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Q02248 (CTNB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Catenin beta-1
Alternative name(s):
Beta-catenin
Gene names
Name:Ctnnb1
Synonyms:Catnb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length781 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML By similarity.

Subunit structure

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20 Ref.21 Ref.24 Ref.25 Ref.32

Subcellular location

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. Ref.15 Ref.27

Post-translational modification

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. Ref.10 Ref.22 Ref.23

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. Ref.10 Ref.22 Ref.23

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.

Sequence similarities

Belongs to the beta-catenin family.

Contains 12 ARM repeats.

Sequence caution

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

Ontologies

Keywords
   Biological processCell adhesion
Transcription
Transcription regulation
Wnt signaling pathway
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   DomainRepeat
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSchwann cell proliferation

Inferred from Biological aspect of Ancestor. Source: RefGenome

T cell differentiation

Inferred from mutant phenotype PubMed 14608382. Source: MGI

T cell differentiation in thymus

Inferred from mutant phenotype PubMed 16025118. Source: MGI

Wnt signaling pathway

Inferred from direct assay PubMed 12235125PubMed 12464179PubMed 12717450. Source: MGI

adherens junction assembly

Inferred from sequence or structural similarity. Source: UniProtKB

anterior/posterior axis specification

Inferred from mutant phenotype PubMed 10662781. Source: MGI

bone resorption

Inferred from mutant phenotype PubMed 15866165. Source: MGI

branching involved in ureteric bud morphogenesis

Inferred from mutant phenotype PubMed 17537789. Source: MGI

canonical Wnt signaling pathway

Inferred from direct assay PubMed 15781477. Source: MGI

canonical Wnt signaling pathway involved in negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation

Inferred from mutant phenotype PubMed 12464179. Source: BHF-UCL

canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: UniProtKB

cardiac muscle cell proliferation

Traceable author statement PubMed 20299672. Source: DFLAT

cardiac vascular smooth muscle cell differentiation

Traceable author statement PubMed 20299672. Source: DFLAT

cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

cell death

Inferred from genetic interaction PubMed 22956852. Source: MGI

cell differentiation

Inferred from mutant phenotype PubMed 15131783PubMed 16192304. Source: MGI

cell fate determination

Inferred from mutant phenotype PubMed 15708565. Source: MGI

cell fate specification

Inferred from mutant phenotype PubMed 15866163. Source: MGI

cell maturation

Inferred from direct assay PubMed 17706960. Source: MGI

cell morphogenesis involved in differentiation

Inferred from mutant phenotype PubMed 16102745. Source: MGI

cell proliferation

Inferred from mutant phenotype PubMed 15131783. Source: MGI

cell-cell adhesion

Inferred from mutant phenotype PubMed 16102745. Source: MGI

cell-matrix adhesion

Inferred from mutant phenotype PubMed 15131783. Source: MGI

cellular process

Inferred from direct assay PubMed 12717450. Source: MGI

cellular protein localization

Inferred from mutant phenotype PubMed 16621792. Source: MGI

cellular response to growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to indole-3-methanol

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from direct assay PubMed 12055200. Source: MGI

central nervous system vasculogenesis

Inferred from mutant phenotype PubMed 19023080. Source: MGI

coronary artery morphogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

cytoskeletal anchoring at plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

