Reviewed, UniProtKB/Swiss-Prot P35222 (CTNB1_HUMAN)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	781 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the regulation of cell adhesion and in signal transduction through the Wnt pathway. Ref.30
Subunit structure	Two separate pools are found in the cytoplasm: one is PSEN1/cadherin/catenin complex which anchors to the actin cytoskeleton. The other 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 with SCRIB By similarity. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain). Interacts with EMD.
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton. Cell junction › adherens junction. 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. Ref.30 Ref.29 Ref.32
Tissue specificity	Expressed in several hair follicle cell types: basal and peripheral matrix cells, and cells of the outer and inner root sheats. Expressed in colon. Ref.32 Ref.12
Post-translational modification	Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-37 and Ser-33. EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding. Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1A, APC and TBL1X Probable. Its ubiquitination leads to its subsequent proteasomal degradation.
Involvement in disease	Defects in CTNNB1 are associated with colorectal cancer (CRC) [MIM:114500]. 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. Defects in CTNNB1 are a cause of pilomatrixoma (PTR) [MIM:132600]; a common benign skin tumor. Ref.12 Ref.21 Ref.45 Defects in CTNNB1 are a cause of medulloblastoma (MDB) [MIM:155255]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Ref.21 Ref.47 Defects in CTNNB1 are associated with ovarian cancer [MIM:167000]. Ovarian cancer is the leading cause of death from gynecologic malignancy. It is characterized by advanced presentation with loco-regional dissemination in the peritoneal cavity and the rare incidence of visceral metastases. These typical features relate to the biology of the disease, which is a principal determinant of outcome. A chromosomal rearrangement involving CTNNB1 may be a cause of salivary gland pleiomorphic adenomas (PA) [181030]. Pleiomorphic adenomas are the most common benign epithelial tumors of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1.
Sequence similarities	Belongs to the beta-catenin family. Contains 12 ARM repeats.

Ontologies

Keywords
Biological process	Cell adhesion Transcription Transcription regulation Wnt signaling pathway
Cellular component	Cell junction Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Disease mutation
Domain	Repeat
Molecular function	Activator
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway through beta-catenin Inferred by curator. Source: UniProtKB androgen receptor signaling pathway Non-traceable author statement. Source: UniProtKB cell-cell adhesion Inferred from mutant phenotype. Source: UniProtKB epithelial to mesenchymal transition Traceable author statement. Source: HGNC positive regulation of gene-specific transcription from RNA polymerase II promoter Ref.40 Inferred from direct assay. Source: UniProtKB positive regulation of heparan sulfate proteoglycan biosynthetic process Inferred from mutant phenotype. Source: UniProtKB regulation of centriole-centriole cohesion Inferred from direct assay. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Axin-APC-beta-catenin-GSK3B complex Inferred from direct assay. Source: UniProtKB beta-catenin destruction complex Inferred from direct assay. Source: UniProtKB beta-catenin-TCF7L2 complex Ref.40 Inferred from direct assay. Source: UniProtKB catenin complex Inferred from direct assay. Source: UniProtKB centrosome Inferred from direct assay. Source: UniProtKB lateral plasma membrane Inferred from direct assay. Source: MGI
Molecular function	I-SMAD binding Inferred from physical interaction. Source: UniProtKB androgen receptor binding Non-traceable author statement. Source: UniProtKB cadherin binding Inferred from physical interaction. Source: UniProtKB kinase binding Inferred from physical interaction. Source: UniProtKB promoter binding Inferred from direct assay. Source: UniProtKB protein C-terminus binding Inferred from physical interaction. Source: UniProtKB protein phosphatase binding Inferred from physical interaction. Source: UniProtKB signal transducer activity Ref.45 Non-traceable author statement. Source: ProtInc transcription coactivator activity Ref.40 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTN4	O43707	1	EBI-491549,EBI-351526
AR	P10275	1	EBI-491549,EBI-608057
axin1	Q9YGY0	1	EBI-491549,EBI-1037449	From a different organism.
BCL9	O00512	1	EBI-491549,EBI-533127
CAV1	P33724	1	EBI-491549,EBI-79998	From a different organism.
CDC73	Q6P1J9	4	EBI-491549,EBI-930143
CDH1	P12830	1	EBI-491549,EBI-727477
CTNNBIP1	Q9NSA3	2	EBI-491549,EBI-747082
FGFR1	P11362	1	EBI-491549,EBI-1028277
GSK3B	P49841	1	EBI-491549,EBI-373586
ipaC	P18012	2	EBI-491563,EBI-491541	From a different organism.
LEO1	Q8WVC0	2	EBI-491549,EBI-932432
NDRG1	Q92597	1	EBI-491563,EBI-716486
PHB2	Q99623	1	EBI-491549,EBI-358348
PSEN1	P49768	2	EBI-491549,EBI-297277
PTPN12	Q05209	1	EBI-491549,EBI-2266035
PTPRB	P23467	1	EBI-491549,EBI-1265766
PTPRC	P08575	1	EBI-491549,EBI-1341
PTPRG	P23470	1	EBI-491549,EBI-2258115
PTPRJ	Q12913	1	EBI-491549,EBI-2264500
PTPRO	Q16827	1	EBI-491549,EBI-723739
RUNX3	Q13761	2	EBI-491549,EBI-925990
TCF7L2	Q9NQB0	6	EBI-491549,EBI-924724

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

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

Modified residue

37

1

Phosphoserine; by GSK3-beta

Modified residue

41

1

Phosphothreonine; by GSK3-beta

Modified residue

45

1

Phosphoserine Ref.19

Modified residue

86

1

Phosphotyrosine; by CSK Ref.14

Modified residue

191

1

Phosphoserine By similarity

Modified residue

551

1

Phosphothreonine Ref.33

Modified residue

552

1

Phosphoserine Ref.33 Ref.31

Modified residue

556

1

Phosphothreonine Ref.33

Modified residue

654

1

Phosphotyrosine; by CSK Ref.14

Modified residue

675

1

Phosphoserine Ref.33 Ref.28

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.21 Ref.46

VAR_017612

Natural variant

25 – 33

9

Missing in hepatocellular carcinoma.

VAR_017613

Natural variant

32

1

D → A in hepatocellular carcinoma. Ref.46

VAR_017614

Natural variant

32

1

D → G in PTR and hepatocellular carcinoma. Ref.45 Ref.46

VAR_017615

Natural variant

32

1

D → Y in PTR, hepatoblastoma and hepatocellular carcinoma. Ref.12 Ref.45 Ref.46 Ref.41

VAR_017616

Natural variant

33

1

S → F in PTR, MDB and hepatocellular carcinoma. Ref.45 Ref.47 Ref.46

VAR_017617

Natural variant

33

1

S → L in hepatocellular carcinoma. Ref.46

VAR_017618

Natural variant

33

1

S → Y in colorectal cancer and PTR; enhances transactivation of target genes. Ref.21 Ref.45 Ref.40

VAR_017619

Natural variant

34

1

G → E in PTR. Ref.45

VAR_017620

Natural variant

34

1

G → R in hepatocellular carcinoma. Ref.46

VAR_017621

Natural variant

34

1

G → V in hepatoblastoma. Ref.41

VAR_017622

Natural variant

35

1

I → S in hepatocellular carcinoma. Ref.46

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.21 Ref.47 Ref.46

VAR_017624

Natural variant

37

1

S → C in PTR, hepatoblastoma and ovarian cancer. Ref.45 Ref.41 Ref.43

VAR_017625

Natural variant

37

1

S → F in PTR. Ref.45

VAR_017626

Natural variant

37

1

S → Y in hepatocellular carcinoma. Ref.46

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.21 Ref.19 Ref.46 Ref.41 Ref.43 Ref.42 Ref.44

VAR_017629

Natural variant

41

1

T → I in PTR, hepatocellular carcinoma and ovarian cancer. Ref.45 Ref.46 Ref.43

VAR_017630

Natural variant

45

1

S → F in hepatocellular carcinoma. Ref.46

VAR_017631

Natural variant

45

1

S → P in hepatocellular carcinoma. Ref.46

VAR_017632

Natural variant

45

1

Missing in colorectal cancer.

VAR_055430

Natural variant

688

1

M → V: dbSNP rs4135384. Ref.3

VAR_018954

Experimental info

Mutagenesis

29

1

S → F: No effect. Ref.21

Mutagenesis

253

1

F → A: Abolishes or strongly reduces AXIN2 binding. Ref.11

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.11

Mutagenesis

292

1

K → A: Abolishes or strongly reduces AXIN1 and AXIN2 binding. Ref.11

Mutagenesis

312

1

K → E: Abolishes TCF7L2 binding. Ref.37

Mutagenesis

345

1

K → A: Abolishes APC binding. Ref.11

Mutagenesis

383

1

W → A: Abolishes APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-386. Ref.11

Mutagenesis

386

1

R → A: Strongly reduces APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-383. Ref.11

Mutagenesis

426

1

N → A: Abolishes TCF7L2 and LEF1 binding. Ref.11

Mutagenesis

435

1

K → A: Strongly reduces or abolishes LEF1 binding. Ref.11 Ref.37

Mutagenesis

435

1

K → E: Abolishes TCF7L2 binding. Ref.11 Ref.37

Mutagenesis

469

1

R → A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding. Ref.11

Mutagenesis

470

1

H → A: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding. Ref.11

Mutagenesis

508

1

K → A: Abolishes TCF7L2 and LEF1 binding. Ref.11

Mutagenesis

654

1

Y → E: Enhances TBP binding and transactivation of target genes. Ref.14

Mutagenesis

654

1

Y → F: Abolishes increase of TBP binding after phosphorylation by CSK. Ref.14

Mutagenesis

660

1

F → A: Abolishes CTNNBIP1 binding; when associated with A-661. Ref.39

Mutagenesis

661

1

R → A: Abolishes CTNNBIP1 binding; when associated with A-660. Ref.39

Secondary structure

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781

Helix Strand Turn

Details...

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 – 242

7

Helix

243 – 245

3

Helix

249 – 265

17

Helix

269 – 275

7

Helix

278 – 284

7

Helix

285 – 287

3

Helix

291 – 305

15

Helix

309 – 317

9

Helix

320 – 328

9

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 – 428

15

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

Helix

504 – 517

14

Helix

521 – 523

3

Helix

524 – 529

6

Helix

532 – 545

14

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 – 643

7

Helix

649 – 663

15

Helix

668 – 682

15

Helix

688 – 690

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. 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 »
[1]	"E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton." Huelsken J., Birchmeier W., Behrens J. J. Cell Biol. 127:2061-2069(1994) [PubMed: 7806582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[5]	"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: 12019147] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-312 (ISOFORM 1).
[6]	"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.
[7]	"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: 9020842] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH PLAG1.
[8]	"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: 10029085] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH PLAG1.
[9]	"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: 10187801] [Abstract] Cited for: STIMULATION OF TYROSINE PHOSPHORYLATION BY EGF, DEPHOSPHORYLATION BY PTPRF.
[10]	"Presenilin-1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts." Georgakopoulos A., Marambaud P., Efthimiopoulos S., Shioi J., Cui W., Li H.-C., Schutte M., Gordon R., Holstein G.R., Martinelli G., Mehta P., Friedrich V.L. Jr., Robakis N.K. Mol. Cell 4:893-902(1999) [PubMed: 10635315] [Abstract] Cited for: COMPONENT OF THE PSEN1/E-CADHERIN/CATENIN ADHESION COMPLEX WITH PSEN1; CDH1; CTNNA1 AND CTNNB1/CTNND1.
[11]	"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: 10966653] [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.
[12]	"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: 11703283] [Abstract] Cited for: TISSUE SPECIFICITY, VARIANT PTR TYR-32.
[13]	"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: 11751639] [Abstract] Cited for: INTERACTION WITH LEF1, INHIBITION BY CTNNBIP1 BINDING.
[14]	"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: 11279024] [Abstract] Cited for: PHOSPHORYLATION AT TYR-86 AND TYR-654, INTERACTION WITH TBP, MUTAGENESIS OF TYR-654.
[15]	"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: 11590244] [Abstract] Cited for: INTERACTION WITH CTNNA3.
[16]	"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: 11389839] [Abstract] Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[17]	"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: 11389840] [Abstract] Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[18]	"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: 12501215] [Abstract] Cited for: INTERACTION WITH PTPRU.
[19]	"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: 12051714] [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.
[20]	"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: 12297051] [Abstract] Cited for: INTERACTION WITH CXADR.
[21]	"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: 12027456] [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.
[22]	"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: 11834740] [Abstract] Cited for: WNT SIGNALING MODULATES PHOSPHORYLATION.
[23]	"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: 12077367] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION OF PHOSPHORYLATED CTNNB1 WITH BTRC.
[24]	"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: 12420223] [Abstract] Cited for: INTERACTION WITH PCDH11Y.
[25]	"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: 12830000] [Abstract] Cited for: INTERACTION WITH SLC9A3R1.
[26]	"Regulation of beta-catenin signaling in the Wnt pathway." Kikuchi A. Biochem. Biophys. Res. Commun. 268:243-248(2000) [PubMed: 10679188] [Abstract] Cited for: REVIEW.
[27]	"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: 14595118] [Abstract] Cited for: INTERACTION WITH AJAP1. Tissue: Brain.
[28]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, MASS SPECTROMETRY. Tissue: Epithelium.
[29]	"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: 16858403] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EMD.
[30]	"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: 17524503] [Abstract] Cited for: INTERACTION WITH MUC1, SUBCELLULAR LOCATION, FUNCTION.
[31]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, MASS SPECTROMETRY.
[32]	"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: 17289029] [Abstract] Cited for: INTERACTION WITH GLIS2, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[33]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551; SER-552; THR-556 AND SER-675, MASS SPECTROMETRY.
[34]	"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: 18378692] [Abstract] Cited for: INTERACTION WITH CHD8.
[35]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[36]	"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: 11136974] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 133-664.
[37]	"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: 11713475] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-664 IN COMPLEX WITH TCF7L2, MUTAGENESIS OF LYS-312 AND LYS-435.
[38]	"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: 11713476] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-668 IN COMPLEX WITH TCF7L2.
[39]	"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: 12408824] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 134-664 IN COMPLEX WITH CTNNBIP1, MUTAGENESIS OF PHE-660 AND ARG-661.
[40]	"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: 9065402] [Abstract] Cited for: VARIANTS COLORECTAL CANCER TYR-33 AND SER-45 DEL.
[41]	"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: 9927029] [Abstract] Cited for: VARIANTS HEPATOBLASTOMA TYR-32; VAL-34; CYS-37 AND ALA-41.
[42]	"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: 10398436] [Abstract] Cited for: VARIANT HEPATOBLASTOMA ALA-41.
[43]	"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: 10391090] [Abstract] Cited for: VARIANTS OVARIAN CANCER CYS-37; ILE-41 AND ALA-41.
[44]	"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: 10655994] [Abstract] Cited for: VARIANT DESMOID TUMOR ALA-41.
[45]	"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: 10192393] [Abstract] Cited for: VARIANTS PTR GLY-32; TYR-32; PHE-33; TYR-33; GLU-34; CYS-37; PHE-37 AND ILE-41.
[46]	"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: 10435629] [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.
[47]	"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: 10666372] [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

