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P35222 (CTNB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:CTNNB
ORF Names:OK/SW-cl.35, PRO2286
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. Ref.37 Ref.40 Ref.41 Ref.47 Ref.56 Ref.60 Ref.61 Ref.62

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. 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. Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 binding. Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits the transcriptional activity of CTNNB1. Interacts with AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1. Interacts with GLIS2 and MUC1. Interacts with SLC30A9. Interacts with XIRP1. Interacts directly with AXIN1; the interaction is regulated by CDK2 phosphorylation of AXIN1. Interacts with SCRIB. Interacts with RAPGEF2. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain). Interacts with EMD. Interacts with TNIK and TCF7L2. Interacts with SESTD1 and TRPC4. Interacts with CAV1. Interacts with TRPV4. The TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with VCL. Interacts with PTPRJ. Interacts with PKT7 and CDK2. Interacts with FAT1 (via the cytoplasmic domain). Interacts with NANOS1 and NDRG2. Interacts with isoform 1 of NEK2. Interacts with both isoform 1 and isoform 2 of CDK5. Interacts with PTK6. 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. The CTNNB1 and TCF7L2/TCF4 complex interacts with PML (isoform PML-4) Interacts with FERMT2. Identified in a complex with TCF7L2/TCF4 and FERMT2. Interacts with RORA. May interact with P-cadherin/CDH3. Ref.10 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.24 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.43 Ref.44 Ref.46 Ref.50 Ref.51 Ref.52 Ref.53 Ref.56 Ref.57 Ref.58 Ref.60 Ref.61 Ref.62 Ref.69

Subcellular location

Cytoplasm. Nucleus. Cytoplasmcytoskeleton. Cell junctionadherens junction. Cell junction. Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle pole. Note: Colocalized with RAPGEF2 and TJP1 at cell-cell contacts By similarity. 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 and MUC1 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. Ref.34 Ref.36 Ref.37 Ref.38 Ref.39 Ref.41 Ref.56 Ref.61

Tissue specificity

Expressed in several hair follicle cell types: basal and peripheral matrix cells, and cells of the outer and inner root sheaths. Expressed in colon. Present in cortical neurons (at protein level). Ref.15 Ref.38 Ref.39

Post-translational modification

Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription By similarity. Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-37 and Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding. Phosphorylated on Ser-33 and Ser-37 by HIPK2. This phosphorylation triggers proteasomal degradation. Phosphorylation on Ser-191 and Ser-246 by CDK5. Phosphorylation by CDK2 regulates insulin internalization. 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. Ref.13 Ref.14 Ref.17 Ref.23 Ref.25 Ref.26 Ref.27 Ref.32 Ref.39 Ref.41 Ref.49 Ref.53 Ref.56

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.13 Ref.14 Ref.17 Ref.23 Ref.25 Ref.26 Ref.27 Ref.32 Ref.39 Ref.41 Ref.49 Ref.53 Ref.56

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 By similarity.

Involvement in disease

Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
Note: The gene represented in this entry may be involved in disease pathogenesis.

Activating mutations in CTNNB1 have oncogenic activity resulting in tumor development. Somatic mutations are found in various tumor types, including colon cancers, ovarian and prostate carcinomas, hepatoblastoma (HB), hepatocellular carcinoma (HCC). HBs are malignant embryonal tumors mainly affecting young children in the first three years of life.

Pilomatrixoma (PTR) [MIM:132600]: Common benign skin tumor.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.25 Ref.75

Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children.
Note: The gene represented in this entry may be involved in disease pathogenesis. Ref.25 Ref.77

Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

A chromosomal aberration involving CTNNB1 is found in salivary gland pleiomorphic adenomas, the most common benign epithelial tumors of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1.

Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle-shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos.
Note: The gene represented in this entry may be involved in disease pathogenesis. Ref.21

Mental retardation, autosomal dominant 19 (MRD19) [MIM:615075]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD19 features include severe intellectual disability with absent or very limited speech, microcephaly, and spasticity which severely impaired the ability to walk.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.63

Sequence similarities

Belongs to the beta-catenin family.

Contains 12 ARM repeats.

Sequence caution

The sequence BAB93475.1 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
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Mental retardation
   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 in thymus

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt signaling pathway

Inferred from direct assay PubMed 10644691. Source: BHF-UCL

adherens junction assembly

Inferred from mutant phenotype PubMed 20086044PubMed 20123964. Source: BHF-UCL

androgen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

anterior/posterior axis specification

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement. Source: Reactome

bone resorption

Inferred from electronic annotation. Source: Ensembl

branching involved in ureteric bud morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

canonical Wnt signaling pathway

Inferred from direct assay PubMed 12937339PubMed 19187541. Source: UniProtKB

canonical Wnt signaling pathway involved in negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 12154096. Source: BHF-UCL

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

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

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

Inferred from mutant phenotype PubMed 17072303. Source: BHF-UCL

cell adhesion

Inferred from mutant phenotype PubMed 19101069. Source: BHF-UCL

cell fate specification

Inferred from electronic annotation. Source: Ensembl

cell maturation

Inferred from electronic annotation. Source: Ensembl

cell-cell adhesion

Inferred from mutant phenotype PubMed 18593713. Source: BHF-UCL

cell-matrix adhesion

Inferred from Biological aspect of Ancestor. Source: RefGenome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cellular response to growth factor stimulus

Inferred from mutant phenotype Ref.36. Source: BHF-UCL

cellular response to indole-3-methanol

Inferred from direct assay PubMed 10868478. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

central nervous system vasculogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoskeletal anchoring at plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

determination of dorsal/ventral asymmetry

Inferred from Biological aspect of Ancestor. Source: RefGenome

dorsal/ventral axis specification

Inferred from Biological aspect of Ancestor. Source: RefGenome

ectoderm development

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic axis specification

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic digit morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic foregut morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic forelimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic heart tube development

Inferred from electronic annotation. Source: Ensembl

embryonic hindlimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic limb morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic skeletal limb joint morphogenesis

