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Q02248

- CTNB1_MOUSE

UniProt

Q02248 - CTNB1_MOUSE

Protein

Catenin beta-1

Gene

Ctnnb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    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 binding Source: UniProtKB
    8. protein kinase binding Source: RefGenome
    9. protein phosphatase binding Source: UniProtKB
    10. repressing transcription factor binding Source: UniProtKB
    11. sequence-specific DNA binding transcription factor activity Source: MGI
    12. structural molecule activity Source: RefGenome
    13. transcription coactivator activity Source: UniProtKB
    14. transcription factor binding Source: MGI
    15. transcription regulatory region DNA binding Source: MGI

    GO - Biological processi

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

    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.

    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. fascia adherens Source: MGI
    22. intercalated disc Source: MGI
    23. lamellipodium Source: MGI
    24. lateral plasma membrane Source: MGI
    25. membrane Source: MGI
    26. microvillus membrane Source: MGI
    27. nucleus Source: BHF-UCL
    28. perinuclear region of cytoplasm Source: UniProtKB
    29. plasma membrane Source: UniProtKB
    30. protein-DNA complex Source: UniProtKB
    31. Scrib-APC-beta-catenin complex Source: BHF-UCL
    32. spindle pole Source: UniProtKB-SubCell
    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

    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

    ArrayExpressiQ02248.
    BgeeiQ02248.
    CleanExiMM_CTNNB1.
    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 – 884
    Helixi90 – 989
    Helixi100 – 1023
    Helixi121 – 14121
    Turni145 – 1484
    Turni150 – 1523
    Helixi153 – 1608
    Beta strandi161 – 1644
    Beta strandi166 – 1683
    Helixi169 – 1713
    Helixi172 – 1787
    Helixi182 – 1898
    Beta strandi192 – 1943
    Helixi195 – 20410
    Helixi208 – 22114
    Helixi225 – 2339
    Helixi236 – 2427
    Helixi243 – 2453
    Helixi249 – 26517
    Helixi269 – 2757
    Helixi278 – 2847
    Helixi285 – 2873
    Helixi291 – 30515
    Helixi309 – 3179
    Helixi320 – 33011
    Helixi334 – 34714
    Helixi353 – 3597
    Helixi362 – 3676
    Turni368 – 3714
    Helixi375 – 38915
    Helixi399 – 40810
    Helixi414 – 42815
    Helixi432 – 4409
    Helixi443 – 45412
    Helixi458 – 47114
    Beta strandi473 – 4753
    Helixi478 – 48710
    Helixi491 – 4966
    Helixi504 – 51714
    Helixi521 – 5233
    Helixi524 – 5296
    Helixi532 – 54716
    Helixi566 – 58015
    Helixi584 – 5929
    Helixi596 – 6027
    Helixi608 – 62114
    Helixi625 – 6339
    Turni634 – 6363
    Helixi637 – 6437
    Helixi649 – 66113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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, 99-665.
    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

    MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG    50
    NPEEEDVDTS QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP 100
    ETLDEGMQIP STQFDAAHPT NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT 150
    RAIPELTKLL NDEDQVVVNK AAVMVHQLSK KEASRHAIMR SPQMVSAIVR 200
    TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL VKMLGSPVDS 250
    VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC 300
    LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC 350
    SSNKPAIVEA GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG 400
    LLGTLVQLLG SDDINVVTCA AGILSNLTCN NYKNKMMVCQ VGGIEALVRT 450
    VLRAGDREDI TEPAICALRH LTSRHQEAEM AQNAVRLHYG LPVVVKLLHP 500
    PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL VRAHQDTQRR 550
    TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV 600
    QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG 650
    VATYAAAVLF RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI 700
    GAQGEALGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV 750
    DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L 781
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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, 99-665.
    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.

    Miscellaneous databases

    ChiTaRSi CTNNB1. mouse.
    EvolutionaryTracei Q02248.
    NextBioi 281106.
    PMAP-CutDB Q02248.
    PROi Q02248.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02248.
    Bgeei Q02248.
    CleanExi MM_CTNNB1.
    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

    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: October 1, 2014
    This is version 172 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