CTNB1_BOVIN
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 03-AUG-2022, entry version 143.
DE RecName: Full=Catenin beta-1;
DE AltName: Full=Beta-catenin;
GN Name=CTNNB1;
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).
CC {ECO:0000250|UniProtKB:P35222, 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 SLC9A3R1. Interacts
CC with GLIS2 and SLC30A9. Interacts with XIRP1 and MUC1. Interacts with
CC PTPRU (via the cytoplasmic juxtamembrane domain) and with EMD.
CC Interacts with SCRIB. Interacts with TNIK. Interacts with SESTD1 and
CC TRPC4. Interacts directly with AXIN1; the interaction is regulated by
CC CDK2 phosphorylation of AXIN1. Interacts with CAV1. Interacts with
CC TRPV4. The TRPV4 and CTNNB1 complex can interact with CDH1. Interacts
CC with VCL. Interacts with PTPRJ. Interacts with PKT7. Interacts with
CC FAT1 (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 {ECO:0000250|UniProtKB:P35222, ECO:0000250|UniProtKB:Q02248,
CC 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 unstabilized (high level of phosphorylation) or bound to
CC CDH1. 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 stabilizion 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 iPTMnet; Q0VCX4; -.
DR PaxDb; Q0VCX4; -.
DR PeptideAtlas; Q0VCX4; -.
DR PRIDE; Q0VCX4; -.
DR Ensembl; ENSBTAT00000021838; ENSBTAP00000021838; ENSBTAG00000016420.
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; 321213at2759; -.
DR TreeFam; TF317997; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000016420; Expressed in thyroid gland and 104 other 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: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:0008013; F:beta-catenin binding; IEA:Ensembl.
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:0008022; F:protein C-terminus 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:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0001221; F:transcription coregulator 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:0044339; P:canonical Wnt signaling pathway involved in osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0061324; P:canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation; IEA:Ensembl.
DR GO; GO:0044334; P:canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
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:0000904; P:cell morphogenesis involved in differentiation; 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: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:0007249; P:I-kappaB kinase/NF-kappaB signaling; 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:2001234; P:negative regulation of apoptotic signaling pathway; 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: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:1903204; P:negative regulation of oxidative stress-induced neuron death; 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:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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:0030316; P:osteoclast differentiation; 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:1904798; P:positive regulation of core promoter binding; IEA:Ensembl.
DR GO; GO:2000017; P:positive regulation of determination of dorsal identity; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
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: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:0051571; P:positive regulation of histone H3-K4 methylation; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
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: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:0051973; P:positive regulation of telomerase activity; 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 from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
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: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: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 Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR013284; Beta-catenin.
DR PANTHER; PTHR45976; PTHR45976; 1.
DR Pfam; PF00514; Arm; 4.
DR PRINTS; PR01869; BCATNINFAMLY.
DR SMART; SM00185; ARM; 12.
DR SUPFAM; SSF48371; SSF48371; 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
