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Catenin beta-1 (Beta-catenin)

 CTNB1_CANLF             Reviewed;         781 AA.
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 1.
05-DEC-2018, entry version 91.
RecName: Full=Catenin beta-1;
AltName: Full=Beta-catenin;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Han J.-I., Na K.-J.;
"Cloning and sequencing of the full-length canine beta-catenin cDNA.";
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
PubMed=16341006; DOI=10.1038/nature04338;
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
"Genome sequence, comparative analysis and haplotype structure of the
domestic dog.";
Nature 438:803-819(2005).
PubMed=10873669; DOI=10.1006/bbrc.2000.3002;
Kawajiri A., Itoh N., Fukata M., Nakagawa M., Yamaga M., Iwamatsu A.,
Kaibuchi K.;
"Identification of a novel beta-catenin-interacting protein.";
Biochem. Biophys. Res. Commun. 273:712-717(2000).
-!- FUNCTION: Key downstream component of the canonical Wnt signaling
pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2,
APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal
Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its
subsequent degradation by the proteasome. In the presence of the
Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the
nucleus, where it acts as a coactivator for transcription factors
of the TCF/LEF family, leading to activation of Wnt responsive
genes. Involved in the regulation of cell adhesion, as component
of an E-cadherin:catenin adhesion complex. Acts as a negative
regulator of centrosome cohesion. Involved in the
CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization.
Blocks anoikis of malignant kidney and intestinal epithelial cells
and promotes their anchorage-independent growth by down-regulating
DAPK2. Disrupts PML function and PML-NB formation by inhibiting
RANBP2-mediated sumoylation of PML. Promotes neurogenesis by
maintaining sympathetic neuroblasts within the cell cycle (By
similarity). {ECO:0000250|UniProtKB:Q02248}.
-!- SUBUNIT: Two separate complex-associated pools are found in the
cytoplasm. The majority is present as part of an E-cadherin/
catenin adhesion complex composed of at least E-cadherin/CDH1 and
beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the
complex is located to adherens junctions. The stable association
of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-
actin when assembled in the complex. Alternatively, the CTNNA1-
containing complex may be linked to F-actin by other proteins such
as LIMA1. Binds SLC9A3R1. Interacts with PTPRU (via the
cytoplasmic juxtamembrane domain) and with EMD. Interacts with
SESTD1 and TRPC4. Interacts with CAV1. Interacts with PTPRJ.
Interacts with PKT7. Interacts with FAT1 (via the cytoplasmic
domain). Interacts with CDK2, NDRG2 and NANOS1. Interacts with
NEK2 and CDK5. Interacts with CARM1, CXADR, PCDH11Y and PTK6.
Interacts with SOX7; this interaction may lead to proteasomal
degradation of active CTNNB1 and thus inhibition of Wnt/beta-
catenin-stimulated transcription. Identified in a complex with
HINT1 and MITF. Interacts with FHIT. Interacts with FERMT2.
Identified in a complex with TCF4 and FERMT2. Another cytoplasmic
pool is part of a large complex containing AXIN1, AXIN2, APC,
CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser
and Thr residues and ubiquitination of CTNNB1 via BTRC and its
subsequent degradation by the proteasome. Wnt-dependent activation
of DVL antagonizes the action of GSK3B. When GSK3B activity is
inhibited, the complex disassociates, CTNNB1 is dephosphorylated
and is no longer targeted for destruction. The stabilized protein
translocates to the nucleus, where it binds TCF/LEF-1 family
members, TBP, BCL9, BCL9L and possibly also RUVBL1 and CHD8.
Interacts with TAX1BP3 (via the PDZ domain); this interaction
inhibits the transcriptional activity of CTNNB1. Interacts with
AJAP1, BAIAP1 and CTNNA3. Interacts with TRPV4; the TRPV4 and
CTNNB1 complex can interact with CDH1. Interacts with VCL. The
CTNNB1 and TCF4 complex interacts with PML. Interacts with XIRP1.
Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with LEF1
and EP300 that is disrupted by CTNNBIP1 binding. Interacts
directly with AXIN1; the interaction is regulated by CDK2
phosphorylation of AXIN1. Interacts with GLIS2. Interacts with
SCRIB. Interacts with TNIK and TCF7L2. Interacts with SLC30A9.
Interacts with RORA. May interact with P-cadherin/CDH3 (By
similarity). Interacts with RAPGEF2. Interacts with RNF220 (By
similarity). Interacts with CTNND2 (By similarity). Interacts (via
the C-terminal region) with CBY1 (By similarity). The complex
composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1;
the interaction requires the inactive form of GSK3B
(phosphorylated at 'Ser-9'). Interacts with DLG5 (By similarity).
Interacts with FAM53B; promoting translocation to the nucleus.
Interacts with TMEM170B (By similarity). Interacts with AHI1 (By
similarity). Interacts with GID8 (By similarity). Component of an
cadherin:catenin adhesion complex composed of at least of CDH26,
beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1
(By similarity). {ECO:0000250|UniProtKB:P35222,
ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:10873669}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35222}.
Nucleus {ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:10873669}. Cell junction, adherens junction
{ECO:0000250|UniProtKB:Q02248}. Cell junction
{ECO:0000269|PubMed:10873669}. Cell membrane
{ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000250|UniProtKB:P35222}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q02248}. Cytoplasm, cytoskeleton, cilium
basal body {ECO:0000250|UniProtKB:Q02248}. Note=Colocalized with
RAPGEF2 and TJP1 at cell-cell contacts (PubMed:10873669).
Cytoplasmic when it is unstabilized (high level of
phosphorylation) or bound to CDH1 (By similarity). Translocates to
the nucleus when it is stabilized (low level of phosphorylation)
(By similarity). Interaction with GLIS2 and MUC1 promotes nuclear
translocation (By similarity). Interaction with EMD inhibits
nuclear localization (By similarity). The majority of beta-catenin
is localized to the cell membrane (By similarity). In interphase,
colocalizes with CROCC between CEP250 puncta at the proximal end
of centrioles, and this localization is dependent on CROCC and
CEP250 (By similarity). In mitosis, when NEK2 activity increases,
it localizes to centrosomes at spindle poles independent of CROCC
(By similarity). Colocalizes with CDK5 in the cell-cell contacts
and plasma membrane of undifferentiated and differentiated
neuroblastoma cells (By similarity). Interaction with FAM53B
promotes translocation to the nucleus (By similarity).
{ECO:0000250|UniProtKB:P35222, ECO:0000269|PubMed:10873669}.
-!- PTM: Phosphorylation by GSK3B requires prior phosphorylation of
Ser-45 by another kinase. Phosphorylation proceeds then from Thr-
41 to Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine
phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding
and enhances TBP binding (By similarity). Phosphorylated on Ser-33
and Ser-37 by HIPK2. This phosphorylation triggers proteasomal
degradation. Phosphorylation at Ser-552 by AMPK promotes
stabilizion of the protein, enhancing TCF/LEF-mediated
transcription. Phosphorylation on Ser-191 and Ser-246 by CDK5.
Phosphorylation by CDK2 regulates insulin internalization (By
similarity). Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331
and/or Tyr-333 with the predominant site at Tyr-64 is not
essential for inhibition of transcriptional activity (By
similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when
phosphorylated by GSK3B, leading to its degradation. Ubiquitinated
by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1,
CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent
proteasomal degradation (By similarity). {ECO:0000250}.
-!- PTM: S-nitrosylation at Cys-619 within adherens junctions promotes
VEGF-induced, NO-dependent endothelial cell permeability by
disrupting interaction with E-cadherin, thus mediating disassembly
adherens junctions. {ECO:0000250}.
-!- PTM: O-glycosylation at Ser-23 decreases nuclear localization and
transcriptional activity, and increases localization to the plasma
membrane and interaction with E-cadherin CDH1.
-!- PTM: Deacetylated at Lys-49 by SIRT1.
-!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; FJ268743; ACJ04159.1; -; mRNA.
EMBL; AAEX03013510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001131124.1; NM_001137652.1.
RefSeq; XP_013961954.1; XM_014106479.1.
RefSeq; XP_013961955.1; XM_014106480.1.
UniGene; Cfa.415; -.
ProteinModelPortal; B6V8E6; -.
SMR; B6V8E6; -.
CORUM; B6V8E6; -.
IntAct; B6V8E6; 7.
MINT; B6V8E6; -.
STRING; 9615.ENSCAFP00000007783; -.
iPTMnet; B6V8E6; -.
PaxDb; B6V8E6; -.
PRIDE; B6V8E6; -.
Ensembl; ENSCAFT00000008400; ENSCAFP00000007783; ENSCAFG00000005204.
GeneID; 477032; -.
KEGG; cfa:477032; -.
CTD; 1499; -.
eggNOG; KOG4203; Eukaryota.
eggNOG; COG0035; LUCA.
GeneTree; ENSGT00940000155471; -.
HOGENOM; HOG000230958; -.
HOVERGEN; HBG000919; -.
InParanoid; B6V8E6; -.
KO; K02105; -.
OrthoDB; EOG091G03A5; -.
TreeFam; TF317997; -.
Reactome; R-CFA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-CFA-196299; Beta-catenin phosphorylation cascade.
Reactome; R-CFA-201681; TCF dependent signaling in response to WNT.
Reactome; R-CFA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-CFA-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
Reactome; R-CFA-351906; Apoptotic cleavage of cell adhesion proteins.
Reactome; R-CFA-375170; CDO in myogenesis.
Reactome; R-CFA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-CFA-4086398; Ca2+ pathway.
Reactome; R-CFA-418990; Adherens junctions interactions.
Reactome; R-CFA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-CFA-5626467; RHO GTPases activate IQGAPs.
Reactome; R-CFA-8951430; RUNX3 regulates WNT signaling.
Proteomes; UP000002254; Chromosome 23.
Bgee; ENSCAFG00000005204; Expressed in 3 organ(s), highest expression level in prefrontal cortex.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISS:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
GO; GO:0016342; C:catenin complex; ISS:UniProtKB.
GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; ISS:UniProtKB.
GO; GO:0071944; C:cell periphery; ISS:BHF-UCL.
GO; GO:0005913; C:cell-cell adherens junction; ISS:UniProtKB.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
GO; GO:0016600; C:flotillin complex; IEA:Ensembl.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
GO; GO:0031528; C:microvillus membrane; IEA:Ensembl.
GO; GO:0005719; C:nuclear euchromatin; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0099092; C:postsynaptic density, intracellular component; IEA:Ensembl.
GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IEA:Ensembl.
GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IEA:Ensembl.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0005667; C:transcription factor complex; ISS:UniProtKB.
GO; GO:1990909; C:Wnt signalosome; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0045294; F:alpha-catenin binding; IBA:GO_Central.
GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:Ensembl.
GO; GO:0030331; F:estrogen receptor binding; IEA:Ensembl.
GO; GO:0070411; F:I-SMAD binding; IEA:Ensembl.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0035257; F:nuclear hormone receptor binding; IBA:GO_Central.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
GO; GO:0070491; F:repressing transcription factor binding; IEA:Ensembl.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IEA:Ensembl.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISS:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl.
GO; GO:0070830; P:bicellular tight junction assembly; IDA:UniProtKB.
GO; GO:0045453; P:bone resorption; IEA:Ensembl.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
GO; GO:0060070; P:canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0061324; P:canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation; IEA:Ensembl.
GO; GO:0044334; P:canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
GO; GO:0048469; P:cell maturation; IEA:Ensembl.
GO; GO:0000904; P:cell morphogenesis involved in differentiation; IEA:Ensembl.
GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
GO; GO:0071681; P:cellular response to indole-3-methanol; ISS:UniProtKB.
GO; GO:0022009; P:central nervous system vasculogenesis; IEA:Ensembl.
GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; IEA:Ensembl.
GO; GO:0061550; P:cranial ganglion development; IEA:Ensembl.
GO; GO:1904888; P:cranial skeletal system development; IEA:Ensembl.
GO; GO:1990791; P:dorsal root ganglion development; IEA:Ensembl.
GO; GO:0009950; P:dorsal/ventral axis specification; IEA:Ensembl.
GO; GO:0007398; P:ectoderm development; IEA:Ensembl.
GO; GO:0000578; P:embryonic axis specification; IEA:Ensembl.
GO; GO:1990403; P:embryonic brain development; IEA:Ensembl.
GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl.
GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
GO; GO:0035050; P:embryonic heart tube development; IEA:Ensembl.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
GO; GO:0036023; P:embryonic skeletal limb joint morphogenesis; IEA:Ensembl.
GO; GO:0001711; P:endodermal cell fate commitment; IEA:Ensembl.
GO; GO:0061154; P:endothelial tube morphogenesis; ISS:UniProtKB.
GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IEA:Ensembl.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
GO; GO:0061198; P:fungiform papilla formation; IEA:Ensembl.
GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
GO; GO:0035112; P:genitalia morphogenesis; IEA:Ensembl.
GO; GO:0007403; P:glial cell fate determination; IEA:Ensembl.
GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
GO; GO:0060789; P:hair follicle placode formation; IEA:Ensembl.
GO; GO:0030902; P:hindbrain development; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl.
GO; GO:0002089; P:lens morphogenesis in camera-type eye; IEA:Ensembl.
GO; GO:0060479; P:lung cell differentiation; IEA:Ensembl.
GO; GO:0060492; P:lung induction; IEA:Ensembl.
GO; GO:0060484; P:lung-associated mesenchyme development; IEA:Ensembl.
GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IEA:Ensembl.
GO; GO:0003338; P:metanephros morphogenesis; IEA:Ensembl.
GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; IEA:Ensembl.
GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; IEA:Ensembl.
GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; ISS:UniProtKB.
GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IEA:Ensembl.
GO; GO:0033234; P:negative regulation of protein sumoylation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0072079; P:nephron tubule formation; IEA:Ensembl.
