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B6V8E6

- CTNB1_CANFA

UniProt

B6V8E6 - CTNB1_CANFA

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Protein

Catenin beta-1

Gene

CTNNB1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
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 the 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 activation of 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. chromatin binding Source: Ensembl
  2. double-stranded DNA binding Source: Ensembl
  3. sequence-specific DNA binding transcription factor activity Source: Ensembl
  4. transcription coactivator activity Source: UniProtKB
  5. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. adherens junction assembly Source: UniProtKB
  2. anterior/posterior axis specification Source: Ensembl
  3. bone resorption Source: Ensembl
  4. branching involved in ureteric bud morphogenesis Source: Ensembl
  5. canonical Wnt signaling pathway Source: UniProtKB
  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: Ensembl
  8. canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition Source: UniProtKB
  9. cell adhesion Source: UniProtKB
  10. cell fate specification Source: Ensembl
  11. cell-matrix adhesion Source: Ensembl
  12. cell maturation Source: Ensembl
  13. cellular response to growth factor stimulus Source: UniProtKB
  14. cellular response to indole-3-methanol Source: UniProtKB
  15. central nervous system vasculogenesis Source: Ensembl
  16. dorsal/ventral axis specification Source: Ensembl
  17. ectoderm development Source: Ensembl
  18. embryonic axis specification Source: Ensembl
  19. embryonic digit morphogenesis Source: Ensembl
  20. embryonic foregut morphogenesis Source: Ensembl
  21. embryonic forelimb morphogenesis Source: Ensembl
  22. embryonic heart tube development Source: Ensembl
  23. embryonic hindlimb morphogenesis Source: Ensembl
  24. embryonic skeletal limb joint morphogenesis Source: Ensembl
  25. endodermal cell fate commitment Source: Ensembl
  26. endothelial tube morphogenesis Source: UniProtKB
  27. epithelial cell differentiation involved in prostate gland development Source: Ensembl
  28. epithelial tube branching involved in lung morphogenesis Source: Ensembl
  29. fungiform papilla formation Source: Ensembl
  30. gastrulation with mouth forming second Source: Ensembl
  31. genitalia morphogenesis Source: Ensembl
  32. glial cell fate determination Source: Ensembl
  33. hair follicle morphogenesis Source: Ensembl
  34. hair follicle placode formation Source: Ensembl
  35. in utero embryonic development Source: Ensembl
  36. layer formation in cerebral cortex Source: Ensembl
  37. lens morphogenesis in camera-type eye Source: Ensembl
  38. lung-associated mesenchyme development Source: Ensembl
  39. lung cell differentiation Source: Ensembl
  40. lung induction Source: Ensembl
  41. male genitalia development Source: Ensembl
  42. mesenchymal cell proliferation involved in lung development Source: Ensembl
  43. mesenchymal to epithelial transition involved in metanephros morphogenesis Source: Ensembl
  44. negative regulation of apoptotic signaling pathway Source: Ensembl
  45. negative regulation of cell proliferation Source: UniProtKB
  46. negative regulation of chondrocyte differentiation Source: Ensembl
  47. negative regulation of neuron death Source: Ensembl
  48. negative regulation of oligodendrocyte differentiation Source: Ensembl
  49. negative regulation of osteoclast differentiation Source: Ensembl
  50. negative regulation of protein sumoylation Source: Ensembl
  51. negative regulation of transcription, DNA-templated Source: UniProtKB
  52. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  53. nephron tubule formation Source: Ensembl
  54. neural plate development Source: Ensembl
  55. neuron migration Source: Ensembl
  56. odontogenesis of dentin-containing tooth Source: Ensembl
  57. oocyte development Source: Ensembl
  58. osteoclast differentiation Source: Ensembl
  59. oviduct development Source: Ensembl
  60. pancreas development Source: Ensembl
  61. patterning of blood vessels Source: Ensembl
  62. positive regulation of apoptotic process Source: UniProtKB
  63. positive regulation of branching involved in lung morphogenesis Source: Ensembl
  64. positive regulation of determination of dorsal identity Source: Ensembl
  65. positive regulation of endothelial cell differentiation Source: Ensembl
  66. positive regulation of epithelial cell proliferation involved in prostate gland development Source: Ensembl
  67. positive regulation of fibroblast growth factor receptor signaling pathway Source: Ensembl
  68. positive regulation of heparan sulfate proteoglycan biosynthetic process Source: UniProtKB
  69. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  70. positive regulation of MAPK cascade Source: Ensembl
  71. positive regulation of mesenchymal cell proliferation Source: Ensembl
  72. positive regulation of neuroblast proliferation Source: Ensembl
  73. positive regulation of osteoblast differentiation Source: Ensembl
  74. positive regulation of transcription, DNA-templated Source: UniProtKB
  75. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  76. protein localization to cell surface Source: UniProtKB
  77. proximal/distal pattern formation Source: Ensembl
  78. regulation of calcium ion import Source: UniProtKB
  79. regulation of centriole-centriole cohesion Source: UniProtKB
  80. regulation of centromeric sister chromatid cohesion Source: UniProtKB
  81. regulation of myelination Source: Ensembl
  82. regulation of nephron tubule epithelial cell differentiation Source: Ensembl
  83. regulation of protein localization to cell surface Source: UniProtKB
  84. regulation of secondary heart field cardioblast proliferation Source: Ensembl
  85. regulation of smooth muscle cell proliferation Source: UniProtKB
  86. regulation of T cell proliferation Source: Ensembl
  87. renal inner medulla development Source: Ensembl
  88. renal outer medulla development Source: Ensembl
  89. renal vesicle formation Source: Ensembl
  90. response to drug Source: Ensembl
  91. response to estradiol Source: UniProtKB
  92. single organismal cell-cell adhesion Source: UniProtKB
  93. smooth muscle cell differentiation Source: Ensembl
  94. synapse organization Source: Ensembl
  95. synaptic vesicle transport Source: Ensembl
  96. T cell differentiation in thymus Source: Ensembl
  97. thymus development Source: Ensembl
  98. tight junction assembly Source: UniProtKB
  99. trachea formation Source: Ensembl
  100. transcription, DNA-templated Source: UniProtKB-KW
  101. Wnt signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell adhesion, Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_175273. Ca2+ pathway.
REACT_202887. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_207387. TCF dependent signaling in response to WNT.
REACT_210055. formation of the beta-catenin:TCF transactivating complex.
REACT_220177. deactivation of the beta-catenin transactivating complex.
REACT_226383. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_231976. Beta-catenin phosphorylation cascade.
REACT_232034. VEGFR2 mediated vascular permeability.
REACT_237840. Apoptotic cleavage of cell adhesion proteins.
REACT_242213. S37 mutants of beta-catenin aren't phosphorylated.
REACT_249616. S33 mutants of beta-catenin aren't phosphorylated.
REACT_251509. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
REACT_253450. S45 mutants of beta-catenin aren't phosphorylated.
REACT_256361. Degradation of beta-catenin by the destruction complex.
REACT_259324. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_259349. Adherens junctions interactions.
REACT_260859. T41 mutants of beta-catenin aren't phosphorylated.
REACT_261000. CDO in myogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Catenin beta-1
Alternative name(s):
Beta-catenin
Gene namesi
Name:CTNNB1
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Chromosome 23

Subcellular locationi

Cell junction 1 Publication. Cytoplasm By similarity. Cytoplasmcytoskeleton 1 Publication. Nucleus By similarity. Cell junctionadherens junction By similarity. Cell membrane By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle pole By similarity
Note: Cytoplasmic when it is unstabilized (high level of phosphorylation) or bound to CDH1. Translocates to the nucleus when it is stabilized (low level of phosphorylation). Interaction with GLIS2 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 (By similarity). Colocalized with RAPGEF2 and TJP1 at cell-cell contacts.By similarity

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. basolateral plasma membrane Source: Ensembl
  3. beta-catenin destruction complex Source: UniProtKB
  4. beta-catenin-TCF7L2 complex Source: UniProtKB
  5. catenin complex Source: UniProtKB
  6. cell-cell adherens junction Source: UniProtKB
  7. cell-cell junction Source: UniProtKB
  8. cell cortex Source: UniProtKB
  9. cell junction Source: UniProtKB
  10. cell periphery Source: BHF-UCL
  11. centrosome Source: UniProtKB
  12. cytoplasm Source: UniProtKB
  13. cytosol Source: UniProtKB
  14. extracellular vesicular exosome Source: Ensembl
  15. fascia adherens Source: Ensembl
  16. lamellipodium Source: Ensembl
  17. lateral plasma membrane Source: Ensembl
  18. microvillus membrane Source: Ensembl
  19. nucleus Source: UniProtKB
  20. perinuclear region of cytoplasm Source: UniProtKB
  21. plasma membrane Source: UniProtKB
  22. protein-DNA complex Source: UniProtKB
  23. Scrib-APC-beta-catenin complex Source: Ensembl
  24. tight junction Source: Ensembl
  25. transcription factor complex Source: UniProtKB
  26. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 781780Catenin beta-1PRO_0000423871Add
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 HIPK2By similarity
Modified residuei37 – 371Phosphoserine; by GSK3-beta and HIPK2By similarity
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 PTK6By similarity
Modified residuei191 – 1911Phosphoserine; by CDK5By similarity
Modified residuei246 – 2461Phosphoserine; by CDK5By similarity
Modified residuei331 – 3311PhosphotyrosineBy similarity
Modified residuei551 – 5511PhosphothreonineBy similarity
Modified residuei552 – 5521Phosphoserine; by AMPKBy similarity
Modified residuei556 – 5561PhosphothreonineBy similarity
Modified residuei619 – 6191S-nitrosocysteineBy similarity
Modified residuei654 – 6541PhosphotyrosineBy similarity
Modified residuei675 – 6751PhosphoserineBy similarity

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.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

PRIDEiB6V8E6.

Interactioni

Subunit structurei

Two separate complex-associated pools are found in the cytoplasm. The majority is present as part 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 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 disassociates, 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 (By similarity). Interacts with RAPGEF2.By similarity1 Publication

Protein-protein interaction databases

IntActiB6V8E6. 7 interactions.
MINTiMINT-7906978.
STRINGi9615.ENSCAFP00000032261.

Structurei

3D structure databases

ProteinModelPortaliB6V8E6.
SMRiB6V8E6. Positions 19-44, 142-691.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati141 – 18040ARM 1Add
BLAST
Repeati181 – 22343ARM 2Add
BLAST
Repeati224 – 26441ARM 3Add
BLAST
Repeati265 – 30642ARM 4Add
BLAST
Repeati308 – 34942ARM 5Add
BLAST
Repeati350 – 39041ARM 6Add
BLAST
Repeati392 – 42938ARM 7Add
BLAST
Repeati430 – 47344ARM 8Add
BLAST
Repeati478 – 51942ARM 9Add
BLAST
Repeati520 – 58263ARM 10Add
BLAST
Repeati583 – 62341ARM 11Add
BLAST
Repeati624 – 66441ARM 12Add
BLAST

Region

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

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.
InParanoidiB6V8E6.
KOiK02105.
OMAiRESHNRA.
OrthoDBiEOG7X9G6B.
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.

B6V8E6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG
60 70 80 90 100
NPEEEDVDTT 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
GAQGEPLGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV
760 770 780
DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L
Length:781
Mass (Da):85,511
Last modified:December 16, 2008 - v1
Checksum:i6148652F953F0723
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ268743 mRNA. Translation: ACJ04159.1.
AAEX03013510 Genomic DNA. No translation available.
RefSeqiNP_001131124.1. NM_001137652.1.
UniGeneiCfa.415.

Genome annotation databases

EnsembliENSCAFT00000008400; ENSCAFP00000007783; ENSCAFG00000005204.
GeneIDi477032.
KEGGicfa:477032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ268743 mRNA. Translation: ACJ04159.1 .
AAEX03013510 Genomic DNA. No translation available.
RefSeqi NP_001131124.1. NM_001137652.1.
UniGenei Cfa.415.

3D structure databases

ProteinModelPortali B6V8E6.
SMRi B6V8E6. Positions 19-44, 142-691.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi B6V8E6. 7 interactions.
MINTi MINT-7906978.
STRINGi 9615.ENSCAFP00000032261.

Proteomic databases

PRIDEi B6V8E6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSCAFT00000008400 ; ENSCAFP00000007783 ; ENSCAFG00000005204 .
GeneIDi 477032.
KEGGi cfa:477032.

Organism-specific databases

CTDi 1499.

Phylogenomic databases

eggNOGi NOG297695.
GeneTreei ENSGT00730000110821.
HOGENOMi HOG000230958.
HOVERGENi HBG000919.
InParanoidi B6V8E6.
KOi K02105.
OMAi RESHNRA.
OrthoDBi EOG7X9G6B.
TreeFami TF317997.

Enzyme and pathway databases

Reactomei REACT_175273. Ca2+ pathway.
REACT_202887. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_207387. TCF dependent signaling in response to WNT.
REACT_210055. formation of the beta-catenin:TCF transactivating complex.
REACT_220177. deactivation of the beta-catenin transactivating complex.
REACT_226383. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_231976. Beta-catenin phosphorylation cascade.
REACT_232034. VEGFR2 mediated vascular permeability.
REACT_237840. Apoptotic cleavage of cell adhesion proteins.
REACT_242213. S37 mutants of beta-catenin aren't phosphorylated.
REACT_249616. S33 mutants of beta-catenin aren't phosphorylated.
REACT_251509. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
REACT_253450. S45 mutants of beta-catenin aren't phosphorylated.
REACT_256361. Degradation of beta-catenin by the destruction complex.
REACT_259324. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_259349. Adherens junctions interactions.
REACT_260859. T41 mutants of beta-catenin aren't phosphorylated.
REACT_261000. CDO in myogenesis.

Miscellaneous databases

NextBioi 20852584.

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. "Cloning and sequencing of the full-length canine beta-catenin cDNA."
    Han J.-I., Na K.-J.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genome sequence, comparative analysis and haplotype structure of the domestic dog."
    Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R.
    , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
    Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Boxer.
  3. Cited for: INTERACTION WITH RAPGEF2, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCTNB1_CANFA
AccessioniPrimary (citable) accession number: B6V8E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: December 16, 2008
Last modified: November 26, 2014
This is version 52 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3