GenomeNet

Database: UniProt
Entry: Q02248
LinkDB: Q02248
Original site: Q02248 
ID   CTNB1_MOUSE             Reviewed;         781 AA.
AC   Q02248; Q922W1; Q9D335;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   26-NOV-2014, entry version 174.
DE   RecName: Full=Catenin beta-1;
DE   AltName: Full=Beta-catenin;
GN   Name=Ctnnb1; Synonyms=Catnb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1509266; DOI=10.1126/science.257.5073.1142-a;
RA   Butz S., Stappert J., Weissig H., Kemler R.;
RT   "Plakoglobin and beta-catenin: distinct but closely related.";
RL   Science 257:1142-1144(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Colon, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary cancer;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
RA   Butz S., Kemler R.;
RT   "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
RT   adhesion.";
RL   FEBS Lett. 355:195-200(1994).
RN   [5]
RP   INTERACTION WITH TCF7; TCF7L1; TCF7L2 AND LEF1.
RX   PubMed=9783587; DOI=10.1038/26989;
RA   Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H.,
RA   Moerer P., van de Wetering M., Destree O., Clevers H.;
RT   "The Xenopus Wnt effector XTcf-3 interacts with Groucho-related
RT   transcriptional repressors.";
RL   Nature 395:608-612(1998).
RN   [6]
RP   INTERACTION WITH AXIN1.
RX   PubMed=10581160; DOI=10.1006/bbrc.1999.1760;
RA   Jho E., Lomvardas S., Costantini F.;
RT   "A GSK3beta phosphorylation site in axin modulates interaction with
RT   beta-catenin and Tcf-mediated gene expression.";
RL   Biochem. Biophys. Res. Commun. 266:28-35(1999).
RN   [7]
RP   INTERACTION WITH BAIAP1.
RX   PubMed=10772923; DOI=10.1006/bbrc.2000.2471;
RA   Dobrosotskaya I.Y., James G.L.;
RT   "MAGI-1 interacts with beta-catenin and is associated with cell-cell
RT   adhesion structures.";
RL   Biochem. Biophys. Res. Commun. 270:903-909(2000).
RN   [8]
RP   INTERACTION WITH CTNNA3.
RX   PubMed=11590244;
RA   Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J.,
RA   Colpaert C., Bruyneel E., Mareel M., van Roy F.;
RT   "AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein
RT   mediating strong cell-cell adhesion.";
RL   J. Cell Sci. 114:3177-3188(2001).
RN   [9]
RP   INTERACTION WITH TAX1BP3.
RX   PubMed=12874278; DOI=10.1074/jbc.M306324200;
RA   Kanamori M., Sandy P., Marzinotto S., Benetti R., Kai C.,
RA   Hayashizaki Y., Schneider C., Suzuki H.;
RT   "The PDZ protein tax-interacting protein-1 inhibits beta-catenin
RT   transcriptional activity and growth of colorectal cancer cells.";
RL   J. Biol. Chem. 278:38758-38764(2003).
RN   [10]
RP   PHOSPHORYLATION AT TYR-142 BY FYN.
RX   PubMed=12640114; DOI=10.1128/MCB.23.7.2287-2297.2003;
RA   Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N.,
RA   Garcia de Herreros A., Dunach M.;
RT   "p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-
RT   catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin
RT   Interaction.";
RL   Mol. Cell. Biol. 23:2287-2297(2003).
RN   [11]
RP   INTERACTION WITH RORA.
RX   PubMed=14687547; DOI=10.1016/S0896-6273(03)00769-4;
RA   Gold D.A., Baek S.H., Schork N.J., Rose D.W., Larsen D.D., Sachs B.D.,
RA   Rosenfeld M.G., Hamilton B.A.;
RT   "RORalpha coordinates reciprocal signaling in cerebellar development
RT   through sonic hedgehog and calcium-dependent pathways.";
RL   Neuron 40:1119-1131(2003).
RN   [12]
RP   INTERACTION WITH AXIN1.
RX   PubMed=15063782; DOI=10.1016/j.bbrc.2004.03.065;
RA   Kim S.I., Park C.S., Lee M.S., Kwon M.S., Jho E.H., Song W.K.;
RT   "Cyclin-dependent kinase 2 regulates the interaction of Axin with
RT   beta-catenin.";
RL   Biochem. Biophys. Res. Commun. 317:478-483(2004).
RN   [13]
RP   RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND LACK OF
RP   ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=16325582; DOI=10.1016/j.cell.2005.09.020;
RA   Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.;
RT   "Deconstructing the cadherin-catenin-actin complex.";
RL   Cell 123:889-901(2005).
RN   [14]
RP   INTERACTION WITH BCL9L.
RX   PubMed=17052462; DOI=10.1016/j.molcel.2006.09.001;
RA   Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.;
RT   "Crystal structure of a beta-catenin/BCL9/Tcf4 complex.";
RL   Mol. Cell 24:293-300(2006).
RN   [15]
RP   INTERACTION WITH GLIS2, AND SUBCELLULAR LOCATION.
RX   PubMed=17289029; DOI=10.1016/j.febslet.2007.01.058;
RA   Kim Y.-S., Kang H.S., Jetten A.M.;
RT   "The Kruppel-like zinc finger protein Glis2 functions as a negative
RT   modulator of the Wnt/beta-catenin signaling pathway.";
RL   FEBS Lett. 581:858-864(2007).
RN   [16]
RP   INTERACTION WITH XIRP1.
RX   PubMed=17925400; DOI=10.1074/jbc.M707639200;
RA   Choi S., Gustafson-Wagner E.A., Wang Q., Harlan S.M., Sinn H.W.,
RA   Lin J.L.-C., Lin J.J.-C.;
RT   "The intercalated disc protein, mXin{alpha}, is capable of interacting
RT   with beta-catenin and bundling actin filaments.";
RL   J. Biol. Chem. 282:36024-36036(2007).
RN   [17]
RP   INTERACTION WITH SLC30A9.
RX   PubMed=17344318; DOI=10.1093/nar/gkm095;
RA   Chen Y.H., Yang C.K., Xia M., Ou C.Y., Stallcup M.R.;
RT   "Role of GAC63 in transcriptional activation mediated by beta-
RT   catenin.";
RL   Nucleic Acids Res. 35:2084-2092(2007).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-552 AND
RP   SER-675, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [19]
RP   LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=18093941; DOI=10.1073/pnas.0710504105;
RA   Abe K., Takeichi M.;
RT   "EPLIN mediates linkage of the cadherin catenin complex to F-actin and
RT   stabilizes the circumferential actin belt.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008).
RN   [20]
RP   INTERACTION WITH TCF7L2 AND TNIK.
RX   PubMed=19816403; DOI=10.1038/emboj.2009.285;
RA   Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J.,
RA   Mohammed S., Heck A.J., Clevers H.;
RT   "The kinase TNIK is an essential activator of Wnt target genes.";
RL   EMBO J. 28:3329-3340(2009).
RN   [21]
RP   INTERACTION WITH SCRIB.
RX   PubMed=19458197; DOI=10.1091/mbc.E08-12-1172;
RA   Sun Y., Aiga M., Yoshida E., Humbert P.O., Bamji S.X.;
RT   "Scribble interacts with beta-catenin to localize synaptic vesicles to
RT   synapses.";
RL   Mol. Biol. Cell 20:3390-3400(2009).
RN   [22]
RP   PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2, AND MUTAGENESIS OF
RP   SER-33 AND SER-37.
RX   PubMed=20307497; DOI=10.1016/j.bbrc.2010.03.099;
RA   Kim E.-A., Kim J.E., Sung K.S., Choi D.W., Lee B.J., Choi C.Y.;
RT   "Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-catenin
RT   for phosphorylation and proteasomal degradation.";
RL   Biochem. Biophys. Res. Commun. 394:966-971(2010).
RN   [23]
RP   PHOSPHORYLATION AT SER-552, AND MUTAGENESIS OF SER-552.
RX   PubMed=20361929; DOI=10.1016/j.bbrc.2010.03.161;
RA   Zhao J., Yue W., Zhu M.J., Sreejayan N., Du M.;
RT   "AMP-activated protein kinase (AMPK) cross-talks with canonical Wnt
RT   signaling via phosphorylation of beta-catenin at Ser 552.";
RL   Biochem. Biophys. Res. Commun. 395:146-151(2010).
RN   [24]
RP   INTERACTION WITH TRPV4 AND CDH1.
RX   PubMed=20413591; DOI=10.1074/jbc.M110.103606;
RA   Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.;
RT   "The TRPV4 channel contributes to intercellular junction formation in
RT   keratinocytes.";
RL   J. Biol. Chem. 285:18749-18758(2010).
RN   [25]
RP   INTERACTION WITH VCL, AND MUTAGENESIS OF MET-8.
RX   PubMed=20086044; DOI=10.1242/jcs.056432;
RA   Peng X., Cuff L.E., Lawton C.D., DeMali K.A.;
RT   "Vinculin regulates cell-surface E-cadherin expression by binding to
RT   beta-catenin.";
RL   J. Cell Sci. 123:567-577(2010).
RN   [26]
RP   REVIEW.
RX   PubMed=10679188; DOI=10.1006/bbrc.1999.1860;
RA   Kikuchi A.;
RT   "Regulation of beta-catenin signaling in the Wnt pathway.";
RL   Biochem. Biophys. Res. Commun. 268:243-248(2000).
RN   [27]
RP   S-NITROSYLATION AT CYS-619, AND SUBCELLULAR LOCATION.
RX   PubMed=20705246; DOI=10.1016/j.molcel.2010.07.013;
RA   Thibeault S., Rautureau Y., Oubaha M., Faubert D., Wilkes B.C.,
RA   Delisle C., Gratton J.P.;
RT   "S-nitrosylation of beta-catenin by eNOS-derived NO promotes VEGF-
RT   induced endothelial cell permeability.";
RL   Mol. Cell 39:468-476(2010).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 150-665.
RX   PubMed=9298899; DOI=10.1016/S0092-8674(00)80352-9;
RA   Huber A.H., Nelson W.J., Weis W.I.;
RT   "Three-dimensional structure of the armadillo repeat region of beta-
RT   catenin.";
RL   Cell 90:871-882(1997).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 118-149 IN COMPLEX WITH
RP   CTNNA1.
RX   PubMed=10882138; DOI=10.1016/S1097-2765(00)80447-5;
RA   Pokutta S., Weis W.I.;
RT   "Structure of the dimerization and beta-catenin-binding region of
RT   alpha-catenin.";
RL   Mol. Cell 5:533-543(2000).
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (2.0 AND 3.0 ANGSTROMS) OF 134-671 IN COMPLEX
RP   WITH PHOSPHORYLATED AND UNPHOSPHORYLATED CDH1.
RX   PubMed=11348595; DOI=10.1016/S0092-8674(01)00330-0;
RA   Huber A.H., Weis W.I.;
RT   "The structure of the beta-catenin/E-cadherin complex and the
RT   molecular basis of diverse ligand recognition by beta-catenin.";
RL   Cell 105:391-402(2001).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH APC.
RX   PubMed=11707392; DOI=10.1093/emboj/20.22.6203;
RA   Eklof Spink K., Fridman S.G., Weis W.I.;
RT   "Molecular mechanisms of beta-catenin recognition by adenomatous
RT   polyposis coli revealed by the structure of an APC-beta-catenin
RT   complex.";
RL   EMBO J. 20:6203-6212(2001).
RN   [32]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH
RP   CTNNBIP1, AND INTERACTION WITH EP300.
RX   PubMed=12408825; DOI=10.1016/S1097-2765(02)00631-7;
RA   Daniels D.L., Weis W.I.;
RT   "ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription
RT   factors and the general coactivator p300 using independent structural
RT   modules.";
RL   Mol. Cell 10:573-584(2002).
CC   -!- FUNCTION: Key downstream component of the canonical Wnt signaling
CC       pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2,
CC       APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal
CC       Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its
CC       subsequent degradation by the proteasome. In the presence of Wnt
CC       ligand, CTNNB1 is not ubiquitinated and accumulates in the
CC       nucleus, where it acts as a coactivator for transcription factors
CC       of the TCF/LEF family, leading to activate Wnt responsive genes.
CC       Involved in the regulation of cell adhesion. Acts as a negative
CC       regulator of centrosome cohesion. Involved in the
CC       CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization.
CC       Blocks anoikis of malignant kidney and intestinal epithelial cells
CC       and promotes their anchorage-independent growth by down-regulating
CC       DAPK2 (By similarity). Disrupts PML function and PML-NB formation
CC       by inhibiting RANBP2-mediated sumoylation of PML (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Two separate complex-associated pools are found in the
CC       cytoplasm. The majority is present as component of an E-cadherin/
CC       catenin adhesion complex composed of at least E-cadherin/CDH1 and
CC       beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the
CC       complex is located to adherens junctions. The stable association
CC       of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-
CC       actin when assembled in the complex. Alternatively, the CTNNA1-
CC       containing complex may be linked to F-actin by other proteins such
CC       as LIMA1. Binds SLC9A3R1. Interacts with PTPRU (via the
CC       cytoplasmic juxtamembrane domain) and with EMD. Interacts with
CC       SESTD1 and TRPC4. Interacts with CAV1. Interacts with PTPRJ.
CC       Interacts with PKT7. Interacts with FAT1 (via the cytoplasmic
CC       domain). Interacts with CDK2, NDRG2 and NANOS1. Interacts with
CC       NEK2 and CDK5. Interacts with CARM1, CXADR, PCDH11Y and PTK6.
CC       Interacts with RAPGEF2. Interacts with SOX7; this interaction may
CC       lead to proteasomal degradation of active CTNNB1 and thus
CC       inhibition of Wnt/beta-catenin-stimulated transcription.
CC       Identified in a complex with HINT1 and MITF. Interacts with FHIT.
CC       Interacts with FERMT2. Identified in a complex with TCF4 and
CC       FERMT2. Another cytoplasmic pool is part of a large complex
CC       containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes
CC       phosphorylation on N-terminal Ser and Thr residues and
CC       ubiquitination of CTNNB1 via BTRC and its subsequent degradation
CC       by the proteasome. Wnt-dependent activation of DVL antagonizes the
CC       action of GSK3B. When GSK3B activity is inhibited the complex
CC       dissociates, CTNNB1 is dephosphorylated and is no longer targeted
CC       for destruction. The stabilized protein translocates to the
CC       nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9, BCL9L
CC       and possibly also RUVBL1 and CHD8. Interacts with TAX1BP3 (via the
CC       PDZ domain); this interaction inhibits the transcriptional
CC       activity of CTNNB1. Interacts with AJAP1, BAIAP1 and CTNNA3.
CC       Interacts with TRPV4; the TRPV4 and CTNNB1 complex can interact
CC       with CDH1. Interacts with VCL. The CTNNB1 and TCF4 complex
CC       interacts with PML. Interacts with XIRP1. Binds CTNNBIP and EP300.
CC       CTNNB1 forms a ternary complex with LEF1 and EP300 that is
CC       disrupted by CTNNBIP1 binding. Interacts directly with AXIN1; the
CC       interaction is regulated by CDK2 phosphorylation of AXIN1.
CC       Interacts with GLIS2. Interacts with SCRIB. Interacts with TNIK
CC       and TCF7L2. Interacts with SLC30A9. Interacts with RORA. May
CC       interact with P-cadherin/CDH3. {ECO:0000269|PubMed:10581160,
CC       ECO:0000269|PubMed:10772923, ECO:0000269|PubMed:10882138,
CC       ECO:0000269|PubMed:11348595, ECO:0000269|PubMed:11590244,
CC       ECO:0000269|PubMed:11707392, ECO:0000269|PubMed:12408825,
CC       ECO:0000269|PubMed:12874278, ECO:0000269|PubMed:14687547,
CC       ECO:0000269|PubMed:15063782, ECO:0000269|PubMed:17052462,
CC       ECO:0000269|PubMed:17289029, ECO:0000269|PubMed:17344318,
CC       ECO:0000269|PubMed:17925400, ECO:0000269|PubMed:19458197,
CC       ECO:0000269|PubMed:19816403, ECO:0000269|PubMed:20086044,
CC       ECO:0000269|PubMed:20413591, ECO:0000269|PubMed:7982500,
CC       ECO:0000269|PubMed:9783587}.