dorsal/ventral axis specification

Inferred from mutant phenotype PubMed 12923052. Source: MGI

dorsal/ventral pattern formation

Inferred from mutant phenotype PubMed 15708565. Source: MGI

ectoderm development

Inferred from mutant phenotype PubMed 8582267. Source: MGI

embryonic axis specification

Inferred from direct assay PubMed 9230313. Source: MGI

embryonic digit morphogenesis

Inferred from mutant phenotype PubMed 12923052PubMed 20043884. Source: MGI

embryonic foregut morphogenesis

Inferred from mutant phenotype PubMed 18692041. Source: MGI

embryonic forelimb morphogenesis

Inferred from direct assay PubMed 15371327. Source: MGI

embryonic heart tube development

Inferred from mutant phenotype PubMed 18231602. Source: MGI

embryonic hindlimb morphogenesis

Inferred from mutant phenotype PubMed 12923052PubMed 18231602. Source: MGI

embryonic skeletal limb joint morphogenesis

Inferred from genetic interaction PubMed 21262216. Source: BHF-UCL

endoderm formation

Inferred from mutant phenotype PubMed 12194849PubMed 23824574. Source: MGI

endodermal cell fate commitment

Inferred from mutant phenotype PubMed 12194849. Source: MGI

endothelial tube morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

epicardium-derived cardiac vascular smooth muscle cell differentiation

Traceable author statement PubMed 20299672. Source: DFLAT

epithelial cell differentiation involved in prostate gland development

Inferred from mutant phenotype PubMed 12813461. Source: MGI

epithelial tube branching involved in lung morphogenesis

Inferred from mutant phenotype PubMed 18231602. Source: MGI

forebrain development

Inferred from mutant phenotype PubMed 15708565. Source: MGI

fungiform papilla formation

Inferred from mutant phenotype PubMed 17128274. Source: MGI

gastrulation with mouth forming second

Inferred from mutant phenotype PubMed 8582267. Source: MGI

genitalia morphogenesis

Inferred from mutant phenotype PubMed 18635608. Source: MGI

glial cell fate determination

Inferred from direct assay PubMed 17706960. Source: MGI

hair cycle process

Inferred from mutant phenotype PubMed 11371349. Source: MGI

hair follicle morphogenesis

Inferred from mutant phenotype PubMed 11371349. Source: MGI

hair follicle placode formation

Inferred from mutant phenotype PubMed 11371349. Source: MGI

heart development

Inferred from mutant phenotype PubMed 12464179. Source: MGI

hemopoiesis

Inferred from direct assay PubMed 12717450. Source: MGI

hindbrain development

Inferred from Biological aspect of Ancestor. Source: RefGenome

in utero embryonic development

Inferred from mutant phenotype PubMed 18231602. Source: MGI

kidney development

Inferred from mutant phenotype PubMed 17537789. Source: MGI

layer formation in cerebral cortex

Inferred from mutant phenotype PubMed 20503375. Source: MGI

lens morphogenesis in camera-type eye

Inferred from mutant phenotype PubMed 16102745. Source: MGI

limb development

Inferred from mutant phenotype PubMed 12569130. Source: MGI

liver development

Inferred from Biological aspect of Ancestor. Source: RefGenome

lung cell differentiation

Inferred from mutant phenotype PubMed 19805295. Source: MGI

lung development

Inferred from mutant phenotype PubMed 12885771PubMed 18231602. Source: MGI

lung induction

Inferred from mutant phenotype PubMed 19686689PubMed 19805295. Source: MGI

lung-associated mesenchyme development

Inferred from mutant phenotype PubMed 18533146. Source: MGI

male genitalia development

Inferred from mutant phenotype PubMed 19282366. Source: MGI

mesenchymal cell proliferation involved in lung development

Inferred from mutant phenotype PubMed 17128274PubMed 18231602. Source: MGI

mesenchymal to epithelial transition involved in metanephros morphogenesis

Inferred from direct assay PubMed 17537789. Source: MGI

mesenchyme development

Traceable author statement PubMed 20299672. Source: DFLAT

mesenchyme morphogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

metanephros morphogenesis

Inferred from mutant phenotype PubMed 19060336. Source: MGI

midgut development

Inferred from electronic annotation. Source: Ensembl

morphogenesis of embryonic epithelium

Inferred from mutant phenotype PubMed 16102745. Source: MGI

myoblast differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic signaling pathway

Inferred from mutant phenotype PubMed 15131783PubMed 20454446. Source: MGI

negative regulation of cell differentiation

Inferred from mutant phenotype PubMed 15866163PubMed 16102745. Source: MGI

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of chondrocyte differentiation

Inferred from genetic interaction PubMed 16818445. Source: MGI

negative regulation of heart induction by canonical Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of oligodendrocyte differentiation

Inferred from mutant phenotype PubMed 19503085. Source: MGI

negative regulation of osteoclast differentiation

Inferred from mutant phenotype PubMed 15866165. Source: MGI

negative regulation of protein sumoylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16040629. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12551949. Source: MGI

nephron tubule formation

Inferred from mutant phenotype PubMed 17537789. Source: MGI

neural plate development

Inferred from direct assay PubMed 22102609. Source: MGI

neuron migration

Inferred from genetic interaction PubMed 21937711. Source: MGI

odontogenesis of dentin-containing tooth

Inferred from mutant phenotype PubMed 15866165. Source: MGI

oocyte development

Inferred from genetic interaction PubMed 20454446. Source: MGI

organ development

Inferred from mutant phenotype PubMed 18635608. Source: MGI

osteoclast differentiation

Inferred from mutant phenotype PubMed 15866165. Source: MGI

oviduct development

Inferred from mutant phenotype PubMed 17532316. Source: MGI

pancreas development

Inferred from mutant phenotype PubMed 16192304. Source: MGI

patterning of blood vessels

Inferred from mutant phenotype PubMed 12975353PubMed 19154719. Source: MGI

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 19619491. Source: MGI

positive regulation of MAPK cascade

Inferred from genetic interaction PubMed 16478791. Source: MGI

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of branching involved in lung morphogenesis

Inferred from mutant phenotype PubMed 18533146. Source: MGI

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 19690384. Source: MGI

positive regulation of determination of dorsal identity

Inferred from direct assay PubMed 18316368. Source: MGI

positive regulation of endothelial cell differentiation

Inferred from mutant phenotype PubMed 18231602. Source: MGI

positive regulation of epithelial cell differentiation

Inferred from mutant phenotype PubMed 16040629. Source: MGI

positive regulation of epithelial cell proliferation involved in prostate gland development

Inferred from mutant phenotype PubMed 12813461. Source: MGI

positive regulation of epithelial to mesenchymal transition

Traceable author statement PubMed 20299672. Source: DFLAT

positive regulation of fibroblast growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 18231602PubMed 18533146. Source: MGI

positive regulation of gene expression

Inferred from mutant phenotype PubMed 18231602PubMed 19690384. Source: MGI

positive regulation of heparan sulfate proteoglycan biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mesenchymal cell proliferation

Inferred from mutant phenotype PubMed 18231602PubMed 18533146. Source: MGI

positive regulation of neuroblast proliferation

Inferred from genetic interaction PubMed 21937711. Source: MGI

positive regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 15866163. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12949260. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein localization to cell surface

Inferred from sequence or structural similarity. Source: UniProtKB

proximal/distal pattern formation

Inferred from mutant phenotype PubMed 12885771. Source: MGI

regulation of T cell proliferation

Inferred from mutant phenotype PubMed 14608382. Source: MGI

regulation of apoptotic process

Inferred from mutant phenotype PubMed 20043884. Source: MGI

regulation of calcium ion import

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell differentiation

Inferred from direct assay PubMed 12717450. Source: MGI

regulation of cell proliferation

Inferred from direct assay PubMed 12235125. Source: MGI

regulation of centriole-centriole cohesion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of centromeric sister chromatid cohesion

Inferred from mutant phenotype PubMed 20300119. Source: BHF-UCL

regulation of epithelial cell differentiation

Inferred from mutant phenotype PubMed 12813461. Source: MGI

regulation of gene expression

Inferred from mutant phenotype PubMed 22102609. Source: MGI

regulation of myelination

Inferred from mutant phenotype PubMed 19515974. Source: MGI

regulation of nephron tubule epithelial cell differentiation

Inferred from mutant phenotype PubMed 19112489. Source: UniProtKB

regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 15576404PubMed 15802266. Source: MGI

regulation of osteoclast differentiation

Inferred from mutant phenotype PubMed 15802266. Source: MGI

regulation of protein localization to cell surface

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of secondary heart field cardioblast proliferation

Inferred from direct assay PubMed 19620969. Source: MGI

regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20043884. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12235125PubMed 12464179. Source: MGI

renal inner medulla development

Inferred from mutant phenotype PubMed 19060336. Source: MGI

renal outer medulla development

Inferred from mutant phenotype PubMed 19060336. Source: MGI

renal system development

Inferred from mutant phenotype PubMed 18635608. Source: MGI

renal vesicle formation

Inferred from mutant phenotype PubMed 17537789. Source: MGI

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from sequence or structural similarity. Source: UniProtKB

response to estrogen

Inferred from Biological aspect of Ancestor. Source: RefGenome

skeletal system development

Inferred from mutant phenotype PubMed 15866163. Source: MGI

skin development

Inferred from mutant phenotype PubMed 19718027. Source: MGI

smooth muscle cell differentiation

Inferred from mutant phenotype PubMed 19690384. Source: MGI

synapse organization

Inferred from mutant phenotype PubMed 14622577. Source: MGI

synaptic transmission

Inferred from mutant phenotype PubMed 14622577. Source: MGI

synaptic vesicle transport

Inferred from mutant phenotype PubMed 14622577. Source: MGI

thymus development

Inferred from mutant phenotype PubMed 16025118. Source: MGI

trachea formation

Inferred from mutant phenotype PubMed 19805295. Source: MGI

trachea morphogenesis

Inferred from mutant phenotype PubMed 18231602PubMed 18692041. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

vasculogenesis

Inferred from mutant phenotype PubMed 18231602. Source: MGI

ventricular compact myocardium morphogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

   Cellular_componentScrib-APC-beta-catenin complex

Inferred from direct assay PubMed 16611247. Source: BHF-UCL

Z disc

Inferred from direct assay PubMed 8821035. Source: MGI

adherens junction

Inferred from direct assay PubMed 12203715PubMed 12695331PubMed 21991385PubMed 23824574. Source: MGI

apical junction complex

Inferred from direct assay PubMed 16249236PubMed 17130295PubMed 17666436. Source: MGI

apical part of cell

Inferred from direct assay PubMed 14758363PubMed 15037549PubMed 16249236. Source: MGI

basolateral plasma membrane

Inferred from direct assay PubMed 12885771PubMed 14625387PubMed 15226261PubMed 17671182PubMed 20016102PubMed 20089884PubMed 9950951. Source: MGI

beta-catenin destruction complex

Inferred from sequence or structural similarity. Source: UniProtKB

beta-catenin-TCF7L2 complex

Inferred from sequence or structural similarity. Source: UniProtKB

catenin complex

Inferred from sequence or structural similarity. Source: UniProtKB

catenin-TCF7L2 complex

Inferred from direct assay PubMed 9488439. Source: BHF-UCL

cell cortex

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from sequence or structural similarity. Source: UniProtKB

cell periphery

Inferred from sequence or structural similarity. Source: BHF-UCL

cell projection membrane

Inferred from direct assay PubMed 16621792. Source: MGI

cell-cell adherens junction

Inferred from direct assay PubMed 11731229PubMed 14657280PubMed 15148305PubMed 15292239PubMed 15645444PubMed 15775979PubMed 16199027PubMed 16892058PubMed 17544522. Source: MGI

cell-cell junction

Inferred from direct assay PubMed 12181493PubMed 14597196PubMed 18816447PubMed 20089884PubMed 21377456PubMed 9950951. Source: MGI

cell-substrate adherens junction

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from direct assay PubMed 20300119. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 11731231PubMed 11731265PubMed 12235125PubMed 12923052PubMed 14981260PubMed 15525667PubMed 15574752PubMed 16489008PubMed 17128274PubMed 19213727. Source: MGI

cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Inferred from direct assay PubMed 12055200PubMed 15673614. Source: MGI