EMBLGenBankDDBJ

X87838 mRNA. Translation: CAA61107.1.
Z19054 mRNA. Translation: CAA79497.1.
AF130085 mRNA. Translation: AAG35511.1.
AY463360 Genomic DNA. Translation: AAR18817.1.
BC058926 mRNA. Translation: AAH58926.1.
AY081165 Genomic DNA. Translation: AAL89457.1.
AB062292 mRNA. Translation: BAB93475.1. Different initiation.

IPI

IPI00017292.
IPI00792321.

PIR

A38973.

RefSeq

NP_001091679.1.
NP_001091680.1.
NP_001895.1.

UniGene

Hs.476018

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:122N.

IntAct

P35222. 41 interactions.

STRING

P35222.

PTM databases

PhosphoSite

P35222.

Proteomic databases

PRIDE

P35222.

Genome annotation databases

Ensembl

ENST00000349496; ENSP00000344456; ENSG00000168036; Homo sapiens. [Genome view]
ENST00000396183; ENSP00000379486; ENSG00000168036; Homo sapiens. [Genome view]
ENST00000396185; ENSP00000379488; ENSG00000168036; Homo sapiens. [Genome view]
ENST00000396190; ENSP00000379493; ENSG00000168036; Homo sapiens. [Genome view]
ENST00000405570; ENSP00000385604; ENSG00000168036; Homo sapiens. [Genome view]
ENST00000426215; ENSP00000400508; ENSG00000168036; Homo sapiens. [Genome view]
ENST00000431914; ENSP00000412219; ENSG00000168036; Homo sapiens. [Genome view]
ENST00000433400; ENSP00000387455; ENSG00000168036; Homo sapiens. [Genome view]
ENST00000441708; ENSP00000401599; ENSG00000168036; Homo sapiens. [Genome view]
ENST00000447363; ENSP00000387443; ENSG00000168036; Homo sapiens. [Genome view]
ENST00000450969; ENSP00000409302; ENSG00000168036; Homo sapiens. [Genome view]
ENST00000453024; ENSP00000411226; ENSG00000168036; Homo sapiens. [Genome view]

GeneID

1499.

KEGG

hsa:1499.

UCSC

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

Organism-specific databases

CTD

1499.

GeneCards

GC03P041216.

H-InvDB

HIX0003197.

HGNC

HGNC:2514. CTNNB1.

HPA

CAB000108.
CAB001950.

MIM

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

Orphanet

873. Desmoid disease.
33402. Hepatocellular carcinoma of childhood.
616. Medulloblastoma.
91414. Pilomatrixoma.

PharmGKB

PA27013.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P35222.

HOVERGEN

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_11045. Signaling by Wnt.
REACT_19331. Cell-cell adhesion systems.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P35222.

Bgee

P35222.

CleanEx

HS_CTNNB1.

Genevestigator

P35222.

GermOnline

ENSG00000168036. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:1.25.10.10. ARM-like. 1 hit.

Pfam

PF00514. Arm. 6 hits.
[Graphical view]

PRINTS

PR01869. BCATNINFAMLY.

SMART

SM00185. ARM. 12 hits.
[Graphical view]

PROSITE

PS50176. ARM_REPEAT. 9 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01356. Lithium.

NextBio

6161.

PMAP-CutDB

P35222.

SOURCE

Search...

Entry information

Entry name

CTNB1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	November 3, 2009
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.