CC   -!- INTERACTION:
CC       P25054:APC (xeno); NbExp=8; IntAct=EBI-397872, EBI-727707;
CC       O15169:AXIN1 (xeno); NbExp=5; IntAct=EBI-397872, EBI-710484;
CC       P09803:Cdh1; NbExp=13; IntAct=EBI-397872, EBI-984420;
CC       P45481:Crebbp; NbExp=3; IntAct=EBI-397872, EBI-296306;
CC       P26231:Ctnna1; NbExp=2; IntAct=EBI-397872, EBI-647895;
CC       Q9NSA3:CTNNBIP1 (xeno); NbExp=7; IntAct=EBI-397872, EBI-747082;
CC       Q9WV60:Gsk3b; NbExp=2; IntAct=EBI-397872, EBI-400793;
CC       P42859:Htt; NbExp=3; IntAct=EBI-397872, EBI-5327353;
CC       P27782:Lef1; NbExp=6; IntAct=EBI-397872, EBI-984464;
CC       P97458:Prop1; NbExp=2; IntAct=EBI-397872, EBI-937831;
CC       F1MSG6:RAPGEF2 (xeno); NbExp=2; IntAct=EBI-397872, EBI-6927068;
CC       Q04207:Rela; NbExp=5; IntAct=EBI-397872, EBI-644400;
CC       Q9DBG9:Tax1bp3; NbExp=6; IntAct=EBI-397872, EBI-1161647;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Nucleus.
CC       Cell junction, adherens junction. Cell membrane {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250}. Note=Cytoplasmic when it is unstabilized (high
CC       level of phosphorylation) or bound to CDH1. Translocates to the
CC       nucleus when it is stabilized (low level of phosphorylation).
CC       Interaction with GLIS2 promotes nuclear translocation. Interaction
CC       with EMD inhibits nuclear localization. The majority of beta-
CC       catenin is localized to the cell membrane. In interphase,
CC       colocalizes with CROCC between CEP250 puncta at the proximal end
CC       of centrioles, and this localization is dependent on CROCC and
CC       CEP250. In mitosis, when NEK2 activity increases, it localizes to
CC       centrosomes at spindle poles independent of CROCC. Colocalizes
CC       with CDK5 in the cell-cell contacts and plasma membrane of
CC       undifferentiated and differentiated neuroblastoma cells.
CC       Colocalized with RAPGEF2 and TJP1 at cell-cell contacts (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylation by GSK3B requires prior phosphorylation of
CC       Ser-45 by another kinase. Phosphorylation proceeds then from Thr-
CC       41 to Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine
CC       phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding
CC       and enhances TBP binding (By similarity). Phosphorylated on Ser-33
CC       and Ser-37 by HIPK2. This phosphorylation triggers proteasomal
CC       degradation. Phosphorylation at Ser-552 by AMPK promotes
CC       stabilizion of the protein, enhancing TCF/LEF-mediated
CC       transcription. Phosphorylation on Ser-191 and Ser-246 by CDK5.
CC       Phosphorylation by CDK2 regulates insulin internalization (By
CC       similarity). Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331
CC       and/or Tyr-333 with the predominant site at Tyr-64 is not
CC       essential for inhibition of transcriptional activity (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when
CC       phosphorylated by GSK3B, leading to its degradation. Ubiquitinated
CC       by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1,
CC       CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent
CC       proteasomal degradation (By similarity). {ECO:0000250}.
CC   -!- PTM: S-nitrosylation at Cys-619 within adherens junctions promotes
CC       VEGF-induced, NO-dependent endothelial cell permeability by
CC       disrupting interaction with E-cadherin, thus mediating disassembly
CC       adherens junctions. {ECO:0000269|PubMed:20705246}.
CC   -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 12 ARM repeats. {ECO:0000255|PROSITE-
CC       ProRule:PRU00259}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH06739.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M90364; AAA37280.1; -; mRNA.
DR   EMBL; AK035311; BAC29027.1; -; mRNA.
DR   EMBL; AK018515; BAB31250.1; -; mRNA.
DR   EMBL; BC006739; AAH06739.1; ALT_INIT; mRNA.
DR   EMBL; BC048153; AAH48153.1; -; mRNA.
DR   EMBL; BC053065; AAH53065.1; -; mRNA.
DR   CCDS; CCDS23630.1; -.
DR   PIR; S35091; S35091.
DR   RefSeq; NP_001159374.1; NM_001165902.1.
DR   RefSeq; NP_031640.1; NM_007614.3.
DR   RefSeq; XP_006511990.1; XM_006511927.1.
DR   UniGene; Mm.291928; -.
DR   PDB; 1DOW; X-ray; 1.80 A; B=118-149.
DR   PDB; 1I7W; X-ray; 2.00 A; A/C=134-671.
DR   PDB; 1I7X; X-ray; 3.00 A; A/C=134-671.
DR   PDB; 1JPP; X-ray; 3.10 A; A/B=134-671.
DR   PDB; 1M1E; X-ray; 2.10 A; A=134-671.
