ID CTNB1_BOVIN Reviewed; 781 AA. AC Q0VCX4; A7E3R2; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 152. DE RecName: Full=Catenin beta-1 {ECO:0000250|UniProtKB:Q02248}; DE AltName: Full=Beta-catenin {ECO:0000303|PubMed:10873669}; GN Name=CTNNB1 {ECO:0000250|UniProtKB:Q02248}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Fetal skin; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP INTERACTION WITH RAPGEF2. RX PubMed=10873669; DOI=10.1006/bbrc.2000.3002; RA Kawajiri A., Itoh N., Fukata M., Nakagawa M., Yamaga M., Iwamatsu A., RA Kaibuchi K.; RT "Identification of a novel beta-catenin-interacting protein."; RL Biochem. Biophys. Res. Commun. 273:712-717(2000). CC -!- FUNCTION: Key downstream component of the canonical Wnt signaling CC pathway (By similarity). In the absence of Wnt, forms a complex with CC AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on CC N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC CC and its subsequent degradation by the proteasome. In the presence of CC Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, CC where it acts as a coactivator for transcription factors of the TCF/LEF CC family, leading to activate Wnt responsive genes (By similarity). CC Involved in the regulation of cell adhesion, as component of an E- CC cadherin:catenin adhesion complex (By similarity). Acts as a negative CC regulator of centrosome cohesion. Involved in the CC CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks CC anoikis of malignant kidney and intestinal epithelial cells and CC promotes their anchorage-independent growth by down-regulating DAPK2. CC Disrupts PML function and PML-NB formation by inhibiting RANBP2- CC mediated sumoylation of PML (By similarity). Promotes neurogenesis by CC maintaining sympathetic neuroblasts within the cell cycle. Involved in CC chondrocyte differentiation via interaction with SOX9: SOX9-binding CC competes with the binding sites of TCF/LEF within CTNNB1, thereby CC inhibiting the Wnt signaling (By similarity). Acts as a positive CC regulator of odontoblast differentiation during mesenchymal tooth germ CC formation, via promoting the transcription of differentiation factors CC such as LEF1, BMP2 and BMP4 (By similarity). Activity is repressed in a CC MSX1-mediated manner at the bell stage of mesenchymal tooth germ CC formation which prevents premature differentiation of odontoblasts (By CC similarity). {ECO:0000250|UniProtKB:P35222, CC ECO:0000250|UniProtKB:Q02248}. CC -!- SUBUNIT: Two separate complex-associated pools are found in the CC cytoplasm. The majority is present as component of an E-cadherin/ CC catenin adhesion complex composed of at least E-cadherin/CDH1 and beta- CC catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is CC located to adherens junctions. The stable association of CTNNA1 is CC controversial as CTNNA1 was shown not to bind to F-actin when assembled CC in the complex. Alternatively, the CTNNA1-containing complex may be CC linked to F-actin by other proteins such as LIMA1. Another cytoplasmic CC pool is part of a large complex containing AXIN1, AXIN2, APC, CSNK1A1 CC and GSK3B that promotes phosphorylation on N-terminal Ser and Thr CC residues and ubiquitination of CTNNB1 via BTRC and its subsequent CC degradation by the proteasome. Wnt-dependent activation of DVL CC antagonizes the action of GSK3B. When GSK3B activity is inhibited the CC complex dissociates, CTNNB1 is dephosphorylated and is no longer CC targeted for destruction. The stabilized protein translocates to the CC nucleus, where it binds TCF/LEF-1 family members, BCL9, BCL9L and CC possibly also RUVBL1 and CHD8. Binds CTNNBIP and EP300. CTNNB1 forms a CC ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 CC binding. Interacts with TAX1BP3 (via the PDZ domain); this interaction CC inhibits the transcriptional activity of CTNNB1. Interacts with AJAP1, CC BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds NHERF1. Interacts with CC GLIS2 and SLC30A9. Interacts with XIRP1 and MUC1. Interacts with PTPRU CC (via the cytoplasmic juxtamembrane domain) and with EMD. Interacts with CC SCRIB. Interacts with TNIK. Interacts with SESTD1 and TRPC4. Interacts CC directly with AXIN1; the interaction is regulated by CDK2 CC phosphorylation of AXIN1. Interacts