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Catenin beta-1 (Beta-catenin)

 CTNB1_RAT               Reviewed;         781 AA.
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
28-FEB-2018, entry version 172.
RecName: Full=Catenin beta-1;
AltName: Full=Beta-catenin;
Name=Ctnnb1; Synonyms=Catnb;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
STRAIN=Sprague-Dawley; TISSUE=Testis;
Chung S.S.W., Lee W.M., Cheng C.Y.;
"Study on the formation of specialized inter-Sertoli cell junctions in
J. Cell. Physiol. 181:258-272(1999).
STRAIN=Fischer 344;
PubMed=11867232; DOI=10.1016/S0378-1119(01)00839-3;
Li Q., Dixon B.M., Al-Fageeh M., Blum C.A., Dashwood R.H.;
"Sequencing of the rat beta-catenin gene (Ctnnb1) and mutational
analysis of liver tumors induced by 2-amino-3-methylimidazo[4,5-
Gene 283:255-262(2002).
PubMed=16815997; DOI=10.1101/gad.1411206;
Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.;
"The role of microtubule actin cross-linking factor 1 (MACF1) in the
Wnt signaling pathway.";
Genes Dev. 20:1933-1945(2006).
PubMed=16682528; DOI=10.1083/jcb.200508121;
Hou R., Liu L., Anees S., Hiroyasu S., Sibinga N.E.;
"The Fat1 cadherin integrates vascular smooth muscle cell growth and
migration signals.";
J. Cell Biol. 173:417-429(2006).
PubMed=10921920; DOI=10.1074/jbc.M004089200;
Sakamoto I., Kishida S., Fukui A., Kishida M., Yamamoto H., Hino S.,
Michiue T., Takada S., Asashima M., Kikuchi A.;
"A novel beta-catenin-binding protein inhibits beta-catenin-dependent
Tcf activation and axis formation.";
J. Biol. Chem. 275:32871-32878(2000).
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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 Wnt
ligand, CTNNB1 is not ubiquitinated and accumulates in the
nucleus, where it acts as a coactivator for transcription factors
of the TCF/LEF family, leading to activate Wnt responsive genes.
Involved in the regulation of cell adhesion, 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).
-!- SUBUNIT: Two separate complex-associated pools are found in the
cytoplasm. The majority is present as component of an E-cadherin/
catenin adhesion complex composed of at least E-cadherin/CDH1 and
beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the
complex is located to adherens junctions. The stable association
of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-
actin when assembled in the complex. Alternatively, the CTNNA1-
containing complex may be linked to F-actin by other proteins such
as LIMA1. Another cytoplasmic pool is part of a large complex
containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes
phosphorylation on N-terminal Ser and Thr residues and
ubiquitination of CTNNB1 Interacts directly with AXIN1; the
interaction is regulated by CK2 via BTRC and its subsequent
degradation by the proteasome. Interacts directly with AXIN1;the
interaction is regulated by CDK2 phosphorylation. Wnt-dependent
activation of DVL antagonizes the action of GSK3B. When GSK3B
activity is inhibited the complex dissociates, CTNNB1 is
dephosphorylated and is no longer targeted for destruction. The
stabilized protein translocates to the nucleus, where it binds
TCF/LEF-1 family members, TBP, BCL9, BCL9L and possibly also
RUVBL1 and CHD8. Binds CTNNBIP and EP300. CTNNB1 forms a ternary
complex with LEF1 and EP300 that is disrupted by CTNNBIP1 binding.
Interacts with TAX1BP3 (via the PDZ domain); this interaction
inhibits the transcriptional activity of CTNNB1. Interacts with
Interacts with GLIS2. Interacts with XIRP1. Interacts with PTPRU
(via the cytoplasmic juxtamembrane domain) and with SLC30A9.
Interacts with EMD. Interacts with SCRIB. Interacts with TNIK and
TCF7L2. Interacts with SESTD1 and TRPC4. Interacts directly with
AXIN1; the interaction is regulated by CDK2 phosphorylation of
AXIN1. Interacts with CAV1. Interacts with TRPV4. The TRPV4 and
CTNNB1 complex can interact with CDH1. Interacts with VCL.
Interacts with PTPRJ. Interacts with PKT7. Interacts with NANOS1.