DR   PDB; 1V18; X-ray; 2.10 A; A=134-671.
DR   PDB; 2BCT; X-ray; 2.90 A; A=150-665.
DR   PDB; 3BCT; X-ray; 2.10 A; A=193-661.
DR   PDB; 3OUW; X-ray; 2.91 A; A=134-671.
DR   PDB; 3OUX; X-ray; 2.40 A; A=134-671.
DR   PDB; 4EV8; X-ray; 1.90 A; A=134-671.
DR   PDB; 4EV9; X-ray; 2.10 A; A=134-671.
DR   PDB; 4EVA; X-ray; 2.00 A; A/C=134-671.
DR   PDB; 4EVP; X-ray; 2.26 A; A=134-671.
DR   PDB; 4EVT; X-ray; 2.34 A; A=134-671.
DR   PDB; 4ONS; X-ray; 2.80 A; B/D=78-151.
DR   PDBsum; 1DOW; -.
DR   PDBsum; 1I7W; -.
DR   PDBsum; 1I7X; -.
DR   PDBsum; 1JPP; -.
DR   PDBsum; 1M1E; -.
DR   PDBsum; 1V18; -.
DR   PDBsum; 2BCT; -.
DR   PDBsum; 3BCT; -.
DR   PDBsum; 3OUW; -.
DR   PDBsum; 3OUX; -.
DR   PDBsum; 4EV8; -.
DR   PDBsum; 4EV9; -.
DR   PDBsum; 4EVA; -.
DR   PDBsum; 4EVP; -.
DR   PDBsum; 4EVT; -.
DR   PDBsum; 4ONS; -.
DR   DisProt; DP00341; -.
DR   ProteinModelPortal; Q02248; -.
DR   SMR; Q02248; 19-44, 84-665.
DR   BioGrid; 198512; 70.
DR   DIP; DIP-31560N; -.
DR   IntAct; Q02248; 58.
DR   MINT; MINT-103426; -.
DR   PhosphoSite; Q02248; -.
DR   MaxQB; Q02248; -.
DR   PaxDb; Q02248; -.
DR   PRIDE; Q02248; -.
DR   Ensembl; ENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932.
DR   Ensembl; ENSMUST00000178812; ENSMUSP00000136294; ENSMUSG00000006932.
DR   GeneID; 12387; -.
DR   KEGG; mmu:12387; -.
DR   UCSC; uc009scu.2; mouse.
DR   CTD; 1499; -.
DR   MGI; MGI:88276; Ctnnb1.
DR   eggNOG; NOG297695; -.
DR   GeneTree; ENSGT00730000110821; -.
DR   HOGENOM; HOG000230958; -.
DR   HOVERGEN; HBG000919; -.
DR   InParanoid; Q02248; -.
DR   KO; K02105; -.
DR   OMA; RESHNRA; -.
DR   OrthoDB; EOG7X9G6B; -.
DR   PhylomeDB; Q02248; -.
DR   TreeFam; TF317997; -.
DR   Reactome; REACT_203336; Degradation of beta-catenin by the destruction complex.
DR   Reactome; REACT_207044; TCF dependent signaling in response to WNT.
DR   Reactome; REACT_212869; Apoptotic cleavage of cell adhesion proteins.
DR   Reactome; REACT_216539; formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; REACT_216784; disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR   Reactome; REACT_218396; Beta-catenin phosphorylation cascade.
DR   Reactome; REACT_219771; deactivation of the beta-catenin transactivating complex.
DR   Reactome; REACT_221970; Ca2+ pathway.
DR   Reactome; REACT_223626; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
DR   Reactome; REACT_230395; Adherens junctions interactions.
DR   Reactome; REACT_234076; S37 mutants of beta-catenin aren't phosphorylated.
DR   Reactome; REACT_248000; S45 mutants of beta-catenin aren't phosphorylated.
DR   Reactome; REACT_258576; T41 mutants of beta-catenin aren't phosphorylated.
DR   Reactome; REACT_258600; CDO in myogenesis.
DR   Reactome; REACT_259776; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR   Reactome; REACT_260752; S33 mutants of beta-catenin aren't phosphorylated.
DR   Reactome; REACT_261276; misspliced GSK3beta mutants stabilize beta-catenin.
DR   Reactome; REACT_261840; VEGFR2 mediated vascular permeability.
DR   ChiTaRS; Ctnnb1; mouse.
DR   EvolutionaryTrace; Q02248; -.
DR   NextBio; 281106; -.
DR   PMAP-CutDB; Q02248; -.
DR   PRO; PR:Q02248; -.
DR   Bgee; Q02248; -.
DR   CleanEx; MM_CTNNB1; -.
DR   ExpressionAtlas; Q02248; baseline and differential.
DR   Genevestigator; Q02248; -.
DR   GO; GO:0005912; C:adherens junction; IDA:MGI.
DR   GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
DR   GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISS:UniProtKB.
DR   GO; GO:0016342; C:catenin complex; ISS:UniProtKB.
DR   GO; GO:0071664; C:catenin-TCF7L2 complex; IDA:BHF-UCL.
DR   GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR   GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR   GO; GO:0071944; C:cell periphery; ISS:BHF-UCL.
DR   GO; GO:0031253; C:cell projection membrane; IDA:MGI.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:RefGenome.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0043198; C:dendritic shaft; IBA:RefGenome.
DR   GO; GO:0030057; C:desmosome; IBA:RefGenome.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl.