with CAV1. Interacts with TRPV4. CC The TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with CC VCL. Interacts with PTPRJ. Interacts with PKT7. Interacts with FAT1 CC (via the cytoplasmic domain). Interacts with NANOS1 and NDRG2. CC Interacts with NEK2, CDK2 and CDK5. Interacts with PTK6. Interacts with CC SOX7; this interaction may lead to proteasomal degradation of active CC CTNNB1 and thus inhibition of Wnt/beta-catenin-stimulated CC transcription. Identified in a complex with HINT1 and MITF. Interacts CC with FHIT. The CTNNB1 and TCF4 complex interacts with PML. Interacts CC with FERMT2. Identified in a complex with TCF4 and FERMT2. Interacts CC with RORA. May interact with P-cadherin/CDH3 (By similarity). Interacts CC with RAPGEF2. Interacts with RNF220 (By similarity). Interacts with CC CTNND2 (By similarity). Interacts (via the C-terminal region) with CBY1 CC (By similarity). The complex composed, at least, of APC, CTNNB1 and CC GSK3B interacts with JPT1; the interaction requires the inactive form CC of GSK3B (phosphorylated at 'Ser-9'). Interacts with DLG5 (By CC similarity). Interacts with FAM53B; promoting translocation to the CC nucleus. Interacts with TMEM170B (By similarity). Interacts with AHI1 CC (By similarity). Interacts with GID8 (By similarity). Component of an CC cadherin:catenin adhesion complex composed of at least of CDH26, beta- CC catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By CC similarity). Forms a complex comprising APPL1, RUVBL2, APPL2, HDAC1 and CC HDAC2 (By similarity). Interacts with IRF2BPL; mediates the CC ubiquitination and degradation of CTNNB1 (By similarity). Interacts CC with LMBR1L and AMFR (By similarity). Interacts with LMBR1L (By CC similarity). Interacts with SOX30; prevents interaction of CTNNB1 with CC TCF7L2/TCF4 and leads to inhibition of Wnt signaling (By similarity). CC Interacts with SOX9; inhibiting CTNNB1 activity by competing with the CC binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt CC signaling (By similarity). Interacts with SPN/CD43 cytoplasmic tail (By CC similarity). Interacts (when phosphorylated at Tyr-333) with isoform M2 CC of PKM (PKM2); promoting transcription activation (By similarity). CC Interacts with PKP2 (via HEAD domain) (By similarity). Interacts with CC CDH1 (By similarity). Interacts (when unphosphorylated) with FLYWCH1, CC perhaps preventing interaction of CTNNB1 with TCF4, and thereby CC regulating transcription activation; phosphorylation of CTNNB1 may CC inhibit the interaction (By similarity). Interacts (via the central CC armadillo domains) with probable transcriptional regulator ADNP (via N- CC terminal region); interaction is direct and stabilizes CTNNB1 by CC modulating its phosphorylation by glycogen synthase kinase-3 beta GSK3B CC (By similarity). {ECO:0000250|UniProtKB:P35222, CC ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:10873669}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35222}. Nucleus CC {ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:B6V8E6}. Cell junction, adherens junction CC {ECO:0000250|UniProtKB:Q02248}. Cell junction CC {ECO:0000250|UniProtKB:B6V8E6}. Cell membrane CC {ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000250|UniProtKB:P35222}. CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P35222}. CC Synapse {ECO:0000250|UniProtKB:Q02248}. Cytoplasm, cytoskeleton, cilium CC basal body {ECO:0000250|UniProtKB:Q02248}. Note=Colocalized with CC RAPGEF2 and TJP1 at cell-cell contacts (By similarity). Cytoplasmic CC when it is un-stable (highly phosphorylated) or bound to CDH1. CC Translocates to the nucleus when it is stabilized (low level of CC phosphorylation). Interaction with GLIS2 and MUC1 promotes nuclear CC translocation. Interaction with EMD inhibits nuclear localization. The CC majority of beta-catenin is localized to the cell membrane. In CC interphase, colocalizes with CROCC between CEP250 puncta at the CC proximal end of centrioles, and this localization is dependent on CROCC CC and CEP250. In mitosis, when NEK2 activity increases, it localizes to CC centrosomes at spindle poles independent of CROCC. Colocalizes with CC CDK5 in the cell-cell contacts and plasma membrane of undifferentiated CC and differentiated neuroblastoma cells. Interaction with FAM53B CC promotes translocation to the nucleus (By similarity). CC {ECO:0000250|UniProtKB:B6V8E6, ECO:0000250|UniProtKB:P35222}. CC -!