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Protein

Catenin beta-1

Gene

Ctnnb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (By similarity). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (PubMed:21325504).By similarity1 Publication

GO - Molecular functioni

  • alpha-catenin binding Source: dictyBase
  • cadherin binding Source: MGI
  • chromatin binding Source: MGI
  • DNA binding Source: MGI
  • double-stranded DNA binding Source: MGI
  • euchromatin binding Source: BHF-UCL
  • nuclear hormone receptor binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • repressing transcription factor binding Source: UniProtKB
  • sequence-specific DNA binding transcription factor activity Source: MGI
  • signal transducer activity Source: InterPro
  • transcription coactivator activity Source: UniProtKB
  • transcription factor binding Source: BHF-UCL
  • transcription regulatory region DNA binding Source: MGI

GO - Biological processi

  • adherens junction assembly Source: UniProtKB
  • adherens junction organization Source: MGI
  • anterior/posterior axis specification Source: MGI
  • bone resorption Source: MGI
  • branching involved in ureteric bud morphogenesis Source: MGI
  • canonical Wnt signaling pathway Source: MGI
  • canonical Wnt signaling pathway involved in negative regulation of apoptotic process Source: Ensembl
  • canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation Source: BHF-UCL
  • canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition Source: UniProtKB
  • cardiac muscle cell proliferation Source: DFLAT
  • cardiac vascular smooth muscle cell differentiation Source: DFLAT
  • cell adhesion Source: UniProtKB
  • cell differentiation Source: MGI
  • cell fate determination Source: MGI
  • cell fate specification Source: MGI
  • cell-matrix adhesion Source: MGI
  • cell maturation Source: MGI
  • cell morphogenesis involved in differentiation Source: MGI
  • cell proliferation Source: MGI
  • cellular process Source: MGI
  • cellular protein localization Source: MGI
  • cellular response to growth factor stimulus Source: UniProtKB
  • cellular response to indole-3-methanol Source: UniProtKB
  • cellular response to insulin-like growth factor stimulus Source: Ensembl
  • cellular response to mechanical stimulus Source: Ensembl
  • cellular response to organic cyclic compound Source: MGI
  • central nervous system vasculogenesis Source: MGI
  • chromatin-mediated maintenance of transcription Source: BHF-UCL
  • coronary artery morphogenesis Source: DFLAT
  • dorsal/ventral axis specification Source: MGI
  • dorsal/ventral pattern formation Source: MGI
  • ectoderm development Source: MGI
  • embryonic axis specification Source: MGI
  • embryonic digit morphogenesis Source: MGI
  • embryonic foregut morphogenesis Source: MGI
  • embryonic forelimb morphogenesis Source: MGI
  • embryonic heart tube development Source: MGI
  • embryonic hindlimb morphogenesis Source: MGI
  • embryonic skeletal limb joint morphogenesis Source: BHF-UCL
  • endodermal cell fate commitment Source: MGI
  • endoderm formation Source: MGI
  • endothelial tube morphogenesis Source: UniProtKB
  • epicardium-derived cardiac vascular smooth muscle cell differentiation Source: DFLAT
  • epithelial cell differentiation involved in prostate gland development Source: MGI
  • epithelial tube branching involved in lung morphogenesis Source: MGI
  • forebrain development Source: MGI
  • fungiform papilla formation Source: MGI
  • gastrulation with mouth forming second Source: MGI
  • genitalia morphogenesis Source: MGI
  • glial cell fate determination Source: MGI
  • hair cycle process Source: MGI
  • hair follicle morphogenesis Source: MGI
  • hair follicle placode formation Source: MGI
  • heart development Source: MGI
  • hemopoiesis Source: MGI
  • in utero embryonic development Source: MGI
  • kidney development Source: MGI
  • layer formation in cerebral cortex Source: MGI
  • lens morphogenesis in camera-type eye Source: MGI
  • limb development Source: MGI
  • liver development Source: Ensembl
  • lung-associated mesenchyme development Source: MGI
  • lung cell differentiation Source: MGI
  • lung development Source: MGI
  • lung induction Source: MGI
  • male genitalia development Source: MGI
  • mesenchymal cell proliferation involved in lung development Source: MGI
  • mesenchymal to epithelial transition involved in metanephros morphogenesis Source: MGI
  • mesenchyme development Source: DFLAT
  • mesenchyme morphogenesis Source: DFLAT
  • metanephros morphogenesis Source: MGI
  • midgut development Source: Ensembl
  • morphogenesis of embryonic epithelium Source: MGI
  • myoblast differentiation Source: Ensembl
  • negative regulation of apoptotic signaling pathway Source: MGI
  • negative regulation of cell differentiation Source: MGI
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of chondrocyte differentiation Source: MGI
  • negative regulation of mitotic cell cycle, embryonic Source: UniProtKB
  • negative regulation of neuron death Source: MGI
  • negative regulation of oligodendrocyte differentiation Source: MGI
  • negative regulation of osteoclast differentiation Source: MGI
  • negative regulation of protein sumoylation Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • nephron tubule formation Source: MGI
  • neural plate development Source: MGI
  • neuron migration Source: MGI
  • odontogenesis of dentin-containing tooth Source: MGI
  • oocyte development Source: MGI
  • organ development Source: MGI
  • osteoclast differentiation Source: MGI
  • oviduct development Source: MGI
  • pancreas development Source: MGI
  • patterning of blood vessels Source: MGI
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of branching involved in lung morphogenesis Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of determination of dorsal identity Source: MGI
  • positive regulation of endothelial cell differentiation Source: MGI
  • positive regulation of epithelial cell differentiation Source: MGI
  • positive regulation of epithelial cell proliferation involved in prostate gland development Source: MGI
  • positive regulation of epithelial to mesenchymal transition Source: DFLAT
  • positive regulation of fibroblast growth factor receptor signaling pathway Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of heparan sulfate proteoglycan biosynthetic process Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of mesenchymal cell proliferation Source: MGI
  • positive regulation of neuroblast proliferation Source: UniProtKB
  • positive regulation of osteoblast differentiation Source: MGI
  • positive regulation of skeletal muscle tissue development Source: CACAO
  • positive regulation of telomerase activity Source: BHF-UCL
  • positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein heterooligomerization Source: Ensembl
  • protein localization to cell surface Source: UniProtKB
  • proximal/distal pattern formation Source: MGI
  • regulation of apoptotic process Source: MGI
  • regulation of calcium ion import Source: UniProtKB
  • regulation of cell differentiation Source: MGI
  • regulation of cell fate specification Source: GO_Central
  • regulation of cell proliferation Source: MGI
  • regulation of centriole-centriole cohesion Source: UniProtKB
  • regulation of centromeric sister chromatid cohesion Source: BHF-UCL
  • regulation of epithelial cell differentiation Source: MGI
  • regulation of gene expression Source: MGI
  • regulation of myelination Source: MGI
  • regulation of nephron tubule epithelial cell differentiation Source: UniProtKB
  • regulation of osteoblast differentiation Source: MGI
  • regulation of osteoclast differentiation Source: MGI
  • regulation of protein localization to cell surface Source: UniProtKB
  • regulation of secondary heart field cardioblast proliferation Source: MGI
  • regulation of smooth muscle cell proliferation Source: UniProtKB
  • regulation of T cell proliferation Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • renal inner medulla development Source: MGI
  • renal outer medulla development Source: MGI
  • renal system development Source: MGI
  • renal vesicle formation Source: MGI
  • response to cadmium ion Source: Ensembl
  • response to cytokine Source: Ensembl
  • response to drug Source: Ensembl
  • response to estradiol Source: UniProtKB
  • Schwann cell proliferation Source: Ensembl
  • single organismal cell-cell adhesion Source: MGI
  • skeletal system development Source: MGI
  • skin development Source: MGI
  • smooth muscle cell differentiation Source: MGI
  • stem cell maintenance Source: BHF-UCL
  • sympathetic ganglion development Source: UniProtKB
  • synapse organization Source: MGI
  • synaptic transmission Source: MGI
  • synaptic vesicle transport Source: MGI
  • T cell differentiation Source: MGI
  • T cell differentiation in thymus Source: MGI
  • thymus development Source: MGI
  • trachea formation Source: MGI
  • trachea morphogenesis Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
  • vasculature development Source: MGI
  • vasculogenesis Source: MGI
  • ventricular compact myocardium morphogenesis Source: DFLAT
  • Wnt signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell adhesion, Neurogenesis, Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_303008. Beta-catenin phosphorylation cascade.
REACT_304595. CDO in myogenesis.
REACT_307189. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_308832. Adherens junctions interactions.
REACT_317277. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_321965. VEGFR2 mediated vascular permeability.
REACT_325952. formation of the beta-catenin:TCF transactivating complex.
REACT_331940. Ca2+ pathway.
REACT_335672. TCF dependent signaling in response to WNT.
REACT_343176. Apoptotic cleavage of cell adhesion proteins.
REACT_351655. deactivation of the beta-catenin transactivating complex.
REACT_358203. RHO GTPases activate IQGAPs.

Names & Taxonomyi

Protein namesi
Recommended name:
Catenin beta-1
Alternative name(s):
Beta-catenin
Gene namesi
Name:Ctnnb1
Synonyms:Catnb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:88276. Ctnnb1.

Subcellular locationi

  • Cytoplasm
  • Cytoplasmcytoskeleton
  • Nucleus
  • Cell junctionadherens junction
  • Cell membrane By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
  • Cytoplasmcytoskeletonspindle pole By similarity

  • 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. Interaction with EMD inhibits nuclear localization. The majority of beta-catenin is localized to the cell membrane. In interphase, colocalizes with CROCC between CEP250 puncta at the proximal end of centrioles, and this localization is dependent on CROCC and CEP250. In mitosis, when NEK2 activity increases, it localizes to centrosomes at spindle poles independent of CROCC. Colocalizes with CDK5 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells. Colocalized with RAPGEF2 and TJP1 at cell-cell contacts (By similarity).By similarity

GO - Cellular componenti

  • adherens junction Source: MGI
  • apical junction complex Source: MGI
  • apical part of cell Source: MGI
  • basolateral plasma membrane Source: MGI
  • beta-catenin destruction complex Source: UniProtKB
  • beta-catenin-TCF7L2 complex Source: UniProtKB
  • catenin complex Source: UniProtKB
  • catenin-TCF7L2 complex Source: BHF-UCL
  • cell-cell adherens junction Source: MGI
  • cell-cell junction Source: MGI
  • cell cortex Source: UniProtKB
  • cell junction Source: UniProtKB
  • cell periphery Source: BHF-UCL
  • cell projection membrane Source: MGI
  • centrosome Source: BHF-UCL
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • dendritic shaft Source: Ensembl
  • extracellular exosome Source: Ensembl
  • fascia adherens Source: MGI
  • focal adhesion Source: Ensembl
  • intercalated disc Source: MGI
  • lamellipodium Source: MGI
  • lateral plasma membrane Source: MGI
  • membrane Source: MGI
  • microvillus membrane Source: MGI
  • nuclear euchromatin Source: BHF-UCL
  • nuclear transcription factor complex Source: BHF-UCL
  • nucleus Source: BHF-UCL
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • protein complex Source: MGI
  • protein-DNA complex Source: UniProtKB
  • Scrib-APC-beta-catenin complex Source: BHF-UCL
  • spindle pole Source: UniProtKB-SubCell
  • synapse Source: Ensembl
  • tight junction Source: MGI
  • transcription factor complex Source: MGI
  • Z disc Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Sympathetic ganglia-specific conditional knockout mice lead to a reduction in sympathetic ganglia size and in progenitor cell number, but does not alter sympathetic innervation of peripheral target organs.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81M → P: Loss of interaction with VCL. 1 Publication
Mutagenesisi33 – 331S → A: Abolished HIPK2-mediated proteasomal degradation. 1 Publication
Mutagenesisi37 – 371S → A: Abolished HIPK2-mediated proteasomal degradation. 1 Publication
Mutagenesisi552 – 5521S → A: Abolishes AMPK-mediated phosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 781780Catenin beta-1PRO_0000064272Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei23 – 231Phosphoserine; by GSK3-beta; alternateBy similarity
Glycosylationi23 – 231O-linked (GlcNAc); alternateBy similarity
Modified residuei29 – 291Phosphoserine; by GSK3-betaBy similarity
Modified residuei33 – 331Phosphoserine; by GSK3-beta and HIPK21 Publication
Modified residuei37 – 371Phosphoserine; by GSK3-beta and HIPK21 Publication
Modified residuei41 – 411Phosphothreonine; by GSK3-betaBy similarity
Modified residuei45 – 451PhosphoserineBy similarity
Modified residuei64 – 641Phosphotyrosine; by PTK6By similarity
Modified residuei86 – 861Phosphotyrosine; by CSKBy similarity
Modified residuei142 – 1421Phosphotyrosine; by FYN and PTK61 Publication
Modified residuei191 – 1911Phosphoserine; alternate1 Publication
Modified residuei191 – 1911Phosphoserine; by CDK5; alternateBy similarity
Modified residuei246 – 2461Phosphoserine; by CDK5By similarity
Modified residuei331 – 3311PhosphotyrosineBy similarity
Modified residuei552 – 5521Phosphoserine; by AMPK2 Publications
Modified residuei556 – 5561PhosphothreonineBy similarity
Modified residuei619 – 6191S-nitrosocysteine1 Publication
Modified residuei654 – 6541PhosphotyrosineBy similarity
Modified residuei675 – 6751Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding (By similarity). Phosphorylated on Ser-33 and Ser-37 by HIPK2. This phosphorylation triggers proteasomal degradation. Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription. Phosphorylation on Ser-191 and Ser-246 by CDK5. Phosphorylation by CDK2 regulates insulin internalization (By similarity). Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or Tyr-333 with the predominant site at Tyr-64 is not essential for inhibition of transcriptional activity (By similarity).By similarity
Ubiquitinated by the SCF(BTRC) E3 ligase complex when phosphorylated by GSK3B, leading to its degradation. Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent proteasomal degradation (By similarity).By similarity
S-nitrosylation at Cys-619 within adherens junctions promotes VEGF-induced, NO-dependent endothelial cell permeability by disrupting interaction with E-cadherin, thus mediating disassembly adherens junctions.1 Publication
O-glycosylation at Ser-23 decreases nuclear localization and transcriptional activity, and increases localization to the plasma membrane and interaction with E-cadherin CDH1.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

