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Q02248

- CTNB1_MOUSE

UniProt

Q02248 - CTNB1_MOUSE

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Protein

Catenin beta-1

Gene

Ctnnb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. alpha-catenin binding Source: dictyBase
  2. cadherin binding Source: MGI
  3. chromatin binding Source: MGI
  4. DNA binding Source: MGI
  5. double-stranded DNA binding Source: MGI
  6. nuclear hormone receptor binding Source: UniProtKB
  7. protein kinase binding Source: RefGenome
  8. protein phosphatase binding Source: UniProtKB
  9. repressing transcription factor binding Source: UniProtKB
  10. sequence-specific DNA binding transcription factor activity Source: MGI
  11. structural molecule activity Source: RefGenome
  12. transcription coactivator activity Source: UniProtKB
  13. transcription factor binding Source: MGI
  14. transcription regulatory region DNA binding Source: MGI

GO - Biological processi

  1. adherens junction assembly Source: UniProtKB
  2. adherens junction organization Source: MGI
  3. anterior/posterior axis specification Source: MGI
  4. bone resorption Source: MGI
  5. branching involved in ureteric bud morphogenesis Source: MGI
  6. canonical Wnt signaling pathway Source: MGI
  7. canonical Wnt signaling pathway involved in negative regulation of apoptotic process Source: Ensembl
  8. canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation Source: BHF-UCL
  9. canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition Source: UniProtKB
  10. cardiac muscle cell proliferation Source: DFLAT
  11. cardiac vascular smooth muscle cell differentiation Source: DFLAT
  12. cell adhesion Source: UniProtKB
  13. cell differentiation Source: MGI
  14. cell fate determination Source: MGI
  15. cell fate specification Source: MGI
  16. cell-matrix adhesion Source: MGI
  17. cell maturation Source: MGI
  18. cell morphogenesis involved in differentiation Source: MGI
  19. cell proliferation Source: MGI
  20. cellular process Source: MGI
  21. cellular protein localization Source: MGI
  22. cellular response to growth factor stimulus Source: UniProtKB
  23. cellular response to indole-3-methanol Source: UniProtKB
  24. cellular response to mechanical stimulus Source: Ensembl
  25. cellular response to organic cyclic compound Source: MGI
  26. central nervous system vasculogenesis Source: MGI
  27. coronary artery morphogenesis Source: DFLAT
  28. cytoskeletal anchoring at plasma membrane Source: RefGenome
  29. dorsal/ventral axis specification Source: MGI
  30. dorsal/ventral pattern formation Source: MGI
  31. ectoderm development Source: MGI
  32. embryonic axis specification Source: MGI
  33. embryonic digit morphogenesis Source: MGI
  34. embryonic foregut morphogenesis Source: MGI
  35. embryonic forelimb morphogenesis Source: MGI
  36. embryonic heart tube development Source: MGI
  37. embryonic hindlimb morphogenesis Source: MGI
  38. embryonic skeletal limb joint morphogenesis Source: BHF-UCL
  39. endodermal cell fate commitment Source: MGI
  40. endoderm formation Source: MGI
  41. endothelial tube morphogenesis Source: UniProtKB
  42. epicardium-derived cardiac vascular smooth muscle cell differentiation Source: DFLAT
  43. epithelial cell differentiation involved in prostate gland development Source: MGI
  44. epithelial tube branching involved in lung morphogenesis Source: MGI
  45. forebrain development Source: MGI
  46. fungiform papilla formation Source: MGI
  47. gastrulation with mouth forming second Source: MGI
  48. genitalia morphogenesis Source: MGI
  49. glial cell fate determination Source: MGI
  50. hair cycle process Source: MGI
  51. hair follicle morphogenesis Source: MGI
  52. hair follicle placode formation Source: MGI
  53. heart development Source: MGI
  54. hemopoiesis Source: MGI
  55. hindbrain development Source: RefGenome
  56. in utero embryonic development Source: MGI
  57. kidney development Source: MGI
  58. layer formation in cerebral cortex Source: MGI
  59. lens morphogenesis in camera-type eye Source: MGI
  60. limb development Source: MGI
  61. liver development Source: RefGenome
  62. lung-associated mesenchyme development Source: MGI
  63. lung cell differentiation Source: MGI
  64. lung development Source: MGI
  65. lung induction Source: MGI
  66. male genitalia development Source: MGI
  67. mesenchymal cell proliferation involved in lung development Source: MGI
  68. mesenchymal to epithelial transition involved in metanephros morphogenesis Source: MGI
  69. mesenchyme development Source: DFLAT
  70. mesenchyme morphogenesis Source: DFLAT
  71. metanephros morphogenesis Source: MGI
  72. midgut development Source: Ensembl
  73. morphogenesis of embryonic epithelium Source: MGI
  74. myoblast differentiation Source: Ensembl
  75. negative regulation of apoptotic signaling pathway Source: MGI
  76. negative regulation of cell differentiation Source: MGI
  77. negative regulation of cell proliferation Source: UniProtKB
  78. negative regulation of chondrocyte differentiation Source: MGI
  79. negative regulation of heart induction by canonical Wnt signaling pathway Source: RefGenome
  80. negative regulation of neuron death Source: MGI
  81. negative regulation of oligodendrocyte differentiation Source: MGI
  82. negative regulation of osteoclast differentiation Source: MGI
  83. negative regulation of protein sumoylation Source: UniProtKB
  84. negative regulation of transcription, DNA-templated Source: MGI
  85. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  86. nephron tubule formation Source: MGI
  87. neural plate development Source: MGI
  88. neuron migration Source: MGI
  89. odontogenesis of dentin-containing tooth Source: MGI
  90. oocyte development Source: MGI
  91. organ development Source: MGI
  92. osteoclast differentiation Source: MGI
  93. oviduct development Source: MGI
  94. pancreas development Source: MGI
  95. patterning of blood vessels Source: MGI
  96. positive regulation of apoptotic process Source: UniProtKB
  97. positive regulation of branching involved in lung morphogenesis Source: MGI
  98. positive regulation of cell proliferation Source: MGI
  99. positive regulation of determination of dorsal identity Source: MGI
  100. positive regulation of endothelial cell differentiation Source: MGI
  101. positive regulation of epithelial cell differentiation Source: MGI
  102. positive regulation of epithelial cell proliferation involved in prostate gland development Source: MGI
  103. positive regulation of epithelial to mesenchymal transition Source: DFLAT
  104. positive regulation of fibroblast growth factor receptor signaling pathway Source: MGI
  105. positive regulation of gene expression Source: MGI
  106. positive regulation of heparan sulfate proteoglycan biosynthetic process Source: UniProtKB
  107. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  108. positive regulation of MAPK cascade Source: MGI
  109. positive regulation of mesenchymal cell proliferation Source: MGI
  110. positive regulation of neuroblast proliferation Source: MGI
  111. positive regulation of osteoblast differentiation Source: MGI
  112. positive regulation of transcription, DNA-templated Source: UniProtKB
