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Q9WU82

- CTNB1_RAT

UniProt

Q9WU82 - CTNB1_RAT

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Protein
Catenin beta-1
Gene
Ctnnb1, Catnb
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.

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 binding Source: UniProtKB
  8. protein complex binding Source: RGD
  9. protein kinase binding Source: RefGenome
  10. sequence-specific DNA binding transcription factor activity Source: Ensembl
  11. structural molecule activity Source: RefGenome
  12. transcription coactivator activity Source: UniProtKB
  13. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

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

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. Cytoplasmcytoskeleton. Nucleus. Cell junctionadherens junction By similarity. Cell junction By similarity. Cell membrane. 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.1 Publication

GO - Cellular componenti

  1. Scrib-APC-beta-catenin complex Source: Ensembl
  2. Z disc Source: RefGenome
  3. apical part of cell Source: Ensembl
  4. basolateral plasma membrane Source: RefGenome
  5. beta-catenin destruction complex Source: UniProtKB
  6. beta-catenin-TCF7L2 complex Source: UniProtKB
  7. catenin complex Source: UniProtKB
  8. cell cortex Source: UniProtKB
  9. cell junction Source: UniProtKB
  10. cell periphery Source: BHF-UCL
  11. cell-cell adherens junction Source: RGD
  12. cell-cell junction Source: UniProtKB
  13. centrosome Source: UniProtKB
  14. cytoplasm Source: UniProtKB
  15. cytoplasmic side of plasma membrane Source: RefGenome
  16. cytosol Source: RGD
  17. dendritic shaft Source: RGD
  18. desmosome Source: RefGenome
  19. fascia adherens Source: RefGenome
  20. lamellipodium Source: RefGenome
  21. lateral plasma membrane Source: Ensembl
  22. membrane Source: UniProtKB
  23. microvillus membrane Source: RefGenome
  24. nucleus Source: RGD
  25. perinuclear region of cytoplasm Source: UniProtKB
  26. plasma membrane Source: UniProtKB
  27. protein complex Source: RGD
  28. protein-DNA complex Source: UniProtKB
  29. spindle pole Source: UniProtKB-SubCell
  30. synapse Source: RGD
  31. transcription factor complex Source: UniProtKB
  32. 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 – 11Removed By similarity
Chaini2 – 781780Catenin beta-1
PRO_0000064273Add
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 HIPK2 By similarity
Modified residuei37 – 371Phosphoserine; by GSK3-beta and HIPK2 By similarity
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 PTK6 By similarity
Modified residuei191 – 1911Phosphoserine; by CDK5 By similarity
Modified residuei246 – 2461Phosphoserine; by CDK5 By similarity
Modified residuei331 – 3311Phosphotyrosine By similarity
Modified residuei551 – 5511Phosphothreonine By similarity
Modified residuei552 – 5521Phosphoserine; by AMPK By similarity
Modified residuei556 – 5561Phosphothreonine By similarity
Modified residuei619 – 6191S-nitrosocysteine By similarity
Modified residuei654 – 6541Phosphotyrosine; by CSK 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. 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.
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.
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

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.

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 By similarity
Add
BLAST
Regioni156 – 17823Interaction with BCL9 By similarity
Add
BLAST
Regioni772 – 78110Interaction with SCRIB By similarity

Sequence similaritiesi

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

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

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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 GGMQALGPHL 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):85,455
Last modified:November 1, 1999 - v1
Checksum:i9C29186B6DD54B87
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti368 – 3681P → L in AAK85253. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF121265 mRNA. Translation: AAD28504.1.
AF397179 Genomic DNA. Translation: AAK85253.1.
RefSeqiNP_445809.2. NM_053357.2.
XP_006244196.1. XM_006244134.1.
XP_006244197.1. XM_006244135.1.
XP_006244198.1. XM_006244136.1.
XP_006244199.1. XM_006244137.1.
XP_006244200.1. XM_006244138.1.
UniGeneiRn.112601.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF121265 mRNA. Translation: AAD28504.1 .
AF397179 Genomic DNA. Translation: AAK85253.1 .
RefSeqi NP_445809.2. NM_053357.2.
XP_006244196.1. XM_006244134.1.
XP_006244197.1. XM_006244135.1.
XP_006244198.1. XM_006244136.1.
XP_006244199.1. XM_006244137.1.
XP_006244200.1. XM_006244138.1.
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.

Miscellaneous databases

NextBioi 616667.
PROi Q9WU82.

Gene expression databases

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: September 3, 2014
This is version 135 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

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