Interacts with CDK2, NDRG2, NEK2 and CDK5. Found in a complex
composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B. Interacts with
PTK6. Interacts with SOX7; this interaction may lead to
proteasomal degradation of active CTNNB1 and thus inhibition of
Wnt/beta-catenin-stimulated transcription. Identified in a complex
with HINT1 and MITF. Interacts with FHIT. The CTNNB1 and TCF4
complex interacts with PML. Interacts with FERMT2. Identified in a
complex with TCF4 and FERMT2. Interacts with RAPGEF2. Interacts
with FAT1 (via the cytoplasmic domain). Interacts with RORA. May
interact with P-cadherin/CDH3. Interacts with RNF220 (By
similarity). Interacts with 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 (By
similarity). {ECO:0000250|UniProtKB:P35222,
ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:10921920,
ECO:0000269|PubMed:16682528, ECO:0000269|PubMed:16815997}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16815997}.
Nucleus {ECO:0000269|PubMed:16815997}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:16815997}. Cell junction, adherens junction
{ECO:0000250|UniProtKB:Q02248}. Cell junction
{ECO:0000250|UniProtKB:B6V8E6}. Cell membrane
{ECO:0000269|PubMed:16815997}. 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}. Note=Colocalized with RAPGEF2 and
TJP1 at cell-cell contacts (By similarity). Cytoplasmic when it is
unstabilized (high level of phosphorylation) or bound to CDH1.
Translocates to the nucleus when it is stabilized (low level of
phosphorylation). Interaction with GLIS2 and MUC1 promotes nuclear
translocation. Interaction with EMD inhibits nuclear localization.
The majority of beta-catenin is localized to the cell membrane. In
interphase, colocalizes with CROCC between CEP250 puncta at the
proximal end of centrioles, and this localization is dependent on
CROCC and CEP250. In mitosis, when NEK2 activity increases, it
localizes to centrosomes at spindle poles independent of CROCC.
Colocalizes with CDK5 in the cell-cell contacts and plasma
membrane of undifferentiated and differentiated neuroblastoma
cells. Interaction with FAM53B promotes translocation to the
nucleus (By similarity). {ECO:0000250|UniProtKB:B6V8E6,
-!- TISSUE SPECIFICITY: Expressed in the testis.
-!- DEVELOPMENTAL STAGE: Highly expressed at E30-60 day DPC in the
testis. Reduced expression at E90 day DPC.
-!- 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. 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-NoDerivs License
EMBL; AF121265; AAD28504.1; -; mRNA.
EMBL; AF397179; AAK85253.1; -; Genomic_DNA.
RefSeq; NP_445809.2; NM_053357.2.
RefSeq; XP_008764913.1; XM_008766691.2.
RefSeq; XP_017451425.1; XM_017595936.1.
RefSeq; XP_017451426.1; XM_017595937.1.
RefSeq; XP_017451428.1; XM_017595939.1.
RefSeq; XP_017451429.1; XM_017595940.1.
UniGene; Rn.112601; -.
ProteinModelPortal; Q9WU82; -.
SMR; Q9WU82; -.
BioGrid; 249913; 12.
CORUM; Q9WU82; -.
DIP; DIP-37053N; -.
IntAct; Q9WU82; 10.
MINT; Q9WU82; -.
STRING; 10116.ENSRNOP00000026016; -.
iPTMnet; Q9WU82; -.
PhosphoSitePlus; Q9WU82; -.
PaxDb; Q9WU82; -.
PRIDE; Q9WU82; -.
GeneID; 84353; -.
KEGG; rno:84353; -.
UCSC; RGD:70487; rat.
CTD; 1499; -.
RGD; 70487; Ctnnb1.
eggNOG; KOG4203; Eukaryota.
eggNOG; COG0035; LUCA.
HOGENOM; HOG000230958; -.
HOVERGEN; HBG000919; -.
InParanoid; Q9WU82; -.
KO; K02105; -.
PhylomeDB; Q9WU82; -.
TreeFam; TF317997; -.
PRO; PR:Q9WU82; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005912; C:adherens junction; ISO:RGD.
GO; GO:0043296; C:apical junction complex; ISO:RGD.
GO; GO:0045177; C:apical part of cell; ISO:RGD.
GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
GO; GO:1990907; C:beta-catenin-TCF complex; ISO:RGD.
GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISS:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
GO; GO:0016342; C:catenin complex; ISS:UniProtKB.
GO; GO:0071664; C:catenin-TCF7L2 complex; ISO:RGD.
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:0031253; C:cell projection membrane; ISO:RGD.
GO; GO:0005913; C:cell-cell adherens junction; IDA:RGD.
GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005916; C:fascia adherens; ISO:RGD.
GO; GO:0016600; C:flotillin complex; ISO:RGD.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0014704; C:intercalated disc; ISO:RGD.
GO; GO:0005622; C:intracellular; ISO:RGD.
GO; GO:0030027; C:lamellipodium; ISO:RGD.
GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0031528; C:microvillus membrane; ISO:RGD.
GO; GO:0005719; C:nuclear euchromatin; ISO:RGD.
GO; GO:0031965; C:nuclear membrane; IDA:ARUK-UCL.
GO; GO:0044798; C:nuclear transcription factor complex; ISO:RGD.
GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
GO; GO:0034750; C:Scrib-APC-beta-catenin complex; ISO:RGD.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0005667; C:transcription factor complex; ISS:UniProtKB.
GO; GO:1990909; C:Wnt signalosome; ISO:RGD.
GO; GO:0030018; C:Z disc; ISO:RGD.
GO; GO:0045294; F:alpha-catenin binding; ISO:RGD.
GO; GO:0045296; F:cadherin binding; IDA:RGD.
GO; GO:0003682; F:chromatin binding; ISO:RGD.
GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
GO; GO:0003677; F:DNA binding; ISO:RGD.
GO; GO:0003700; F:DNA binding transcription factor activity; ISO:RGD.
GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
GO; GO:0019899; F:enzyme binding; ISO:RGD.
GO; GO:0030331; F:estrogen receptor binding; ISO:RGD.
GO; GO:0070411; F:I-SMAD binding; ISO:RGD.
GO; GO:0044325; F:ion channel binding; ISO:RGD.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
GO; GO:0019900; F:kinase binding; ISO:RGD.
GO; GO:0050998; F:nitric-oxide synthase binding; IPI:RGD.
GO; GO:0035257; F:nuclear hormone receptor binding; ISO:RGD.
GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; ISO:RGD.
GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
GO; GO:0070491; F:repressing transcription factor binding; ISO:RGD.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:RGD.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:RGD.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; ISO:RGD.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISS:UniProtKB.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0046332; F:SMAD binding; ISO:RGD.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; ISO:RGD.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:RGD.
GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
GO; GO:0034332; P:adherens junction organization; ISO:RGD.
GO; GO:0048513; P:animal organ development; ISO:RGD.
GO; GO:0009948; P:anterior/posterior axis specification; ISO:RGD.
GO; GO:0045453; P:bone resorption; ISO:RGD.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISO:RGD.
GO; GO:0060070; P:canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; ISO:RGD.
GO; GO:0061324; P:canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation; ISO:RGD.
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:0030154; P:cell differentiation; ISO:RGD.
GO; GO:0001709; P:cell fate determination; ISO:RGD.
GO; GO:0001708; P:cell fate specification; ISO:RGD.
GO; GO:0048469; P:cell maturation; ISO:RGD.
GO; GO:0000904; P:cell morphogenesis involved in differentiation; ISO:RGD.
GO; GO:0008283; P:cell proliferation; ISO:RGD.
GO; GO:0098609; P:cell-cell adhesion; IDA:RGD.
GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
GO; GO:0009987; P:cellular process; ISO:RGD.
GO; GO:0034613; P:cellular protein localization; ISO:RGD.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
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:1990314; P:cellular response to insulin-like growth factor stimulus; IMP:RGD.
GO; GO:0071285; P:cellular response to lithium ion; IEP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:RGD.
GO; GO:0022009; P:central nervous system vasculogenesis; ISO:RGD.
GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; ISO:RGD.
GO; GO:0061550; P:cranial ganglion development; ISO:RGD.
GO; GO:1904888; P:cranial skeletal system development; ISO:RGD.
GO; GO:1990791; P:dorsal root ganglion development; ISO:RGD.
GO; GO:0009950; P:dorsal/ventral axis specification; ISO:RGD.
