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P35222

- CTNB1_HUMAN

UniProt

P35222 - CTNB1_HUMAN

Protein

Catenin beta-1

Gene

CTNNB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 184 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML.8 Publications

    GO - Molecular functioni

    1. alpha-catenin binding Source: BHF-UCL
    2. androgen receptor binding Source: UniProtKB
    3. cadherin binding Source: UniProtKB
    4. chromatin binding Source: Ensembl
    5. double-stranded DNA binding Source: Ensembl
    6. enzyme binding Source: BHF-UCL
    7. estrogen receptor binding Source: BHF-UCL
    8. ion channel binding Source: BHF-UCL
    9. I-SMAD binding Source: BHF-UCL
    10. kinase binding Source: BHF-UCL
    11. nuclear hormone receptor binding Source: BHF-UCL
    12. protein binding Source: IntAct
    13. protein C-terminus binding Source: UniProtKB
    14. protein kinase binding Source: RefGenome
    15. protein phosphatase binding Source: UniProtKB
    16. RNA polymerase II activating transcription factor binding Source: BHF-UCL
    17. R-SMAD binding Source: BHF-UCL
    18. sequence-specific DNA binding transcription factor activity Source: Ensembl
    19. signal transducer activity Source: ProtInc
    20. SMAD binding Source: BHF-UCL
    21. structural molecule activity Source: RefGenome
    22. transcription coactivator activity Source: UniProtKB
    23. transcription factor binding Source: BHF-UCL
    24. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Cell adhesion, Transcription, Transcription regulation, Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_13579. Apoptotic cleavage of cell adhesion proteins.
    REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
    REACT_172761. Ca2+ pathway.
    REACT_19195. Adherens junctions interactions.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_200777. TCF dependent signaling in response to WNT.
    REACT_200799. binding of TCF/LEF:CTNNB1 to target gene promoters.
    REACT_21402. CDO in myogenesis.
    REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
    SignaLinkiP35222.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catenin beta-1
    Alternative name(s):
    Beta-catenin
    Gene namesi
    Name:CTNNB1
    Synonyms:CTNNB
    ORF Names:OK/SW-cl.35, PRO2286
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:2514. CTNNB1.

    Subcellular locationi

    Cytoplasm. Nucleus. Cytoplasmcytoskeleton. Cell junctionadherens junction. Cell junction. Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle pole
    Note: Colocalized with RAPGEF2 and TJP1 at cell-cell contacts By similarity. 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 and MUC1 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

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB
    2. apical part of cell Source: Ensembl
    3. basolateral plasma membrane Source: Ensembl
    4. beta-catenin destruction complex Source: BHF-UCL
    5. beta-catenin-TCF7L2 complex Source: BHF-UCL
    6. catenin complex Source: BHF-UCL
    7. cell-cell adherens junction Source: UniProtKB
    8. cell-cell junction Source: BHF-UCL
    9. cell cortex Source: BHF-UCL
    10. cell junction Source: UniProtKB
    11. cell periphery Source: BHF-UCL
    12. centrosome Source: UniProtKB
    13. cytoplasm Source: UniProtKB
    14. cytoplasmic side of plasma membrane Source: RefGenome
    15. cytosol Source: UniProtKB
    16. dendritic shaft Source: RefGenome
    17. desmosome Source: RefGenome
    18. extracellular vesicular exosome Source: UniProt
    19. fascia adherens Source: RefGenome
    20. lamellipodium Source: RefGenome
    21. lateral plasma membrane Source: MGI
    22. membrane Source: UniProtKB
    23. microvillus membrane Source: RefGenome
    24. nucleoplasm Source: Reactome
    25. nucleus Source: UniProtKB
    26. perinuclear region of cytoplasm Source: UniProtKB
    27. plasma membrane Source: UniProtKB
    28. protein-DNA complex Source: BHF-UCL
    29. Scrib-APC-beta-catenin complex Source: Ensembl
    30. spindle pole Source: UniProtKB-SubCell
    31. synapse Source: RefGenome
    32. transcription factor complex Source: BHF-UCL
    33. Z disc Source: RefGenome
    34. zonula adherens Source: RefGenome

