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Catenin beta-1 (Beta-catenin)

 CTNB1_MOUSE             Reviewed;         781 AA.
Q02248; Q922W1; Q9D335;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
30-AUG-2017, entry version 204.
RecName: Full=Catenin beta-1;
AltName: Full=Beta-catenin;
Name=Ctnnb1; Synonyms=Catnb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1509266; DOI=10.1126/science.257.5073.1142-a;
Butz S., Stappert J., Weissig H., Kemler R.;
"Plakoglobin and beta-catenin: distinct but closely related.";
Science 257:1142-1144(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Colon, and Urinary bladder;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain, and Mammary cancer;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
Butz S., Kemler R.;
"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
adhesion.";
FEBS Lett. 355:195-200(1994).
[5]
INTERACTION WITH TCF7; TCF7L1; TCF7L2 AND LEF1.
PubMed=9783587; DOI=10.1038/26989;
Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H.,
Moerer P., van de Wetering M., Destree O., Clevers H.;
"The Xenopus Wnt effector XTcf-3 interacts with Groucho-related
transcriptional repressors.";
Nature 395:608-612(1998).
[6]
INTERACTION WITH AXIN1.
PubMed=10581160; DOI=10.1006/bbrc.1999.1760;
Jho E., Lomvardas S., Costantini F.;
"A GSK3beta phosphorylation site in axin modulates interaction with
beta-catenin and Tcf-mediated gene expression.";
Biochem. Biophys. Res. Commun. 266:28-35(1999).
[7]
INTERACTION WITH BAIAP1.
PubMed=10772923; DOI=10.1006/bbrc.2000.2471;
Dobrosotskaya I.Y., James G.L.;
"MAGI-1 interacts with beta-catenin and is associated with cell-cell
adhesion structures.";
Biochem. Biophys. Res. Commun. 270:903-909(2000).
[8]
INTERACTION WITH CTNNA3.
PubMed=11590244;
Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J.,
Colpaert C., Bruyneel E., Mareel M., van Roy F.;
"AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein
mediating strong cell-cell adhesion.";
J. Cell Sci. 114:3177-3188(2001).
[9]
INTERACTION WITH TAX1BP3.
PubMed=12874278; DOI=10.1074/jbc.M306324200;
Kanamori M., Sandy P., Marzinotto S., Benetti R., Kai C.,
Hayashizaki Y., Schneider C., Suzuki H.;
"The PDZ protein tax-interacting protein-1 inhibits beta-catenin
transcriptional activity and growth of colorectal cancer cells.";
J. Biol. Chem. 278:38758-38764(2003).
[10]
PHOSPHORYLATION AT TYR-142 BY FYN.
PubMed=12640114; DOI=10.1128/MCB.23.7.2287-2297.2003;
Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N.,
Garcia de Herreros A., Dunach M.;
"p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-
catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin
Interaction.";
Mol. Cell. Biol. 23:2287-2297(2003).
[11]
INTERACTION WITH RORA.
PubMed=14687547; DOI=10.1016/S0896-6273(03)00769-4;
Gold D.A., Baek S.H., Schork N.J., Rose D.W., Larsen D.D., Sachs B.D.,
Rosenfeld M.G., Hamilton B.A.;
"RORalpha coordinates reciprocal signaling in cerebellar development
through sonic hedgehog and calcium-dependent pathways.";
Neuron 40:1119-1131(2003).
[12]
INTERACTION WITH AXIN1.
PubMed=15063782; DOI=10.1016/j.bbrc.2004.03.065;
Kim S.I., Park C.S., Lee M.S., Kwon M.S., Jho E.H., Song W.K.;
"Cyclin-dependent kinase 2 regulates the interaction of Axin with
beta-catenin.";
Biochem. Biophys. Res. Commun. 317:478-483(2004).
[13]
RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, LACK OF
ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND
FUNCTION.
PubMed=16325582; DOI=10.1016/j.cell.2005.09.020;
Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.;
"Deconstructing the cadherin-catenin-actin complex.";
Cell 123:889-901(2005).
[14]
INTERACTION WITH BCL9L.
PubMed=17052462; DOI=10.1016/j.molcel.2006.09.001;
Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.;
"Crystal structure of a beta-catenin/BCL9/Tcf4 complex.";
Mol. Cell 24:293-300(2006).
[15]
INTERACTION WITH GLIS2, AND SUBCELLULAR LOCATION.
PubMed=17289029; DOI=10.1016/j.febslet.2007.01.058;
Kim Y.-S., Kang H.S., Jetten A.M.;
"The Kruppel-like zinc finger protein Glis2 functions as a negative
modulator of the Wnt/beta-catenin signaling pathway.";
FEBS Lett. 581:858-864(2007).
[16]
INTERACTION WITH XIRP1.
PubMed=17925400; DOI=10.1074/jbc.M707639200;
Choi S., Gustafson-Wagner E.A., Wang Q., Harlan S.M., Sinn H.W.,
Lin J.L.-C., Lin J.J.-C.;
"The intercalated disc protein, mXin{alpha}, is capable of interacting
with beta-catenin and bundling actin filaments.";
J. Biol. Chem. 282:36024-36036(2007).
[17]
INTERACTION WITH SLC30A9.
PubMed=17344318; DOI=10.1093/nar/gkm095;
Chen Y.H., Yang C.K., Xia M., Ou C.Y., Stallcup M.R.;
"Role of GAC63 in transcriptional activation mediated by beta-
catenin.";
Nucleic Acids Res. 35:2084-2092(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-552 AND
SER-675, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[19]
LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND
FUNCTION.
PubMed=18093941; DOI=10.1073/pnas.0710504105;
Abe K., Takeichi M.;
"EPLIN mediates linkage of the cadherin catenin complex to F-actin and
stabilizes the circumferential actin belt.";
Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008).
[20]
INTERACTION WITH TCF7L2 AND TNIK.
PubMed=19816403; DOI=10.1038/emboj.2009.285;
Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J.,
Mohammed S., Heck A.J., Clevers H.;
"The kinase TNIK is an essential activator of Wnt target genes.";
EMBO J. 28:3329-3340(2009).
[21]
INTERACTION WITH SCRIB.
PubMed=19458197; DOI=10.1091/mbc.E08-12-1172;
Sun Y., Aiga M., Yoshida E., Humbert P.O., Bamji S.X.;
"Scribble interacts with beta-catenin to localize synaptic vesicles to
synapses.";
Mol. Biol. Cell 20:3390-3400(2009).
[22]
PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2, AND MUTAGENESIS OF
SER-33 AND SER-37.
PubMed=20307497; DOI=10.1016/j.bbrc.2010.03.099;
Kim E.-A., Kim J.E., Sung K.S., Choi D.W., Lee B.J., Choi C.Y.;
"Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-catenin
for phosphorylation and proteasomal degradation.";
Biochem. Biophys. Res. Commun. 394:966-971(2010).
[23]
PHOSPHORYLATION AT SER-552, AND MUTAGENESIS OF SER-552.
PubMed=20361929; DOI=10.1016/j.bbrc.2010.03.161;
Zhao J., Yue W., Zhu M.J., Sreejayan N., Du M.;
"AMP-activated protein kinase (AMPK) cross-talks with canonical Wnt
signaling via phosphorylation of beta-catenin at Ser 552.";
Biochem. Biophys. Res. Commun. 395:146-151(2010).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-191 AND SER-675,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[25]
INTERACTION WITH TRPV4 AND CDH1.
PubMed=20413591; DOI=10.1074/jbc.M110.103606;
Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.;
"The TRPV4 channel contributes to intercellular junction formation in
keratinocytes.";
J. Biol. Chem. 285:18749-18758(2010).
[26]
INTERACTION WITH VCL, AND MUTAGENESIS OF MET-8.
PubMed=20086044; DOI=10.1242/jcs.056432;
Peng X., Cuff L.E., Lawton C.D., DeMali K.A.;
"Vinculin regulates cell-surface E-cadherin expression by binding to
beta-catenin.";
J. Cell Sci. 123:567-577(2010).
[27]
REVIEW.
PubMed=10679188; DOI=10.1006/bbrc.1999.1860;
Kikuchi A.;
"Regulation of beta-catenin signaling in the Wnt pathway.";
Biochem. Biophys. Res. Commun. 268:243-248(2000).
[28]
S-NITROSYLATION AT CYS-619, AND SUBCELLULAR LOCATION.
PubMed=20705246; DOI=10.1016/j.molcel.2010.07.013;
Thibeault S., Rautureau Y., Oubaha M., Faubert D., Wilkes B.C.,
Delisle C., Gratton J.P.;
"S-nitrosylation of beta-catenin by eNOS-derived NO promotes VEGF-
induced endothelial cell permeability.";
Mol. Cell 39:468-476(2010).