GO; GO:0009953; P:dorsal/ventral pattern formation; ISO:RGD.
GO; GO:0007398; P:ectoderm development; ISO:RGD.
GO; GO:0000578; P:embryonic axis specification; ISO:RGD.
GO; GO:1990403; P:embryonic brain development; ISO:RGD.
GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
GO; GO:0048617; P:embryonic foregut morphogenesis; ISO:RGD.
GO; GO:0035115; P:embryonic forelimb morphogenesis; ISO:RGD.
GO; GO:0035050; P:embryonic heart tube development; ISO:RGD.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; ISO:RGD.
GO; GO:0036023; P:embryonic skeletal limb joint morphogenesis; ISO:RGD.
GO; GO:0001706; P:endoderm formation; ISO:RGD.
GO; GO:0001711; P:endodermal cell fate commitment; ISO:RGD.
GO; GO:0061154; P:endothelial tube morphogenesis; ISS:UniProtKB.
GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; ISO:RGD.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; ISO:RGD.
GO; GO:0030900; P:forebrain development; ISO:RGD.
GO; GO:0061198; P:fungiform papilla formation; ISO:RGD.
GO; GO:0001702; P:gastrulation with mouth forming second; ISO:RGD.
GO; GO:0035112; P:genitalia morphogenesis; ISO:RGD.
GO; GO:0007403; P:glial cell fate determination; ISO:RGD.
GO; GO:0022405; P:hair cycle process; ISO:RGD.
GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
GO; GO:0060789; P:hair follicle placode formation; ISO:RGD.
GO; GO:0007507; P:heart development; ISO:RGD.
GO; GO:0030097; P:hemopoiesis; ISO:RGD.
GO; GO:0030902; P:hindbrain development; ISO:RGD.
GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
GO; GO:0001822; P:kidney development; ISO:RGD.
GO; GO:0021819; P:layer formation in cerebral cortex; ISO:RGD.
GO; GO:0002089; P:lens morphogenesis in camera-type eye; ISO:RGD.
GO; GO:0060173; P:limb development; ISO:RGD.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0060479; P:lung cell differentiation; ISO:RGD.
GO; GO:0030324; P:lung development; ISO:RGD.
GO; GO:0060492; P:lung induction; ISO:RGD.
GO; GO:0060484; P:lung-associated mesenchyme development; ISO:RGD.
GO; GO:0030539; P:male genitalia development; ISO:RGD.
GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; ISO:RGD.
GO; GO:0003338; P:metanephros morphogenesis; ISO:RGD.
GO; GO:0030901; P:midbrain development; ISO:RGD.
GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; ISO:RGD.
GO; GO:0007494; P:midgut development; IEP:RGD.
GO; GO:0016331; P:morphogenesis of embryonic epithelium; ISO:RGD.
GO; GO:0045445; P:myoblast differentiation; IEP:RGD.
GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
GO; GO:0045596; P:negative regulation of cell differentiation; ISO:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISO:RGD.
GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; ISO:RGD.
GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; ISS:UniProtKB.
GO; GO:1901215; P:negative regulation of neuron death; ISO:RGD.
GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISO:RGD.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISO:RGD.
GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; ISO:RGD.
GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0072079; P:nephron tubule formation; ISO:RGD.
GO; GO:0001840; P:neural plate development; ISO:RGD.
GO; GO:0030182; P:neuron differentiation; ISO:RGD.
GO; GO:0001764; P:neuron migration; ISO:RGD.
GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:RGD.
GO; GO:0048599; P:oocyte development; ISO:RGD.
GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
GO; GO:0060066; P:oviduct development; ISO:RGD.
GO; GO:0031016; P:pancreas development; ISO:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0061047; P:positive regulation of branching involved in lung morphogenesis; ISO:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:RGD.
GO; GO:1904501; P:positive regulation of chromatin-mediated maintenance of transcription; ISO:RGD.
GO; GO:1904798; P:positive regulation of core promoter binding; ISO:RGD.
GO; GO:2000017; P:positive regulation of determination of dorsal identity; ISO:RGD.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; ISO:RGD.
GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; ISO:RGD.
GO; GO:0045603; P:positive regulation of endothelial cell differentiation; ISO:RGD.