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.1 Publication
    Note: The gene represented in this entry may be involved in disease pathogenesis.
    Activating mutations in CTNNB1 have oncogenic activity resulting in tumor development. Somatic mutations are found in various tumor types, including colon cancers, ovarian and prostate carcinomas, hepatoblastoma (HB), hepatocellular carcinoma (HCC). HBs are malignant embryonal tumors mainly affecting young children in the first three years of life.
    Pilomatrixoma (PTR) [MIM:132600]: Common benign skin tumor.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321D → G in PTR and hepatocellular carcinoma. 2 Publications
    VAR_017615
    Natural varianti32 – 321D → Y in PTR, hepatoblastoma and hepatocellular carcinoma. 4 Publications
    Corresponds to variant rs28931588 [ dbSNP | Ensembl ].
    VAR_017616
    Natural varianti33 – 331S → F in PTR, MDB and hepatocellular carcinoma. 3 Publications
    VAR_017617
    Natural varianti33 – 331S → Y in colorectal cancer and PTR; enhances transactivation of target genes. 2 Publications
    VAR_017619
    Natural varianti34 – 341G → E in PTR. 1 Publication
    VAR_017620
    Natural varianti37 – 371S → C in PTR, hepatoblastoma and ovarian cancer. 3 Publications
    VAR_017625
    Natural varianti37 – 371S → F in PTR. 1 Publication
    VAR_017626
    Natural varianti41 – 411T → I in PTR, hepatocellular carcinoma and ovarian cancer. 3 Publications
    VAR_017630
    Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children.1 Publication
    Note: The gene represented in this entry may be involved in disease pathogenesis.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331S → F in PTR, MDB and hepatocellular carcinoma. 3 Publications
    VAR_017617
    Natural varianti37 – 371S → A in MDB and hepatocellular carcinoma; enhances transactivation of target genes. 2 Publications
    VAR_017624
    Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    A chromosomal aberration involving CTNNB1 is found in salivary gland pleiomorphic adenomas, the most common benign epithelial tumors of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1.
    Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle-shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos.1 Publication
    Note: The gene represented in this entry may be involved in disease pathogenesis.
    Mental retardation, autosomal dominant 19 (MRD19) [MIM:615075]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD19 features include severe intellectual disability with absent or very limited speech, microcephaly, and spasticity which severely impaired the ability to walk.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291S → F: No effect. 1 Publication
    Mutagenesisi64 – 641Y → F: Abolishes phosphorylation by PTK6. 1 Publication
    Mutagenesisi142 – 1421Y → E: No effect on interaction with BCL9 and BCL9L. 1 Publication
    Mutagenesisi156 – 1561L → A: Abolishes interaction with BCL9 but no effect on interaction with CDH3; when associated with A-159. 1 Publication
    Mutagenesisi159 – 1591L → A: No effect on interaction with BCL9 and CDH3. Abolishes interaction with BCL9 but no effect on interaction with CDH3; when associated with A-156. 1 Publication
    Mutagenesisi178 – 1781L → A: No effect on interaction with BCL9 and CDH3. 1 Publication
    Mutagenesisi253 – 2531F → A: Abolishes or strongly reduces AXIN2 binding. 1 Publication
    Mutagenesisi260 – 2601H → A: Abolishes or strongly reduces AXIN1 and AXIN2 binding. Strongly reduces phosphorylation and degradation; when associated with A-386 and A-383. 1 Publication
    Mutagenesisi292 – 2921K → A: Abolishes or strongly reduces AXIN1 and AXIN2 binding. 1 Publication
    Mutagenesisi312 – 3121K → E: Abolishes TCF7L2 binding. 1 Publication
    Mutagenesisi345 – 3451K → A: Abolishes APC binding. 1 Publication
    Mutagenesisi383 – 3831W → A: Abolishes APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-386. 1 Publication
    Mutagenesisi386 – 3861R → A: Strongly reduces APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-383. 1 Publication
    Mutagenesisi426 – 4261N → A: Abolishes TCF7L2 and LEF1 binding. 1 Publication
    Mutagenesisi435 – 4351K → A: Strongly reduces or abolishes LEF1 binding. 2 Publications
    Mutagenesisi435 – 4351K → E: Abolishes TCF7L2 binding. 2 Publications
    Mutagenesisi469 – 4691R → A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding. 1 Publication
    Mutagenesisi470 – 4701H → A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding. 1 Publication
    Mutagenesisi508 – 5081K → A: Abolishes TCF7L2 and LEF1 binding. 1 Publication
    Mutagenesisi654 – 6541Y → E: Enhances TBP binding and transactivation of target genes. 1 Publication
    Mutagenesisi654 – 6541Y → F: Abolishes increase of TBP binding after phosphorylation by CSK. 1 Publication
    Mutagenesisi660 – 6601F → A: Abolishes CTNNBIP1 binding; when associated with A-661. 1 Publication
    Mutagenesisi661 – 6611R → A: Abolishes CTNNBIP1 binding; when associated with A-660. 1 Publication

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi114500. phenotype.
    132600. phenotype.
    155255. phenotype.
    156240. phenotype.
    167000. phenotype.
    181030. phenotype.
    615075. phenotype.
    Orphaneti85142. Aldosterone-producing adenoma.
    178469. Autosomal dominant nonsyndromic intellectual disability.
    54595. Craniopharyngioma.
    873. Desmoid tumor.
    33402. Hepatocellular carcinoma, childhood-onset.
    91414. Pilomatrixoma.
    PharmGKBiPA27013.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 781780Catenin beta-1PRO_0000064271Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei23 – 231Phosphoserine; by GSK3-beta1 Publication
    Modified residuei29 – 291Phosphoserine; by GSK3-beta1 Publication
    Modified residuei33 – 331Phosphoserine; by GSK3-beta and HIPK21 Publication
    Modified residuei37 – 371Phosphoserine; by GSK3-beta and HIPK21 Publication
    Modified residuei41 – 411Phosphothreonine; by GSK3-beta1 Publication
    Modified residuei45 – 451Phosphoserine1 Publication
    Modified residuei64 – 641Phosphotyrosine; by PTK61 Publication
    Modified residuei86 – 861Phosphotyrosine; by CSK1 Publication
    Modified residuei142 – 1421Phosphotyrosine; by FYN and PTK62 Publications
    Modified residuei191 – 1911Phosphoserine; by CDK52 Publications
    Modified residuei246 – 2461Phosphoserine; by CDK51 Publication
    Modified residuei331 – 3311Phosphotyrosine; by PTK61 Publication
    Modified residuei333 – 3331Phosphotyrosine; by PTK61 Publication
    Modified residuei551 – 5511Phosphothreonine
    Modified residuei552 – 5521Phosphoserine1 Publication
    Modified residuei556 – 5561Phosphothreonine1 Publication
    Modified residuei619 – 6191S-nitrosocysteineBy similarity
    Modified residuei654 – 6541Phosphotyrosine; by CSK1 Publication
    Modified residuei675 – 6751Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription By similarity. Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-37 and 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 on Ser-191 and Ser-246 by CDK5. Phosphorylation by CDK2 regulates insulin internalization. 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 similarity15 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.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

    MaxQBiP35222.
    PaxDbiP35222.
    PRIDEiP35222.

    PTM databases

    PhosphoSiteiP35222.

    Miscellaneous databases

    PMAP-CutDBP35222.

    Expressioni

    Tissue specificityi

    Expressed in several hair follicle cell types: basal and peripheral matrix cells, and cells of the outer and inner root sheaths. Expressed in colon. Present in cortical neurons (at protein level).3 Publications

    Gene expression databases

    ArrayExpressiP35222.
    BgeeiP35222.
    CleanExiHS_CTNNB1.
    GenevestigatoriP35222.

    Organism-specific databases

    HPAiCAB000108.
    CAB001950.
    HPA029159.
    HPA029160.

    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 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. 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 and MUC1. Interacts with SLC30A9. Interacts with XIRP1. Interacts directly with AXIN1; the interaction is regulated by CDK2 phosphorylation of AXIN1. Interacts with SCRIB. Interacts with RAPGEF2. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain). Interacts with EMD. Interacts with TNIK and TCF7L2. Interacts with SESTD1 and TRPC4. Interacts with CAV1. Interacts with TRPV4. The TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with VCL. Interacts with PTPRJ. Interacts with PKT7 and CDK2. Interacts with FAT1 (via the cytoplasmic domain). Interacts with NANOS1 and NDRG2. Interacts with isoform 1 of NEK2. Interacts with both isoform 1 and isoform 2 of CDK5. 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 TCF7L2/TCF4 complex interacts with PML (isoform PML-4). Interacts with FERMT2. Identified in a complex with TCF7L2/TCF4 and FERMT2. Interacts with RORA. May interact with P-cadherin/CDH3.38 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL1P005192EBI-491549,EBI-375543
    ACTN4O437077EBI-491549,EBI-351526
    APCP2505410EBI-491549,EBI-727707
    ARP102758EBI-491549,EBI-608057
    AXIN1O1516926EBI-491549,EBI-710484
    Axin1O356254EBI-491549,EBI-2365912From a different organism.
    BCL9O005122EBI-491549,EBI-533127
    BCR/ABL fusionA1Z1992EBI-491549,EBI-7286259
    BTRCQ9Y2975EBI-491549,EBI-307461
    CAV1P337245EBI-491549,EBI-79998From a different organism.
    CDC73Q6P1J99EBI-491549,EBI-930143
    CDH1P1283010EBI-491549,EBI-727477
    CDH2P190222EBI-491549,EBI-2256711
    CDH5P331516EBI-491549,EBI-2903122
    CREBBPQ927932EBI-491549,EBI-81215
    Ctnna1P262312EBI-491549,EBI-647895From a different organism.
    CTNNBIP1Q9NSA39EBI-491549,EBI-747082
    DACT1Q9NYF03EBI-491549,EBI-3951744
    EGR1P181467EBI-491549,EBI-2834611
    EMDP504023EBI-491549,EBI-489887
    FBXW11Q9UKB12EBI-491549,EBI-355189
    FERMT2Q96AC113EBI-491549,EBI-4399465
    FGFR1P113622EBI-491549,EBI-1028277
    FLT1P179482EBI-491549,EBI-1026718
    FOXM1Q0805016EBI-491549,EBI-866480
    GLIS2Q9BZE06EBI-491549,EBI-7251368
    GSK3BP498419EBI-491549,EBI-373586
    HTTP428585EBI-491549,EBI-466029
    IGF1RP080693EBI-491549,EBI-475981
    ipaCP180124EBI-491563,EBI-491541From a different organism.
    IQGAP1P469403EBI-491549,EBI-297509
    JRKO755643EBI-491549,EBI-8607681
    KANK1Q146782EBI-491549,EBI-2556221
    KIAA1109Q2LD372EBI-491549,EBI-2683809
    LEF1Q9UJU25EBI-491549,EBI-926131
    LEO1Q8WVC02EBI-491549,EBI-932432
    MAP1LC3BQ9GZQ85EBI-491549,EBI-373144
    NFKB1P198383EBI-491549,EBI-300010
    PARD3Q8TEW02EBI-491549,EBI-81968
    PECAM1P162843EBI-491549,EBI-716404
    PITX2Q996972EBI-491549,EBI-1175211
    PSEN1P497682EBI-491549,EBI-297277
    PTH1RQ034314EBI-491549,EBI-2860297
    PTK7Q133085EBI-491549,EBI-2803245
    PTPRCP085752EBI-491549,EBI-1341
    PTPRGP234702EBI-491549,EBI-2258115
    PTPRJQ129132EBI-491549,EBI-2264500
    PXNP490234EBI-491549,EBI-702209
    RELAQ042062EBI-491549,EBI-73886
    RUNX3Q1376112EBI-491549,EBI-925990
    SKP1P632083EBI-491549,EBI-307486
    SOX17Q9H6I22EBI-491549,EBI-9106753
    TCF4P1588419EBI-491549,EBI-533224
    TCF7P364022EBI-491549,EBI-2119465
    TCF7L2Q9NQB030EBI-491549,EBI-924724
    TNIKQ9UKE53EBI-491549,EBI-1051794
    TOP2AP113885EBI-491549,EBI-539628
    WWTR1Q9GZV54EBI-491549,EBI-747743
    Wwtr1Q9EPK52EBI-491549,EBI-1211920From a different organism.
    YAP1P4693712EBI-491549,EBI-1044059
    YAP1P46937-32EBI-491549,EBI-6558686

    Protein-protein interaction databases

    BioGridi107880. 247 interactions.
    DIPiDIP-122N.
    IntActiP35222. 161 interactions.
    MINTiMINT-105089.
    STRINGi9606.ENSP00000344456.

    Structurei

    Secondary structure

    1
    781
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi135 – 15016
    Helixi152 – 1609
    Helixi165 – 17915
    Helixi182 – 1898
    Helixi192 – 20413
    Helixi208 – 22114
    Helixi225 – 2339
    Helixi236 – 2438
    Helixi249 – 26517
    Helixi269 – 2768
    Helixi278 – 2847
    Helixi285 – 2873
    Helixi291 – 30515
    Helixi309 – 3179
    Helixi320 – 33011
    Helixi334 – 34714
    Helixi353 – 3597
    Helixi362 – 3676
    Turni368 – 3714
    Helixi375 – 38915
    Helixi399 – 40810
    Helixi414 – 42714
    Turni428 – 4303
    Helixi432 – 4409
    Helixi443 – 45412
    Helixi458 – 47114
    Beta strandi473 – 4753
    Helixi478 – 48710
    Helixi491 – 4966
    Beta strandi499 – 5013
    Helixi504 – 51714
    Helixi521 – 5233
    Helixi524 – 5296
    Helixi532 – 54716
    Beta strandi550 – 5523
    Beta strandi554 – 5574
    Beta strandi561 – 5633
    Helixi566 – 58015
    Helixi584 – 5929
    Helixi596 – 6016
    Helixi602 – 6043
    Helixi608 – 62114
    Helixi625 – 6339
    Helixi637 – 6426
    Helixi643 – 6453
    Helixi649 – 66214
    Turni663 – 6653
    Helixi668 – 68215
    Helixi688 – 6903
    Beta strandi778 – 7803

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G3JX-ray2.10A/C133-664[»]
    1JDHX-ray1.90A135-663[»]
    1JPWX-ray2.50A/B/C131-670[»]
    1LUJX-ray2.50A150-663[»]
    1P22X-ray2.95C19-44[»]
    1QZ7X-ray2.20A133-665[»]
    1T08X-ray2.10A146-664[»]
    1TH1X-ray2.50A/B133-664[»]
    2G57NMR-A19-44[»]
    2GL7X-ray2.60A/D138-686[»]
    2Z6HX-ray2.20A138-781[»]
    3DIWX-ray2.10C/D772-781[»]
    3FQNX-ray1.65C30-39[»]
    3FQRX-ray1.70C30-39[»]
    3SL9X-ray2.20A/B/E/G141-305[»]
    3SLAX-ray2.50A/B/C/D/E141-306[»]
    3TX7X-ray2.76A138-663[»]
    4DJSX-ray3.03A148-665[»]
    ProteinModelPortaliP35222.
    SMRiP35222. Positions 19-44, 99-665.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35222.

    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 BCL9Add
    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.
    HOGENOMiHOG000230958.
    HOVERGENiHBG000919.
    InParanoidiP35222.
    KOiK02105.
    OMAiRESHNRA.
    OrthoDBiEOG7X9G6B.
    PhylomeDBiP35222.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35222-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG    50
    NPEEEDVDTS QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP 100
    ETLDEGMQIP STQFDAAHPT NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT 150
    RAIPELTKLL NDEDQVVVNK AAVMVHQLSK KEASRHAIMR SPQMVSAIVR 200
    TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL VKMLGSPVDS 250
    VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC 300
    LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC 350
    SSNKPAIVEA GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG 400
    LLGTLVQLLG SDDINVVTCA AGILSNLTCN NYKNKMMVCQ VGGIEALVRT 450
    VLRAGDREDI TEPAICALRH LTSRHQEAEM AQNAVRLHYG LPVVVKLLHP 500
    PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL VRAHQDTQRR 550
    TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV 600
    QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG 650
    VATYAAAVLF RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI 700
    GAQGEPLGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV 750
    DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L 781
    Length:781
    Mass (Da):85,497
    Last modified:February 1, 1994 - v1
    Checksum:iCB78F165A3EEF86E
    GO
    Isoform 2 (identifier: P35222-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-565: Missing.
         652-653: AT → GK
         654-781: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:88
    Mass (Da):9,501
    Checksum:i7AC26A6AA23E438C
    GO

    Sequence cautioni

    The sequence BAB93475.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231S → R in hepatocellular carcinoma; no effect. 1 Publication
    VAR_017612
    Natural varianti25 – 339Missing in hepatocellular carcinoma.
    VAR_017613
    Natural varianti32 – 321D → A in hepatocellular carcinoma. 1 Publication
    VAR_017614
    Natural varianti32 – 321D → G in PTR and hepatocellular carcinoma. 2 Publications
    VAR_017615
    Natural varianti32 – 321D → Y in PTR, hepatoblastoma and hepatocellular carcinoma. 4 Publications
    Corresponds to variant rs28931588 [ dbSNP | Ensembl ].
    VAR_017616
    Natural varianti33 – 331S → F in PTR, MDB and hepatocellular carcinoma. 3 Publications
    VAR_017617
    Natural varianti33 – 331S → L in hepatocellular carcinoma. 1 Publication
    VAR_017618
    Natural varianti33 – 331S → Y in colorectal cancer and PTR; enhances transactivation of target genes. 2 Publications
    VAR_017619
    Natural varianti34 – 341G → E in PTR. 1 Publication
    VAR_017620
    Natural varianti34 – 341G → R in hepatocellular carcinoma. 1 Publication
    VAR_017621
    Natural varianti34 – 341G → V in hepatoblastoma. 1 Publication
    Corresponds to variant rs28931589 [ dbSNP | Ensembl ].
    VAR_017622
    Natural varianti35 – 351I → S in hepatocellular carcinoma. 1 Publication
    VAR_017623
    Natural varianti37 – 382SG → W in hepatocellular carcinoma. 1 Publication
    VAR_017628
    Natural varianti37 – 371S → A in MDB and hepatocellular carcinoma; enhances transactivation of target genes. 2 Publications
    VAR_017624
    Natural varianti37 – 371S → C in PTR, hepatoblastoma and ovarian cancer. 3 Publications
    VAR_017625
    Natural varianti37 – 371S → F in PTR. 1 Publication
    VAR_017626
    Natural varianti37 – 371S → Y in hepatocellular carcinoma. 1 Publication
    VAR_017627
    Natural varianti41 – 411T → A in hepatoblastoma and hepatocellular carcinoma; also in a desmoid tumor; strongly reduces phosphorylation and degradation; abolishes phosphorylation on Ser-33 and Ser-37 and enhances transactivation of target genes. 5 Publications
    VAR_017629
    Natural varianti41 – 411T → I in PTR, hepatocellular carcinoma and ovarian cancer. 3 Publications
    VAR_017630
    Natural varianti45 – 451S → F in hepatocellular carcinoma. 1 Publication
    VAR_017631
    Natural varianti45 – 451S → P in hepatocellular carcinoma. 1 Publication
    VAR_017632
    Natural varianti45 – 451Missing in colorectal cancer. 1 Publication
    VAR_055430
    Natural varianti688 – 6881M → V.1 Publication
    Corresponds to variant rs4135384 [ dbSNP | Ensembl ].
    VAR_018954

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 565565Missing in isoform 2. 1 PublicationVSP_006984Add
    BLAST
    Alternative sequencei652 – 6532AT → GK in isoform 2. 1 PublicationVSP_006985
    Alternative sequencei654 – 781128Missing in isoform 2. 1 PublicationVSP_006986Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87838 mRNA. Translation: CAA61107.1.
    Z19054 mRNA. Translation: CAA79497.1.
    AF130085 mRNA. Translation: AAG35511.1.
    AY463360 Genomic DNA. Translation: AAR18817.1.
    AK289932 mRNA. Translation: BAF82621.1.
    AC104307 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64625.1.
    BC058926 mRNA. Translation: AAH58926.1.
    AY081165 Genomic DNA. Translation: AAL89457.1.
    AB062292 mRNA. Translation: BAB93475.1. Different initiation.
    CCDSiCCDS2694.1. [P35222-1]
    PIRiA38973.
    RefSeqiNP_001091679.1. NM_001098209.1. [P35222-1]
    NP_001091680.1. NM_001098210.1. [P35222-1]
    NP_001895.1. NM_001904.3. [P35222-1]
    XP_005264943.1. XM_005264886.2. [P35222-1]
    UniGeneiHs.476018.

