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Q0VCX4 (CTNB1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catenin beta-1
Alternative name(s):
Beta-catenin
Gene names
Name:CTNNB1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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 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. Ref.3

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Nucleus By similarity. Cell junctionadherens junction By similarity. Cell junction By similarity. Cell membrane By similarity. 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 and MUC1 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.

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
Wnt signaling pathway
   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 Biological aspect of Ancestor. Source: RefGenome

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-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

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

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 Biological aspect of Ancestor. Source: RefGenome

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

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 Biological aspect of Ancestor. Source: RefGenome

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 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 drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from sequence or structural similarity. Source: UniProtKB

response to estrogen

Inferred from Biological aspect of Ancestor. Source: RefGenome

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 sequence or structural similarity. Source: UniProtKB

cell-cell junction

Inferred from sequence or structural similarity. Source: UniProtKB

cell-substrate adherens junction

Inferred from electronic annotation. Source: Ensembl

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 sequence or structural similarity. Source: UniProtKB

dendritic shaft

Inferred from Biological aspect of Ancestor. Source: RefGenome

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 sequence or structural similarity. Source: UniProtKB

microvillus membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

protein-DNA complex

Inferred from sequence or structural similarity. Source: UniProtKB

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from Biological aspect of Ancestor. Source: RefGenome

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 Biological aspect of Ancestor. Source: RefGenome

chromatin binding

Inferred from electronic annotation. Source: Ensembl

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

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_0000282881

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 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0VCX4 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 6148652F953F0723

FASTA78185,511
        10         20         30         40         50         60 
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTT 

        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 
GGMQALGLHL 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 GAQGEPLGYR QDDPSYRSFH 

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


L 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal skin.
[3]"Identification of a novel beta-catenin-interacting protein."
Kawajiri A., Itoh N., Fukata M., Nakagawa M., Yamaga M., Iwamatsu A., Kaibuchi K.
Biochem. Biophys. Res. Commun. 273:712-717(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAPGEF2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT030683 mRNA. Translation: ABS44999.1.
BC119949 mRNA. Translation: AAI19950.1.
RefSeqNP_001069609.1. NM_001076141.1.
XP_005222580.1. XM_005222523.1.
XP_005222581.1. XM_005222524.1.
XP_005222582.1. XM_005222525.1.
UniGeneBt.33687.

3D structure databases

ProteinModelPortalQ0VCX4.
SMRQ0VCX4. Positions 19-44, 142-691.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ0VCX4. 1 interaction.

Proteomic databases

PaxDbQ0VCX4.
PRIDEQ0VCX4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000021838; ENSBTAP00000021838; ENSBTAG00000016420.
GeneID539003.
KEGGbta:539003.

Organism-specific databases

CTD1499.

Phylogenomic databases

eggNOGNOG297695.
GeneTreeENSGT00730000110821.
HOGENOMHOG000230958.
HOVERGENHBG000919.
InParanoidQ0VCX4.
KOK02105.
OMAQLSQTRS.
OrthoDBEOG7X9G6B.
TreeFamTF317997.

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

NextBio20877720.

Entry information

Entry nameCTNB1_BOVIN
AccessionPrimary (citable) accession number: Q0VCX4
Secondary accession number(s): A7E3R2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: September 5, 2006
Last modified: April 16, 2014
This is version 76 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