GO; GO:0030858; P:positive regulation of epithelial cell differentiation; ISO:RGD.
GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; ISO:RGD.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:RGD.
GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
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; ISO:RGD.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:RGD.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:RGD.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; ISO:RGD.
GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IPI:RGD.
GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
GO; GO:0009954; P:proximal/distal pattern formation; ISO:RGD.
GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
GO; GO:0090279; P:regulation of calcium ion import; ISS:UniProtKB.
GO; GO:0045595; P:regulation of cell differentiation; ISO:RGD.
GO; GO:0042127; P:regulation of cell proliferation; ISO:RGD.
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:1904796; P:regulation of core promoter binding; ISO:RGD.
GO; GO:0030856; P:regulation of epithelial cell differentiation; ISO:RGD.
GO; GO:1904793; P:regulation of euchromatin binding; ISO:RGD.
GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
GO; GO:0031641; P:regulation of myelination; ISO:RGD.
GO; GO:0072182; P:regulation of nephron tubule epithelial cell differentiation; ISO:RGD.
GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:RGD.
GO; GO:0045670; P:regulation of osteoclast differentiation; ISO:RGD.
GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB.
GO; GO:0003266; P:regulation of secondary heart field cardioblast proliferation; ISO:RGD.
GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:0042129; P:regulation of T cell proliferation; ISO:RGD.
GO; GO:0051884; P:regulation of timing of anagen; ISO:RGD.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0072053; P:renal inner medulla development; ISO:RGD.
GO; GO:0072054; P:renal outer medulla development; ISO:RGD.
GO; GO:0072001; P:renal system development; ISO:RGD.
GO; GO:0072033; P:renal vesicle formation; ISO:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
GO; GO:0034097; P:response to cytokine; IDA:RGD.
GO; GO:0042493; P:response to drug; ISO:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IDA:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0014010; P:Schwann cell proliferation; IMP:RGD.
GO; GO:0001501; P:skeletal system development; ISO:RGD.
GO; GO:0043588; P:skin development; ISO:RGD.
GO; GO:0051145; P:smooth muscle cell differentiation; ISO:RGD.
GO; GO:0061549; P:sympathetic ganglion development; ISS:UniProtKB.
GO; GO:0050808; P:synapse organization; ISO:RGD.
GO; GO:0048489; P:synaptic vesicle transport; ISO:RGD.
GO; GO:0030217; P:T cell differentiation; ISO:RGD.
GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
GO; GO:0048538; P:thymus development; ISO:RGD.
GO; GO:0060440; P:trachea formation; ISO:RGD.
GO; GO:0060439; P:trachea morphogenesis; ISO:RGD.
GO; GO:0006351; P:transcription, DNA-templated; NAS:ARUK-UCL.
GO; GO:0001944; P:vasculature development; ISO:RGD.
GO; GO:0001570; P:vasculogenesis; ISO:RGD.
GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
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;
Complete proteome; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane;
Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
S-nitrosylation; Synapse; Transcription; Transcription regulation;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P35222}.
CHAIN 2 781 Catenin beta-1.
REPEAT 151 191 ARM 1.
REPEAT 193 234 ARM 2.
REPEAT 235 276 ARM 3.
REPEAT 277 318 ARM 4.
REPEAT 319 360 ARM 5.
REPEAT 361 389 ARM 6.
REPEAT 400 441 ARM 7.
REPEAT 442 484 ARM 8.
REPEAT 489 530 ARM 9.
REPEAT 531 571 ARM 10.
REPEAT 594 636 ARM 11.
REPEAT 637 666 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.
MOD_RES 246 246 Phosphoserine; by CDK5.
MOD_RES 331 331 Phosphotyrosine.
MOD_RES 333 333 Phosphotyrosine.
MOD_RES 552 552 Phosphoserine.
MOD_RES 556 556 Phosphothreonine.
MOD_RES 619 619 S-nitrosocysteine.
MOD_RES 654 654 Phosphotyrosine; by CSK.
MOD_RES 675 675 Phosphoserine.
CARBOHYD 23 23 O-linked (GlcNAc) serine; alternate.
CONFLICT 368 368 P -> L (in Ref. 2; AAK85253).
SEQUENCE 781 AA; 85455 MW; 9C29186B6DD54B87 CRC64;

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