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

endodermal cell fate commitment

Inferred from Biological aspect of Ancestor. Source: RefGenome

endothelial tube morphogenesis

Inferred from mutant phenotype PubMed 20123964. Source: BHF-UCL

epithelial cell differentiation involved in prostate gland development

Inferred from electronic annotation. Source: Ensembl

epithelial to mesenchymal transition

Traceable author statement PubMed 14679171. Source: HGNC

epithelial tube branching involved in lung morphogenesis

Inferred from electronic annotation. Source: Ensembl

fungiform papilla formation

Inferred from electronic annotation. Source: Ensembl

gastrulation with mouth forming second

Inferred from Biological aspect of Ancestor. Source: RefGenome

genitalia morphogenesis

Inferred from electronic annotation. Source: Ensembl

glial cell fate determination

Inferred from Biological aspect of Ancestor. Source: RefGenome

hair cell differentiation

Traceable author statement PubMed 19251162. Source: BHF-UCL

hair follicle morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

hair follicle placode formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

hindbrain development

Inferred from Biological aspect of Ancestor. Source: RefGenome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

layer formation in cerebral cortex

Inferred from electronic annotation. Source: Ensembl

lens morphogenesis in camera-type eye

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from Biological aspect of Ancestor. Source: RefGenome

lung cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

lung induction

Inferred from Biological aspect of Ancestor. Source: RefGenome

lung-associated mesenchyme development

Inferred from Biological aspect of Ancestor. Source: RefGenome

male genitalia development

Inferred from Biological aspect of Ancestor. Source: RefGenome

mesenchymal cell proliferation involved in lung development

Inferred from Biological aspect of Ancestor. Source: RefGenome

mesenchymal to epithelial transition involved in metanephros morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

midgut development

Inferred from electronic annotation. Source: Ensembl

muscle cell differentiation

Traceable author statement. Source: Reactome

myoblast differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from direct assay PubMed 12970740. Source: UniProtKB

negative regulation of chondrocyte differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

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 electronic annotation. Source: Ensembl

negative regulation of osteoclast differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of protein sumoylation

Inferred from direct assay Ref.62. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 19653274. Source: UniProtKB

nephron tubule formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

neural plate development

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

odontogenesis of dentin-containing tooth

Inferred from Biological aspect of Ancestor. Source: RefGenome

oocyte development

Inferred from Biological aspect of Ancestor. Source: RefGenome

osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

oviduct development

Inferred from electronic annotation. Source: Ensembl

pancreas development

Inferred from Biological aspect of Ancestor. Source: RefGenome

patterning of blood vessels

Inferred by curator PubMed 20123964. Source: BHF-UCL

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

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of MAPK cascade

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of apoptotic process

Inferred from direct assay PubMed 12970740. Source: UniProtKB

positive regulation of branching involved in lung morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of determination of dorsal identity

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell proliferation involved in prostate gland development

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of fibroblast growth factor receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of heparan sulfate proteoglycan biosynthetic process

Inferred from mutant phenotype PubMed 15853773. Source: BHF-UCL

positive regulation of mesenchymal cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of muscle cell differentiation

Traceable author statement. Source: Reactome

positive regulation of neuroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.16PubMed 14660579Ref.70. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12970740. Source: UniProtKB

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein localization to cell surface

Inferred from mutant phenotype PubMed 20086044. Source: BHF-UCL

proximal/distal pattern formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of T cell proliferation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of angiogenesis

Traceable author statement PubMed 18756595. Source: BHF-UCL

regulation of calcium ion import

Inferred from direct assay Ref.51. Source: BHF-UCL

regulation of centriole-centriole cohesion

Inferred from direct assay Ref.41. Source: UniProtKB

regulation of centromeric sister chromatid cohesion

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

regulation of fibroblast proliferation

Traceable author statement Ref.36. Source: BHF-UCL

regulation of myelination

Inferred from electronic annotation. Source: Ensembl

regulation of nephron tubule epithelial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein localization to cell surface

Inferred from direct assay Ref.51. Source: BHF-UCL

regulation of secondary heart field cardioblast proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of smooth muscle cell proliferation

Inferred from mutant phenotype PubMed 17122440. Source: BHF-UCL

renal inner medulla development

Inferred from Biological aspect of Ancestor. Source: RefGenome

renal outer medulla development

Inferred from Biological aspect of Ancestor. Source: RefGenome

renal vesicle formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from expression pattern PubMed 18291362. Source: UniProtKB

response to estradiol

Inferred from direct assay PubMed 15304487. Source: BHF-UCL

smooth muscle cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

synapse organization

Inferred from Biological aspect of Ancestor. Source: RefGenome

synaptic vesicle transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

thymus development

Inferred from Biological aspect of Ancestor. Source: RefGenome

tongue morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

trachea formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentScrib-APC-beta-catenin complex

Inferred from electronic annotation. Source: Ensembl

Z disc

Inferred from Biological aspect of Ancestor. Source: RefGenome

adherens junction

Inferred from direct assay Ref.36. Source: UniProtKB

apical part of cell

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

beta-catenin destruction complex

Inferred from direct assay PubMed 16188939PubMed 8638126. Source: BHF-UCL

beta-catenin-TCF7L2 complex

Inferred from direct assay PubMed 9065401Ref.70. Source: BHF-UCL

catenin complex

Inferred from direct assay PubMed 18593713PubMed 20302655PubMed 7650039. Source: BHF-UCL

cell cortex

Inferred from direct assay PubMed 19038973. Source: BHF-UCL

cell junction

Traceable author statement Ref.34. Source: UniProtKB

cell periphery

Inferred from direct assay PubMed 19038973. Source: BHF-UCL

cell-cell adherens junction

Inferred from direct assay PubMed 10403777Ref.41. Source: UniProtKB

cell-cell junction

Inferred from direct assay Ref.51. Source: BHF-UCL

centrosome

Inferred from direct assay Ref.41. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 11793365PubMed 12937339PubMed 12970740PubMed 17976063PubMed 19095296. Source: UniProtKB

cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Inferred from direct assay PubMed 10980594PubMed 19187541. Source: UniProtKB

dendritic shaft

Inferred from Biological aspect of Ancestor. Source: RefGenome

desmosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

fascia adherens

Inferred from Biological aspect of Ancestor. Source: RefGenome

lamellipodium

Inferred from Biological aspect of Ancestor. Source: RefGenome

lateral plasma membrane

Inferred from direct assay PubMed 12072559. Source: MGI

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

microvillus membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 10980594Ref.36PubMed 17976063PubMed 18193033PubMed 19095296PubMed 19187541. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 19038973. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 12970740PubMed 17976063. Source: UniProtKB

protein-DNA complex

Inferred from direct assay PubMed 10825188. Source: BHF-UCL

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription factor complex

Inferred from direct assay Ref.16. Source: BHF-UCL

zonula adherens

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionI-SMAD binding

Inferred from physical interaction PubMed 18593713. Source: BHF-UCL

R-SMAD binding

Inferred from physical interaction PubMed 20097766. Source: BHF-UCL

RNA polymerase II activating transcription factor binding

Inferred from physical interaction PubMed 19443654. Source: BHF-UCL

SMAD binding

Inferred from physical interaction PubMed 18593713. Source: BHF-UCL

alpha-catenin binding

Inferred from physical interaction PubMed 7650039PubMed 7890674. Source: BHF-UCL

androgen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

cadherin binding

Inferred from physical interaction PubMed 12734196PubMed 19038973. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from physical interaction PubMed 18356165. Source: BHF-UCL

estrogen receptor binding

Inferred from physical interaction PubMed 15304487. Source: BHF-UCL

ion channel binding

Inferred from physical interaction Ref.51. Source: BHF-UCL

kinase binding

Inferred from physical interaction PubMed 8638126. Source: BHF-UCL

nuclear hormone receptor binding

Inferred from physical interaction PubMed 12799378. Source: BHF-UCL

protein C-terminus binding

Inferred from physical interaction PubMed 10773885PubMed 15843474. Source: UniProtKB

protein kinase binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein phosphatase binding

Inferred from physical interaction PubMed 16574648PubMed 8663237. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

signal transducer activity

Non-traceable author statement Ref.75. Source: ProtInc

structural molecule activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription coactivator activity

Inferred from mutant phenotype PubMed 12949260. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 20123964. Source: BHF-UCL

transcription regulatory region DNA binding

Inferred from direct assay PubMed 18193033PubMed 18579517. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABL1P005192EBI-491549,EBI-375543
ACTN4O437076EBI-491549,EBI-351526
APCP250548EBI-491549,EBI-727707
ARP102758EBI-491549,EBI-608057
AXIN1O1516926EBI-491549,EBI-710484
Axin1O356252EBI-491549,EBI-2365912From a different organism.
BCL9O005122EBI-491549,EBI-533127
BCR/ABL fusionA1Z1992EBI-491549,EBI-7286259
BTRCQ9Y2975EBI-491549,EBI-307461
CAV1P337245EBI-491549,EBI-79998From a different organism.
CDC73Q6P1J99EBI-491549,EBI-930143
CDH1P128307EBI-491549,EBI-727477
CDH2P190222EBI-491549,EBI-2256711
CDH5P331516EBI-491549,EBI-2903122
CREBBPQ927932EBI-491549,EBI-81215
Ctnna1P262312EBI-491549,EBI-647895From a different organism.
CTNNBIP1Q9NSA39EBI-491549,EBI-747082
DACT1Q9NYF03EBI-491549,EBI-3951744
EGR1P181467EBI-491549,EBI-2834611
EMDP504023EBI-491549,EBI-489887
FBXW11Q9UKB12EBI-491549,EBI-355189
FERMT2Q96AC113EBI-491549,EBI-4399465
FLT1P179482EBI-491549,EBI-1026718
FOXM1Q0805016EBI-491549,EBI-866480
GLIS2Q9BZE06EBI-491549,EBI-7251368
GSK3BP498418EBI-491549,EBI-373586
HTTP428585EBI-491549,EBI-466029
IGF1RP080693EBI-491549,EBI-475981
ipaCP180124EBI-491563,EBI-491541From a different organism.
IQGAP1P469403EBI-491549,EBI-297509
JRKO755643EBI-491549,EBI-8607681
KANK1Q146782EBI-491549,EBI-2556221
KIAA1109Q2LD372EBI-491549,EBI-2683809
LEF1Q9UJU25EBI-491549,EBI-926131
LEO1Q8WVC02EBI-491549,EBI-932432
MAP1LC3BQ9GZQ85EBI-491549,EBI-373144
NFKB1P198382EBI-491549,EBI-300010
PSEN1P497682EBI-491549,EBI-297277
PTH1RQ034314EBI-491549,EBI-2860297
PTK7Q133085EBI-491549,EBI-2803245
PTPRCP085752EBI-491549,EBI-1341
PTPRGP234702EBI-491549,EBI-2258115
PTPRJQ129132EBI-491549,EBI-2264500
PXNP490234EBI-491549,EBI-702209
RELAQ042062EBI-491549,EBI-73886
RUNX3Q1376112EBI-491549,EBI-925990
TCF4P1588416EBI-491549,EBI-533224
TCF7P364022EBI-491549,EBI-2119465
TCF7L2Q9NQB030EBI-491549,EBI-924724
TNIKQ9UKE53EBI-491549,EBI-1051794
TOP2AP113885EBI-491549,EBI-539628
WWTR1Q9GZV54EBI-491549,EBI-747743
Wwtr1Q9EPK52EBI-491549,EBI-1211920From a different organism.
YAP1P4693712EBI-491549,EBI-1044059
YAP1P46937-32EBI-491549,EBI-6558686

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35222-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P35222-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-565: Missing.
     652-653: AT → GK
     654-781: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.64
Chain2 – 781780Catenin beta-1
PRO_0000064271

