CTNB1_MOUSE
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 03-AUG-2022, entry version 242.
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; 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, Pancreas,
RC 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 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 [33]
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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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). {ECO:0000250|UniProtKB:P35222,
CC ECO:0000269|PubMed:15132997, ECO:0000269|PubMed:16325582,
CC ECO:0000269|PubMed:18093941, ECO:0000269|PubMed:21325504}.
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 SLC9A3R1.
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 {ECO:0000250|UniProtKB:P35222, 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:15132997,
CC ECO:0000269|PubMed:17052462, ECO:0000269|PubMed:17289029,
CC ECO:0000269|PubMed:17344318, ECO:0000269|PubMed:17925400,
CC ECO:0000269|PubMed:19458197, ECO:0000269|PubMed:19816403,
CC ECO:0000269|PubMed:20086044, ECO:0000269|PubMed:20413591,
CC ECO:0000269|PubMed:25232112, ECO:0000269|PubMed:31073040,
CC ECO:0000269|PubMed:7982500, ECO:0000269|PubMed:9783587}.
CC -!- INTERACTION:
CC Q02248; P09803: Cdh1; NbExp=16; 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; 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 unstabilized (high level of phosphorylation) or bound to CDH1.
CC Translocates to the nucleus when it is stabilized (low level of
CC phosphorylation). Interaction with GLIS2 and MUC1 promotes nuclear
CC translocation. Interaction with EMD inhibits nuclear localization. The
CC majority of beta-catenin is localized to the cell membrane. In
CC interphase, colocalizes with CROCC between CEP250 puncta at the
CC proximal end of centrioles, and this localization is dependent on CROCC
CC and CEP250. In mitosis, when NEK2 activity increases, it localizes to
CC centrosomes at spindle poles independent of CROCC. Colocalizes with
CC CDK5 in the cell-cell contacts and plasma membrane of undifferentiated
CC and differentiated neuroblastoma cells. Interaction with FAM53B
CC promotes translocation to the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:B6V8E6, ECO:0000250|UniProtKB:P35222}.
CC -!- TISSUE SPECIFICITY: Expressed in cerebellar granule neurons (at protein
CC level). {ECO:0000269|PubMed:21623382}.
CC -!- PTM: Phosphorylation at Ser-552 by AMPK promotes stabilizion 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 ---------------------------------------------------------------------------
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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; 120.
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; 77.
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 GlyGen; Q02248; 1 site.
DR iPTMnet; Q02248; -.
DR PhosphoSitePlus; Q02248; -.
DR SwissPalm; Q02248; -.
DR jPOST; Q02248; -.
DR MaxQB; Q02248; -.
DR PaxDb; Q02248; -.
DR PeptideAtlas; Q02248; -.
DR PRIDE; Q02248; -.
DR ProteomicsDB; 285221; -.
DR Antibodypedia; 3432; 5066 antibodies from 57 providers.
DR DNASU; 12387; -.
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 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; 321213at2759; -.
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 BioGRID-ORCS; 12387; 5 hits in 78 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 304 other tissues.
DR ExpressionAtlas; Q02248; baseline and differential.
DR Genevisible; Q02248; MM.
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: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:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
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:0008013; F:beta-catenin binding; ISO: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: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:0008022; F:protein C-terminus binding; ISO:MGI.
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: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:0044325; F:transmembrane transporter 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:ARUK-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:1904954; P:canonical Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; IC:ParkinsonsUK-UCL.
DR GO; GO:0044339; P:canonical Wnt signaling pathway involved in osteoblast differentiation; ISO:MGI.
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: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 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: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: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: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:0007249; P:I-kappaB kinase/NF-kappaB signaling; 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; ISO: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: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: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:1903204; P:negative regulation of oxidative stress-induced neuron death; 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: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: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: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; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:1904798; P:positive regulation of core promoter binding; IDA:BHF-UCL.
DR GO; GO:2000017; P:positive regulation of determination of dorsal identity; IDA:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:ParkinsonsUK-UCL.
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:0051571; P:positive regulation of histone H3-K4 methylation; IMP:BHF-UCL.
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:0044093; P:positive regulation of molecular function; IDA: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: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:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL.
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 from RNA polymerase II promoter; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; 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:1904796; P:regulation of core promoter binding; IDA: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; IC: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: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: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:0006351; P:transcription, DNA-templated; IMP: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 DisProt; DP00341; -.
DR Gene3D; 1.25.10.10; -; 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; PTHR45976; 1.
DR Pfam; PF00514; Arm; 4.
DR PRINTS; PR01869; BCATNINFAMLY.
DR SMART; SM00185; ARM; 12.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Cell adhesion; Cell junction;
KW Cell membrane; Cell projection; 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
