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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
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • 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
  • RNA polymerase II transcription factor binding Source: ParkinsonsUK-UCL
  • signal transducer activity Source: ProtInc
  • SMAD binding Source: BHF-UCL
  • transcription coactivator activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: Ensembl
  • transcription factor binding Source: ParkinsonsUK-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

BioCyciZFISH:ENSG00000168036-MONOMER.
ReactomeiR-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-201681. TCF dependent signaling in response to WNT.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-3134973. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
R-HSA-351906. Apoptotic cleavage of cell adhesion proteins.
R-HSA-375170. CDO in myogenesis.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-381771. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
R-HSA-4086398. Ca2+ pathway.
R-HSA-418990. Adherens junctions interactions.
R-HSA-4411364. Binding of TCF/LEF:CTNNB1 to target gene promoters.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-4641265. Repression of WNT target genes.
R-HSA-5218920. VEGFR2 mediated vascular permeability.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5626467. RHO GTPases activate IQGAPs.
SignaLinkiP35222.
SIGNORiP35222.

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
Proteomesi
  • UP000005640 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: UniProtKB
  • beta-catenin destruction complex Source: BHF-UCL
  • beta-catenin-TCF7L2 complex Source: BHF-UCL
  • beta-catenin-TCF complex Source: ParkinsonsUK-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
  • flotillin complex 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
  • 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
  • Wnt signalosome Source: ParkinsonsUK-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)DescriptionActionsGraphical viewLength
Natural variantiVAR_01761532D → G in PTR and hepatocellular carcinoma. 2 PublicationsCorresponds to variant rs121913396dbSNPEnsembl.1
Natural variantiVAR_01761632D → Y in PTR, hepatoblastoma and hepatocellular carcinoma. 4 PublicationsCorresponds to variant rs28931588dbSNPEnsembl.1
Natural variantiVAR_01761733S → F in PTR, MDB and hepatocellular carcinoma. 3 PublicationsCorresponds to variant rs121913400dbSNPEnsembl.1
Natural variantiVAR_01761933S → Y in colorectal cancer and PTR; enhances transactivation of target genes. 3 PublicationsCorresponds to variant rs121913400dbSNPEnsembl.1
Natural variantiVAR_01762034G → E in PTR. 1 PublicationCorresponds to variant rs28931589dbSNPEnsembl.1
Natural variantiVAR_01762537S → C in PTR, hepatoblastoma and ovarian cancer. 3 PublicationsCorresponds to variant rs121913403dbSNPEnsembl.1
Natural variantiVAR_01762637S → F in PTR. 1 PublicationCorresponds to variant rs121913403dbSNPEnsembl.1
Natural variantiVAR_01763041T → I in PTR, hepatocellular carcinoma and ovarian cancer. 3 PublicationsCorresponds to variant rs121913413dbSNPEnsembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_01761733S → F in PTR, MDB and hepatocellular carcinoma. 3 PublicationsCorresponds to variant rs121913400dbSNPEnsembl.1
Natural variantiVAR_01762437S → A in MDB and hepatocellular carcinoma; enhances transactivation of target genes. 3 PublicationsCorresponds to variant rs121913228dbSNPEnsembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_072282388L → P in MRD19. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi29S → F: No effect. 1 Publication1
Mutagenesisi64Y → F: Abolishes phosphorylation by PTK6. 1 Publication1
Mutagenesisi142Y → E: No effect on interaction with BCL9 and BCL9L. 1 Publication1
Mutagenesisi156L → A: Abolishes interaction with BCL9 but no effect on interaction with CDH3; when associated with A-159. 1 Publication1
Mutagenesisi159L → 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 Publication1
Mutagenesisi178L → A: No effect on interaction with BCL9 and CDH3. 1 Publication1
Mutagenesisi253F → A: Abolishes or strongly reduces AXIN2 binding. 1 Publication1
Mutagenesisi260H → A: Abolishes or strongly reduces AXIN1 and AXIN2 binding. Strongly reduces phosphorylation and degradation; when associated with A-386 and A-383. 1 Publication1
Mutagenesisi292K → A: Abolishes or strongly reduces AXIN1 and AXIN2 binding. 1 Publication1
Mutagenesisi312K → E: Abolishes TCF7L2 binding. 1 Publication1
Mutagenesisi345K → A: Abolishes APC binding. 1 Publication1
Mutagenesisi383W → A: Abolishes APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-386. 1 Publication1
Mutagenesisi386R → A: Strongly reduces APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-383. 1 Publication1
Mutagenesisi426N → A: Abolishes TCF7L2 and LEF1 binding. 1 Publication1
Mutagenesisi435K → A: Strongly reduces or abolishes LEF1 binding. 2 Publications1
Mutagenesisi435K → E: Abolishes TCF7L2 binding. 2 Publications1
Mutagenesisi469R → A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding. 1 Publication1
Mutagenesisi470H → A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding. 1 Publication1
Mutagenesisi508K → A: Abolishes TCF7L2 and LEF1 binding. 1 Publication1
Mutagenesisi654Y → E: Enhances TBP binding and transactivation of target genes. 1 Publication1
Mutagenesisi654Y → F: Abolishes increase of TBP binding after phosphorylation by CSK. 1 Publication1
Mutagenesisi660F → A: Abolishes CTNNBIP1 binding; when associated with A-661. 1 Publication1
Mutagenesisi661R → A: Abolishes CTNNBIP1 binding; when associated with A-660. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi1499.
MalaCardsiCTNNB1.
MIMi114500. phenotype.
132600. phenotype.
155255. phenotype.
156240. phenotype.
167000. phenotype.
181030. phenotype.
615075. phenotype.
OpenTargetsiENSG00000168036.
Orphaneti85142. Aldosterone-producing adenoma.
54595. Craniopharyngioma.
873. Desmoid tumor.
91414. Pilomatrixoma.
404473. Severe intellectual disability-progressive spastic diplegia syndrome.
PharmGKBiPA27013.

Chemistry databases

ChEMBLiCHEMBL5866.
DrugBankiDB03904. Urea.

Polymorphism and mutation databases

BioMutaiCTNNB1.
DMDMi461854.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000642712 – 781Catenin beta-1Add BLAST780

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei23Phosphoserine; by GSK3-beta; alternate1 Publication1
Glycosylationi23O-linked (GlcNAc); alternate1 Publication1
Modified residuei29Phosphoserine; by GSK3-beta1 Publication1
Modified residuei33Phosphoserine; by GSK3-beta and HIPK21 Publication1
Modified residuei37Phosphoserine; by GSK3-beta and HIPK21 Publication1
Modified residuei41Phosphothreonine; by GSK3-beta1 Publication1
Modified residuei45Phosphoserine1 Publication1
Modified residuei49N6-acetyllysine1 Publication1
Modified residuei64Phosphotyrosine; by PTK61 Publication1
Modified residuei86Phosphotyrosine; by CSK1 Publication1
Modified residuei142Phosphotyrosine; by FYN and PTK62 Publications1
Modified residuei191Phosphoserine; by CDK5Combined sources1 Publication1
Modified residuei246Phosphoserine; by CDK51 Publication1
Modified residuei331Phosphotyrosine; by PTK61 Publication1
Modified residuei333Phosphotyrosine; by PTK61 Publication1
Modified residuei552PhosphoserineCombined sources1
Modified residuei556PhosphothreonineCombined sources1
Modified residuei619S-nitrosocysteineBy similarity1
Modified residuei654Phosphotyrosine; by CSK1 Publication1
Modified residuei675PhosphoserineCombined sources1

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

EPDiP35222.
MaxQBiP35222.
PaxDbiP35222.
PeptideAtlasiP35222.
PRIDEiP35222.

PTM databases

iPTMnetiP35222.
PhosphoSitePlusiP35222.
SwissPalmiP35222.

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

BgeeiENSG00000168036.
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). Interacts (via the C-terminal region) with CBY1 (PubMed:12712206, PubMed:16424001).42 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005192EBI-491549,EBI-375543
ACTN4O437077EBI-491549,EBI-351526
AMER1Q5JTC69EBI-491549,EBI-6169747
APCP2505416EBI-491549,EBI-727707
ARP102758EBI-491549,EBI-608057
AXIN1O1516944EBI-491549,EBI-710484
Axin1O356254EBI-491549,EBI-2365912From a different organism.
BCL9O005122EBI-491549,EBI-533127
BCR/ABL fusionA1Z1992EBI-491549,EBI-7286259
BTRCQ9Y2976EBI-491549,EBI-307461
CAV1P337245EBI-491549,EBI-79998From a different organism.
CDC73Q6P1J99EBI-491549,EBI-930143
CDH1P1283011EBI-491549,EBI-727477
CDH2P190223EBI-491549,EBI-2256711
CDH5P331516EBI-491549,EBI-2903122
CREBBPQ927932EBI-491549,EBI-81215
Ctnna1P262312EBI-491549,EBI-647895From a different organism.
CTNNBIP1Q9NSA310EBI-491549,EBI-747082
DACT1Q9NYF03EBI-491549,EBI-3951744
EGR1P181467EBI-491549,EBI-2834611
EMDP504023EBI-491549,EBI-489887
FBXW11Q9UKB14EBI-491549,EBI-355189
FERMT2Q96AC113EBI-491549,EBI-4399465
FGFR1P113622EBI-491549,EBI-1028277
FLT1P179482EBI-491549,EBI-1026718
FOXM1Q0805016EBI-491549,EBI-866480
GLIS2Q9BZE06EBI-491549,EBI-7251368
GSK3BP4984116EBI-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
JUPP149233EBI-491549,EBI-702484
KANK1Q146782EBI-491549,EBI-2556221
KIAA1109Q2LD372EBI-491549,EBI-2683809
LEF1Q9UJU26EBI-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
TCF4P1588420EBI-491549,EBI-533224
TCF7P364024EBI-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

GO - Molecular functioni

  • alpha-catenin binding Source: BHF-UCL
  • androgen receptor binding Source: UniProtKB
  • cadherin binding Source: UniProtKB
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • estrogen receptor 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
  • RNA polymerase II transcription factor binding Source: ParkinsonsUK-UCL
  • SMAD binding Source: BHF-UCL
  • transcription factor binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi107880. 302 interactors.
DIPiDIP-122N.
IntActiP35222. 187 interactors.
MINTiMINT-105089.
STRINGi9606.ENSP00000344456.

Chemistry databases

BindingDBiP35222.

Structurei

Secondary structure

1781
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi135 – 150Combined sources16
Helixi152 – 160Combined sources9
Helixi165 – 179Combined sources15
Helixi182 – 189Combined sources8
Helixi192 – 204Combined sources13
Helixi208 – 221Combined sources14
Helixi225 – 233Combined sources9
Helixi236 – 243Combined sources8
Helixi249 – 265Combined sources17
Helixi269 – 276Combined sources8
Helixi278 – 284Combined sources7
Helixi285 – 287Combined sources3
Helixi291 – 305Combined sources15
Helixi309 – 317Combined sources9
Helixi320 – 330Combined sources11
Helixi334 – 347Combined sources14
Helixi353 – 359Combined sources7
Helixi362 – 367Combined sources6
Turni368 – 371Combined sources4
Helixi375 – 389Combined sources15
Helixi399 – 408Combined sources10
Helixi414 – 427Combined sources14
Turni428 – 430Combined sources3
Helixi432 – 440Combined sources9
Helixi443 – 454Combined sources12
Helixi458 – 471Combined sources14
Beta strandi473 – 475Combined sources3
Helixi478 – 487Combined sources10
Helixi491 – 496Combined sources6
Beta strandi499 – 501Combined sources3
Helixi504 – 517Combined sources14
Helixi521 – 523Combined sources3
Helixi524 – 529Combined sources6
Helixi532 – 547Combined sources16
Beta strandi550 – 552Combined sources3
Beta strandi554 – 557Combined sources4
Beta strandi561 – 563Combined sources3
Helixi566 – 580Combined sources15
Helixi584 – 592Combined sources9
Helixi596 – 601Combined sources6
Helixi602 – 604Combined sources3
Helixi608 – 621Combined sources14
Helixi625 – 633Combined sources9
Helixi637 – 642Combined sources6
Helixi643 – 645Combined sources3
Helixi649 – 662Combined sources14
Turni663 – 665Combined sources3
Helixi668 – 682Combined sources15
Helixi688 – 690Combined sources3
Beta strandi778 – 780Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP35222.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 23Interaction with VCLBy similarityAdd BLAST22
Regioni156 – 178Interaction with BCL91 PublicationAdd BLAST23
Regioni772 – 781Interaction with SCRIBBy similarity10

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4203. Eukaryota.
COG0035. LUCA.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
InParanoidiP35222.
KOiK02105.
OMAiFRTEPMT.
OrthoDBiEOG091G03A5.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01761223S → R in hepatocellular carcinoma; no effect. 2 Publications1
Natural variantiVAR_01761325 – 33Missing in hepatocellular carcinoma. 1 Publication9
Natural variantiVAR_01761432D → A in hepatocellular carcinoma. 1 PublicationCorresponds to variant rs121913396dbSNPEnsembl.1
Natural variantiVAR_01761532D → G in PTR and hepatocellular carcinoma. 2 PublicationsCorresponds to variant rs121913396dbSNPEnsembl.1
Natural variantiVAR_01761632D → Y in PTR, hepatoblastoma and hepatocellular carcinoma. 4 PublicationsCorresponds to variant rs28931588dbSNPEnsembl.1
Natural variantiVAR_01761733S → F in PTR, MDB and hepatocellular carcinoma. 3 PublicationsCorresponds to variant rs121913400dbSNPEnsembl.1
Natural variantiVAR_01761833S → L in hepatocellular carcinoma. 1 Publication1
Natural variantiVAR_01761933S → Y in colorectal cancer and PTR; enhances transactivation of target genes. 3 PublicationsCorresponds to variant rs121913400dbSNPEnsembl.1
Natural variantiVAR_01762034G → E in PTR. 1 PublicationCorresponds to variant rs28931589dbSNPEnsembl.1
Natural variantiVAR_01762134G → R in hepatocellular carcinoma. 1 PublicationCorresponds to variant rs121913399dbSNPEnsembl.1
Natural variantiVAR_01762234G → V in hepatoblastoma. 1 PublicationCorresponds to variant rs28931589dbSNPEnsembl.1
Natural variantiVAR_01762335I → S in hepatocellular carcinoma. 1 Publication1
Natural variantiVAR_01762837 – 38SG → W in hepatocellular carcinoma. 1 Publication2
Natural variantiVAR_01762437S → A in MDB and hepatocellular carcinoma; enhances transactivation of target genes. 3 PublicationsCorresponds to variant rs121913228dbSNPEnsembl.1
Natural variantiVAR_01762537S → C in PTR, hepatoblastoma and ovarian cancer. 3 PublicationsCorresponds to variant rs121913403dbSNPEnsembl.1
Natural variantiVAR_01762637S → F in PTR. 1 PublicationCorresponds to variant rs121913403dbSNPEnsembl.1
Natural variantiVAR_01762737S → Y in hepatocellular carcinoma. 1 PublicationCorresponds to variant rs121913403dbSNPEnsembl.1
Natural variantiVAR_01762941T → 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 PublicationsCorresponds to variant rs121913412dbSNPEnsembl.1
Natural variantiVAR_01763041T → I in PTR, hepatocellular carcinoma and ovarian cancer. 3 PublicationsCorresponds to variant rs121913413dbSNPEnsembl.1
Natural variantiVAR_01763145S → F in hepatocellular carcinoma. 1 PublicationCorresponds to variant rs121913409dbSNPEnsembl.1
Natural variantiVAR_01763245S → P in hepatocellular carcinoma. 1 PublicationCorresponds to variant rs121913407dbSNPEnsembl.1
Natural variantiVAR_05543045Missing in colorectal cancer. 1 Publication1
Natural variantiVAR_072282388L → P in MRD19. 1 Publication1
Natural variantiVAR_018954688M → V.1 PublicationCorresponds to variant rs4135384dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0069841 – 565Missing in isoform 2. 1 PublicationAdd BLAST565
Alternative sequenceiVSP_006985652 – 653AT → GK in isoform 2. 1 Publication2
Alternative sequenceiVSP_006986654 – 781Missing in isoform 2. 1 PublicationAdd BLAST128

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]
XP_016861227.1. XM_017005738.1. [P35222-1]
UniGeneiHs.476018.
Hs.712929.

Genome annotation databases

EnsembliENST00000349496; ENSP00000344456; ENSG00000168036. [P35222-1]
ENST00000396183; ENSP00000379486; ENSG00000168036. [P35222-1]
ENST00000396185; ENSP00000379488; ENSG00000168036. [P35222-1]
ENST00000405570; ENSP00000385604; ENSG00000168036. [P35222-1]
GeneIDi1499.
KEGGihsa:1499.
UCSCiuc003ckp.3. human. [P35222-1]

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]
XP_016861227.1. XM_017005738.1. [P35222-1]
UniGeneiHs.476018.
Hs.712929.

3D structure databases

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

Protein-protein interaction databases

BioGridi107880. 302 interactors.
DIPiDIP-122N.
IntActiP35222. 187 interactors.
MINTiMINT-105089.
STRINGi9606.ENSP00000344456.

Chemistry databases

BindingDBiP35222.
ChEMBLiCHEMBL5866.
DrugBankiDB03904. Urea.

PTM databases

iPTMnetiP35222.
PhosphoSitePlusiP35222.
SwissPalmiP35222.

Polymorphism and mutation databases

BioMutaiCTNNB1.
DMDMi461854.

Proteomic databases

EPDiP35222.
MaxQBiP35222.
PaxDbiP35222.
PeptideAtlasiP35222.
PRIDEiP35222.

Protocols and materials databases

DNASUi1499.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000349496; ENSP00000344456; ENSG00000168036. [P35222-1]
ENST00000396183; ENSP00000379486; ENSG00000168036. [P35222-1]
ENST00000396185; ENSP00000379488; ENSG00000168036. [P35222-1]
ENST00000405570; ENSP00000385604; ENSG00000168036. [P35222-1]
GeneIDi1499.
KEGGihsa:1499.
UCSCiuc003ckp.3. human. [P35222-1]

Organism-specific databases

CTDi1499.
DisGeNETi1499.
GeneCardsiCTNNB1.
H-InvDBHIX0163439.
HIX0163473.
HGNCiHGNC:2514. CTNNB1.
HPAiCAB000108.
CAB001950.
HPA029159.
HPA029160.
MalaCardsiCTNNB1.
MIMi114500. phenotype.
116806. gene.
132600. phenotype.
155255. phenotype.
156240. phenotype.
167000. phenotype.
181030. phenotype.
615075. phenotype.
neXtProtiNX_P35222.
OpenTargetsiENSG00000168036.
Orphaneti85142. Aldosterone-producing adenoma.
54595. Craniopharyngioma.
873. Desmoid tumor.
91414. Pilomatrixoma.
404473. Severe intellectual disability-progressive spastic diplegia syndrome.
PharmGKBiPA27013.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4203. Eukaryota.
COG0035. LUCA.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
InParanoidiP35222.
KOiK02105.
OMAiFRTEPMT.
OrthoDBiEOG091G03A5.
PhylomeDBiP35222.
TreeFamiTF317997.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000168036-MONOMER.
ReactomeiR-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-201681. TCF dependent signaling in response to WNT.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-3134973. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
R-HSA-351906. Apoptotic cleavage of cell adhesion proteins.
R-HSA-375170. CDO in myogenesis.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-381771. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
R-HSA-4086398. Ca2+ pathway.
R-HSA-418990. Adherens junctions interactions.
R-HSA-4411364. Binding of TCF/LEF:CTNNB1 to target gene promoters.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-4641265. Repression of WNT target genes.
R-HSA-5218920. VEGFR2 mediated vascular permeability.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5626467. RHO GTPases activate IQGAPs.
SignaLinkiP35222.
SIGNORiP35222.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000168036.
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...

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: November 30, 2016
This is version 209 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

Similar proteinsi

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