Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Catenin beta-1  

UniProtKB / Swiss-Prot ID :  CTNB1_MOUSE

Gene Name (Synonyms) : 
Ctnnb1, Catnb  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm. Cytoplasm, cytoskeleton. Nucleus. Cell junction, adherens junction (By similarity). Cell junction (By similarity). Cell membrane (By similarity). Cytoplasm, cytoskeleton, centrosome (By similarity). Cytoplasm, cytoskeleton, spindle pole (By si 

Protein 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. 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 (By similarity). 

Protein Sequence MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGF...
Predicted Secondary Structure CCCHHHHHHHHCCCCHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCHHEEECHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
23PhosphoserineKAAVSHWQQ
HHHHHHHHH
17.80Phosphositeplus
Link-
29PhosphoserineWQQQSYLDS
HHHHHHHHH
24.27Phosphositeplus
Link-
33PhosphoserineSYLDSGIHS
HHHHHHHHC
36.73Phosphositeplus
Link-
33Phosphoserine; by GSK3-beta and HIPK2.SYLDSGIHS
HHHHHHHHC
36.73UniProtKB
Link-
37PhosphoserineSGIHSGATT
HHHHCCCCC
28.36Phosphositeplus
Link-
37Phosphoserine; by GSK3-beta and HIPK2.SGIHSGATT
HHHHCCCCC
28.36UniProtKB
Link-
41PhosphothreonineSGATTTAPS
CCCCCCCCC
22.04Phosphositeplus
Link-
45PhosphoserineTTAPSLSGK
CCCCCCCCC
32.48Phosphositeplus
Link-
49N6-acetyllysineSLSGKGNPE
CCCCCCCCC
52.73Phosphositeplus
Link-
86PhosphotyrosineIDGQYAMTR
HHHHHHHHH
12.13Phosphositeplus
Link-
142PhosphotyrosineNLINYQDDA
HHHHHHHHH
13.31Phosphositeplus
Link
191PhosphoserineAIMRSPQMV
HHHHCCCCH
11.34Phosphositeplus
Link-
191PhosphoserineAIMRSPQMV
HHHHCCCCH
11.34SysPTM
Link-
194Methionine sulfoneRSPQMVSAI
HCCCCHHHH
2.67SysPTM
Link-
213S-nitrosocysteineETARCTAGT
HHHHHHHHH
2.58dbSNO
Link-
393PhosphothreonineSDAATKQEG
CCCHHHHHH
34.67Phosphositeplus
Link-
489PhosphotyrosineVRLHYGLPV
HHHHCCHHH
25.58Phosphositeplus
Link-
551PhosphothreonineTQRRTSMGG
HHHHHHCCC
25.84PhosphoELM
Link-
551PhosphothreonineTQRRTSMGG
HHHHHHCCC
25.84Phosphositeplus
Link-
551PhosphothreonineTQRRTSMGG
HHHHHHCCC
25.84SysPTM
Link-
551Phosphothreonine.TQRRTSMGG
HHHHHHCCC
25.84UniProtKB
Link-
552PhosphoserineQRRTSMGGT
HHHHHCCCC
17.39PhosphoELM
Link-
552PhosphoserineQRRTSMGGT
HHHHHCCCC
17.39Phosphositeplus
Link-
552PhosphoserineQRRTSMGGT
HHHHHCCCC
17.39SysPTM
Link-
552Phosphoserine; by AMPK.QRRTSMGGT
HHHHHCCCC
17.39UniProtKB
Link-
553Methionine sulfoneRRTSMGGTQ
HHHHCCCCH
5.92SysPTM
Link-
556PhosphothreonineSMGGTQQQF
HCCCCHHHH
19.92PhosphoELM
Link-
556PhosphothreonineSMGGTQQQF
HCCCCHHHH
19.92Phosphositeplus
Link-
556PhosphothreonineSMGGTQQQF
HCCCCHHHH
19.92SysPTM
Link-
556Phosphothreonine.SMGGTQQQF
HCCCCHHHH
19.92UniProtKB
Link-
605PhosphoserineQLLYSPIEN
HHHCCCCHH
21.26Phosphositeplus
Link-
653PhosphothreonineEGVATYAAA
HHHHHHHHH
15.99Phosphositeplus
Link-
654PhosphotyrosineGVATYAAAV
HHHHHHHHH
5.63Phosphositeplus
Link-
654PhosphotyrosineGVATYAAAV
HHHHHHHHH
5.63SysPTM
Link-
654Phosphotyrosine.GVATYAAAV
HHHHHHHHH
5.63UniProtKB
Link-
675PhosphoserineKKRLSVELT
HHHHHHHHH
19.99Phosphositeplus
Link-
675PhosphoserineKKRLSVELT
HHHHHHHHH
19.99SysPTM
Link-
675Phosphoserine.KKRLSVELT
HHHHHHHHH
19.99UniProtKB
Link-
679PhosphothreonineSVELTSSLF
HHHHHHHHH
11.63Phosphositeplus
Link-
681PhosphoserineELTSSLFRT
HHHHHHHHC
26.71Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551 AND THR-556, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551; SER-552 ANDTHR-556, AND MASS SPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-654, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND SER-675, ANDMASS SPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND MASSSPECTROMETRY.
"Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-cateninfor phosphorylation and proteasomal degradation.";
Kim E.-A., Kim J.E., Sung K.S., Choi D.W., Lee B.J., Choi C.Y.;
Biochem. Biophys. Res. Commun. 394:966-971(2010).
Cited for: PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2, AND MUTAGENESIS OFSER-33 AND SER-37.
"AMP-activated protein kinase (AMPK) cross-talks with canonical Wntsignaling via phosphorylation of beta-catenin at Ser 552.";
Zhao J., Yue W., Zhu M.J., Sreejayan N., Du M.;
Biochem. Biophys. Res. Commun. 395:146-151(2010).
Cited for: PHOSPHORYLATION AT SER-552, AND MUTAGENESIS OF SER-552.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures