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Protein

Catenin beta-1

Gene

CTNNB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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, as component of an E-cadherin:catenin adhesion complex. 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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator
Biological processCell adhesion, Host-virus interaction, Neurogenesis, Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-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-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
R-HSA-8876493 InlA-mediated entry of Listeria monocytogenes into host cells
R-HSA-8951430 RUNX3 regulates WNT signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P35222

SIGNOR Signaling Network Open Resource

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SIGNORi
P35222

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Catenin beta-1
Alternative name(s):
Beta-catenin
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CTNNB1
Synonyms:CTNNB
ORF Names:OK/SW-cl.35, PRO2286
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000168036.16

Human Gene Nomenclature Database

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HGNCi
HGNC:2514 CTNNB1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
116806 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P35222

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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)3 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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01761632D → Y in PTR, hepatoblastoma and hepatocellular carcinoma. 4 PublicationsCorresponds to variant dbSNP:rs28931588EnsemblClinVar.1
Natural variantiVAR_01761733S → F in PTR, MDB and hepatocellular carcinoma. 3 PublicationsCorresponds to variant dbSNP:rs121913400EnsemblClinVar.1
Natural variantiVAR_01762034G → E in PTR. 1 PublicationCorresponds to variant dbSNP:rs28931589EnsemblClinVar.1
Natural variantiVAR_01762537S → C in PTR, hepatoblastoma and ovarian cancer. 3 PublicationsCorresponds to variant dbSNP:rs121913403EnsemblClinVar.1
Natural variantiVAR_01762637S → F in PTR. 1 PublicationCorresponds to variant dbSNP:rs121913403EnsemblClinVar.1
Natural variantiVAR_01763041T → I in PTR, hepatocellular carcinoma and ovarian cancer. 3 PublicationsCorresponds to variant dbSNP:rs121913413EnsemblClinVar.1
Medulloblastoma (MDB)2 Publications
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
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)3 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
Natural variantiVAR_079199558 – 781Missing in MRD19; the patient also manifest features of exudative vitreoretinopathy. 1 PublicationAdd BLAST224
Vitreoretinopathy, exudative 7 (EVR7)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of exudative vitreoretinopathy, a disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery.
See also OMIM:617572
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_079200710R → C in EVR7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs748653573EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

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DisGeNETi
1499

MalaCards human disease database

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MalaCardsi
CTNNB1
MIMi114500 phenotype
132600 phenotype
155255 phenotype
156240 phenotype
167000 phenotype
181030 phenotype
615075 phenotype
617572 phenotype

Open Targets

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OpenTargetsi
ENSG00000168036

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
210159 Adult hepatocellular carcinoma
54595 Craniopharyngioma
873 Desmoid tumor
891 Familial exudative vitreoretinopathy
85142 NON RARE IN EUROPE: Aldosterone-producing adenoma
33402 Pediatric hepatocellular carcinoma
91414 Pilomatrixoma
404473 Severe intellectual disability-progressive spastic diplegia syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27013

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5866

Drug and drug target database

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DrugBanki
DB03904 Urea

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CTNNB1

Domain mapping of disease mutations (DMDM)

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DMDMi
461854

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000642712 – 781Catenin beta-1Add BLAST780

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1
Modified residuei23Phosphoserine; by GSK3-beta; alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi23O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei29Phosphoserine; by GSK3-beta1 Publication1
Modified residuei33Phosphoserine; by GSK3-beta and HIPK22 Publications1
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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 and GSK3B, this phosphorylation triggers proteasomal degradation (PubMed:25169422). 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 similarity12 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

Encyclopedia of Proteome Dynamics

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EPDi
P35222

MaxQB - The MaxQuant DataBase

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MaxQBi
P35222

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P35222

PeptideAtlas

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PeptideAtlasi
P35222

PRoteomics IDEntifications database

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PRIDEi
P35222

ProteomicsDB human proteome resource

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ProteomicsDBi
54988

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P35222

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P35222

SwissPalm database of S-palmitoylation events

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SwissPalmi
P35222

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P35222

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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). Expressed in breast cancer tissues (at protein level) (PubMed:29367600).4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000168036 Expressed in 240 organ(s), highest expression level in adrenal tissue

