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Entry version 225 (03 Jul 2019)
Sequence version 1 (01 Jul 1993)
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Protein

Catenin beta-1

Gene

Ctnnb1

Organism
Mus musculus (Mouse)
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 (By similarity). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (PubMed:21325504).By similarity3 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, Neurogenesis, Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-195253 Degradation of beta-catenin by the destruction complex
R-MMU-196299 Beta-catenin phosphorylation cascade
R-MMU-201681 TCF dependent signaling in response to WNT
R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
R-MMU-3134973 LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-MMU-351906 Apoptotic cleavage of cell adhesion proteins
R-MMU-3769402 Deactivation of the beta-catenin transactivating complex
R-MMU-4086398 Ca2+ pathway
R-MMU-418990 Adherens junctions interactions
R-MMU-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-MMU-5218920 VEGFR2 mediated vascular permeability
R-MMU-525793 Myogenesis
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-8951430 RUNX3 regulates WNT signaling

<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:Catnb
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 9

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:88276 Ctnnb1

<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 & Seán O’Donoghue; 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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Sympathetic ganglia-specific conditional knockout mice lead to a reduction in sympathetic ganglia size and in progenitor cell number, but does not alter sympathetic innervation of peripheral target organs.1 Publication

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>Mutagenesisi8M → P: Loss of interaction with VCL. 1 Publication1
Mutagenesisi33S → A: Abolished HIPK2-mediated proteasomal degradation. 1 Publication1
Mutagenesisi37S → A: Abolished HIPK2-mediated proteasomal degradation. 1 Publication1
Mutagenesisi552S → A: Abolishes AMPK-mediated phosphorylation. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4105846

<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 methionineiRemovedBy similarity
<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_00000642722 – 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-acetylalanineBy similarity1
Modified residuei23Phosphoserine; by GSK3-beta; alternateBy similarity1
<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; alternateBy similarity1
Modified residuei29Phosphoserine; by GSK3-betaBy similarity1
Modified residuei33Phosphoserine; by GSK3-beta and HIPK21 Publication1
Modified residuei37Phosphoserine; by GSK3-beta and HIPK21 Publication1
Modified residuei41Phosphothreonine; by GSK3-betaBy similarity1
Modified residuei45PhosphoserineCombined sources1
Modified residuei49N6-acetyllysineBy similarity1
Modified residuei64Phosphotyrosine; by PTK6By similarity1
Modified residuei86Phosphotyrosine; by CSKBy similarity1
Modified residuei142Phosphotyrosine; by FYN and PTK61 Publication1
Modified residuei191PhosphoserineCombined sources1
Modified residuei246Phosphoserine; by CDK5By similarity1
Modified residuei331PhosphotyrosineBy similarity1
Modified residuei333PhosphotyrosineBy similarity1
Modified residuei552Phosphoserine; by AMPKCombined sources1 Publication1
Modified residuei556PhosphothreonineBy similarity1
Modified residuei619S-nitrosocysteine1 Publication1
Modified residuei654PhosphotyrosineBy similarity1
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 by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding (By similarity). Phosphorylated on Ser-33 and Ser-37 by HIPK2. This phosphorylation triggers proteasomal degradation. Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription. Phosphorylation on Ser-191 and Ser-246 by CDK5. Phosphorylation by CDK2 regulates insulin internalization (By similarity). Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or Tyr-333 with the predominant site at Tyr-64 is not essential for inhibition of transcriptional activity (By similarity).By similarity
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.1 Publication
O-glycosylation at Ser-23 decreases nuclear localization and transcriptional activity, and increases localization to the plasma membrane and interaction with E-cadherin CDH1.By similarity
Deacetylated at Lys-49 by SIRT1.By similarity

Keywords - PTMi

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

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q02248

MaxQB - The MaxQuant DataBase

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MaxQBi
Q02248

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

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PaxDbi
Q02248

PeptideAtlas

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PeptideAtlasi
Q02248

PRoteomics IDEntifications database

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PRIDEi
Q02248

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q02248

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

More...
PhosphoSitePlusi
Q02248

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q02248

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
Q02248

<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 cerebellar granule neurons (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000006932 Expressed in 363 organ(s), highest expression level in olfactory bulb

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q02248 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q02248 MM

<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. Binds SLC9A3R1.

Interacts with PTPRU (via the cytoplasmic juxtamembrane domain) and with EMD.

Interacts with SESTD1 and TRPC4.

Interacts with CAV1.

Interacts with PTPRJ.

Interacts with PKT7.

Interacts with FAT1 (via the cytoplasmic domain).

Interacts with CDK2, NDRG2 and NANOS1.

Interacts with NEK2 and CDK5.

Interacts with CARM1, CXADR, PCDH11Y and PTK6.

Interacts with RAPGEF2.

Interacts with SOX7; this interaction may lead to proteasomal degradation of active CTNNB1 and thus inhibition of Wnt/beta-catenin-stimulated transcription.

Identified in a complex with HINT1 and MITF.

Interacts with FHIT.

Interacts with FERMT2.

Identified in a complex with TCF4 and FERMT2. Another cytoplasmic pool is part of a large complex containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. Wnt-dependent activation of DVL antagonizes the action of GSK3B. When GSK3B activity is inhibited the complex dissociates, CTNNB1 is dephosphorylated and is no longer targeted for destruction. The stabilized protein translocates to the nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9, BCL9L and possibly also RUVBL1 and CHD8.

Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits the transcriptional activity of CTNNB1.

Interacts with AJAP1, BAIAP1 and CTNNA3.

Interacts with TRPV4; the TRPV4 and CTNNB1 complex can interact with CDH1.

Interacts with VCL. The CTNNB1 and TCF4 complex interacts with PML.

Interacts with XIRP1. Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 binding.

Interacts directly with AXIN1; the interaction is regulated by CDK2 phosphorylation of AXIN1.

Interacts with GLIS2.

Interacts with SCRIB.

Interacts with TNIK and TCF7L2.

Interacts with SLC30A9.

Interacts with RORA. May interact with P-cadherin/CDH3.

Interacts with RNF220 (By similarity).

Interacts with CTNND2 (By similarity).

Interacts (via the C-terminal region) with CBY1 (By similarity). 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') (By similarity).

Interacts with DLG5 (PubMed:25232112).

Interacts with FAM53B; promoting translocation to the nucleus.

Interacts with TMEM170B (By similarity).

Interacts with AHI1 (By similarity).

Interacts with GID8 (By similarity).

Component of an cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By similarity).

Forms a complex comprising APPL1, RUVBL2, APPL2, HDAC1 and HDAC2 (By similarity).

Interacts with IRF2BPL; mediates the ubiquitination and degradation of CTNNB1 (By similarity).

By similarity21 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
198512, 91 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-318 beta1-catenin - LEF1 complex
CPX-86 Beta-catenin-ICAT complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q02248

Database of interacting proteins

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DIPi
DIP-31560N

Protein interaction database and analysis system

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IntActi
Q02248, 77 interactors

Molecular INTeraction database

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MINTi
Q02248

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000007130

<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

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

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SMRi
Q02248

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q02248

<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 VCL1 PublicationAdd BLAST22
Regioni156 – 178Interaction with BCL9By similarityAdd BLAST23
Regioni772 – 781Interaction with SCRIB1 Publication10

<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

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eggNOGi
KOG4203 Eukaryota
COG0035 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155471

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230958

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q02248

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
321213at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q02248

TreeFam database of animal gene trees

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TreeFami
TF317997

Family and domain databases

Database of protein disorder

More...
DisProti
DP00341

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

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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

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SUPFAMi
SSF48371 SSF48371, 1 hit

PROSITE; a protein domain and family database

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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>. The information is filed in different subsections. The current subsections and their content are listed below:<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 8 potential isoforms that are computationally mapped.Show allAlign All

Q02248-1 [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
GAQGEALGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV
760 770 780
DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L
Length:781
Mass (Da):85,471
Last modified:July 1, 1993 - 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:iD708F170A3FBED6E
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 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9Q6A9E9Q6A9_MOUSE
Catenin beta-1
Ctnnb1
607Annotation 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>
D3YUH4D3YUH4_MOUSE
Catenin beta-1
Ctnnb1
174Annotation 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>
F7BAC9F7BAC9_MOUSE
Catenin beta-1
Ctnnb1
169Annotation 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>
D3Z5Q1D3Z5Q1_MOUSE
Catenin beta-1
Ctnnb1
83Annotation 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>
E9PW26E9PW26_MOUSE
Catenin beta-1
Ctnnb1
90Annotation 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>
F7CRC6F7CRC6_MOUSE
Catenin beta-1
Ctnnb1
174Annotation 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>
F6QZ47F6QZ47_MOUSE
Catenin beta-1
Ctnnb1
145Annotation 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>
D3Z7S6D3Z7S6_MOUSE
Catenin beta-1
Ctnnb1
42Annotation 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>

<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 AAH06739 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti371T → I in BAB31250 (PubMed:16141072).Curated1
Sequence conflicti478A → T in BAB31250 (PubMed:16141072).Curated1
Sequence conflicti487L → F in BAB31250 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M90364 mRNA Translation: AAA37280.1
AK035311 mRNA Translation: BAC29027.1
AK018515 mRNA Translation: BAB31250.1
BC006739 mRNA Translation: AAH06739.1 Different initiation.
BC048153 mRNA Translation: AAH48153.1
BC053065 mRNA Translation: AAH53065.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS23630.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S35091

NCBI Reference Sequences

More...
RefSeqi
NP_001159374.1, NM_001165902.1
NP_031640.1, NM_007614.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932
ENSMUST00000178812; ENSMUSP00000136294; ENSMUSG00000006932

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
12387

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:12387

UCSC genome browser

More...
UCSCi
uc009scu.2 mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90364 mRNA Translation: AAA37280.1
AK035311 mRNA Translation: BAC29027.1
AK018515 mRNA Translation: BAB31250.1
BC006739 mRNA Translation: AAH06739.1 Different initiation.
BC048153 mRNA Translation: AAH48153.1
BC053065 mRNA Translation: AAH53065.1
CCDSiCCDS23630.1
PIRiS35091
RefSeqiNP_001159374.1, NM_001165902.1
NP_031640.1, NM_007614.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DOWX-ray1.80B118-149[»]
1I7WX-ray2.00A/C134-671[»]
1I7XX-ray3.00A/C134-671[»]
1JPPX-ray3.10A/B134-671[»]
1M1EX-ray2.10A134-671[»]
1V18X-ray2.10A134-671[»]
2BCTX-ray2.90A150-665[»]
3BCTX-ray2.10A193-661[»]
3OUWX-ray2.91A134-671[»]
3OUXX-ray2.40A134-671[»]
4EV8X-ray1.90A134-671[»]
4EV9X-ray2.10A134-671[»]
4EVAX-ray2.00A/C134-671[»]
4EVPX-ray2.26A134-671[»]
4EVTX-ray2.34A134-671[»]
4ONSX-ray2.80B/D78-151[»]
SMRiQ02248
ModBaseiSearch...

Protein-protein interaction databases

BioGridi198512, 91 interactors
ComplexPortaliCPX-318 beta1-catenin - LEF1 complex
CPX-86 Beta-catenin-ICAT complex
CORUMiQ02248
DIPiDIP-31560N
IntActiQ02248, 77 interactors
MINTiQ02248
STRINGi10090.ENSMUSP00000007130

Chemistry databases

ChEMBLiCHEMBL4105846

PTM databases

iPTMnetiQ02248
PhosphoSitePlusiQ02248
SwissPalmiQ02248

Proteomic databases

jPOSTiQ02248
MaxQBiQ02248
PaxDbiQ02248
PeptideAtlasiQ02248
PRIDEiQ02248

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932
ENSMUST00000178812; ENSMUSP00000136294; ENSMUSG00000006932
GeneIDi12387
KEGGimmu:12387
UCSCiuc009scu.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1499
MGIiMGI:88276 Ctnnb1

Phylogenomic databases

eggNOGiKOG4203 Eukaryota
COG0035 LUCA
GeneTreeiENSGT00940000155471
HOGENOMiHOG000230958
InParanoidiQ02248
KOiK02105
OMAiFNQNFSQ
OrthoDBi321213at2759
PhylomeDBiQ02248
TreeFamiTF317997

Enzyme and pathway databases

ReactomeiR-MMU-195253 Degradation of beta-catenin by the destruction complex
R-MMU-196299 Beta-catenin phosphorylation cascade
R-MMU-201681 TCF dependent signaling in response to WNT
R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
R-MMU-3134973 LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-MMU-351906 Apoptotic cleavage of cell adhesion proteins
R-MMU-3769402 Deactivation of the beta-catenin transactivating complex
R-MMU-4086398 Ca2+ pathway
R-MMU-418990 Adherens junctions interactions
R-MMU-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-MMU-5218920 VEGFR2 mediated vascular permeability
R-MMU-525793 Myogenesis
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-8951430 RUNX3 regulates WNT signaling

Miscellaneous databases

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

More...
ChiTaRSi
Ctnnb1 mouse
EvolutionaryTraceiQ02248
PMAP-CutDBiQ02248

Protein Ontology

More...
PROi
PR:Q02248

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000006932 Expressed in 363 organ(s), highest expression level in olfactory bulb
ExpressionAtlasiQ02248 baseline and differential
GenevisibleiQ02248 MM

Family and domain databases

DisProtiDP00341
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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_MOUSE
<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: Q02248
Secondary accession number(s): Q922W1, Q9D335
<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: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 3, 2019
This is version 225 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

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