  113. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  114. protein heterooligomerization Source: Ensembl
  115. protein localization to cell surface Source: UniProtKB
  116. proximal/distal pattern formation Source: MGI
  117. regulation of apoptotic process Source: MGI
  118. regulation of calcium ion import Source: UniProtKB
  119. regulation of cell differentiation Source: MGI
  120. regulation of cell proliferation Source: MGI
  121. regulation of centriole-centriole cohesion Source: UniProtKB
  122. regulation of centromeric sister chromatid cohesion Source: BHF-UCL
  123. regulation of epithelial cell differentiation Source: MGI
  124. regulation of gene expression Source: MGI
  125. regulation of myelination Source: MGI
  126. regulation of nephron tubule epithelial cell differentiation Source: UniProtKB
  127. regulation of osteoblast differentiation Source: MGI
  128. regulation of osteoclast differentiation Source: MGI
  129. regulation of protein localization to cell surface Source: UniProtKB
  130. regulation of secondary heart field cardioblast proliferation Source: MGI
  131. regulation of smooth muscle cell proliferation Source: UniProtKB
  132. regulation of T cell proliferation Source: MGI
  133. regulation of transcription, DNA-templated Source: MGI
  134. regulation of transcription from RNA polymerase II promoter Source: MGI
  135. renal inner medulla development Source: MGI
  136. renal outer medulla development Source: MGI
  137. renal system development Source: MGI
  138. renal vesicle formation Source: MGI
  139. response to cadmium ion Source: Ensembl
  140. response to cytokine Source: Ensembl
  141. response to drug Source: Ensembl
  142. response to estradiol Source: UniProtKB
  143. response to estrogen Source: RefGenome
  144. Schwann cell proliferation Source: RefGenome
  145. single organismal cell-cell adhesion Source: MGI
  146. skeletal system development Source: MGI
  147. skin development Source: MGI
  148. smooth muscle cell differentiation Source: MGI
  149. synapse organization Source: MGI
  150. synaptic transmission Source: MGI
  151. synaptic vesicle transport Source: MGI
  152. T cell differentiation Source: MGI
  153. T cell differentiation in thymus Source: MGI
  154. thymus development Source: MGI
  155. trachea formation Source: MGI
  156. trachea morphogenesis Source: MGI
  157. transcription, DNA-templated Source: UniProtKB-KW
  158. vasculature development Source: MGI
  159. vasculogenesis Source: MGI
  160. ventricular compact myocardium morphogenesis Source: DFLAT
  161. Wnt signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell adhesion, Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_207044. TCF dependent signaling in response to WNT.
REACT_212869. Apoptotic cleavage of cell adhesion proteins.
REACT_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_218396. Beta-catenin phosphorylation cascade.
REACT_219771. deactivation of the beta-catenin transactivating complex.
REACT_221970. Ca2+ pathway.
REACT_223626. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_230395. Adherens junctions interactions.
REACT_234076. S37 mutants of beta-catenin aren't phosphorylated.
REACT_248000. S45 mutants of beta-catenin aren't phosphorylated.
REACT_258576. T41 mutants of beta-catenin aren't phosphorylated.
REACT_258600. CDO in myogenesis.
REACT_259776. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
REACT_260752. S33 mutants of beta-catenin aren't phosphorylated.
REACT_261276. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_261840. VEGFR2 mediated vascular permeability.

