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Catenin beta-1 (Beta-catenin)

 CTNB1_BOVIN             Reviewed;         781 AA.
Q0VCX4; A7E3R2;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 1.
25-OCT-2017, entry version 113.
RecName: Full=Catenin beta-1;
AltName: Full=Beta-catenin;
Name=CTNNB1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Fetal skin;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH RAPGEF2.
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 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).
{ECO:0000250|UniProtKB:Q02248}.
-!- 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 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
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 AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y.
Binds SLC9A3R1. Interacts with GLIS2 and SLC30A9. Interacts with
XIRP1 and MUC1. Interacts with PTPRU (via the cytoplasmic
juxtamembrane domain) and with EMD. Interacts with SCRIB.
Interacts with TNIK. 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 FAT1 (via the cytoplasmic domain). Interacts with
NANOS1 and NDRG2. Interacts with NEK2, CDK2 and CDK5. 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 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 (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:0000250|UniProtKB:B6V8E6}. Cell junction, adherens junction
{ECO:0000250|UniProtKB:Q02248}. Cell junction
{ECO:0000250|UniProtKB:B6V8E6}. 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}. 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,
ECO:0000250|UniProtKB:P35222}.
-!- 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.
{ECO:0000250|UniProtKB:Q96S06}.
-!- PTM: Deacetylated at Lys-49 by SIRT1.
{ECO:0000250|UniProtKB:P35222}.
-!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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EMBL; BT030683; ABS44999.1; -; mRNA.
EMBL; BC119949; AAI19950.1; -; mRNA.
RefSeq; NP_001069609.1; NM_001076141.1.
RefSeq; XP_005222580.1; XM_005222523.3.
RefSeq; XP_005222581.1; XM_005222524.3.
RefSeq; XP_005222582.1; XM_005222525.3.
UniGene; Bt.33687; -.
ProteinModelPortal; Q0VCX4; -.
SMR; Q0VCX4; -.
IntAct; Q0VCX4; 1.
STRING; 9913.ENSBTAP00000021838; -.
iPTMnet; Q0VCX4; -.
PaxDb; Q0VCX4; -.
PeptideAtlas; Q0VCX4; -.
PRIDE; Q0VCX4; -.
Ensembl; ENSBTAT00000021838; ENSBTAP00000021838; ENSBTAG00000016420.
GeneID; 539003; -.
KEGG; bta:539003; -.
CTD; 1499; -.
eggNOG; KOG4203; Eukaryota.
eggNOG; COG0035; LUCA.
GeneTree; ENSGT00730000110821; -.
HOGENOM; HOG000230958; -.
HOVERGEN; HBG000919; -.
InParanoid; Q0VCX4; -.
KO; K02105; -.
OMA; WEQGFNQ; -.
OrthoDB; EOG091G03A5; -.
TreeFam; TF317997; -.
Reactome; R-BTA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-BTA-196299; Beta-catenin phosphorylation cascade.
Reactome; R-BTA-201681; TCF dependent signaling in response to WNT.
Reactome; R-BTA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-BTA-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
Reactome; R-BTA-351906; Apoptotic cleavage of cell adhesion proteins.
Reactome; R-BTA-375170; CDO in myogenesis.
Reactome; R-BTA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-BTA-4086398; Ca2+ pathway.
Reactome; R-BTA-418990; Adherens junctions interactions.
Reactome; R-BTA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-BTA-5626467; RHO GTPases activate IQGAPs.
Reactome; R-BTA-8951430; RUNX3 regulates WNT signaling.
Proteomes; UP000009136; Chromosome 22.
Bgee; ENSBTAG00000016420; -.
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; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
GO; GO:0016600; C:flotillin complex; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
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: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: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:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl.
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:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; IEA:Ensembl.
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; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; 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; IEA:Ensembl.
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: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:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; 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 from RNA polymerase II promoter; 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:0042493; P:response to drug; 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: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.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; ISS:UniProtKB.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000225; Armadillo.
InterPro; IPR013284; Beta-catenin.
Pfam; PF00514; Arm; 4.
PRINTS; PR01869; BCATNINFAMLY.
SMART; SM00185; ARM; 12.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50176; ARM_REPEAT; 9.
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; Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P35222}.
CHAIN 2 781 Catenin beta-1.
/FTId=PRO_0000282881.
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.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 23 23 Phosphoserine; by GSK3-beta; alternate.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 29 29 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 33 33 Phosphoserine; by GSK3-beta and HIPK2.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 37 37 Phosphoserine; by GSK3-beta and HIPK2.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 41 41 Phosphothreonine; by GSK3-beta.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 49 49 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 64 64 Phosphotyrosine; by PTK6.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 86 86 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 142 142 Phosphotyrosine; by FYN and PTK6.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 191 191 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 246 246 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 331 331 Phosphotyrosine.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 552 552 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:Q02248}.
MOD_RES 556 556 Phosphothreonine.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 619 619 S-nitrosocysteine.
{ECO:0000250|UniProtKB:Q02248}.
MOD_RES 654 654 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000250|UniProtKB:P35222}.
CARBOHYD 23 23 O-linked (GlcNAc) serine; alternate.
{ECO:0000250|UniProtKB:Q96S06}.
SEQUENCE 781 AA; 85511 MW; 6148652F953F0723 CRC64;
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTT
QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDAAHPT
NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK
KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL
VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC
LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC SSNKPAIVEA
GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA
AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM
AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL
VRAHQDTQRR TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV
QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF
RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI GAQGEPLGYR QDDPSYRSFH
SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD
L


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