CleanEx database of gene expression profiles

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CleanExi
HS_CTNNB1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P35222 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P35222 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB000108
CAB001950
HPA029159
HPA029160

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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). The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (PubMed:25169422). Interacts with DLG5 (By similarity). Interacts with FAM53B; promoting translocation to the nucleus (PubMed:25183871). Interacts with TMEM170B (PubMed:29367600). Interacts with AHI1 (PubMed:21623382). Interacts with GID8 (PubMed:28829046). Component of an cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (PubMed:28051089).By similarity49 Publications
(Microbial infection) Interacts with herpes virus 8 protein vPK; this interaction inhibits the Wnt signaling pathway.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005192EBI-491549,EBI-375543
ACTN4O437077EBI-491549,EBI-351526
AMER1Q5JTC69EBI-491549,EBI-6169747
APCP2505417EBI-491549,EBI-727707
ARP1027511EBI-491549,EBI-608057
AXIN1O1516944EBI-491549,EBI-710484
Axin1O356254EBI-491549,EBI-2365912From Mus musculus.
axin1Q9YGY02EBI-491549,EBI-1037449From Xenopus laevis.
AXIN2Q9Y2T12EBI-491549,EBI-4400025
BCL9O005122EBI-491549,EBI-533127
BCR/ABL fusionA1Z1992EBI-491549,EBI-7286259
BTRCQ9Y2978EBI-491549,EBI-307461
CAV1P337245EBI-491549,EBI-79998From Canis lupus familiaris.
CDC73Q6P1J99EBI-491549,EBI-930143
CDH1P1283014EBI-491549,EBI-727477
CDH2P190228EBI-491549,EBI-2256711
CDH5P331516EBI-491549,EBI-2903122
CREBBPQ927932EBI-491549,EBI-81215
CTNNA1P352213EBI-491549,EBI-701918
Ctnna1P262312EBI-491549,EBI-647895From Mus musculus.
CTNNBIP1Q9NSA310EBI-491549,EBI-747082
DACT1Q9NYF03EBI-491549,EBI-3951744
DNMT1P263588EBI-491549,EBI-719459
EGR1P181467EBI-491549,EBI-2834611
EMDP504023EBI-491549,EBI-489887
EPHA2P293172EBI-491549,EBI-702104
FBXW11Q9UKB14EBI-491549,EBI-355189
FERMT2Q96AC113EBI-491549,EBI-4399465
FGFR1P113622EBI-491549,EBI-1028277
FHITP497894EBI-491549,EBI-741760
FLT1P179482EBI-491549,EBI-1026718
FOXM1Q0805016EBI-491549,EBI-866480
GLIS2Q9BZE06EBI-491549,EBI-7251368
GSK3BP4984119EBI-491549,EBI-373586
HIF1AQ166654EBI-491549,EBI-447269
HTTP428585EBI-491549,EBI-466029
IGF1RP080693EBI-491549,EBI-475981
ipaCP180124EBI-491549,EBI-491541From Shigella flexneri.
IQGAP1P469403EBI-491549,EBI-297509
JRKO755643EBI-491549,EBI-8607681
JUPP149233EBI-491549,EBI-702484
KANK1Q146782EBI-491549,EBI-2556221
KIAA1109Q2LD372EBI-491549,EBI-2683809
LEF1Q9UJU29EBI-491549,EBI-926131
Lef1P277822EBI-491549,EBI-984464From Mus musculus.
LEO1Q8WVC02EBI-491549,EBI-932432
Lztfl1Q9JHQ52EBI-491549,EBI-6142879From Mus musculus.
MAP1LC3BQ9GZQ85EBI-491549,EBI-373144
MLLT10P551974EBI-491549,EBI-1104952
NDRG1Q925973EBI-491549,EBI-716486
NFKB1P198383EBI-491549,EBI-300010
NOS3P294744EBI-491549,EBI-1391623
NR5A2O00482-15EBI-491549,EBI-15960777
NUMBP497572EBI-491549,EBI-915016
NUMBP49757-33EBI-491549,EBI-10692196
PARD3Q8TEW02EBI-491549,EBI-81968
PECAM1P162843EBI-491549,EBI-716404
PITX2Q996972EBI-491549,EBI-1175211
PKMP146184EBI-491549,EBI-353408
PKMP14618-13EBI-491549,EBI-4304679
PTH1RQ034314EBI-491549,EBI-2860297
PTK7Q133085EBI-491549,EBI-2803245
PTPRCP085752EBI-491549,EBI-1341
PTPRGP234702EBI-491549,EBI-2258115
PTPRJQ129132EBI-491549,EBI-2264500
PXNP490234EBI-491549,EBI-702209
RELAQ042063EBI-491549,EBI-73886
RUNX3Q1376112EBI-491549,EBI-925990
RUVBL1Q9Y2653EBI-491549,EBI-353675
RykQ018872EBI-491549,EBI-16110594From Mus musculus.
SATB1Q018269EBI-491549,EBI-743747
SKP1P632083EBI-491549,EBI-307486
SOX17Q9H6I22EBI-491549,EBI-9106753
SRCP129312EBI-491549,EBI-621482
TCF4P1588422EBI-491549,EBI-533224
TCF7P364024EBI-491549,EBI-2119465
TCF7L2Q9NQB025EBI-491549,EBI-924724
TERTO147462EBI-491549,EBI-1772203
TNIKQ9UKE53EBI-491549,EBI-1051794
TOP2AP113885EBI-491549,EBI-539628
TP53BP2Q136255EBI-491549,EBI-77642
UBR5O950716EBI-491549,EBI-358329
WWTR1Q9GZV54EBI-491549,EBI-747743
Wwtr1Q9EPK52EBI-491549,EBI-1211920From Mus musculus.
YAP1P4693713EBI-491549,EBI-1044059
YAP1P46937-32EBI-491549,EBI-6558686

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
107880, 330 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-316 beta1-catenin - LEF1 complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P35222

Database of interacting proteins

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DIPi
DIP-122N

Protein interaction database and analysis system

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IntActi
P35222, 219 interactors

Molecular INTeraction database

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MINTi
P35222

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000344456

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P35222

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1781
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P35222

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P35222

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P35222

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 23Interaction with VCLBy similarityAdd BLAST22
Regioni156 – 178Interaction with BCL91 PublicationAdd BLAST23
Regioni772 – 781Interaction with SCRIBBy similarity10

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the beta-catenin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4203 Eukaryota
COG0035 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155471

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230958

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000919

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35222

KEGG Orthology (KO)

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KOi
K02105

Identification of Orthologs from Complete Genome Data

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OMAi
FNQNFSQ

Database of Orthologous Groups

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OrthoDBi
EOG091G03A5

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P35222

TreeFam database of animal gene trees

More...
TreeFami
TF317997

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000225 Armadillo
IPR013284 Beta-catenin

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00514 Arm, 4 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01869 BCATNINFAMLY

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00185 ARM, 12 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48371 SSF48371, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50176 ARM_REPEAT, 9 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 17 potential isoforms that are computationally mapped.Show allAlign All

P35222-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG
60 70 80 90 100
NPEEEDVDTS QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP
110 120 130 140 150
ETLDEGMQIP STQFDAAHPT NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT
160 170 180 190 200
RAIPELTKLL NDEDQVVVNK AAVMVHQLSK KEASRHAIMR SPQMVSAIVR
210 220 230 240 250
TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL VKMLGSPVDS
260 270 280 290 300
VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC
310 320 330 340 350
LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC
360 370 380 390 400
SSNKPAIVEA GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG
410 420 430 440 450
LLGTLVQLLG SDDINVVTCA AGILSNLTCN NYKNKMMVCQ VGGIEALVRT
460 470 480 490 500
VLRAGDREDI TEPAICALRH LTSRHQEAEM AQNAVRLHYG LPVVVKLLHP
510 520 530 540 550
PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL VRAHQDTQRR
560 570 580 590 600
TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV
610 620 630 640 650
QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG
660 670 680 690 700
VATYAAAVLF RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI
710 720 730 740 750
GAQGEPLGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV
760 770 780
DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L
Length:781
Mass (Da):85,497
Last modified:February 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCB78F165A3EEF86E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 17 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B4DGU4B4DGU4_HUMAN
Catenin beta-1
CTNNB1
774Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EMJ5E7EMJ5_HUMAN
Catenin beta-1
CTNNB1
149Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y804A0A2R8Y804_HUMAN
Catenin beta-1
CTNNB1
702Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y5C3A0A2R8Y5C3_HUMAN
Catenin beta-1
CTNNB1
737Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y7Z0A0A2R8Y7Z0_HUMAN
Catenin beta-1
CTNNB1
780Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y750A0A2R8Y750_HUMAN
Catenin beta-1
CTNNB1
744Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y543A0A2R8Y543_HUMAN
Catenin beta-1
CTNNB1
715Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y5A3A0A2R8Y5A3_HUMAN
Catenin beta-1
CTNNB1
783Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8YCH5A0A2R8YCH5_HUMAN
Catenin beta-1
CTNNB1
779Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y5Z1A0A2R8Y5Z1_HUMAN
Catenin beta-1
CTNNB1
752Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There are more potential isoformsShow all

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAG35511 differs from that shown. Probable cloning artifact.Curated
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 PublicationsCorresponds to variant dbSNP:rs1413975856Ensembl.1
Natural variantiVAR_01761325 – 33Missing in hepatocellular carcinoma. 1 Publication9
Natural variantiVAR_01761432D → A in hepatocellular carcinoma. 1 PublicationCorresponds to variant dbSNP:rs121913396EnsemblClinVar.1
Natural variantiVAR_01761532D → G in PTR and hepatocellular carcinoma. 2 PublicationsCorresponds to variant dbSNP:rs121913396EnsemblClinVar.1
Natural variantiVAR_01761632D → Y in PTR, hepatoblastoma and hepatocellular carcinoma. 4 PublicationsCorresponds to variant dbSNP:rs28931588EnsemblClinVar.1
Natural variantiVAR_01761733S → F in PTR, MDB and hepatocellular carcinoma. 3 PublicationsCorresponds to variant dbSNP:rs121913400EnsemblClinVar.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 dbSNP:rs121913400EnsemblClinVar.1
Natural variantiVAR_01762034G → E in PTR. 1 PublicationCorresponds to variant dbSNP:rs28931589EnsemblClinVar.1
Natural variantiVAR_01762134G → R in hepatocellular carcinoma. 1 PublicationCorresponds to variant dbSNP:rs121913399EnsemblClinVar.1
Natural variantiVAR_01762234G → V in hepatoblastoma. 1 PublicationCorresponds to variant dbSNP:rs28931589EnsemblClinVar.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 dbSNP:rs121913228EnsemblClinVar.1
Natural variantiVAR_01762537S → C in PTR, hepatoblastoma and ovarian cancer. 3 PublicationsCorresponds to variant dbSNP:rs121913403EnsemblClinVar.1
Natural variantiVAR_01762637S → F in PTR. 1 PublicationCorresponds to variant dbSNP:rs121913403EnsemblClinVar.1
Natural variantiVAR_01762737S → Y in hepatocellular carcinoma. 1 PublicationCorresponds to variant dbSNP:rs121913403EnsemblClinVar.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 dbSNP:rs121913412EnsemblClinVar.1
Natural variantiVAR_01763041T → I in PTR, hepatocellular carcinoma and ovarian cancer. 3 PublicationsCorresponds to variant dbSNP:rs121913413EnsemblClinVar.1
Natural variantiVAR_01763145S → F in hepatocellular carcinoma. 1 PublicationCorresponds to variant dbSNP:rs121913409EnsemblClinVar.1
Natural variantiVAR_01763245S → P in hepatocellular carcinoma. 1 PublicationCorresponds to variant dbSNP:rs121913407EnsemblClinVar.1
Natural variantiVAR_05543045Missing in colorectal cancer. 1 Publication1
Natural variantiVAR_072282388L → P in MRD19. 1 Publication1
Natural variantiVAR_079199558 – 781Missing in MRD19; the patient also manifest features of exudative vitreoretinopathy. 1 PublicationAdd BLAST224
Natural variantiVAR_018954688M → V1 PublicationCorresponds to variant dbSNP:rs4135384Ensembl.1
Natural variantiVAR_079200710R → C in EVR7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs748653573EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X87838 mRNA Translation: CAA61107.1
Z19054 mRNA Translation: CAA79497.1
AF130085 mRNA Translation: AAG35511.1 Sequence problems.
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.

The Consensus CDS (CCDS) project

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CCDSi
CCDS2694.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A38973

NCBI Reference Sequences

More...
RefSeqi
NP_001091679.1, NM_001098209.1
NP_001091680.1, NM_001098210.1
NP_001895.1, NM_001904.3
XP_005264943.1, XM_005264886.2
XP_016861227.1, XM_017005738.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.476018
Hs.712929

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000349496; ENSP00000344456; ENSG00000168036
ENST00000396183; ENSP00000379486; ENSG00000168036
ENST00000396185; ENSP00000379488; ENSG00000168036
ENST00000405570; ENSP00000385604; ENSG00000168036
ENST00000431914; ENSP00000412219; ENSG00000168036
ENST00000433400; ENSP00000387455; ENSG00000168036
ENST00000441708; ENSP00000401599; ENSG00000168036
ENST00000450969; ENSP00000409302; ENSG00000168036
ENST00000642248; ENSP00000495244; ENSG00000168036
ENST00000642315; ENSP00000495076; ENSG00000168036
ENST00000642426; ENSP00000495719; ENSG00000168036
ENST00000642992; ENSP00000496385; ENSG00000168036
ENST00000643031; ENSP00000495450; ENSG00000168036
ENST00000643297; ENSP00000494677; ENSG00000168036
ENST00000643541; ENSP00000494411; ENSG00000168036
ENST00000643977; ENSP00000494053; ENSG00000168036
ENST00000643992; ENSP00000493610; ENSG00000168036
ENST00000644867; ENSP00000495992; ENSG00000168036
ENST00000645210; ENSP00000496180; ENSG00000168036
ENST00000645320; ENSP00000495360; ENSG00000168036
ENST00000645982; ENSP00000494845; ENSG00000168036
ENST00000646369; ENSP00000494914; ENSG00000168036
ENST00000646725; ENSP00000496021; ENSG00000168036
ENST00000647390; ENSP00000493533; ENSG00000168036

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1499

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1499

UCSC genome browser

More...
UCSCi
uc003ckp.3 human

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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 Sequence problems.
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
PIRiA38973
RefSeqiNP_001091679.1, NM_001098209.1
NP_001091680.1, NM_001098210.1
NP_001895.1, NM_001904.3
XP_005264943.1, XM_005264886.2
XP_016861227.1, XM_017005738.1
UniGeneiHs.476018
Hs.712929

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
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, 330 interactors
ComplexPortaliCPX-316 beta1-catenin - LEF1 complex
CORUMiP35222
DIPiDIP-122N
IntActiP35222, 219 interactors
MINTiP35222
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
ProteomicsDBi54988

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1499
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000349496; ENSP00000344456; ENSG00000168036
ENST00000396183; ENSP00000379486; ENSG00000168036
ENST00000396185; ENSP00000379488; ENSG00000168036
ENST00000405570; ENSP00000385604; ENSG00000168036
ENST00000431914; ENSP00000412219; ENSG00000168036
ENST00000433400; ENSP00000387455; ENSG00000168036
ENST00000441708; ENSP00000401599; ENSG00000168036
ENST00000450969; ENSP00000409302; ENSG00000168036
ENST00000642248; ENSP00000495244; ENSG00000168036
ENST00000642315; ENSP00000495076; ENSG00000168036
ENST00000642426; ENSP00000495719; ENSG00000168036
ENST00000642992; ENSP00000496385; ENSG00000168036
ENST00000643031; ENSP00000495450; ENSG00000168036
ENST00000643297; ENSP00000494677; ENSG00000168036
ENST00000643541; ENSP00000494411; ENSG00000168036
ENST00000643977; ENSP00000494053; ENSG00000168036
ENST00000643992; ENSP00000493610; ENSG00000168036
ENST00000644867; ENSP00000495992; ENSG00000168036
ENST00000645210; ENSP00000496180; ENSG00000168036
ENST00000645320; ENSP00000495360; ENSG00000168036
ENST00000645982; ENSP00000494845; ENSG00000168036
ENST00000646369; ENSP00000494914; ENSG00000168036
ENST00000646725; ENSP00000496021; ENSG00000168036
ENST00000647390; ENSP00000493533; ENSG00000168036
GeneIDi1499
KEGGihsa:1499
UCSCiuc003ckp.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1499
DisGeNETi1499
EuPathDBiHostDB:ENSG00000168036.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CTNNB1

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0163439
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
617572 phenotype
neXtProtiNX_P35222
OpenTargetsiENSG00000168036
Orphaneti210159 Adult hepatocellular carcinoma
54595 Craniopharyngioma
873 Desmoid tumor
891 Familial exudative vitreoretinopathy
85142 NON RARE IN EUROPE: Aldosterone-producing adenoma
33402 Pediatric hepatocellular carcinoma
91414 Pilomatrixoma
404473 Severe intellectual disability-progressive spastic diplegia syndrome
PharmGKBiPA27013

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4203 Eukaryota
COG0035 LUCA
GeneTreeiENSGT00940000155471
HOGENOMiHOG000230958
HOVERGENiHBG000919
InParanoidiP35222
KOiK02105
OMAiFNQNFSQ
OrthoDBiEOG091G03A5
PhylomeDBiP35222
TreeFamiTF317997

Enzyme and pathway databases

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-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
R-HSA-8876493 InlA-mediated entry of Listeria monocytogenes into host cells
R-HSA-8951430 RUNX3 regulates WNT signaling
SignaLinkiP35222
SIGNORiP35222

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
CTNNB1 human
EvolutionaryTraceiP35222

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Beta-catenin

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
1499
PMAP-CutDBiP35222

Protein Ontology

More...
PROi
PR:P35222

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000168036 Expressed in 240 organ(s), highest expression level in adrenal tissue
CleanExiHS_CTNNB1
ExpressionAtlasiP35222 baseline and differential
GenevisibleiP35222 HS

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000225 Armadillo
IPR013284 Beta-catenin
PfamiView protein in Pfam
PF00514 Arm, 4 hits
PRINTSiPR01869 BCATNINFAMLY
SMARTiView protein in SMART
SM00185 ARM, 12 hits
SUPFAMiSSF48371 SSF48371, 1 hit
PROSITEiView protein in PROSITE
PS50176 ARM_REPEAT, 9 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCTNB1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P35222
Secondary accession number(s): A8K1L7
, Q8NEW9, Q8NI94, Q9H391
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: December 5, 2018
This is version 231 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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