Names & Taxonomyi

Protein namesi
Recommended name:
Catenin beta-1
Alternative name(s):
Beta-catenin
Gene namesi
Name:Ctnnb1
Synonyms:Catnb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:88276. Ctnnb1.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeleton. Nucleus. Cell junctionadherens junction. 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 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).By similarity

GO - Cellular componenti

  1. adherens junction Source: MGI
  2. apical junction complex Source: MGI
  3. apical part of cell Source: MGI
  4. basolateral plasma membrane Source: MGI
  5. beta-catenin destruction complex Source: UniProtKB
  6. beta-catenin-TCF7L2 complex Source: UniProtKB
  7. catenin complex Source: UniProtKB
  8. catenin-TCF7L2 complex Source: BHF-UCL
  9. cell-cell adherens junction Source: MGI
  10. cell-cell junction Source: MGI
  11. cell cortex Source: UniProtKB
  12. cell junction Source: UniProtKB
  13. cell periphery Source: BHF-UCL
  14. cell projection membrane Source: MGI
  15. centrosome Source: BHF-UCL
  16. cytoplasm Source: MGI
  17. cytoplasmic side of plasma membrane Source: RefGenome
  18. cytosol Source: MGI
  19. dendritic shaft Source: RefGenome
  20. desmosome Source: RefGenome
  21. extracellular vesicular exosome Source: Ensembl
  22. fascia adherens Source: MGI
  23. intercalated disc Source: MGI
  24. lamellipodium Source: MGI
  25. lateral plasma membrane Source: MGI
  26. membrane Source: MGI
  27. microvillus membrane Source: MGI
  28. nucleus Source: BHF-UCL
  29. perinuclear region of cytoplasm Source: UniProtKB
  30. plasma membrane Source: UniProtKB
  31. protein-DNA complex Source: UniProtKB
  32. Scrib-APC-beta-catenin complex Source: BHF-UCL
  33. synapse Source: RefGenome
  34. tight junction Source: MGI
  35. transcription factor complex Source: MGI
  36. Z disc Source: MGI
  37. zonula adherens Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81M → P: Loss of interaction with VCL. 1 Publication
Mutagenesisi33 – 331S → A: Abolished HIPK2-mediated proteasomal degradation. 1 Publication
Mutagenesisi37 – 371S → A: Abolished HIPK2-mediated proteasomal degradation. 1 Publication
Mutagenesisi552 – 5521S → A: Abolishes AMPK-mediated phosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 781780Catenin beta-1PRO_0000064272Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei23 – 231Phosphoserine; by GSK3-betaBy similarity
Modified residuei29 – 291Phosphoserine; by GSK3-betaBy similarity
Modified residuei33 – 331Phosphoserine; by GSK3-beta and HIPK21 Publication
Modified residuei37 – 371Phosphoserine; by GSK3-beta and HIPK21 Publication
Modified residuei41 – 411Phosphothreonine; by GSK3-betaBy similarity
Modified residuei45 – 451PhosphoserineBy similarity
Modified residuei64 – 641Phosphotyrosine; by PTK6By similarity
Modified residuei86 – 861Phosphotyrosine; by CSKBy similarity
Modified residuei142 – 1421Phosphotyrosine; by FYN and PTK61 Publication
Modified residuei191 – 1911Phosphoserine; alternate1 Publication
Modified residuei191 – 1911Phosphoserine; by CDK5; alternateBy similarity
Modified residuei246 – 2461Phosphoserine; by CDK5By similarity
Modified residuei331 – 3311PhosphotyrosineBy similarity
Modified residuei551 – 5511PhosphothreonineBy similarity
Modified residuei552 – 5521Phosphoserine; by AMPK2 Publications
Modified residuei556 – 5561PhosphothreonineBy similarity
Modified residuei619 – 6191S-nitrosocysteine1 Publication
Modified residuei654 – 6541PhosphotyrosineBy similarity
Modified residuei675 – 6751Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding (By similarity). 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).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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

MaxQBiQ02248.
PaxDbiQ02248.
PRIDEiQ02248.

PTM databases

PhosphoSiteiQ02248.

Miscellaneous databases

PMAP-CutDBQ02248.

Expressioni

Gene expression databases

BgeeiQ02248.
CleanExiMM_CTNNB1.
ExpressionAtlasiQ02248. baseline and differential.
GenevestigatoriQ02248.

Interactioni

Subunit structurei

Two separate complex-associated pools are found in the cytoplasm. The majority is present as component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1 and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. 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 RAPGEF2. 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 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. 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/CDH3.20 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APCP250548EBI-397872,EBI-727707From a different organism.
AXIN1O151695EBI-397872,EBI-710484From a different organism.
Cdh1P0980313EBI-397872,EBI-984420
CrebbpP454813EBI-397872,EBI-296306
Ctnna1P262312EBI-397872,EBI-647895
CTNNBIP1Q9NSA37EBI-397872,EBI-747082From a different organism.
Gsk3bQ9WV602EBI-397872,EBI-400793
HttP428593EBI-397872,EBI-5327353
Lef1P277826EBI-397872,EBI-984464
Prop1P974582EBI-397872,EBI-937831
RAPGEF2F1MSG62EBI-397872,EBI-6927068From a different organism.
RelaQ042075EBI-397872,EBI-644400
Tax1bp3Q9DBG96EBI-397872,EBI-1161647

Protein-protein interaction databases

BioGridi198512. 70 interactions.
DIPiDIP-31560N.
IntActiQ02248. 58 interactions.
MINTiMINT-103426.

Structurei

Secondary structure

1
781
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi85 – 884Combined sources
Helixi90 – 989Combined sources
Helixi100 – 1023Combined sources
Helixi121 – 14121Combined sources
Turni145 – 1484Combined sources
Turni150 – 1523Combined sources
Helixi153 – 1608Combined sources
Beta strandi161 – 1644Combined sources
Beta strandi166 – 1683Combined sources
Helixi169 – 1713Combined sources
Helixi172 – 1787Combined sources
Helixi182 – 1898Combined sources
Beta strandi192 – 1943Combined sources
Helixi195 – 20410Combined sources
Helixi208 – 22114Combined sources
Helixi225 – 2339Combined sources
Helixi236 – 2427Combined sources
Helixi243 – 2453Combined sources
Helixi249 – 26517Combined sources
Helixi269 – 2757Combined sources
Helixi278 – 2847Combined sources
Helixi285 – 2873Combined sources
Helixi291 – 30515Combined sources
Helixi309 – 3179Combined sources
Helixi320 – 33011Combined sources
Helixi334 – 34714Combined sources
Helixi353 – 3597Combined sources
Helixi362 – 3676Combined sources
Turni368 – 3714Combined sources
Helixi375 – 38915Combined sources
Helixi399 – 40810Combined sources
Helixi414 – 42815Combined sources
Helixi432 – 4409Combined sources
Helixi443 – 45412Combined sources
Helixi458 – 47114Combined sources
Beta strandi473 – 4753Combined sources
Helixi478 – 48710Combined sources
Helixi491 – 4966Combined sources
Helixi504 – 51714Combined sources
Helixi521 – 5233Combined sources
Helixi524 – 5296Combined sources
Helixi532 – 54716Combined sources
Helixi566 – 58015Combined sources
Helixi584 – 5929Combined sources
Helixi596 – 6027Combined sources
Helixi608 – 62114Combined sources
Helixi625 – 6339Combined sources
Turni634 – 6363Combined sources
Helixi637 – 6437Combined sources
Helixi649 – 66113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DOWX-ray1.80B118-149[»]
1I7WX-ray2.00A/C134-671[»]
1I7XX-ray3.00A/C134-671[»]
1JPPX-ray3.10A/B134-671[»]
1M1EX-ray2.10A134-671[»]
1V18X-ray2.10A134-671[»]
2BCTX-ray2.90A150-665[»]
3BCTX-ray2.10A193-661[»]
3OUWX-ray2.91A134-671[»]
3OUXX-ray2.40A134-671[»]
4EV8X-ray1.90A134-671[»]
4EV9X-ray2.10A134-671[»]
4EVAX-ray2.00A/C134-671[»]
4EVPX-ray2.26A134-671[»]
4EVTX-ray2.34A134-671[»]
4ONSX-ray2.80B/D78-151[»]
DisProtiDP00341.
ProteinModelPortaliQ02248.
SMRiQ02248. Positions 19-44, 84-665.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02248.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati151 – 19141ARM 1Add
BLAST
Repeati193 – 23442ARM 2Add
BLAST
Repeati235 – 27642ARM 3Add
BLAST
Repeati277 – 31842ARM 4Add
BLAST
Repeati319 – 36042ARM 5Add
BLAST
Repeati361 – 38929ARM 6Add
BLAST
Repeati400 – 44142ARM 7Add
BLAST
Repeati442 – 48443ARM 8Add
BLAST
Repeati489 – 53042ARM 9Add
BLAST
Repeati531 – 57141ARM 10Add
BLAST
Repeati594 – 63643ARM 11Add
BLAST
Repeati637 – 66630ARM 12Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2322Interaction with VCLAdd
BLAST
Regioni156 – 17823Interaction with BCL9By similarityAdd
BLAST
Regioni772 – 78110Interaction with SCRIB

Sequence similaritiesi

Belongs to the beta-catenin family.Curated
Contains 12 ARM repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG297695.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
InParanoidiQ02248.
KOiK02105.
OMAiRESHNRA.
OrthoDBiEOG7X9G6B.
PhylomeDBiQ02248.
TreeFamiTF317997.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamiPF00514. Arm. 4 hits.
[Graphical view]
PRINTSiPR01869. BCATNINFAMLY.
SMARTiSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02248-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG
60 70 80 90 100
NPEEEDVDTS 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
GAQGEALGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV
760 770 780
DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L
Length:781
Mass (Da):85,471
Last modified:July 1, 1993 - v1
Checksum:iD708F170A3FBED6E
GO

