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Protein

Catenin beta-1

Gene

CTNNB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22647378, PubMed:22699938, PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity).By similarity8 Publications

GO - Molecular functioni

  • alpha-catenin binding Source: BHF-UCL
  • androgen receptor binding Source: UniProtKB
  • cadherin binding Source: UniProtKB
  • double-stranded DNA binding Source: Ensembl
  • enzyme binding Source: UniProtKB
  • estrogen receptor binding Source: BHF-UCL
  • euchromatin binding Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • I-SMAD binding Source: BHF-UCL
  • kinase binding Source: BHF-UCL
  • nuclear hormone receptor binding Source: BHF-UCL
  • protein C-terminus binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • R-SMAD binding Source: BHF-UCL
  • sequence-specific DNA binding transcription factor activity Source: Ensembl
  • signal transducer activity Source: ProtInc
  • SMAD binding Source: BHF-UCL
  • transcription coactivator activity Source: UniProtKB
  • transcription factor binding Source: BHF-UCL
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_13579. Apoptotic cleavage of cell adhesion proteins.
REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_19195. Adherens junctions interactions.
REACT_21402. CDO in myogenesis.
REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
REACT_263982. Ca2+ pathway.
REACT_263991. VEGFR2 mediated vascular permeability.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264178. deactivation of the beta-catenin transactivating complex.
REACT_264242. formation of the beta-catenin:TCF transactivating complex.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264532. binding of TCF/LEF:CTNNB1 to target gene promoters.
REACT_264567. repression of WNT target genes.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264596. TCF dependent signaling in response to WNT.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.
REACT_355469. RHO GTPases activate IQGAPs.
SignaLinkiP35222.

Names & Taxonomyi

Protein namesi
Recommended name:
Catenin beta-1
Alternative name(s):
Beta-catenin
Gene namesi
Name:CTNNB1
Synonyms:CTNNB
ORF Names:OK/SW-cl.35, PRO2286
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:2514. CTNNB1.

Subcellular locationi

  • Cytoplasm
  • Nucleus 1 Publication
  • Cytoplasmcytoskeleton
  • Cell junctionadherens junction
  • Cell junction
  • Cell membrane 1 Publication
  • 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.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Colorectal cancer (CRC)1 Publication

The gene represented in this entry may be involved in disease pathogenesis.

Disease descriptionA 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.

See also OMIM:114500

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)2 Publications

The gene represented in this entry is involved in disease pathogenesis.

Disease descriptionCommon benign skin tumor.

See also OMIM:132600
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321D → G in PTR and hepatocellular carcinoma. 2 Publications
VAR_017615
Natural varianti32 – 321D → Y in PTR, hepatoblastoma and hepatocellular carcinoma. 4 Publications
Corresponds to variant rs28931588 [ dbSNP | Ensembl ].
VAR_017616
Natural varianti33 – 331S → F in PTR, MDB and hepatocellular carcinoma. 3 Publications
VAR_017617
Natural varianti33 – 331S → Y in colorectal cancer and PTR; enhances transactivation of target genes. 3 Publications
VAR_017619
Natural varianti34 – 341G → E in PTR. 1 Publication
VAR_017620
Natural varianti37 – 371S → C in PTR, hepatoblastoma and ovarian cancer. 3 Publications
VAR_017625
Natural varianti37 – 371S → F in PTR. 1 Publication
VAR_017626
Natural varianti41 – 411T → I in PTR, hepatocellular carcinoma and ovarian cancer. 3 Publications
VAR_017630
Medulloblastoma (MDB)1 Publication

The gene represented in this entry may be involved in disease pathogenesis.

Disease descriptionMalignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children.

See also OMIM:155255
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331S → F in PTR, MDB and hepatocellular carcinoma. 3 Publications
VAR_017617
Natural varianti37 – 371S → A in MDB and hepatocellular carcinoma; enhances transactivation of target genes. 3 Publications
VAR_017624
Ovarian cancer (OC)1 Publication

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionThe 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.

See also OMIM:167000

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)1 Publication

The gene represented in this entry may be involved in disease pathogenesis.

Disease descriptionAn 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.

See also OMIM:156240
Mental retardation, autosomal dominant 19 (MRD19)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:615075
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti388 – 3881L → P in MRD19. 1 Publication
VAR_072282

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 291S → F: No effect. 1 Publication
Mutagenesisi64 – 641Y → F: Abolishes phosphorylation by PTK6. 1 Publication
Mutagenesisi142 – 1421Y → E: No effect on interaction with BCL9 and BCL9L. 1 Publication
Mutagenesisi156 – 1561L → A: Abolishes interaction with BCL9 but no effect on interaction with CDH3; when associated with A-159. 1 Publication
Mutagenesisi159 – 1591L → 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. 1 Publication
Mutagenesisi178 – 1781L → A: No effect on interaction with BCL9 and CDH3. 1 Publication
Mutagenesisi253 – 2531F → A: Abolishes or strongly reduces AXIN2 binding. 1 Publication
Mutagenesisi260 – 2601H → A: Abolishes or strongly reduces AXIN1 and AXIN2 binding. Strongly reduces phosphorylation and degradation; when associated with A-386 and A-383. 1 Publication
Mutagenesisi292 – 2921K → A: Abolishes or strongly reduces AXIN1 and AXIN2 binding. 1 Publication
Mutagenesisi312 – 3121K → E: Abolishes TCF7L2 binding. 1 Publication
Mutagenesisi345 – 3451K → A: Abolishes APC binding. 1 Publication
Mutagenesisi383 – 3831W → A: Abolishes APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-386. 1 Publication
Mutagenesisi386 – 3861R → A: Strongly reduces APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-383. 1 Publication
Mutagenesisi426 – 4261N → A: Abolishes TCF7L2 and LEF1 binding. 1 Publication
Mutagenesisi435 – 4351K → A: Strongly reduces or abolishes LEF1 binding. 2 Publications
Mutagenesisi435 – 4351K → E: Abolishes TCF7L2 binding. 2 Publications
Mutagenesisi469 – 4691R → A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding. 1 Publication
Mutagenesisi470 – 4701H → A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding. 1 Publication
Mutagenesisi508 – 5081K → A: Abolishes TCF7L2 and LEF1 binding. 1 Publication
Mutagenesisi654 – 6541Y → E: Enhances TBP binding and transactivation of target genes. 1 Publication
Mutagenesisi654 – 6541Y → F: Abolishes increase of TBP binding after phosphorylation by CSK. 1 Publication
Mutagenesisi660 – 6601F → A: Abolishes CTNNBIP1 binding; when associated with A-661. 1 Publication
Mutagenesisi661 – 6611R → A: Abolishes CTNNBIP1 binding; when associated with A-660. 1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi114500. phenotype.
132600. phenotype.
155255. phenotype.
156240. phenotype.
167000. phenotype.
181030. phenotype.
615075. phenotype.
Orphaneti85142. Aldosterone-producing adenoma.
54595. Craniopharyngioma.
873. Desmoid tumor.
91414. Pilomatrixoma.
404473. Severe intellectual disability-progressive spastic diplegia syndrome.
PharmGKBiPA27013.

Polymorphism and mutation databases

BioMutaiCTNNB1.
DMDMi461854.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 781780Catenin beta-1PRO_0000064271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei23 – 231Phosphoserine; by GSK3-beta; alternate1 Publication
Glycosylationi23 – 231O-linked (GlcNAc); alternate1 Publication
Modified residuei29 – 291Phosphoserine; by GSK3-beta1 Publication
Modified residuei33 – 331Phosphoserine; by GSK3-beta and HIPK21 Publication
Modified residuei37 – 371Phosphoserine; by GSK3-beta and HIPK21 Publication
Modified residuei41 – 411Phosphothreonine; by GSK3-beta1 Publication
Modified residuei45 – 451Phosphoserine1 Publication
Modified residuei49 – 491N6-acetyllysine1 Publication
Modified residuei64 – 641Phosphotyrosine; by PTK61 Publication
Modified residuei86 – 861Phosphotyrosine; by CSK1 Publication
Modified residuei142 – 1421Phosphotyrosine; by FYN and PTK62 Publications
Modified residuei191 – 1911Phosphoserine; by CDK53 Publications
Modified residuei246 – 2461Phosphoserine; by CDK51 Publication
Modified residuei331 – 3311Phosphotyrosine; by PTK61 Publication
Modified residuei333 – 3331Phosphotyrosine; by PTK61 Publication
Modified residuei552 – 5521Phosphoserine2 Publications
Modified residuei556 – 5561Phosphothreonine1 Publication
Modified residuei619 – 6191S-nitrosocysteineBy similarity
Modified residuei654 – 6541Phosphotyrosine; by CSK1 Publication
Modified residuei675 – 6751Phosphoserine3 Publications

Post-translational modificationi

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.By similarity11 Publications
Ubiquitinated by the SCF(BTRC) E3 ligase complex when phosphorylated by GSK3B, leading to its degradation. Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent proteasomal degradation (By similarity).By similarity
S-nitrosylation at Cys-619 within adherens junctions promotes VEGF-induced, NO-dependent endothelial cell permeability by disrupting interaction with E-cadherin, thus mediating disassembly adherens junctions.By similarity
O-glycosylation at Ser-23 decreases nuclear localization and transcriptional activity, and increases localization to the plasma membrane and interaction with E-cadherin CDH1.1 Publication
Deacetylated at Lys-49 by SIRT1.1 Publication

Keywords - PTMi

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

Proteomic databases

MaxQBiP35222.
PaxDbiP35222.
PRIDEiP35222.

PTM databases

PhosphoSiteiP35222.

Miscellaneous databases

PMAP-CutDBP35222.

Expressioni

Tissue specificityi

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).3 Publications

Gene expression databases

BgeeiP35222.
CleanExiHS_CTNNB1.
ExpressionAtlasiP35222. baseline and differential.
GenevisibleiP35222. HS.

Organism-specific databases

HPAiCAB000108.
CAB001950.
HPA029159.
HPA029160.

Interactioni

Subunit structurei

Two separate complex-associated pools are found in the cytoplasm. The majority is present as component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1 and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. 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. Interacts with RNF220 (PubMed:25266658). Interacts with CTNND2 (PubMed:25807484).40 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005192EBI-491549,EBI-375543
ACTN4O437077EBI-491549,EBI-351526
APCP2505413EBI-491549,EBI-727707
ARP102758EBI-491549,EBI-608057
AXIN1O1516941EBI-491549,EBI-710484
Axin1O356254EBI-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
CDH1P1283011EBI-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
FGFR1P113622EBI-491549,EBI-1028277
FLT1P179482EBI-491549,EBI-1026718
FOXM1Q0805016EBI-491549,EBI-866480
GLIS2Q9BZE06EBI-491549,EBI-7251368
GSK3BP4984115EBI-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
Lztfl1Q9JHQ52EBI-491549,EBI-6142879From a different organism.
MAP1LC3BQ9GZQ85EBI-491549,EBI-373144
NFKB1P198383EBI-491549,EBI-300010
NOS3P294744EBI-491549,EBI-1391623
PARD3Q8TEW02EBI-491549,EBI-81968
PECAM1P162843EBI-491549,EBI-716404
PITX2Q996972EBI-491549,EBI-1175211
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
SKP1P632083EBI-491549,EBI-307486
SOX17Q9H6I22EBI-491549,EBI-9106753
TCF4P1588419EBI-491549,EBI-533224
TCF7P364022EBI-491549,EBI-2119465
TCF7L2Q9NQB030EBI-491549,EBI-924724
TNIKQ9UKE53EBI-491549,EBI-1051794
TOP2AP113885EBI-491549,EBI-539628
UBR5O950716EBI-491549,EBI-358329
WWTR1Q9GZV54EBI-491549,EBI-747743
Wwtr1Q9EPK52EBI-491549,EBI-1211920From a different organism.
YAP1P4693713EBI-491549,EBI-1044059
YAP1P46937-32EBI-491549,EBI-6558686

Protein-protein interaction databases

BioGridi107880. 269 interactions.
DIPiDIP-122N.
IntActiP35222. 168 interactions.
MINTiMINT-105089.
STRINGi9606.ENSP00000344456.

