CTNNB1
entrez
1499
canonical
uniprot
P35222
canonical
ensembl
ENSG00000168036
resolver
ensp
ENSP00000344456
resolver
ensp
ENSP00000379486
resolver
ensp
ENSP00000379488
resolver
ensp
ENSP00000385604
resolver
ensp
ENSP00000387455
resolver
ensp
ENSP00000400508
resolver
ensp
ENSP00000401599
resolver
ensp
ENSP00000409302
resolver
ensp
ENSP00000411226
resolver
ensp
ENSP00000412219
resolver
ensp
ENSP00000493533
resolver
ensp
ENSP00000493583
resolver
ensp
ENSP00000493610
resolver
ensp
ENSP00000494053
resolver
ensp
ENSP00000494411
resolver
ensp
ENSP00000494467
resolver
ensp
ENSP00000494677
resolver
ensp
ENSP00000494780
resolver
ensp
ENSP00000494845
resolver
ensp
ENSP00000494914
resolver
ensp
ENSP00000495076
resolver
ensp
ENSP00000495161
resolver
ensp
ENSP00000495244
resolver
ensp
ENSP00000495286
resolver
ensp
ENSP00000495360
resolver
ensp
ENSP00000495426
resolver
ensp
ENSP00000495450
resolver
ensp
ENSP00000495719
resolver
ensp
ENSP00000495794
resolver
ensp
ENSP00000495992
resolver
ensp
ENSP00000496021
resolver
ensp
ENSP00000496067
resolver
ensp
ENSP00000496180
resolver
ensp
ENSP00000496295
resolver
ensp
ENSP00000496385
resolver
ensp
ENSP00000580271
resolver
ensp
ENSP00000580273
resolver
ensp
ENSP00000580274
resolver
ensp
ENSP00000602615
resolver
ensp
ENSP00000638500
resolver
ensp
ENSP00000638501
resolver
ensp
ENSP00000790563
resolver
enst
ENST00000349496
resolver
enst
ENST00000396183
resolver
enst
ENST00000396185
resolver
enst
ENST00000405570
resolver
enst
ENST00000426215
resolver
enst
ENST00000431914
resolver
enst
ENST00000433400
resolver
enst
ENST00000441708
resolver
enst
ENST00000450969
resolver
enst
ENST00000453024
resolver
enst
ENST00000642248
resolver
enst
ENST00000642315
resolver
enst
ENST00000642426
resolver
enst
ENST00000642836
resolver
enst
ENST00000642992
resolver
enst
ENST00000643031
resolver
enst
ENST00000643297
resolver
enst
ENST00000643541
resolver
enst
ENST00000643977
resolver
enst
ENST00000643992
resolver
enst
ENST00000644524
resolver
enst
ENST00000644678
resolver
enst
ENST00000644867
resolver
enst
ENST00000645210
resolver
enst
ENST00000645320
resolver
enst
ENST00000645493
resolver
enst
ENST00000645900
resolver
enst
ENST00000645982
resolver
enst
ENST00000646116
resolver
enst
ENST00000646174
resolver
enst
ENST00000646369
resolver
enst
ENST00000646381
resolver
enst
ENST00000646725
resolver
enst
ENST00000647390
resolver
enst
ENST00000647413
resolver
enst
ENST00000910212
resolver
enst
ENST00000910214
resolver
enst
ENST00000910215
resolver
enst
ENST00000932556
resolver
enst
ENST00000968441
resolver
enst
ENST00000968442
resolver
genesymbol
CTNNB1
resolver
genesymbol_syn
CTNNB
resolver
hgnc
HGNC:2514
resolver
uniprot
A0ACM8QGB4
resolver
uniprot
A8K1L7
resolver
uniprot
B4DGU4
resolver
uniprot
C9IZ65
resolver
uniprot
Q8NEW9
resolver
uniprot
Q8NI94
resolver
uniprot
Q9H391
resolver
uniprot_entry
A0ACM8QGB4_HUMAN
resolver
uniprot_entry
B4DGU4_HUMAN
resolver
uniprot_entry
CTNB1_HUMAN
resolver
uniprot_sec
A8K1L7
resolver
uniprot_sec
C9IZ65
resolver
uniprot_sec
Q8NEW9
resolver
uniprot_sec
Q8NI94
resolver
uniprot_sec
Q9H391
resolver
amino_acid_sequence
MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL
uniprot
proteins
disease_involvement
DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:9065402}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Note=Activating mutations in CTNNB1 have oncogenic activity resulting in tumor development. Somatic mutations are found in various tumor types, including colon cancers, ovarian and prostate carcinomas, hepatoblastoma (HB), hepatocellular carcinoma (HCC). HBs are malignant embryonal tumors mainly affecting young children in the first three years of life.; DISEASE: Pilomatrixoma (PTR) [MIM:132600]: Common benign skin tumor. {ECO:0000269|PubMed:10192393, ECO:0000269|PubMed:11703283, ECO:0000269|PubMed:12027456}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. {ECO:0000269|PubMed:10666372, ECO:0000269|PubMed:12027456}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. {ECO:0000269|PubMed:10391090}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving CTNNB1 is found in salivary gland pleiomorphic adenomas, the most common benign epithelial tumors of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1. {ECO:0000269|PubMed:10029085, ECO:0000269|PubMed:9020842}.; DISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle-shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos. {ECO:0000269|PubMed:11464291}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Neurodevelopmental disorder with spastic diplegia and visual defects (NEDSDV) [MIM:615075]: An autosomal dominant disorder characterized by global developmental delay, severe intellectual disability with absent or very limited speech, microcephaly, spasticity, and visual abnormalities. {ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:25326669, ECO:0000269|PubMed:28514307}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Vitreoretinopathy, exudative 7 (EVR7) [MIM:617572]: An autosomal dominant form of exudative vitreoretinopathy, a disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery. {ECO:0000269|PubMed:28575650}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Key downstream component of the canonical Wnt signaling pathway (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). 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 (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). 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 (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). Also acts as a coactivator for other transcription factors, such as NR5A2 (PubMed:22187462). Promotes epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via driving transcription of CTNNB1/TCF-target genes (PubMed:29910125). Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex (By similarity). Acts as a negative regulator of centrosome cohesion (PubMed:18086858). Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization (PubMed:21262353). Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2 (PubMed:18957423). Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity). 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 (By similarity). 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 (By similarity). Activity is repressed in a MSX1-mediated manner at the bell stage of mesenchymal tooth germ formation which prevents premature differentiation of odontoblasts (By similarity). {ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:17524503, ECO:0000269|PubMed:18077326, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18957423, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22187462, ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:22699938, ECO:0000269|PubMed:29910125}.
uniprot
proteins
mass_dalton
85497
uniprot
proteins
mutagenesis
MUTAGEN 29; /note="S->F: No effect."; /evidence="ECO:0000269|PubMed:12027456"; MUTAGEN 64; /note="Y->F: Abolishes phosphorylation by PTK6."; /evidence="ECO:0000269|PubMed:20026641"; MUTAGEN 142; /note="Y->E: No effect on interaction with BCL9 and BCL9L."; /evidence="ECO:0000269|PubMed:17052462"; MUTAGEN 156; /note="L->A: Abolishes interaction with BCL9 but no effect on interaction with CDH3; when associated with A-159."; /evidence="ECO:0000269|PubMed:17052462"; MUTAGEN 159; /note="L->A: No effect on interaction with BCL9 and CDH3. Abolishes interaction with BCL9 but no effect on interaction with CDH3; when associated with A-156."; /evidence="ECO:0000269|PubMed:17052462"; MUTAGEN 178; /note="L->A: No effect on interaction with BCL9 and CDH3."; /evidence="ECO:0000269|PubMed:17052462"; MUTAGEN 253; /note="F->A: Abolishes or strongly reduces AXIN2 binding."; /evidence="ECO:0000269|PubMed:10966653"; MUTAGEN 260; /note="H->A: Abolishes or strongly reduces AXIN1 and AXIN2 binding. Strongly reduces phosphorylation and degradation; when associated with A-386 and A-383."; /evidence="ECO:0000269|PubMed:10966653"; MUTAGEN 292; /note="K->A: Abolishes or strongly reduces AXIN1 and AXIN2 binding."; /evidence="ECO:0000269|PubMed:10966653"; MUTAGEN 312; /note="K->E: Abolishes TCF7L2 binding."; /evidence="ECO:0000269|PubMed:11713475"; MUTAGEN 333; /note="Y->F: Abolished phosphorylation by SRC and interaction with isoform M2 of PKM (PKM2)."; /evidence="ECO:0000269|PubMed:22056988"; MUTAGEN 345; /note="K->A: Abolishes APC binding."; /evidence="ECO:0000269|PubMed:10966653"; MUTAGEN 383; /note="W->A: Abolishes APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-386."; /evidence="ECO:0000269|PubMed:10966653"; MUTAGEN 386; /note="R->A: Strongly reduces APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-383."; /evidence="ECO:0000269|PubMed:10966653"; MUTAGEN 426; /note="N->A: Abolishes TCF7L2 and LEF1 binding."; /evidence="ECO:0000269|PubMed:10966653"; MUTAGEN 435; /note="K->A: Strongly reduces or abolishes LEF1 binding."; /evidence="ECO:0000269|PubMed:10966653, ECO:0000269|PubMed:11713475"; MUTAGEN 435; /note="K->E: Abolishes TCF7L2 binding."; /evidence="ECO:0000269|PubMed:10966653, ECO:0000269|PubMed:11713475"; MUTAGEN 469; /note="R->A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding."; /evidence="ECO:0000269|PubMed:10966653"; MUTAGEN 470; /note="H->A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding."; /evidence="ECO:0000269|PubMed:10966653"; MUTAGEN 508; /note="K->A: Abolishes TCF7L2 and LEF1 binding."; /evidence="ECO:0000269|PubMed:10966653"; MUTAGEN 660; /note="F->A: Abolishes CTNNBIP1 binding; when associated with A-661."; /evidence="ECO:0000269|PubMed:12408824"; MUTAGEN 661; /note="R->A: Abolishes CTNNBIP1 binding; when associated with A-660."; /evidence="ECO:0000269|PubMed:12408824
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-552 by AMPK promotes stabilization of the protein, enhancing TCF/LEF-mediated transcription (By similarity). Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase (PubMed:10966653, PubMed:12027456, PubMed:12051714). Phosphorylation proceeds then from Thr-41 to Ser-37 and Ser-33 (PubMed:12077367, PubMed:25169422). Phosphorylated by NEK2 (PubMed:18086858). EGF stimulates tyrosine phosphorylation (PubMed:10187801). 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 (PubMed:17009320). Phosphorylation by CDK2 regulates insulin internalization (PubMed:21262353). 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 (PubMed:20026641). Phosphorylation by SRC at Tyr-333 promotes interaction with isoform M2 of PKM (PKM2); promoting transcription activation (PubMed:22056988). {ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:10187801, ECO:0000269|PubMed:10966653, ECO:0000269|PubMed:12027456, ECO:0000269|PubMed:12051714, ECO:0000269|PubMed:12077367, ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:20026641, ECO:0000269|PubMed:20307497, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:22056988, ECO:0000269|PubMed:25169422}.; PTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when phosphorylated by GSK3B, leading to its degradation (PubMed:12077367). Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent proteasomal degradation (PubMed:11389839, PubMed:11389840, PubMed:20307497). Ubiquitinated and degraded following interaction with SOX9 (By similarity). Ubiquitinated via 'Lys-11'- and 'Lys-29'-linked ubiquitin chains by UBR5, leading to its stabilization (PubMed:21118991). Ubiquitinated by the SCF-FBXO16 E3 ubiquitin ligase, leading to proteasomal degradation (PubMed:30714168). {ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:11389839, ECO:0000269|PubMed:11389840, ECO:0000269|PubMed:12077367, ECO:0000269|PubMed:20307497, ECO:0000269|PubMed:21118991, ECO:0000269|PubMed:30714168}.; 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|UniProtKB:Q02248}.; 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:0000269|PubMed:24342833}.; PTM: Deacetylated at Lys-49 by SIRT1. {ECO:0000269|PubMed:24824780}.; PTM: Phosphorylated at Thr-556 by herpes virus 1/HHV-1 leading to CTNNB1 inhibition. {ECO:0000269|PubMed:24824780}.
uniprot
proteins
protein_family
Beta-catenin family
uniprot
proteins
pubmed
10029085
uniprot
proteins
pubmed
10187801
uniprot
proteins
pubmed
10192393
uniprot
proteins
pubmed
10391090
uniprot
proteins
pubmed
10398436
uniprot
proteins
pubmed
10435629
uniprot
proteins
pubmed
10655994
uniprot
proteins
pubmed
10666372
uniprot
proteins
pubmed
10679188
uniprot
proteins
pubmed
10725230
uniprot
proteins
pubmed
10966653
uniprot
proteins
pubmed
11136974
uniprot
proteins
pubmed
11279024
uniprot
proteins
pubmed
11389839
uniprot
proteins
pubmed
11389840
uniprot
proteins
pubmed
11464291
uniprot
proteins
pubmed
11590244
uniprot
proteins
pubmed
11703283
uniprot
proteins
pubmed
11713475
uniprot
proteins
pubmed
11713476
uniprot
proteins
pubmed
11751639
uniprot
proteins
pubmed
11790773
uniprot
proteins
pubmed
11834740
uniprot
proteins
pubmed
12019147
uniprot
proteins
pubmed
12027456
uniprot
proteins
pubmed
12051714
uniprot
proteins
pubmed
12077367
uniprot
proteins
pubmed
12297051
uniprot
proteins
pubmed
12370829
uniprot
proteins
pubmed
12408824
uniprot
proteins
pubmed
12420223
uniprot
proteins
pubmed
12501215
uniprot
proteins
pubmed
12640114
uniprot
proteins
pubmed
12712206
uniprot
proteins
pubmed
12830000
uniprot
proteins
pubmed
14595118
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15003504
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16424001
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16858403
uniprot
proteins
pubmed
17009320
uniprot
proteins
pubmed
17047063
uniprot
proteins
pubmed
17052462
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17289029
uniprot
proteins
pubmed
17524503
uniprot
proteins
pubmed
18077326
uniprot
proteins
pubmed
18086858
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18378692
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18819930
uniprot
proteins
pubmed
18957423
uniprot
proteins
pubmed
19433865
uniprot
proteins
pubmed
19435523
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19693690
uniprot
proteins
pubmed
19816403
uniprot
proteins
pubmed
19996314
uniprot
proteins
pubmed
20026641
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20164195
uniprot
proteins
pubmed
20307497
uniprot
proteins
pubmed
21118991
uniprot
proteins
pubmed
21132015
uniprot
proteins
pubmed
21247902
uniprot
proteins
pubmed
21262353
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21623382
uniprot
proteins
pubmed
22056988
uniprot
proteins
pubmed
22155184
uniprot
proteins
pubmed
22187462
uniprot
proteins
pubmed
22294297
uniprot
proteins
pubmed
22647378
uniprot
proteins
pubmed
22699938
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23033978
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24342833
uniprot
proteins
pubmed
24824780
uniprot
proteins
pubmed
25169422
uniprot
proteins
pubmed
25183871
uniprot
proteins
pubmed
25266658
uniprot
proteins
pubmed
25326669
uniprot
proteins
pubmed
25807484
uniprot
proteins
pubmed
27226643
uniprot
proteins
pubmed
28051089
uniprot
proteins
pubmed
28514307
uniprot
proteins
pubmed
28575650
uniprot
proteins
pubmed
28829046
uniprot
proteins
pubmed
29367600
uniprot
proteins
pubmed
29374064
uniprot
proteins
pubmed
29432739
uniprot
proteins
pubmed
29739711
uniprot
proteins
pubmed
29910125
uniprot
proteins
pubmed
30097457
uniprot
proteins
pubmed
30714168
uniprot
proteins
pubmed
31073040
uniprot
proteins
pubmed
31801859
uniprot
proteins
pubmed
38173341
uniprot
proteins
pubmed
7806582
uniprot
proteins
pubmed
7982500
uniprot
proteins
pubmed
9020842
uniprot
proteins
pubmed
9065402
uniprot
proteins
pubmed
9927029
uniprot
proteins
sequence_length
781
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22294297, ECO:0000269|PubMed:25183871, ECO:0000269|PubMed:29739711, ECO:0000269|PubMed:29910125, ECO:0000269|PubMed:31801859}. Nucleus {ECO:0000269|PubMed:21118991, ECO:0000269|PubMed:24342833, ECO:0000269|PubMed:25183871, ECO:0000269|PubMed:28829046, ECO:0000269|PubMed:29367600, ECO:0000269|PubMed:29739711, ECO:0000269|PubMed:29910125, ECO:0000269|PubMed:30714168, ECO:0000269|PubMed:31801859}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:B6V8E6}. Cell junction, adherens junction {ECO:0000269|PubMed:10725230, ECO:0000269|PubMed:22294297}. Cell junction {ECO:0000250|UniProtKB:B6V8E6}. Cell membrane {ECO:0000269|PubMed:11790773, ECO:0000269|PubMed:24342833}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. 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 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 (PubMed:25183871). 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 (By similarity). Localizes to cell-cell contacts as keratinocyte differentiation progresses (By similarity). {ECO:0000250|UniProtKB:B6V8E6, ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:25183871}.
uniprot
proteins