    Genome annotation databases

    EnsembliENST00000349496; ENSP00000344456; ENSG00000168036. [P35222-1]
    ENST00000396183; ENSP00000379486; ENSG00000168036. [P35222-1]
    ENST00000396185; ENSP00000379488; ENSG00000168036. [P35222-1]
    ENST00000405570; ENSP00000385604; ENSG00000168036. [P35222-1]
    GeneIDi1499.
    KEGGihsa:1499.
    UCSCiuc003ckp.2. human. [P35222-1]
    uc003ckt.1. human. [P35222-2]

    Polymorphism databases

    DMDMi461854.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs
    Wikipedia

    Beta-catenin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87838 mRNA. Translation: CAA61107.1 .
    Z19054 mRNA. Translation: CAA79497.1 .
    AF130085 mRNA. Translation: AAG35511.1 .
    AY463360 Genomic DNA. Translation: AAR18817.1 .
    AK289932 mRNA. Translation: BAF82621.1 .
    AC104307 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64625.1 .
    BC058926 mRNA. Translation: AAH58926.1 .
    AY081165 Genomic DNA. Translation: AAL89457.1 .
    AB062292 mRNA. Translation: BAB93475.1 . Different initiation.
    CCDSi CCDS2694.1. [P35222-1 ]
    PIRi A38973.
    RefSeqi NP_001091679.1. NM_001098209.1. [P35222-1 ]
    NP_001091680.1. NM_001098210.1. [P35222-1 ]
    NP_001895.1. NM_001904.3. [P35222-1 ]
    XP_005264943.1. XM_005264886.2. [P35222-1 ]
    UniGenei Hs.476018.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G3J X-ray 2.10 A/C 133-664 [» ]
    1JDH X-ray 1.90 A 135-663 [» ]
    1JPW X-ray 2.50 A/B/C 131-670 [» ]
    1LUJ X-ray 2.50 A 150-663 [» ]
    1P22 X-ray 2.95 C 19-44 [» ]
    1QZ7 X-ray 2.20 A 133-665 [» ]
    1T08 X-ray 2.10 A 146-664 [» ]
    1TH1 X-ray 2.50 A/B 133-664 [» ]
    2G57 NMR - A 19-44 [» ]
    2GL7 X-ray 2.60 A/D 138-686 [» ]
    2Z6H X-ray 2.20 A 138-781 [» ]
    3DIW X-ray 2.10 C/D 772-781 [» ]
    3FQN X-ray 1.65 C 30-39 [» ]
    3FQR X-ray 1.70 C 30-39 [» ]
    3SL9 X-ray 2.20 A/B/E/G 141-305 [» ]
    3SLA X-ray 2.50 A/B/C/D/E 141-306 [» ]
    3TX7 X-ray 2.76 A 138-663 [» ]
    4DJS X-ray 3.03 A 148-665 [» ]
    ProteinModelPortali P35222.
    SMRi P35222. Positions 19-44, 99-665.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107880. 247 interactions.
    DIPi DIP-122N.
    IntActi P35222. 161 interactions.
    MINTi MINT-105089.
    STRINGi 9606.ENSP00000344456.

    Chemistry

    BindingDBi P35222.
    ChEMBLi CHEMBL3038511.
    DrugBanki DB01356. Lithium.

    PTM databases

    PhosphoSitei P35222.

    Polymorphism databases

    DMDMi 461854.

    Proteomic databases

    MaxQBi P35222.
    PaxDbi P35222.
    PRIDEi P35222.

    Protocols and materials databases

    DNASUi 1499.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000349496 ; ENSP00000344456 ; ENSG00000168036 . [P35222-1 ]
    ENST00000396183 ; ENSP00000379486 ; ENSG00000168036 . [P35222-1 ]
    ENST00000396185 ; ENSP00000379488 ; ENSG00000168036 . [P35222-1 ]
    ENST00000405570 ; ENSP00000385604 ; ENSG00000168036 . [P35222-1 ]
    GeneIDi 1499.
    KEGGi hsa:1499.
    UCSCi uc003ckp.2. human. [P35222-1 ]
    uc003ckt.1. human. [P35222-2 ]

    Organism-specific databases

    CTDi 1499.
    GeneCardsi GC03P041236.
    H-InvDB HIX0163439.
    HIX0163473.
    HGNCi HGNC:2514. CTNNB1.
    HPAi CAB000108.
    CAB001950.
    HPA029159.
    HPA029160.
    MIMi 114500. phenotype.
    116806. gene.
    132600. phenotype.
    155255. phenotype.
    156240. phenotype.
    167000. phenotype.
    181030. phenotype.
    615075. phenotype.
    neXtProti NX_P35222.
    Orphaneti 85142. Aldosterone-producing adenoma.
    178469. Autosomal dominant nonsyndromic intellectual disability.
    54595. Craniopharyngioma.
    873. Desmoid tumor.
    33402. Hepatocellular carcinoma, childhood-onset.
    91414. Pilomatrixoma.
    PharmGKBi PA27013.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297695.
    HOGENOMi HOG000230958.
    HOVERGENi HBG000919.
    InParanoidi P35222.
    KOi K02105.
    OMAi RESHNRA.
    OrthoDBi EOG7X9G6B.
    PhylomeDBi P35222.
    TreeFami TF317997.

    Enzyme and pathway databases

    Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_13579. Apoptotic cleavage of cell adhesion proteins.
    REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
    REACT_172761. Ca2+ pathway.
    REACT_19195. Adherens junctions interactions.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_200777. TCF dependent signaling in response to WNT.
    REACT_200799. binding of TCF/LEF:CTNNB1 to target gene promoters.
    REACT_21402. CDO in myogenesis.
    REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
    SignaLinki P35222.

    Miscellaneous databases

    ChiTaRSi CTNNB1. human.
    EvolutionaryTracei P35222.
    GeneWikii Beta-catenin.
    GenomeRNAii 1499.
    NextBioi 6161.
    PMAP-CutDB P35222.
    PROi P35222.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35222.
    Bgeei P35222.
    CleanExi HS_CTNNB1.
    Genevestigatori P35222.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR013284. Beta-catenin.
    [Graphical view ]
    Pfami PF00514. Arm. 4 hits.
    [Graphical view ]
    PRINTSi PR01869. BCATNINFAMLY.
    SMARTi SM00185. ARM. 12 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50176. ARM_REPEAT. 9 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton."
      Huelsken J., Birchmeier W., Behrens J.
      J. Cell Biol. 127:2061-2069(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Functional prediction of the coding sequences of 75 new genes deduced by analysis of cDNA clones from human fetal liver."
      Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W., Gao F., Liu M., He F.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Fetal liver.
    3. NIEHS SNPs program
      Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-688.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hippocampus.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Skin.
    8. "Oncogenic beta-catenin is required for bone morphogenetic protein 4 expression in human cancer cells."
      Kim J.-S., Crooks H., Dracheva T., Nishanian T.G., Singh B., Jen J., Waldman T.
      Cancer Res. 62:2744-2748(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-312 (ISOFORM 1).
    9. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 258-781 (ISOFORM 1).
      Tissue: Colon adenocarcinoma.
    10. "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.
    11. "Promoter swapping between the genes for a novel zinc finger protein and beta-catenin in pleiomorphic adenomas with t(3;8)(p21;q12) translocations."
      Kas K., Voz M.L., Roeijer E., Astroem A.-K., Meyen E., Stenman G., Van de Ven W.J.M.
      Nat. Genet. 15:170-174(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH PLAG1.
    12. "Conserved mechanism of PLAG1 activation in salivary gland tumors with and without chromosome 8q12 abnormalities: identification of SII as a new fusion partner gene."
      Astroem A.-K., Voz M.L., Kas K., Roeijer E., Wedell B., Mandahl N., Van de Ven W., Mark J., Stenman G.
      Cancer Res. 59:918-923(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH PLAG1.
    13. "Phosphorylation and free pool of beta-catenin are regulated by tyrosine kinases and tyrosine phosphatases during epithelial cell migration."
      Mueller T., Choidas A., Reichmann E., Ullrich A.
      J. Biol. Chem. 274:10173-10183(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STIMULATION OF TYROSINE PHOSPHORYLATION BY EGF, DEPHOSPHORYLATION BY PTPRF.
    14. Cited for: INTERACTION WITH LEF1; APC; AXIN1; AXIN2 AND TCF7L2, PHOSPHORYLATION BY GSK3B, MUTAGENESIS OF PHE-253; HIS-260; LYS-292; LYS-345; TRP-383; ARG-386; ASN-426; LYS-435; ARG-469; HIS-470 AND LYS-508.
    15. "Beta-catenin expression in pilomatrixomas. Relationship with beta-catenin gene mutations and comparison with beta-catenin expression in normal hair follicles."
      Moreno-Bueno G., Gamallo C., Perez-Gallego L., Contreras F., Palacios J.
      Br. J. Dermatol. 145:576-581(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, VARIANT PTR TYR-32.
    16. "Chromatin-specific regulation of LEF-1-beta-catenin transcription activation and inhibition in vitro."
      Tutter A.V., Fryer C.J., Jones K.A.
      Genes Dev. 15:3342-3354(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LEF1, INHIBITION BY CTNNBIP1 BINDING.
    17. "Regulation of beta-catenin structure and activity by tyrosine phosphorylation."
      Piedra J., Martinez D., Castano J., Miravet S., Dunach M., de Herreros A.G.
      J. Biol. Chem. 276:20436-20443(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-86 AND TYR-654, INTERACTION WITH TBP, MUTAGENESIS OF TYR-654.
    18. "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.
    19. "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses."
      Matsuzawa S., Reed J.C.
      Mol. Cell 7:915-926(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIAH1, DEGRADATION.
    20. "Siah-1 mediates a novel beta-catenin degradation pathway linking p53 to the adenomatous polyposis coli protein."
      Liu J., Stevens J., Rote C.A., Yost H.J., Hu Y., Neufeld K.L., White R.L., Matsunami N.
      Mol. Cell 7:927-936(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIAH1, DEGRADATION.
    21. "Genetic alteration of the beta-catenin gene (CTNNB1) in human lung cancer and malignant mesothelioma and identification of a new 3p21.3 homozygous deletion."
      Shigemitsu K., Sekido Y., Usami N., Mori S., Sato M., Horio Y., Hasegawa Y., Bader S.A., Gazdar A.F., Minna J.D., Hida T., Yoshioka H., Imaizumi M., Ueda Y., Takahashi M., Shimokata K.
      Oncogene 20:4249-4257(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MESOM.
    22. "Physical and functional interaction between receptor-like protein tyrosine phosphatase PCP-2 and beta-catenin."
      Yan H.-X., He Y.-Q., Dong H., Zhang P., Zeng J.-Z., Cao H.-F., Wu M.-C., Wang H.-Y.
      Biochemistry 41:15854-15860(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPRU.
    23. "Characterisation of the phosphorylation of beta-catenin at the GSK-3 priming site Ser45."
      Hagen T., Vidal-Puig A.
      Biochem. Biophys. Res. Commun. 294:324-328(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-45, CHARACTERIZATION OF VARIANT HEPATOCELLULAR CARCINOMA ALA-41, CHARACTERIZATION OF VARIANT DESMOID TUMOR ALA-41, CHARACTERIZATION OF VARIANT HEPATOBLASTOMA ALA-41.
    24. "Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape."
      Walters R.W., Freimuth P., Moninger T.O., Ganske I., Zabner J., Welsh M.J.
      Cell 110:789-799(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CXADR.
    25. "Identification of two novel regulated serines in the N-terminus of beta-catenin."
      van Noort M., van de Wetering M., Clevers H.
      Exp. Cell Res. 276:264-272(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-23 AND SER-29 BY GSK3B, PHOSPHORYLATION AT THR-41, MUTAGENESIS OF SER-29, CHARACTERIZATION OF VARIANTS HEPATOCELLULAR CARCINOMA ARG-23; ALA-37 AND ALA-41, CHARACTERIZATION OF VARIANT PTR TYR-33, CHARACTERIZATION OF VARIANT MDB ALA-37, CHARACTERIZATION OF VARIANT DESMOID TUMOR ALA-41, CHARACTERIZATION OF VARIANT HEPATOBLASTOMA ALA-41.
    26. "Wnt signaling controls the phosphorylation status of beta-catenin."
      van Noort M., Meeldijk J., van der Zee R., Destree O., Clevers H.
      J. Biol. Chem. 277:17901-17905(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: WNT SIGNALING MODULATES PHOSPHORYLATION.
    27. "Regulation of S33/S37 phosphorylated beta-catenin in normal and transformed cells."
      Sadot E., Conacci-Sorrell M., Zhurinsky J., Shnizer D., Lando Z., Zharhary D., Kam Z., Ben-Ze'ev A., Geiger B.
      J. Cell Sci. 115:2771-2780(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION OF PHOSPHORYLATED CTNNB1 WITH BTRC.
    28. "The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)."
      Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.
      Oncogene 21:7067-7076(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPRJ.
    29. "The emergence of protocadherin-PC expression during the acquisition of apoptosis-resistance by prostate cancer cells."
      Chen M.-W., Vacherot F., De La Taille A., Gil-Diez-De-Medina S., Shen R., Friedman R.A., Burchardt M., Chopin D.K., Buttyan R.
      Oncogene 21:7861-7871(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PCDH11Y.
    30. "EBP50, a beta-catenin-associating protein, enhances Wnt signaling and is over-expressed in hepatocellular carcinoma."
      Shibata T., Chuma M., Kokubu A., Sakamoto M., Hirohashi S.
      Hepatology 38:178-186(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC9A3R1.
    31. "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.
    32. "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.
    33. "Novel membrane protein shrew-1 targets to cadherin-mediated junctions in polarized epithelial cells."
      Bharti S., Handrow-Metzmacher H., Zickenheiner S., Zeitvogel A., Baumann R., Starzinski-Powitz A.
      Mol. Biol. Cell 15:397-406(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AJAP1.
      Tissue: Brain.
    34. "E-cadherin regulates human Nanos1, which interacts with p120ctn and induces tumor cell migration and invasion."
      Strumane K., Bonnomet A., Stove C., Vandenbroucke R., Nawrocki-Raby B., Bruyneel E., Mareel M., Birembaut P., Berx G., van Roy F.
      Cancer Res. 66:10007-10015(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NANOS1.
    35. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    36. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EMD.
    37. "MUC1 inhibits cell proliferation by a beta-catenin-dependent mechanism."
      Lillehoj E.P., Lu W., Kiser T., Goldblum S.E., Kim K.C.
      Biochim. Biophys. Acta 1773:1028-1038(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MUC1, SUBCELLULAR LOCATION, FUNCTION.
    38. "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, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    39. "cdk5 modulates beta- and delta-catenin/Pin1 interactions in neuronal cells."
      Munoz J.P., Huichalaf C.H., Orellana D., Maccioni R.B.
      J. Cell. Biochem. 100:738-749(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-191 AND SER-246, INTERACTION WITH CDK5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    40. "The tumor suppressor Fhit acts as a repressor of beta-catenin transcriptional activity."
      Weiske J., Albring K.F., Huber O.
      Proc. Natl. Acad. Sci. U.S.A. 104:20344-20349(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FHIT, IDENTIFICATION IN A COMPLEX WITH LEF1, FUNCTION.
    41. Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH NEK2.
    42. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-556 AND SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    43. "Sox7 Is an independent checkpoint for beta-catenin function in prostate and colon epithelial cells."
      Guo L., Zhong D., Lau S., Liu X., Dong X.Y., Sun X., Yang V.W., Vertino P.M., Moreno C.S., Varma V., Dong J.T., Zhou W.
      Mol. Cancer Res. 6:1421-1430(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SOX7.
    44. "CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-catenin target genes."
      Thompson B.A., Tremblay V., Lin G., Bochar D.A.
      Mol. Cell. Biol. 28:3894-3904(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHD8.
    45. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    46. "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.
    47. "Down-regulation of death-associated protein kinase-2 is required for beta-catenin-induced anoikis resistance of malignant epithelial cells."
      Li H., Ray G., Yoo B.H., Erdogan M., Rosen K.V.
      J. Biol. Chem. 284:2012-2022(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    48. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    49. "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.
    50. "The phospholipid-binding protein SESTD1 is a novel regulator of the transient receptor potential channels TRPC4 and TRPC5."
      Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C.
      J. Biol. Chem. 285:12426-12434(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SESTD1.
    51. "Cell-cell contact formation governs Ca2+ signaling by TRPC4 in the vascular endothelium: evidence for a regulatory TRPC4-beta-catenin interaction."
      Graziani A., Poteser M., Heupel W.M., Schleifer H., Krenn M., Drenckhahn D., Romanin C., Baumgartner W., Groschner K.
      J. Biol. Chem. 285:4213-4223(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRPC4.
    52. "Characterization of a novel human CDK5 splicing variant that inhibits Wnt/beta-catenin signaling."
      Li Q., Liu X., Zhang M., Ye G., Qiao Q., Ling Y., Wu Y., Zhang Y., Yu L.
      Mol. Biol. Rep. 37:2415-2421(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDK5.
    53. "Identification of beta-catenin as a target of the intracellular tyrosine kinase PTK6."
      Palka-Hamblin H.L., Gierut J.J., Bie W., Brauer P.M., Zheng Y., Asara J.M., Tyner A.L.
      J. Cell Sci. 123:236-245(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-64; TYR-142; TYR-331 AND TYR-333, INTERACTION WITH PTK6, MUTAGENESIS OF TYR-64.
    54. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    55. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    56. "Compartmentalized CDK2 is connected with SHP-1 and beta-catenin and regulates insulin internalization."
      Fiset A., Xu E., Bergeron S., Marette A., Pelletier G., Siminovitch K.A., Olivier M., Beauchemin N., Faure R.L.
      Cell. Signal. 23:911-919(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN INSULIN INTERNALIZATION, SUBCELLULAR LOCATION, INTERACTION WITH CDK2, PHOSPHORYLATION BY CDK2.
    57. Cited for: INTERACTION WITH PKT7.
    58. "Crystal structure of the human N-Myc downstream-regulated gene 2 protein provides insight into its role as a tumor suppressor."
      Hwang J., Kim Y., Kang H.B., Jaroszewski L., Deacon A.M., Lee H., Choi W.C., Kim K.J., Kim C.H., Kang B.S., Lee J.O., Oh T.K., Kim J.W., Wilson I.A., Kim M.H.
      J. Biol. Chem. 286:12450-12460(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NDRG2.
    59. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    60. "The tumor suppressor HINT1 regulates MITF and beta-catenin transcriptional activity in melanoma cells."
      Genovese G., Ghosh P., Li H., Rettino A., Sioletic S., Cittadini A., Sgambato A.
      Cell Cycle 11:2206-2215(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH HINT1 AND MITF, FUNCTION.
    61. "Kindlin 2 forms a transcriptional complex with beta-catenin and TCF4 to enhance Wnt signalling."
      Yu Y., Wu J., Wang Y., Zhao T., Ma B., Liu Y., Fang W., Zhu W.G., Zhang H.
      EMBO Rep. 13:750-758(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FERMT2, IDENTIFICATION IN A COMPLEX WITH FERMT2 AND TCF7L2, SUBCELLULAR LOCATION.
    62. "Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells."
      Satow R., Shitashige M., Jigami T., Fukami K., Honda K., Kitabayashi I., Yamada T.
      Gastroenterology 142:572-581(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PML.
    63. Cited for: INVOLVEMENT IN MRD19.
    64. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    65. "Crystal structure of a beta-catenin/Tcf complex."
      Graham T.A., Weaver C., Mao F., Kimelman D., Xu W.
      Cell 103:885-896(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 133-664.
    66. "Tcf4 can specifically recognize beta-catenin using alternative conformations."
      Graham T.A., Ferkey D.M., Mao F., Kimelman D., Xu W.
      Nat. Struct. Biol. 8:1048-1052(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-664 IN COMPLEX WITH TCF7L2, MUTAGENESIS OF LYS-312 AND LYS-435.
    67. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-668 IN COMPLEX WITH TCF7L2.
    68. "The crystal structure of the beta-catenin/ICAT complex reveals the inhibitory mechanism of ICAT."
      Graham T.A., Clements W.K., Kimelman D., Xu W.
      Mol. Cell 10:563-571(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-664 IN COMPLEX WITH CTNNBIP1, MUTAGENESIS OF PHE-660 AND ARG-661.
    69. "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: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-136 IN COMPLEX WITH BCL9 AND TCF7L2, INTERACTION WITH BCL9; BCL9L CDH3 AND TCF7L2, MUTAGENESIS OF TYR-142; LEU-156; LEU-159 AND LEU-178.
    70. "Activation of beta-catenin-Tcf signaling in colon cancer by mutations in beta-catenin or APC."
      Morin P.J., Sparks A.B., Korinek V., Barker N., Clevers H., Vogelstein B., Kinzler K.W.
      Science 275:1787-1790(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS COLORECTAL CANCER TYR-33 AND SER-45 DEL.
    71. "Childhood hepatoblastomas frequently carry a mutated degradation targeting box of the beta-catenin gene."
      Koch A., Denkhaus D., Albrecht S., Leuschner I., von Schweinitz D., Pietsch T.
      Cancer Res. 59:269-273(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HEPATOBLASTOMA TYR-32; VAL-34; CYS-37 AND ALA-41.
    72. "Beta-catenin accumulation and mutation of the CTNNB1 gene in hepatoblastoma."
      Blaeker H., Hofmann W.J., Rieker R.J., Penzel R., Graf M., Otto H.F.
      Genes Chromosomes Cancer 25:399-402(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HEPATOBLASTOMA ALA-41.
    73. "Mutational analysis of beta-catenin gene in Japanese ovarian carcinomas: frequent mutations in endometrioid carcinomas."
      Sagae S., Kobayashi K., Nishioka Y., Sugimura M., Ishioka S., Nagata M., Terasawa K., Tokino T., Kudo R.
      Jpn. J. Cancer Res. 90:510-515(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OVARIAN CANCER CYS-37; ILE-41 AND ALA-41.
    74. "A novel case of a sporadic desmoid tumour with mutation of the beta catenin gene."
      Shitoh K., Konishi F., Iijima T., Ohdaira T., Sakai K., Kanazawa K., Miyaki M.
      J. Clin. Pathol. 52:695-696(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DESMOID TUMOR ALA-41.
    75. "A common human skin tumour is caused by activating mutations in beta-catenin."
      Chan E.F., Gat U., McNiff J.M., Fuchs E.
      Nat. Genet. 21:410-413(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PTR GLY-32; TYR-32; PHE-33; TYR-33; GLU-34; CYS-37; PHE-37 AND ILE-41.
    76. "Beta-catenin mutations in hepatocellular carcinoma correlate with a low rate of loss of heterozygosity."
      Legoix P., Bluteau O., Bayer J., Perret C., Balabaud C., Belghiti J., Franco D., Thomas G., Laurent-Puig P., Zucman-Rossi J.
      Oncogene 18:4044-4046(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HEPATOCELLULAR CARCINOMA ARG-23; 25-TRP--SER-33 DEL; ALA-32; GLY-32; TYR-32; LEU-33; PHE-33; ARG-34; SER-35; ALA-37; 37-SER-GLY-38 DELINS TRP; TYR-37; ALA-41; ILE-41; PHE-45 AND PRO-45.
    77. Cited for: VARIANTS MDB PHE-33 AND ALA-37.

    Entry informationi

    Entry nameiCTNB1_HUMAN
    AccessioniPrimary (citable) accession number: P35222
    Secondary accession number(s): A8K1L7
    , Q8NEW9, Q8NI94, Q9H391
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 184 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3