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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
  • cadherin binding involved in cell-cell adhesion Source: MGI
  • chromatin binding Source: MGI
  • DNA binding Source: MGI
  • double-stranded DNA binding Source: MGI
  • enzyme binding Source: ParkinsonsUK-UCL
  • estrogen receptor binding Source: MGI
  • euchromatin binding Source: BHF-UCL
  • histone methyltransferase binding Source: BHF-UCL
  • ion channel binding Source: MGI
  • I-SMAD binding Source: MGI
  • kinase binding Source: MGI
  • nuclear hormone receptor binding Source: UniProtKB
  • protein C-terminus binding Source: MGI
  • protein heterodimerization activity Source: MGI
  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein phosphatase binding Source: UniProtKB
  • repressing transcription factor binding Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: MGI
  • RNA polymerase II transcription factor binding Source: MGI
  • signal transducer activity Source: InterPro
  • SMAD binding Source: MGI
  • transcription coactivator activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: MGI
  • transcription factor binding Source: BHF-UCL
  • transcription regulatory region DNA binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • adherens junction assembly Source: UniProtKB
  • adherens junction organization Source: MGI
  • animal organ development Source: MGI
  • anterior/posterior axis specification Source: MGI
  • beta-catenin destruction complex disassembly Source: Reactome
  • bone resorption Source: MGI
  • branching involved in ureteric bud morphogenesis Source: MGI
  • canonical Wnt signaling pathway Source: MGI
  • canonical Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation Source: ParkinsonsUK-UCL
  • canonical Wnt signaling pathway involved in negative regulation of apoptotic process Source: MGI
  • 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
  • central nervous system vasculogenesis Source: MGI
  • chemical synaptic transmission Source: MGI
  • chromatin-mediated maintenance of transcription Source: BHF-UCL
  • coronary artery morphogenesis Source: DFLAT
  • cranial ganglion development Source: ParkinsonsUK-UCL
  • cranial skeletal system development Source: ParkinsonsUK-UCL
  • dorsal/ventral axis specification Source: MGI
  • dorsal/ventral pattern formation Source: MGI
  • dorsal root ganglion development Source: ParkinsonsUK-UCL
  • ectoderm development Source: MGI
  • embryonic axis specification Source: MGI
  • embryonic brain development Source: ParkinsonsUK-UCL
  • 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
  • hindbrain development Source: ParkinsonsUK-UCL
  • 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
  • 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
  • mesenchyme development Source: DFLAT
  • mesenchyme morphogenesis Source: DFLAT
  • metanephros morphogenesis Source: MGI
  • midbrain development Source: ParkinsonsUK-UCL
  • midbrain dopaminergic neuron differentiation Source: ParkinsonsUK-UCL
  • morphogenesis of embryonic epithelium Source: MGI
  • 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 gene expression Source: ParkinsonsUK-UCL
  • negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis 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 oxidative stress-induced neuron death Source: ParkinsonsUK-UCL
  • 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 differentiation Source: ParkinsonsUK-UCL
  • neuron migration Source: MGI
  • odontogenesis of dentin-containing tooth Source: MGI
  • oocyte 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 chromatin-mediated maintenance of transcription Source: BHF-UCL
  • positive regulation of determination of dorsal identity Source: MGI
  • positive regulation of DNA-templated transcription, initiation Source: BHF-UCL
  • 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 neuron apoptotic process Source: MGI
  • positive regulation of osteoblast differentiation Source: MGI
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: ParkinsonsUK-UCL
  • 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 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 proliferation Source: MGI
  • regulation of centriole-centriole cohesion Source: UniProtKB
  • regulation of centromeric sister chromatid cohesion Source: BHF-UCL
  • regulation of chromatin-mediated maintenance of transcription Source: BHF-UCL
  • regulation of core promoter binding Source: BHF-UCL
  • regulation of epithelial cell differentiation Source: MGI
  • regulation of euchromatin binding Source: BHF-UCL
  • regulation of gene expression Source: MGI
  • regulation of histone demethylase activity (H3-K4 specific) Source: BHF-UCL
  • regulation of histone H3-K4 methylation Source: BHF-UCL
  • 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 drug Source: Ensembl
  • response to estradiol Source: UniProtKB
  • single organismal cell-cell adhesion Source: MGI
  • skeletal system development Source: MGI
  • skin development Source: MGI
  • smooth muscle cell differentiation Source: MGI
  • stem cell population maintenance Source: BHF-UCL
  • sympathetic ganglion development Source: UniProtKB
  • synapse organization 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

ReactomeiR-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-196299. Beta-catenin phosphorylation cascade.
R-MMU-201681. TCF dependent signaling in response to WNT.
R-MMU-201722. Formation of the beta-catenin:TCF transactivating complex.
R-MMU-3134973. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
R-MMU-351906. Apoptotic cleavage of cell adhesion proteins.
R-MMU-375170. CDO in myogenesis.
R-MMU-3769402. Deactivation of the beta-catenin transactivating complex.
R-MMU-4086398. Ca2+ pathway.
R-MMU-418990. Adherens junctions interactions.
R-MMU-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-MMU-5218920. VEGFR2 mediated vascular permeability.
R-MMU-5626467. 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
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:88276. Ctnnb1.

Subcellular locationi

  • Cytoplasm
  • Cytoplasmcytoskeleton
  • Nucleus 1 Publication
  • 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
  • beta-catenin-TCF complex Source: ParkinsonsUK-UCL
  • bicellular tight junction Source: MGI
  • 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: ParkinsonsUK-UCL
  • extracellular exosome Source: MGI
  • fascia adherens Source: MGI
  • flotillin complex Source: UniProtKB
  • focal adhesion Source: MGI
  • intercalated disc Source: MGI
  • lamellipodium Source: MGI
  • lateral plasma membrane Source: MGI
  • membrane Source: ParkinsonsUK-UCL
  • microvillus membrane Source: MGI
  • nuclear euchromatin Source: BHF-UCL
  • nuclear transcription factor complex Source: BHF-UCL
  • nucleus Source: UniProtKB
  • 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
  • transcription factor complex Source: MGI
  • Wnt signalosome Source: ParkinsonsUK-UCL
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi8M → P: Loss of interaction with VCL. 1 Publication1
Mutagenesisi33S → A: Abolished HIPK2-mediated proteasomal degradation. 1 Publication1
Mutagenesisi37S → A: Abolished HIPK2-mediated proteasomal degradation. 1 Publication1
Mutagenesisi552S → A: Abolishes AMPK-mediated phosphorylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000642722 – 781Catenin beta-1Add BLAST780

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei23Phosphoserine; by GSK3-beta; alternateBy similarity1
Glycosylationi23O-linked (GlcNAc); alternateBy similarity1
Modified residuei29Phosphoserine; by GSK3-betaBy similarity1
Modified residuei33Phosphoserine; by GSK3-beta and HIPK21 Publication1
Modified residuei37Phosphoserine; by GSK3-beta and HIPK21 Publication1
Modified residuei41Phosphothreonine; by GSK3-betaBy similarity1
Modified residuei45PhosphoserineCombined sources1
Modified residuei49N6-acetyllysineBy similarity1
Modified residuei64Phosphotyrosine; by PTK6By similarity1
Modified residuei86Phosphotyrosine; by CSKBy similarity1
Modified residuei142Phosphotyrosine; by FYN and PTK61 Publication1
Modified residuei191PhosphoserineCombined sources1
Modified residuei246Phosphoserine; by CDK5By similarity1
Modified residuei331PhosphotyrosineBy similarity1
Modified residuei552Phosphoserine; by AMPKCombined sources1 Publication1
Modified residuei556PhosphothreonineBy similarity1
Modified residuei619S-nitrosocysteine1 Publication1
Modified residuei654PhosphotyrosineBy similarity1
Modified residuei675PhosphoserineCombined sources1

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
Deacetylated at Lys-49 by SIRT1.By similarity

Keywords - PTMi

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

Proteomic databases

MaxQBiQ02248.
PaxDbiQ02248.
PeptideAtlasiQ02248.
PRIDEiQ02248.

PTM databases

iPTMnetiQ02248.
PhosphoSitePlusiQ02248.
SwissPalmiQ02248.

Miscellaneous databases

PMAP-CutDBQ02248.

Expressioni

Gene expression databases

BgeeiENSMUSG00000006932.
CleanExiMM_CTNNB1.
ExpressionAtlasiQ02248. baseline and differential.
GenevisibleiQ02248. MM.

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). Interacts with CTNND2 (By similarity). Interacts (via the C-terminal region) with CBY1 (By similarity).By similarity20 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APCP250548EBI-397872,EBI-727707From a different organism.
AXIN1O151695EBI-397872,EBI-710484From a different organism.
Cdh1P0980314EBI-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
PSEN1P497683EBI-397872,EBI-297277From a different organism.
RAPGEF2F1MSG62EBI-397872,EBI-6927068From a different organism.
RelaQ042075EBI-397872,EBI-644400
Tax1bp3Q9DBG96EBI-397872,EBI-1161647

GO - Molecular functioni

  • alpha-catenin binding Source: dictyBase
  • cadherin binding Source: MGI
  • cadherin binding involved in cell-cell adhesion Source: MGI
  • enzyme binding Source: ParkinsonsUK-UCL
  • estrogen receptor binding Source: MGI
  • histone methyltransferase binding Source: BHF-UCL
  • ion channel binding Source: MGI
  • I-SMAD binding Source: MGI
  • kinase binding Source: MGI
  • nuclear hormone receptor binding Source: UniProtKB
  • protein C-terminus binding Source: MGI
  • protein heterodimerization activity Source: MGI
  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein phosphatase binding Source: UniProtKB
  • repressing transcription factor binding Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: MGI
  • RNA polymerase II transcription factor binding Source: MGI
  • SMAD binding Source: MGI
  • transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi198512. 75 interactors.
DIPiDIP-31560N.
IntActiQ02248. 61 interactors.
MINTiMINT-103426.
STRINGi10090.ENSMUSP00000007130.

Structurei

Secondary structure

1781
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi85 – 88Combined sources4
Helixi90 – 98Combined sources9
Helixi100 – 102Combined sources3
Helixi121 – 141Combined sources21
Turni145 – 148Combined sources4
Turni150 – 152Combined sources3
Helixi153 – 160Combined sources8
Beta strandi161 – 164Combined sources4
Beta strandi166 – 168Combined sources3
Helixi169 – 171Combined sources3
Helixi172 – 178Combined sources7
Helixi182 – 189Combined sources8
Beta strandi192 – 194Combined sources3
Helixi195 – 204Combined sources10
Helixi208 – 221Combined sources14
Helixi225 – 233Combined sources9
Helixi236 – 242Combined sources7
Helixi243 – 245Combined sources3
Helixi249 – 265Combined sources17
Helixi269 – 275Combined sources7
Helixi278 – 284Combined sources7
Helixi285 – 287Combined sources3
Helixi291 – 305Combined sources15
Helixi309 – 317Combined sources9
Helixi320 – 330Combined sources11
Helixi334 – 347Combined sources14
Helixi353 – 359Combined sources7
Helixi362 – 367Combined sources6
Turni368 – 371Combined sources4
Helixi375 – 389Combined sources15
Helixi399 – 408Combined sources10
Helixi414 – 428Combined sources15
Helixi432 – 440Combined sources9
Helixi443 – 454Combined sources12
Helixi458 – 471Combined sources14
Beta strandi473 – 475Combined sources3
Helixi478 – 487Combined sources10
Helixi491 – 496Combined sources6
Helixi504 – 517Combined sources14
Helixi521 – 523Combined sources3
Helixi524 – 529Combined sources6
Helixi532 – 547Combined sources16
Helixi566 – 580Combined sources15
Helixi584 – 592Combined sources9
Helixi596 – 602Combined sources7
Helixi608 – 621Combined sources14
Helixi625 – 633Combined sources9
Turni634 – 636Combined sources3
Helixi637 – 643Combined sources7
Helixi649 – 661Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02248.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati151 – 191ARM 1Add BLAST41
Repeati193 – 234ARM 2Add BLAST42
Repeati235 – 276ARM 3Add BLAST42
Repeati277 – 318ARM 4Add BLAST42
Repeati319 – 360ARM 5Add BLAST42
Repeati361 – 389ARM 6Add BLAST29
Repeati400 – 441ARM 7Add BLAST42
Repeati442 – 484ARM 8Add BLAST43
Repeati489 – 530ARM 9Add BLAST42
Repeati531 – 571ARM 10Add BLAST41
Repeati594 – 636ARM 11Add BLAST43
Repeati637 – 666ARM 12Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 23Interaction with VCL1 PublicationAdd BLAST22
Regioni156 – 178Interaction with BCL9By similarityAdd BLAST23
Regioni772 – 781Interaction with SCRIB1 Publication10

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4203. Eukaryota.
COG0035. LUCA.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
InParanoidiQ02248.
KOiK02105.
OMAiFRTEPMT.
OrthoDBiEOG091G03A5.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti371T → I in BAB31250 (PubMed:16141072).Curated1
Sequence conflicti478A → T in BAB31250 (PubMed:16141072).Curated1
Sequence conflicti487L → F in BAB31250 (PubMed:16141072).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198512. 75 interactors.
DIPiDIP-31560N.
IntActiQ02248. 61 interactors.
MINTiMINT-103426.
STRINGi10090.ENSMUSP00000007130.

PTM databases

iPTMnetiQ02248.
PhosphoSitePlusiQ02248.
SwissPalmiQ02248.

Proteomic databases

MaxQBiQ02248.
PaxDbiQ02248.
PeptideAtlasiQ02248.
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

eggNOGiKOG4203. Eukaryota.
COG0035. LUCA.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
InParanoidiQ02248.
KOiK02105.
OMAiFRTEPMT.
OrthoDBiEOG091G03A5.
PhylomeDBiQ02248.
TreeFamiTF317997.

Enzyme and pathway databases

ReactomeiR-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-196299. Beta-catenin phosphorylation cascade.
R-MMU-201681. TCF dependent signaling in response to WNT.
R-MMU-201722. Formation of the beta-catenin:TCF transactivating complex.
R-MMU-3134973. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
R-MMU-351906. Apoptotic cleavage of cell adhesion proteins.
R-MMU-375170. CDO in myogenesis.
R-MMU-3769402. Deactivation of the beta-catenin transactivating complex.
R-MMU-4086398. Ca2+ pathway.
R-MMU-418990. Adherens junctions interactions.
R-MMU-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-MMU-5218920. VEGFR2 mediated vascular permeability.
R-MMU-5626467. RHO GTPases activate IQGAPs.

Miscellaneous databases

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

Gene expression databases

BgeeiENSMUSG00000006932.
CleanExiMM_CTNNB1.
ExpressionAtlasiQ02248. baseline and differential.
GenevisibleiQ02248. MM.

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...

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: November 30, 2016
This is version 197 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

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 one 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.