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Entry version 252 (29 Sep 2021)
Sequence version 1 (01 Feb 1994)
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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 (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938).

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 (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938).

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 (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938).

Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex (By similarity).

Acts as a negative regulator of centrosome cohesion (PubMed:18086858).

Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization (PubMed:21262353).

Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2 (PubMed:18957423).

Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:22155184).

Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity).

Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling (By similarity).

By similarity8 Publications

Caution

A paper showing an interaction with TBP and phosphorylation at Tyr-86 and Tyr-654 has been retracted due to panel duplication in several figures.1 Publication1 Publication

<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

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
P35222

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-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-525793, Myogenesis
R-HSA-5339716, Signaling by GSK3beta mutants
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-8853884, Transcriptional Regulation by VENTX
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

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

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000168036

<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

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.
Related information in OMIM
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.
Related information in OMIM
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_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_01761933S → Y in colorectal cancer and PTR; constitutively active Wnt signaling pathway; enhances transactivation of target genes. 4 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01762437S → A in MDB and hepatocellular carcinoma; enhances transactivation of target genes. 3 PublicationsCorresponds to variant dbSNP:rs121913228EnsemblClinVar.1
Ovarian cancer (OC)1 Publication
Disease susceptibility is associated with variants 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.
Related information in OMIM
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.
Related information in OMIM
Neurodevelopmental disorder with spastic diplegia and visual defects (NEDSDV)3 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by global developmental delay, severe intellectual disability with absent or very limited speech, microcephaly, spasticity, and visual abnormalities.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072282388L → P in NEDSDV. 1 Publication1
Natural variantiVAR_079199558 – 781Missing in NEDSDV; the patient also manifest features of exudative vitreoretinopathy. 1 PublicationAdd BLAST224
Vitreoretinopathy, exudative 7 (EVR7)1 Publication
The disease is caused by variants 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.
Related information in OMIM
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
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 variant, 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
569248, Microcystic stromal tumor
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

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P35222, Tchem

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

Genetic variation 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 or proteolytic cleavage.<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 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 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. 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 similarity11 Publications
Ubiquitinated by the SCF(BTRC) E3 ligase complex when phosphorylated by GSK3B, leading to its degradation (PubMed:12077367). Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent proteasomal degradation (PubMed:11389839, PubMed:11389840, PubMed:20307497). Ubiquitinated and degraded following interaction with SOX9 (By similarity).By similarity4 Publications
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

The CPTAC Assay portal

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CPTACi
CPTAC-1745

Encyclopedia of Proteome Dynamics

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EPDi
P35222

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P35222

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
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

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
P35222, 4 sites, 1 O-linked glycan (4 sites)

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P35222

MetOSite database of methionine sulfoxide sites

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MetOSitei
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

<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 adrenal tissue and 252 other tissues

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
ENSG00000168036, Low tissue specificity

<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, 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 (PubMed:29739711, PubMed:22699938).

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).

Forms a complex comprising APPL1, RUVBL2, APPL2, HDAC1 and HDAC2 (PubMed:19433865).

Interacts with IRF2BPL; mediates the ubiquitination and degradation of CTNNB1 (PubMed:29374064).

Interacts with AMFR (By similarity).

Interacts with LMBR1L (PubMed:31073040).

Interacts with SOX30; prevents interaction of CTNNB1 with TCF7L2/TCF4 and leads to inhibition of Wnt signaling (PubMed:29739711).

Interacts with SOX9; inhibiting CTNNB1 activity by competing with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling (By similarity).

Interacts with SPN/CD43 cytoplasmic tail (PubMed:15003504).

By similarity1 Publication53 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">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P35222
With#Exp.IntAct
A2M [P01023]3EBI-491549,EBI-640741
ABL1 [P00519]2EBI-491549,EBI-375543
ACTN4 [O43707]7EBI-491549,EBI-351526
AMER1 [Q5JTC6]9EBI-491549,EBI-6169747
APC [P25054]19EBI-491549,EBI-727707
AR [P10275]11EBI-491549,EBI-608057
AXIN1 [O15169]44EBI-491549,EBI-710484
AXIN2 [Q9Y2T1]2EBI-491549,EBI-4400025
BCL9 [O00512]5EBI-491549,EBI-533127
BCR/ABL fusion [A1Z199]2EBI-491549,EBI-7286259
BDNF - isoform 2 [P23560-2]3EBI-491549,EBI-12275524
BTRC [Q9Y297]8EBI-491549,EBI-307461
CASP6 [P55212]3EBI-491549,EBI-718729
CBSL [P0DN79]3EBI-491549,EBI-14245939
CDC73 [Q6P1J9]10EBI-491549,EBI-930143
CDH1 [P12830]14EBI-491549,EBI-727477
CDH2 [P19022]8EBI-491549,EBI-2256711
CDH5 [P33151]7EBI-491549,EBI-2903122
CREBBP [Q92793]2EBI-491549,EBI-81215
CRYAB [P02511]6EBI-491549,EBI-739060
CTNNA1 [P35221]5EBI-491549,EBI-701918
CTNNA3 - isoform 1 [Q9UI47-1]4EBI-491549,EBI-21980640
CTNNBIP1 [Q9NSA3]14EBI-491549,EBI-747082
DACT1 [Q9NYF0]3EBI-491549,EBI-3951744
DMWD [G5E9A7]3EBI-491549,EBI-10976677
DNMT1 [P26358]8EBI-491549,EBI-719459
EGR1 [P18146]7EBI-491549,EBI-2834611
EMD [P50402]3EBI-491549,EBI-489887
EPHA2 [P29317]2EBI-491549,EBI-702104
FBXW11 [Q9UKB1]4EBI-491549,EBI-355189
FERMT2 [Q96AC1]13EBI-491549,EBI-4399465
FGF14 - isoform 2 [Q92915-2]3EBI-491549,EBI-12836320
FHIT [P49789]4EBI-491549,EBI-741760
FOXM1 [Q08050]16EBI-491549,EBI-866480
GAPDH [P04406]3EBI-491549,EBI-354056
GFAP [P14136]3EBI-491549,EBI-744302
GLIS2 [Q9BZE0]6EBI-491549,EBI-7251368
GSK3B [P49841]19EBI-491549,EBI-373586
HDAC6 [Q9UBN7]4EBI-491549,EBI-301697
HIF1A [Q16665]4EBI-491549,EBI-447269
HIP1 [O00291]3EBI-491549,EBI-473886
HSP90AA1 [P07900]3EBI-491549,EBI-296047
HTT [P42858]14EBI-491549,EBI-466029
IGF1R [P08069]3EBI-491549,EBI-475981
IQGAP1 [P46940]3EBI-491549,EBI-297509
JPH3 [Q8WXH2]3EBI-491549,EBI-1055254
JRK [O75564]3EBI-491549,EBI-8607681
KANK1 [Q14678]2EBI-491549,EBI-2556221
KIAA1109 [Q2LD37]2EBI-491549,EBI-2683809
LAMP2 - isoform LAMP-2B [P13473-2]3EBI-491549,EBI-21591415
LEF1 [Q9UJU2]10EBI-491549,EBI-926131
LEO1 [Q8WVC0]2EBI-491549,EBI-932432
LRP8 - isoform 3 [Q14114-3]3EBI-491549,EBI-25832196
MAP1LC3B [Q9GZQ8]5EBI-491549,EBI-373144
MECP2 [P51608]3EBI-491549,EBI-1189067
MLLT10 [P55197]4EBI-491549,EBI-1104952
NDRG1 [Q92597]3EBI-491549,EBI-716486
NDUFV2 [P19404]3EBI-491549,EBI-713665
NFKB1 [P19838]3EBI-491549,EBI-300010
NOS3 [P29474]4EBI-491549,EBI-1391623
NR5A2 - isoform 2 [O00482-1]5EBI-491549,EBI-15960777
NUMB [P49757]2EBI-491549,EBI-915016
NUMB - isoform 3 [P49757-3]3EBI-491549,EBI-10692196
PKM [P14618]4EBI-491549,EBI-353408
PKM - isoform M2 [P14618-1]3EBI-491549,EBI-4304679
PRPF40A - isoform 2 [O75400-2]3EBI-491549,EBI-5280197
PTH1R [Q03431]4EBI-491549,EBI-2860297
PTK7 [Q13308]5EBI-491549,EBI-2803245
PTPRC [P08575]2EBI-491549,EBI-1341
PTPRG [P23470]2EBI-491549,EBI-2258115
PTPRJ [Q12913]2EBI-491549,EBI-2264500
PXN [P49023]4EBI-491549,EBI-702209
RAN [P62826]3EBI-491549,EBI-286642
RELA [Q04206]3EBI-491549,EBI-73886
RUNX3 [Q13761]12EBI-491549,EBI-925990
RUVBL1 [Q9Y265]3EBI-491549,EBI-353675
SATB1 [Q01826]9EBI-491549,EBI-743747
SOX17 [Q9H6I2]2EBI-491549,EBI-9106753
SPRED1 [Q7Z699]3EBI-491549,EBI-5235340
SRC [P12931]2EBI-491549,EBI-621482
TCF4 [P15884]22EBI-491549,EBI-533224
TCF7 [P36402]4EBI-491549,EBI-2119465
TCF7L2 [Q9NQB0]27EBI-491549,EBI-924724
TERT [O14746]2EBI-491549,EBI-1772203
TNIK [Q9UKE5]3EBI-491549,EBI-1051794
TOP2A [P11388]5EBI-491549,EBI-539628
TOR1A - isoform 2 [O14656-2]3EBI-491549,EBI-25847109
TP53BP2 [Q13625]5EBI-491549,EBI-77642
UBR5 [O95071]6EBI-491549,EBI-358329
WWTR1 [Q9GZV5]4EBI-491549,EBI-747743
YAP1 [P46937]13EBI-491549,EBI-1044059
YAP1 - isoform 3 [P46937-3]2EBI-491549,EBI-6558686
Axin1 [O35625] from Mus musculus.4EBI-491549,EBI-2365912
axin1 [Q9YGY0] from Xenopus laevis.2EBI-491549,EBI-1037449
Bcl9l [Q67FY2] from Mus musculus.2EBI-491549,EBI-5234367
CAV1 [P33724] from Canis lupus familiaris.5EBI-491549,EBI-79998
Ctnna1 [P26231] from Mus musculus.2EBI-491549,EBI-647895
ipaC [P18012] from Shigella flexneri.4EBI-491549,EBI-491541
Lef1 [P27782] from Mus musculus.2EBI-491549,EBI-984464
Ryk [Q01887] from Mus musculus.2EBI-491549,EBI-16110594
Tax1bp3 [Q9DBG9] from Mus musculus.3EBI-491549,EBI-1161647
Wwtr1 [Q9EPK5] from Mus musculus.2EBI-491549,EBI-1211920

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
107880, 735 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, 257 interactors

Molecular INTeraction database

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MINTi
P35222

STRING: functional protein association networks

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STRINGi
9606.ENSP00000344456

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P35222

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P35222, protein

<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
P35222

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
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
Regioni34 – 57DisorderedSequence analysisAdd BLAST24
Regioni156 – 178Interaction with BCL91 PublicationAdd BLAST23
Regioni705 – 781DisorderedSequence analysisAdd BLAST77
Regioni772 – 781Interaction with SCRIBBy similarity10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi34 – 48Polar residuesSequence analysisAdd BLAST15

<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

Ensembl GeneTree

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GeneTreei
ENSGT00940000155471

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35222

Identification of Orthologs from Complete Genome Data

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OMAi
EDDVDNQ

Database of Orthologous Groups

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OrthoDBi
321213at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P35222

TreeFam database of animal gene trees

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TreeFami
TF317997

Family and domain databases

Database of protein disorder

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DisProti
DP01119

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.10.10, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

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IDEALi
IID00039

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

The PANTHER Classification System

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PANTHERi
PTHR45976, PTHR45976, 1 hit

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

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>. 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 13 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 13 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:2 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:2 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:2 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:2 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:2 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:2 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:2 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:2 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:2 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>
A0A2R8Y815A0A2R8Y815_HUMAN
Catenin beta-1
CTNNB1
186Annotation 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. Truncated N-terminus.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; constitutively active Wnt signaling pathway; enhances transactivation of target genes. 4 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 NEDSDV. 1 Publication1
Natural variantiVAR_079199558 – 781Missing in NEDSDV; the patient also manifest features of exudative vitreoretinopathy. 1 PublicationAdd BLAST224
Natural variantiVAR_018954688M → V1 PublicationCorresponds to variant dbSNP:rs4135384EnsemblClinVar.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

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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

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PIRi
A38973

NCBI Reference Sequences

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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

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000349496; ENSP00000344456; ENSG00000168036
ENST00000396183; ENSP00000379486; ENSG00000168036
ENST00000396185; ENSP00000379488; ENSG00000168036
ENST00000405570; ENSP00000385604; ENSG00000168036
ENST00000431914; ENSP00000412219; ENSG00000168036
ENST00000433400; ENSP00000387455; ENSG00000168036
ENST00000441708; ENSP00000401599; ENSG00000168036
ENST00000450969; ENSP0000