Sequence cautioni

The sequence AAH06739.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti371 – 3711T → I in BAB31250. (PubMed:16141072)Curated
Sequence conflicti478 – 4781A → T in BAB31250. (PubMed:16141072)Curated
Sequence conflicti487 – 4871L → F in BAB31250. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90364 mRNA. Translation: AAA37280.1.
AK035311 mRNA. Translation: BAC29027.1.
AK018515 mRNA. Translation: BAB31250.1.
BC006739 mRNA. Translation: AAH06739.1. Different initiation.
BC048153 mRNA. Translation: AAH48153.1.
BC053065 mRNA. Translation: AAH53065.1.
CCDSiCCDS23630.1.
PIRiS35091.
RefSeqiNP_001159374.1. NM_001165902.1.
NP_031640.1. NM_007614.3.
XP_006511990.1. XM_006511927.1.
UniGeneiMm.291928.

Genome annotation databases

EnsembliENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932.
ENSMUST00000178812; ENSMUSP00000136294; ENSMUSG00000006932.
GeneIDi12387.
KEGGimmu:12387.
UCSCiuc009scu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90364 mRNA. Translation: AAA37280.1 .
AK035311 mRNA. Translation: BAC29027.1 .
AK018515 mRNA. Translation: BAB31250.1 .
BC006739 mRNA. Translation: AAH06739.1 . Different initiation.
BC048153 mRNA. Translation: AAH48153.1 .
BC053065 mRNA. Translation: AAH53065.1 .
CCDSi CCDS23630.1.
PIRi S35091.
RefSeqi NP_001159374.1. NM_001165902.1.
NP_031640.1. NM_007614.3.
XP_006511990.1. XM_006511927.1.
UniGenei Mm.291928.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DOW X-ray 1.80 B 118-149 [» ]
1I7W X-ray 2.00 A/C 134-671 [» ]
1I7X X-ray 3.00 A/C 134-671 [» ]
1JPP X-ray 3.10 A/B 134-671 [» ]
1M1E X-ray 2.10 A 134-671 [» ]
1V18 X-ray 2.10 A 134-671 [» ]
2BCT X-ray 2.90 A 150-665 [» ]
3BCT X-ray 2.10 A 193-661 [» ]
3OUW X-ray 2.91 A 134-671 [» ]
3OUX X-ray 2.40 A 134-671 [» ]
4EV8 X-ray 1.90 A 134-671 [» ]
4EV9 X-ray 2.10 A 134-671 [» ]
4EVA X-ray 2.00 A/C 134-671 [» ]
4EVP X-ray 2.26 A 134-671 [» ]
4EVT X-ray 2.34 A 134-671 [» ]
4ONS X-ray 2.80 B/D 78-151 [» ]
DisProti DP00341.
ProteinModelPortali Q02248.
SMRi Q02248. Positions 19-44, 84-665.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198512. 70 interactions.
DIPi DIP-31560N.
IntActi Q02248. 58 interactions.
MINTi MINT-103426.

PTM databases

PhosphoSitei Q02248.

Proteomic databases

MaxQBi Q02248.
PaxDbi Q02248.
PRIDEi Q02248.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000007130 ; ENSMUSP00000007130 ; ENSMUSG00000006932 .
ENSMUST00000178812 ; ENSMUSP00000136294 ; ENSMUSG00000006932 .
GeneIDi 12387.
KEGGi mmu:12387.
UCSCi uc009scu.2. mouse.

Organism-specific databases

CTDi 1499.
MGIi MGI:88276. Ctnnb1.

Phylogenomic databases

eggNOGi NOG297695.
GeneTreei ENSGT00730000110821.
HOGENOMi HOG000230958.
HOVERGENi HBG000919.
InParanoidi Q02248.
KOi K02105.
OMAi RESHNRA.
OrthoDBi EOG7X9G6B.
PhylomeDBi Q02248.
TreeFami TF317997.

Enzyme and pathway databases

Reactomei REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_207044. TCF dependent signaling in response to WNT.
REACT_212869. Apoptotic cleavage of cell adhesion proteins.
REACT_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_218396. Beta-catenin phosphorylation cascade.
REACT_219771. deactivation of the beta-catenin transactivating complex.
REACT_221970. Ca2+ pathway.
REACT_223626. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_230395. Adherens junctions interactions.
REACT_234076. S37 mutants of beta-catenin aren't phosphorylated.
REACT_248000. S45 mutants of beta-catenin aren't phosphorylated.
REACT_258576. T41 mutants of beta-catenin aren't phosphorylated.
REACT_258600. CDO in myogenesis.
REACT_259776. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
REACT_260752. S33 mutants of beta-catenin aren't phosphorylated.
REACT_261276. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_261840. VEGFR2 mediated vascular permeability.

Miscellaneous databases

ChiTaRSi Ctnnb1. mouse.
EvolutionaryTracei Q02248.
NextBioi 281106.
PMAP-CutDB Q02248.
PROi Q02248.
SOURCEi Search...

Gene expression databases

Bgeei Q02248.
CleanExi MM_CTNNB1.
ExpressionAtlasi Q02248. baseline and differential.
Genevestigatori Q02248.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view ]
Pfami PF00514. Arm. 4 hits.
[Graphical view ]
PRINTSi PR01869. BCATNINFAMLY.
SMARTi SM00185. ARM. 12 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS50176. ARM_REPEAT. 9 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Plakoglobin and beta-catenin: distinct but closely related."
    Butz S., Stappert J., Weissig H., Kemler R.
    Science 257:1142-1144(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Colon and Urinary bladder.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain and Mammary cancer.
  4. "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion."
    Butz S., Kemler R.
    FEBS Lett. 355:195-200(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
  5. "The Xenopus Wnt effector XTcf-3 interacts with Groucho-related transcriptional repressors."
    Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H., Moerer P., van de Wetering M., Destree O., Clevers H.
    Nature 395:608-612(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TCF7; TCF7L1; TCF7L2 AND LEF1.
  6. "A GSK3beta phosphorylation site in axin modulates interaction with beta-catenin and Tcf-mediated gene expression."
    Jho E., Lomvardas S., Costantini F.
    Biochem. Biophys. Res. Commun. 266:28-35(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXIN1.
  7. "MAGI-1 interacts with beta-catenin and is associated with cell-cell adhesion structures."
    Dobrosotskaya I.Y., James G.L.
    Biochem. Biophys. Res. Commun. 270:903-909(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAIAP1.
  8. "AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein mediating strong cell-cell adhesion."
    Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J., Colpaert C., Bruyneel E., Mareel M., van Roy F.
    J. Cell Sci. 114:3177-3188(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTNNA3.
  9. "The PDZ protein tax-interacting protein-1 inhibits beta-catenin transcriptional activity and growth of colorectal cancer cells."
    Kanamori M., Sandy P., Marzinotto S., Benetti R., Kai C., Hayashizaki Y., Schneider C., Suzuki H.
    J. Biol. Chem. 278:38758-38764(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAX1BP3.
  10. "p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction."
    Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N., Garcia de Herreros A., Dunach M.
    Mol. Cell. Biol. 23:2287-2297(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-142 BY FYN.
  11. "RORalpha coordinates reciprocal signaling in cerebellar development through sonic hedgehog and calcium-dependent pathways."
    Gold D.A., Baek S.H., Schork N.J., Rose D.W., Larsen D.D., Sachs B.D., Rosenfeld M.G., Hamilton B.A.
    Neuron 40:1119-1131(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RORA.
  12. "Cyclin-dependent kinase 2 regulates the interaction of Axin with beta-catenin."
    Kim S.I., Park C.S., Lee M.S., Kwon M.S., Jho E.H., Song W.K.
    Biochem. Biophys. Res. Commun. 317:478-483(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXIN1.
  13. "Deconstructing the cadherin-catenin-actin complex."
    Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.
    Cell 123:889-901(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
  14. "Crystal structure of a beta-catenin/BCL9/Tcf4 complex."
    Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.
    Mol. Cell 24:293-300(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL9L.
  15. "The Kruppel-like zinc finger protein Glis2 functions as a negative modulator of the Wnt/beta-catenin signaling pathway."
    Kim Y.-S., Kang H.S., Jetten A.M.
    FEBS Lett. 581:858-864(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GLIS2, SUBCELLULAR LOCATION.
  16. "The intercalated disc protein, mXin{alpha}, is capable of interacting with beta-catenin and bundling actin filaments."
    Choi S., Gustafson-Wagner E.A., Wang Q., Harlan S.M., Sinn H.W., Lin J.L.-C., Lin J.J.-C.
    J. Biol. Chem. 282:36024-36036(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XIRP1.
  17. "Role of GAC63 in transcriptional activation mediated by beta-catenin."
    Chen Y.H., Yang C.K., Xia M., Ou C.Y., Stallcup M.R.
    Nucleic Acids Res. 35:2084-2092(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC30A9.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-552 AND SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt."
    Abe K., Takeichi M.
    Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
  20. "The kinase TNIK is an essential activator of Wnt target genes."
    Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., Heck A.J., Clevers H.
    EMBO J. 28:3329-3340(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TCF7L2 AND TNIK.
  21. "Scribble interacts with beta-catenin to localize synaptic vesicles to synapses."
    Sun Y., Aiga M., Yoshida E., Humbert P.O., Bamji S.X.
    Mol. Biol. Cell 20:3390-3400(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCRIB.
  22. "Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-catenin for phosphorylation and proteasomal degradation."
    Kim E.-A., Kim J.E., Sung K.S., Choi D.W., Lee B.J., Choi C.Y.
    Biochem. Biophys. Res. Commun. 394:966-971(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2, MUTAGENESIS OF SER-33 AND SER-37.
  23. "AMP-activated protein kinase (AMPK) cross-talks with canonical Wnt signaling via phosphorylation of beta-catenin at Ser 552."
    Zhao J., Yue W., Zhu M.J., Sreejayan N., Du M.
    Biochem. Biophys. Res. Commun. 395:146-151(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-552, MUTAGENESIS OF SER-552.
  24. "The TRPV4 channel contributes to intercellular junction formation in keratinocytes."
    Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.
    J. Biol. Chem. 285:18749-18758(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRPV4 AND CDH1.
  25. "Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin."
    Peng X., Cuff L.E., Lawton C.D., DeMali K.A.
    J. Cell Sci. 123:567-577(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VCL, MUTAGENESIS OF MET-8.
  26. "Regulation of beta-catenin signaling in the Wnt pathway."
    Kikuchi A.
    Biochem. Biophys. Res. Commun. 268:243-248(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  27. "S-nitrosylation of beta-catenin by eNOS-derived NO promotes VEGF-induced endothelial cell permeability."
    Thibeault S., Rautureau Y., Oubaha M., Faubert D., Wilkes B.C., Delisle C., Gratton J.P.
    Mol. Cell 39:468-476(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION AT CYS-619, SUBCELLULAR LOCATION.
  28. "Three-dimensional structure of the armadillo repeat region of beta-catenin."
    Huber A.H., Nelson W.J., Weis W.I.
    Cell 90:871-882(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 150-665.
  29. "Structure of the dimerization and beta-catenin-binding region of alpha-catenin."
    Pokutta S., Weis W.I.
    Mol. Cell 5:533-543(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 118-149 IN COMPLEX WITH CTNNA1.
  30. "The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin."
    Huber A.H., Weis W.I.
    Cell 105:391-402(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 AND 3.0 ANGSTROMS) OF 134-671 IN COMPLEX WITH PHOSPHORYLATED AND UNPHOSPHORYLATED CDH1.
  31. "Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex."
    Eklof Spink K., Fridman S.G., Weis W.I.
    EMBO J. 20:6203-6212(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH APC.
  32. "ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules."
    Daniels D.L., Weis W.I.
    Mol. Cell 10:573-584(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH CTNNBIP1, INTERACTION WITH EP300.

Entry informationi

Entry nameiCTNB1_MOUSE
AccessioniPrimary (citable) accession number: Q02248
Secondary accession number(s): Q922W1, Q9D335
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 26, 2014
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3