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UniProtKB/Swiss-Prot entry Q02248


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CTNB1_MOUSE
Primary accession number Q02248
Secondary accession numbers Q922W1 Q9D335
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 103)
Name and origin of the protein
Protein name Catenin beta-1
Synonym Beta-catenin
Gene name
Name: Ctnnb1
Synonyms: Catnb
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1509266 [NCBI, ExPASy, EBI, Israel, Japan]
Butz S., Stappert J., Weissig H., Kemler R.;
"Plakoglobin and beta-catenin: distinct but closely related.";
Science 257:1142-1144(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Colon, and Urinary bladder;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6;
TISSUE=Brain, and Mammary cancer;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH TCF7; TCF7L1; TCF7L2 AND LEF1.
DOI=10.1038/26989; PubMed=9783587 [NCBI, ExPASy, EBI, Israel, Japan]
Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H., Moerer P., van de Wetering M., Destree O., Clevers H.;
"The Xenopus Wnt effector XTcf-3 interacts with Groucho-related transcriptional repressors.";
Nature 395:608-612(1998).
[5]
INTERACTION WITH XIRP1.
DOI=10.1074/jbc.M707639200; PubMed=17925400 [NCBI, ExPASy, EBI, Israel, Japan]
Choi S., Gustafson-Wagner E.A., Wang Q., Harlan S.M., Sinn H.W., Lin J.L.-C., Lin J.J.-C.;
"The intercalated disc protein, mXin{alpha}, is capable of interacting with beta-catenin and bundling actin filaments.";
J. Biol. Chem. 282:36024-36036(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-654, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[7]
INTERACTION WITH SLC30A9.
DOI=10.1093/nar/gkm095; PubMed=17344318 [NCBI, ExPASy, EBI, Israel, Japan]
Chen Y.H., Yang C.K., Xia M., Ou C.Y., Stallcup M.R.;
"Role of GAC63 in transcriptional activation mediated by beta-catenin.";
Nucleic Acids Res. 35:2084-2092(2007).
[8]
REVIEW.
DOI=10.1006/bbrc.1999.1860; PubMed=10679188 [NCBI, ExPASy, EBI, Israel, Japan]
Kikuchi A.;
"Regulation of beta-catenin signaling in the Wnt pathway.";
Biochem. Biophys. Res. Commun. 268:243-248(2000).
[9]
INTERACTION WITH BAIAP1.
DOI=10.1006/bbrc.2000.2471; PubMed=10772923 [NCBI, ExPASy, EBI, Israel, Japan]
Dobrosotskaya I.Y., James G.L.;
"MAGI-1 interacts with beta-catenin and is associated with cell-cell adhesion structures.";
Biochem. Biophys. Res. Commun. 270:903-909(2000).
[10]
INTERACTION WITH CTNNA3.
PubMed=11590244 [NCBI, ExPASy, EBI, Israel, Japan]
Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J., Colpaert C., Bruyneel E., Mareel M., van Roy F.;
"AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein mediating strong cell-cell adhesion.";
J. Cell Sci. 114:3177-3188(2001).
[11]
INTERACTION WITH TAX1BP3.
DOI=10.1074/jbc.M306324200; PubMed=12874278 [NCBI, ExPASy, EBI, Israel, Japan]
Kanamori M., Sandy P., Marzinotto S., Benetti R., Kai C., Hayashizaki Y., Schneider C., Suzuki H.;
"The PDZ protein tax-interacting protein-1 inhibits beta-catenin transcriptional activity and growth of colorectal cancer cells.";
J. Biol. Chem. 278:38758-38764(2003).
[12]
INTERACTION WITH GLIS2, AND SUBCELLULAR LOCATION.
DOI=10.1016/j.febslet.2007.01.058; PubMed=17289029 [NCBI, ExPASy, EBI, Israel, Japan]
Kim Y.-S., Kang H.S., Jetten A.M.;
"The Kruppel-like zinc finger protein Glis2 functions as a negative modulator of the Wnt/beta-catenin signaling pathway.";
FEBS Lett. 581:858-864(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551 AND THR-556, AND MASS SPECTROMETRY.
TISSUE=Brain cortex;
DOI=10.1074/mcp.M600046-MCP200; PubMed=17114649 [NCBI, ExPASy, EBI, Israel, Japan]
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551; SER-552 AND THR-556, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan]
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[15]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 150-665.
DOI=10.1016/S0092-8674(00)80352-9; PubMed=9298899 [NCBI, ExPASy, EBI, Israel, Japan]
Huber A.H., Nelson W.J., Weis W.I.;
"Three-dimensional structure of the armadillo repeat region of beta-catenin.";
Cell 90:871-882(1997).
[16]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 118-149 IN COMPLEX WITH CTNNA1.