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 By similarity
Region156 – 17823Interaction with BCL9
Region772 – 78110Interaction with SCRIB By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.64
Modified residue231Phosphoserine; by GSK3-beta
Modified residue291Phosphoserine; by GSK3-beta
Modified residue331Phosphoserine; by GSK3-beta and HIPK2 Ref.49
Modified residue371Phosphoserine; by GSK3-beta and HIPK2 Ref.49
Modified residue411Phosphothreonine; by GSK3-beta
Modified residue451Phosphoserine Ref.23
Modified residue641Phosphotyrosine; by PTK6 Ref.53
Modified residue861Phosphotyrosine; by CSK Ref.17
Modified residue1421Phosphotyrosine; by FYN and PTK6 Ref.32 Ref.53
Modified residue1911Phosphoserine; by CDK5 Ref.39 Ref.59
Modified residue2461Phosphoserine; by CDK5 Ref.39
Modified residue3311Phosphotyrosine; by PTK6 Ref.53
Modified residue3331Phosphotyrosine; by PTK6 Probable
Modified residue5511Phosphothreonine
Modified residue5521Phosphoserine Ref.59
Modified residue5561Phosphothreonine Ref.42
Modified residue6191S-nitrosocysteine By similarity
Modified residue6541Phosphotyrosine; by CSK Ref.17
Modified residue6751Phosphoserine Ref.35 Ref.42 Ref.54

Natural variations

Alternative sequence1 – 565565Missing in isoform 2.
VSP_006984
Alternative sequence652 – 6532AT → GK in isoform 2.
VSP_006985
Alternative sequence654 – 781128Missing in isoform 2.
VSP_006986
Natural variant231S → R in hepatocellular carcinoma; no effect. Ref.25 Ref.76
VAR_017612
Natural variant25 – 339Missing in hepatocellular carcinoma.
VAR_017613
Natural variant321D → A in hepatocellular carcinoma. Ref.76
VAR_017614
Natural variant321D → G in PTR and hepatocellular carcinoma. Ref.75 Ref.76
VAR_017615
Natural variant321D → Y in PTR, hepatoblastoma and hepatocellular carcinoma. Ref.15 Ref.71 Ref.75 Ref.76
Corresponds to variant rs28931588 [ dbSNP | Ensembl ].
VAR_017616
Natural variant331S → F in PTR, MDB and hepatocellular carcinoma. Ref.75 Ref.76 Ref.77
VAR_017617
Natural variant331S → L in hepatocellular carcinoma. Ref.76
VAR_017618
Natural variant331S → Y in colorectal cancer and PTR; enhances transactivation of target genes. Ref.25 Ref.70 Ref.75
VAR_017619
Natural variant341G → E in PTR. Ref.75
VAR_017620
Natural variant341G → R in hepatocellular carcinoma. Ref.76
VAR_017621
Natural variant341G → V in hepatoblastoma. Ref.71
Corresponds to variant rs28931589 [ dbSNP | Ensembl ].
VAR_017622
Natural variant351I → S in hepatocellular carcinoma. Ref.76
VAR_017623
Natural variant37 – 382SG → W in hepatocellular carcinoma.
VAR_017628
Natural variant371S → A in MDB and hepatocellular carcinoma; enhances transactivation of target genes. Ref.25 Ref.76 Ref.77
VAR_017624
Natural variant371S → C in PTR, hepatoblastoma and ovarian cancer. Ref.71 Ref.73 Ref.75
VAR_017625
Natural variant371S → F in PTR. Ref.75
VAR_017626
Natural variant371S → Y in hepatocellular carcinoma. Ref.76
VAR_017627
Natural variant411T → A in hepatoblastoma and hepatocellular carcinoma; also in a desmoid tumor; strongly reduces phosphorylation and degradation; abolishes phosphorylation on Ser-33 and Ser-37 and enhances transactivation of target genes. Ref.23 Ref.25 Ref.71 Ref.72 Ref.73 Ref.74 Ref.76
VAR_017629
Natural variant411T → I in PTR, hepatocellular carcinoma and ovarian cancer. Ref.73 Ref.75 Ref.76
VAR_017630
Natural variant451S → F in hepatocellular carcinoma. Ref.76
VAR_017631
Natural variant451S → P in hepatocellular carcinoma. Ref.76
VAR_017632
Natural variant451Missing in colorectal cancer. Ref.70
VAR_055430
Natural variant6881M → V. Ref.3
Corresponds to variant rs4135384 [ dbSNP | Ensembl ].
VAR_018954

Experimental info

Mutagenesis291S → F: No effect. Ref.25
Mutagenesis641Y → F: Abolishes phosphorylation by PTK6. Ref.53
Mutagenesis1421Y → E: No effect on interaction with BCL9 and BCL9L. Ref.69
Mutagenesis1561L → A: Abolishes interaction with BCL9 but no effect on interaction with CDH3; when associated with A-159. Ref.69
Mutagenesis1591L → A: No effect on interaction with BCL9 and CDH3. Abolishes interaction with BCL9 but no effect on interaction with CDH3; when associated with A-156. Ref.69
Mutagenesis1781L → A: No effect on interaction with BCL9 and CDH3. Ref.69
Mutagenesis2531F → A: Abolishes or strongly reduces AXIN2 binding. Ref.14
Mutagenesis2601H → A: Abolishes or strongly reduces AXIN1 and AXIN2 binding. Strongly reduces phosphorylation and degradation; when associated with A-386 and A-383. Ref.14
Mutagenesis2921K → A: Abolishes or strongly reduces AXIN1 and AXIN2 binding. Ref.14
Mutagenesis3121K → E: Abolishes TCF7L2 binding. Ref.66
Mutagenesis3451K → A: Abolishes APC binding. Ref.14
Mutagenesis3831W → A: Abolishes APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-386. Ref.14
Mutagenesis3861R → A: Strongly reduces APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-383. Ref.14
Mutagenesis4261N → A: Abolishes TCF7L2 and LEF1 binding. Ref.14
Mutagenesis4351K → A: Strongly reduces or abolishes LEF1 binding. Ref.14 Ref.66
Mutagenesis4351K → E: Abolishes TCF7L2 binding. Ref.14 Ref.66
Mutagenesis4691R → A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding. Ref.14
Mutagenesis4701H → A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding. Ref.14
Mutagenesis5081K → A: Abolishes TCF7L2 and LEF1 binding. Ref.14
Mutagenesis6541Y → E: Enhances TBP binding and transactivation of target genes. Ref.17
Mutagenesis6541Y → F: Abolishes increase of TBP binding after phosphorylation by CSK. Ref.17
Mutagenesis6601F → A: Abolishes CTNNBIP1 binding; when associated with A-661. Ref.68
Mutagenesis6611R → A: Abolishes CTNNBIP1 binding; when associated with A-660. Ref.68

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: CB78F165A3EEF86E

FASTA78185,497
        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 GAQGEPLGYR QDDPSYRSFH 

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


L 

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Isoform 2 [UniParc].

Checksum: 7AC26A6AA23E438C
Show »

FASTA889,501

References

« Hide 'large scale' references
[1]"E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton."
Huelsken J., Birchmeier W., Behrens J.
J. Cell Biol. 127:2061-2069(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"Functional prediction of the coding sequences of 75 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W., Gao F., Liu M., He F.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal liver.
[3]NIEHS SNPs program
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-688.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hippocampus.
[5]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 1).
Tissue: Skin.
[8]"Oncogenic beta-catenin is required for bone morphogenetic protein 4 expression in human cancer cells."
Kim J.-S., Crooks H., Dracheva T., Nishanian T.G., Singh B., Jen J., Waldman T.
Cancer Res. 62:2744-2748(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-312 (ISOFORM 1).
[9]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 258-781 (ISOFORM 1).
Tissue: Colon adenocarcinoma.
[10]"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.
[11]"Promoter swapping between the genes for a novel zinc finger protein and beta-catenin in pleiomorphic adenomas with t(3;8)(p21;q12) translocations."
Kas K., Voz M.L., Roeijer E., Astroem A.-K., Meyen E., Stenman G., Van de Ven W.J.M.
Nat. Genet. 15:170-174(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH PLAG1.
[12]"Conserved mechanism of PLAG1 activation in salivary gland tumors with and without chromosome 8q12 abnormalities: identification of SII as a new fusion partner gene."
Astroem A.-K., Voz M.L., Kas K., Roeijer E., Wedell B., Mandahl N., Van de Ven W., Mark J., Stenman G.
Cancer Res. 59:918-923(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH PLAG1.
[13]"Phosphorylation and free pool of beta-catenin are regulated by tyrosine kinases and tyrosine phosphatases during epithelial cell migration."
Mueller T., Choidas A., Reichmann E., Ullrich A.
J. Biol. Chem. 274:10173-10183(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STIMULATION OF TYROSINE PHOSPHORYLATION BY EGF, DEPHOSPHORYLATION BY PTPRF.
[14]"Hot spots in beta-catenin for interactions with LEF-1, conductin and APC."
von Kries J.P., Winbeck G., Asbrand C., Schwarz-Romond T., Sochnikova N., Dell'Oro A., Behrens J., Birchmeier W.
Nat. Struct. Biol. 7:800-807(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LEF1; APC; AXIN1; AXIN2 AND TCF7L2, PHOSPHORYLATION BY GSK3B, MUTAGENESIS OF PHE-253; HIS-260; LYS-292; LYS-345; TRP-383; ARG-386; ASN-426; LYS-435; ARG-469; HIS-470 AND LYS-508.
[15]"Beta-catenin expression in pilomatrixomas. Relationship with beta-catenin gene mutations and comparison with beta-catenin expression in normal hair follicles."
Moreno-Bueno G., Gamallo C., Perez-Gallego L., Contreras F., Palacios J.
Br. J. Dermatol. 145:576-581(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, VARIANT PTR TYR-32.
[16]"Chromatin-specific regulation of LEF-1-beta-catenin transcription activation and inhibition in vitro."
Tutter A.V., Fryer C.J., Jones K.A.
Genes Dev. 15:3342-3354(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LEF1, INHIBITION BY CTNNBIP1 BINDING.
[17]"Regulation of beta-catenin structure and activity by tyrosine phosphorylation."
Piedra J., Martinez D., Castano J., Miravet S., Dunach M., de Herreros A.G.
J. Biol. Chem. 276:20436-20443(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-86 AND TYR-654, INTERACTION WITH TBP, MUTAGENESIS OF TYR-654.
[18]"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.
[19]"Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses."
Matsuzawa S., Reed J.C.
Mol. Cell 7:915-926(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[20]"Siah-1 mediates a novel beta-catenin degradation pathway linking p53 to the adenomatous polyposis coli protein."
Liu J., Stevens J., Rote C.A., Yost H.J., Hu Y., Neufeld K.L., White R.L., Matsunami N.
Mol. Cell 7:927-936(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[21]"Genetic alteration of the beta-catenin gene (CTNNB1) in human lung cancer and malignant mesothelioma and identification of a new 3p21.3 homozygous deletion."
Shigemitsu K., Sekido Y., Usami N., Mori S., Sato M., Horio Y., Hasegawa Y., Bader S.A., Gazdar A.F., Minna J.D., Hida T., Yoshioka H., Imaizumi M., Ueda Y., Takahashi M., Shimokata K.
Oncogene 20:4249-4257(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MESOM.
[22]"Physical and functional interaction between receptor-like protein tyrosine phosphatase PCP-2 and beta-catenin."
Yan H.-X., He Y.-Q., Dong H., Zhang P., Zeng J.-Z., Cao H.-F., Wu M.-C., Wang H.-Y.
Biochemistry 41:15854-15860(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPRU.
[23]"Characterisation of the phosphorylation of beta-catenin at the GSK-3 priming site Ser45."
Hagen T., Vidal-Puig A.
Biochem. Biophys. Res. Commun. 294:324-328(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-45, CHARACTERIZATION OF VARIANT HEPATOCELLULAR CARCINOMA ALA-41, CHARACTERIZATION OF VARIANT DESMOID TUMOR ALA-41, CHARACTERIZATION OF VARIANT HEPATOBLASTOMA ALA-41.
[24]"Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape."
Walters R.W., Freimuth P., Moninger T.O., Ganske I., Zabner J., Welsh M.J.
Cell 110:789-799(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CXADR.
[25]"Identification of two novel regulated serines in the N-terminus of beta-catenin."
van Noort M., van de Wetering M., Clevers H.
Exp. Cell Res. 276:264-272(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY GSK3B, MUTAGENESIS OF SER-29, CHARACTERIZATION OF VARIANTS HEPATOCELLULAR CARCINOMA ARG-23; ALA-37 AND ALA-41, CHARACTERIZATION OF VARIANT PTR TYR-33, CHARACTERIZATION OF VARIANT MDB ALA-37, CHARACTERIZATION OF VARIANT DESMOID TUMOR ALA-41, CHARACTERIZATION OF VARIANT HEPATOBLASTOMA ALA-41.
[26]"Wnt signaling controls the phosphorylation status of beta-catenin."
van Noort M., Meeldijk J., van der Zee R., Destree O., Clevers H.
J. Biol. Chem. 277:17901-17905(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: WNT SIGNALING MODULATES PHOSPHORYLATION.
[27]"Regulation of S33/S37 phosphorylated beta-catenin in normal and transformed cells."
Sadot E., Conacci-Sorrell M., Zhurinsky J., Shnizer D., Lando Z., Zharhary D., Kam Z., Ben-Ze'ev A., Geiger B.
J. Cell Sci. 115:2771-2780(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION OF PHOSPHORYLATED CTNNB1 WITH BTRC.
[28]"The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)."
Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.
Oncogene 21:7067-7076(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPRJ.
[29]"The emergence of protocadherin-PC expression during the acquisition of apoptosis-resistance by prostate cancer cells."
Chen M.-W., Vacherot F., De La Taille A., Gil-Diez-De-Medina S., Shen R., Friedman R.A., Burchardt M., Chopin D.K., Buttyan R.
Oncogene 21:7861-7871(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PCDH11Y.
[30]"EBP50, a beta-catenin-associating protein, enhances Wnt signaling and is over-expressed in hepatocellular carcinoma."
Shibata T., Chuma M., Kokubu A., Sakamoto M., Hirohashi S.
Hepatology 38:178-186(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC9A3R1.
[31]"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.
[32]"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.
[33]"Novel membrane protein shrew-1 targets to cadherin-mediated junctions in polarized epithelial cells."
Bharti S., Handrow-Metzmacher H., Zickenheiner S., Zeitvogel A., Baumann R., Starzinski-Powitz A.
Mol. Biol. Cell 15:397-406(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AJAP1.
Tissue: Brain.
[34]"E-cadherin regulates human Nanos1, which interacts with p120ctn and induces tumor cell migration and invasion."
Strumane K., Bonnomet A., Stove C., Vandenbroucke R., Nawrocki-Raby B., Bruyneel E., Mareel M., Birembaut P., Berx G., van Roy F.
Cancer Res. 66:10007-10015(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NANOS1.
[35]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[36]"The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus."
Markiewicz E., Tilgner K., Barker N., van de Wetering M., Clevers H., Dorobek M., Hausmanowa-Petrusewicz I., Ramaekers F.C.S., Broers J.L.V., Blankesteijn W.M., Salpingidou G., Wilson R.G., Ellis J.A., Hutchison C.J.
EMBO J. 25:3275-3285(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EMD.
[37]"MUC1 inhibits cell proliferation by a beta-catenin-dependent mechanism."
Lillehoj E.P., Lu W., Kiser T., Goldblum S.E., Kim K.C.
Biochim. Biophys. Acta 1773:1028-1038(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MUC1, SUBCELLULAR LOCATION, FUNCTION.
[38]"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, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[39]"cdk5 modulates beta- and delta-catenin/Pin1 interactions in neuronal cells."
Munoz J.P., Huichalaf C.H., Orellana D., Maccioni R.B.
J. Cell. Biochem. 100:738-749(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-191 AND SER-246, INTERACTION WITH CDK5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[40]"The tumor suppressor Fhit acts as a repressor of beta-catenin transcriptional activity."
Weiske J., Albring K.F., Huber O.
Proc. Natl. Acad. Sci. U.S.A. 104:20344-20349(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FHIT, IDENTIFICATION IN A COMPLEX WITH LEF1, FUNCTION.
[41]"beta-Catenin is a Nek2 substrate involved in centrosome separation."
Bahmanyar S., Kaplan D.D., Deluca J.G., Giddings T.H. Jr., O'Toole E.T., Winey M., Salmon E.D., Casey P.J., Nelson W.J., Barth A.I.
Genes Dev. 22:91-105(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH NEK2.
[42]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-556 AND SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[43]"Sox7 Is an independent checkpoint for beta-catenin function in prostate and colon epithelial cells."
Guo L., Zhong D., Lau S., Liu X., Dong X.Y., Sun X., Yang V.W., Vertino P.M., Moreno C.S., Varma V., Dong J.T., Zhou W.
Mol. Cancer Res. 6:1421-1430(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SOX7.
[44]"CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-catenin target genes."
Thompson B.A., Tremblay V., Lin G., Bochar D.A.
Mol. Cell. Biol. 28:3894-3904(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHD8.
[45]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[46]"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.
[47]"Down-regulation of death-associated protein kinase-2 is required for beta-catenin-induced anoikis resistance of malignant epithelial cells."
Li H., Ray G., Yoo B.H., Erdogan M., Rosen K.V.
J. Biol. Chem. 284:2012-2022(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[48]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[49]"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.
[50]"The phospholipid-binding protein SESTD1 is a novel regulator of the transient receptor potential channels TRPC4 and TRPC5."
Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C.
J. Biol. Chem. 285:12426-12434(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SESTD1.
[51]"Cell-cell contact formation governs Ca2+ signaling by TRPC4 in the vascular endothelium: evidence for a regulatory TRPC4-beta-catenin interaction."
Graziani A., Poteser M., Heupel W.M., Schleifer H., Krenn M., Drenckhahn D., Romanin C., Baumgartner W., Groschner K.
J. Biol. Chem. 285:4213-4223(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRPC4.
[52]"Characterization of a novel human CDK5 splicing variant that inhibits Wnt/beta-catenin signaling."
Li Q., Liu X., Zhang M., Ye G., Qiao Q., Ling Y., Wu Y., Zhang Y., Yu L.
Mol. Biol. Rep. 37:2415-2421(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK5.
[53]"Identification of beta-catenin as a target of the intracellular tyrosine kinase PTK6."
Palka-Hamblin H.L., Gierut J.J., Bie W., Brauer P.M., Zheng Y., Asara J.M., Tyner A.L.
J. Cell Sci. 123:236-245(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-64; TYR-142; TYR-331 AND TYR-333, INTERACTION WITH PTK6, MUTAGENESIS OF TYR-64.
[54]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[55]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[56]"Compartmentalized CDK2 is connected with SHP-1 and beta-catenin and regulates insulin internalization."
Fiset A., Xu E., Bergeron S., Marette A., Pelletier G., Siminovitch K.A., Olivier M., Beauchemin N., Faure R.L.
Cell. Signal. 23:911-919(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN INSULIN INTERNALIZATION, SUBCELLULAR LOCATION, INTERACTION WITH CDK2, PHOSPHORYLATION BY CDK2.
[57]"Protein tyrosine kinase 7 has a conserved role in Wnt/beta-catenin canonical signalling."
Puppo F., Thome V., Lhoumeau A.-C., Cibois M., Gangar A., Lembo F., Belotti E., Marchetto S., Lecine P., Prebet T., Sebbagh M., Shin W.-S., Lee S.-T., Kodjabachian L., Borg J.-P.
EMBO Rep. 12:43-49(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PKT7.