MaxQBiQ02248.
PaxDbiQ02248.
PRIDEiQ02248.

PTM databases

PhosphoSiteiQ02248.

Miscellaneous databases

PMAP-CutDBQ02248.

Expressioni

Gene expression databases

BgeeiQ02248.
CleanExiMM_CTNNB1.
ExpressionAtlasiQ02248. baseline and differential.
GenevestigatoriQ02248.

Interactioni

Subunit structurei

Two separate complex-associated pools are found in the cytoplasm. The majority is present as component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1 and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Binds SLC9A3R1. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain) and with EMD. Interacts with SESTD1 and TRPC4. Interacts with CAV1. Interacts with PTPRJ. Interacts with PKT7. Interacts with FAT1 (via the cytoplasmic domain). Interacts with CDK2, NDRG2 and NANOS1. Interacts with NEK2 and CDK5. Interacts with CARM1, CXADR, PCDH11Y and PTK6. Interacts with RAPGEF2. Interacts with SOX7; this interaction may lead to proteasomal degradation of active CTNNB1 and thus inhibition of Wnt/beta-catenin-stimulated transcription. Identified in a complex with HINT1 and MITF. Interacts with FHIT. Interacts with FERMT2. Identified in a complex with TCF4 and FERMT2. Another cytoplasmic pool is part of a large complex containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. Wnt-dependent activation of DVL antagonizes the action of GSK3B. When GSK3B activity is inhibited the complex dissociates, CTNNB1 is dephosphorylated and is no longer targeted for destruction. The stabilized protein translocates to the nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9, BCL9L and possibly also RUVBL1 and CHD8. Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits the transcriptional activity of CTNNB1. Interacts with AJAP1, BAIAP1 and CTNNA3. Interacts with TRPV4; the TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with VCL. The CTNNB1 and TCF4 complex interacts with PML. Interacts with XIRP1. Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 binding. Interacts directly with AXIN1; the interaction is regulated by CDK2 phosphorylation of AXIN1. Interacts with GLIS2. Interacts with SCRIB. Interacts with TNIK and TCF7L2. Interacts with SLC30A9. Interacts with RORA. May interact with P-cadherin/CDH3. Interacts with RNF220 (By similarity).By similarity20 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APCP250548EBI-397872,EBI-727707From a different organism.
AXIN1O151695EBI-397872,EBI-710484From a different organism.
Cdh1P0980313EBI-397872,EBI-984420
CrebbpP454813EBI-397872,EBI-296306
Ctnna1P262312EBI-397872,EBI-647895
CTNNBIP1Q9NSA37EBI-397872,EBI-747082From a different organism.
Gsk3bQ9WV602EBI-397872,EBI-400793
HttP428593EBI-397872,EBI-5327353
Lef1P277826EBI-397872,EBI-984464
Prop1P974582EBI-397872,EBI-937831
RAPGEF2F1MSG62EBI-397872,EBI-6927068From a different organism.
RelaQ042075EBI-397872,EBI-644400
Tax1bp3Q9DBG96EBI-397872,EBI-1161647

Protein-protein interaction databases

BioGridi198512. 73 interactions.
DIPiDIP-31560N.
IntActiQ02248. 58 interactions.
MINTiMINT-103426.

