P35222 (CTNB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catenin beta-1

Alternative name(s):
Beta-catenin

Gene names

Name:	CTNNB1
Synonyms:	CTNNB
ORF Names:	OK/SW-cl.35, PRO2286

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	781 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. Ref.37 Ref.40 Ref.41 Ref.47 Ref.56 Ref.60 Ref.61
Subunit structure	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 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 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 By similarity. Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits the transcriptional activity of CTNNB1 By similarity. Interacts with AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1. Interacts with GLIS2 and MUC1. Interacts with SLC30A9. Interacts with XIRP1 By similarity. Interacts directly with AXIN1; the interaction is regulated by CDK2 phosphorylation of AXIN1 By similarity. Interacts with SCRIB By similarity. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain). Interacts with EMD. Interacts with TNIK and TCF7L2. Interacts with SESTD1 and TRPC4. Interacts with CAV1. Interacts with TRPV4. The TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with VCL By similarity. Interacts with PTPRJ. Interacts with PKT7 and CDK2. Interacts with FAT1 (via the cytoplasmic domain) By similarity. Interacts with NANOS1 and NDRG2. Interacts with isoform 1 of NEK2. Interacts with both isoform 1 and isoform 2 of CDK5. 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 (isoform PML-4). Ref.10 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.24 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.43 Ref.44 Ref.46 Ref.50 Ref.51 Ref.52 Ref.53 Ref.56 Ref.57 Ref.58 Ref.60 Ref.61
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton. Cell junction › adherens junction. Cell junction. Cell membrane. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle pole. Note: 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. Co-localizes with CDK5 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells. Ref.34 Ref.36 Ref.37 Ref.38 Ref.39 Ref.41 Ref.56
Tissue specificity	Expressed in several hair follicle cell types: basal and peripheral matrix cells, and cells of the outer and inner root sheaths. Expressed in colon. Present in cortical neurons (at protein level). Ref.15 Ref.38 Ref.39
Post-translational modification	Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription By similarity. Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-37 and 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 on Ser-191 and Ser-246 by CDK5. Phosphorylation by CDK2 regulates insulin internalization. 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. Ref.13 Ref.14 Ref.17 Ref.23 Ref.25 Ref.26 Ref.27 Ref.32 Ref.39 Ref.41 Ref.49 Ref.53 Ref.56 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. Ref.13 Ref.14 Ref.17 Ref.23 Ref.25 Ref.26 Ref.27 Ref.32 Ref.39 Ref.41 Ref.49 Ref.53 Ref.56 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 By similarity.
Involvement in 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. Note: The gene represented in this entry may be involved in disease pathogenesis. 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. Pilomatrixoma (PTR) [MIM:132600]: Common benign skin tumor. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.25 Ref.71 Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Note: The gene represented in this entry may be involved in disease pathogenesis. Ref.25 Ref.73 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. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. 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. 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. Note: The gene represented in this entry may be involved in disease pathogenesis. Ref.21
Sequence similarities	Belongs to the beta-catenin family. Contains 12 ARM repeats.
Sequence caution	The sequence BAB93475.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell adhesion Transcription Transcription regulation Wnt signaling pathway
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Disease mutation
Domain	Repeat
Molecular function	Activator
PTM	Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Schwann cell proliferation Inferred from Biological aspect of Ancestor. Source: RefGenome T cell differentiation in thymus Inferred from Biological aspect of Ancestor. Source: RefGenome adherens junction assembly Inferred from mutant phenotype PubMed 20086044PubMed 20123964. Source: BHF-UCL androgen receptor signaling pathway Non-traceable author statement PubMed 15572661. Source: UniProtKB anterior/posterior axis specification Inferred from electronic annotation. Source: Compara bone resorption Inferred from electronic annotation. Source: Compara branching involved in ureteric bud morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome canonical Wnt receptor signaling pathway involved in negative regulation of apoptotic process Inferred from mutant phenotype PubMed 12154096. Source: BHF-UCL canonical Wnt receptor signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation Inferred from sequence or structural similarity. Source: BHF-UCL canonical Wnt receptor signaling pathway involved in positive regulation of epithelial to mesenchymal transition Inferred from mutant phenotype PubMed 17072303. Source: BHF-UCL cell fate specification Inferred from electronic annotation. Source: Compara cell maturation Inferred from electronic annotation. Source: Compara cell-cell adhesion Inferred from mutant phenotype PubMed 18593713. Source: BHF-UCL cell-matrix adhesion Inferred from Biological aspect of Ancestor. Source: RefGenome cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome cellular response to growth factor stimulus Inferred from mutant phenotype Ref.36. Source: BHF-UCL cellular response to indole-3-methanol Inferred from direct assay PubMed 10868478. Source: UniProtKB central nervous system vasculogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome cytoskeletal anchoring at plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome determination of dorsal/ventral asymmetry Inferred from Biological aspect of Ancestor. Source: RefGenome dorsal/ventral axis specification Inferred from Biological aspect of Ancestor. Source: RefGenome ectoderm development Inferred from Biological aspect of Ancestor. Source: RefGenome embryonic axis specification Inferred from Biological aspect of Ancestor. Source: RefGenome embryonic digit morphogenesis Inferred from electronic annotation. Source: Compara embryonic foregut morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome embryonic forelimb morphogenesis Inferred from electronic annotation. Source: Compara embryonic heart tube development Inferred from electronic annotation. Source: Compara embryonic hindlimb morphogenesis Inferred from electronic annotation. Source: Compara embryonic skeletal limb joint morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL endodermal cell fate commitment Inferred from Biological aspect of Ancestor. Source: RefGenome endothelial tube morphogenesis Inferred from mutant phenotype PubMed 20123964. Source: BHF-UCL epithelial cell differentiation involved in prostate gland development Inferred from electronic annotation. Source: Compara epithelial to mesenchymal transition Traceable author statement PubMed 14679171. Source: HGNC epithelial tube branching involved in lung morphogenesis Inferred from electronic annotation. Source: Compara forebrain development Inferred from electronic annotation. Source: Compara fungiform papilla formation Inferred from electronic annotation. Source: Compara gastrulation with mouth forming second Inferred from Biological aspect of Ancestor. Source: RefGenome genitalia morphogenesis Inferred from electronic annotation. Source: Compara glial cell fate determination Inferred from Biological aspect of Ancestor. Source: RefGenome hair cell differentiation Traceable author statement PubMed 19251162. Source: BHF-UCL hair follicle morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome hair follicle placode formation Inferred from Biological aspect of Ancestor. Source: RefGenome hindbrain development Inferred from Biological aspect of Ancestor. Source: RefGenome in utero embryonic development Inferred from electronic annotation. Source: Compara lens morphogenesis in camera-type eye Inferred from electronic annotation. Source: Compara liver development Inferred from Biological aspect of Ancestor. Source: RefGenome lung cell differentiation Inferred from Biological aspect of Ancestor. Source: RefGenome lung induction Inferred from Biological aspect of Ancestor. Source: RefGenome lung-associated mesenchyme development Inferred from Biological aspect of Ancestor. Source: RefGenome male genitalia development Inferred from Biological aspect of Ancestor. Source: RefGenome mesenchymal cell proliferation involved in lung development Inferred from Biological aspect of Ancestor. Source: RefGenome mesenchymal to epithelial transition involved in metanephros morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome midgut development Inferred from electronic annotation. Source: Compara myoblast differentiation Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from direct assay PubMed 12970740. Source: UniProtKB negative regulation of chondrocyte differentiation Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of heart induction by canonical Wnt receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of oligodendrocyte differentiation Inferred from electronic annotation. Source: Compara negative regulation of osteoclast differentiation Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of protein sumoylation Inferred from direct assay Ref.61. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from Biological aspect of Ancestor. Source: RefGenome nephron tubule formation Inferred from Biological aspect of Ancestor. Source: RefGenome neural plate development Inferred from electronic annotation. Source: Compara neuron migration Inferred from electronic annotation. Source: Compara odontogenesis of dentin-containing tooth Inferred from Biological aspect of Ancestor. Source: RefGenome oocyte development Inferred from Biological aspect of Ancestor. Source: RefGenome osteoclast differentiation Inferred from electronic annotation. Source: Compara oviduct development Inferred from electronic annotation. Source: Compara pancreas development Inferred from Biological aspect of Ancestor. Source: RefGenome patterning of blood vessels Inferred by curator PubMed 20123964. Source: BHF-UCL positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of MAPK cascade Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of apoptotic process Inferred from direct assay PubMed 12970740. Source: UniProtKB positive regulation of branching involved in lung morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of determination of dorsal identity Inferred from electronic annotation. Source: Compara positive regulation of endothelial cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of epithelial cell proliferation involved in prostate gland development Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of fibroblast growth factor receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of heparan sulfate proteoglycan biosynthetic process Inferred from mutant phenotype PubMed 15853773. Source: BHF-UCL positive regulation of mesenchymal cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of muscle cell differentiation Traceable author statement. Source: Reactome positive regulation of neuroblast proliferation Inferred from electronic annotation. Source: Compara positive regulation of osteoblast differentiation Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.16PubMed 14660579Ref.66. Source: BHF-UCL protein heterooligomerization Inferred from electronic annotation. Source: Compara protein localization to cell surface Inferred from mutant phenotype PubMed 20086044. Source: BHF-UCL proximal/distal pattern formation Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of T cell proliferation Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of angiogenesis Traceable author statement PubMed 18756595. Source: BHF-UCL regulation of calcium ion import Inferred from direct assay Ref.51. Source: BHF-UCL regulation of centriole-centriole cohesion Inferred from direct assay Ref.41. Source: UniProtKB regulation of centromeric sister chromatid cohesion Inferred from mutant phenotype PubMed 20300119. Source: BHF-UCL regulation of fibroblast proliferation Traceable author statement Ref.36. Source: BHF-UCL regulation of myelination Inferred from electronic annotation. Source: Compara regulation of nephron tubule epithelial cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB regulation of protein localization to cell surface Inferred from direct assay Ref.51. Source: BHF-UCL regulation of secondary heart field cardioblast proliferation Inferred from electronic annotation. Source: Compara regulation of smooth muscle cell proliferation Inferred from mutant phenotype PubMed 17122440. Source: BHF-UCL renal inner medulla development Inferred from Biological aspect of Ancestor. Source: RefGenome renal outer medulla development Inferred from Biological aspect of Ancestor. Source: RefGenome renal vesicle formation Inferred from Biological aspect of Ancestor. Source: RefGenome response to cadmium ion Inferred from electronic annotation. Source: Compara response to cytokine stimulus Inferred from electronic annotation. Source: Compara response to drug Inferred from expression pattern PubMed 18291362. Source: UniProtKB response to estradiol stimulus Inferred from direct assay PubMed 15304487. Source: BHF-UCL skin development Inferred from electronic annotation. Source: Compara smooth muscle cell differentiation Inferred from Biological aspect of Ancestor. Source: RefGenome synapse organization Inferred from Biological aspect of Ancestor. Source: RefGenome synaptic vesicle transport Inferred from Biological aspect of Ancestor. Source: RefGenome thymus development Inferred from Biological aspect of Ancestor. Source: RefGenome tongue morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome trachea formation Inferred from Biological aspect of Ancestor. Source: RefGenome transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Scrib-APC-beta-catenin complex Inferred from electronic annotation. Source: Compara Z disc Inferred from Biological aspect of Ancestor. Source: RefGenome apical part of cell Inferred from electronic annotation. Source: Compara basolateral plasma membrane Inferred from electronic annotation. Source: Compara beta-catenin destruction complex Inferred from direct assay PubMed 16188939PubMed 8638126. Source: BHF-UCL beta-catenin-TCF7L2 complex Inferred from direct assay PubMed 9065401Ref.66. Source: BHF-UCL catenin complex Inferred from direct assay PubMed 18593713PubMed 20302655PubMed 7650039. Source: BHF-UCL cell cortex Inferred from direct assay PubMed 19038973. Source: BHF-UCL cell-substrate adherens junction Inferred from direct assay PubMed 20399743. Source: BHF-UCL centrosome Inferred from direct assay Ref.41. Source: UniProtKB cytosol Inferred from direct assay PubMed 10980594PubMed 19187541. Source: UniProtKB dendritic shaft Inferred from Biological aspect of Ancestor. Source: RefGenome desmosome Inferred from Biological aspect of Ancestor. Source: RefGenome fascia adherens Inferred from Biological aspect of Ancestor. Source: RefGenome internal side of plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome lamellipodium Inferred from Biological aspect of Ancestor. Source: RefGenome lateral plasma membrane Inferred from direct assay PubMed 12072559. Source: MGI microvillus membrane Inferred from Biological aspect of Ancestor. Source: RefGenome perinuclear region of cytoplasm Inferred from direct assay PubMed 19038973. Source: UniProtKB protein-DNA complex Inferred from direct assay PubMed 10825188. Source: BHF-UCL spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from Biological aspect of Ancestor. Source: RefGenome transcription factor complex Inferred from direct assay Ref.16. Source: BHF-UCL zonula adherens Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	androgen receptor binding Non-traceable author statement PubMed 15572661. Source: UniProtKB chromatin binding Inferred from electronic annotation. Source: Compara double-stranded DNA binding Inferred from electronic annotation. Source: Compara protein kinase binding Inferred from Biological aspect of Ancestor. Source: RefGenome sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara signal transducer activity Non-traceable author statement Ref.71. Source: ProtInc structural molecule activity Inferred from Biological aspect of Ancestor. Source: RefGenome transcription coactivator activity Inferred from mutant phenotype PubMed 12949260. Source: UniProtKB transcription factor binding Traceable author statement PubMed 16344550. Source: AgBase transcription regulatory region DNA binding Inferred from direct assay PubMed 18193033PubMed 18579517. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTN4	O43707	6	EBI-491549,EBI-351526
APC	P25054	7	EBI-491549,EBI-727707
AR	P10275	8	EBI-491549,EBI-608057
AXIN1	O15169	20	EBI-491549,EBI-710484
BCL9	O00512	2	EBI-491549,EBI-533127
CAV1	P33724	5	EBI-491549,EBI-79998	From a different organism.
CDC73	Q6P1J9	9	EBI-491549,EBI-930143
CDH1	P12830	6	EBI-491549,EBI-727477
Ctnna1	P26231	2	EBI-491549,EBI-647895	From a different organism.
CTNNBIP1	Q9NSA3	6	EBI-491549,EBI-747082
DACT1	Q9NYF0	3	EBI-491549,EBI-3951744
EGR1	P18146	7	EBI-491549,EBI-2834611
FBXW11	Q9UKB1	2	EBI-491549,EBI-355189
FOXM1	Q08050	16	EBI-491549,EBI-866480
GSK3B	P49841	5	EBI-491549,EBI-373586
ipaC	P18012	4	EBI-491563,EBI-491541	From a different organism.
KANK1	Q14678	2	EBI-491549,EBI-2556221
KIAA1109	Q2LD37	2	EBI-491549,EBI-2683809
LEF1	Q9UJU2	4	EBI-491549,EBI-926131
LEO1	Q8WVC0	2	EBI-491549,EBI-932432
PSEN1	P49768	2	EBI-491549,EBI-297277
RUNX3	Q13761	12	EBI-491549,EBI-925990
TCF4	P15884	9	EBI-491549,EBI-533224
TCF7L2	Q9NQB0	27	EBI-491549,EBI-924724
TOP2A	P11388	5	EBI-491549,EBI-539628

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P35222-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P35222-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-565: Missing.
     652-653: AT → GK
     654-781: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 781

781

Catenin beta-1

PRO_0000064271

Regions

Repeat

151 – 191

41

ARM 1

Repeat

193 – 234

42

ARM 2

Repeat

235 – 276

42

ARM 3

Repeat

277 – 318

42

ARM 4

Repeat

319 – 360

42

ARM 5

Repeat

361 – 389

29

ARM 6

Repeat

400 – 441

42

ARM 7

Repeat

442 – 484

43

ARM 8

Repeat

489 – 530

42

ARM 9

Repeat

531 – 571

41

ARM 10

Repeat

594 – 636

43

ARM 11

Repeat

637 – 666

30

ARM 12

Region

1 – 23

23

Interaction with VCL By similarity

Region

772 – 781

10

Interaction with SCRIB By similarity

Amino acid modifications

Modified residue

23

1

Phosphoserine; by GSK3-beta

Modified residue

29

1

Phosphoserine; by GSK3-beta

Modified residue

33

1

Phosphoserine; by GSK3-beta and HIPK2 Ref.49

Modified residue

37

1

Phosphoserine; by GSK3-beta and HIPK2 Ref.49

Modified residue

41

1

Phosphothreonine; by GSK3-beta

Modified residue

45

1

Phosphoserine Ref.23

Modified residue

64

1

Phosphotyrosine; by PTK6 Ref.53

Modified residue

86

1

Phosphotyrosine; by CSK Ref.17

Modified residue

142

1

Phosphotyrosine; by FYN and PTK6 Ref.32 Ref.53

Modified residue

191

1

Phosphoserine; by CDK5 Ref.39 Ref.59

Modified residue

246

1

Phosphoserine; by CDK5 Ref.39

Modified residue

331

1

Phosphotyrosine; by PTK6 Ref.53

Modified residue

333

1

Phosphotyrosine; by PTK6 Probable

Modified residue

551

1

Phosphothreonine

Modified residue

552

1

Phosphoserine Ref.59

Modified residue

556

1

Phosphothreonine Ref.42

Modified residue

619

1

S-nitrosocysteine By similarity

Modified residue

654

1

Phosphotyrosine; by CSK Ref.17

Modified residue

675

1

Phosphoserine Ref.35 Ref.42 Ref.54

Natural variations

Alternative sequence

1 – 565

565

Missing in isoform 2.

VSP_006984

Alternative sequence

652 – 653

2

AT → GK in isoform 2.

VSP_006985

Alternative sequence

654 – 781

128

Missing in isoform 2.

VSP_006986

Natural variant

23

1

S → R in hepatocellular carcinoma; no effect. Ref.25 Ref.72

VAR_017612

Natural variant

25 – 33

9

Missing in hepatocellular carcinoma.

VAR_017613

Natural variant

32

1

D → A in hepatocellular carcinoma. Ref.72

VAR_017614

Natural variant

32

1

D → G in PTR and hepatocellular carcinoma. Ref.71 Ref.72

VAR_017615

Natural variant

32

1

D → Y in PTR, hepatoblastoma and hepatocellular carcinoma. Ref.15 Ref.67 Ref.71 Ref.72
Corresponds to variant rs28931588 [ dbSNP | Ensembl ].

VAR_017616

Natural variant

33

1

S → F in PTR, MDB and hepatocellular carcinoma. Ref.71 Ref.72 Ref.73

VAR_017617

Natural variant

33

1

S → L in hepatocellular carcinoma. Ref.72

VAR_017618

Natural variant

33

1

S → Y in colorectal cancer and PTR; enhances transactivation of target genes. Ref.25 Ref.66 Ref.71

VAR_017619

Natural variant

34

1

G → E in PTR. Ref.71

VAR_017620

Natural variant

34

1

G → R in hepatocellular carcinoma. Ref.72

VAR_017621

Natural variant

34

1

G → V in hepatoblastoma. Ref.67
Corresponds to variant rs28931589 [ dbSNP | Ensembl ].

VAR_017622

Natural variant

35

1

I → S in hepatocellular carcinoma. Ref.72

VAR_017623

Natural variant

37 – 38

2

SG → W in hepatocellular carcinoma.

VAR_017628

Natural variant

37

1

S → A in MDB and hepatocellular carcinoma; enhances transactivation of target genes. Ref.25 Ref.72 Ref.73

VAR_017624

Natural variant

37

1

S → C in PTR, hepatoblastoma and ovarian cancer. Ref.67 Ref.69 Ref.71

VAR_017625

Natural variant

37

1

S → F in PTR. Ref.71

VAR_017626

Natural variant

37

1

S → Y in hepatocellular carcinoma. Ref.72

VAR_017627

Natural variant

41

1

T → A in hepatoblastoma and hepatocellular carcinoma; also in a desmoid tumor; strongly reduces phosphorylation and degradation; abolishes phosphorylation on Ser-33 and Ser-37 and enhances transactivation of target genes. Ref.23 Ref.25 Ref.67 Ref.68 Ref.69 Ref.70 Ref.72

VAR_017629

Natural variant

41

1

T → I in PTR, hepatocellular carcinoma and ovarian cancer. Ref.69 Ref.71 Ref.72

VAR_017630

Natural variant

45

1

S → F in hepatocellular carcinoma. Ref.72

VAR_017631

Natural variant

45

1

S → P in hepatocellular carcinoma. Ref.72

VAR_017632

Natural variant

45

1

Missing in colorectal cancer. Ref.66

VAR_055430

Natural variant

688

1

M → V. Ref.3
Corresponds to variant rs4135384 [ dbSNP | Ensembl ].

VAR_018954

Experimental info

Mutagenesis

29

1

S → F: No effect. Ref.25

Mutagenesis

64

1

Y → F: Abolishes phosphorylation by PTK6. Ref.53

Mutagenesis

253

1

F → A: Abolishes or strongly reduces AXIN2 binding. Ref.14

Mutagenesis

260

1

H → A: Abolishes or strongly reduces AXIN1 and AXIN2 binding. Strongly reduces phosphorylation and degradation; when associated with A-386 and A-383. Ref.14

Mutagenesis

292

1

K → A: Abolishes or strongly reduces AXIN1 and AXIN2 binding. Ref.14

Mutagenesis

312

1

K → E: Abolishes TCF7L2 binding. Ref.63

Mutagenesis

345

1

K → A: Abolishes APC binding. Ref.14

Mutagenesis

383

1

W → A: Abolishes APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-386. Ref.14

Mutagenesis

386

1

R → A: Strongly reduces APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-383. Ref.14

Mutagenesis

426

1

N → A: Abolishes TCF7L2 and LEF1 binding. Ref.14

Mutagenesis

435

1

K → A: Strongly reduces or abolishes LEF1 binding. Ref.14 Ref.63

Mutagenesis

435

1

K → E: Abolishes TCF7L2 binding. Ref.14 Ref.63

Mutagenesis

469

1

R → A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding. Ref.14

Mutagenesis

470

1

H → A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding. Ref.14

Mutagenesis

508

1

K → A: Abolishes TCF7L2 and LEF1 binding. Ref.14

Mutagenesis

654

1

Y → E: Enhances TBP binding and transactivation of target genes. Ref.17

Mutagenesis

654

1

Y → F: Abolishes increase of TBP binding after phosphorylation by CSK. Ref.17

Mutagenesis

660

1

F → A: Abolishes CTNNBIP1 binding; when associated with A-661. Ref.65

Mutagenesis

661

1

R → A: Abolishes CTNNBIP1 binding; when associated with A-660. Ref.65

Secondary structure

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781

Helix Strand Turn

Details...

Turn

20 – 22

3

Beta strand

23 – 26

4

Turn

27 – 29

3

Turn

39 – 41

3

Helix

135 – 150

16

Helix

152 – 160

9

Helix

165 – 179

15

Helix

182 – 189

8

Helix

192 – 204

13

Helix

208 – 221

14

Helix

225 – 233

9

Helix

236 – 243

8

Helix

249 – 265

17

Helix

269 – 276

8

Helix

278 – 284

7

Helix

285 – 287

3

Helix

291 – 305

15

Helix

309 – 317

9

Helix

320 – 330

11

Helix

334 – 347

14

Helix

353 – 359

7

Helix

362 – 367

6

Turn

368 – 371

4

Helix

375 – 389

15

Helix

399 – 408

10

Helix

414 – 427

14

Turn

428 – 430

3

Helix

432 – 440

9

Helix

443 – 454

12

Helix

458 – 471

14

Beta strand

473 – 475

3

Helix

478 – 487

10

Helix

491 – 496

6

Beta strand

499 – 501

3

Helix

504 – 517

14

Helix

521 – 523

3

Helix

524 – 529

6

Helix

532 – 547

16

Beta strand

550 – 552

3

Beta strand

554 – 557

4

Beta strand

561 – 563

3

Helix

566 – 580

15

Helix

584 – 592

9

Helix

596 – 601

6

Helix

602 – 604

3

Helix

608 – 621

14

Helix

625 – 633

9

Helix

637 – 642

6

Helix

643 – 645

3

Helix

649 – 662

14

Turn

663 – 665

3

Helix

668 – 682

15

Helix

688 – 690

3

Beta strand

778 – 780

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: CB78F165A3EEF86E	FASTA	781	85,497
	10 20 30 40 50 60 MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTS 70 80 90 100 110 120 QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDAAHPT 130 140 150 160 170 180 NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK 190 200 210 220 230 240 KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL 250 260 270 280 290 300 VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC 310 320 330 340 350 360 LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC SSNKPAIVEA 370 380 390 400 410 420 GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA 430 440 450 460 470 480 AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM 490 500 510 520 530 540 AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL 550 560 570 580 590 600 VRAHQDTQRR TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV 610 620 630 640 650 660 QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF 670 680 690 700 710 720 RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI GAQGEPLGYR QDDPSYRSFH 730 740 750 760 770 780 SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L
	Isoform 2 [UniParc]. Checksum: 7AC26A6AA23E438C	FASTA	88	9,501
	10 20 30 40 50 60 MEEIVEGCTG ALHILARDVH NRIVIRGLNT IPLFVQLLYS PIENIQRVAA GVLCELAQDK 70 80 EAAEAIEAEG ATAPLTELLH SRNEGVGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
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[2]	"Functional prediction of the coding sequences of 75 new genes deduced by analysis of cDNA clones from human fetal liver." Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W., Gao F., Liu M., He F. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Fetal liver.
[3]	NIEHS SNPs program Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-688.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Hippocampus.
[5]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[8]	"Oncogenic beta-catenin is required for bone morphogenetic protein 4 expression in human cancer cells." Kim J.-S., Crooks H., Dracheva T., Nishanian T.G., Singh B., Jen J., Waldman T. Cancer Res. 62:2744-2748(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-312 (ISOFORM 1).
[9]	"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients." Shichijo S., Itoh K. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 258-781 (ISOFORM 1). Tissue: Colon adenocarcinoma.
[10]	"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion." Butz S., Kemler R. FEBS Lett. 355:195-200(1994) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
[11]	"Promoter swapping between the genes for a novel zinc finger protein and beta-catenin in pleiomorphic adenomas with t(3;8)(p21;q12) translocations." Kas K., Voz M.L., Roeijer E., Astroem A.-K., Meyen E., Stenman G., Van de Ven W.J.M. Nat. Genet. 15:170-174(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH PLAG1.
[12]	"Conserved mechanism of PLAG1 activation in salivary gland tumors with and without chromosome 8q12 abnormalities: identification of SII as a new fusion partner gene." Astroem A.-K., Voz M.L., Kas K., Roeijer E., Wedell B., Mandahl N., Van de Ven W., Mark J., Stenman G. Cancer Res. 59:918-923(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH PLAG1.
[13]	"Phosphorylation and free pool of beta-catenin are regulated by tyrosine kinases and tyrosine phosphatases during epithelial cell migration." Mueller T., Choidas A., Reichmann E., Ullrich A. J. Biol. Chem. 274:10173-10183(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STIMULATION OF TYROSINE PHOSPHORYLATION BY EGF, DEPHOSPHORYLATION BY PTPRF.
[14]	"Hot spots in beta-catenin for interactions with LEF-1, conductin and APC." von Kries J.P., Winbeck G., Asbrand C., Schwarz-Romond T., Sochnikova N., Dell'Oro A., Behrens J., Birchmeier W. Nat. Struct. Biol. 7:800-807(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LEF1; APC; AXIN1; AXIN2 AND TCF7L2, PHOSPHORYLATION BY GSK3B, MUTAGENESIS OF PHE-253; HIS-260; LYS-292; LYS-345; TRP-383; ARG-386; ASN-426; LYS-435; ARG-469; HIS-470 AND LYS-508.
[15]	"Beta-catenin expression in pilomatrixomas. Relationship with beta-catenin gene mutations and comparison with beta-catenin expression in normal hair follicles." Moreno-Bueno G., Gamallo C., Perez-Gallego L., Contreras F., Palacios J. Br. J. Dermatol. 145:576-581(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, VARIANT PTR TYR-32.
[16]	"Chromatin-specific regulation of LEF-1-beta-catenin transcription activation and inhibition in vitro." Tutter A.V., Fryer C.J., Jones K.A. Genes Dev. 15:3342-3354(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LEF1, INHIBITION BY CTNNBIP1 BINDING.
[17]	"Regulation of beta-catenin structure and activity by tyrosine phosphorylation." Piedra J., Martinez D., Castano J., Miravet S., Dunach M., de Herreros A.G. J. Biol. Chem. 276:20436-20443(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-86 AND TYR-654, INTERACTION WITH TBP, MUTAGENESIS OF TYR-654.
[18]	"AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein mediating strong cell-cell adhesion." Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J., Colpaert C., Bruyneel E., Mareel M., van Roy F. J. Cell Sci. 114:3177-3188(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CTNNA3.
[19]	"Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses." Matsuzawa S., Reed J.C. Mol. Cell 7:915-926(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[20]	"Siah-1 mediates a novel beta-catenin degradation pathway linking p53 to the adenomatous polyposis coli protein." Liu J., Stevens J., Rote C.A., Yost H.J., Hu Y., Neufeld K.L., White R.L., Matsunami N. Mol. Cell 7:927-936(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[21]	"Genetic alteration of the beta-catenin gene (CTNNB1) in human lung cancer and malignant mesothelioma and identification of a new 3p21.3 homozygous deletion." Shigemitsu K., Sekido Y., Usami N., Mori S., Sato M., Horio Y., Hasegawa Y., Bader S.A., Gazdar A.F., Minna J.D., Hida T., Yoshioka H., Imaizumi M., Ueda Y., Takahashi M., Shimokata K. Oncogene 20:4249-4257(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MESOM.
[22]	"Physical and functional interaction between receptor-like protein tyrosine phosphatase PCP-2 and beta-catenin." Yan H.-X., He Y.-Q., Dong H., Zhang P., Zeng J.-Z., Cao H.-F., Wu M.-C., Wang H.-Y. Biochemistry 41:15854-15860(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTPRU.
[23]	"Characterisation of the phosphorylation of beta-catenin at the GSK-3 priming site Ser45." Hagen T., Vidal-Puig A. Biochem. Biophys. Res. Commun. 294:324-328(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-45, CHARACTERIZATION OF VARIANT HEPATOCELLULAR CARCINOMA ALA-41, CHARACTERIZATION OF VARIANT DESMOID TUMOR ALA-41, CHARACTERIZATION OF VARIANT HEPATOBLASTOMA ALA-41.
[24]	"Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape." Walters R.W., Freimuth P., Moninger T.O., Ganske I., Zabner J., Welsh M.J. Cell 110:789-799(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CXADR.
[25]	"Identification of two novel regulated serines in the N-terminus of beta-catenin." van Noort M., van de Wetering M., Clevers H. Exp. Cell Res. 276:264-272(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY GSK3B, MUTAGENESIS OF SER-29, CHARACTERIZATION OF VARIANTS HEPATOCELLULAR CARCINOMA ARG-23; ALA-37 AND ALA-41, CHARACTERIZATION OF VARIANT PTR TYR-33, CHARACTERIZATION OF VARIANT MDB ALA-37, CHARACTERIZATION OF VARIANT DESMOID TUMOR ALA-41, CHARACTERIZATION OF VARIANT HEPATOBLASTOMA ALA-41.
[26]	"Wnt signaling controls the phosphorylation status of beta-catenin." van Noort M., Meeldijk J., van der Zee R., Destree O., Clevers H. J. Biol. Chem. 277:17901-17905(2002) [PubMed] [Europe PMC] [Abstract] Cited for: WNT SIGNALING MODULATES PHOSPHORYLATION.
[27]	"Regulation of S33/S37 phosphorylated beta-catenin in normal and transformed cells." Sadot E., Conacci-Sorrell M., Zhurinsky J., Shnizer D., Lando Z., Zharhary D., Kam Z., Ben-Ze'ev A., Geiger B. J. Cell Sci. 115:2771-2780(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION OF PHOSPHORYLATED CTNNB1 WITH BTRC.
[28]	"The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)." Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B. Oncogene 21:7067-7076(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTPRJ.
[29]	"The emergence of protocadherin-PC expression during the acquisition of apoptosis-resistance by prostate cancer cells." Chen M.-W., Vacherot F., De La Taille A., Gil-Diez-De-Medina S., Shen R., Friedman R.A., Burchardt M., Chopin D.K., Buttyan R. Oncogene 21:7861-7871(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PCDH11Y.
[30]	"EBP50, a beta-catenin-associating protein, enhances Wnt signaling and is over-expressed in hepatocellular carcinoma." Shibata T., Chuma M., Kokubu A., Sakamoto M., Hirohashi S. Hepatology 38:178-186(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SLC9A3R1.
[31]	"Regulation of beta-catenin signaling in the Wnt pathway." Kikuchi A. Biochem. Biophys. Res. Commun. 268:243-248(2000) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[32]	"p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction." Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N., Garcia de Herreros A., Dunach M. Mol. Cell. Biol. 23:2287-2297(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-142 BY FYN.
[33]	"Novel membrane protein shrew-1 targets to cadherin-mediated junctions in polarized epithelial cells." Bharti S., Handrow-Metzmacher H., Zickenheiner S., Zeitvogel A., Baumann R., Starzinski-Powitz A. Mol. Biol. Cell 15:397-406(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AJAP1. Tissue: Brain.
[34]	"E-cadherin regulates human Nanos1, which interacts with p120ctn and induces tumor cell migration and invasion." Strumane K., Bonnomet A., Stove C., Vandenbroucke R., Nawrocki-Raby B., Bruyneel E., Mareel M., Birembaut P., Berx G., van Roy F. Cancer Res. 66:10007-10015(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NANOS1.
[35]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[36]	"The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus." Markiewicz E., Tilgner K., Barker N., van de Wetering M., Clevers H., Dorobek M., Hausmanowa-Petrusewicz I., Ramaekers F.C.S., Broers J.L.V., Blankesteijn W.M., Salpingidou G., Wilson R.G., Ellis J.A., Hutchison C.J. EMBO J. 25:3275-3285(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EMD.
[37]	"MUC1 inhibits cell proliferation by a beta-catenin-dependent mechanism." Lillehoj E.P., Lu W., Kiser T., Goldblum S.E., Kim K.C. Biochim. Biophys. Acta 1773:1028-1038(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MUC1, SUBCELLULAR LOCATION, FUNCTION.
[38]	"The Kruppel-like zinc finger protein Glis2 functions as a negative modulator of the Wnt/beta-catenin signaling pathway." Kim Y.-S., Kang H.S., Jetten A.M. FEBS Lett. 581:858-864(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GLIS2, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[39]	"cdk5 modulates beta- and delta-catenin/Pin1 interactions in neuronal cells." Munoz J.P., Huichalaf C.H., Orellana D., Maccioni R.B. J. Cell. Biochem. 100:738-749(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-191 AND SER-246, INTERACTION WITH CDK5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[40]	"The tumor suppressor Fhit acts as a repressor of beta-catenin transcriptional activity." Weiske J., Albring K.F., Huber O. Proc. Natl. Acad. Sci. U.S.A. 104:20344-20349(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FHIT, IDENTIFICATION IN A COMPLEX WITH LEF1, FUNCTION.
[41]	"beta-Catenin is a Nek2 substrate involved in centrosome separation." Bahmanyar S., Kaplan D.D., Deluca J.G., Giddings T.H. Jr., O'Toole E.T., Winey M., Salmon E.D., Casey P.J., Nelson W.J., Barth A.I. Genes Dev. 22:91-105(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH NEK2.
[42]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-556 AND SER-675, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[43]	"Sox7 Is an independent checkpoint for beta-catenin function in prostate and colon epithelial cells." Guo L., Zhong D., Lau S., Liu X., Dong X.Y., Sun X., Yang V.W., Vertino P.M., Moreno C.S., Varma V., Dong J.T., Zhou W. Mol. Cancer Res. 6:1421-1430(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SOX7.
[44]	"CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-catenin target genes." Thompson B.A., Tremblay V., Lin G., Bochar D.A. Mol. Cell. Biol. 28:3894-3904(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHD8.
[45]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[46]	"The kinase TNIK is an essential activator of Wnt target genes." Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., Heck A.J., Clevers H. EMBO J. 28:3329-3340(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TCF7L2 AND TNIK.
[47]	"Down-regulation of death-associated protein kinase-2 is required for beta-catenin-induced anoikis resistance of malignant epithelial cells." Li H., Ray G., Yoo B.H., Erdogan M., Rosen K.V. J. Biol. Chem. 284:2012-2022(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[48]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[49]	"Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-catenin for 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2.
[50]	"The phospholipid-binding protein SESTD1 is a novel regulator of the transient receptor potential channels TRPC4 and TRPC5." Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C. J. Biol. Chem. 285:12426-12434(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SESTD1.
[51]	"Cell-cell contact formation governs Ca2+ signaling by TRPC4 in the vascular endothelium: evidence for a regulatory TRPC4-beta-catenin interaction." Graziani A., Poteser M., Heupel W.M., Schleifer H., Krenn M., Drenckhahn D., Romanin C., Baumgartner W., Groschner K. J. Biol. Chem. 285:4213-4223(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRPC4.
[52]	"Characterization of a novel human CDK5 splicing variant that inhibits Wnt/beta-catenin signaling." Li Q., Liu X., Zhang M., Ye G., Qiao Q., Ling Y., Wu Y., Zhang Y., Yu L. Mol. Biol. Rep. 37:2415-2421(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CDK5.
[53]	"Identification of beta-catenin as a target of the intracellular tyrosine kinase PTK6." Palka-Hamblin H.L., Gierut J.J., Bie W., Brauer P.M., Zheng Y., Asara J.M., Tyner A.L. J. Cell Sci. 123:236-245(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-64; TYR-142; TYR-331 AND TYR-333, INTERACTION WITH PTK6, MUTAGENESIS OF TYR-64.
[54]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[55]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[56]	"Compartmentalized CDK2 is connected with SHP-1 and beta-catenin and regulates insulin internalization." Fiset A., Xu E., Bergeron S., Marette A., Pelletier G., Siminovitch K.A., Olivier M., Beauchemin N., Faure R.L. Cell. Signal. 23:911-919(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN INSULIN INTERNALIZATION, SUBCELLULAR LOCATION, INTERACTION WITH CDK2, PHOSPHORYLATION BY CDK2.
[57]	"Protein tyrosine kinase 7 has a conserved role in Wnt/beta-catenin canonical signalling." Puppo F., Thome V., Lhoumeau A.-C., Cibois M., Gangar A., Lembo F., Belotti E., Marchetto S., Lecine P., Prebet T., Sebbagh M., Shin W.-S., Lee S.-T., Kodjabachian L., Borg J.-P. EMBO Rep. 12:43-49(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PKT7.
[58]	"Crystal structure of the human N-Myc downstream-regulated gene 2 protein provides insight into its role as a tumor suppressor." Hwang J., Kim Y., Kang H.B., Jaroszewski L., Deacon A.M., Lee H., Choi W.C., Kim K.J., Kim C.H., Kang B.S., Lee J.O., Oh T.K., Kim J.W., Wilson I.A., Kim M.H. J. Biol. Chem. 286:12450-12460(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NDRG2.
[59]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-552, MASS SPECTROMETRY.
[60]	"The tumor suppressor HINT1 regulates MITF and beta-catenin transcriptional activity in melanoma cells." Genovese G., Ghosh P., Li H., Rettino A., Sioletic S., Cittadini A., Sgambato A. Cell Cycle 11:2206-2215(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH HINT1 AND MITF, FUNCTION.
[61]	"Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells." Satow R., Shitashige M., Jigami T., Fukami K., Honda K., Kitabayashi I., Yamada T. Gastroenterology 142:572-581(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PML.
[62]	"Crystal structure of a beta-catenin/Tcf complex." Graham T.A., Weaver C., Mao F., Kimelman D., Xu W. Cell 103:885-896(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 133-664.
[63]	"Tcf4 can specifically recognize beta-catenin using alternative conformations." Graham T.A., Ferkey D.M., Mao F., Kimelman D., Xu W. Nat. Struct. Biol. 8:1048-1052(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-664 IN COMPLEX WITH TCF7L2, MUTAGENESIS OF LYS-312 AND LYS-435.
[64]	"Structure of a human Tcf4-beta-catenin complex." Poy F., Lepourcelet M., Shivdasani R.A., Eck M.J. Nat. Struct. Biol. 8:1053-1057(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-668 IN COMPLEX WITH TCF7L2.
[65]	"The crystal structure of the beta-catenin/ICAT complex reveals the inhibitory mechanism of ICAT." Graham T.A., Clements W.K., Kimelman D., Xu W. Mol. Cell 10:563-571(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-664 IN COMPLEX WITH CTNNBIP1, MUTAGENESIS OF PHE-660 AND ARG-661.
[66]	"Activation of beta-catenin-Tcf signaling in colon cancer by mutations in beta-catenin or APC." Morin P.J., Sparks A.B., Korinek V., Barker N., Clevers H., Vogelstein B., Kinzler K.W. Science 275:1787-1790(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS COLORECTAL CANCER TYR-33 AND SER-45 DEL.
[67]	"Childhood hepatoblastomas frequently carry a mutated degradation targeting box of the beta-catenin gene." Koch A., Denkhaus D., Albrecht S., Leuschner I., von Schweinitz D., Pietsch T. Cancer Res. 59:269-273(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEPATOBLASTOMA TYR-32; VAL-34; CYS-37 AND ALA-41.
[68]	"Beta-catenin accumulation and mutation of the CTNNB1 gene in hepatoblastoma." Blaeker H., Hofmann W.J., Rieker R.J., Penzel R., Graf M., Otto H.F. Genes Chromosomes Cancer 25:399-402(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEPATOBLASTOMA ALA-41.
[69]	"Mutational analysis of beta-catenin gene in Japanese ovarian carcinomas: frequent mutations in endometrioid carcinomas." Sagae S., Kobayashi K., Nishioka Y., Sugimura M., Ishioka S., Nagata M., Terasawa K., Tokino T., Kudo R. Jpn. J. Cancer Res. 90:510-515(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OVARIAN CANCER CYS-37; ILE-41 AND ALA-41.
[70]	"A novel case of a sporadic desmoid tumour with mutation of the beta catenin gene." Shitoh K., Konishi F., Iijima T., Ohdaira T., Sakai K., Kanazawa K., Miyaki M. J. Clin. Pathol. 52:695-696(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DESMOID TUMOR ALA-41.
[71]	"A common human skin tumour is caused by activating mutations in beta-catenin." Chan E.F., Gat U., McNiff J.M., Fuchs E. Nat. Genet. 21:410-413(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PTR GLY-32; TYR-32; PHE-33; TYR-33; GLU-34; CYS-37; PHE-37 AND ILE-41.
[72]	"Beta-catenin mutations in hepatocellular carcinoma correlate with a low rate of loss of heterozygosity." Legoix P., Bluteau O., Bayer J., Perret C., Balabaud C., Belghiti J., Franco D., Thomas G., Laurent-Puig P., Zucman-Rossi J. Oncogene 18:4044-4046(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEPATOCELLULAR CARCINOMA ARG-23; 25-TRP--SER-33 DEL; ALA-32; GLY-32; TYR-32; LEU-33; PHE-33; ARG-34; SER-35; ALA-37; 37-SER-GLY-38 DELINS TRP; TYR-37; ALA-41; ILE-41; PHE-45 AND PRO-45.
[73]	"APC mutations in sporadic medulloblastomas." Huang H., Mahler-Araujo B.M., Sankila A., Chimelli L., Yonekawa Y., Kleihues P., Ohgaki H. Am. J. Pathol. 156:433-437(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MDB PHE-33 AND ALA-37.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Wikipedia

Beta-catenin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X87838 mRNA. Translation: CAA61107.1.
Z19054 mRNA. Translation: CAA79497.1.
AF130085 mRNA. Translation: AAG35511.1.
AY463360 Genomic DNA. Translation: AAR18817.1.
AK289932 mRNA. Translation: BAF82621.1.
AC104307 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64625.1.
BC058926 mRNA. Translation: AAH58926.1.
AY081165 Genomic DNA. Translation: AAL89457.1.
AB062292 mRNA. Translation: BAB93475.1. Different initiation.

IPI

IPI00017292.
IPI00927799.

PIR

A38973.

RefSeq

NP_001091679.1. NM_001098209.1.
NP_001091680.1. NM_001098210.1.
NP_001895.1. NM_001904.3.

UniGene

Hs.476018.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G3J	X-ray	2.10	A/C	133-664	[»]
1JDH	X-ray	1.90	A	135-663	[»]
1JPW	X-ray	2.50	A/B/C	134-670	[»]
1LUJ	X-ray	2.50	A	150-663	[»]
1P22	X-ray	2.95	C	19-44	[»]
1QZ7	X-ray	2.20	A	133-665	[»]
1T08	X-ray	2.10	A	146-664	[»]
1TH1	X-ray	2.50	A/B	133-664	[»]
2G57	NMR	-	A	19-44	[»]
2GL7	X-ray	2.60	A/D	138-686	[»]
2Z6H	X-ray	2.20	A	138-781	[»]
3DIW	X-ray	2.10	C/D	772-781	[»]
3FQN	X-ray	1.65	C	30-39	[»]
3FQR	X-ray	1.70	C	30-39	[»]
3SL9	X-ray	2.20	A/B/E/G	141-305	[»]
3SLA	X-ray	2.50	A/B/C/D/E	141-306	[»]
3TX7	X-ray	2.76	A	138-663	[»]
4DJS	X-ray	3.03	A	148-665	[»]

ProteinModelPortal

P35222.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-122N.

IntAct

P35222. 87 interactions.

MINT

MINT-105089.

STRING

9606.ENSP00000344456.

PTM databases

PhosphoSite

P35222.

Polymorphism databases

DMDM

461854.

Proteomic databases

PaxDb

P35222.

PRIDE

P35222.

Protocols and materials databases

DNASU

1499.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000349496; ENSP00000344456; ENSG00000168036.
ENST00000396183; ENSP00000379486; ENSG00000168036.
ENST00000396185; ENSP00000379488; ENSG00000168036.
ENST00000405570; ENSP00000385604; ENSG00000168036.

GeneID

1499.

KEGG

hsa:1499.

UCSC

uc003ckp.2. human.
uc003ckt.1. human.

Organism-specific databases

CTD

1499.

GeneCards

GC03P041236.

H-InvDB

HIX0163439.
HIX0163473.

HGNC

HGNC:2514. CTNNB1.

HPA

CAB000108.
CAB001950.
HPA029159.
HPA029160.

MIM

114500. phenotype.
116806. gene.
132600. phenotype.
155255. phenotype.
156240. phenotype.
167000. phenotype.
181030. phenotype.

neXtProt

NX_P35222.

Orphanet

873. Desmoid disease.
33402. Hepatocellular carcinoma, childhood-onset.
91414. Pilomatrixoma.

PharmGKB

PA27013.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG297695.

HOGENOM

HOG000230958.

HOVERGEN

HBG000919.

InParanoid

P35222.

KO

K02105.

OMA

QLSQTRS.

OrthoDB

EOG4FN4H2.

PhylomeDB

P35222.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6_traffickingpathway. Arf6 trafficking events.
wnt_canonical_pathway. Canonical Wnt signaling pathway.
ar_pathway. Coregulation of Androgen receptor activity.
foxopathway. FoxO family signaling.
ps1pathway. Presenilin action in Notch and Wnt signaling.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P35222.

Bgee

P35222.

CleanEx

HS_CTNNB1.

Genevestigator

P35222.

GermOnline

ENSG00000168036. Homo sapiens.

Family and domain databases

Gene3D

1.25.10.10. 1 hit.

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]

Pfam

PF00514. Arm. 4 hits.
[Graphical view]

PRINTS

PR01869. BCATNINFAMLY.

SMART

SM00185. ARM. 12 hits.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

PROSITE

PS50176. ARM_REPEAT. 9 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P35222.

ChEMBL

CHEMBL5866.

ChiTaRS

CTNNB1. human.

DrugBank

DB01356. Lithium.

EvolutionaryTrace

P35222.

GenomeRNAi

1499.

NextBio

6161.

PMAP-CutDB

P35222.

SOURCE

Search...

Entry information

Entry name

CTNB1_HUMAN

Accession

Primary (citable) accession number: P35222
Secondary accession number(s): A8K1L7 , Q8NEW9, Q8NI94, Q9H391

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 1, 2013
This is version 168 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.