DR   GO; GO:0005916; C:fascia adherens; IDA:MGI.
DR   GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0031528; C:microvillus membrane; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
DR   GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IDA:BHF-UCL.
DR   GO; GO:0045202; C:synapse; IBA:RefGenome.
DR   GO; GO:0005923; C:tight junction; IDA:MGI.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0005915; C:zonula adherens; IBA:RefGenome.
DR   GO; GO:0045294; F:alpha-catenin binding; IPI:dictyBase.
DR   GO; GO:0045296; F:cadherin binding; IPI:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
DR   GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IBA:RefGenome.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR   GO; GO:0070491; F:repressing transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0005198; F:structural molecule activity; IBA:RefGenome.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IPI:MGI.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:MGI.
DR   GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
DR   GO; GO:0034332; P:adherens junction organization; IMP:MGI.
DR   GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
DR   GO; GO:0045453; P:bone resorption; IMP:MGI.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI.
DR   GO; GO:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0061324; P:canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0044334; P:canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR   GO; GO:0060038; P:cardiac muscle cell proliferation; TAS:DFLAT.
DR   GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; TAS:DFLAT.
DR   GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR   GO; GO:0001709; P:cell fate determination; IMP:MGI.
DR   GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR   GO; GO:0048469; P:cell maturation; IDA:MGI.
DR   GO; GO:0000904; P:cell morphogenesis involved in differentiation; IMP:MGI.
DR   GO; GO:0008283; P:cell proliferation; IMP:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR   GO; GO:0009987; P:cellular process; IDA:MGI.
DR   GO; GO:0034613; P:cellular protein localization; IMP:MGI.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0071681; P:cellular response to indole-3-methanol; ISS:UniProtKB.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR   GO; GO:0022009; P:central nervous system vasculogenesis; IMP:MGI.
DR   GO; GO:0060982; P:coronary artery morphogenesis; TAS:DFLAT.
DR   GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; IBA:RefGenome.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IMP:MGI.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR   GO; GO:0007398; P:ectoderm development; IMP:MGI.
DR   GO; GO:0000578; P:embryonic axis specification; IDA:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR   GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:MGI.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IDA:MGI.
DR   GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0036023; P:embryonic skeletal limb joint morphogenesis; IGI:BHF-UCL.
DR   GO; GO:0001706; P:endoderm formation; IMP:MGI.
DR   GO; GO:0001711; P:endodermal cell fate commitment; IMP:MGI.
DR   GO; GO:0061154; P:endothelial tube morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060983; P:epicardium-derived cardiac vascular smooth muscle cell differentiation; TAS:DFLAT.
DR   GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IMP:MGI.
DR   GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0061198; P:fungiform papilla formation; IMP:MGI.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR   GO; GO:0035112; P:genitalia morphogenesis; IMP:MGI.
DR   GO; GO:0007403; P:glial cell fate determination; IDA:MGI.
DR   GO; GO:0022405; P:hair cycle process; IMP:MGI.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR   GO; GO:0060789; P:hair follicle placode formation; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0030097; P:hemopoiesis; IDA:MGI.
DR   GO; GO:0030902; P:hindbrain development; IBA:RefGenome.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0021819; P:layer formation in cerebral cortex; IMP:MGI.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR   GO; GO:0060173; P:limb development; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IBA:RefGenome.
DR   GO; GO:0060479; P:lung cell differentiation; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0060492; P:lung induction; IMP:MGI.
DR   GO; GO:0060484; P:lung-associated mesenchyme development; IMP:MGI.
DR   GO; GO:0030539; P:male genitalia development; IMP:MGI.
DR   GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IMP:MGI.
DR   GO; GO:0003337; P:mesenchymal to epithelial transition involved in metanephros morphogenesis; IDA:MGI.
DR   GO; GO:0060485; P:mesenchyme development; TAS:DFLAT.
DR   GO; GO:0072132; P:mesenchyme morphogenesis; TAS:DFLAT.
DR   GO; GO:0003338; P:metanephros morphogenesis; IMP:MGI.
DR   GO; GO:0007494; P:midgut development; IEA:Ensembl.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
DR   GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR   GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
DR   GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IGI:MGI.
DR   GO; GO:0003136; P:negative regulation of heart induction by canonical Wnt signaling pathway; IBA:RefGenome.
DR   GO; GO:1901215; P:negative regulation of neuron death; IGI:MGI.
DR   GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IMP:MGI.
DR   GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP:MGI.
DR   GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0072079; P:nephron tubule formation; IMP:MGI.
DR   GO; GO:0001840; P:neural plate development; IDA:MGI.
DR   GO; GO:0001764; P:neuron migration; IGI:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR   GO; GO:0048599; P:oocyte development; IGI:MGI.
DR   GO; GO:0048513; P:organ development; IMP:MGI.
DR   GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
DR   GO; GO:0060066; P:oviduct development; IMP:MGI.
DR   GO; GO:0031016; P:pancreas development; IMP:MGI.
DR   GO; GO:0001569; P:patterning of blood vessels; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0061047; P:positive regulation of branching involved in lung morphogenesis; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   GO; GO:2000017; P:positive regulation of determination of dorsal identity; IDA:MGI.
DR   GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IMP:MGI.
DR   GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IMP:MGI.
DR   GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; TAS:DFLAT.
DR   GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR   GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IGI:MGI.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IGI:MGI.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
DR   GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
DR   GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
DR   GO; GO:0090279; P:regulation of calcium ion import; ISS:UniProtKB.
DR   GO; GO:0045595; P:regulation of cell differentiation; IDA:MGI.
DR   GO; GO:0042127; P:regulation of cell proliferation; IDA:MGI.
DR   GO; GO:0030997; P:regulation of centriole-centriole cohesion; ISS:UniProtKB.
DR   GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; IMP:BHF-UCL.
DR   GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0031641; P:regulation of myelination; IMP:MGI.
DR   GO; GO:0072182; P:regulation of nephron tubule epithelial cell differentiation; IMP:UniProtKB.
DR   GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:MGI.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:MGI.
DR   GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB.
DR   GO; GO:0003266; P:regulation of secondary heart field cardioblast proliferation; IDA:MGI.
DR   GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR   GO; GO:0042129; P:regulation of T cell proliferation; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0072053; P:renal inner medulla development; IMP:MGI.
DR   GO; GO:0072054; P:renal outer medulla development; IMP:MGI.
DR   GO; GO:0072001; P:renal system development; IMP:MGI.
DR   GO; GO:0072033; P:renal vesicle formation; IMP:MGI.
DR   GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR   GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; ISS:UniProtKB.
DR   GO; GO:0043627; P:response to estrogen; IBA:RefGenome.
DR   GO; GO:0014010; P:Schwann cell proliferation; IBA:RefGenome.
DR   GO; GO:0016337; P:single organismal cell-cell adhesion; IMP:MGI.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   GO; GO:0043588; P:skin development; IMP:MGI.
DR   GO; GO:0051145; P:smooth muscle cell differentiation; IMP:MGI.
DR   GO; GO:0050808; P:synapse organization; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   GO; GO:0048489; P:synaptic vesicle transport; IMP:MGI.
DR   GO; GO:0030217; P:T cell differentiation; IMP:MGI.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR   GO; GO:0048538; P:thymus development; IMP:MGI.
DR   GO; GO:0060440; P:trachea formation; IMP:MGI.
DR   GO; GO:0060439; P:trachea morphogenesis; IMP:MGI.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0001944; P:vasculature development; IMP:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   GO; GO:0003223; P:ventricular compact myocardium morphogenesis; TAS:DFLAT.
DR   GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR013284; Beta-catenin.
DR   Pfam; PF00514; Arm; 4.
DR   PRINTS; PR01869; BCATNINFAMLY.
DR   SMART; SM00185; ARM; 12.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 9.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Cell adhesion; Cell junction;
KW   Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Membrane;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; S-nitrosylation;
KW   Transcription; Transcription regulation; Ubl conjugation;
KW   Wnt signaling pathway.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    781       Catenin beta-1.
FT                                /FTId=PRO_0000064272.
FT   REPEAT      151    191       ARM 1.
FT   REPEAT      193    234       ARM 2.
FT   REPEAT      235    276       ARM 3.
FT   REPEAT      277    318       ARM 4.
FT   REPEAT      319    360       ARM 5.
FT   REPEAT      361    389       ARM 6.
FT   REPEAT      400    441       ARM 7.
FT   REPEAT      442    484       ARM 8.
FT   REPEAT      489    530       ARM 9.
FT   REPEAT      531    571       ARM 10.
FT   REPEAT      594    636       ARM 11.
FT   REPEAT      637    666       ARM 12.
FT   REGION        2     23       Interaction with VCL.
FT   REGION      156    178       Interaction with BCL9. {ECO:0000250}.
FT   REGION      772    781       Interaction with SCRIB.
FT   MOD_RES       2      2       N-acetylalanine. {ECO:0000250}.
FT   MOD_RES      23     23       Phosphoserine; by GSK3-beta.
FT                                {ECO:0000250}.
FT   MOD_RES      29     29       Phosphoserine; by GSK3-beta.
FT                                {ECO:0000250}.
FT   MOD_RES      33     33       Phosphoserine; by GSK3-beta and HIPK2.
FT                                {ECO:0000269|PubMed:20307497}.
FT   MOD_RES      37     37       Phosphoserine; by GSK3-beta and HIPK2.
FT                                {ECO:0000269|PubMed:20307497}.
FT   MOD_RES      41     41       Phosphothreonine; by GSK3-beta.
FT                                {ECO:0000250}.
FT   MOD_RES      45     45       Phosphoserine. {ECO:0000250}.
FT   MOD_RES      64     64       Phosphotyrosine; by PTK6. {ECO:0000250}.
FT   MOD_RES      86     86       Phosphotyrosine; by CSK. {ECO:0000250}.
FT   MOD_RES     142    142       Phosphotyrosine; by FYN and PTK6.
FT                                {ECO:0000269|PubMed:12640114}.
FT   MOD_RES     191    191       Phosphoserine; alternate.
FT                                {ECO:0000269|PubMed:17242355}.
FT   MOD_RES     191    191       Phosphoserine; by CDK5; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES     246    246       Phosphoserine; by CDK5. {ECO:0000250}.
FT   MOD_RES     331    331       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES     551    551       Phosphothreonine. {ECO:0000250}.
FT   MOD_RES     552    552       Phosphoserine; by AMPK.
FT                                {ECO:0000269|PubMed:17242355,
FT                                ECO:0000269|PubMed:20361929}.
FT   MOD_RES     556    556       Phosphothreonine. {ECO:0000250}.
FT   MOD_RES     619    619       S-nitrosocysteine.
FT                                {ECO:0000269|PubMed:20705246}.
FT   MOD_RES     654    654       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES     675    675       Phosphoserine.
FT                                {ECO:0000269|PubMed:17242355}.
FT   MUTAGEN       8      8       M->P: Loss of interaction with VCL.
FT                                {ECO:0000269|PubMed:20086044}.
FT   MUTAGEN      33     33       S->A: Abolished HIPK2-mediated
FT                                proteasomal degradation.
FT                                {ECO:0000269|PubMed:20307497}.
FT   MUTAGEN      37     37       S->A: Abolished HIPK2-mediated
FT                                proteasomal degradation.
FT                                {ECO:0000269|PubMed:20307497}.
FT   MUTAGEN     552    552       S->A: Abolishes AMPK-mediated
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:20361929}.
FT   CONFLICT    371    371       T -> I (in Ref. 2; BAB31250).
FT                                {ECO:0000305}.
FT   CONFLICT    478    478       A -> T (in Ref. 2; BAB31250).
FT                                {ECO:0000305}.
FT   CONFLICT    487    487       L -> F (in Ref. 2; BAB31250).
FT                                {ECO:0000305}.
FT   HELIX        85     88       {ECO:0000244|PDB:4ONS}.
FT   HELIX        90     98       {ECO:0000244|PDB:4ONS}.
FT   HELIX       100    102       {ECO:0000244|PDB:4ONS}.
FT   HELIX       121    141       {ECO:0000244|PDB:1DOW}.
FT   TURN        145    148       {ECO:0000244|PDB:1DOW}.
FT   TURN        150    152       {ECO:0000244|PDB:1I7W}.
FT   HELIX       153    160       {ECO:0000244|PDB:1I7W}.
FT   STRAND      161    164       {ECO:0000244|PDB:1JPP}.
FT   STRAND      166    168       {ECO:0000244|PDB:4EVP}.
FT   HELIX       169    171       {ECO:0000244|PDB:4EVP}.
FT   HELIX       172    178       {ECO:0000244|PDB:4EV8}.
FT   HELIX       182    189       {ECO:0000244|PDB:4EV8}.
FT   STRAND      192    194       {ECO:0000244|PDB:4EV8}.
FT   HELIX       195    204       {ECO:0000244|PDB:4EV8}.
FT   HELIX       208    221       {ECO:0000244|PDB:4EV8}.
FT   HELIX       225    233       {ECO:0000244|PDB:4EV8}.
FT   HELIX       236    242       {ECO:0000244|PDB:4EV8}.
FT   HELIX       243    245       {ECO:0000244|PDB:4EV8}.
FT   HELIX       249    265       {ECO:0000244|PDB:4EV8}.
FT   HELIX       269    275       {ECO:0000244|PDB:4EV8}.
FT   HELIX       278    284       {ECO:0000244|PDB:4EV8}.
FT   HELIX       285    287       {ECO:0000244|PDB:4EV8}.
FT   HELIX       291    305       {ECO:0000244|PDB:4EV8}.
FT   HELIX       309    317       {ECO:0000244|PDB:4EV8}.
FT   HELIX       320    330       {ECO:0000244|PDB:4EV8}.
FT   HELIX       334    347       {ECO:0000244|PDB:4EV8}.
FT   HELIX       353    359       {ECO:0000244|PDB:4EV8}.
FT   HELIX       362    367       {ECO:0000244|PDB:4EV8}.
FT   TURN        368    371       {ECO:0000244|PDB:4EV8}.
FT   HELIX       375    389       {ECO:0000244|PDB:4EV8}.
FT   HELIX       399    408       {ECO:0000244|PDB:4EV8}.
FT   HELIX       414    428       {ECO:0000244|PDB:4EV8}.
FT   HELIX       432    440       {ECO:0000244|PDB:4EV8}.
FT   HELIX       443    454       {ECO:0000244|PDB:4EV8}.
FT   HELIX       458    471       {ECO:0000244|PDB:4EV8}.
FT   STRAND      473    475       {ECO:0000244|PDB:4EV8}.
FT   HELIX       478    487       {ECO:0000244|PDB:4EV8}.
FT   HELIX       491    496       {ECO:0000244|PDB:4EV8}.
FT   HELIX       504    517       {ECO:0000244|PDB:4EV8}.
FT   HELIX       521    523       {ECO:0000244|PDB:4EV8}.
FT   HELIX       524    529       {ECO:0000244|PDB:4EV8}.
FT   HELIX       532    547       {ECO:0000244|PDB:4EV8}.
FT   HELIX       566    580       {ECO:0000244|PDB:4EV8}.
FT   HELIX       584    592       {ECO:0000244|PDB:4EV8}.
FT   HELIX       596    602       {ECO:0000244|PDB:4EV8}.
FT   HELIX       608    621       {ECO:0000244|PDB:4EV8}.
FT   HELIX       625    633       {ECO:0000244|PDB:4EV8}.
FT   TURN        634    636       {ECO:0000244|PDB:3OUX}.
FT   HELIX       637    643       {ECO:0000244|PDB:4EV8}.
FT   HELIX       649    661       {ECO:0000244|PDB:4EV8}.
SQ   SEQUENCE   781 AA;  85471 MW;  D708F170A3FBED6E 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 GAQGEALGYR QDDPSYRSFH
     SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD
     L
//
DBGET integrated database retrieval system