Structurei

Secondary structure

1
781
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi85 – 884Combined sources
Helixi90 – 989Combined sources
Helixi100 – 1023Combined sources
Helixi121 – 14121Combined sources
Turni145 – 1484Combined sources
Turni150 – 1523Combined sources
Helixi153 – 1608Combined sources
Beta strandi161 – 1644Combined sources
Beta strandi166 – 1683Combined sources
Helixi169 – 1713Combined sources
Helixi172 – 1787Combined sources
Helixi182 – 1898Combined sources
Beta strandi192 – 1943Combined sources
Helixi195 – 20410Combined sources
Helixi208 – 22114Combined sources
Helixi225 – 2339Combined sources
Helixi236 – 2427Combined sources
Helixi243 – 2453Combined sources
Helixi249 – 26517Combined sources
Helixi269 – 2757Combined sources
Helixi278 – 2847Combined sources
Helixi285 – 2873Combined sources
Helixi291 – 30515Combined sources
Helixi309 – 3179Combined sources
Helixi320 – 33011Combined sources
Helixi334 – 34714Combined sources
Helixi353 – 3597Combined sources
Helixi362 – 3676Combined sources
Turni368 – 3714Combined sources
Helixi375 – 38915Combined sources
Helixi399 – 40810Combined sources
Helixi414 – 42815Combined sources
Helixi432 – 4409Combined sources
Helixi443 – 45412Combined sources
Helixi458 – 47114Combined sources
Beta strandi473 – 4753Combined sources
Helixi478 – 48710Combined sources
Helixi491 – 4966Combined sources
Helixi504 – 51714Combined sources
Helixi521 – 5233Combined sources
Helixi524 – 5296Combined sources
Helixi532 – 54716Combined sources
Helixi566 – 58015Combined sources
Helixi584 – 5929Combined sources
Helixi596 – 6027Combined sources
Helixi608 – 62114Combined sources
Helixi625 – 6339Combined sources
Turni634 – 6363Combined sources
Helixi637 – 6437Combined sources
Helixi649 – 66113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DOWX-ray1.80B118-149[»]
1I7WX-ray2.00A/C134-671[»]
1I7XX-ray3.00A/C134-671[»]
1JPPX-ray3.10A/B134-671[»]
1M1EX-ray2.10A134-671[»]
1V18X-ray2.10A134-671[»]
2BCTX-ray2.90A150-665[»]
3BCTX-ray2.10A193-661[»]
3OUWX-ray2.91A134-671[»]
3OUXX-ray2.40A134-671[»]
4EV8X-ray1.90A134-671[»]
4EV9X-ray2.10A134-671[»]
4EVAX-ray2.00A/C134-671[»]
4EVPX-ray2.26A134-671[»]
4EVTX-ray2.34A134-671[»]
4ONSX-ray2.80B/D78-151[»]
DisProtiDP00341.
ProteinModelPortaliQ02248.
SMRiQ02248. Positions 19-44, 84-665.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02248.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati151 – 19141ARM 1Add
BLAST
Repeati193 – 23442ARM 2Add
BLAST
Repeati235 – 27642ARM 3Add
BLAST
Repeati277 – 31842ARM 4Add
BLAST
Repeati319 – 36042ARM 5Add
BLAST
Repeati361 – 38929ARM 6Add
BLAST
Repeati400 – 44142ARM 7Add
BLAST
Repeati442 – 48443ARM 8Add
BLAST
Repeati489 – 53042ARM 9Add
BLAST
Repeati531 – 57141ARM 10Add
BLAST
Repeati594 – 63643ARM 11Add
BLAST
Repeati637 – 66630ARM 12Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2322Interaction with VCLAdd
BLAST
Regioni156 – 17823Interaction with BCL9By similarityAdd
BLAST
Regioni772 – 78110Interaction with SCRIB