dendritic shaft

Inferred from Biological aspect of Ancestor. Source: RefGenome

desmosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

fascia adherens

Inferred from direct assay PubMed 16481394. Source: MGI

intercalated disc

Inferred from direct assay PubMed 17535849. Source: MGI

lamellipodium

Inferred from direct assay PubMed 14657280. Source: MGI

lateral plasma membrane

Inferred from direct assay PubMed 15645444. Source: MGI

membrane

Inferred from direct assay PubMed 11731231PubMed 12055200PubMed 12432063PubMed 12611902PubMed 14657280PubMed 15987773PubMed 16364283PubMed 16510873PubMed 21991325PubMed 8821035. Source: MGI

microvillus membrane

Inferred from direct assay PubMed 16439479. Source: MGI

nucleus

Inferred from direct assay PubMed 11731231PubMed 11731265PubMed 11872843Ref.9PubMed 12885771PubMed 12923052PubMed 15371327PubMed 15574752PubMed 15778706PubMed 15866163PubMed 15866165PubMed 16439479PubMed 16489008PubMed 16678815PubMed 16858399PubMed 16936075PubMed 16989802PubMed 17128274PubMed 17560563PubMed 17596282PubMed 17615359PubMed 19213727PubMed 19497282PubMed 19796622PubMed 19850029PubMed 21991325PubMed 23266329PubMed 23610556. Source: MGI

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 17976063. Source: UniProtKB

protein-DNA complex

Inferred from sequence or structural similarity. Source: UniProtKB

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from Biological aspect of Ancestor. Source: RefGenome

tight junction

Inferred from direct assay PubMed 17130295. Source: MGI

transcription factor complex

Inferred from direct assay PubMed 12464179PubMed 12861022PubMed 16678101. Source: MGI

zonula adherens

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionDNA binding

Inferred from direct assay PubMed 12235125. Source: MGI

alpha-catenin binding

Inferred from physical interaction PubMed 21393547. Source: dictyBase

cadherin binding

Inferred from physical interaction PubMed 15057752. Source: MGI

chromatin binding

Inferred from direct assay PubMed 15024079PubMed 15778706PubMed 15907834PubMed 16581771PubMed 16678101PubMed 16818445PubMed 17767158PubMed 19619491PubMed 19620969PubMed 19690384PubMed 20159597PubMed 21350016PubMed 21512031. Source: MGI

double-stranded DNA binding

Inferred from direct assay PubMed 16678101. Source: MGI

protein kinase binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein phosphatase binding

Inferred from physical interaction PubMed 16973135. Source: UniProtKB

repressing transcription factor binding

Inferred from physical interaction PubMed 17331723. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12235125. Source: MGI

structural molecule activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription coactivator activity

Inferred from direct assay PubMed 12949260. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 16678101. Source: MGI

transcription regulatory region DNA binding

Inferred from direct assay PubMed 19056892. Source: MGI

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 781780Catenin beta-1
PRO_0000064272

Regions

Repeat151 – 19141ARM 1
Repeat193 – 23442ARM 2
Repeat235 – 27642ARM 3
Repeat277 – 31842ARM 4
Repeat319 – 36042ARM 5
Repeat361 – 38929ARM 6
Repeat400 – 44142ARM 7
Repeat442 – 48443ARM 8
Repeat489 – 53042ARM 9
Repeat531 – 57141ARM 10
Repeat594 – 63643ARM 11
Repeat637 – 66630ARM 12
Region2 – 2322Interaction with VCL
Region156 – 17823Interaction with BCL9 By similarity
Region772 – 78110Interaction with SCRIB

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue231Phosphoserine; by GSK3-beta By similarity
Modified residue291Phosphoserine; by GSK3-beta By similarity
Modified residue331Phosphoserine; by GSK3-beta and HIPK2 Ref.22
Modified residue371Phosphoserine; by GSK3-beta and HIPK2 Ref.22
Modified residue411Phosphothreonine; by GSK3-beta By similarity
Modified residue451Phosphoserine By similarity
Modified residue641Phosphotyrosine; by PTK6 By similarity
Modified residue861Phosphotyrosine; by CSK By similarity
Modified residue1421Phosphotyrosine; by FYN and PTK6 Ref.10
Modified residue1911Phosphoserine; alternate Ref.18
Modified residue1911Phosphoserine; by CDK5; alternate By similarity
Modified residue2461Phosphoserine; by CDK5 By similarity
Modified residue3311Phosphotyrosine By similarity
Modified residue5511Phosphothreonine By similarity
Modified residue5521Phosphoserine; by AMPK Ref.18 Ref.23
Modified residue5561Phosphothreonine By similarity
Modified residue6191S-nitrosocysteine Ref.27
Modified residue6541Phosphotyrosine By similarity
Modified residue6751Phosphoserine Ref.18