[58]"Crystal structure of the human N-Myc downstream-regulated gene 2 protein provides insight into its role as a tumor suppressor."
Hwang J., Kim Y., Kang H.B., Jaroszewski L., Deacon A.M., Lee H., Choi W.C., Kim K.J., Kim C.H., Kang B.S., Lee J.O., Oh T.K., Kim J.W., Wilson I.A., Kim M.H.
J. Biol. Chem. 286:12450-12460(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NDRG2.
[59]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[60]"The tumor suppressor HINT1 regulates MITF and beta-catenin transcriptional activity in melanoma cells."
Genovese G., Ghosh P., Li H., Rettino A., Sioletic S., Cittadini A., Sgambato A.
Cell Cycle 11:2206-2215(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH HINT1 AND MITF, FUNCTION.
[61]"Kindlin 2 forms a transcriptional complex with beta-catenin and TCF4 to enhance Wnt signalling."
Yu Y., Wu J., Wang Y., Zhao T., Ma B., Liu Y., Fang W., Zhu W.G., Zhang H.
EMBO Rep. 13:750-758(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FERMT2, IDENTIFICATION IN A COMPLEX WITH FERMT2 AND TCF7L2, SUBCELLULAR LOCATION.
[62]"Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells."
Satow R., Shitashige M., Jigami T., Fukami K., Honda K., Kitabayashi I., Yamada T.
Gastroenterology 142:572-581(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PML.
[63]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRD19.
[64]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[65]"Crystal structure of a beta-catenin/Tcf complex."
Graham T.A., Weaver C., Mao F., Kimelman D., Xu W.
Cell 103:885-896(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 133-664.
[66]"Tcf4 can specifically recognize beta-catenin using alternative conformations."
Graham T.A., Ferkey D.M., Mao F., Kimelman D., Xu W.
Nat. Struct. Biol. 8:1048-1052(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-664 IN COMPLEX WITH TCF7L2, MUTAGENESIS OF LYS-312 AND LYS-435.
[67]"Structure of a human Tcf4-beta-catenin complex."
Poy F., Lepourcelet M., Shivdasani R.A., Eck M.J.
Nat. Struct. Biol. 8:1053-1057(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-668 IN COMPLEX WITH TCF7L2.
[68]"The crystal structure of the beta-catenin/ICAT complex reveals the inhibitory mechanism of ICAT."
Graham T.A., Clements W.K., Kimelman D., Xu W.
Mol. Cell 10:563-571(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-664 IN COMPLEX WITH CTNNBIP1, MUTAGENESIS OF PHE-660 AND ARG-661.
[69]"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: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-136 IN COMPLEX WITH BCL9 AND TCF7L2, INTERACTION WITH BCL9; BCL9L CDH3 AND TCF7L2, MUTAGENESIS OF TYR-142; LEU-156; LEU-159 AND LEU-178.
[70]"Activation of beta-catenin-Tcf signaling in colon cancer by mutations in beta-catenin or APC."
Morin P.J., Sparks A.B., Korinek V., Barker N., Clevers H., Vogelstein B., Kinzler K.W.
Science 275:1787-1790(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS COLORECTAL CANCER TYR-33 AND SER-45 DEL.
[71]"Childhood hepatoblastomas frequently carry a mutated degradation targeting box of the beta-catenin gene."
Koch A., Denkhaus D., Albrecht S., Leuschner I., von Schweinitz D., Pietsch T.
Cancer Res. 59:269-273(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HEPATOBLASTOMA TYR-32; VAL-34; CYS-37 AND ALA-41.
[72]"Beta-catenin accumulation and mutation of the CTNNB1 gene in hepatoblastoma."
Blaeker H., Hofmann W.J., Rieker R.J., Penzel R., Graf M., Otto H.F.
Genes Chromosomes Cancer 25:399-402(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HEPATOBLASTOMA ALA-41.
[73]"Mutational analysis of beta-catenin gene in Japanese ovarian carcinomas: frequent mutations in endometrioid carcinomas."
Sagae S., Kobayashi K., Nishioka Y., Sugimura M., Ishioka S., Nagata M., Terasawa K., Tokino T., Kudo R.
Jpn. J. Cancer Res. 90:510-515(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OVARIAN CANCER CYS-37; ILE-41 AND ALA-41.
[74]"A novel case of a sporadic desmoid tumour with mutation of the beta catenin gene."
Shitoh K., Konishi F., Iijima T., Ohdaira T., Sakai K., Kanazawa K., Miyaki M.
J. Clin. Pathol. 52:695-696(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DESMOID TUMOR ALA-41.
[75]"A common human skin tumour is caused by activating mutations in beta-catenin."
Chan E.F., Gat U., McNiff J.M., Fuchs E.
Nat. Genet. 21:410-413(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PTR GLY-32; TYR-32; PHE-33; TYR-33; GLU-34; CYS-37; PHE-37 AND ILE-41.
[76]"Beta-catenin mutations in hepatocellular carcinoma correlate with a low rate of loss of heterozygosity."
Legoix P., Bluteau O., Bayer J., Perret C., Balabaud C., Belghiti J., Franco D., Thomas G., Laurent-Puig P., Zucman-Rossi J.
Oncogene 18:4044-4046(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HEPATOCELLULAR CARCINOMA ARG-23; 25-TRP--SER-33 DEL; ALA-32; GLY-32; TYR-32; LEU-33; PHE-33; ARG-34; SER-35; ALA-37; 37-SER-GLY-38 DELINS TRP; TYR-37; ALA-41; ILE-41; PHE-45 AND PRO-45.
[77]"APC mutations in sporadic medulloblastomas."
Huang H., Mahler-Araujo B.M., Sankila A., Chimelli L., Yonekawa Y., Kleihues P., Ohgaki H.
Am. J. Pathol. 156:433-437(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDB PHE-33 AND ALA-37.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X87838 mRNA. Translation: CAA61107.1.
Z19054 mRNA. Translation: CAA79497.1.
AF130085 mRNA. Translation: AAG35511.1.
AY463360 Genomic DNA. Translation: AAR18817.1.
AK289932 mRNA. Translation: BAF82621.1.
AC104307 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64625.1.
BC058926 mRNA. Translation: AAH58926.1.
AY081165 Genomic DNA. Translation: AAL89457.1.
AB062292 mRNA. Translation: BAB93475.1. Different initiation.
PIRA38973.
RefSeqNP_001091679.1. NM_001098209.1.
NP_001091680.1. NM_001098210.1.
NP_001895.1. NM_001904.3.
XP_005264943.1. XM_005264886.2.
UniGeneHs.476018.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G3JX-ray2.10A/C133-664[»]
1JDHX-ray1.90A135-663[»]
1JPWX-ray2.50A/B/C134-670[»]
1LUJX-ray2.50A150-663[»]
1P22X-ray2.95C19-44[»]
1QZ7X-ray2.20A133-665[»]
1T08X-ray2.10A146-664[»]
1TH1X-ray2.50A/B133-664[»]
2G57NMR-A19-44[»]
2GL7X-ray2.60A/D138-686[»]
2Z6HX-ray2.20A138-781[»]
3DIWX-ray2.10C/D772-781[»]
3FQNX-ray1.65C30-39[»]
3FQRX-ray1.70C30-39[»]
3SL9X-ray2.20A/B/E/G141-305[»]
3SLAX-ray2.50A/B/C/D/E141-306[»]
3TX7X-ray2.76A138-663[»]
4DJSX-ray3.03A148-665[»]
ProteinModelPortalP35222.
SMRP35222. Positions 19-44, 99-665.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107880. 243 interactions.
DIPDIP-122N.
IntActP35222. 144 interactions.
MINTMINT-105089.
STRING9606.ENSP00000344456.