Sequence similaritiesi

Belongs to the beta-catenin family.Curated
Contains 12 ARM repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG297695.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
InParanoidiQ02248.
KOiK02105.
OMAiMRAFQDT.
OrthoDBiEOG7X9G6B.
PhylomeDBiQ02248.
TreeFamiTF317997.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamiPF00514. Arm. 4 hits.
[Graphical view]
PRINTSiPR01869. BCATNINFAMLY.
SMARTiSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG
60 70 80 90 100
NPEEEDVDTS QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP
110 120 130 140 150
ETLDEGMQIP STQFDAAHPT NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT
160 170 180 190 200
RAIPELTKLL NDEDQVVVNK AAVMVHQLSK KEASRHAIMR SPQMVSAIVR
210 220 230 240 250
TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL VKMLGSPVDS
260 270 280 290 300
VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC
310 320 330 340 350
LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC
360 370 380 390 400
SSNKPAIVEA GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG
410 420 430 440 450
LLGTLVQLLG SDDINVVTCA AGILSNLTCN NYKNKMMVCQ VGGIEALVRT
460 470 480 490 500
VLRAGDREDI TEPAICALRH LTSRHQEAEM AQNAVRLHYG LPVVVKLLHP
510 520 530 540 550
PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL VRAHQDTQRR
560 570 580 590 600
TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV
610 620 630 640 650
QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG
660 670 680 690 700
VATYAAAVLF RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI
710 720 730 740 750
GAQGEALGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV
760 770 780
DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L
Length:781
Mass (Da):85,471
Last modified:July 1, 1993 - v1
Checksum:iD708F170A3FBED6E
GO

Sequence cautioni

The sequence AAH06739.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti371 – 3711T → I in BAB31250 (PubMed:16141072).Curated
Sequence conflicti478 – 4781A → T in BAB31250 (PubMed:16141072).Curated
Sequence conflicti487 – 4871L → F in BAB31250 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90364 mRNA. Translation: AAA37280.1.
AK035311 mRNA. Translation: BAC29027.1.
AK018515 mRNA. Translation: BAB31250.1.
BC006739 mRNA. Translation: AAH06739.1. Different initiation.
BC048153 mRNA. Translation: AAH48153.1.
BC053065 mRNA. Translation: AAH53065.1.
CCDSiCCDS23630.1.
PIRiS35091.
RefSeqiNP_001159374.1. NM_001165902.1.
NP_031640.1. NM_007614.3.
UniGeneiMm.291928.

Genome annotation databases

EnsembliENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932.
ENSMUST00000178812; ENSMUSP00000136294; ENSMUSG00000006932.
GeneIDi12387.
KEGGimmu:12387.
UCSCiuc009scu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90364 mRNA. Translation: AAA37280.1.
AK035311 mRNA. Translation: BAC29027.1.
AK018515 mRNA. Translation: BAB31250.1.
BC006739 mRNA. Translation: AAH06739.1. Different initiation.
BC048153 mRNA. Translation: AAH48153.1.
BC053065 mRNA. Translation: AAH53065.1.
CCDSiCCDS23630.1.
PIRiS35091.
RefSeqiNP_001159374.1. NM_001165902.1.
NP_031640.1. NM_007614.3.
UniGeneiMm.291928.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DOWX-ray1.80B118-149[»]
1I7WX-ray2.00A/C134-671[»]
1I7XX-ray3.00A/C134-671[»]
1JPPX-ray3.10A/B134-671[»]
1M1EX-ray2.10A134-671[»]
1V18X-ray2.10A134-671[»]
2BCTX-ray2.90A150-665[»]
3BCTX-ray2.10A193-661[»]
3OUWX-ray2.91A134-671[»]
3OUXX-ray2.40A134-671[»]
4EV8X-ray1.90A134-671[»]
4EV9X-ray2.10A134-671[»]
4EVAX-ray2.00A/C134-671[»]
4EVPX-ray2.26A134-671[»]
4EVTX-ray2.34A134-671[»]
4ONSX-ray2.80B/D78-151[»]
DisProtiDP00341.
ProteinModelPortaliQ02248.
SMRiQ02248. Positions 19-44, 84-665.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198512. 73 interactions.
DIPiDIP-31560N.
IntActiQ02248. 58 interactions.
MINTiMINT-103426.

PTM databases

PhosphoSiteiQ02248.

Proteomic databases

MaxQBiQ02248.
PaxDbiQ02248.
PRIDEiQ02248.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932.
ENSMUST00000178812; ENSMUSP00000136294; ENSMUSG00000006932.
GeneIDi12387.
KEGGimmu:12387.
UCSCiuc009scu.2. mouse.