Structurei

Secondary structure

1
781
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi135 – 15016Combined sources
Helixi152 – 1609Combined sources
Helixi165 – 17915Combined sources
Helixi182 – 1898Combined sources
Helixi192 – 20413Combined sources
Helixi208 – 22114Combined sources
Helixi225 – 2339Combined sources
Helixi236 – 2438Combined sources
Helixi249 – 26517Combined sources
Helixi269 – 2768Combined sources
Helixi278 – 2847Combined sources
Helixi285 – 2873Combined sources
Helixi291 – 30515Combined sources
Helixi309 – 3179Combined sources
Helixi320 – 33011Combined sources
Helixi334 – 34714Combined sources
Helixi353 – 3597Combined sources
Helixi362 – 3676Combined sources
Turni368 – 3714Combined sources
Helixi375 – 38915Combined sources
Helixi399 – 40810Combined sources
Helixi414 – 42714Combined sources
Turni428 – 4303Combined sources
Helixi432 – 4409Combined sources
Helixi443 – 45412Combined sources
Helixi458 – 47114Combined sources
Beta strandi473 – 4753Combined sources
Helixi478 – 48710Combined sources
Helixi491 – 4966Combined sources
Beta strandi499 – 5013Combined sources
Helixi504 – 51714Combined sources
Helixi521 – 5233Combined sources
Helixi524 – 5296Combined sources
Helixi532 – 54716Combined sources
Beta strandi550 – 5523Combined sources
Beta strandi554 – 5574Combined sources
Beta strandi561 – 5633Combined sources
Helixi566 – 58015Combined sources
Helixi584 – 5929Combined sources
Helixi596 – 6016Combined sources
Helixi602 – 6043Combined sources
Helixi608 – 62114Combined sources
Helixi625 – 6339Combined sources
Helixi637 – 6426Combined sources
Helixi643 – 6453Combined sources
Helixi649 – 66214Combined sources
Turni663 – 6653Combined sources
Helixi668 – 68215Combined sources
Helixi688 – 6903Combined sources
Beta strandi778 – 7803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G3JX-ray2.10A/C133-664[»]
1JDHX-ray1.90A135-663[»]
1JPWX-ray2.50A/B/C131-670[»]
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[»]
ProteinModelPortaliP35222.
SMRiP35222. Positions 19-44, 84-665.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35222.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2322Interaction with VCLBy similarityAdd
BLAST
Regioni156 – 17823Interaction with BCL9Add
BLAST
Regioni772 – 78110Interaction with SCRIBBy similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG297695.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
InParanoidiP35222.
KOiK02105.
OMAiWEQGFNQ.
OrthoDBiEOG7X9G6B.
PhylomeDBiP35222.
TreeFamiTF317997.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35222-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG
60 70 80 90 100
NPEEEDVDTS QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP
110 120 130 140 150
ETLDEGMQIP STQFDAAHPT NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT
160 170 180 190 200
RAIPELTKLL NDEDQVVVNK AAVMVHQLSK KEASRHAIMR SPQMVSAIVR
210 220 230 240 250
TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL VKMLGSPVDS
260 270 280 290 300
VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC
310 320 330 340 350
LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC
360 370 380 390 400
SSNKPAIVEA GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG
410 420 430 440 450
LLGTLVQLLG SDDINVVTCA AGILSNLTCN NYKNKMMVCQ VGGIEALVRT
460 470 480 490 500
VLRAGDREDI TEPAICALRH LTSRHQEAEM AQNAVRLHYG LPVVVKLLHP
510 520 530 540 550
PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL VRAHQDTQRR
560 570 580 590 600
TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV
610 620 630 640 650
QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG
660 670 680 690 700
VATYAAAVLF RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI
710 720 730 740 750
GAQGEPLGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV
760 770 780
DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L
Length:781
Mass (Da):85,497
Last modified:February 1, 1994 - v1
Checksum:iCB78F165A3EEF86E
GO
Isoform 2 (identifier: P35222-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:88
Mass (Da):9,501
Checksum:i7AC26A6AA23E438C
GO

Sequence cautioni

The sequence BAB93475.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231S → R in hepatocellular carcinoma; no effect. 2 Publications
VAR_017612
Natural varianti25 – 339Missing in hepatocellular carcinoma. 1 Publication
VAR_017613
Natural varianti32 – 321D → A in hepatocellular carcinoma. 1 Publication
VAR_017614
Natural varianti32 – 321D → G in PTR and hepatocellular carcinoma. 2 Publications
VAR_017615
Natural varianti32 – 321D → Y in PTR, hepatoblastoma and hepatocellular carcinoma. 4 Publications
Corresponds to variant rs28931588 [ dbSNP | Ensembl ].
VAR_017616
Natural varianti33 – 331S → F in PTR, MDB and hepatocellular carcinoma. 3 Publications
VAR_017617
Natural varianti33 – 331S → L in hepatocellular carcinoma. 1 Publication
VAR_017618
Natural varianti33 – 331S → Y in colorectal cancer and PTR; enhances transactivation of target genes. 3 Publications
VAR_017619
Natural varianti34 – 341G → E in PTR. 1 Publication
VAR_017620
Natural varianti34 – 341G → R in hepatocellular carcinoma. 1 Publication
VAR_017621
Natural varianti34 – 341G → V in hepatoblastoma. 1 Publication
Corresponds to variant rs28931589 [ dbSNP | Ensembl ].
VAR_017622
Natural varianti35 – 351I → S in hepatocellular carcinoma. 1 Publication
VAR_017623
Natural varianti37 – 382SG → W in hepatocellular carcinoma. 1 Publication
VAR_017628
Natural varianti37 – 371S → A in MDB and hepatocellular carcinoma; enhances transactivation of target genes. 3 Publications
VAR_017624
Natural varianti37 – 371S → C in PTR, hepatoblastoma and ovarian cancer. 3 Publications
VAR_017625
Natural varianti37 – 371S → F in PTR. 1 Publication
VAR_017626
Natural varianti37 – 371S → Y in hepatocellular carcinoma. 1 Publication
VAR_017627
Natural varianti41 – 411T → 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. 7 Publications
VAR_017629
Natural varianti41 – 411T → I in PTR, hepatocellular carcinoma and ovarian cancer. 3 Publications
VAR_017630
Natural varianti45 – 451S → F in hepatocellular carcinoma. 1 Publication
VAR_017631
Natural varianti45 – 451S → P in hepatocellular carcinoma. 1 Publication
VAR_017632
Natural varianti45 – 451Missing in colorectal cancer. 1 Publication
VAR_055430
Natural varianti388 – 3881L → P in MRD19. 1 Publication
VAR_072282
Natural varianti688 – 6881M → V.1 Publication
Corresponds to variant rs4135384 [ dbSNP | Ensembl ].
VAR_018954

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 565565Missing in isoform 2. 1 PublicationVSP_006984Add
BLAST
Alternative sequencei652 – 6532AT → GK in isoform 2. 1 PublicationVSP_006985
Alternative sequencei654 – 781128Missing in isoform 2. 1 PublicationVSP_006986Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2694.1. [P35222-1]
PIRiA38973.
RefSeqiNP_001091679.1. NM_001098209.1. [P35222-1]
NP_001091680.1. NM_001098210.1. [P35222-1]
NP_001895.1. NM_001904.3. [P35222-1]
XP_005264943.1. XM_005264886.2. [P35222-1]
UniGeneiHs.476018.

Genome annotation databases

EnsembliENST00000349496; ENSP00000344456; ENSG00000168036.
ENST00000396183; ENSP00000379486; ENSG00000168036.
ENST00000396185; ENSP00000379488; ENSG00000168036.
ENST00000405570; ENSP00000385604; ENSG00000168036.
GeneIDi1499.
KEGGihsa:1499.
UCSCiuc003ckp.2. human. [P35222-1]
uc003ckt.1. human. [P35222-2]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
Wikipedia

Beta-catenin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2694.1. [P35222-1]
PIRiA38973.
RefSeqiNP_001091679.1. NM_001098209.1. [P35222-1]
NP_001091680.1. NM_001098210.1. [P35222-1]
NP_001895.1. NM_001904.3. [P35222-1]
XP_005264943.1. XM_005264886.2. [P35222-1]
UniGeneiHs.476018.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G3JX-ray2.10A/C133-664[»]
1JDHX-ray1.90A135-663[»]
1JPWX-ray2.50A/B/C131-670[»]
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[»]
ProteinModelPortaliP35222.
SMRiP35222. Positions 19-44, 84-665.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107880. 269 interactions.
DIPiDIP-122N.
IntActiP35222. 168 interactions.
MINTiMINT-105089.
STRINGi9606.ENSP00000344456.

Chemistry

BindingDBiP35222.
ChEMBLiCHEMBL3038464.

PTM databases

PhosphoSiteiP35222.

Polymorphism and mutation databases

BioMutaiCTNNB1.
DMDMi461854.

Proteomic databases

MaxQBiP35222.
PaxDbiP35222.
PRIDEiP35222.

Protocols and materials databases

DNASUi1499.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000349496; ENSP00000344456; ENSG00000168036.
ENST00000396183; ENSP00000379486; ENSG00000168036.
ENST00000396185; ENSP00000379488; ENSG00000168036.
ENST00000405570; ENSP00000385604; ENSG00000168036.
GeneIDi1499.
KEGGihsa:1499.
UCSCiuc003ckp.2. human. [P35222-1]
uc003ckt.1. human. [P35222-2]

Organism-specific databases

CTDi1499.
GeneCardsiGC03P041236.
H-InvDBHIX0163439.
HIX0163473.
HGNCiHGNC:2514. CTNNB1.
HPAiCAB000108.
CAB001950.
HPA029159.
HPA029160.
MIMi114500. phenotype.
116806. gene.
132600. phenotype.
155255. phenotype.
156240. phenotype.
167000. phenotype.
181030. phenotype.
615075. phenotype.
neXtProtiNX_P35222.
Orphaneti85142. Aldosterone-producing adenoma.
54595. Craniopharyngioma.
873. Desmoid tumor.
91414. Pilomatrixoma.
404473. Severe intellectual disability-progressive spastic diplegia syndrome.
PharmGKBiPA27013.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG297695.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
InParanoidiP35222.
KOiK02105.
OMAiWEQGFNQ.
OrthoDBiEOG7X9G6B.
PhylomeDBiP35222.
TreeFamiTF317997.

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_13579. Apoptotic cleavage of cell adhesion proteins.
REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_19195. Adherens junctions interactions.
REACT_21402. CDO in myogenesis.
REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
REACT_263982. Ca2+ pathway.
REACT_263991. VEGFR2 mediated vascular permeability.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264178. deactivation of the beta-catenin transactivating complex.
REACT_264242. formation of the beta-catenin:TCF transactivating complex.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264532. binding of TCF/LEF:CTNNB1 to target gene promoters.
REACT_264567. repression of WNT target genes.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264596. TCF dependent signaling in response to WNT.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.
REACT_355469. RHO GTPases activate IQGAPs.
SignaLinkiP35222.

Miscellaneous databases

ChiTaRSiCTNNB1. human.
EvolutionaryTraceiP35222.
GeneWikiiBeta-catenin.
GenomeRNAii1499.
NextBioi6161.
PMAP-CutDBP35222.
PROiP35222.
SOURCEiSearch...

Gene expression databases

BgeeiP35222.
CleanExiHS_CTNNB1.
ExpressionAtlasiP35222. baseline and differential.
GenevisibleiP35222. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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.
    , 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. 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. 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 AT SER-23 AND SER-29 BY GSK3B, PHOSPHORYLATION AT THR-41, 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. 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. 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. 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. 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. 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. Cited for: INVOLVEMENT IN MRD19.
  64. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  65. "beta-catenin is O-GlcNAc glycosylated at Serine 23: implications for beta-catenin's subcellular localization and transactivator function."
    Ha J.R., Hao L., Venkateswaran G., Huang Y.H., Garcia E., Persad S.
    Exp. Cell Res. 321:153-166(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-23, SUBCELLULAR LOCATION.
  66. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  67. "The ubiquitin ligase RNF220 enhances canonical Wnt signaling through USP7-mediated deubiquitination of beta-catenin."
    Ma P., Yang X., Kong Q., Li C., Yang S., Li Y., Mao B.
    Mol. Cell. Biol. 34:4355-4366(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF220.
  68. "MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in the cytoplasm."
    Pangon L., Mladenova D., Watkins L., Van Kralingen C., Currey N., Al-Sohaily S., Lecine P., Borg J.P., Kohonen-Corish M.R.
    Int. J. Cancer 136:55-64(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-49, DEACETYLATION.
  69. Cited for: INTERACTION WITH CTNND2.
  70. "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.
  71. "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.
  72. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-668 IN COMPLEX WITH TCF7L2.
  73. "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.
  74. "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.
  75. "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.
  76. "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.
  77. "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.
  78. "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.
  79. "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.
  80. "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.
  81. "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.
  82. Cited for: VARIANTS MDB PHE-33 AND ALA-37.
  83. Cited for: VARIANT MRD19 PRO-388.

Entry informationi

Entry nameiCTNB1_HUMAN
AccessioniPrimary (citable) accession number: P35222
Secondary accession number(s): A8K1L7
, Q8NEW9, Q8NI94, Q9H391
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 22, 2015
This is version 194 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

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