Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9WU82

- CTNB1_RAT

UniProt

Q9WU82 - CTNB1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Catenin beta-1

Gene

Ctnnb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2 (By similarity). Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (By similarity).By similarity

GO - Molecular functioni

  1. alpha-catenin binding Source: RefGenome
  2. cadherin binding Source: RGD
  3. chromatin binding Source: Ensembl
  4. double-stranded DNA binding Source: Ensembl
  5. ionotropic glutamate receptor binding Source: RGD
  6. nitric-oxide synthase binding Source: RGD
  7. protein complex binding Source: RGD
  8. protein kinase binding Source: RefGenome
  9. sequence-specific DNA binding transcription factor activity Source: Ensembl
  10. structural molecule activity Source: RefGenome
  11. transcription coactivator activity Source: UniProtKB
  12. 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: RefGenome
  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: RefGenome
  12. cell maturation Source: Ensembl
  13. cellular response to growth factor stimulus Source: UniProtKB
  14. cellular response to indole-3-methanol Source: UniProtKB
  15. cellular response to insulin-like growth factor stimulus Source: RGD
  16. cellular response to mechanical stimulus Source: RGD
  17. central nervous system vasculogenesis Source: RefGenome
  18. cytoskeletal anchoring at plasma membrane Source: RefGenome
  19. determination of dorsal/ventral asymmetry Source: RefGenome
  20. dorsal/ventral axis specification Source: RefGenome
  21. ectoderm development Source: RefGenome
  22. embryonic axis specification Source: RefGenome
  23. embryonic digit morphogenesis Source: Ensembl
  24. embryonic foregut morphogenesis Source: RefGenome
  25. embryonic forelimb morphogenesis Source: Ensembl
  26. embryonic heart tube development Source: Ensembl
  27. embryonic hindlimb morphogenesis Source: Ensembl
  28. embryonic limb morphogenesis Source: RefGenome
  29. embryonic skeletal limb joint morphogenesis Source: Ensembl
  30. endodermal cell fate commitment Source: RefGenome
  31. endothelial tube morphogenesis Source: UniProtKB
  32. epithelial cell differentiation involved in prostate gland development Source: Ensembl
  33. epithelial tube branching involved in lung morphogenesis Source: Ensembl
  34. fungiform papilla formation Source: Ensembl
  35. gastrulation with mouth forming second Source: RefGenome
  36. genitalia morphogenesis Source: Ensembl
  37. glial cell fate determination Source: RefGenome
  38. hair follicle morphogenesis Source: RefGenome
  39. hair follicle placode formation Source: RefGenome
  40. hindbrain development Source: RefGenome
  41. in utero embryonic development Source: Ensembl
  42. layer formation in cerebral cortex Source: Ensembl
  43. lens morphogenesis in camera-type eye Source: Ensembl
  44. liver development Source: RGD
  45. lung-associated mesenchyme development Source: RefGenome
  46. lung cell differentiation Source: RefGenome
  47. lung induction Source: RefGenome
  48. male genitalia development Source: RefGenome
  49. mesenchymal cell proliferation involved in lung development Source: RefGenome
  50. mesenchymal to epithelial transition involved in metanephros morphogenesis Source: RefGenome
  51. midgut development Source: RGD
  52. myoblast differentiation Source: RGD
  53. negative regulation of apoptotic process Source: RefGenome
  54. negative regulation of apoptotic signaling pathway Source: Ensembl
  55. negative regulation of cell proliferation Source: UniProtKB
  56. negative regulation of chondrocyte differentiation Source: RefGenome
  57. negative regulation of heart induction by canonical Wnt signaling pathway Source: RefGenome
  58. negative regulation of neuron death Source: Ensembl
  59. negative regulation of oligodendrocyte differentiation Source: Ensembl
  60. negative regulation of osteoclast differentiation Source: RefGenome
  61. negative regulation of protein sumoylation Source: UniProtKB
  62. negative regulation of transcription, DNA-templated Source: UniProtKB
  63. negative regulation of transcription from RNA polymerase II promoter Source: RefGenome
  64. nephron tubule formation Source: RefGenome
  65. neural plate development Source: Ensembl
  66. neuron migration Source: Ensembl
  67. odontogenesis of dentin-containing tooth Source: RGD
  68. oocyte development Source: RefGenome
  69. osteoclast differentiation Source: Ensembl
  70. oviduct development Source: Ensembl
  71. pancreas development Source: RefGenome
  72. patterning of blood vessels Source: RefGenome
  73. positive regulation of apoptotic process Source: UniProtKB
  74. positive regulation of branching involved in lung morphogenesis Source: RefGenome
  75. positive regulation of determination of dorsal identity Source: Ensembl
  76. positive regulation of endothelial cell differentiation Source: Ensembl
  77. positive regulation of epithelial cell proliferation involved in prostate gland development Source: RefGenome
  78. positive regulation of fibroblast growth factor receptor signaling pathway Source: RefGenome
  79. positive regulation of heparan sulfate proteoglycan biosynthetic process Source: UniProtKB
  80. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: RefGenome
  81. positive regulation of MAPK cascade Source: RefGenome
  82. positive regulation of mesenchymal cell proliferation Source: Ensembl
  83. positive regulation of neuroblast proliferation Source: Ensembl
  84. positive regulation of osteoblast differentiation Source: RefGenome
  85. positive regulation of transcription, DNA-templated Source: UniProtKB
  86. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  87. protein heterooligomerization Source: RGD
  88. protein localization to cell surface Source: UniProtKB
  89. proximal/distal pattern formation Source: RefGenome
  90. regulation of calcium ion import Source: UniProtKB
  91. regulation of centriole-centriole cohesion Source: UniProtKB
  92. regulation of centromeric sister chromatid cohesion Source: UniProtKB
  93. regulation of myelination Source: Ensembl
  94. regulation of nephron tubule epithelial cell differentiation Source: Ensembl
  95. regulation of protein localization to cell surface Source: UniProtKB
  96. regulation of secondary heart field cardioblast proliferation Source: Ensembl
  97. regulation of smooth muscle cell proliferation Source: UniProtKB
  98. regulation of T cell proliferation Source: RefGenome
  99. renal inner medulla development Source: RefGenome
  100. renal outer medulla development Source: RefGenome
  101. renal vesicle formation Source: RefGenome
  102. response to cadmium ion Source: RGD
  103. response to cytokine Source: RGD
  104. response to drug Source: Ensembl
  105. response to estradiol Source: UniProtKB
  106. response to estrogen Source: RGD
  107. response to hormone Source: RGD
  108. response to organic cyclic compound Source: RGD
  109. Schwann cell proliferation Source: RGD
  110. single organismal cell-cell adhesion Source: UniProtKB
  111. smooth muscle cell differentiation Source: RefGenome
  112. synapse organization Source: RefGenome
  113. synaptic vesicle transport Source: RefGenome
  114. T cell differentiation in thymus Source: RefGenome
  115. thymus development Source: RefGenome
  116. tongue morphogenesis Source: RefGenome
  117. trachea formation Source: RefGenome
  118. transcription, DNA-templated Source: UniProtKB-KW
  119. Wnt signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell adhesion, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_194690. Ca2+ pathway.
REACT_198375. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_212065. TCF dependent signaling in response to WNT.
REACT_214025. deactivation of the beta-catenin transactivating complex.
REACT_216976. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_226234. formation of the beta-catenin:TCF transactivating complex.
REACT_234350. Beta-catenin phosphorylation cascade.
REACT_234411. Apoptotic cleavage of cell adhesion proteins.
REACT_237110. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_242544. T41 mutants of beta-catenin aren't phosphorylated.
REACT_246486. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
REACT_248040. S37 mutants of beta-catenin aren't phosphorylated.
REACT_248864. CDO in myogenesis.
REACT_250136. S33 mutants of beta-catenin aren't phosphorylated.
REACT_251328. S45 mutants of beta-catenin aren't phosphorylated.
REACT_254281. Adherens junctions interactions.
REACT_256841. VEGFR2 mediated vascular permeability.
REACT_257365. Degradation of beta-catenin by the destruction complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Catenin beta-1
Alternative name(s):
Beta-catenin
Gene namesi
Name:Ctnnb1
Synonyms:Catnb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 8

Organism-specific databases

RGDi70487. Ctnnb1.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication. Nucleus 1 Publication. Cell junctionadherens junction By similarity. Cell junction By similarity. Cell membrane 1 Publication. 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. apical part of cell Source: Ensembl
  2. basolateral plasma membrane Source: RefGenome
  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: RGD
  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. cytoplasmic side of plasma membrane Source: RefGenome
  14. cytosol Source: RGD
  15. dendritic shaft Source: RGD
  16. desmosome Source: RefGenome
  17. extracellular vesicular exosome Source: Ensembl
  18. fascia adherens Source: RefGenome
  19. lamellipodium Source: RefGenome
  20. lateral plasma membrane Source: Ensembl
  21. membrane Source: UniProtKB
  22. microvillus membrane Source: RefGenome
  23. nucleus Source: RGD
  24. perinuclear region of cytoplasm Source: UniProtKB
  25. plasma membrane Source: UniProtKB
  26. protein complex Source: RGD
  27. protein-DNA complex Source: UniProtKB
  28. Scrib-APC-beta-catenin complex Source: Ensembl
  29. synapse Source: RGD
  30. tight junction Source: Ensembl
  31. transcription factor complex Source: UniProtKB
  32. Z disc Source: RefGenome
  33. zonula adherens Source: RefGenome
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_0000064273Add
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 – 6541Phosphotyrosine; by CSKBy 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. 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

PaxDbiQ9WU82.
PRIDEiQ9WU82.

PTM databases

PhosphoSiteiQ9WU82.

Expressioni

Tissue specificityi

Expressed in the testis.

Developmental stagei

Highly expressed at E30-60 day DPC in the testis. Reduced expression at E90 day DPC.

Gene expression databases

ExpressionAtlasiQ9WU82. baseline.
GenevestigatoriQ9WU82.

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. 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 Interacts directly with AXIN1; the interaction is regulated by CK2 via BTRC and its subsequent degradation by the proteasome. Interacts directly with AXIN1;the interaction is regulated by CDK2 phosphorylation. Wnt-dependent activation of DVL antagonizes the action of GSK3B. When GSK3B activity is inhibited the complex dissociates, CTNNB1 is dephosphorylated and is no longer targeted for destruction. The stabilized protein translocates to the nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9, BCL9L and possibly also RUVBL1 and CHD8. Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 binding. Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits the transcriptional activity of CTNNB1. Interacts with AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1. Interacts with GLIS2. Interacts with XIRP1. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain) and with SLC30A9. Interacts with EMD. Interacts with SCRIB. Interacts with TNIK and TCF7L2. Interacts with SESTD1 and TRPC4. Interacts directly with AXIN1; the interaction is regulated by CDK2 phosphorylation of AXIN1. Interacts with CAV1. Interacts with TRPV4. The TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with VCL. Interacts with PTPRJ. Interacts with PKT7. Interacts with NANOS1. Interacts with CDK2, NDRG2, NEK2 and CDK5. Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B. Interacts with PTK6. Interacts with SOX7; this interaction may lead to proteasomal degradation of active CTNNB1 and thus inhibition of Wnt/beta-catenin-stimulated transcription. Identified in a complex with HINT1 and MITF. Interacts with FHIT. The CTNNB1 and TCF4 complex interacts with PML. Interacts with FERMT2. Identified in a complex with TCF4 and FERMT2. Interacts with RAPGEF2. Interacts with FAT1 (via the cytoplasmic domain). Interacts with RORA. May interact with P-cadherin/CDH3.3 Publications

Protein-protein interaction databases

BioGridi249913. 11 interactions.
DIPiDIP-37053N.
IntActiQ9WU82. 4 interactions.
MINTiMINT-87458.

Structurei

3D structure databases

ProteinModelPortaliQ9WU82.
SMRiQ9WU82. Positions 19-44, 118-682.
ModBaseiSearch...
MobiDBiSearch...

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 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.
InParanoidiQ9WU82.
KOiK02105.
OrthoDBiEOG7X9G6B.
PhylomeDBiQ9WU82.
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.

Q9WU82-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG
60 70 80 90 100
NPEEEDVDTS QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP
110 120 130 140 150
ETLDEGMQIP STQFDAAHPT NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT
160 170 180 190 200
RAIPELTKLL NDEDQVVVNK AAVMVHQLSK KEASRHAIMR SPQMVSAIVR
210 220 230 240 250
TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL VKMLGSPVDS
260 270 280 290 300
VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC
310 320 330 340 350
LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC
360 370 380 390 400
SSNKPAIVEA GGMQALGPHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG
410 420 430 440 450
LLGTLVQLLG SDDINVVTCA AGILSNLTCN NYKNKMMVCQ VGGIEALVRT
460 470 480 490 500
VLRAGDREDI TEPAICALRH LTSRHQEAEM AQNAVRLHYG LPVVVKLLHP
510 520 530 540 550
PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL VRAHQDTQRR
560 570 580 590 600
TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV
610 620 630 640 650
QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG
660 670 680 690 700
VATYAAAVLF RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI
710 720 730 740 750
GAQGEALGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV
760 770 780
DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L
Length:781
Mass (Da):85,455
Last modified:November 1, 1999 - v1
Checksum:i9C29186B6DD54B87
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti368 – 3681P → L in AAK85253. (PubMed:11867232)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121265 mRNA. Translation: AAD28504.1.
AF397179 Genomic DNA. Translation: AAK85253.1.
RefSeqiNP_445809.2. NM_053357.2.
XP_008764913.1. XM_008766691.1.
UniGeneiRn.112601.

Genome annotation databases

EnsembliENSRNOT00000026016; ENSRNOP00000026016; ENSRNOG00000019139.
GeneIDi84353.
KEGGirno:84353.
UCSCiRGD:70487. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121265 mRNA. Translation: AAD28504.1 .
AF397179 Genomic DNA. Translation: AAK85253.1 .
RefSeqi NP_445809.2. NM_053357.2.
XP_008764913.1. XM_008766691.1.
UniGenei Rn.112601.

3D structure databases

ProteinModelPortali Q9WU82.
SMRi Q9WU82. Positions 19-44, 118-682.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249913. 11 interactions.
DIPi DIP-37053N.
IntActi Q9WU82. 4 interactions.
MINTi MINT-87458.

PTM databases

PhosphoSitei Q9WU82.

Proteomic databases

PaxDbi Q9WU82.
PRIDEi Q9WU82.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000026016 ; ENSRNOP00000026016 ; ENSRNOG00000019139 .
GeneIDi 84353.
KEGGi rno:84353.
UCSCi RGD:70487. rat.

Organism-specific databases

CTDi 1499.
RGDi 70487. Ctnnb1.

Phylogenomic databases

eggNOGi NOG297695.
GeneTreei ENSGT00730000110821.
HOGENOMi HOG000230958.
HOVERGENi HBG000919.
InParanoidi Q9WU82.
KOi K02105.
OrthoDBi EOG7X9G6B.
PhylomeDBi Q9WU82.
TreeFami TF317997.

Enzyme and pathway databases

Reactomei REACT_194690. Ca2+ pathway.
REACT_198375. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_212065. TCF dependent signaling in response to WNT.
REACT_214025. deactivation of the beta-catenin transactivating complex.
REACT_216976. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_226234. formation of the beta-catenin:TCF transactivating complex.
REACT_234350. Beta-catenin phosphorylation cascade.
REACT_234411. Apoptotic cleavage of cell adhesion proteins.
REACT_237110. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_242544. T41 mutants of beta-catenin aren't phosphorylated.
REACT_246486. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
REACT_248040. S37 mutants of beta-catenin aren't phosphorylated.
REACT_248864. CDO in myogenesis.
REACT_250136. S33 mutants of beta-catenin aren't phosphorylated.
REACT_251328. S45 mutants of beta-catenin aren't phosphorylated.
REACT_254281. Adherens junctions interactions.
REACT_256841. VEGFR2 mediated vascular permeability.
REACT_257365. Degradation of beta-catenin by the destruction complex.

Miscellaneous databases

NextBioi 616667.
PROi Q9WU82.

Gene expression databases

ExpressionAtlasi Q9WU82. baseline.
Genevestigatori Q9WU82.

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. "Study on the formation of specialized inter-Sertoli cell junctions in vitro."
    Chung S.S.W., Lee W.M., Cheng C.Y.
    J. Cell. Physiol. 181:258-272(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  2. "Sequencing of the rat beta-catenin gene (Ctnnb1) and mutational analysis of liver tumors induced by 2-amino-3-methylimidazo[4,5-f]quinoline."
    Li Q., Dixon B.M., Al-Fageeh M., Blum C.A., Dashwood R.H.
    Gene 283:255-262(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Fischer 344.
  3. "The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway."
    Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.
    Genes Dev. 20:1933-1945(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH MACF1; APC; AXIN1 AND GSK3B.
  4. "The Fat1 cadherin integrates vascular smooth muscle cell growth and migration signals."
    Hou R., Liu L., Anees S., Hiroyasu S., Sibinga N.E.
    J. Cell Biol. 173:417-429(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAT1.
  5. "A novel beta-catenin-binding protein inhibits beta-catenin-dependent Tcf activation and axis formation."
    Sakamoto I., Kishida S., Fukui A., Kishida M., Yamamoto H., Hino S., Michiue T., Takada S., Asashima M., Kikuchi A.
    J. Biol. Chem. 275:32871-32878(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHD8.
  6. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCTNB1_RAT
AccessioniPrimary (citable) accession number: Q9WU82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: November 26, 2014
This is version 138 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