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Entry version 134 (12 Aug 2020)
Sequence version 1 (05 Sep 2006)
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Protein

Catenin beta-1

Gene

CTNNB1

Organism
Bos taurus (Bovine)
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 (By similarity). 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 (By similarity). 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. 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. 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 similarity

<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-BTA-195253, Degradation of beta-catenin by the destruction complex
R-BTA-196299, Beta-catenin phosphorylation cascade
R-BTA-201681, TCF dependent signaling in response to WNT
R-BTA-201722, Formation of the beta-catenin:TCF transactivating complex
R-BTA-3134973, LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-BTA-3769402, Deactivation of the beta-catenin transactivating complex
R-BTA-4086398, Ca2+ pathway
R-BTA-418990, Adherens junctions interactions
R-BTA-5218920, VEGFR2 mediated vascular permeability
R-BTA-525793, Myogenesis
R-BTA-5626467, RHO GTPases activate IQGAPs
R-BTA-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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 22

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:27802, 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 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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002828812 – 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%5Fprocessing%5Fsection">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 HIPK2By similarity1
Modified residuei37Phosphoserine; by GSK3-beta and HIPK2By similarity1
Modified residuei41Phosphothreonine; by GSK3-betaBy similarity1
Modified residuei45PhosphoserineBy similarity1
Modified residuei49N6-acetyllysineBy similarity1
Modified residuei64Phosphotyrosine; by PTK6By similarity1
Modified residuei86Phosphotyrosine; by CSKBy similarity1
Modified residuei142Phosphotyrosine; by FYN and PTK6By similarity1
Modified residuei191Phosphoserine; by CDK5By similarity1
Modified residuei246Phosphoserine; by CDK5By similarity1
Modified residuei331PhosphotyrosineBy similarity1
Modified residuei333PhosphotyrosineBy similarity1
Modified residuei552Phosphoserine; by AMPKBy similarity1
Modified residuei556PhosphothreonineBy similarity1
Modified residuei619S-nitrosocysteineBy similarity1
Modified residuei654Phosphotyrosine; by CSKBy similarity1
Modified residuei675PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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. 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). Ubiquitinated and degraded following interaction with SOX9 (By similarity).By similarity
S-nitrosylation at Cys-619 within adherens junctions promotes VEGF-induced, NO-dependent endothelial cell permeability by disrupting interaction with E-cadherin, thus mediating disassembly adherens junctions.By similarity
O-glycosylation at Ser-23 decreases nuclear localization and transcriptional activity, and increases localization to the plasma membrane and interaction with E-cadherin CDH1.By similarity
Deacetylated at Lys-49 by SIRT1.By similarity

Keywords - PTMi

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

Proteomic databases

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

More...
PaxDbi
Q0VCX4

PeptideAtlas

More...
PeptideAtlasi
Q0VCX4

PRoteomics IDEntifications database

More...
PRIDEi
Q0VCX4

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q0VCX4

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSBTAG00000016420, Expressed in placenta and 18 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q0VCX4, baseline and differential

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Two separate complex-associated pools are found in the cytoplasm. The majority is present as component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1 and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Another cytoplasmic pool is part of a large complex containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. Wnt-dependent activation of DVL antagonizes the action of GSK3B. When GSK3B activity is inhibited the complex dissociates, CTNNB1 is dephosphorylated and is no longer targeted for destruction. The stabilized protein translocates to the nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9, BCL9L and possibly also RUVBL1 and CHD8. Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 binding.

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

Interacts with AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1.

Interacts with GLIS2 and SLC30A9.

Interacts with XIRP1 and MUC1.

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

Interacts with SCRIB.

Interacts with TNIK.

Interacts with SESTD1 and TRPC4.

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

Interacts with CAV1.

Interacts with TRPV4. The TRPV4 and CTNNB1 complex can interact with CDH1.

Interacts with VCL.

Interacts with PTPRJ.

Interacts with PKT7.

Interacts with FAT1 (via the cytoplasmic domain).

Interacts with NANOS1 and NDRG2.

Interacts with NEK2, CDK2 and 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 TCF4 complex interacts with PML.

Interacts with FERMT2.

Identified in a complex with TCF4 and FERMT2.

Interacts with RORA. May interact with P-cadherin/CDH3 (By similarity).

Interacts with RAPGEF2.

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').

Interacts with DLG5 (By similarity).

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).

Interacts with LMBR1L and AMFR (By similarity).

Interacts with LMBR1L (By similarity).

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

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

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q0VCX4, 1 interactor

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000021838

<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

3D structure databases

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

More...
SMRi
Q0VCX4

Database of comparative protein structure models

More...
ModBasei
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati151 – 191ARM 1Add BLAST41
Repeati193 – 234ARM 2Add BLAST42
Repeati235 – 276ARM 3Add BLAST42
Repeati277 – 318ARM 4Add BLAST42
Repeati319 – 360ARM 5Add BLAST42
Repeati361 – 389ARM 6Add BLAST29
Repeati400 – 441ARM 7Add BLAST42
Repeati442 – 484ARM 8Add BLAST43
Repeati489 – 530ARM 9Add BLAST42
Repeati531 – 571ARM 10Add BLAST41
Repeati594 – 636ARM 11Add BLAST43
Repeati637 – 666ARM 12Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 23Interaction with VCLBy similarityAdd BLAST22
Regioni156 – 178Interaction with BCL9By similarityAdd BLAST23
Regioni772 – 781Interaction with SCRIBBy similarity10

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

Belongs to the beta-catenin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4203, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000155471

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_008757_1_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q0VCX4

KEGG Orthology (KO)

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KOi
K02105

Identification of Orthologs from Complete Genome Data

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OMAi
MAWNEXP

Database of Orthologous Groups

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OrthoDBi
321213at2759

TreeFam database of animal gene trees

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TreeFami
TF317997

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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

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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 2 potential isoforms that are computationally mapped.Show allAlign All

Q0VCX4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG
60 70 80 90 100
NPEEEDVDTT 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):85,511
Last modified:September 5, 2006 - 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:i6148652F953F0723
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A3Q1LJ64A0A3Q1LJ64_BOVIN
Catenin beta-1
CTNNB1
636Annotation 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>
A0A3Q1NES2A0A3Q1NES2_BOVIN
Catenin beta-1
CTNNB1
774Annotation score:

Annotation score:1 out of 5

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

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
BT030683 mRNA Translation: ABS44999.1
BC119949 mRNA Translation: AAI19950.1

NCBI Reference Sequences

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RefSeqi
NP_001069609.1, NM_001076141.1
XP_005222580.1, XM_005222523.3
XP_005222581.1, XM_005222524.3
XP_005222582.1, XM_005222525.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSBTAT00000021838; ENSBTAP00000021838; ENSBTAG00000016420

Database of genes from NCBI RefSeq genomes

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GeneIDi
539003

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
bta:539003

<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
BT030683 mRNA Translation: ABS44999.1
BC119949 mRNA Translation: AAI19950.1
RefSeqiNP_001069609.1, NM_001076141.1
XP_005222580.1, XM_005222523.3
XP_005222581.1, XM_005222524.3
XP_005222582.1, XM_005222525.3

3D structure databases

SMRiQ0VCX4
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ0VCX4, 1 interactor
STRINGi9913.ENSBTAP00000021838

PTM databases

iPTMnetiQ0VCX4

Proteomic databases

PaxDbiQ0VCX4
PeptideAtlasiQ0VCX4
PRIDEiQ0VCX4

Genome annotation databases

EnsembliENSBTAT00000021838; ENSBTAP00000021838; ENSBTAG00000016420
GeneIDi539003
KEGGibta:539003

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1499
VGNCiVGNC:27802, CTNNB1

Phylogenomic databases

eggNOGiKOG4203, Eukaryota
GeneTreeiENSGT00940000155471
HOGENOMiCLU_008757_1_1_1
InParanoidiQ0VCX4
KOiK02105
OMAiMAWNEXP
OrthoDBi321213at2759
TreeFamiTF317997

Enzyme and pathway databases

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

Gene expression databases

BgeeiENSBTAG00000016420, Expressed in placenta and 18 other tissues
ExpressionAtlasiQ0VCX4, baseline and differential

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR011989, ARM-like
IPR016024, ARM-type_fold
IPR000225, Armadillo
IPR013284, Beta-catenin
PANTHERiPTHR45976, PTHR45976, 1 hit
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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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_BOVIN
<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: Q0VCX4
Secondary accession number(s): A7E3R2
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: September 5, 2006
Last modified: August 12, 2020
This is version 134 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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