GO; GO:0001840; P:neural plate development; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0048599; P:oocyte development; IEA:Ensembl.
GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
GO; GO:0060066; P:oviduct development; IEA:Ensembl.
GO; GO:0031016; P:pancreas development; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:1904501; P:positive regulation of chromatin-mediated maintenance of transcription; IEA:Ensembl.
GO; GO:1904798; P:positive regulation of core promoter binding; IEA:Ensembl.
GO; GO:2000017; P:positive regulation of determination of dorsal identity; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IEA:Ensembl.
GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IEA:Ensembl.
GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IEA:Ensembl.
GO; GO:0051973; P:positive regulation of telomerase activity; IEA:Ensembl.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
GO; GO:0090279; P:regulation of calcium ion import; ISS:UniProtKB.
GO; GO:0030997; P:regulation of centriole-centriole cohesion; ISS:UniProtKB.
GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; ISS:UniProtKB.
GO; GO:1904793; P:regulation of euchromatin binding; IEA:Ensembl.
GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
GO; GO:0072182; P:regulation of nephron tubule epithelial cell differentiation; IEA:Ensembl.
GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB.
GO; GO:0003266; P:regulation of secondary heart field cardioblast proliferation; IEA:Ensembl.
GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:0042129; P:regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0051884; P:regulation of timing of anagen; IEA:Ensembl.
GO; GO:0072053; P:renal inner medulla development; IEA:Ensembl.
GO; GO:0072054; P:renal outer medulla development; IEA:Ensembl.
GO; GO:0072033; P:renal vesicle formation; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; ISS:UniProtKB.
GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl.
GO; GO:0061549; P:sympathetic ganglion development; ISS:UniProtKB.
GO; GO:0050808; P:synapse organization; IEA:Ensembl.
GO; GO:0097091; P:synaptic vesicle clustering; IEA:Ensembl.
GO; GO:0048489; P:synaptic vesicle transport; IEA:Ensembl.
GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
GO; GO:0060440; P:trachea formation; IEA:Ensembl.
Gene3D;; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000225; Armadillo.
InterPro; IPR013284; Beta-catenin.
Pfam; PF00514; Arm; 4.
SMART; SM00185; ARM; 12.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Acetylation; Activator; Cell adhesion; Cell junction; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
Glycoprotein; Membrane; Neurogenesis; Nucleus; Phosphoprotein;
Reference proteome; Repeat; S-nitrosylation; Synapse; Transcription;
Transcription regulation; Ubl conjugation; Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P35222}.
CHAIN 2 781 Catenin beta-1.
REPEAT 141 180 ARM 1.
REPEAT 181 223 ARM 2.
REPEAT 224 264 ARM 3.
REPEAT 265 306 ARM 4.
REPEAT 308 349 ARM 5.
REPEAT 350 390 ARM 6.
REPEAT 392 429 ARM 7.
REPEAT 430 473 ARM 8.
REPEAT 478 519 ARM 9.
REPEAT 520 582 ARM 10.
REPEAT 583 623 ARM 11.
REPEAT 624 664 ARM 12.
REGION 2 23 Interaction with VCL. {ECO:0000250}.
REGION 156 178 Interaction with BCL9. {ECO:0000250}.
REGION 772 781 Interaction with SCRIB. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
MOD_RES 23 23 Phosphoserine; by GSK3-beta; alternate.
MOD_RES 29 29 Phosphoserine; by GSK3-beta.
MOD_RES 33 33 Phosphoserine; by GSK3-beta and HIPK2.
MOD_RES 37 37 Phosphoserine; by GSK3-beta and HIPK2.
MOD_RES 41 41 Phosphothreonine; by GSK3-beta.
MOD_RES 45 45 Phosphoserine.
MOD_RES 49 49 N6-acetyllysine.
MOD_RES 64 64 Phosphotyrosine; by PTK6.
MOD_RES 86 86 Phosphotyrosine; by CSK.
MOD_RES 142 142 Phosphotyrosine; by FYN and PTK6.
MOD_RES 191 191 Phosphoserine; by CDK5.
MOD_RES 246 246 Phosphoserine; by CDK5.
MOD_RES 331 331 Phosphotyrosine.
MOD_RES 333 333 Phosphotyrosine.
MOD_RES 552 552 Phosphoserine; by AMPK.
MOD_RES 556 556 Phosphothreonine.
MOD_RES 619 619 S-nitrosocysteine.
MOD_RES 654 654 Phosphotyrosine.
MOD_RES 675 675 Phosphoserine.
CARBOHYD 23 23 O-linked (GlcNAc) serine; alternate.
SEQUENCE 781 AA; 85511 MW; 6148652F953F0723 CRC64;

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