CTNB1_RAT
ID CTNB1_RAT Reviewed; 781 AA.
AC Q9WU82;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Catenin beta-1;
DE AltName: Full=Beta-catenin;
GN Name=Ctnnb1; Synonyms=Catnb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=10497305;
RX DOI=10.1002/(sici)1097-4652(199911)181:2<258::aid-jcp8>3.0.co;2-q;
RA Chung S.S.W., Lee W.M., Cheng C.Y.;
RT "Study on the formation of specialized inter-Sertoli cell junctions in
RT vitro.";
RL J. Cell. Physiol. 181:258-272(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Fischer 344;
RX PubMed=11867232; DOI=10.1016/s0378-1119(01)00839-3;
RA Li Q., Dixon B.M., Al-Fageeh M., Blum C.A., Dashwood R.H.;
RT "Sequencing of the rat beta-catenin gene (Ctnnb1) and mutational analysis
RT of liver tumors induced by 2-amino-3-methylimidazo[4,5-f]quinoline.";
RL Gene 283:255-262(2002).
RN [3]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH MACF1; APC;
RP AXIN1 AND GSK3B.
RX PubMed=16815997; DOI=10.1101/gad.1411206;
RA Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.;
RT "The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt
RT signaling pathway.";
RL Genes Dev. 20:1933-1945(2006).
RN [4]
RP INTERACTION WITH FAT1.
RX PubMed=16682528; DOI=10.1083/jcb.200508121;
RA Hou R., Liu L., Anees S., Hiroyasu S., Sibinga N.E.;
RT "The Fat1 cadherin integrates vascular smooth muscle cell growth and
RT migration signals.";
RL J. Cell Biol. 173:417-429(2006).
RN [5]
RP INTERACTION WITH CHD8.
RX PubMed=10921920; DOI=10.1074/jbc.m004089200;
RA Sakamoto I., Kishida S., Fukui A., Kishida M., Yamamoto H., Hino S.,
RA Michiue T., Takada S., Asashima M., Kikuchi A.;
RT "A novel beta-catenin-binding protein inhibits beta-catenin-dependent Tcf
RT activation and axis formation.";
RL J. Biol. Chem. 275:32871-32878(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-552 AND SER-675, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Interacts directly with AXIN1;
CC the interaction is regulated by CK2 via BTRC and its subsequent
CC degradation by the proteasome. Interacts directly with AXIN1; the
CC interaction is regulated by CDK2 phosphorylation. Wnt-dependent
CC activation of DVL antagonizes the action of GSK3B. When GSK3B activity
CC is inhibited the complex dissociates, CTNNB1 is dephosphorylated and is
CC no longer targeted for destruction. The stabilized protein translocates
CC to the nucleus, where it binds TCF/LEF-1 family members, BCL9, BCL9L
CC and possibly also RUVBL1 and CHD8. Binds CTNNBIP and EP300. CTNNB1
CC forms a ternary complex with LEF1 and EP300 that is disrupted by
CC CTNNBIP1 binding. Interacts with TAX1BP3 (via the PDZ domain); this
CC interaction inhibits the transcriptional activity of CTNNB1. Interacts
CC with AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1.
CC Interacts with GLIS2. Interacts with XIRP1. Interacts with PTPRU (via
CC the cytoplasmic juxtamembrane domain) and with SLC30A9. Interacts with
CC EMD. Interacts with SCRIB. Interacts with TNIK and TCF7L2. Interacts
CC with SESTD1 and TRPC4. Interacts directly with AXIN1; the interaction
CC is regulated by CDK2 phosphorylation of AXIN1. Interacts with CAV1.
CC Interacts with TRPV4. The TRPV4 and CTNNB1 complex can interact with
CC CDH1. Interacts with VCL. Interacts with PTPRJ. Interacts with PKT7.
CC Interacts with NANOS1. Interacts with CDK2, NDRG2, NEK2 and CDK5. Found
CC in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B. Interacts
CC with PTK6. Interacts with SOX7; this interaction may lead to
CC proteasomal degradation of active CTNNB1 and thus inhibition of
CC Wnt/beta-catenin-stimulated transcription. Identified in a complex with
CC HINT1 and MITF. Interacts with FHIT. The CTNNB1 and TCF4 complex
CC interacts with PML. Interacts with FERMT2. Identified in a complex with
CC TCF4 and FERMT2. Interacts with RAPGEF2. Interacts with FAT1 (via the
CC cytoplasmic domain). Interacts with RORA. May interact with P-
CC cadherin/CDH3. 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 AMFR (By similarity). Interacts with LMBR1L (By similarity).
CC Interacts with SOX30; prevents interaction of CTNNB1 with TCF7L2/TCF4
CC and leads to inhibition of Wnt signaling (By similarity). Interacts
CC with SOX9; inhibiting CTNNB1 activity by competing with the binding
CC sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling
CC (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:10921920, ECO:0000269|PubMed:16682528,
CC ECO:0000269|PubMed:16815997}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16815997}. Nucleus
CC {ECO:0000269|PubMed:16815997}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16815997}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q02248}. Cell junction
CC {ECO:0000250|UniProtKB:B6V8E6}. Cell membrane
CC {ECO:0000269|PubMed:16815997}. 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 -!- TISSUE SPECIFICITY: Expressed in the testis.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at E30-60 day DPC in the testis.
