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Q9WU82 (CTNB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length781 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. 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 By similarity. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML By similarity.

Subunit structure

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 Interacts directly with AXIN1; the interaction is regulated by CK2 via BTRC and its subsequent degradation by the proteasome. Interacts directly with AXIN1;the interaction is regulated by CDK2 phosphorylation. 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. Interacts with XIRP1. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain) and with SLC30A9. Interacts with EMD. Interacts with SCRIB. Interacts with TNIK and TCF7L2. 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 NANOS1. Interacts with CDK2, NDRG2, NEK2 and CDK5. Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B. 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 RAPGEF2. Interacts with FAT1 (via the cytoplasmic domain). Interacts with RORA. May interact with P-cadherin/CDH3. Ref.3 Ref.4 Ref.5

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Nucleus. Cell junctionadherens junction By similarity. Cell junction By similarity. Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle pole 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. The majority of beta- catenin is localized to the cell membrane. In interphase, colocalizes with CROCC between CEP250 puncta at the proximal end of centrioles, and this localization is dependent on CROCC and CEP250. In mitosis, when NEK2 activity increases, it localizes to centrosomes at spindle poles independent of CROCC. Colocalizes with CDK5 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells. Colocalized with RAPGEF2 and TJP1 at cell-cell contacts By similarity. Ref.3

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. 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.

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.

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.

Sequence similarities

Belongs to the beta-catenin family.

Contains 12 ARM repeats.

Ontologies

Keywords
   Biological processCell adhesion
Transcription
Transcription regulation
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   DomainRepeat
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSchwann cell proliferation

Inferred from mutant phenotype PubMed 17941050. Source: RGD

T cell differentiation in thymus

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

adherens junction assembly

Inferred from sequence or structural similarity. Source: UniProtKB

anterior/posterior axis specification

Inferred from electronic annotation. Source: Ensembl

bone resorption

Inferred from electronic annotation. Source: Ensembl

branching involved in ureteric bud morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

canonical Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

canonical Wnt signaling pathway involved in negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: UniProtKB

cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

cell fate specification

Inferred from electronic annotation. Source: Ensembl

cell maturation

Inferred from electronic annotation. Source: Ensembl

cell-matrix adhesion

Inferred from Biological aspect of Ancestor. Source: RefGenome

cellular response to growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to indole-3-methanol

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to insulin-like growth factor stimulus

Inferred from mutant phenotype PubMed 20042609. Source: RGD

cellular response to mechanical stimulus

Inferred from direct assay PubMed 20042609. Source: RGD

central nervous system vasculogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoskeletal anchoring at plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

determination of dorsal/ventral asymmetry

Inferred from Biological aspect of Ancestor. Source: RefGenome

dorsal/ventral axis specification

Inferred from Biological aspect of Ancestor. Source: RefGenome

ectoderm development

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic axis specification

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic digit morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic foregut morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic forelimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic heart tube development

Inferred from electronic annotation. Source: Ensembl

embryonic hindlimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic limb morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic skeletal limb joint morphogenesis

Inferred from electronic annotation. Source: Ensembl

endodermal cell fate commitment

Inferred from Biological aspect of Ancestor. Source: RefGenome

endothelial tube morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

epithelial cell differentiation involved in prostate gland development

Inferred from electronic annotation. Source: Ensembl

epithelial tube branching involved in lung morphogenesis

Inferred from electronic annotation. Source: Ensembl

fungiform papilla formation

Inferred from electronic annotation. Source: Ensembl

gastrulation with mouth forming second

Inferred from Biological aspect of Ancestor. Source: RefGenome

genitalia morphogenesis

Inferred from electronic annotation. Source: Ensembl

glial cell fate determination

Inferred from Biological aspect of Ancestor. Source: RefGenome

hair follicle morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

hair follicle placode formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

hindbrain development

Inferred from Biological aspect of Ancestor. Source: RefGenome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

layer formation in cerebral cortex

Inferred from electronic annotation. Source: Ensembl

lens morphogenesis in camera-type eye

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from expression pattern PubMed 17236583. Source: RGD

lung cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

lung induction

Inferred from Biological aspect of Ancestor. Source: RefGenome

lung-associated mesenchyme development

Inferred from Biological aspect of Ancestor. Source: RefGenome

male genitalia development

Inferred from Biological aspect of Ancestor. Source: RefGenome

mesenchymal cell proliferation involved in lung development

Inferred from Biological aspect of Ancestor. Source: RefGenome

mesenchymal to epithelial transition involved in metanephros morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

midgut development

Inferred from expression pattern PubMed 17356920. Source: RGD

myoblast differentiation

Inferred from expression pattern PubMed 17222478. Source: RGD

negative regulation of apoptotic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of chondrocyte differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of heart induction by canonical Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of oligodendrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of osteoclast differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of protein sumoylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

nephron tubule formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

neural plate development

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

odontogenesis of dentin-containing tooth

Inferred from expression pattern PubMed 10681393. Source: RGD

oocyte development

Inferred from Biological aspect of Ancestor. Source: RefGenome

osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

oviduct development

Inferred from electronic annotation. Source: Ensembl

pancreas development

Inferred from Biological aspect of Ancestor. Source: RefGenome

patterning of blood vessels

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of MAPK cascade

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of branching involved in lung morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of determination of dorsal identity

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell proliferation involved in prostate gland development

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of fibroblast growth factor receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of heparan sulfate proteoglycan biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mesenchymal cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

protein heterooligomerization

Inferred from physical interaction PubMed 8834786. Source: RGD

protein localization to cell surface

Inferred from sequence or structural similarity. Source: UniProtKB

proximal/distal pattern formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of T cell proliferation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of calcium ion import

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of centriole-centriole cohesion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of centromeric sister chromatid cohesion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of myelination

Inferred from electronic annotation. Source: Ensembl

regulation of nephron tubule epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of protein localization to cell surface

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of secondary heart field cardioblast proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

renal inner medulla development

Inferred from Biological aspect of Ancestor. Source: RefGenome

renal outer medulla development

Inferred from Biological aspect of Ancestor. Source: RefGenome

renal vesicle formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to cadmium ion

Inferred from expression pattern PubMed 17136310. Source: RGD

response to cytokine

Inferred from direct assay PubMed 17888912. Source: RGD

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from sequence or structural similarity. Source: UniProtKB

response to estrogen

Inferred from direct assay PubMed 17170212. Source: RGD

response to hormone

Inferred from expression pattern PubMed 17708712. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 18174280. Source: RGD

single organismal cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

smooth muscle cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

synapse organization

Inferred from Biological aspect of Ancestor. Source: RefGenome

synaptic vesicle transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

thymus development

Inferred from Biological aspect of Ancestor. Source: RefGenome

tongue morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

trachea formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentScrib-APC-beta-catenin complex

Inferred from electronic annotation. Source: Ensembl

Z disc

Inferred from Biological aspect of Ancestor. Source: RefGenome

apical part of cell

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

beta-catenin destruction complex

Inferred from sequence or structural similarity. Source: UniProtKB

beta-catenin-TCF7L2 complex

Inferred from sequence or structural similarity. Source: UniProtKB

catenin complex

Inferred from sequence or structural similarity. Source: UniProtKB

cell cortex

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from sequence or structural similarity. Source: UniProtKB

cell periphery

Inferred from sequence or structural similarity. Source: BHF-UCL

cell-cell adherens junction

Inferred from direct assay PubMed 12533412PubMed 8834786. Source: RGD

cell-cell junction

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Inferred from direct assay PubMed 17170212. Source: RGD

dendritic shaft

Inferred from direct assay PubMed 12123611. Source: RGD

desmosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

fascia adherens

Inferred from Biological aspect of Ancestor. Source: RefGenome

lamellipodium

Inferred from Biological aspect of Ancestor. Source: RefGenome

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay Ref.3. Source: UniProtKB

microvillus membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay PubMed 17170212. Source: RGD

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 12533412. Source: RGD

protein-DNA complex

Inferred from sequence or structural similarity. Source: UniProtKB

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from direct assay PubMed 12123611. Source: RGD

transcription factor complex

Inferred from sequence or structural similarity. Source: UniProtKB

zonula adherens

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionalpha-catenin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

cadherin binding

Inferred from direct assay PubMed 12123611PubMed 9515794. Source: RGD

chromatin binding

Inferred from electronic annotation. Source: Ensembl

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

ionotropic glutamate receptor binding

Inferred from physical interaction PubMed 20007479. Source: RGD

nitric-oxide synthase binding

Inferred from physical interaction PubMed 15858215. Source: RGD

protein binding

Inferred from physical interaction PubMed 10753743Ref.4. Source: UniProtKB

protein complex binding

Inferred from physical interaction PubMed 15930126. Source: RGD

protein kinase binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

structural molecule activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 781780Catenin 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
Region2 – 2322Interaction with VCL By similarity
Region156 – 17823Interaction with BCL9 By similarity
Region772 – 78110Interaction with SCRIB By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue231Phosphoserine; by GSK3-beta By similarity
Modified residue291Phosphoserine; by GSK3-beta By similarity
Modified residue331Phosphoserine; by GSK3-beta and HIPK2 By similarity
Modified residue371Phosphoserine; by GSK3-beta and HIPK2 By similarity
Modified residue411Phosphothreonine; by GSK3-beta By similarity
Modified residue451Phosphoserine By similarity
Modified residue641Phosphotyrosine; by PTK6 By similarity
Modified residue861Phosphotyrosine; by CSK By similarity
Modified residue1421Phosphotyrosine; by FYN and PTK6 By similarity
Modified residue1911Phosphoserine; by CDK5 By similarity
Modified residue2461Phosphoserine; by CDK5 By similarity
Modified residue3311Phosphotyrosine By similarity
Modified residue5511Phosphothreonine By similarity
Modified residue5521Phosphoserine; by AMPK By similarity
Modified residue5561Phosphothreonine By similarity
Modified residue6191S-nitrosocysteine By similarity
Modified residue6541Phosphotyrosine; by CSK By similarity
Modified residue6751Phosphoserine Ref.6

Experimental info

Sequence conflict3681P → L in AAK85253. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9WU82 [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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Fischer 344.
[3]"The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway."
Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.
Genes Dev. 20:1933-1945(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH MACF1; APC; AXIN1 AND GSK3B.
[4]"The Fat1 cadherin integrates vascular smooth muscle cell growth and migration signals."
Hou R., Liu L., Anees S., Hiroyasu S., Sibinga N.E.
J. Cell Biol. 173:417-429(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FAT1.
[5]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHD8.
[6]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF121265 mRNA. Translation: AAD28504.1.
AF397179 Genomic DNA. Translation: AAK85253.1.
RefSeqNP_445809.2. NM_053357.2.
XP_006244196.1. XM_006244134.1.
XP_006244197.1. XM_006244135.1.
XP_006244198.1. XM_006244136.1.
XP_006244199.1. XM_006244137.1.
XP_006244200.1. XM_006244138.1.
UniGeneRn.112601.

3D structure databases

ProteinModelPortalQ9WU82.
SMRQ9WU82. Positions 19-44, 118-682.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249913. 11 interactions.
DIPDIP-37053N.
IntActQ9WU82. 4 interactions.
MINTMINT-87458.

PTM databases

PhosphoSiteQ9WU82.

Proteomic databases

PaxDbQ9WU82.
PRIDEQ9WU82.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026016; ENSRNOP00000026016; ENSRNOG00000019139.
GeneID84353.
KEGGrno:84353.
UCSCRGD:70487. rat.

Organism-specific databases

CTD1499.
RGD70487. Ctnnb1.

Phylogenomic databases

eggNOGNOG297695.
GeneTreeENSGT00730000110821.
HOGENOMHOG000230958.
HOVERGENHBG000919.
InParanoidQ9WU82.
KOK02105.
OrthoDBEOG7X9G6B.
PhylomeDBQ9WU82.
TreeFamTF317997.

Gene expression databases

GenevestigatorQ9WU82.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamPF00514. Arm. 4 hits.
[Graphical view]
PRINTSPR01869. BCATNINFAMLY.
SMARTSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50176. ARM_REPEAT. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio616667.
PROQ9WU82.

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: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families