DOI=10.1016/S1097-2765(00)80447-5; PubMed=10882138 [NCBI, ExPASy, EBI, Israel, Japan]
Pokutta S., Weis W.I.;
"Structure of the dimerization and beta-catenin-binding region of alpha-catenin.";
Mol. Cell 5:533-543(2000).
[17]
X-RAY CRYSTALLOGRAPHY (2.0 AND 3.0 ANGSTROMS) OF 134-671 IN COMPLEX WITH PHOSPHORYLATED AND AND UNPHOSPHORYLATED CDH1.
DOI=10.1016/S0092-8674(01)00330-0; PubMed=11348595 [NCBI, ExPASy, EBI, Israel, Japan]
Huber A.H., Weis W.I.;
"The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin.";
Cell 105:391-402(2001).
[18]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH APC.
DOI=10.1093/emboj/20.22.6203; PubMed=11707392 [NCBI, ExPASy, EBI, Israel, Japan]
Eklof Spink K., Fridman S.G., Weis W.I.;
"Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex.";
EMBO J. 20:6203-6212(2001).
[19]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH CTNNBIP1, AND INTERACTION WITH EP300.
DOI=10.1016/S1097-2765(02)00631-7; PubMed=12408825 [NCBI, ExPASy, EBI, Israel, Japan]
Daniels D.L., Weis W.I.;
"ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules.";
Mol. Cell 10:573-584(2002).
Comments
  • FUNCTION: Involved in the regulation of cell adhesion and in signal transduction through the Wnt pathway.
  • SUBUNIT: Two separate pools are found in the cytoplasm: one is PSEN1/cadherin/catenin complex which anchors to the actin cytoskeleton. The other pool is part of a large complex containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. Wnt-dependent activation of DVL antagonizes the action of GSK3B. When GSK3B activity is inhibited the complex dissociates, CTNNB1 is dephosphorylated and is no longer targeted for destruction. The stabilized protein translocates to the nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9 and possibly also RUVBL1 and DUPLIN. Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 binding (By similarity). Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits the transcriptional activity of CTNNB1. Interacts with AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1 (By similarity). Interacts with GLIS2. Interacts with SLC30A9. Interacts with XIRP1. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain) (By similarity).
  • INTERACTION:
    P25054:APC (xeno); NbExp=3; IntAct=EBI-397872, EBI-727707;
    O15169:AXIN1 (xeno); NbExp=2; IntAct=EBI-397872, EBI-710484;
    P09803:Cdh1; NbExp=4; IntAct=EBI-397872, EBI-984420;
    P26231:Ctnna1; NbExp=1; IntAct=EBI-397872, EBI-647895;
    Q9NSA3:CTNNBIP1 (xeno); NbExp=3; IntAct=EBI-397872, EBI-747082;
    P27782:Lef1; NbExp=2; IntAct=EBI-397872, EBI-984464;
    P45984-1:MAPK9 (xeno); NbExp=1; IntAct=EBI-397872, EBI-713586;
    P26450:Pik3r1; NbExp=2; IntAct=EBI-397872, EBI-641764;
    P97458:Prop1; NbExp=2; IntAct=EBI-397872, EBI-937831;
    P49768:PSEN1 (xeno); NbExp=1; IntAct=EBI-397872, EBI-297277;
    P49769:Psen1; NbExp=1; IntAct=EBI-397872, EBI-990067;
    Q9DBG9:Tax1bp3; NbExp=4; IntAct=EBI-397872, EBI-1161647;
  • SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Nucleus. Note=Cytoplasmic when it is unstabilized (high level of phosphorylation) or bound to CDH1. Translocates to the nucleus when it is stabilized (low level of phosphorylation). Interaction with GLIS2 promotes nuclear translocation.
  • PTM: Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-33 (By similarity).
  • PTM: EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding (By similarity).
  • PTM: Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1A, APC and TBL1X (Probable). Its ubiquitination leads to its subsequent proteasomal degradation (By similarity).
  • SIMILARITY: Belongs to the beta-catenin family.
  • SIMILARITY: Contains 12 ARM repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M90364; AAA37280.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK035311; BAC29027.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK018515; BAB31250.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006739; AAH06739.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC048153; AAH48153.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC053065; AAH53065.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S35091; S35091.
RefSeq NP_031640.1; -.
UniGene Mm.291928
3D structure databases
PDB
1DOW; X-ray; 1.80 A; B=118-149.[ExPASy / RCSB / EBI]
1I7W; X-ray; 2.00 A; A/C=134-671.[ExPASy / RCSB / EBI]
1I7X; X-ray; 3.00 A; A/C=134-671.[ExPASy / RCSB / EBI]
1JPP; X-ray; 3.10 A; A/B=134-671.[ExPASy / RCSB / EBI]
1M1E; X-ray; 2.10 A; A=134-671.[ExPASy / RCSB / EBI]
1V18; X-ray; 2.10 A; A=134-671.[ExPASy / RCSB / EBI]
2BCT; X-ray; 2.90 A; A=150-665.[ExPASy / RCSB / EBI]
3BCT; X-ray; 2.10 A; A=193-662.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DOW; -.
1I7W; -.
1I7X; -.
1JPP; -.
1M1E; -.
1V18; -.
2BCT; -.
3BCT; -.
DisProt DP00341; -.
ModBase Q02248.
Protein-protein interaction databases
IntAct Q02248; -.
PTM databases
PhosphoSite Q02248; -.
Organism-specific databases
MGI MGI:88276; Ctnnb1.
Gene expression databases
ArrayExpress Q02248; -.
CleanEx MM_CTNNB1; -.
GermOnline ENSMUSG00000006932; Mus musculus.
Ontologies
GO
GO:0043296; Cellular component: apical junction complex (inferred from direct assay from MGI).
GO:0045177; Cellular component: apical part of cell (inferred from direct assay from MGI).
GO:0016323; Cellular component: basolateral plasma membrane (inferred from direct assay from MGI).
GO:0005856; Cellular component: cytoskeleton (inferred from electronic annotation from UniProtKB-KW).
GO:0005916; Cellular component: fascia adherens (inferred from direct assay from MGI).
GO:0030027; Cellular component: lamellipodium (inferred from direct assay from MGI).
GO:0016328; Cellular component: lateral plasma membrane (inferred from direct assay from MGI).
GO:0005624; Cellular component: membrane fraction (inferred from direct assay from MGI).
GO:0031528; Cellular component: microvillus membrane (inferred from direct assay from MGI).
GO:0005667; Cellular component: transcription factor complex (inferred from direct assay from MGI).
GO:0030018; Cellular component: Z disc (inferred from direct assay from MGI).
GO:0045294; Molecular function: alpha-catenin binding (inferred from physical interaction from MGI).
GO:0045296; Molecular function: cadherin binding (inferred from physical interaction from MGI).
GO:0003682; Molecular function: chromatin binding (inferred from direct assay from MGI).
GO:0003690; Molecular function: double-stranded DNA binding (inferred from direct assay from MGI).
GO:0005198; Molecular function: structural molecule activity (inferred from electronic annotation from UniProtKB-KW).
GO:0003713; Molecular function: transcription coactivator activity (inferred from direct assay from MGI).
GO:0003700; Molecular function: transcription factor activity (inferred from direct assay from MGI).
GO:0009948; Biological process: anterior/posterior axis specification (inferred from mutant phenotype from MGI).
GO:0006915; Biological process: apoptosis (inferred from mutant phenotype from MGI).
GO:0045453; Biological process: bone resorption (inferred from genetic interaction from MGI).
GO:0048593; Biological process: camera-type eye morphogenesis (inferred from mutant phenotype from MGI).
GO:0001709; Biological process: cell fate determination (inferred from mutant phenotype from MGI).
GO:0001708; Biological process: cell fate specification (inferred from mutant phenotype from MGI).
GO:0048469; Biological process: cell maturation (inferred from mutant phenotype from MGI).
GO:0000904; Biological process: cell morphogenesis involved in differentiation (inferred from mutant phenotype from MGI).
GO:0016337; Biological process: cell-cell adhesion (inferred from mutant phenotype from MGI).
GO:0007160; Biological process: cell-matrix adhesion (inferred from mutant phenotype from MGI).
GO:0009950; Biological process: dorsal/ventral axis specification (inferred from mutant phenotype from MGI).
GO:0007398; Biological process: ectoderm development (inferred from mutant phenotype from MGI).
GO:0035117; Biological process: embryonic arm morphogenesis (inferred from direct assay from MGI).
GO:0042733; Biological process: embryonic digit morphogenesis (inferred from mutant phenotype from MGI).
GO:0035116; Biological process: embryonic hindlimb morphogenesis (inferred from mutant phenotype from MGI).
GO:0001706; Biological process: endoderm formation (inferred from mutant phenotype from MGI).
GO:0001711; Biological process: endodermal cell fate commitment (inferred from mutant phenotype from MGI).
GO:0030900; Biological process: forebrain development (inferred from mutant phenotype from MGI).
GO:0001702; Biological process: gastrulation with mouth forming second (inferred from mutant phenotype from MGI).
GO:0007507; Biological process: heart development (inferred from mutant phenotype from MGI).
GO:0030324; Biological process: lung development (inferred from mutant phenotype from MGI).
GO:0016331; Biological process: morphogenesis of embryonic epithelium (inferred from mutant phenotype from MGI).
GO:0032331; Biological process: negative regulation of chondrocyte differentiation (inferred from genetic interaction from MGI).
GO:0045671; Biological process: negative regulation of osteoclast differentiation (inferred from mutant phenotype from MGI).
GO:0000122; Biological process: negative regulation of transcription from RNA polymerase II promoter (inferred from direct assay from MGI).
GO:0042475; Biological process: odontogenesis of dentine-containing tooth (inferred from mutant phenotype from MGI).
GO:0031016; Biological process: pancreas development (inferred from mutant phenotype from MGI).
GO:0001569; Biological process: patterning of blood vessels (inferred from mutant phenotype from MGI).
GO:0030858; Biological process: positive regulation of epithelial cell differentiation (inferred from mutant phenotype from MGI).
GO:0045669; Biological process: positive regulation of osteoblast differentiation (inferred from mutant phenotype from MGI).
GO:0045944; Biological process: positive regulation of transcription from RNA polymerase II promoter (inferred from direct assay from MGI).
GO:0009954; Biological process: proximal/distal pattern formation (inferred from mutant phenotype from MGI).
GO:0042127; Biological process: regulation of cell proliferation (inferred from direct assay from MGI).
GO:0050808; Biological process: synapse organization (inferred from mutant phenotype from MGI).
GO:0007268; Biological process: synaptic transmission (inferred from mutant phenotype from MGI).
GO:0048489; Biological process: synaptic vesicle transport (inferred from mutant phenotype from MGI).
GO:0060070; Biological process: Wnt receptor signaling pathway through beta-catenin (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR011989; ARM-like.
IPR000225; Armadillo.
IPR013284; Beta-catenin.
IPR000357; HEAT.
Graphical view of domain structure.
Gene3D G3DSA:1.25.10.10; ARM-like; 1.
Pfam PF00514; Arm; 6.
PF02985; HEAT; 1.
Pfam graphical view of domain structure.
PRINTS PR01869; BCATNINFAMLY.
SMART SM00185; ARM; 12.
SMART graphical view of domain structure.
PROSITE PS50176; ARM_REPEAT; 9.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q02248.
Genome annotation databases
Ensembl ENSMUSG00000006932; Mus musculus. [Contig view]
GeneID 12387; -.
KEGG mmu:12387; -.
Phylogenomic databases
HOGENOM Q02248; -.
HOVERGEN Q02248; -.
Other
LinkHub Q02248; -.
NextBio 281106; -.
SOURCE Ctnnb1; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Activator; Cell adhesion; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Repeat; Transcription; Transcription regulation; Ubl conjugation; Wnt signaling pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   781  781     Catenin beta-1. PRO_0000064272
REPEAT   151   191  41     ARM 1. 
REPEAT   193   234  42     ARM 2. 
REPEAT   235   276  42     ARM 3. 
REPEAT   277   318  42     ARM 4. 
REPEAT   319   360  42     ARM 5. 
REPEAT   361   389  29     ARM 6. 
REPEAT   400   441  42     ARM 7. 
REPEAT   442   484  43     ARM 8. 
REPEAT   489   530  42     ARM 9. 
REPEAT   531   571  41     ARM 10. 
REPEAT   594   636  43     ARM 11. 
REPEAT   637   666  30     ARM 12. 
MOD_RES   23    23        Phosphoserine; by GSK3-beta (By similarity). 
MOD_RES   29    29        Phosphoserine; by GSK3-beta (By similarity). 
MOD_RES   33    33        Phosphoserine; by GSK3-beta (By similarity). 
MOD_RES   37    37        Phosphoserine; by GSK3-beta (By similarity). 
MOD_RES   41    41        Phosphothreonine; by GSK3-beta (By similarity). 
MOD_RES   45    45        Phosphoserine (By similarity). 
MOD_RES   86    86        Phosphotyrosine; by CSK (By similarity). 
MOD_RES   191   191        Phosphoserine (By similarity). 
MOD_RES   551   551        Phosphothreonine. 
MOD_RES   552   552        Phosphoserine. 
MOD_RES   556   556        Phosphothreonine. 
MOD_RES   654   654        Phosphotyrosine. 
MOD_RES   675   675        Phosphoserine (By similarity). 
CONFLICT   371   371        T -> I (in Ref. 2; BAB31250). 
CONFLICT   478   478        A -> T (in Ref. 2; BAB31250). 
CONFLICT   487   487        L -> F (in Ref. 2; BAB31250). 
HELIX   121   141  21      
TURN   145   148  4      
TURN   150   152  3      
HELIX   153   160  8      
HELIX   165   180  16      
HELIX   182   189  8      
HELIX   192   204  13      
HELIX   208   221  14      
HELIX   225   233  9      
HELIX   236   242  7      
HELIX   243   245  3      
HELIX   249   265  17      
HELIX   269   275  7      
HELIX   278   284  7      
HELIX   285   287  3      
HELIX   291   305  15      
HELIX   309   317  9