CC Reduced expression at E90 day DPC.
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}.
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DR EMBL; AF121265; AAD28504.1; -; mRNA.
DR EMBL; AF397179; AAK85253.1; -; Genomic_DNA.
DR RefSeq; NP_445809.2; NM_053357.2.
DR RefSeq; XP_008764913.1; XM_008766691.2.
DR RefSeq; XP_017451425.1; XM_017595936.1.
DR RefSeq; XP_017451426.1; XM_017595937.1.
DR RefSeq; XP_017451428.1; XM_017595939.1.
DR RefSeq; XP_017451429.1; XM_017595940.1.
DR AlphaFoldDB; Q9WU82; -.
DR SMR; Q9WU82; -.
DR BioGRID; 249913; 154.
DR CORUM; Q9WU82; -.
DR DIP; DIP-37053N; -.
DR IntAct; Q9WU82; 18.
DR MINT; Q9WU82; -.
DR STRING; 10116.ENSRNOP00000026016; -.
DR GlyGen; Q9WU82; 1 site.
DR iPTMnet; Q9WU82; -.
DR PhosphoSitePlus; Q9WU82; -.
DR jPOST; Q9WU82; -.
DR PaxDb; Q9WU82; -.
DR PRIDE; Q9WU82; -.
DR GeneID; 84353; -.
DR KEGG; rno:84353; -.
DR UCSC; RGD:70487; rat.
DR CTD; 1499; -.
DR RGD; 70487; Ctnnb1.
DR eggNOG; KOG4203; Eukaryota.
DR InParanoid; Q9WU82; -.
DR OrthoDB; 321213at2759; -.
DR PhylomeDB; Q9WU82; -.
DR TreeFam; TF317997; -.
DR Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-RNO-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-RNO-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-RNO-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-RNO-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
DR Reactome; R-RNO-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-RNO-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-RNO-4086398; Ca2+ pathway.
DR Reactome; R-RNO-418990; Adherens junctions interactions.
DR Reactome; R-RNO-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-RNO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-RNO-525793; Myogenesis.
DR Reactome; R-RNO-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-RNO-8951430; RUNX3 regulates WNT signaling.
DR PRO; PR:Q9WU82; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; IDA:RGD.
DR GO; GO:0043296; C:apical junction complex; ISO:RGD.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
DR GO; GO:1990711; C:beta-catenin-ICAT complex; ISO:RGD.
DR GO; GO:1990907; C:beta-catenin-TCF complex; ISO:RGD.
DR GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
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:0031253; C:cell projection membrane; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0005916; C:fascia adherens; ISO:RGD.
DR GO; GO:0016600; C:flotillin complex; ISO:RGD.
DR GO; GO:0014704; C:intercalated disc; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; IDA:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; ISO:RGD.
DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0034750; C:Scrib-APC-beta-catenin complex; ISO:RGD.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0070160; C:tight junction; IDA:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB.
DR GO; GO:1990909; C:Wnt signalosome; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0045294; F:alpha-catenin binding; IPI:RGD.
DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR GO; GO:0045296; F:cadherin binding; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0070097; F:delta-catenin binding; IPI:RGD.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:1990226; F:histone methyltransferase binding; ISO:RGD.
DR GO; GO:0070411; F:I-SMAD binding; ISO:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:RGD.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:RGD.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
DR GO; GO:0034332; P:adherens junction organization; ISO:RGD.
DR GO; GO:0048513; P:animal organ development; ISO:RGD.
DR GO; GO:0009948; P:anterior/posterior axis specification; ISO:RGD.
DR GO; GO:0036520; P:astrocyte-dopaminergic neuron signaling; ISO:RGD.
DR GO; GO:0046849; P:bone remodeling; IEP:RGD.
DR GO; GO:0045453; P:bone resorption; ISO:RGD.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0044339; P:canonical Wnt signaling pathway involved in osteoblast differentiation; ISO:RGD.
DR GO; GO:0061324; P:canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation; ISO:RGD.
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:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0001709; P:cell fate determination; ISO:RGD.
DR GO; GO:0001708; P:cell fate specification; ISO:RGD.
DR GO; GO:0048469; P:cell maturation; ISO:RGD.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
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:1990314; P:cellular response to insulin-like growth factor stimulus; IMP:RGD.
DR GO; GO:0071285; P:cellular response to lithium ion; IEP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:RGD.
DR GO; GO:0022009; P:central nervous system vasculogenesis; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0061550; P:cranial ganglion development; ISO:RGD.
DR GO; GO:1904888; P:cranial skeletal system development; ISO:RGD.
DR GO; GO:1990791; P:dorsal root ganglion development; ISO:RGD.
DR GO; GO:0009950; P:dorsal/ventral axis specification; ISO:RGD.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; ISO:RGD.
DR GO; GO:0007398; P:ectoderm development; ISO:RGD.
DR GO; GO:0000578; P:embryonic axis specification; ISO:RGD.
DR GO; GO:1990403; P:embryonic brain development; ISO:RGD.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; ISO:RGD.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; ISO:RGD.
DR GO; GO:0035050; P:embryonic heart tube development; ISO:RGD.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; ISO:RGD.
DR GO; GO:0048568; P:embryonic organ development; ISO:RGD.
DR GO; GO:0036023; P:embryonic skeletal limb joint morphogenesis; ISO:RGD.
DR GO; GO:0001706; P:endoderm formation; ISO:RGD.
DR GO; GO:0001711; P:endodermal cell fate commitment; ISO:RGD.
DR GO; GO:0061154; P:endothelial tube morphogenesis; ISS:UniProtKB.
DR GO; GO:1905867; P:epididymis development; IEP:RGD.
DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; ISO:RGD.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; ISO:RGD.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:0061198; P:fungiform papilla formation; ISO:RGD.
DR GO; GO:0001702; P:gastrulation with mouth forming second; ISO:RGD.
DR GO; GO:0035112; P:genitalia morphogenesis; ISO:RGD.
DR GO; GO:0007403; P:glial cell fate determination; ISO:RGD.
DR GO; GO:0022405; P:hair cycle process; ISO:RGD.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR GO; GO:0060789; P:hair follicle placode formation; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0030902; P:hindbrain development; ISO:RGD.
DR GO; GO:0021854; P:hypothalamus development; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0021819; P:layer formation in cerebral cortex; ISO:RGD.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; ISO:RGD.
DR GO; GO:0060173; P:limb development; ISO:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0060479; P:lung cell differentiation; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0060492; P:lung induction; ISO:RGD.
DR GO; GO:0060484; P:lung-associated mesenchyme development; ISO:RGD.
DR GO; GO:0030539; P:male genitalia development; ISO:RGD.
DR GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; ISO:RGD.
DR GO; GO:0072497; P:mesenchymal stem cell differentiation; ISO:RGD.
DR GO; GO:0003338; P:metanephros morphogenesis; ISO:RGD.
DR GO; GO:0030901; P:midbrain development; ISO:RGD.
DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; ISO:RGD.
DR GO; GO:0007494; P:midgut development; IEP:RGD.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; ISO:RGD.
DR GO; GO:0045445; P:myoblast differentiation; IEP:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0045596; P:negative regulation of cell differentiation; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; ISO:RGD.
DR GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; ISS:UniProtKB.
DR GO; GO:0050768; P:negative regulation of neurogenesis; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:RGD.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISO:RGD.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0072079; P:nephron tubule formation; ISO:RGD.
DR GO; GO:0001840; P:neural plate development; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:RGD.
DR GO; GO:0048599; P:oocyte development; ISO:RGD.
DR GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
DR GO; GO:0060066; P:oviduct development; ISO:RGD.
DR GO; GO:0031016; P:pancreas development; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:1904798; P:positive regulation of core promoter binding; ISO:RGD.
DR GO; GO:2000017; P:positive regulation of determination of dorsal identity; ISO:RGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0045603; P:positive regulation of endothelial cell differentiation; ISO:RGD.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; ISO:RGD.
DR GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; ISO:RGD.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:RGD.
DR GO; GO:0044093; P:positive regulation of molecular function; ISO:RGD.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISO:RGD.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
DR GO; GO:0009954; P:proximal/distal pattern formation; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR GO; GO:0090279; P:regulation of calcium ion import; ISS:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
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:1904796; P:regulation of core promoter binding; ISO:RGD.
DR GO; GO:0030856; P:regulation of epithelial cell differentiation; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0031641; P:regulation of myelination; ISO:RGD.
DR GO; GO:0072182; P:regulation of nephron tubule epithelial cell differentiation; ISO:RGD.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0042129; P:regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0051884; P:regulation of timing of anagen; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0072053; P:renal inner medulla development; ISO:RGD.
DR GO; GO:0072054; P:renal outer medulla development; ISO:RGD.
DR GO; GO:0072033; P:renal vesicle formation; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IDA:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IDA:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0014010; P:Schwann cell proliferation; IMP:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:0051145; P:smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0061549; P:sympathetic ganglion development; ISS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0097091; P:synaptic vesicle clustering; ISO:RGD.
DR GO; GO:0048489; P:synaptic vesicle transport; ISO:RGD.
DR GO; GO:0030217; P:T cell differentiation; ISO:RGD.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
DR GO; GO:0048538; P:thymus development; ISO:RGD.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR GO; GO:0060440; P:trachea formation; ISO:RGD.
DR GO; GO:0060439; P:trachea morphogenesis; ISO:RGD.
DR GO; GO:0001944; P:vasculature development; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
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.
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_0000064273"
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..57
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 720..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"
FT /evidence="ECO:0007744|PubMed:22673903"
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"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT CARBOHYD 23
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96S06"
FT CONFLICT 368
FT /note="P -> L (in Ref. 2; AAK85253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 781 AA; 85455 MW; 9C29186B6DD54B87 CRC64;
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTS
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
GGMQALGPHL 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 GAQGEALGYR QDDPSYRSFH
SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD
L