Organism-specific databases

CTDi1499.
MGIiMGI:88276. Ctnnb1.

Phylogenomic databases

eggNOGiNOG297695.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
InParanoidiQ02248.
KOiK02105.
OMAiMRAFQDT.
OrthoDBiEOG7X9G6B.
PhylomeDBiQ02248.
TreeFamiTF317997.

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_303008. Beta-catenin phosphorylation cascade.
REACT_304595. CDO in myogenesis.
REACT_307189. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_308832. Adherens junctions interactions.
REACT_317277. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_321965. VEGFR2 mediated vascular permeability.
REACT_325952. formation of the beta-catenin:TCF transactivating complex.
REACT_331940. Ca2+ pathway.
REACT_335672. TCF dependent signaling in response to WNT.
REACT_343176. Apoptotic cleavage of cell adhesion proteins.
REACT_351655. deactivation of the beta-catenin transactivating complex.
REACT_358203. RHO GTPases activate IQGAPs.

Miscellaneous databases

ChiTaRSiCtnnb1. mouse.
EvolutionaryTraceiQ02248.
NextBioi281106.
PMAP-CutDBQ02248.
PROiQ02248.
SOURCEiSearch...

Gene expression databases

BgeeiQ02248.
CleanExiMM_CTNNB1.
ExpressionAtlasiQ02248. baseline and differential.
GenevestigatoriQ02248.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamiPF00514. Arm. 4 hits.
[Graphical view]
PRINTSiPR01869. BCATNINFAMLY.
SMARTiSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Plakoglobin and beta-catenin: distinct but closely related."
    Butz S., Stappert J., Weissig H., Kemler R.
    Science 257:1142-1144(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Colon and Urinary bladder.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain and Mammary cancer.
  4. "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion."
    Butz S., Kemler R.
    FEBS Lett. 355:195-200(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
  5. "The Xenopus Wnt effector XTcf-3 interacts with Groucho-related transcriptional repressors."
    Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H., Moerer P., van de Wetering M., Destree O., Clevers H.
    Nature 395:608-612(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TCF7; TCF7L1; TCF7L2 AND LEF1.
  6. "A GSK3beta phosphorylation site in axin modulates interaction with beta-catenin and Tcf-mediated gene expression."
    Jho E., Lomvardas S., Costantini F.
    Biochem. Biophys. Res. Commun. 266:28-35(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXIN1.
  7. "MAGI-1 interacts with beta-catenin and is associated with cell-cell adhesion structures."
    Dobrosotskaya I.Y., James G.L.
    Biochem. Biophys. Res. Commun. 270:903-909(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAIAP1.
  8. "AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein mediating strong cell-cell adhesion."
    Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J., Colpaert C., Bruyneel E., Mareel M., van Roy F.
    J. Cell Sci. 114:3177-3188(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTNNA3.
  9. "The PDZ protein tax-interacting protein-1 inhibits beta-catenin transcriptional activity and growth of colorectal cancer cells."
    Kanamori M., Sandy P., Marzinotto S., Benetti R., Kai C., Hayashizaki Y., Schneider C., Suzuki H.
    J. Biol. Chem. 278:38758-38764(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAX1BP3.
  10. "p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction."
    Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N., Garcia de Herreros A., Dunach M.
    Mol. Cell. Biol. 23:2287-2297(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-142 BY FYN.
  11. "RORalpha coordinates reciprocal signaling in cerebellar development through sonic hedgehog and calcium-dependent pathways."
    Gold D.A., Baek S.H., Schork N.J., Rose D.W., Larsen D.D., Sachs B.D., Rosenfeld M.G., Hamilton B.A.
    Neuron 40:1119-1131(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RORA.
  12. "Cyclin-dependent kinase 2 regulates the interaction of Axin with beta-catenin."
    Kim S.I., Park C.S., Lee M.S., Kwon M.S., Jho E.H., Song W.K.
    Biochem. Biophys. Res. Commun. 317:478-483(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXIN1.
  13. "Deconstructing the cadherin-catenin-actin complex."
    Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.
    Cell 123:889-901(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
  14. "Crystal structure of a beta-catenin/BCL9/Tcf4 complex."
    Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.
    Mol. Cell 24:293-300(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL9L.
  15. "The Kruppel-like zinc finger protein Glis2 functions as a negative modulator of the Wnt/beta-catenin signaling pathway."
    Kim Y.-S., Kang H.S., Jetten A.M.
    FEBS Lett. 581:858-864(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GLIS2, SUBCELLULAR LOCATION.
  16. "The intercalated disc protein, mXin{alpha}, is capable of interacting with beta-catenin and bundling actin filaments."
    Choi S., Gustafson-Wagner E.A., Wang Q., Harlan S.M., Sinn H.W., Lin J.L.-C., Lin J.J.-C.
    J. Biol. Chem. 282:36024-36036(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XIRP1.
  17. "Role of GAC63 in transcriptional activation mediated by beta-catenin."
    Chen Y.H., Yang C.K., Xia M., Ou C.Y., Stallcup M.R.
    Nucleic Acids Res. 35:2084-2092(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC30A9.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-552 AND SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt."
    Abe K., Takeichi M.
    Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
  20. "The kinase TNIK is an essential activator of Wnt target genes."
    Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., Heck A.J., Clevers H.
    EMBO J. 28:3329-3340(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TCF7L2 AND TNIK.
  21. "Scribble interacts with beta-catenin to localize synaptic vesicles to synapses."
    Sun Y., Aiga M., Yoshida E., Humbert P.O., Bamji S.X.
    Mol. Biol. Cell 20:3390-3400(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCRIB.
  22. "Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-catenin for phosphorylation and proteasomal degradation."
    Kim E.-A., Kim J.E., Sung K.S., Choi D.W., Lee B.J., Choi C.Y.
    Biochem. Biophys. Res. Commun. 394:966-971(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2, MUTAGENESIS OF SER-33 AND SER-37.
  23. "AMP-activated protein kinase (AMPK) cross-talks with canonical Wnt signaling via phosphorylation of beta-catenin at Ser 552."
    Zhao J., Yue W., Zhu M.J., Sreejayan N., Du M.
    Biochem. Biophys. Res. Commun. 395:146-151(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-552, MUTAGENESIS OF SER-552.
  24. "The TRPV4 channel contributes to intercellular junction formation in keratinocytes."
    Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.
    J. Biol. Chem. 285:18749-18758(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRPV4 AND CDH1.
  25. "Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin."
    Peng X., Cuff L.E., Lawton C.D., DeMali K.A.
    J. Cell Sci. 123:567-577(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VCL, MUTAGENESIS OF MET-8.
  26. "Regulation of beta-catenin signaling in the Wnt pathway."
    Kikuchi A.
    Biochem. Biophys. Res. Commun. 268:243-248(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  27. "S-nitrosylation of beta-catenin by eNOS-derived NO promotes VEGF-induced endothelial cell permeability."
    Thibeault S., Rautureau Y., Oubaha M., Faubert D., Wilkes B.C., Delisle C., Gratton J.P.
    Mol. Cell 39:468-476(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION AT CYS-619, SUBCELLULAR LOCATION.
  28. "Frizzled3 is required for neurogenesis and target innervation during sympathetic nervous system development."
    Armstrong A., Ryu Y.K., Chieco D., Kuruvilla R.
    J. Neurosci. 31:2371-2381(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUT.
  29. "Three-dimensional structure of the armadillo repeat region of beta-catenin."
    Huber A.H., Nelson W.J., Weis W.I.
    Cell 90:871-882(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 150-665.
  30. "Structure of the dimerization and beta-catenin-binding region of alpha-catenin."
    Pokutta S., Weis W.I.
    Mol. Cell 5:533-543(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 118-149 IN COMPLEX WITH CTNNA1.
  31. "The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin."
    Huber A.H., Weis W.I.
    Cell 105:391-402(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 AND 3.0 ANGSTROMS) OF 134-671 IN COMPLEX WITH PHOSPHORYLATED AND UNPHOSPHORYLATED CDH1.
  32. "Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex."
    Eklof Spink K., Fridman S.G., Weis W.I.
    EMBO J. 20:6203-6212(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH APC.
  33. "ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules."
    Daniels D.L., Weis W.I.
    Mol. Cell 10:573-584(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH CTNNBIP1, INTERACTION WITH EP300.

Entry informationi

Entry nameiCTNB1_MOUSE
AccessioniPrimary (citable) accession number: Q02248
Secondary accession number(s): Q922W1, Q9D335
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 27, 2015
This is version 180 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.