Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Catenin beta-1 (Beta-catenin)

 CTNB1_RAT               Reviewed;         781 AA.
Q9WU82;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 178.
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.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Testis;
PubMed=10497305;
DOI=10.1002/(SICI)1097-4652(199911)181:2<258::AID-JCP8>3.0.CO;2-Q;
Chung S.S.W., Lee W.M., Cheng C.Y.;
"Study on the formation of specialized inter-Sertoli cell junctions in
vitro.";
J. Cell. Physiol. 181:258-272(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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-
f]quinoline.";
Gene 283:255-262(2002).
[3]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH MACF1; APC;
AXIN1 AND GSK3B.
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).
[4]
INTERACTION WITH FAT1.
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).
[5]
INTERACTION WITH CHD8.
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-552 AND
SER-675, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
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).
{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 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
AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1.
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 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).
{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}. Cytoplasm, cytoskeleton, cilium
basal body {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}.
-!- 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.
{ECO:0000250|UniProtKB:Q96S06}.
-!- PTM: Deacetylated at Lys-49 by SIRT1.
{ECO:0000250|UniProtKB:P35222}.
-!- 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; 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:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISS:UniProtKB.
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; 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:0014704; C:intercalated disc; IDA:RGD.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:ARUK-UCL.
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:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
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:0045294; F:alpha-catenin binding; IBA:GO_Central.
GO; GO:0045296; F:cadherin binding; IDA:RGD.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
GO; GO:0050998; F:nitric-oxide synthase binding; IPI:RGD.
GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
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:0060070; P:canonical Wnt signaling pathway; ISS:UniProtKB.
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:0098609; P:cell-cell adhesion; IDA: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:0061154; P:endothelial tube morphogenesis; ISS:UniProtKB.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0007494; P:midgut development; IEP:RGD.
GO; GO:0045445; P:myoblast differentiation; IEP:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; ISS:UniProtKB.
GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:UniProtKB.
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:0051291; P:protein heterooligomerization; IPI:RGD.
GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
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:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB.
GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB.
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: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:0061549; P:sympathetic ganglion development; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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;
Cell projection; 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.
/FTId=PRO_0000064273.
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.
{ECO:0000244|PubMed:22673903}.
MOD_RES 246 246 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 331 331 Phosphotyrosine.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 333 333 Phosphotyrosine.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 552 552 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
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:0000244|PubMed:16641100,
ECO:0000244|PubMed:22673903}.
CARBOHYD 23 23 O-linked (GlcNAc) serine; alternate.
{ECO:0000250|UniProtKB:Q96S06}.
CONFLICT 368 368 P -> L (in Ref. 2; AAK85253).
{ECO:0000305}.
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


Related products :

Catalog number Product name Quantity
EIAAB08137 Beta-catenin-interacting protein 1,Catnbip1,Ctnnbip1,Icat,Inhibitor of beta-catenin and Tcf-4,Mouse,Mus musculus
E1021h ELISA kit Beta-catenin,Catenin beta-1,CTNNB,CTNNB1,Homo sapiens,Human,OK_SW-cl.35,PRO2286 96T
EIAAB08136 Beta-catenin-interacting protein 1,CTNNBIP1,Homo sapiens,Human,ICAT,Inhibitor of beta-catenin and Tcf-4
E1021h ELISA Beta-catenin,Catenin beta-1,CTNNB,CTNNB1,Homo sapiens,Human,OK_SW-cl.35,PRO2286 96T
U1021h CLIA Beta-catenin,Catenin beta-1,CTNNB,CTNNB1,Homo sapiens,Human,OK_SW-cl.35,PRO2286 96T
bs-2063P Peptides: p- Beta catenin(p-beta Catenin(phosphor-Y142)) Protein Length:12-25 amino acids. 200ug lyophilized
20-321-175182 BETA-CATENIN - MONOCLONAL ANTIBODY TO HUMAN BETA-CATENIN; Beta-catenin Monoclonal 0.1 mg
20-272-191813 beta Catenin - Mouse monoclonal [BDI920] to beta Catenin; Beta-catenin Monoclonal 0.05 mg
20-272-191814 beta Catenin - Mouse monoclonal [BDI710] to beta Catenin; Beta-catenin Monoclonal 0.05 mg
20-272-190467 beta Catenin ( Cy3 ) - Mouse monoclonal [15B8] to beta Catenin ( Cy3 ); Beta-catenin Monoclonal 0.1 ml
E1021r ELISA kit Beta-catenin,Catenin beta-1,Catnb,Ctnnb1,Rat,Rattus norvegicus 96T
E1021m ELISA Beta-catenin,Catenin beta-1,Catnb,Ctnnb1,Mouse,Mus musculus 96T
E1021r ELISA Beta-catenin,Catenin beta-1,Catnb,Ctnnb1,Rat,Rattus norvegicus 96T
E1021m ELISA kit Beta-catenin,Catenin beta-1,Catnb,Ctnnb1,Mouse,Mus musculus 96T
U1021m CLIA Beta-catenin,Catenin beta-1,Catnb,Ctnnb1,Mouse,Mus musculus 96T
U1021r CLIA Beta-catenin,Catenin beta-1,Catnb,Ctnnb1,Rat,Rattus norvegicus 96T
U1021b CLIA Beta-catenin,Bos taurus,Bovine,Catenin beta-1,CTNNB1 96T
E1021b ELISA Beta-catenin,Bos taurus,Bovine,Catenin beta-1,CTNNB1 96T
E1021b ELISA kit Beta-catenin,Bos taurus,Bovine,Catenin beta-1,CTNNB1 96T
18-785-210043 beta-Catenin (Phospho-Ser33) - Beta-catenin Polyclonal 0.1 mg
18-785-210044 beta-Catenin (Phospho-Ser37) - Beta-catenin Polyclonal 0.1 mg
18-785-210041 beta-Catenin (Phospho-Thr41_Ser45) - Beta-catenin Polyclonal 0.05 mg
18-785-210041 beta-Catenin (Phospho-Thr41_Ser45) - Beta-catenin Polyclonal 0.1 mg
18-785-210044 beta-Catenin (Phospho-Ser37) - Beta-catenin Polyclonal 0.05 mg
18-785-210043 beta-Catenin (Phospho-Ser33) - Beta-catenin Polyclonal 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur