Ctnnb1
entrez
12387
canonical
uniprot
Q02248
canonical
ensembl
ENSMUSG00000006932
resolver
ensp
ENSMUSP00000007130
resolver
ensp
ENSMUSP00000136294
resolver
enst
ENSMUST00000007130
resolver
enst
ENSMUST00000178812
resolver
genesymbol
Ctnnb1
resolver
genesymbol_syn
Catnb
resolver
uniprot
Q922W1
resolver
uniprot
Q9D335
resolver
uniprot_entry
CTNB1_MOUSE
resolver
uniprot_sec
Q922W1
resolver
uniprot_sec
Q9D335
resolver
amino_acid_sequence
MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEALGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL
uniprot
proteins
function
FUNCTION: Key downstream component of the canonical Wnt signaling pathway (PubMed:15132997). 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 (By similarity). Also acts as a coactivator for other transcription factors, such as NR5A2 (By similarity). Promotes epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via driving transcription of CTNNB1/TCF-target genes (By similarity). Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex (PubMed:16325582, PubMed:18093941). 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). Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling (PubMed:15132997). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, via promoting the transcription of differentiation factors such as LEF1, BMP2 and BMP4 (PubMed:29148101). Activity is repressed in a MSX1-mediated manner at the bell stage of mesenchymal tooth germ formation which prevents premature differentiation of odontoblasts (PubMed:29148101). {ECO:0000250|UniProtKB:P35222, ECO:0000269|PubMed:15132997, ECO:0000269|PubMed:16325582, ECO:0000269|PubMed:18093941, ECO:0000269|PubMed:21325504, ECO:0000269|PubMed:29148101}.
uniprot
proteins
mass_dalton
85471
uniprot
proteins
mutagenesis
MUTAGEN 8; /note="M->P: Loss of interaction with VCL."; /evidence="ECO:0000269|PubMed:20086044"; MUTAGEN 33; /note="S->A: Abolished HIPK2-mediated proteasomal degradation."; /evidence="ECO:0000269|PubMed:20307497"; MUTAGEN 37; /note="S->A: Abolished HIPK2-mediated proteasomal degradation."; /evidence="ECO:0000269|PubMed:20307497"; MUTAGEN 552; /note="S->A: Abolishes AMPK-mediated phosphorylation."; /evidence="ECO:0000269|PubMed:20361929
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-552 by AMPK promotes stabilization of the protein, enhancing TCF/LEF-mediated transcription (PubMed:20361929). Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase (By similarity). Phosphorylation proceeds then from Thr-41 to Ser-37 and Ser-33 (By similarity). Phosphorylated by NEK2 (By similarity). EGF stimulates tyrosine phosphorylation (By similarity). Phosphorylated on Ser-33 and Ser-37 by HIPK2 and GSK3B, this phosphorylation triggers proteasomal degradation (PubMed:20307497). Phosphorylation on Ser-191 and Ser-246 by CDK5 (By similarity). 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). Phosphorylation by SRC at Tyr-333 promotes interaction with isoform M2 of PKM (PKM2); promoting transcription activation (By similarity). {ECO:0000250|UniProtKB:P35222, ECO:0000269|PubMed:20307497, ECO:0000269|PubMed:20361929}.; PTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when phosphorylated by GSK3B, leading to its degradation (By similarity). Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent proteasomal degradation (By similarity). Ubiquitinated and degraded following interaction with SOX9 (PubMed:15132997). Ubiquitinated via 'Lys-11'- and 'Lys-29'-linked ubiquitin chains by UBR5, leading to its stabilization (By similarity). Ubiquitinated by the SCF-FBXO16 E3 ubiquitin ligase, leading to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P35222, ECO:0000305|PubMed:15132997}.; 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}.
uniprot
proteins
protein_family
Beta-catenin family
uniprot
proteins
pubmed
10581160
uniprot
proteins
pubmed
10679188
uniprot
proteins
pubmed
10772923
uniprot
proteins
pubmed
10882138
uniprot
proteins
pubmed
11348595
uniprot
proteins
pubmed
11590244
uniprot
proteins
pubmed
11707392
uniprot
proteins
pubmed
12408825
uniprot
proteins
pubmed
12494996
uniprot
proteins
pubmed
12640114
uniprot
proteins
pubmed
12874278
uniprot
proteins
pubmed
14687547
uniprot
proteins
pubmed
15063782
uniprot
proteins
pubmed
1509266
uniprot
proteins
pubmed
15132997
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16325582
uniprot
proteins
pubmed
17052462
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17289029
uniprot
proteins
pubmed
17344318
uniprot
proteins
pubmed
17925400
uniprot
proteins
pubmed
18093941
uniprot
proteins
pubmed
19458197
uniprot
proteins
pubmed
19816403
uniprot
proteins
pubmed
20086044
uniprot
proteins
pubmed
20307497
uniprot
proteins
pubmed
20361929
uniprot
proteins
pubmed
20413591
uniprot
proteins
pubmed
20705246
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21325504
uniprot
proteins
pubmed
21623382
uniprot
proteins
pubmed
22510880
uniprot
proteins
pubmed
25232112
uniprot
proteins
pubmed
25979161
uniprot
proteins
pubmed
27015268
uniprot
proteins
pubmed
27375112
uniprot
proteins
pubmed
29148101
uniprot
proteins
pubmed
30389919
uniprot
proteins
pubmed
31073040
uniprot
proteins
pubmed
32533114
uniprot
proteins
pubmed
7982500
uniprot
proteins
pubmed
9298899
uniprot
proteins
pubmed
9783587
uniprot
proteins
sequence_length
781
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27015268, ECO:0000269|PubMed:27375112, ECO:0000269|PubMed:30389919}. Nucleus {ECO:0000269|PubMed:27015268, ECO:0000269|PubMed:30389919}. Cytoplasm, cytoskeleton. Cell junction, adherens junction {ECO:0000269|PubMed:20705246, ECO:0000269|PubMed:27375112}. Cell junction {ECO:0000269|PubMed:12494996}. Cell membrane {ECO:0000269|PubMed:27015268}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P35222}. Synapse {ECO:0000269|PubMed:20705246}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21623382}. Note=Colocalized with RAPGEF2 and TJP1 at cell-cell contacts (By similarity). Cytoplasmic when it is un-stable (highly phosphorylated) 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 CTNNB1 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). Translocates to the nucleus in the presence of SNAIL1 (By similarity). Ca(2+)-mediated localization to the cell membrane in dental epithelial cells is inhibited via WNT3A (PubMed:27015268). Localizes to cell-cell contacts as keratinocyte differentiation progresses (PubMed:27375112). {ECO:0000250|UniProtKB:B6V8E6, ECO:0000250|UniProtKB:P35222, ECO:0000269|PubMed:27015268, ECO:0000269|PubMed:27375112}.
uniprot
proteins