[29]
FUNCTION, DISRUPTION PHENOTYPE, AND CONDITIONAL KNOCKOUT.
PubMed=21325504; DOI=10.1523/JNEUROSCI.4243-10.2011;
Armstrong A., Ryu Y.K., Chieco D., Kuruvilla R.;
"Frizzled3 is required for neurogenesis and target innervation during
sympathetic nervous system development.";
J. Neurosci. 31:2371-2381(2011).
[30]
SUBCELLULAR LOCATION, AND INTERACTION WITH DLG5.
PubMed=25232112; DOI=10.1523/JNEUROSCI.1280-14.2014;
Wang S.H., Celic I., Choi S.Y., Riccomagno M., Wang Q., Sun L.O.,
Mitchell S.P., Vasioukhin V., Huganir R.L., Kolodkin A.L.;
"Dlg5 regulates dendritic spine formation and synaptogenesis by
controlling subcellular N-cadherin localization.";
J. Neurosci. 34:12745-12761(2014).
[31]
SUBCELLULAR LOCATION.
PubMed=25979161; DOI=10.1016/j.bone.2015.05.009;
Jeong B.C., Kim T.S., Kim H.S., Lee S.H., Choi Y.;
"Transmembrane protein 64 reciprocally regulates osteoblast and
adipocyte differentiation by modulating Wnt/beta-catenin signaling.";
Bone 78:165-173(2015).
[32]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 150-665.
PubMed=9298899; DOI=10.1016/S0092-8674(00)80352-9;
Huber A.H., Nelson W.J., Weis W.I.;
"Three-dimensional structure of the armadillo repeat region of beta-
catenin.";
Cell 90:871-882(1997).
[33]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 118-149 IN COMPLEX WITH
CTNNA1.
PubMed=10882138; DOI=10.1016/S1097-2765(00)80447-5;
Pokutta S., Weis W.I.;
"Structure of the dimerization and beta-catenin-binding region of
alpha-catenin.";
Mol. Cell 5:533-543(2000).
[34]
X-RAY CRYSTALLOGRAPHY (2.0 AND 3.0 ANGSTROMS) OF 134-671 IN COMPLEX
WITH PHOSPHORYLATED AND UNPHOSPHORYLATED CDH1.
PubMed=11348595; DOI=10.1016/S0092-8674(01)00330-0;
Huber A.H., Weis W.I.;
"The structure of the beta-catenin/E-cadherin complex and the
molecular basis of diverse ligand recognition by beta-catenin.";
Cell 105:391-402(2001).
[35]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH APC.
PubMed=11707392; DOI=10.1093/emboj/20.22.6203;
Eklof Spink K., Fridman S.G., Weis W.I.;
"Molecular mechanisms of beta-catenin recognition by adenomatous
polyposis coli revealed by the structure of an APC-beta-catenin
complex.";
EMBO J. 20:6203-6212(2001).
[36]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH
CTNNBIP1, AND INTERACTION WITH EP300.
PubMed=12408825; DOI=10.1016/S1097-2765(02)00631-7;
Daniels D.L., Weis W.I.;
"ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription
factors and the general coactivator p300 using independent structural
modules.";
Mol. Cell 10:573-584(2002).
-!- 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 (By similarity). Promotes neurogenesis by
maintaining sympathetic neuroblasts within the cell cycle
(PubMed:21325504). {ECO:0000250|UniProtKB:P35222,
ECO:0000269|PubMed:16325582, ECO:0000269|PubMed:18093941,
ECO:0000269|PubMed:21325504}.
-!- 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. 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 RAPGEF2. 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
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. 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. 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') (By similarity). Interacts with DLG5
(PubMed:25232112). Interacts with FAM53B; promoting translocation
to the nucleus (By similarity). {ECO:0000250|UniProtKB:P35222,
ECO:0000269|PubMed:10581160, ECO:0000269|PubMed:10772923,
ECO:0000269|PubMed:10882138, ECO:0000269|PubMed:11348595,
ECO:0000269|PubMed:11590244, ECO:0000269|PubMed:11707392,
ECO:0000269|PubMed:12408825, ECO:0000269|PubMed:12874278,
ECO:0000269|PubMed:14687547, ECO:0000269|PubMed:15063782,
ECO:0000269|PubMed:17052462, ECO:0000269|PubMed:17289029,
ECO:0000269|PubMed:17344318, ECO:0000269|PubMed:17925400,
ECO:0000269|PubMed:19458197, ECO:0000269|PubMed:19816403,
ECO:0000269|PubMed:20086044, ECO:0000269|PubMed:20413591,
ECO:0000269|PubMed:25232112, ECO:0000269|PubMed:7982500,
ECO:0000269|PubMed:9783587}.
-!- INTERACTION:
P25054:APC (xeno); NbExp=8; IntAct=EBI-397872, EBI-727707;
O15169:AXIN1 (xeno); NbExp=5; IntAct=EBI-397872, EBI-710484;
P09803:Cdh1; NbExp=14; IntAct=EBI-397872, EBI-984420;
P45481:Crebbp; NbExp=3; IntAct=EBI-397872, EBI-296306;
P26231:Ctnna1; NbExp=2; IntAct=EBI-397872, EBI-647895;
Q9NSA3:CTNNBIP1 (xeno); NbExp=7; IntAct=EBI-397872, EBI-747082;
P49841:GSK3B (xeno); NbExp=3; IntAct=EBI-397872, EBI-373586;
Q9WV60:Gsk3b; NbExp=2; IntAct=EBI-397872, EBI-400793;
P42859:Htt; NbExp=3; IntAct=EBI-397872, EBI-5327353;
P27782:Lef1; NbExp=6; IntAct=EBI-397872, EBI-984464;
P97458:Prop1; NbExp=2; IntAct=EBI-397872, EBI-937831;
P49768:PSEN1 (xeno); NbExp=3; IntAct=EBI-397872, EBI-297277;
F1MSG6:RAPGEF2 (xeno); NbExp=2; IntAct=EBI-397872, EBI-6927068;
Q04207:Rela; NbExp=5; IntAct=EBI-397872, EBI-644400;
Q9DBG9:Tax1bp3; NbExp=6; IntAct=EBI-397872, EBI-1161647;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton.
Cell junction, adherens junction {ECO:0000269|PubMed:20705246}.
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:0000269|PubMed:20705246}. 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 (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:0000269|PubMed:20705246}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Sympathetic ganglia-specific conditional
knockout mice lead to a reduction in sympathetic ganglia size and
in progenitor cell number, but does not alter sympathetic
innervation of peripheral target organs.
{ECO:0000269|PubMed:21325504}.
-!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH06739.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M90364; AAA37280.1; -; mRNA.
EMBL; AK035311; BAC29027.1; -; mRNA.
EMBL; AK018515; BAB31250.1; -; mRNA.
EMBL; BC006739; AAH06739.1; ALT_INIT; mRNA.
EMBL; BC048153; AAH48153.1; -; mRNA.
EMBL; BC053065; AAH53065.1; -; mRNA.
CCDS; CCDS23630.1; -.
PIR; S35091; S35091.
RefSeq; NP_001159374.1; NM_001165902.1.
RefSeq; NP_031640.1; NM_007614.3.
UniGene; Mm.291928; -.
PDB; 1DOW; X-ray; 1.80 A; B=118-149.
PDB; 1I7W; X-ray; 2.00 A; A/C=134-671.
PDB; 1I7X; X-ray; 3.00 A; A/C=134-671.
PDB; 1JPP; X-ray; 3.10 A; A/B=134-671.
PDB; 1M1E; X-ray; 2.10 A; A=134-671.
PDB; 1V18; X-ray; 2.10 A; A=134-671.
PDB; 2BCT; X-ray; 2.90 A; A=150-665.
PDB; 3BCT; X-ray; 2.10 A; A=193-661.
PDB; 3OUW; X-ray; 2.91 A; A=134-671.
PDB; 3OUX; X-ray; 2.40 A; A=134-671.
PDB; 4EV8; X-ray; 1.90 A; A=134-671.
PDB; 4EV9; X-ray; 2.10 A; A=134-671.
PDB; 4EVA; X-ray; 2.00 A; A/C=134-671.
PDB; 4EVP; X-ray; 2.26 A; A=134-671.
PDB; 4EVT; X-ray; 2.34 A; A=134-671.
PDB; 4ONS; X-ray; 2.80 A; B/D=78-151.
PDBsum; 1DOW; -.
PDBsum; 1I7W; -.
PDBsum; 1I7X; -.
PDBsum; 1JPP; -.
PDBsum; 1M1E; -.
PDBsum; 1V18; -.
PDBsum; 2BCT; -.
PDBsum; 3BCT; -.
PDBsum; 3OUW; -.
PDBsum; 3OUX; -.
PDBsum; 4EV8; -.
PDBsum; 4EV9; -.
PDBsum; 4EVA; -.
PDBsum; 4EVP; -.
PDBsum; 4EVT; -.
PDBsum; 4ONS; -.
DisProt; DP00341; -.
ProteinModelPortal; Q02248; -.
SMR; Q02248; -.
BioGrid; 198512; 78.
DIP; DIP-31560N; -.
IntAct; Q02248; 62.
MINT; MINT-103426; -.
STRING; 10090.ENSMUSP00000007130; -.
iPTMnet; Q02248; -.
PhosphoSitePlus; Q02248; -.
SwissPalm; Q02248; -.
MaxQB; Q02248; -.
PaxDb; Q02248; -.
PeptideAtlas; Q02248; -.
PRIDE; Q02248; -.
Ensembl; ENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932.
Ensembl; ENSMUST00000178812; ENSMUSP00000136294; ENSMUSG00000006932.
GeneID; 12387; -.
KEGG; mmu:12387; -.
UCSC; uc009scu.2; mouse.
CTD; 1499; -.
MGI; MGI:88276; Ctnnb1.
eggNOG; KOG4203; Eukaryota.
eggNOG; COG0035; LUCA.
GeneTree; ENSGT00730000110821; -.
HOGENOM; HOG000230958; -.
HOVERGEN; HBG000919; -.
InParanoid; Q02248; -.
KO; K02105; -.
OMA; WEQGFNQ; -.
OrthoDB; EOG091G03A5; -.
PhylomeDB; Q02248; -.
TreeFam; TF317997; -.
Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade.
Reactome; R-MMU-201681; TCF dependent signaling in response to WNT.
Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-MMU-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
Reactome; R-MMU-351906; Apoptotic cleavage of cell adhesion proteins.
Reactome; R-MMU-375170; CDO in myogenesis.
Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-MMU-4086398; Ca2+ pathway.
Reactome; R-MMU-418990; Adherens junctions interactions.
Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
Reactome; R-MMU-8951430; RUNX3 regulates WNT signaling.
ChiTaRS; Ctnnb1; mouse.
EvolutionaryTrace; Q02248; -.
PMAP-CutDB; Q02248; -.
PRO; PR:Q02248; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000006932; -.
CleanEx; MM_CTNNB1; -.
ExpressionAtlas; Q02248; baseline and differential.
Genevisible; Q02248; MM.
GO; GO:0005912; C:adherens junction; IDA:MGI.
GO; GO:0043296; C:apical junction complex; IDA:MGI.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
GO; GO:0030877; C:beta-catenin destruction complex; IDA:MGI.
GO; GO:1990907; C:beta-catenin-TCF complex; ISO:MGI.
GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISS:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
GO; GO:0016342; C:catenin complex; IDA:MGI.
GO; GO:0071664; C:catenin-TCF7L2 complex; IDA:BHF-UCL.
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; IDA:MGI.
GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005916; C:fascia adherens; IDA:MGI.
GO; GO:0016600; C:flotillin complex; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0014704; C:intercalated disc; IDA:MGI.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:MGI.
GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0031528; C:microvillus membrane; IDA:MGI.
GO; GO:0005719; C:nuclear euchromatin; IDA:BHF-UCL.
GO; GO:0044798; C:nuclear transcription factor complex; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IDA:BHF-UCL.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:1990909; C:Wnt signalosome; IDA:ParkinsonsUK-UCL.
GO; GO:0030018; C:Z disc; IDA:MGI.
GO; GO:0045294; F:alpha-catenin binding; IDA:MGI.
GO; GO:0045296; F:cadherin binding; IPI:CAFA.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL.
GO; GO:0030331; F:estrogen receptor binding; ISO:MGI.
GO; GO:1990226; F:histone methyltransferase binding; NAS:BHF-UCL.
GO; GO:0070411; F:I-SMAD binding; ISO:MGI.
GO; GO:0044325; F:ion channel binding; ISO:MGI.
GO; GO:0019900; F:kinase binding; ISO:MGI.
GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; IPI:UniProtKB.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0046332; F:SMAD binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
GO; GO:0034332; P:adherens junction organization; IMP:MGI.
GO; GO:0048513; P:animal organ development; IMP:MGI.
GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
GO; GO:1904886; P:beta-catenin destruction complex disassembly; TAS:Reactome.
GO; GO:0045453; P:bone resorption; IMP:MGI.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:CAFA.
GO; GO:1904954; P:canonical Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; IC:ParkinsonsUK-UCL.
GO; GO:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; ISO:MGI.
GO; GO:0061324; P:canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation; IMP:BHF-UCL.
GO; GO:0044334; P:canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0060038; P:cardiac muscle cell proliferation; TAS:DFLAT.
GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; TAS:DFLAT.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IMP:MGI.
GO; GO:0001709; P:cell fate determination; IMP:MGI.
GO; GO:0001708; P:cell fate specification; IMP:MGI.
GO; GO:0048469; P:cell maturation; IDA:MGI.
GO; GO:0000904; P:cell morphogenesis involved in differentiation; IMP:MGI.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
GO; GO:0009987; P:cellular process; IDA:MGI.
GO; GO:0034613; P:cellular protein localization; IMP:MGI.
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; IMP:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; IMP:BHF-UCL.
GO; GO:0060982; P:coronary artery morphogenesis; TAS:DFLAT.
GO; GO:0061550; P:cranial ganglion development; IMP:ParkinsonsUK-UCL.
GO; GO:1904888; P:cranial skeletal system development; IMP:ParkinsonsUK-UCL.
GO; GO:1990791; P:dorsal root ganglion development; IMP:ParkinsonsUK-UCL.
GO; GO:0009950; P:dorsal/ventral axis specification; IMP:MGI.
GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
GO; GO:0007398; P:ectoderm development; IMP:MGI.
GO; GO:0000578; P:embryonic axis specification; IDA:MGI.
GO; GO:1990403; P:embryonic brain development; IMP:ParkinsonsUK-UCL.
GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:MGI.
GO; GO:0035115; P:embryonic forelimb morphogenesis; IDA:MGI.
GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
GO; GO:0036023; P:embryonic skeletal limb joint morphogenesis; IGI:BHF-UCL.
GO; GO:0001706; P:endoderm formation; IMP:MGI.
GO; GO:0001711; P:endodermal cell fate commitment; IMP:MGI.
GO; GO:0061154; P:endothelial tube morphogenesis; ISS:UniProtKB.
GO; GO:0060983; P:epicardium-derived cardiac vascular smooth muscle cell differentiation; TAS:DFLAT.
GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IMP:MGI.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0061198; P:fungiform papilla formation; IMP:MGI.
GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
GO; GO:0035112; P:genitalia morphogenesis; IMP:MGI.
GO; GO:0007403; P:glial cell fate determination; IDA:MGI.
GO; GO:0022405; P:hair cycle process; IMP:MGI.
GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
GO; GO:0060789; P:hair follicle placode formation; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0030097; P:hemopoiesis; IDA:MGI.
GO; GO:0030902; P:hindbrain development; IMP:ParkinsonsUK-UCL.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0021819; P:layer formation in cerebral cortex; IMP:MGI.
GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
GO; GO:0060173; P:limb development; IMP:MGI.
GO; GO:0060479; P:lung cell differentiation; IMP:MGI.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0060492; P:lung induction; IMP:MGI.
GO; GO:0060484; P:lung-associated mesenchyme development; IMP:MGI.
GO; GO:0030539; P:male genitalia development; IMP:MGI.
GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IMP:MGI.
GO; GO:0060485; P:mesenchyme development; TAS:DFLAT.
GO; GO:0072132; P:mesenchyme morphogenesis; TAS:DFLAT.
GO; GO:0003338; P:metanephros morphogenesis; IMP:MGI.
GO; GO:0030901; P:midbrain development; IMP:ParkinsonsUK-UCL.
GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; IMP:ParkinsonsUK-UCL.
GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:BHF-UCL.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IGI:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL.
GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; IDA:MGI.
GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; IMP:UniProtKB.
GO; GO:1901215; P:negative regulation of neuron death; IGI:MGI.
GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IMP:MGI.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP:MGI.
GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IMP:ParkinsonsUK-UCL.
GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0072079; P:nephron tubule formation; IMP:MGI.
GO; GO:0001840; P:neural plate development; IDA:MGI.
GO; GO:0030182; P:neuron differentiation; IMP:ParkinsonsUK-UCL.
GO; GO:0001764; P:neuron migration; IGI:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0048599; P:oocyte development; IGI:MGI.
GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
GO; GO:0060066; P:oviduct development; IMP:MGI.
GO; GO:0031016; P:pancreas development; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0061047; P:positive regulation of branching involved in lung morphogenesis; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
GO; GO:1904501; P:positive regulation of chromatin-mediated maintenance of transcription; IMP:BHF-UCL.
GO; GO:1904798; P:positive regulation of core promoter binding; IDA:BHF-UCL.
GO; GO:2000017; P:positive regulation of determination of dorsal identity; IDA:MGI.
GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IMP:BHF-UCL.
GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IMP:MGI.
GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IMP:MGI.
GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
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; IMP:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; IGI:MGI.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:ParkinsonsUK-UCL.
GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IMP:CACAO.
GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
GO; GO:0090279; P:regulation of calcium ion import; ISS:UniProtKB.
GO; GO:0045595; P:regulation of cell differentiation; IDA:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IDA:MGI.
GO; GO:0030997; P:regulation of centriole-centriole cohesion; ISS:UniProtKB.
GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; IMP:BHF-UCL.
GO; GO:1904499; P:regulation of chromatin-mediated maintenance of transcription; NAS:BHF-UCL.
GO; GO:1904796; P:regulation of core promoter binding; IDA:BHF-UCL.
GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI.
GO; GO:1904793; P:regulation of euchromatin binding; IDA:BHF-UCL.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:1904173; P:regulation of histone demethylase activity (H3-K4 specific); TAS:BHF-UCL.
GO; GO:0051569; P:regulation of histone H3-K4 methylation; TAS:BHF-UCL.
GO; GO:0031641; P:regulation of myelination; IMP:MGI.
GO; GO:0072182; P:regulation of nephron tubule epithelial cell differentiation; IMP:UniProtKB.
GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:MGI.
GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:MGI.
GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB.
GO; GO:0003266; P:regulation of secondary heart field cardioblast proliferation; IDA:MGI.
GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:0042129; P:regulation of T cell proliferation; IMP:MGI.
GO; GO:0051884; P:regulation of timing of anagen; IDA:CAFA.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0072053; P:renal inner medulla development; IMP:MGI.
GO; GO:0072054; P:renal outer medulla development; IMP:MGI.
GO; GO:0072001; P:renal system development; IMP:MGI.
GO; GO:0072033; P:renal vesicle formation; IMP:MGI.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; ISS:UniProtKB.
GO; GO:0016337; P:single organismal cell-cell adhesion; IMP:MGI.
GO; GO:0001501; P:skeletal system development; IMP:MGI.
GO; GO:0043588; P:skin development; IMP:MGI.
GO; GO:0051145; P:smooth muscle cell differentiation; IMP:MGI.
GO; GO:0019827; P:stem cell population maintenance; TAS:BHF-UCL.
GO; GO:0061549; P:sympathetic ganglion development; IMP:UniProtKB.
GO; GO:0050808; P:synapse organization; IMP:MGI.
GO; GO:0048489; P:synaptic vesicle transport; IMP:MGI.
GO; GO:0030217; P:T cell differentiation; IMP:MGI.
GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
GO; GO:0048538; P:thymus development; IMP:MGI.
GO; GO:0060440; P:trachea formation; IMP:MGI.
GO; GO:0060439; P:trachea morphogenesis; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0001944; P:vasculature development; IMP:MGI.
GO; GO:0001570; P:vasculogenesis; IMP:MGI.
GO; GO:0003223; P:ventricular compact myocardium morphogenesis; TAS:DFLAT.
GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
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;
3D-structure; 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_0000064272.
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:0000269|PubMed:20086044}.
REGION 156 178 Interaction with BCL9. {ECO:0000250}.
REGION 772 781 Interaction with SCRIB.
{ECO:0000269|PubMed:19458197}.
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:0000269|PubMed:20307497}.
MOD_RES 37 37 Phosphoserine; by GSK3-beta and HIPK2.
{ECO:0000269|PubMed:20307497}.
MOD_RES 41 41 Phosphothreonine; by GSK3-beta.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
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:0000269|PubMed:12640114}.
MOD_RES 191 191 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
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:0000244|PubMed:17242355,
ECO:0000269|PubMed:20361929}.
MOD_RES 556 556 Phosphothreonine.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 619 619 S-nitrosocysteine.
{ECO:0000269|PubMed:20705246}.
MOD_RES 654 654 Phosphotyrosine.
{ECO:0000250|UniProtKB:P35222}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
CARBOHYD 23 23 O-linked (GlcNAc) serine; alternate.
{ECO:0000250|UniProtKB:Q96S06}.
MUTAGEN 8 8 M->P: Loss of interaction with VCL.
{ECO:0000269|PubMed:20086044}.
MUTAGEN 33 33 S->A: Abolished HIPK2-mediated
proteasomal degradation.
{ECO:0000269|PubMed:20307497}.
MUTAGEN 37 37 S->A: Abolished HIPK2-mediated
proteasomal degradation.
{ECO:0000269|PubMed:20307497}.
MUTAGEN 552 552 S->A: Abolishes AMPK-mediated
phosphorylation.
{ECO:0000269|PubMed:20361929}.
CONFLICT 371 371 T -> I (in Ref. 2; BAB31250).
{ECO:0000305}.
CONFLICT 478 478 A -> T (in Ref. 2; BAB31250).
{ECO:0000305}.
CONFLICT 487 487 L -> F (in Ref. 2; BAB31250).
{ECO:0000305}.
HELIX 85 88 {ECO:0000244|PDB:4ONS}.
HELIX 90 98 {ECO:0000244|PDB:4ONS}.
HELIX 100 102 {ECO:0000244|PDB:4ONS}.
HELIX 121 141 {ECO:0000244|PDB:1DOW}.
TURN 145 148 {ECO:0000244|PDB:1DOW}.
TURN 150 152 {ECO:0000244|PDB:1I7W}.
HELIX 153 160 {ECO:0000244|PDB:1I7W}.
STRAND 161 164 {ECO:0000244|PDB:1JPP}.
STRAND 166 168 {ECO:0000244|PDB:4EVP}.
HELIX 169 171 {ECO:0000244|PDB:4EVP}.
HELIX 172 178 {ECO:0000244|PDB:4EV8}.
HELIX 182 189 {ECO:0000244|PDB:4EV8}.
STRAND 192 194 {ECO:0000244|PDB:4EV8}.
HELIX 195 204 {ECO:0000244|PDB:4EV8}.
HELIX 208 221 {ECO:0000244|PDB:4EV8}.
HELIX 225 233 {ECO:0000244|PDB:4EV8}.
HELIX 236 242 {ECO:0000244|PDB:4EV8}.
HELIX 243 245 {ECO:0000244|PDB:4EV8}.
HELIX 249 265 {ECO:0000244|PDB:4EV8}.
HELIX 269 275 {ECO:0000244|PDB:4EV8}.
HELIX 278 284 {ECO:0000244|PDB:4EV8}.
HELIX 285 287 {ECO:0000244|PDB:4EV8}.
HELIX 291 305 {ECO:0000244|PDB:4EV8}.
HELIX 309 317 {ECO:0000244|PDB:4EV8}.
HELIX 320 330 {ECO:0000244|PDB:4EV8}.
HELIX 334 347 {ECO:0000244|PDB:4EV8}.
HELIX 353 359 {ECO:0000244|PDB:4EV8}.
HELIX 362 367 {ECO:0000244|PDB:4EV8}.
TURN 368 371 {ECO:0000244|PDB:4EV8}.
HELIX 375 389 {ECO:0000244|PDB:4EV8}.
HELIX 399 408 {ECO:0000244|PDB:4EV8}.
HELIX 414 428 {ECO:0000244|PDB:4EV8}.
HELIX 432 440 {ECO:0000244|PDB:4EV8}.
HELIX 443 454 {ECO:0000244|PDB:4EV8}.
HELIX 458 471 {ECO:0000244|PDB:4EV8}.
STRAND 473 475 {ECO:0000244|PDB:4EV8}.
HELIX 478 487 {ECO:0000244|PDB:4EV8}.
HELIX 491 496 {ECO:0000244|PDB:4EV8}.
HELIX 504 517 {ECO:0000244|PDB:4EV8}.
HELIX 521 523 {ECO:0000244|PDB:4EV8}.
HELIX 524 529 {ECO:0000244|PDB:4EV8}.
HELIX 532 547 {ECO:0000244|PDB:4EV8}.
HELIX 566 580 {ECO:0000244|PDB:4EV8}.
HELIX 584 592 {ECO:0000244|PDB:4EV8}.
HELIX 596 602 {ECO:0000244|PDB:4EV8}.
HELIX 608 621 {ECO:0000244|PDB:4EV8}.
HELIX 625 633 {ECO:0000244|PDB:4EV8}.
TURN 634 636 {ECO:0000244|PDB:3OUX}.
HELIX 637 643 {ECO:0000244|PDB:4EV8}.
HELIX 649 661 {ECO:0000244|PDB:4EV8}.
SEQUENCE 781 AA; 85471 MW; D708F170A3FBED6E 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
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 GAQGEALGYR QDDPSYRSFH
SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD
L


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