318 ARM 4.
REPEAT 319 360 ARM 5.
REPEAT 361 389 ARM 6.
REPEAT 400 441 ARM 7.
REPEAT 442 484 ARM 8.
REPEAT 489 530 ARM 9.
REPEAT 531 571 ARM 10.
REPEAT 594 636 ARM 11.
REPEAT 637 666 ARM 12.
REGION 2 23 Interaction with VCL. {ECO:0000250}.
REGION 156 178 Interaction with BCL9.
{ECO:0000269|PubMed:17052462}.
REGION 772 781 Interaction with SCRIB. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 23 23 Phosphoserine; by GSK3-beta; alternate.
{ECO:0000269|PubMed:12027456}.
MOD_RES 29 29 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:12027456}.
MOD_RES 33 33 Phosphoserine; by GSK3-beta and HIPK2.
{ECO:0000269|PubMed:20307497,
ECO:0000269|PubMed:25169422}.
MOD_RES 37 37 Phosphoserine; by GSK3-beta and HIPK2.
{ECO:0000269|PubMed:20307497}.
MOD_RES 41 41 Phosphothreonine; by GSK3-beta.
{ECO:0000269|PubMed:12027456}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000269|PubMed:12051714}.
MOD_RES 49 49 N6-acetyllysine.
{ECO:0000269|PubMed:24824780}.
MOD_RES 64 64 Phosphotyrosine; by PTK6.
{ECO:0000269|PubMed:20026641}.
MOD_RES 86 86 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:11279024}.
MOD_RES 142 142 Phosphotyrosine; by FYN and PTK6.
{ECO:0000269|PubMed:12640114,
ECO:0000269|PubMed:20026641}.
MOD_RES 191 191 Phosphoserine; by CDK5.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:17009320}.
MOD_RES 246 246 Phosphoserine; by CDK5.
{ECO:0000269|PubMed:17009320}.
MOD_RES 331 331 Phosphotyrosine; by PTK6.
{ECO:0000269|PubMed:20026641}.
MOD_RES 333 333 Phosphotyrosine; by PTK6.
{ECO:0000305|PubMed:20026641}.
MOD_RES 552 552 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 556 556 Phosphothreonine.
{ECO:0000244|PubMed:18220336}.
MOD_RES 619 619 S-nitrosocysteine.
{ECO:0000250|UniProtKB:Q02248}.
MOD_RES 654 654 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:11279024}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:20068231}.
CARBOHYD 23 23 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:24342833}.
VAR_SEQ 1 565 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_006984.
VAR_SEQ 652 653 AT -> GK (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_006985.
VAR_SEQ 654 781 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_006986.
VARIANT 23 23 S -> R (in hepatocellular carcinoma; no
effect). {ECO:0000269|PubMed:10435629,
ECO:0000269|PubMed:12027456}.
/FTId=VAR_017612.
VARIANT 25 33 Missing (in hepatocellular carcinoma).
{ECO:0000269|PubMed:10435629}.
/FTId=VAR_017613.
VARIANT 32 32 D -> A (in hepatocellular carcinoma;
dbSNP:rs121913396).
{ECO:0000269|PubMed:10435629}.
/FTId=VAR_017614.
VARIANT 32 32 D -> G (in PTR and hepatocellular
carcinoma; dbSNP:rs121913396).
{ECO:0000269|PubMed:10192393,
ECO:0000269|PubMed:10435629}.
/FTId=VAR_017615.
VARIANT 32 32 D -> Y (in PTR, hepatoblastoma and
hepatocellular carcinoma;
dbSNP:rs28931588).
{ECO:0000269|PubMed:10192393,
ECO:0000269|PubMed:10435629,
ECO:0000269|PubMed:11703283,
ECO:0000269|PubMed:9927029}.
/FTId=VAR_017616.
VARIANT 33 33 S -> F (in PTR, MDB and hepatocellular
carcinoma; dbSNP:rs121913400).
{ECO:0000269|PubMed:10192393,
ECO:0000269|PubMed:10435629,
ECO:0000269|PubMed:10666372}.
/FTId=VAR_017617.
VARIANT 33 33 S -> L (in hepatocellular carcinoma).
{ECO:0000269|PubMed:10435629}.
/FTId=VAR_017618.
VARIANT 33 33 S -> Y (in colorectal cancer and PTR;
enhances transactivation of target genes;
dbSNP:rs121913400).
{ECO:0000269|PubMed:10192393,
ECO:0000269|PubMed:12027456,
ECO:0000269|PubMed:9065402}.
/FTId=VAR_017619.
VARIANT 34 34 G -> E (in PTR; dbSNP:rs28931589).
{ECO:0000269|PubMed:10192393}.
/FTId=VAR_017620.
VARIANT 34 34 G -> R (in hepatocellular carcinoma;
dbSNP:rs121913399).
{ECO:0000269|PubMed:10435629}.
/FTId=VAR_017621.
VARIANT 34 34 G -> V (in hepatoblastoma;
dbSNP:rs28931589).
{ECO:0000269|PubMed:9927029}.
/FTId=VAR_017622.
VARIANT 35 35 I -> S (in hepatocellular carcinoma).
{ECO:0000269|PubMed:10435629}.
/FTId=VAR_017623.
VARIANT 37 38 SG -> W (in hepatocellular carcinoma).
{ECO:0000269|PubMed:10435629}.
/FTId=VAR_017628.
VARIANT 37 37 S -> A (in MDB and hepatocellular
carcinoma; enhances transactivation of
target genes; dbSNP:rs121913228).
{ECO:0000269|PubMed:10435629,
ECO:0000269|PubMed:10666372,
ECO:0000269|PubMed:12027456}.
/FTId=VAR_017624.
VARIANT 37 37 S -> C (in PTR, hepatoblastoma and
ovarian cancer; dbSNP:rs121913403).
{ECO:0000269|PubMed:10192393,
ECO:0000269|PubMed:10391090,
ECO:0000269|PubMed:9927029}.
/FTId=VAR_017625.
VARIANT 37 37 S -> F (in PTR; dbSNP:rs121913403).
{ECO:0000269|PubMed:10192393}.
/FTId=VAR_017626.
VARIANT 37 37 S -> Y (in hepatocellular carcinoma;
dbSNP:rs121913403).
{ECO:0000269|PubMed:10435629}.
/FTId=VAR_017627.
VARIANT 41 41 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).
{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}.
/FTId=VAR_017629.
VARIANT 41 41 T -> I (in PTR, hepatocellular carcinoma
and ovarian cancer; dbSNP:rs121913413).
{ECO:0000269|PubMed:10192393,
ECO:0000269|PubMed:10391090,
ECO:0000269|PubMed:10435629}.
/FTId=VAR_017630.
VARIANT 45 45 S -> F (in hepatocellular carcinoma;
dbSNP:rs121913409).
{ECO:0000269|PubMed:10435629}.
/FTId=VAR_017631.
VARIANT 45 45 S -> P (in hepatocellular carcinoma;
dbSNP:rs121913407).
{ECO:0000269|PubMed:10435629}.
/FTId=VAR_017632.
VARIANT 45 45 Missing (in colorectal cancer).
{ECO:0000269|PubMed:9065402}.
/FTId=VAR_055430.
VARIANT 388 388 L -> P (in MRD19).
{ECO:0000269|PubMed:25326669}.
/FTId=VAR_072282.
VARIANT 688 688 M -> V (in dbSNP:rs4135384).
{ECO:0000269|Ref.3}.
/FTId=VAR_018954.
MUTAGEN 29 29 S->F: No effect.
{ECO:0000269|PubMed:12027456}.
MUTAGEN 64 64 Y->F: Abolishes phosphorylation by PTK6.
{ECO:0000269|PubMed:20026641}.
MUTAGEN 142 142 Y->E: No effect on interaction with BCL9
and BCL9L. {ECO:0000269|PubMed:17052462}.
MUTAGEN 156 156 L->A: Abolishes interaction with BCL9 but
no effect on interaction with CDH3; when
associated with A-159.
{ECO:0000269|PubMed:17052462}.
MUTAGEN 159 159 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.
{ECO:0000269|PubMed:17052462}.
MUTAGEN 178 178 L->A: No effect on interaction with BCL9
and CDH3. {ECO:0000269|PubMed:17052462}.
MUTAGEN 253 253 F->A: Abolishes or strongly reduces AXIN2
binding. {ECO:0000269|PubMed:10966653}.
MUTAGEN 260 260 H->A: Abolishes or strongly reduces AXIN1
and AXIN2 binding. Strongly reduces
phosphorylation and degradation; when
associated with A-386 and A-383.
{ECO:0000269|PubMed:10966653}.
MUTAGEN 292 292 K->A: Abolishes or strongly reduces AXIN1
and AXIN2 binding.
{ECO:0000269|PubMed:10966653}.
MUTAGEN 312 312 K->E: Abolishes TCF7L2 binding.
{ECO:0000269|PubMed:11713475}.
MUTAGEN 345 345 K->A: Abolishes APC binding.
{ECO:0000269|PubMed:10966653}.
MUTAGEN 383 383 W->A: Abolishes APC binding. Strongly
reduces phosphorylation and degradation;
when associated with A-260 and A-386.
{ECO:0000269|PubMed:10966653}.
MUTAGEN 386 386 R->A: Strongly reduces APC binding.
Strongly reduces phosphorylation and
degradation; when associated with A-260
and A-383. {ECO:0000269|PubMed:10966653}.
MUTAGEN 426 426 N->A: Abolishes TCF7L2 and LEF1 binding.
{ECO:0000269|PubMed:10966653}.
MUTAGEN 435 435 K->A: Strongly reduces or abolishes LEF1
binding. {ECO:0000269|PubMed:10966653,
ECO:0000269|PubMed:11713475}.
MUTAGEN 435 435 K->E: Abolishes TCF7L2 binding.
{ECO:0000269|PubMed:10966653,
ECO:0000269|PubMed:11713475}.
MUTAGEN 469 469 R->A: Abolishes TCF7L2 binding, and
strongly reduces or abolishes LEF1
binding. {ECO:0000269|PubMed:10966653}.
MUTAGEN 470 470 H->A: Abolishes TCF7L2 binding, and
strongly reduces or abolishes LEF1
binding. {ECO:0000269|PubMed:10966653}.
MUTAGEN 508 508 K->A: Abolishes TCF7L2 and LEF1 binding.
{ECO:0000269|PubMed:10966653}.
MUTAGEN 654 654 Y->E: Enhances TBP binding and
transactivation of target genes.
{ECO:0000269|PubMed:11279024}.
MUTAGEN 654 654 Y->F: Abolishes increase of TBP binding
after phosphorylation by CSK.
{ECO:0000269|PubMed:11279024}.
MUTAGEN 660 660 F->A: Abolishes CTNNBIP1 binding; when
associated with A-661.
{ECO:0000269|PubMed:12408824}.
MUTAGEN 661 661 R->A: Abolishes CTNNBIP1 binding; when
associated with A-660.
{ECO:0000269|PubMed:12408824}.
HELIX 135 150 {ECO:0000244|PDB:1G3J}.
HELIX 152 160 {ECO:0000244|PDB:1JDH}.
HELIX 165 179 {ECO:0000244|PDB:1JDH}.
HELIX 182 189 {ECO:0000244|PDB:1JDH}.
HELIX 192 204 {ECO:0000244|PDB:1JDH}.
HELIX 208 221 {ECO:0000244|PDB:1JDH}.
HELIX 225 233 {ECO:0000244|PDB:1JDH}.
HELIX 236 243 {ECO:0000244|PDB:1JDH}.
HELIX 249 265 {ECO:0000244|PDB:1JDH}.
HELIX 269 276 {ECO:0000244|PDB:1JDH}.
HELIX 278 284 {ECO:0000244|PDB:1JDH}.
HELIX 285 287 {ECO:0000244|PDB:1JDH}.
HELIX 291 305 {ECO:0000244|PDB:1JDH}.
HELIX 309 317 {ECO:0000244|PDB:1JDH}.
HELIX 320 330 {ECO:0000244|PDB:1JDH}.
HELIX 334 347 {ECO:0000244|PDB:1JDH}.
HELIX 353 359 {ECO:0000244|PDB:1JDH}.
HELIX 362 367 {ECO:0000244|PDB:1JDH}.
TURN 368 371 {ECO:0000244|PDB:1JDH}.
HELIX 375 389 {ECO:0000244|PDB:1JDH}.
HELIX 399 408 {ECO:0000244|PDB:1JDH}.
HELIX 414 427 {ECO:0000244|PDB:1JDH}.
TURN 428 430 {ECO:0000244|PDB:1JDH}.
HELIX 432 440 {ECO:0000244|PDB:1JDH}.
HELIX 443 454 {ECO:0000244|PDB:1JDH}.
HELIX 458 471 {ECO:0000244|PDB:1JDH}.
STRAND 473 475 {ECO:0000244|PDB:1JDH}.
HELIX 478 487 {ECO:0000244|PDB:1JDH}.
HELIX 491 496 {ECO:0000244|PDB:1JDH}.
STRAND 499 501 {ECO:0000244|PDB:4DJS}.
HELIX 504 517 {ECO:0000244|PDB:1JDH}.
HELIX 521 523 {ECO:0000244|PDB:1JDH}.
HELIX 524 529 {ECO:0000244|PDB:1JDH}.
HELIX 532 547 {ECO:0000244|PDB:1JDH}.
STRAND 550 552 {ECO:0000244|PDB:1QZ7}.
STRAND 554 557 {ECO:0000244|PDB:1QZ7}.
STRAND 561 563 {ECO:0000244|PDB:1T08}.
HELIX 566 580 {ECO:0000244|PDB:1JDH}.
HELIX 584 592 {ECO:0000244|PDB:1JDH}.
HELIX 596 601 {ECO:0000244|PDB:1JDH}.
HELIX 602 604 {ECO:0000244|PDB:1JDH}.
HELIX 608 621 {ECO:0000244|PDB:1JDH}.
HELIX 625 633 {ECO:0000244|PDB:1JDH}.
HELIX 637 642 {ECO:0000244|PDB:1JDH}.
HELIX 643 645 {ECO:0000244|PDB:1JDH}.
HELIX 649 662 {ECO:0000244|PDB:1JDH}.
TURN 663 665 {ECO:0000244|PDB:2Z6H}.
HELIX 668 682 {ECO:0000244|PDB:2Z6H}.
HELIX 688 690 {ECO:0000244|PDB:2Z6H}.
STRAND 778 780 {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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