- PTM: Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 CC by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-33. CC Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. CC Phosphorylated on Ser-33 and Ser-37 by HIPK2. This phosphorylation CC triggers proteasomal degradation. Phosphorylation at Ser-552 by AMPK CC promotes stabilization of the protein, enhancing TCF/LEF-mediated CC transcription. Phosphorylation on Ser-191 and Ser-246 by CDK5. CC Phosphorylation by CDK2 regulates insulin internalization. CC Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or Tyr-333 with CC the predominant site at Tyr-64 is not essential for inhibition of CC transcriptional activity. Phosphorylation by SRC at Tyr-333 promotes CC interaction with isoform M2 of PKM (PKM2); promoting transcription CC activation. {ECO:0000250|UniProtKB:P35222, CC ECO:0000250|UniProtKB:Q02248}. CC -!- PTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when CC phosphorylated by GSK3B, leading to its degradation. Ubiquitinated by a CC E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, CC APC and TBL1X, leading to its subsequent proteasomal degradation (By CC similarity). Ubiquitinated and degraded following interaction with SOX9 CC (By similarity). {ECO:0000250|UniProtKB:P35222, CC ECO:0000250|UniProtKB:Q02248}. CC -!- PTM: S-nitrosylation at Cys-619 within adherens junctions promotes CC VEGF-induced, NO-dependent endothelial cell permeability by disrupting CC interaction with E-cadherin, thus mediating disassembly adherens CC junctions. {ECO:0000250}. CC -!- PTM: O-glycosylation at Ser-23 decreases nuclear localization and CC transcriptional activity, and increases localization to the plasma CC membrane and interaction with E-cadherin CDH1. CC {ECO:0000250|UniProtKB:Q96S06}. CC -!- PTM: Deacetylated at Lys-49 by SIRT1. {ECO:0000250|UniProtKB:P35222}. CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BT030683; ABS44999.1; -; mRNA. DR EMBL; BC119949; AAI19950.1; -; mRNA. DR RefSeq; NP_001069609.1; NM_001076141.1. DR RefSeq; XP_005222580.1; XM_005222523.3. DR RefSeq; XP_005222581.1; XM_005222524.3. DR RefSeq; XP_005222582.1; XM_005222525.3. DR AlphaFoldDB; Q0VCX4; -. DR SMR; Q0VCX4; -. DR IntAct; Q0VCX4; 1. DR STRING; 9913.ENSBTAP00000021838; -. DR GlyCosmos; Q0VCX4; 1 site, No reported glycans. DR iPTMnet; Q0VCX4; -. DR PaxDb; 9913-ENSBTAP00000021838; -. DR PeptideAtlas; Q0VCX4; -. DR Ensembl; ENSBTAT00000021838.5; ENSBTAP00000021838.4; ENSBTAG00000016420.5. DR GeneID; 539003; -. DR KEGG; bta:539003; -. DR CTD; 1499; -. DR VEuPathDB; HostDB:ENSBTAG00000016420; -. DR VGNC; VGNC:27802; CTNNB1. DR eggNOG; KOG4203; Eukaryota. DR GeneTree; ENSGT00940000155471; -. DR HOGENOM; CLU_008757_1_1_1; -. DR InParanoid; Q0VCX4; -. DR OMA; YPKLVYT; -. DR OrthoDB; 50711at2759; -. DR TreeFam; TF317997; -. DR Reactome; R-BTA-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-BTA-196299; Beta-catenin phosphorylation cascade. DR Reactome; R-BTA-201681; TCF dependent signaling in response to WNT. DR Reactome; R-BTA-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-BTA-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production. DR Reactome; R-BTA-351906; Apoptotic cleavage of cell adhesion proteins. DR Reactome; R-BTA-3769402; Deactivation of the beta-catenin transactivating complex. DR Reactome; R-BTA-4086398; Ca2+ pathway. DR Reactome; R-BTA-418990; Adherens junctions interactions. DR Reactome; R-BTA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane. DR Reactome; R-BTA-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-BTA-525793; Myogenesis. DR Reactome; R-BTA-5626467; RHO GTPases activate IQGAPs. DR Reactome; R-BTA-8951430; RUNX3 regulates WNT signaling. DR Reactome; R-BTA-9762292; Regulation of CDH11 function. DR Proteomes; UP000009136; Chromosome 22. DR Bgee; ENSBTAG00000016420; Expressed in thyroid gland and 104 other cell types or tissues. DR ExpressionAtlas; Q0VCX4; baseline and differential. DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB. DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl. DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl. DR GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB. DR GO; GO:1990711; C:beta-catenin-ICAT complex; IEA:Ensembl. DR GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISS:UniProtKB. DR GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl. DR GO; GO:0016342; C:catenin complex; ISS:UniProtKB. DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB. DR GO; GO:0030054; C:cell junction; ISS:UniProtKB. DR GO; GO:0071944; C:cell periphery; ISS:UniProtKB. DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0000791; C:euchromatin; IEA:Ensembl. DR GO; GO:0005916; C:fascia adherens; IEA:Ensembl. DR GO; GO:0016600; C:flotillin complex; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl. DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0031528; C:microvillus membrane; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0099092; C:postsynaptic density, intracellular component; IEA:Ensembl. DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl. DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IEA:Ensembl. DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl. DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IEA:Ensembl. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; ISS:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB. DR GO; GO:1990909; C:Wnt signalosome; IEA:Ensembl. DR GO; GO:0030018; C:Z disc; IEA:Ensembl. DR GO; GO:0045294; F:alpha-catenin binding; IBA:GO_Central. DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central. DR GO; GO:1990226; F:histone methyltransferase binding; IEA:Ensembl. DR GO; GO:0070411; F:I-SMAD binding; IEA:Ensembl. DR GO; GO:0030331; F:nuclear estrogen receptor binding; IEA:Ensembl. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl. DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB. DR GO; GO:0001222; F:transcription corepressor binding; IEA:Ensembl. DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl. DR GO; GO:0090425; P:acinar cell differentiation; IEA:Ensembl. DR GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB. DR GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl. DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0036520; P:astrocyte-dopaminergic neuron signaling; IEA:Ensembl. DR GO; GO:0045453; P:bone resorption; IEA:Ensembl. DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl. DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl. DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISS:UniProtKB. DR GO; GO:0044338; P:canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB. DR GO; GO:0001708; P:cell fate specification; IEA:Ensembl. DR GO; GO:0048469; P:cell maturation; IEA:Ensembl. DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB. DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl. DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB. DR GO; GO:0071681; P:cellular response to indole-3-methanol; ISS:UniProtKB. DR GO; GO:0022009; P:central nervous system vasculogenesis; IEA:Ensembl. DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl. DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl. DR GO; GO:0061550; P:cranial ganglion development; IEA:Ensembl. DR GO; GO:1904888; P:cranial skeletal system development; IEA:Ensembl. DR GO; GO:1990791; P:dorsal root ganglion development; IEA:Ensembl. DR GO; GO:0009950; P:dorsal/ventral axis specification; IEA:Ensembl. DR GO; GO:0007398; P:ectoderm development; IEA:Ensembl. DR GO; GO:0000578; P:embryonic axis specification; IEA:Ensembl. DR GO; GO:1990403; P:embryonic brain development; IEA:Ensembl. DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl. DR GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl. DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl. DR GO; GO:0035050; P:embryonic heart tube development; IEA:Ensembl. DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl. DR GO; GO:0036023; P:embryonic skeletal limb joint morphogenesis; IEA:Ensembl. DR GO; GO:0001711; P:endodermal cell fate commitment; IEA:Ensembl. DR GO; GO:0061154; P:endothelial tube morphogenesis; ISS:UniProtKB. DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IEA:Ensembl. DR GO; GO:0060767; P:epithelial cell proliferation involved in prostate gland development; IEA:Ensembl. DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl. DR GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl. DR GO; GO:1990963; P:establishment of blood-retinal barrier; IEA:Ensembl. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0061198; P:fungiform papilla formation; IEA:Ensembl. DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl. DR GO; GO:0035112; P:genitalia morphogenesis; IEA:Ensembl. DR GO; GO:0007403; P:glial cell fate determination; IEA:Ensembl. DR GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl. DR GO; GO:0060789; P:hair follicle placode formation; IEA:Ensembl. DR GO; GO:0030902; P:hindbrain development; IEA:Ensembl. DR GO; GO:0021854; P:hypothalamus development; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl. DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IEA:Ensembl. DR GO; GO:0060487; P:lung epithelial cell differentiation; IEA:Ensembl. DR GO; GO:0060492; P:lung induction; IEA:Ensembl. DR GO; GO:0060484; P:lung-associated mesenchyme development; IEA:Ensembl. DR GO; GO:0030539; P:male genitalia development; IEA:Ensembl. DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl. DR GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IEA:Ensembl. DR GO; GO:0003338; P:metanephros morphogenesis; IEA:Ensembl. DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; IEA:Ensembl. DR GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl. DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; IEA:Ensembl. DR GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; ISS:UniProtKB. DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IEA:Ensembl. DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl. DR GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0072079; P:nephron tubule formation; IEA:Ensembl. DR GO; GO:0001840; P:neural plate development; IEA:Ensembl. DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl. DR GO; GO:0048664; P:neuron fate determination; IEA:Ensembl. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl. DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl. DR GO; GO:0048599; P:oocyte development; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl. DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl. DR GO; GO:0060066; P:oviduct development; IEA:Ensembl. DR GO; GO:0031016; P:pancreas development; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0061047; P:positive regulation of branching involved in lung morphogenesis; IEA:Ensembl. DR GO; GO:2000017; P:positive regulation of determination of dorsal identity; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IEA:Ensembl. DR GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl. DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl. DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl. DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl. DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IEA:Ensembl. DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:UniProtKB. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:1901331; P:positive regulation of odontoblast differentiation; IEA:Ensembl. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl. DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IEA:Ensembl. DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:Ensembl. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl. DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl. DR GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl. DR GO; GO:0090279; P:regulation of calcium ion import; ISS:UniProtKB. DR GO; GO:0030997; P:regulation of centriole-centriole cohesion; ISS:UniProtKB. DR GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; ISS:UniProtKB. DR GO; GO:0031641; P:regulation of myelination; IEA:Ensembl. DR GO; GO:0072182; P:regulation of nephron tubule epithelial cell differentiation; IEA:Ensembl. DR GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB. DR GO; GO:0031396; P:regulation of protein ubiquitination; IEA:Ensembl. DR GO; GO:0003266; P:regulation of secondary heart field cardioblast proliferation; IEA:Ensembl. DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB. DR GO; GO:0051963; P:regulation of synapse assembly; IEA:Ensembl. DR GO; GO:0042129; P:regulation of T cell proliferation; IEA:Ensembl. DR GO; GO:0051884; P:regulation of timing of anagen; IEA:Ensembl. DR GO; GO:0072053; P:renal inner medulla development; IEA:Ensembl. DR GO; GO:0072054; P:renal outer medulla development; IEA:Ensembl. DR GO; GO:0072033; P:renal vesicle formation; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; ISS:UniProtKB. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl. DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl. DR GO; GO:0061549; P:sympathetic ganglion development; ISS:UniProtKB. DR GO; GO:0050808; P:synapse organization; IEA:Ensembl. DR GO; GO:0097091; P:synaptic vesicle clustering; IEA:Ensembl. DR GO; GO:0048489; P:synaptic vesicle transport; IEA:Ensembl. DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl. DR GO; GO:0048538; P:thymus development; IEA:Ensembl. DR GO; GO:0060440; P:trachea formation; IEA:Ensembl. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl. DR CDD; cd21724; CTNNAbd_CTNNB1; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000225; Armadillo. DR InterPro; IPR013284; Beta-catenin. DR PANTHER; PTHR45976; ARMADILLO SEGMENT POLARITY PROTEIN; 1. DR PANTHER; PTHR45976:SF4; CATENIN BETA-1; 1. DR Pfam; PF00514; Arm; 4. DR PRINTS; PR01869; BCATNINFAMLY. DR SMART; SM00185; ARM; 12. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50176; ARM_REPEAT; 9. PE 1: Evidence at protein level; KW Acetylation; Activator; Cell adhesion; Cell junction; Cell membrane; KW Cell projection; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane; KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW S-nitrosylation; Synapse; Transcription; Transcription regulation; KW Ubl conjugation; Wnt signaling pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P35222" FT CHAIN 2..781 FT /note="Catenin beta-1" FT /id="PRO_0000282881" FT REPEAT 151..191 FT /note="ARM 1" FT REPEAT 193..234 FT /note="ARM 2" FT REPEAT 235..276 FT /note="ARM 3" FT REPEAT 277..318 FT /note="ARM 4" FT REPEAT 319..360 FT /note="ARM 5" FT REPEAT 361..389 FT /note="ARM 6" FT REPEAT 400..441 FT /note="ARM 7" FT REPEAT 442..484 FT /note="ARM 8" FT REPEAT 489..530 FT /note="ARM 9" FT REPEAT 531..571 FT /note="ARM 10" FT REPEAT 594..636 FT /note="ARM 11" FT REPEAT 637..666 FT /note="ARM 12" FT REGION 2..23 FT /note="Interaction with VCL" FT /evidence="ECO:0000250" FT REGION 34..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 156..178 FT /note="Interaction with BCL9" FT /evidence="ECO:0000250" FT REGION 705..781 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 772..781 FT /note="Interaction with SCRIB" FT /evidence="ECO:0000250" FT COMPBIAS 34..48 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 23 FT /note="Phosphoserine; by GSK3-beta; alternate" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 29 FT /note="Phosphoserine; by GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 33 FT /note="Phosphoserine; by GSK3-beta and HIPK2" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 37 FT /note="Phosphoserine; by GSK3-beta and HIPK2" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 41 FT /note="Phosphothreonine; by GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 49 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 64 FT /note="Phosphotyrosine; by PTK6" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 142 FT /note="Phosphotyrosine; by FYN and PTK6" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 191 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 246 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 331 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 333 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 552 FT /note="Phosphoserine; by AMPK" FT /evidence="ECO:0000250|UniProtKB:Q02248" FT MOD_RES 556 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 619 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:Q02248" FT MOD_RES 675 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT CARBOHYD 23 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q96S06" SQ SEQUENCE 781 AA; 85511 MW; 6148652F953F0723 CRC64; MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTT QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDAAHPT NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC SSNKPAIVEA GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL VRAHQDTQRR TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI GAQGEPLGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L //