Experimental info

Mutagenesis81M → P: Loss of interaction with VCL. Ref.25
Mutagenesis331S → A: Abolished HIPK2-mediated proteasomal degradation. Ref.22
Mutagenesis371S → A: Abolished HIPK2-mediated proteasomal degradation. Ref.22
Mutagenesis5521S → A: Abolishes AMPK-mediated phosphorylation. Ref.23
Sequence conflict3711T → I in BAB31250. Ref.2
Sequence conflict4781A → T in BAB31250. Ref.2
Sequence conflict4871L → F in BAB31250. Ref.2

Secondary structure

.................................................................................... 781
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02248 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: D708F170A3FBED6E

FASTA78185,471
        10         20         30         40         50         60 
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTS 

        70         80         90        100        110        120 
QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDAAHPT 

       130        140        150        160        170        180 
NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK 

       190        200        210        220        230        240 
KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL 

       250        260        270        280        290        300 
VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC 

       310        320        330        340        350        360 
LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC SSNKPAIVEA 

       370        380        390        400        410        420 
GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA 

       430        440        450        460        470        480 
AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM 

       490        500        510        520        530        540 
AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL 

       550        560        570        580        590        600 
VRAHQDTQRR TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV 

       610        620        630        640        650        660 
QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF 

       670        680        690        700        710        720 
RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI GAQGEALGYR QDDPSYRSFH 

       730        740        750        760        770        780 
SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD 


L 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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]"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.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS35091.
RefSeqNP_001159374.1. NM_001165902.1.
NP_031640.1. NM_007614.3.
XP_006511990.1. XM_006511927.1.
UniGeneMm.291928.

3D structure databases

PDBe
RCSB PDB
PDBj
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-ray2.10A193-662[»]
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[»]
DisProtDP00341.
ProteinModelPortalQ02248.
SMRQ02248. Positions 19-44, 99-665.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198512. 69 interactions.
DIPDIP-31560N.
IntActQ02248. 53 interactions.
MINTMINT-103426.

PTM databases

PhosphoSiteQ02248.

Proteomic databases

PaxDbQ02248.
PRIDEQ02248.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932.
ENSMUST00000178812; ENSMUSP00000136294; ENSMUSG00000006932.
GeneID12387.
KEGGmmu:12387.
UCSCuc009scu.2. mouse.

Organism-specific databases

CTD1499.
MGIMGI:88276. Ctnnb1.

Phylogenomic databases

eggNOGNOG297695.
GeneTreeENSGT00730000110821.
HOGENOMHOG000230958.
HOVERGENHBG000919.
InParanoidQ02248.
KOK02105.
OMAQLSQTRS.
OrthoDBEOG7X9G6B.
PhylomeDBQ02248.
TreeFamTF317997.

Gene expression databases

ArrayExpressQ02248.
BgeeQ02248.
CleanExMM_CTNNB1.
GenevestigatorQ02248.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamPF00514. Arm. 4 hits.
[Graphical view]
PRINTSPR01869. BCATNINFAMLY.
SMARTSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50176. ARM_REPEAT. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTNNB1. mouse.
EvolutionaryTraceQ02248.
NextBio281106.
PMAP-CutDBQ02248.
PROQ02248.
SOURCESearch...

Entry information

Entry nameCTNB1_MOUSE
AccessionPrimary (citable) accession number: Q02248
Secondary accession number(s): Q922W1, Q9D335
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot