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 27-MAR-2024, entry version 251. DE RecName: Full=Catenin beta-1 {ECO:0000312|MGI:MGI:88276}; DE AltName: Full=Beta-catenin {ECO:0000303|PubMed:1509266}; GN Name=Ctnnb1 {ECO:0000312|MGI:MGI:88276}; GN Synonyms=Catnb {ECO:0000312|MGI:MGI:88276}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., 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., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., 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/6J; 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 project: RT 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., Moerer P., RA 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 beta- RT 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; DOI=10.1242/jcs.114.17.3177; RA Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J., Colpaert C., RA Bruyneel E., Mareel M., van Roy F.; RT "AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein RT mediating strong cell-cell adhesion."; RL J. Cell Sci. 114:3177-3188(2001). RN [9] RP INTERACTION WITH TAX1BP3. RX PubMed=12874278; DOI=10.1074/jbc.m306324200; RA Kanamori M., Sandy P., Marzinotto S., Benetti R., Kai C., Hayashizaki Y., RA 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-catenin RT Tyr-142 phosphorylation and beta-catenin-alpha-catenin 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 beta- RT catenin."; RL Biochem. Biophys. Res. Commun. 317:478-483(2004). RN [13] RP FUNCTION, INTERACTION WITH SOX9, AND UBIQUITINATION. RX PubMed=15132997; DOI=10.1101/gad.1171104; RA Akiyama H., Lyons J.P., Mori-Akiyama Y., Yang X., Zhang R., Zhang Z., RA Deng J.M., Taketo M.M., Nakamura T., Behringer R.R., McCrea P.D., RA de Crombrugghe B.; RT "Interactions between Sox9 and beta-catenin control chondrocyte RT differentiation."; RL Genes Dev. 18:1072-1087(2004). RN [14] RP RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, LACK OF RP ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND FUNCTION. 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 [15] 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 [16] 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 [17] 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 with RT beta-catenin and bundling actin filaments."; RL J. Biol. Chem. 282:36024-36036(2007). RN [18] 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-catenin."; RL Nucleic Acids Res. 35:2084-2092(2007). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-552 AND SER-675, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [20] RP LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND RP FUNCTION. 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 [21] RP INTERACTION WITH TCF7L2 AND TNIK. RX PubMed=19816403; DOI=10.1038/emboj.2009.285; RA Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., RA Heck A.J., Clevers H.; RT "The kinase TNIK is an essential activator of Wnt target genes."; RL EMBO J. 28:3329-3340(2009). RN [22] 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 [23] RP PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2, AND MUTAGENESIS OF SER-33 RP 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 for RT phosphorylation and proteasomal degradation."; RL Biochem. Biophys. Res. Commun. 394:966-971(2010). RN [24] 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 [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-191 AND SER-675, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [26] 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 [27] 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 beta- RT catenin."; RL J. Cell Sci. 123:567-577(2010). RN [28] 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 [29] 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., Delisle C., RA Gratton J.P.; RT "S-nitrosylation of beta-catenin by eNOS-derived NO promotes VEGF-induced RT endothelial cell permeability."; RL Mol. Cell 39:468-476(2010). RN [30] RP FUNCTION, DISRUPTION PHENOTYPE, AND CONDITIONAL KNOCKOUT. RX PubMed=21325504; DOI=10.1523/jneurosci.4243-10.2011; RA Armstrong A., Ryu Y.K., Chieco D., Kuruvilla R.; RT "Frizzled3 is required for neurogenesis and target innervation during RT sympathetic nervous system development."; RL J. Neurosci. 31:2371-2381(2011). RN [31] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=21623382; DOI=10.1038/nm.2380; RA Lancaster M.A., Gopal D.J., Kim J., Saleem S.N., Silhavy J.L., Louie C.M., RA Thacker B.E., Williams Y., Zaki M.S., Gleeson J.G.; RT "Defective Wnt-dependent cerebellar midline fusion in a mouse model of RT Joubert syndrome."; RL Nat. Med. 17:726-731(2011). RN [32] RP TISSUE SPECIFICITY. RX PubMed=22510880; DOI=10.1038/emboj.2012.91; RA Wilson C.H., Crombie C., van der Weyden L., Poulogiannis G., Rust A.G., RA Pardo M., Gracia T., Yu L., Choudhary J., Poulin G.B., McIntyre R.E., RA Winton D.J., March H.N., Arends M.J., Fraser A.G., Adams D.J.; RT "Nuclear receptor binding protein 1 regulates intestinal progenitor cell RT homeostasis and tumour formation."; RL EMBO J. 31:2486-2497(2012). RN [33] RP SUBCELLULAR LOCATION, AND INTERACTION WITH DLG5. RX PubMed=25232112; DOI=10.1523/jneurosci.1280-14.2014; RA Wang S.H., Celic I., Choi S.Y., Riccomagno M., Wang Q., Sun L.O., RA Mitchell S.P., Vasioukhin V., Huganir R.L., Kolodkin A.L.; RT "Dlg5 regulates dendritic spine formation and synaptogenesis by controlling RT subcellular N-cadherin localization."; RL J. Neurosci. 34:12745-12761(2014). RN [34] RP SUBCELLULAR LOCATION. RX PubMed=25979161; DOI=10.1016/j.bone.2015.05.009; RA Jeong B.C., Kim T.S., Kim H.S., Lee S.H., Choi Y.; RT "Transmembrane protein 64 reciprocally regulates osteoblast and adipocyte RT differentiation by modulating Wnt/beta-catenin signaling."; RL Bone 78:165-173(2015). RN [35] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=29148101; DOI=10.1111/eos.12390; RA Feng X.Y., Wu X.S., Wang J.S., Zhang C.M., Wang S.L.; RT "Homeobox protein MSX-1 inhibits expression of bone morphogenetic protein RT 2, bone morphogenetic protein 4, and lymphoid enhancer-binding factor 1 via RT Wnt/beta-catenin signaling to prevent differentiation of dental mesenchymal RT cells during the late bell stage."; RL Eur. J. Oral Sci. 126:1-12(2018). RN [36] RP SUBCELLULAR LOCATION. RX PubMed=30389919; DOI=10.1038/s41467-018-06941-4; RA Koren E., Yosefzon Y., Ankawa R., Soteriou D., Jacob A., Nevelsky A., RA Ben-Yosef R., Bar-Sela G., Fuchs Y.; RT "ARTS mediates apoptosis and regeneration of the intestinal stem cell RT niche."; RL Nat. Commun. 9:4582-4582(2018). RN [37] RP INTERACTION WITH LMBR1L AND AMFR. RX PubMed=31073040; DOI=10.1126/science.aau0812; RA Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J., RA Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M., RA Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y., RA Beutler B.; RT "LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling."; RL Science 364:0-0(2019). RN [38] RP INTERACTION WITH ADNP. RX PubMed=32533114; DOI=10.1038/s41467-020-16799-0; RA Sun X., Peng X., Cao Y., Zhou Y., Sun Y.; RT "ADNP promotes neural differentiation by modulating Wnt/beta-catenin RT signaling."; RL Nat. Commun. 11:2984-2984(2020). RN [39] 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 [40] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 118-149 IN COMPLEX WITH 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 alpha- RT catenin."; RL Mol. Cell 5:533-543(2000). RN [41] RP X-RAY CRYSTALLOGRAPHY (2.0 AND 3.0 ANGSTROMS) OF 134-671 IN COMPLEX WITH RP 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 molecular RT basis of diverse ligand recognition by beta-catenin."; RL Cell 105:391-402(2001). RN [42] 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 polyposis RT coli revealed by the structure of an APC-beta-catenin complex."; RL EMBO J. 20:6203-6212(2001). RN [43] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH CTNNBIP1, RP 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 factors RT and the general coactivator p300 using independent structural modules."; RL Mol. Cell 10:573-584(2002). CC -!- FUNCTION: Key downstream component of the canonical Wnt signaling CC pathway (PubMed:15132997). In the absence of Wnt, forms a complex with CC AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on CC N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC CC and its subsequent degradation by the proteasome. In the presence of CC Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, CC where it acts as a coactivator for transcription factors of the TCF/LEF CC family, leading to activate Wnt responsive genes (By similarity). CC Involved in the regulation of cell adhesion, as component of an E- CC cadherin:catenin adhesion complex (PubMed:16325582, PubMed:18093941). CC Acts as a negative regulator of centrosome cohesion. Involved in the CC CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks CC anoikis of malignant kidney and intestinal epithelial cells and CC promotes their anchorage-independent growth by down-regulating DAPK2. CC Disrupts PML function and PML-NB formation by inhibiting RANBP2- CC mediated sumoylation of PML (By similarity). Promotes neurogenesis by CC maintaining sympathetic neuroblasts within the cell cycle CC (PubMed:21325504). Involved in chondrocyte differentiation via CC interaction with SOX9: SOX9-binding competes with the binding sites of CC TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling CC (PubMed:15132997). Acts as a positive regulator of odontoblast CC differentiation during mesenchymal tooth germ formation, via promoting CC the transcription of differentiation factors such as LEF1, BMP2 and CC BMP4 (PubMed:29148101). Activity is repressed in a MSX1-mediated manner CC at the bell stage of mesenchymal tooth germ formation which prevents CC premature differentiation of odontoblasts (PubMed:29148101). CC {ECO:0000250|UniProtKB:P35222, ECO:0000269|PubMed:15132997, CC ECO:0000269|PubMed:16325582, ECO:0000269|PubMed:18093941, CC ECO:0000269|PubMed:21325504, ECO:0000269|PubMed:29148101}. 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 beta- CC catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is CC located to adherens junctions. The stable association of CTNNA1 is CC controversial as CTNNA1 was shown not to bind to F-actin when assembled CC in the complex. Alternatively, the CTNNA1-containing complex may be CC linked to F-actin by other proteins such as LIMA1. Binds NHERF1. CC Interacts with PTPRU (via the cytoplasmic juxtamembrane domain) and CC with EMD. Interacts with SESTD1 and TRPC4. Interacts with CAV1. CC Interacts with PTPRJ. Interacts with PKT7. Interacts with FAT1 (via the CC cytoplasmic domain). Interacts with CDK2, NDRG2 and NANOS1. Interacts CC with NEK2 and CDK5. Interacts with CARM1, CXADR, PCDH11Y and PTK6. CC Interacts with RAPGEF2. Interacts with SOX7; this interaction may lead CC to proteasomal degradation of active CTNNB1 and thus inhibition of CC Wnt/beta-catenin-stimulated transcription. Identified in a complex with CC HINT1 and MITF. Interacts with FHIT. Interacts with FERMT2. Identified CC in a complex with TCF4 and FERMT2. Another cytoplasmic pool is part of CC a large complex containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that CC promotes phosphorylation on N-terminal Ser and Thr residues and CC ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the CC proteasome. Wnt-dependent activation of DVL antagonizes the action of CC GSK3B. When GSK3B activity is inhibited the complex dissociates, CTNNB1 CC is dephosphorylated and is no longer targeted for destruction. The CC stabilized protein translocates to the nucleus, where it binds TCF/LEF- CC 1 family members, BCL9, BCL9L and possibly also RUVBL1 and CHD8. CC Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits CC the transcriptional activity of CTNNB1. Interacts with AJAP1, BAIAP1 CC and CTNNA3. Interacts with TRPV4; the TRPV4 and CTNNB1 complex can CC interact 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 disrupted by CC CTNNBIP1 binding. Interacts directly with AXIN1; the interaction is CC regulated by CDK2 phosphorylation of AXIN1. Interacts with GLIS2. CC Interacts with SCRIB. Interacts with TNIK and TCF7L2. Interacts with CC SLC30A9. Interacts with RORA. May interact with P-cadherin/CDH3. CC Interacts with RNF220 (By similarity). Interacts with CTNND2 (By CC similarity). Interacts (via the C-terminal region) with CBY1 (By CC similarity). The complex composed, at least, of APC, CTNNB1 and GSK3B CC interacts with JPT1; the interaction requires the inactive form of CC GSK3B (phosphorylated at 'Ser-9') (By similarity). Interacts with DLG5 CC (PubMed:25232112). Interacts with FAM53B; promoting translocation to CC the nucleus. Interacts with TMEM170B (By similarity). Interacts with CC AHI1 (By similarity). Interacts with GID8 (By similarity). Component of CC an cadherin:catenin adhesion complex composed of at least of CDH26, CC beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By CC similarity). Forms a complex comprising APPL1, RUVBL2, APPL2, HDAC1 and CC HDAC2 (By similarity). Interacts with IRF2BPL; mediates the CC ubiquitination and degradation of CTNNB1 (By similarity). Interacts CC with AMFR (PubMed:31073040). Interacts with LMBR1L (PubMed:31073040). CC Interacts with SOX30; prevents interaction of CTNNB1 with TCF7L2/TCF4 CC and leads to inhibition of Wnt signaling (By similarity). Interacts CC with SOX9; inhibiting CTNNB1 activity by competing with the binding CC sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling CC (PubMed:15132997). Interacts with SPN/CD43 cytoplasmic tail (By CC similarity). Interacts (when phosphorylated at Tyr-333) with isoform M2 CC of PKM (PKM2); promoting transcription activation (By similarity). CC Interacts with PKP2 (via HEAD domain) (By similarity). Interacts with CC CDH1 (By similarity). Interacts (when unphosphorylated) with FLYWCH1, CC perhaps preventing interaction of CTNNB1 with TCF4, and thereby CC regulating transcription activation; phosphorylation of CTNNB1 may CC inhibit the interaction (By similarity). Interacts (via the central CC armadillo domains) with probable transcriptional regulator ADNP (via N- CC terminal region); interaction is direct and stabilizes CTNNB1 by CC modulating its phosphorylation by glycogen synthase kinase-3 beta GSK3B CC (PubMed:32533114). {ECO:0000250|UniProtKB:P35222, CC ECO:0000269|PubMed:10581160, ECO:0000269|PubMed:10772923, CC ECO:0000269|PubMed:10882138, ECO:0000269|PubMed:11348595, CC ECO:0000269|PubMed:11590244, ECO:0000269|PubMed:11707392, CC ECO:0000269|PubMed:12408825, ECO:0000269|PubMed:12874278, CC ECO:0000269|PubMed:14687547, ECO:0000269|PubMed:15063782, CC ECO:0000269|PubMed:15132997, 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:25232112, CC ECO:0000269|PubMed:31073040, ECO:0000269|PubMed:32533114, CC ECO:0000269|PubMed:7982500, ECO:0000269|PubMed:9783587}. CC -!- INTERACTION: CC Q02248; P09803: Cdh1; NbExp=17; IntAct=EBI-397872, EBI-984420; CC Q02248; P45481: Crebbp; NbExp=3; IntAct=EBI-397872, EBI-296306; CC Q02248; P26231: Ctnna1; NbExp=2; IntAct=EBI-397872, EBI-647895; CC Q02248; Q9WV60: Gsk3b; NbExp=2; IntAct=EBI-397872, EBI-400793; CC Q02248; P42859: Htt; NbExp=3; IntAct=EBI-397872, EBI-5327353; CC Q02248; P27782: Lef1; NbExp=6; IntAct=EBI-397872, EBI-984464; CC Q02248; O54826: Mllt10; NbExp=2; IntAct=EBI-397872, EBI-8459555; CC Q02248; P97458: Prop1; NbExp=2; IntAct=EBI-397872, EBI-937831; CC Q02248; Q04207: Rela; NbExp=5; IntAct=EBI-397872, EBI-644400; CC Q02248; P40645: Sox6; NbExp=2; IntAct=EBI-397872, EBI-3505685; CC Q02248; Q9DBG9: Tax1bp3; NbExp=6; IntAct=EBI-397872, EBI-1161647; CC Q02248; P25054: APC; Xeno; NbExp=8; IntAct=EBI-397872, EBI-727707; CC Q02248; O15169: AXIN1; Xeno; NbExp=5; IntAct=EBI-397872, EBI-710484; CC Q02248; Q9NSA3: CTNNBIP1; Xeno; NbExp=7; IntAct=EBI-397872, EBI-747082; CC Q02248; P49841: GSK3B; Xeno; NbExp=3; IntAct=EBI-397872, EBI-373586; CC Q02248; F1MSG6: RAPGEF2; Xeno; NbExp=2; IntAct=EBI-397872, EBI-6927068; CC Q02248; O15047: SETD1A; Xeno; NbExp=2; IntAct=EBI-397872, EBI-540779; CC Q02248; P33148; Xeno; NbExp=4; IntAct=EBI-397872, EBI-15603953; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30389919}. Nucleus CC {ECO:0000269|PubMed:30389919}. Cytoplasm, cytoskeleton. Cell junction, CC adherens junction {ECO:0000269|PubMed:20705246}. Cell junction CC {ECO:0000250|UniProtKB:B6V8E6}. Cell membrane CC {ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000250|UniProtKB:P35222}. CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P35222}. CC Synapse {ECO:0000269|PubMed:20705246}. Cytoplasm, cytoskeleton, cilium CC basal body {ECO:0000269|PubMed:21623382}. Note=Colocalized with RAPGEF2 CC and TJP1 at cell-cell contacts (By similarity). Cytoplasmic when it is CC un-stable (highly phosphorylated) or bound to CDH1. Translocates to the CC nucleus when it is stabilized (low level of phosphorylation). CC Interaction with GLIS2 and MUC1 promotes nuclear translocation. CC Interaction with EMD inhibits nuclear localization. The majority of CC beta-catenin is localized to the cell membrane. In interphase, CC colocalizes with CROCC between CEP250 puncta at the proximal end of CC centrioles, and this localization is dependent on CROCC and CEP250. In CC mitosis, when NEK2 activity increases, it localizes to centrosomes at CC spindle poles independent of CROCC. Colocalizes with CDK5 in the cell- CC cell contacts and plasma membrane of undifferentiated and CC differentiated neuroblastoma cells. Interaction with FAM53B promotes CC translocation to the nucleus (By similarity). CC {ECO:0000250|UniProtKB:B6V8E6, ECO:0000250|UniProtKB:P35222}. CC -!- TISSUE SPECIFICITY: Expressed in cerebellar granule neurons (at protein CC level) (PubMed:21623382). Expressed in the intestinal epithelium (at CC protein level) (PubMed:22510880). {ECO:0000269|PubMed:21623382, CC ECO:0000269|PubMed:22510880}. CC -!- DEVELOPMENTAL STAGE: Expressed in bell stage dental mesenchymal cells CC at 17.5 dpc (at protein level). {ECO:0000269|PubMed:29148101}. CC -!- PTM: Phosphorylation at Ser-552 by AMPK promotes stabilization of the CC protein, enhancing TCF/LEF-mediated transcription (PubMed:20361929). CC Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by CC another kinase (By similarity). Phosphorylation proceeds then from Thr- CC 41 to Ser-37 and Ser-33 (By similarity). Phosphorylated by NEK2 (By CC similarity). EGF stimulates tyrosine phosphorylation (By similarity). CC Phosphorylated on Ser-33 and Ser-37 by HIPK2 and GSK3B, this CC phosphorylation triggers proteasomal degradation (PubMed:20307497). CC Phosphorylation on Ser-191 and Ser-246 by CDK5 (By similarity). CC Phosphorylation by CDK2 regulates insulin internalization (By CC similarity). Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or CC Tyr-333 with the predominant site at Tyr-64 is not essential for CC inhibition of transcriptional activity (By similarity). Phosphorylation CC by SRC at Tyr-333 promotes interaction with isoform M2 of PKM (PKM2); CC promoting transcription activation (By similarity). CC {ECO:0000250|UniProtKB:P35222, ECO:0000269|PubMed:20307497, CC ECO:0000269|PubMed:20361929}. CC -!- PTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when CC phosphorylated by GSK3B, leading to its degradation (By similarity). CC Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, CC SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent CC proteasomal degradation (By similarity). Ubiquitinated and degraded CC following interaction with SOX9 (Probable). CC {ECO:0000250|UniProtKB:P35222, ECO:0000305|PubMed:15132997}. CC -!- PTM: S-nitrosylation at Cys-619 within adherens junctions promotes CC VEGF-induced, NO-dependent endothelial cell permeability by disrupting CC interaction with E-cadherin, thus mediating disassembly adherens CC junctions. {ECO:0000269|PubMed:20705246}. CC -!- PTM: O-glycosylation at Ser-23 decreases nuclear localization and CC transcriptional activity, and increases localization to the plasma CC membrane and interaction with E-cadherin CDH1. CC {ECO:0000250|UniProtKB:Q96S06}. CC -!- PTM: Deacetylated at Lys-49 by SIRT1. {ECO:0000250|UniProtKB:P35222}. CC -!- DISRUPTION PHENOTYPE: Sympathetic ganglia-specific conditional knockout CC mice lead to a reduction in sympathetic ganglia size and in progenitor CC cell number, but does not alter sympathetic innervation of peripheral CC target organs. {ECO:0000269|PubMed:21325504}. CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH06739.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 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 AlphaFoldDB; Q02248; -. DR SMR; Q02248; -. DR BioGRID; 198512; 126. DR ComplexPortal; CPX-318; beta1-catenin - LEF1 complex. DR ComplexPortal; CPX-86; Beta-catenin-ICAT complex. DR CORUM; Q02248; -. DR DIP; DIP-31560N; -. DR IntAct; Q02248; 79. DR MINT; Q02248; -. DR STRING; 10090.ENSMUSP00000007130; -. DR BindingDB; Q02248; -. DR ChEMBL; CHEMBL4105846; -. DR TCDB; 8.A.160.2.1; the catenin (catenin) family. DR GlyCosmos; Q02248; 1 site, No reported glycans. DR GlyGen; Q02248; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q02248; -. DR MetOSite; Q02248; -. DR PhosphoSitePlus; Q02248; -. DR SwissPalm; Q02248; -. DR jPOST; Q02248; -. DR MaxQB; Q02248; -. DR PaxDb; 10090-ENSMUSP00000007130; -. DR PeptideAtlas; Q02248; -. DR ProteomicsDB; 285221; -. DR Pumba; Q02248; -. DR Antibodypedia; 3432; 5983 antibodies from 57 providers. DR DNASU; 12387; -. DR Ensembl; ENSMUST00000007130.15; ENSMUSP00000007130.9; ENSMUSG00000006932.18. DR Ensembl; ENSMUST00000178812.9; ENSMUSP00000136294.2; ENSMUSG00000006932.18. DR GeneID; 12387; -. DR KEGG; mmu:12387; -. DR UCSC; uc009scu.2; mouse. DR AGR; MGI:88276; -. DR CTD; 1499; -. DR MGI; MGI:88276; Ctnnb1. DR VEuPathDB; HostDB:ENSMUSG00000006932; -. DR eggNOG; KOG4203; Eukaryota. DR GeneTree; ENSGT00940000155471; -. DR HOGENOM; CLU_008757_1_1_1; -. DR InParanoid; Q02248; -. DR OMA; YPKLVYT; -. DR OrthoDB; 50711at2759; -. DR PhylomeDB; Q02248; -. DR TreeFam; TF317997; -. DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade. DR Reactome; R-MMU-201681; TCF dependent signaling in response to WNT. DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-MMU-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production. DR Reactome; R-MMU-351906; Apoptotic cleavage of cell adhesion proteins. DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex. DR Reactome; R-MMU-4086398; Ca2+ pathway. DR Reactome; R-MMU-418990; Adherens junctions interactions. DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane. DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-MMU-525793; Myogenesis. DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs. DR Reactome; R-MMU-8853884; Transcriptional Regulation by VENTX. DR Reactome; R-MMU-8951430; RUNX3 regulates WNT signaling. DR Reactome; R-MMU-9762292; Regulation of CDH11 function. DR BioGRID-ORCS; 12387; 5 hits in 83 CRISPR screens. DR ChiTaRS; Ctnnb1; mouse. DR EvolutionaryTrace; Q02248; -. DR PRO; PR:Q02248; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q02248; Protein. DR Bgee; ENSMUSG00000006932; Expressed in primitive streak and 308 other cell types or tissues. DR ExpressionAtlas; Q02248; baseline and differential. DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB. DR GO; GO:0043296; C:apical junction complex; IDA:MGI. DR GO; GO:0045177; C:apical part of cell; IDA:MGI. DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI. DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:MGI. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI. DR GO; GO:0030877; C:beta-catenin destruction complex; IDA:MGI. DR GO; GO:1990711; C:beta-catenin-ICAT complex; IPI:ComplexPortal. DR GO; GO:1990907; C:beta-catenin-TCF complex; IDA:ParkinsonsUK-UCL. DR GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISS:UniProtKB. DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI. DR GO; GO:0016342; C:catenin complex; IDA:MGI. 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:UniProtKB. DR GO; GO:0031253; C:cell projection membrane; IDA:MGI. DR GO; GO:0005911; C:cell-cell junction; IDA:BHF-UCL. DR GO; GO:0005813; C:centrosome; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL. DR GO; GO:0043198; C:dendritic shaft; ISO:MGI. DR GO; GO:0000791; C:euchromatin; IDA:BHF-UCL. DR GO; GO:0005916; C:fascia adherens; IDA:MGI. DR GO; GO:0016600; C:flotillin complex; IDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. 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:ParkinsonsUK-UCL. DR GO; GO:0031528; C:microvillus membrane; IDA:MGI. DR GO; GO:0031965; C:nuclear membrane; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO. DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO. DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO. DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO. DR GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IDA:BHF-UCL. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; IDA:UniProtKB. DR GO; GO:0070160; C:tight junction; ISO:MGI. DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL. DR GO; GO:1990909; C:Wnt signalosome; IDA:ParkinsonsUK-UCL. DR GO; GO:0030018; C:Z disc; IDA:MGI. DR GO; GO:0045294; F:alpha-catenin binding; IDA:MGI. DR GO; GO:0045296; F:cadherin binding; IPI:CAFA. DR GO; GO:0003682; F:chromatin binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0070097; F:delta-catenin binding; ISO:MGI. DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL. DR GO; GO:1990226; F:histone methyltransferase binding; IPI:BHF-UCL. DR GO; GO:0070411; F:I-SMAD binding; ISO:MGI. DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI. DR GO; GO:0019900; F:kinase binding; ISO:MGI. DR GO; GO:0140677; F:molecular function activator activity; EXP:DisProt. DR GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI. DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI. DR GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB. DR GO; GO:0003676; F:nucleic acid binding; EXP:DisProt. DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:MGI. DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI. DR GO; GO:0046332; F:SMAD binding; ISO:MGI. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0001221; F:transcription coregulator binding; IPI:BHF-UCL. DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI. DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0090425; P:acinar cell differentiation; IMP:MGI. DR GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB. DR GO; GO:0034332; P:adherens junction organization; IMP:MGI. DR GO; GO:0048513; P:animal organ development; IMP:MGI. DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI. DR GO; GO:0097190; P:apoptotic signaling pathway; IMP:MGI. DR GO; GO:0036520; P:astrocyte-dopaminergic neuron signaling; IMP:ParkinsonsUK-UCL. DR GO; GO:0045453; P:bone resorption; IMP:MGI. DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; 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:CAFA. DR GO; GO:0044338; P:canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation; IMP:MGI. 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:0001708; P:cell fate specification; IMP:MGI. DR GO; GO:0048469; P:cell maturation; IDA:MGI. DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI. DR GO; GO:0008283; P:cell population proliferation; IMP:MGI. DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI. DR GO; GO:0007160; P:cell-matrix adhesion; 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:1990314; P:cellular response to insulin-like growth factor stimulus; ISO:MGI. DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI. DR GO; GO:0022009; P:central nervous system vasculogenesis; IMP:MGI. DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI. DR GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI. DR GO; GO:0060982; P:coronary artery morphogenesis; TAS:DFLAT. DR GO; GO:0061550; P:cranial ganglion development; IMP:ParkinsonsUK-UCL. DR GO; GO:1904888; P:cranial skeletal system development; IMP:ParkinsonsUK-UCL. DR GO; GO:0006351; P:DNA-templated transcription; IMP:MGI. DR GO; GO:1990791; P:dorsal root ganglion development; IMP:ParkinsonsUK-UCL. 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:1990403; P:embryonic brain development; IMP:ParkinsonsUK-UCL. 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:0048568; P:embryonic organ development; 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:0060767; P:epithelial cell proliferation involved in prostate gland development; IMP:MGI. DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI. DR GO; GO:0060856; P:establishment of blood-brain barrier; IMP:MGI. DR GO; GO:1990963; P:establishment of blood-retinal barrier; IMP:MGI. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; 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:0010467; P:gene expression; IMP:MGI. DR GO; GO:0035112; P:genitalia morphogenesis; IMP:MGI. DR GO; GO:0002067; P:glandular epithelial cell differentiation; 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; IMP:ParkinsonsUK-UCL. DR GO; GO:0021854; P:hypothalamus development; IMP:MGI. 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:0060479; P:lung cell differentiation; IMP:MGI. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0060487; P:lung epithelial cell differentiation; 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:0000165; P:MAPK cascade; IGI:MGI. DR GO; GO:0010463; P:mesenchymal cell proliferation; IMP:MGI. DR GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IMP:MGI. DR GO; GO:0072497; P:mesenchymal stem cell differentiation; IMP: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:0030901; P:midbrain development; IMP:ParkinsonsUK-UCL. DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; IMP:ParkinsonsUK-UCL. DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI. DR GO; GO:0051450; P:myoblast proliferation; IMP:MGI. DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:BHF-UCL. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:ComplexPortal. DR GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL. DR GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; IDA:MGI. DR GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; IMP:UniProtKB. DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:UniProtKB. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; 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:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL. DR GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0072079; P:nephron tubule formation; IMP:MGI. DR GO; GO:0001840; P:neural plate development; IDA:MGI. DR GO; GO:0007405; P:neuroblast proliferation; IGI:MGI. DR GO; GO:0030182; P:neuron differentiation; IMP:ParkinsonsUK-UCL. DR GO; GO:0048664; P:neuron fate determination; IMP:MGI. DR GO; GO:0001764; P:neuron migration; IGI:MGI. DR GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI. DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI. DR GO; GO:0048599; P:oocyte development; IGI:MGI. DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI. DR GO; GO:0030316; P:osteoclast differentiation; IMP:MGI. DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL. DR GO; GO:0060066; P:oviduct development; IMP:MGI. DR GO; GO:0031016; P:pancreas development; 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:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL. DR GO; GO:2000017; P:positive regulation of determination of dorsal identity; IDA:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. 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; ISO:MGI. 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: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:2000288; P:positive regulation of myoblast proliferation; IMP:MGI. DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:UniProtKB. DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:UniProtKB. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI. DR GO; GO:1901331; P:positive regulation of odontoblast differentiation; IMP:UniProtKB. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI. DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IMP:CACAO. DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IMP:MGI. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI. DR GO; GO:0008104; P:protein localization; IMP:MGI. DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI. 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 population 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:0050767; P:regulation of neurogenesis; NAS:ComplexPortal. 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:0031396; P:regulation of protein ubiquitination; ISO:MGI. 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:0051963; P:regulation of synapse assembly; IDA:SynGO. DR GO; GO:0042129; P:regulation of T cell proliferation; IMP:MGI. DR GO; GO:0051884; P:regulation of timing of anagen; IDA:CAFA. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; 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:0072033; P:renal vesicle formation; IMP:MGI. DR GO; GO:0034097; P:response to cytokine; ISO:MGI. DR GO; GO:0032355; P:response to estradiol; ISS:UniProtKB. DR GO; GO:0043627; P:response to estrogen; ISO:MGI. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0014010; P:Schwann cell proliferation; ISO: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:0072089; P:stem cell proliferation; IMP:MGI. DR GO; GO:0061549; P:sympathetic ganglion development; IMP:UniProtKB. DR GO; GO:0050808; P:synapse organization; IMP:MGI. DR GO; GO:0097091; P:synaptic vesicle clustering; IDA:SynGO. 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:0001894; P:tissue homeostasis; IMP:MGI. DR GO; GO:0060440; P:trachea formation; IMP:MGI. DR GO; GO:0060439; P:trachea morphogenesis; IMP:MGI. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI. 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 CDD; cd21724; CTNNAbd_CTNNB1; 1. DR DisProt; DP00341; -. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR IDEAL; IID50011; -. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000225; Armadillo. DR InterPro; IPR013284; Beta-catenin. DR PANTHER; PTHR45976; ARMADILLO SEGMENT POLARITY PROTEIN; 1. DR PANTHER; PTHR45976:SF4; CATENIN BETA-1; 1. DR Pfam; PF00514; Arm; 4. DR PRINTS; PR01869; BCATNINFAMLY. DR SMART; SM00185; ARM; 12. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50176; ARM_REPEAT; 9. DR Genevisible; Q02248; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Cell adhesion; Cell junction; KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Glycoprotein; KW Membrane; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; S-nitrosylation; Synapse; Transcription; Transcription regulation; KW Ubl conjugation; Wnt signaling pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P35222" FT CHAIN 2..781 FT /note="Catenin beta-1" FT /id="PRO_0000064272" FT REPEAT 151..191 FT /note="ARM 1" FT REPEAT 193..234 FT /note="ARM 2" FT REPEAT 235..276 FT /note="ARM 3" FT REPEAT 277..318 FT /note="ARM 4" FT REPEAT 319..360 FT /note="ARM 5" FT REPEAT 361..389 FT /note="ARM 6" FT REPEAT 400..441 FT /note="ARM 7" FT REPEAT 442..484 FT /note="ARM 8" FT REPEAT 489..530 FT /note="ARM 9" FT REPEAT 531..571 FT /note="ARM 10" FT REPEAT 594..636 FT /note="ARM 11" FT REPEAT 637..666 FT /note="ARM 12" FT REGION 2..23 FT /note="Interaction with VCL" FT /evidence="ECO:0000269|PubMed:20086044" FT REGION 34..57 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 156..178 FT /note="Interaction with BCL9" FT /evidence="ECO:0000250" FT REGION 720..781 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 772..781 FT /note="Interaction with SCRIB" FT /evidence="ECO:0000269|PubMed:19458197" FT COMPBIAS 34..48 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 23 FT /note="Phosphoserine; by GSK3-beta; alternate" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 29 FT /note="Phosphoserine; by GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 33 FT /note="Phosphoserine; by GSK3-beta and HIPK2" FT /evidence="ECO:0000269|PubMed:20307497" FT MOD_RES 37 FT /note="Phosphoserine; by GSK3-beta and HIPK2" FT /evidence="ECO:0000269|PubMed:20307497" FT MOD_RES 41 FT /note="Phosphothreonine; by GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 49 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 64 FT /note="Phosphotyrosine; by PTK6" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 142 FT /note="Phosphotyrosine; by FYN and PTK6" FT /evidence="ECO:0000269|PubMed:12640114" FT MOD_RES 191 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 246 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 331 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 333 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 552 FT /note="Phosphoserine; by AMPK" FT /evidence="ECO:0000269|PubMed:20361929, FT ECO:0007744|PubMed:17242355" FT MOD_RES 556 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 619 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000269|PubMed:20705246" FT MOD_RES 675 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT CARBOHYD 23 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q96S06" FT MUTAGEN 8 FT /note="M->P: Loss of interaction with VCL." FT /evidence="ECO:0000269|PubMed:20086044" FT MUTAGEN 33 FT /note="S->A: Abolished HIPK2-mediated proteasomal FT degradation." FT /evidence="ECO:0000269|PubMed:20307497" FT MUTAGEN 37 FT /note="S->A: Abolished HIPK2-mediated proteasomal FT degradation." FT /evidence="ECO:0000269|PubMed:20307497" FT MUTAGEN 552 FT /note="S->A: Abolishes AMPK-mediated phosphorylation." FT /evidence="ECO:0000269|PubMed:20361929" FT CONFLICT 371 FT /note="T -> I (in Ref. 2; BAB31250)" FT /evidence="ECO:0000305" FT CONFLICT 478 FT /note="A -> T (in Ref. 2; BAB31250)" FT /evidence="ECO:0000305" FT CONFLICT 487 FT /note="L -> F (in Ref. 2; BAB31250)" FT /evidence="ECO:0000305" FT HELIX 85..88 FT /evidence="ECO:0007829|PDB:4ONS" FT HELIX 90..98 FT /evidence="ECO:0007829|PDB:4ONS" FT HELIX 100..102 FT /evidence="ECO:0007829|PDB:4ONS" FT HELIX 121..141 FT /evidence="ECO:0007829|PDB:1DOW" FT TURN 145..148 FT /evidence="ECO:0007829|PDB:1DOW" FT TURN 150..152 FT /evidence="ECO:0007829|PDB:1I7W" FT HELIX 153..160 FT /evidence="ECO:0007829|PDB:1I7W" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:1JPP" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:4EVP" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:4EVP" FT HELIX 172..178 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 182..189 FT /evidence="ECO:0007829|PDB:4EV8" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 195..204 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 208..221 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 225..233 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 236..242 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 243..245 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 249..265 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 269..275 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 278..284 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 285..287 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 291..305 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 309..317 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 320..330 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 334..347 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 353..359 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 362..367 FT /evidence="ECO:0007829|PDB:4EV8" FT TURN 368..371 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 375..389 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 399..408 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 414..428 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 432..440 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 443..454 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 458..471 FT /evidence="ECO:0007829|PDB:4EV8" FT STRAND 473..475 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 478..487 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 491..496 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 504..517 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 521..523 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 524..529 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 532..547 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 566..580 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 584..592 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 596..602 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 608..621 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 625..633 FT /evidence="ECO:0007829|PDB:4EV8" FT TURN 634..636 FT /evidence="ECO:0007829|PDB:3OUX" FT HELIX 637..643 FT /evidence="ECO:0007829|PDB:4EV8" FT HELIX 649..661 FT /evidence="ECO:0007829|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 //