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Q02248

- CTNB1_MOUSE

UniProt

Q02248 - CTNB1_MOUSE

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Protein
Catenin beta-1
Gene
Ctnnb1, Catnb
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.

GO - Molecular functioni

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

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.2 Publications

GO - Cellular componenti

  1. Scrib-APC-beta-catenin complex Source: BHF-UCL
  2. Z disc Source: MGI
  3. adherens junction Source: MGI
  4. apical junction complex Source: MGI
  5. apical part of cell Source: MGI
  6. basolateral plasma membrane Source: MGI
  7. beta-catenin destruction complex Source: UniProtKB
  8. beta-catenin-TCF7L2 complex Source: UniProtKB
  9. catenin complex Source: UniProtKB
  10. catenin-TCF7L2 complex Source: BHF-UCL
  11. cell cortex Source: UniProtKB
  12. cell junction Source: UniProtKB
  13. cell periphery Source: BHF-UCL
  14. cell projection membrane Source: MGI
  15. cell-cell adherens junction Source: MGI
  16. cell-cell junction Source: MGI
  17. centrosome Source: BHF-UCL
  18. cytoplasm Source: MGI
  19. cytoplasmic side of plasma membrane Source: RefGenome
  20. cytosol Source: MGI
  21. dendritic shaft Source: RefGenome
  22. desmosome Source: RefGenome
  23. fascia adherens Source: MGI
  24. intercalated disc Source: MGI
  25. lamellipodium Source: MGI
  26. lateral plasma membrane Source: MGI
  27. membrane Source: MGI
  28. microvillus membrane Source: MGI
  29. nucleus Source: BHF-UCL
  30. perinuclear region of cytoplasm Source: UniProtKB
  31. plasma membrane Source: UniProtKB
  32. protein-DNA complex Source: UniProtKB
  33. spindle pole Source: UniProtKB-SubCell
  34. synapse Source: RefGenome
  35. tight junction Source: MGI
  36. transcription factor complex 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 – 11Removed By similarity
Chaini2 – 781780Catenin beta-1
PRO_0000064272Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei23 – 231Phosphoserine; by GSK3-beta By similarity
Modified residuei29 – 291Phosphoserine; by GSK3-beta By similarity
Modified residuei33 – 331Phosphoserine; by GSK3-beta and HIPK21 Publication
Modified residuei37 – 371Phosphoserine; by GSK3-beta and HIPK21 Publication
Modified residuei41 – 411Phosphothreonine; by GSK3-beta By similarity
Modified residuei45 – 451Phosphoserine By similarity
Modified residuei64 – 641Phosphotyrosine; by PTK6 By similarity
Modified residuei86 – 861Phosphotyrosine; by CSK By similarity
Modified residuei142 – 1421Phosphotyrosine; by FYN and PTK61 Publication
Modified residuei191 – 1911Phosphoserine; alternate1 Publication
Modified residuei191 – 1911Phosphoserine; by CDK5; alternate By similarity
Modified residuei246 – 2461Phosphoserine; by CDK5 By similarity
Modified residuei331 – 3311Phosphotyrosine By similarity
Modified residuei551 – 5511Phosphothreonine By similarity
Modified residuei552 – 5521Phosphoserine; by AMPK2 Publications
Modified residuei556 – 5561Phosphothreonine By similarity
Modified residuei619 – 6191S-nitrosocysteine1 Publication
Modified residuei654 – 6541Phosphotyrosine By 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.3 Publications
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.3 Publications
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.

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/CDH3.17 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. 55 interactions.
MINTiMINT-103426.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ02248.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2322Interaction with VCL
Add
BLAST
Regioni156 – 17823Interaction with BCL9 By similarity
Add
BLAST
Regioni772 – 78110Interaction with SCRIB

Sequence similaritiesi

Belongs to the beta-catenin family.
Contains 12 ARM repeats.

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

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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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti371 – 3711T → I in BAB31250. 1 Publication
Sequence conflicti478 – 4781A → T in BAB31250. 1 Publication
Sequence conflicti487 – 4871L → F in BAB31250. 1 Publication

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. 55 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

« 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: September 3, 2014
This is version 171 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

Similar proteinsi