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UniProtKB - B6V8E6 (CTNB1_CANLF)

Entry version 108 (23 Feb 2022)
Sequence version 1 (16 Dec 2008)
Previous versions | rss
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Protein

Catenin beta-1

Gene

CTNNB1

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

<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>OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
<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 identifieri9615 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›
<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
  • UP000002254 <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: Unplaced

<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 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_00004238712 – 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 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 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. 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		B6V8E6

PRoteomics IDEntifications database

More...PRIDEi		B6V8E6

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		B6V8E6

<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		ENSCAFG00000005204, Expressed in mucosa of urinary bladder and 54 other tissues

<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 part of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1 and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Binds SLC9A3R1.

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

Interacts with SESTD1 and TRPC4.

Interacts with CAV1.

Interacts with PTPRJ.

Interacts with PKT7.

Interacts with FAT1 (via the cytoplasmic domain).

Interacts with CDK2, NDRG2 and NANOS1.

Interacts with NEK2 and CDK5.

Interacts with CARM1, CXADR, PCDH11Y and PTK6.

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

Identified in a complex with HINT1 and MITF.

Interacts with FHIT.

Interacts with FERMT2.

Identified in a complex with TCF4 and FERMT2. Another cytoplasmic pool is part of a large complex containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. Wnt-dependent activation of DVL antagonizes the action of GSK3B. When GSK3B activity is inhibited, the complex disassociates, 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.

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

Interacts with AJAP1, BAIAP1 and CTNNA3.

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

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

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

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

Interacts with GLIS2.

Interacts with SCRIB.

Interacts with TNIK and TCF7L2.

Interacts with SLC30A9.

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

Interacts with RAPGEF2 (PubMed:10873669).

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 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).

Interacts with SPN/CD43 cytoplasmic tail (By similarity).

By similarity1 Publication

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		B6V8E6

Protein interaction database and analysis system

More...IntActi		B6V8E6, 7 interactors

Molecular INTeraction database

More...MINTi		B6V8E6

STRING: functional protein association networks

More...STRINGi		9615.ENSCAFP00000007783

<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		B6V8E6

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>Repeati141 – 180ARM 1Add BLAST40
Repeati181 – 223ARM 2Add BLAST43
Repeati224 – 264ARM 3Add BLAST41
Repeati265 – 306ARM 4Add BLAST42
Repeati308 – 349ARM 5Add BLAST42
Repeati350 – 390ARM 6Add BLAST41
Repeati392 – 429ARM 7Add BLAST38
Repeati430 – 473ARM 8Add BLAST44
Repeati478 – 519ARM 9Add BLAST42
Repeati520 – 582ARM 10Add BLAST63
Repeati583 – 623ARM 11Add BLAST41
Repeati624 – 664ARM 12Add BLAST41

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 – 56DisorderedSequence analysisAdd BLAST23
Regioni156 – 178Interaction with BCL9By similarityAdd 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

More...eggNOGi		KOG4203, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_008757_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		B6V8E6

Identification of Orthologs from Complete Genome Data

More...OMAi		EDDVDNQ

Database of Orthologous Groups

More...OrthoDBi		321213at2759

TreeFam database of animal gene trees

More...TreeFami		TF317997

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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

The PANTHER Classification System

More...PANTHERi		PTHR45976, PTHR45976, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01869, BCATNINFAMLY

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00185, ARM, 12 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48371, SSF48371, 1 hit

PROSITE; a protein domain and family database

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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%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>Sequencei

<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.

B6V8E6-1 [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:December 16, 2008 - 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

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
FJ268743 mRNA Translation: ACJ04159.1
AAEX03013510 Genomic DNA No translation available.

NCBI Reference Sequences

More...RefSeqi		NP_001131124.1, NM_001137652.1
XP_013961954.1, XM_014106479.1
XP_013961955.1, XM_014106480.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		477032

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		cfa:477032

<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
FJ268743 mRNA Translation: ACJ04159.1
AAEX03013510 Genomic DNA No translation available.
RefSeqiNP_001131124.1, NM_001137652.1
XP_013961954.1, XM_014106479.1
XP_013961955.1, XM_014106480.1

3D structure databases

SMRiB6V8E6
ModBaseiSearch...

Protein-protein interaction databases

CORUMiB6V8E6
IntActiB6V8E6, 7 interactors
MINTiB6V8E6
STRINGi9615.ENSCAFP00000007783

PTM databases

iPTMnetiB6V8E6

Proteomic databases

PaxDbiB6V8E6
PRIDEiB6V8E6

Genome annotation databases

GeneIDi477032
KEGGicfa:477032

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1499

Phylogenomic databases

eggNOGiKOG4203, Eukaryota
HOGENOMiCLU_008757_1_1_1
InParanoidiB6V8E6
OMAiEDDVDNQ
OrthoDBi321213at2759
TreeFamiTF317997

Gene expression databases

BgeeiENSCAFG00000005204, Expressed in mucosa of urinary bladder and 54 other tissues

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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCTNB1_CANLF
<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: B6V8E6
<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: October 16, 2013
Last sequence update: December 16, 2008
Last modified: February 23, 2022
This is version 108 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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