Chemistry

BindingDBP35222.
ChEMBLCHEMBL5866.
DrugBankDB01356. Lithium.

PTM databases

PhosphoSiteP35222.

Polymorphism databases

DMDM461854.

Proteomic databases

PaxDbP35222.
PRIDEP35222.

Protocols and materials databases

DNASU1499.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000349496; ENSP00000344456; ENSG00000168036. [P35222-1]
ENST00000396183; ENSP00000379486; ENSG00000168036. [P35222-1]
ENST00000396185; ENSP00000379488; ENSG00000168036. [P35222-1]
ENST00000405570; ENSP00000385604; ENSG00000168036. [P35222-1]
GeneID1499.
KEGGhsa:1499.
UCSCuc003ckp.2. human. [P35222-1]
uc003ckt.1. human. [P35222-2]

Organism-specific databases

CTD1499.
GeneCardsGC03P041236.
H-InvDBHIX0163439.
HIX0163473.
HGNCHGNC:2514. CTNNB1.
HPACAB000108.
CAB001950.
HPA029159.
HPA029160.
MIM114500. phenotype.
116806. gene.
132600. phenotype.
155255. phenotype.
156240. phenotype.
167000. phenotype.
181030. phenotype.
615075. phenotype.
neXtProtNX_P35222.
Orphanet85142. Aldosterone-producing adenoma.
178469. Autosomal dominant nonsyndromic intellectual deficit.
873. Desmoid tumor.
33402. Hepatocellular carcinoma, childhood-onset.
91414. Pilomatrixoma.
PharmGKBPA27013.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297695.
HOGENOMHOG000230958.
HOVERGENHBG000919.
InParanoidP35222.
KOK02105.
OMAQLSQTRS.
OrthoDBEOG7X9G6B.
PhylomeDBP35222.
TreeFamTF317997.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_578. Apoptosis.
REACT_6900. Immune System.
SignaLinkP35222.

Gene expression databases

ArrayExpressP35222.
BgeeP35222.
CleanExHS_CTNNB1.
GenevestigatorP35222.

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. human.
EvolutionaryTraceP35222.
GeneWikiBeta-catenin.
GenomeRNAi1499.
NextBio6161.
PMAP-CutDBP35222.
PROP35222.
SOURCESearch...

Entry information

Entry nameCTNB1_HUMAN
AccessionPrimary (citable) accession number: P35222
Secondary accession number(s): A8K1L7 expand/collapse secondary AC list , Q8NEW9, Q8NI94, Q9H391
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 179 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM