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Reviewed, UniProtKB/Swiss-Prot Q9WU82 (CTNB1_RAT)

Last modified January 19, 2010. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Catenin beta-1
Alternative name(s):
    Beta-catenin
Gene names
Name: Ctnnb1
Synonyms: Catnb
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length781 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Involved in the regulation of cell adhesion and in signal transduction through the Wnt pathway.

Subunit structure

Two separate pools are found in the cytoplasm: one is PSEN1/cadherin/catenin complex which anchors to the actin cytoskeleton. The other 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 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 By similarity. Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits the transcriptional activity of CTNNB1 By similarity. Interacts with AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1. Interacts with GLIS2. Interacts with XIRP1 By similarity. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain) and with SLC30A9. Interacts with EMD By similarity. Interacts with SCRIB By similarity. Interacts with TNIK and TCF7L2 By similarity. Ref.3

Subcellular location

Cytoplasm. Cytoplasm › cytoskeleton. Nucleus. Cell junction › adherens junction By similarity. Note: Cytoplasmic when it is unstabilized (high level of phosphorylation) or bound to CDH1. Translocates to the nucleus when it is stabilized (low level of phosphorylation). Interaction with GLIS2 promotes nuclear translocation. Interaction with EMD inhibits nuclear localization By similarity.

Tissue specificity

Expressed in the testis.

Developmental stage

Highly expressed at E30-60 day DPC in the testis. Reduced expression at E90 day DPC.

Post-translational modification

Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-33 By similarity.

EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding By similarity.

Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1A, APC and TBL1X Probable. Its ubiquitination leads to its subsequent proteasomal degradation By similarity.

Sequence similarities

Belongs to the beta-catenin family.

Contains 12 ARM repeats.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 781781Catenin beta-1
PRO_0000064273

Regions

Repeat151 – 19141ARM 1
Repeat193 – 23442ARM 2
Repeat235 – 27642ARM 3
Repeat277 – 31842ARM 4
Repeat319 – 36042ARM 5
Repeat361 – 38929ARM 6
Repeat400 – 44142ARM 7
Repeat442 – 48443ARM 8
Repeat489 – 53042ARM 9
Repeat531 – 57141ARM 10
Repeat594 – 63643ARM 11
Repeat637 – 66630ARM 12
Region772 – 78110Interaction with SCRIB By similarity

Amino acid modifications

Modified residue231Phosphoserine; by GSK3-beta By similarity
Modified residue291Phosphoserine; by GSK3-beta By similarity
Modified residue331Phosphoserine; by GSK3-beta By similarity
Modified residue371Phosphoserine; by GSK3-beta By similarity
Modified residue411Phosphothreonine; by GSK3-beta By similarity
Modified residue451Phosphoserine By similarity
Modified residue861Phosphotyrosine; by CSK By similarity
Modified residue1911Phosphoserine Ref.4
Modified residue5511Phosphothreonine By similarity
Modified residue5521Phosphoserine By similarity
Modified residue5561Phosphothreonine By similarity
Modified residue6541Phosphotyrosine; by CSK By similarity
Modified residue6751Phosphoserine Ref.4

Experimental info

Sequence conflict3681P → L in AAK85253. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q9WU82-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 9C29186B6DD54B87

FASTA78185,455
        10         20         30         40         50         60 
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTS 

        70         80         90        100        110        120 
QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDAAHPT 

       130        140        150        160        170        180 
NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK 

       190        200        210        220        230        240 
KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL 

       250        260        270        280        290        300 
VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC 

       310        320        330        340        350        360 
LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC SSNKPAIVEA 

       370        380        390        400        410        420 
GGMQALGPHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA 

       430        440        450        460        470        480 
AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM 

       490        500        510        520        530        540 
AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL 

       550        560        570        580        590        600 
VRAHQDTQRR TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV 

       610        620        630        640        650        660 
QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF 

       670        680        690        700        710        720 
RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI GAQGEALGYR QDDPSYRSFH 

       730        740        750        760        770        780 
SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD 


L

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References

« Hide 'large scale' references
[1]"Study on the formation of specialized inter-Sertoli cell junctions in vitro."
Chung S.S.W., Lee W.M., Cheng C.Y.
J. Cell. Physiol. 181:258-272(1999) [PubMed: 10497305] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Testis.
[2]"Sequencing of the rat beta-catenin gene (Ctnnb1) and mutational analysis of liver tumors induced by 2-amino-3-methylimidazo[4,5-f]quinoline."
Li Q., Dixon B.M., Al-Fageeh M., Blum C.A., Dashwood R.H.
Gene 283:255-262(2002) [PubMed: 11867232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Fischer 344.
[3]"A novel beta-catenin-binding protein inhibits beta-catenin-dependent Tcf activation and axis formation."
Sakamoto I., Kishida S., Fukui A., Kishida M., Yamamoto H., Hino S., Michiue T., Takada S., Asashima M., Kikuchi A.
J. Biol. Chem. 275:32871-32878(2000) [PubMed: 10921920] [Abstract]
Cited for: INTERACTION WITH CHD8.
[4]"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
Moser K., White F.M.
J. Proteome Res. 5:98-104(2006) [PubMed: 16396499] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-675, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF121265 mRNA. Translation: AAD28504.1.
AF397179 Genomic DNA. Translation: AAK85253.1.
IPIIPI00325912.
RefSeqNP_445809.2.
UniGeneRn.112601

3D structure databases

SMRQ9WU82. Positions 19-44, 118-149, 127-682.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9WU82.

PTM databases

PhosphoSiteQ9WU82.

Genome annotation databases

EnsemblENSRNOT00000026016; ENSRNOP00000026016; ENSRNOG00000019139; Rattus norvegicus. [Genome view]
GeneID84353.
KEGGrno:84353.

Organism-specific databases

CTD84353.
RGD70487. Ctnnb1.

Phylogenomic databases

eggNOGroNOG10531.
HOVERGENQ9WU82.
InParanoidQ9WU82.

Gene expression databases

ArrayExpressQ9WU82.
GenevestigatorQ9WU82.
GermOnlineENSRNOG00000019139. Rattus norvegicus.

Family and domain databases

InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
Gene3DG3DSA:1.25.10.10. ARM-like. 1 hit.
PfamPF00514. Arm. 5 hits.
[Graphical view]
PRINTSPR01869. BCATNINFAMLY.
SMARTSM00185. ARM. 12 hits.
[Graphical view]
PROSITEPS50176. ARM_REPEAT. 9 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio616667.

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Entry information

Entry nameCTNB1_RAT
AccessionPrimary (citable) accession number: Q9WU82
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: January 19, 2010
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents