Q02248 (CTNB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catenin beta-1

Alternative name(s):
Beta-catenin

Gene names

Name:	Ctnnb1
Synonyms:	Catnb

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

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

General annotation (Comments)

Function	Key dowstream 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 downregulating DAPK2 By similarity.
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. Interacts with AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1 By similarity. Interacts with GLIS2. Interacts with SLC30A9. Interacts with XIRP1. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain) and with EMD By similarity. Interacts with SCRIB. Interacts with TNIK and TCF7L2. Interacts with SESTD1 and TRPC4 By similarity. Interacts directly with AXIN1; the interaction is regulated by CDK2 phosphorylation of AXIN1. Interacts with CAV1. Interacts with PTPRJ By similarity. Interacts with TRPV4; the TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with VCL. Interacts with PKT7 By similarity. Interacts with FAT1 (via the cytoplasmic domain) By similarity. Interacts with CDK2, NDRG2 and NANOS1 By similarity. Interacts with NEK2 and CDK5 By similarity. Interacts with PTK6 By similarity. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.20 Ref.21 Ref.25 Ref.26 Ref.32
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Nucleus. Cell junction › adherens junction By similarity. Cell junction By similarity. Cell membrane By similarity. Cytoplasm › cytoskeleton › centrosome By similarity. Cytoplasm › cytoskeleton › spindle pole By similarity. 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 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 By similarity. 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-33. Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding By similarity. Phosphorylated on Ser-33 and Ser-37 by HIPK2. This phosphorylation triggers proteasomal degradation. Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription. Phosphorylation on Ser-191 and Ser-246 by CDK5. Phosphorylation by CDK2 regulates insulin internalization By similarity. Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or Tyr-333 with the predominant site at Tyr-64 is not essential for inhibition of transcriptional activity By similarity. Ref.14 Ref.16 Ref.17 Ref.18 Ref.22 Ref.23 Ref.24 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.14 Ref.16 Ref.17 Ref.18 Ref.22 Ref.23 Ref.24
Sequence similarities	Belongs to the beta-catenin family. Contains 12 ARM repeats.
Sequence caution	The sequence AAH06739.1 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
Domain	Repeat
Molecular function	Activator
PTM	Phosphoprotein 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 mutant phenotype. Source: MGI adherens junction assembly Inferred from sequence or structural similarity. Source: UniProtKB anterior/posterior axis specification Inferred from mutant phenotype. Source: MGI apoptotic process Inferred from mutant phenotype. Source: MGI bone resorption Inferred from mutant phenotype. Source: MGI branching involved in ureteric bud morphogenesis Inferred from mutant phenotype. Source: MGI canonical Wnt receptor signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation Inferred from mutant phenotype. Source: BHF-UCL canonical Wnt receptor signaling pathway involved in positive regulation of epithelial to mesenchymal transition Inferred from sequence or structural similarity. Source: UniProtKB cardiac muscle cell proliferation Traceable author statement. Source: DFLAT cell fate specification Inferred from mutant phenotype. Source: MGI cell maturation Inferred from direct assay. Source: MGI cell-cell adhesion Inferred from mutant phenotype. Source: MGI cell-matrix adhesion Inferred from mutant phenotype. Source: MGI cellular response to growth factor stimulus Inferred from sequence or structural similarity. Source: UniProtKB cellular response to indole-3-methanol Inferred from sequence or structural similarity. Source: UniProtKB cellular response to organic cyclic compound Inferred from direct assay. Source: MGI central nervous system vasculogenesis Inferred from mutant phenotype. Source: MGI coronary artery morphogenesis Traceable author statement. Source: DFLAT cytoskeletal anchoring at plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome dorsal/ventral axis specification Inferred from mutant phenotype. Source: MGI ectoderm development Inferred from mutant phenotype. Source: MGI embryonic arm morphogenesis Inferred from direct assay. Source: MGI embryonic axis specification Inferred from direct assay. Source: MGI embryonic digit morphogenesis Inferred from mutant phenotype. Source: MGI embryonic foregut morphogenesis Inferred from mutant phenotype. Source: MGI embryonic heart tube development Inferred from mutant phenotype. Source: MGI embryonic hindlimb morphogenesis Inferred from mutant phenotype. Source: MGI embryonic skeletal limb joint morphogenesis Inferred from genetic interaction. Source: BHF-UCL endodermal cell fate commitment Inferred from mutant phenotype. Source: MGI endothelial tube morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB epicardium-derived cardiac vascular smooth muscle cell differentiation Traceable author statement. Source: DFLAT epithelial cell differentiation involved in prostate gland development Inferred from mutant phenotype. Source: MGI epithelial tube branching involved in lung morphogenesis Inferred from mutant phenotype. Source: MGI forebrain development Inferred from mutant phenotype. Source: MGI fungiform papilla formation Inferred from mutant phenotype. Source: MGI gastrulation with mouth forming second Inferred from mutant phenotype. Source: MGI genitalia morphogenesis Inferred from mutant phenotype. Source: MGI glial cell fate determination Inferred from direct assay. Source: MGI hair follicle morphogenesis Inferred from mutant phenotype. Source: MGI hair follicle placode formation Inferred from mutant phenotype. Source: MGI hindbrain development Inferred from Biological aspect of Ancestor. Source: RefGenome in utero embryonic development Inferred from mutant phenotype. Source: MGI lens morphogenesis in camera-type eye Inferred from mutant phenotype. Source: MGI liver development Inferred from Biological aspect of Ancestor. Source: RefGenome lung cell differentiation Inferred from mutant phenotype. Source: MGI lung induction Inferred from mutant phenotype. Source: MGI lung-associated mesenchyme development Inferred from mutant phenotype. Source: MGI male genitalia development Inferred from mutant phenotype. Source: MGI mesenchymal cell proliferation involved in lung development Inferred from mutant phenotype. Source: MGI mesenchymal to epithelial transition involved in metanephros morphogenesis Inferred from direct assay. Source: MGI mesenchyme morphogenesis Traceable author statement. Source: DFLAT negative regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of chondrocyte differentiation Inferred from genetic interaction. Source: MGI 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 mutant phenotype. Source: MGI negative regulation of osteoclast differentiation Inferred from mutant phenotype. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: MGI nephron tubule formation Inferred from mutant phenotype. Source: MGI odontogenesis of dentin-containing tooth Inferred from mutant phenotype. Source: MGI oocyte development Inferred from genetic interaction. Source: MGI osteoclast differentiation Inferred from mutant phenotype. Source: MGI oviduct development Inferred from mutant phenotype. Source: MGI pancreas development Inferred from mutant phenotype. Source: MGI patterning of blood vessels Inferred from mutant phenotype. Source: MGI positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype. Source: MGI positive regulation of MAPKKK cascade Inferred from genetic interaction. Source: MGI positive regulation of anti-apoptosis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of branching involved in lung morphogenesis Inferred from mutant phenotype. Source: MGI positive regulation of determination of dorsal identity Inferred from direct assay. Source: MGI positive regulation of endothelial cell differentiation Inferred from mutant phenotype. Source: MGI positive regulation of epithelial cell proliferation involved in prostate gland development Inferred from mutant phenotype. Source: MGI positive regulation of fibroblast growth factor receptor signaling pathway Inferred from mutant phenotype. Source: MGI positive regulation of heparan sulfate proteoglycan biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of mesenchymal cell proliferation Inferred from mutant phenotype. Source: MGI positive regulation of osteoblast differentiation Inferred from mutant phenotype. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB protein localization at cell surface Inferred from sequence or structural similarity. Source: UniProtKB proximal/distal pattern formation Inferred from mutant phenotype. Source: MGI regulation of T cell proliferation Inferred from mutant phenotype. Source: MGI regulation of calcium ion import Inferred from sequence or structural similarity. Source: UniProtKB regulation of centriole-centriole cohesion Inferred from sequence or structural similarity. Source: UniProtKB regulation of centromeric sister chromatid cohesion Inferred from mutant phenotype. Source: BHF-UCL regulation of myelination Inferred from mutant phenotype. Source: MGI regulation of nephron tubule epithelial cell differentiation Inferred from mutant phenotype. Source: UniProtKB regulation of protein localization at cell surface Inferred from sequence or structural similarity. Source: UniProtKB regulation of secondary heart field cardioblast proliferation Inferred from direct assay. Source: MGI regulation of smooth muscle cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB renal inner medulla development Inferred from mutant phenotype. Source: MGI renal outer medulla development Inferred from mutant phenotype. Source: MGI renal vesicle formation Inferred from mutant phenotype. Source: MGI response to estradiol stimulus Inferred from sequence or structural similarity. Source: UniProtKB skin development Inferred from mutant phenotype. Source: MGI synapse organization Inferred from mutant phenotype. Source: MGI synaptic vesicle transport Inferred from mutant phenotype. Source: MGI thymus development Inferred from mutant phenotype. Source: MGI trachea formation Inferred from mutant phenotype. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW ventricular compact myocardium morphogenesis Traceable author statement. Source: DFLAT
Cellular component	APC-Axin-1-beta-catenin complex Inferred from sequence or structural similarity. Source: UniProtKB Axin-APC-beta-catenin-GSK3B complex Inferred from direct assay. Source: MGI Scrib-APC-beta-catenin complex Inferred from direct assay. Source: BHF-UCL Z disc Inferred from direct assay. Source: MGI apical part of cell Inferred from direct assay. Source: MGI beta-catenin-TCF7L2 complex Inferred from sequence or structural similarity. Source: UniProtKB catenin complex Inferred from sequence or structural similarity. Source: UniProtKB cell cortex Inferred from sequence or structural similarity. Source: UniProtKB cell-substrate adherens junction Inferred from sequence or structural similarity. Source: UniProtKB centrosome Inferred from direct assay. Source: BHF-UCL dendritic shaft Inferred from Biological aspect of Ancestor. Source: RefGenome desmosome Inferred from Biological aspect of Ancestor. Source: RefGenome fascia adherens Inferred from direct assay. Source: MGI internal side of plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome lamellipodium Inferred from direct assay. Source: MGI lateral plasma membrane Inferred from direct assay. Source: MGI membrane fraction Inferred from direct assay. Source: MGI microvillus membrane Inferred from direct assay. Source: MGI perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB protein-DNA complex Inferred from sequence or structural similarity. Source: UniProtKB 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. Source: MGI zonula adherens Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	RPTP-like protein binding Inferred from Biological aspect of Ancestor. Source: RefGenome alpha-catenin binding Inferred from physical interaction. Source: MGI cadherin binding Inferred from physical interaction. Source: MGI chromatin binding Inferred from direct assay. Source: MGI double-stranded DNA binding Inferred from direct assay. Source: MGI protein kinase binding Inferred from Biological aspect of Ancestor. Source: RefGenome protein phosphatase binding Inferred from physical interaction. Source: UniProtKB repressing transcription factor binding Inferred from physical interaction. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from direct assay. Source: MGI structural molecule activity Inferred from Biological aspect of Ancestor. Source: RefGenome transcription coactivator activity Inferred from direct assay. Source: UniProtKB transcription regulatory region DNA binding Inferred from direct assay. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APC	P25054	8	EBI-397872,EBI-727707	From a different organism.
AXIN1	O15169	5	EBI-397872,EBI-710484	From a different organism.
Cdh1	P09803	13	EBI-397872,EBI-984420
Crebbp	P45481	2	EBI-397872,EBI-296306
CTNNBIP1	Q9NSA3	7	EBI-397872,EBI-747082	From a different organism.
Lef1	P27782	6	EBI-397872,EBI-984464
Prop1	P97458	2	EBI-397872,EBI-937831
Tax1bp3	Q9DBG9	6	EBI-397872,EBI-1161647

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 781

781

Catenin beta-1

PRO_0000064272

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

Region

772 – 781

10

Interaction with SCRIB

Amino acid modifications

Modified residue

23

1

Phosphoserine; by GSK3-beta By similarity

Modified residue

29

1

Phosphoserine; by GSK3-beta By similarity

Modified residue

33

1

Phosphoserine; by GSK3-beta and HIPK2 Ref.23

Modified residue

37

1

Phosphoserine; by GSK3-beta and HIPK2 Ref.23

Modified residue

41

1

Phosphothreonine; by GSK3-beta By similarity

Modified residue

45

1

Phosphoserine By similarity

Modified residue

64

1

Phosphotyrosine; by PTK6 By similarity

Modified residue

86

1

Phosphotyrosine; by CSK By similarity

Modified residue

142

1

Phosphotyrosine; by FYN and PTK6 By similarity

Modified residue

191

1

Phosphoserine By similarity

Modified residue

191

1

Phosphoserine; by CDK5 By similarity

Modified residue

246

1

Phosphoserine; by CDK5 By similarity

Modified residue

551

1

Phosphothreonine Ref.14 Ref.16

Modified residue

552

1

Phosphoserine; by AMPK Ref.16 Ref.18 Ref.24

Modified residue

556

1

Phosphothreonine Ref.14 Ref.16

Modified residue

654

1

Phosphotyrosine Ref.17

Modified residue

675

1

Phosphoserine Ref.18 Ref.22

Experimental info

Mutagenesis

8

1

M → P: Loss of interaction with VCL. Ref.26

Mutagenesis

33

1

S → A: Abolished HIPK2-mediated proteasomal degradation. Ref.23

Mutagenesis

37

1

S → A: Abolished HIPK2-mediated proteasomal degradation. Ref.23

Mutagenesis

552

1

S → A: Abolishes AMPK-mediated phosphorylation. Ref.24

Sequence conflict

371

1

T → I in BAB31250. Ref.2

Sequence conflict

478

1

A → T in BAB31250. Ref.2

Sequence conflict

487

1

L → F in BAB31250. Ref.2

Secondary structure

1

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781

Helix Strand Turn

Details...

Helix

121 – 141

21

Turn

145 – 148

4

Turn

150 – 152

3

Helix

153 – 160

8

Helix

165 – 180

16

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 – 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 – 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 – 547

16

Helix

566 – 580

15

Helix

584 – 592

9

Helix

596 – 602

7

Helix

608 – 621

14

Helix

625 – 632

8

Turn

633 – 636

4

Helix

637 – 643

7

Helix

649 – 661

13

Sequences

	Sequence		Length	Mass (Da)
	Q02248 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: D708F170A3FBED6E	FASTA	781	85,471
	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 GAQGEALGYR QDDPSYRSFH 730 740 750 760 770 780 SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Plakoglobin and beta-catenin: distinct but closely related." Butz S., Stappert J., Weissig H., Kemler R. Science 257:1142-1144(1992) [PubMed: 1509266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Colon and Urinary bladder.
[3]	"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]. Strain: C57BL/6. Tissue: Brain and Mammary cancer.
[4]	"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion." Butz S., Kemler R. FEBS Lett. 355:195-200(1994) [PubMed: 7982500] [Abstract] Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
[5]	"The Xenopus Wnt effector XTcf-3 interacts with Groucho-related transcriptional repressors." Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H., Moerer P., van de Wetering M., Destree O., Clevers H. Nature 395:608-612(1998) [PubMed: 9783587] [Abstract] Cited for: INTERACTION WITH TCF7; TCF7L1; TCF7L2 AND LEF1.
[6]	"A GSK3beta phosphorylation site in axin modulates interaction with beta-catenin and Tcf-mediated gene expression." Jho E., Lomvardas S., Costantini F. Biochem. Biophys. Res. Commun. 266:28-35(1999) [PubMed: 10581160] [Abstract] Cited for: INTERACTION WITH AXIN1.
[7]	"MAGI-1 interacts with beta-catenin and is associated with cell-cell adhesion structures." Dobrosotskaya I.Y., James G.L. Biochem. Biophys. Res. Commun. 270:903-909(2000) [PubMed: 10772923] [Abstract] Cited for: INTERACTION WITH BAIAP1.
[8]	"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.
[9]	"The PDZ protein tax-interacting protein-1 inhibits beta-catenin transcriptional activity and growth of colorectal cancer cells." Kanamori M., Sandy P., Marzinotto S., Benetti R., Kai C., Hayashizaki Y., Schneider C., Suzuki H. J. Biol. Chem. 278:38758-38764(2003) [PubMed: 12874278] [Abstract] Cited for: INTERACTION WITH TAX1BP3.
[10]	"Cyclin-dependent kinase 2 regulates the interaction of Axin with beta-catenin." Kim S.I., Park C.S., Lee M.S., Kwon M.S., Jho E.H., Song W.K. Biochem. Biophys. Res. Commun. 317:478-483(2004) [PubMed: 15063782] [Abstract] Cited for: INTERACTION WITH AXIN1.
[11]	"Deconstructing the cadherin-catenin-actin complex." Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J. Cell 123:889-901(2005) [PubMed: 16325582] [Abstract] Cited for: RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
[12]	"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, SUBCELLULAR LOCATION.
[13]	"The intercalated disc protein, mXin{alpha}, is capable of interacting with beta-catenin and bundling actin filaments." Choi S., Gustafson-Wagner E.A., Wang Q., Harlan S.M., Sinn H.W., Lin J.L.-C., Lin J.J.-C. J. Biol. Chem. 282:36024-36036(2007) [PubMed: 17925400] [Abstract] Cited for: INTERACTION WITH XIRP1.
[14]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551 AND THR-556, MASS SPECTROMETRY. Tissue: Brain cortex.
[15]	"Role of GAC63 in transcriptional activation mediated by beta-catenin." Chen Y.H., Yang C.K., Xia M., Ou C.Y., Stallcup M.R. Nucleic Acids Res. 35:2084-2092(2007) [PubMed: 17344318] [Abstract] Cited for: INTERACTION WITH SLC30A9.
[16]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551; SER-552 AND THR-556, MASS SPECTROMETRY. Tissue: Liver.
[17]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-654, MASS SPECTROMETRY. Tissue: Brain.
[18]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND SER-675, MASS SPECTROMETRY. Tissue: Melanoma.
[19]	"EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt." Abe K., Takeichi M. Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008) [PubMed: 18093941] [Abstract] Cited for: LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
[20]	"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: 19816403] [Abstract] Cited for: INTERACTION WITH TCF7L2 AND TNIK.
[21]	"Scribble interacts with beta-catenin to localize synaptic vesicles to synapses." Sun Y., Aiga M., Yoshida E., Humbert P.O., Bamji S.X. Mol. Biol. Cell 20:3390-3400(2009) [PubMed: 19458197] [Abstract] Cited for: INTERACTION WITH SCRIB.
[22]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[23]	"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: 20307497] [Abstract] Cited for: PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2, MUTAGENESIS OF SER-33 AND SER-37.
[24]	"AMP-activated protein kinase (AMPK) cross-talks with canonical Wnt signaling via phosphorylation of beta-catenin at Ser 552." Zhao J., Yue W., Zhu M.J., Sreejayan N., Du M. Biochem. Biophys. Res. Commun. 395:146-151(2010) [PubMed: 20361929] [Abstract] Cited for: PHOSPHORYLATION AT SER-552, MUTAGENESIS OF SER-552.
[25]	"The TRPV4 channel contributes to intercellular junction formation in keratinocytes." Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M. J. Biol. Chem. 285:18749-18758(2010) [PubMed: 20413591] [Abstract] Cited for: INTERACTION WITH TRPV4 AND CDH1.
[26]	"Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin." Peng X., Cuff L.E., Lawton C.D., DeMali K.A. J. Cell Sci. 123:567-577(2010) [PubMed: 20086044] [Abstract] Cited for: INTERACTION WITH VCL, MUTAGENESIS OF MET-8.
[27]	"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.
[28]	"Three-dimensional structure of the armadillo repeat region of beta-catenin." Huber A.H., Nelson W.J., Weis W.I. Cell 90:871-882(1997) [PubMed: 9298899] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 150-665.
[29]	"Structure of the dimerization and beta-catenin-binding region of alpha-catenin." Pokutta S., Weis W.I. Mol. Cell 5:533-543(2000) [PubMed: 10882138] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 118-149 IN COMPLEX WITH CTNNA1.
[30]	"The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin." Huber A.H., Weis W.I. Cell 105:391-402(2001) [PubMed: 11348595] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 AND 3.0 ANGSTROMS) OF 134-671 IN COMPLEX WITH PHOSPHORYLATED AND UNPHOSPHORYLATED CDH1.
[31]	"Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex." Eklof Spink K., Fridman S.G., Weis W.I. EMBO J. 20:6203-6212(2001) [PubMed: 11707392] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH APC.
[32]	"ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules." Daniels D.L., Weis W.I. Mol. Cell 10:573-584(2002) [PubMed: 12408825] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH CTNNBIP1, INTERACTION WITH EP300.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M90364 mRNA. Translation: AAA37280.1.
AK035311 mRNA. Translation: BAC29027.1.
AK018515 mRNA. Translation: BAB31250.1.
BC006739 mRNA. Translation: AAH06739.1. Different initiation.
BC048153 mRNA. Translation: AAH48153.1.
BC053065 mRNA. Translation: AAH53065.1.

IPI

IPI00125899.

PIR

S35091.

RefSeq

NP_001159374.1. NM_001165902.1.
NP_031640.1. NM_007614.3.

UniGene

Mm.291928.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DOW	X-ray	1.80	B	118-149	[»]
1I7W	X-ray	2.00	A/C	134-671	[»]
1I7X	X-ray	3.00	A/C	134-671	[»]
1JPP	X-ray	3.10	A/B	134-671	[»]
1M1E	X-ray	2.10	A	134-671	[»]
1V18	X-ray	2.10	A	134-671	[»]
2BCT	X-ray	2.90	A	150-665	[»]
3BCT	X-ray	2.10	A	193-662	[»]
3OUW	X-ray	2.91	A	134-671	[»]
3OUX	X-ray	2.40	A	134-671	[»]

ProteinModelPortal

Q02248.

SMR

Q02248. Positions 19-44, 142-665.

DisProt

DP00341.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31560N.

IntAct

Q02248. 29 interactions.

MINT

MINT-103426.

STRING

Q02248.

PTM databases

PhosphoSite

Q02248.

Proteomic databases

PRIDE

Q02248.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932.

GeneID

12387.

KEGG

mmu:12387.

UCSC

uc009scu.2. mouse.

Organism-specific databases

CTD

1499.

MGI

MGI:88276. Ctnnb1.

Phylogenomic databases

eggNOG

roNOG10531.

HOGENOM

HBG357527.

HOVERGEN

HBG000919.

InParanoid

Q02248.

OMA

TVCQVGG.

OrthoDB

EOG4FN4H2.

PhylomeDB

Q02248.

Gene expression databases

ArrayExpress

Q02248.

Bgee

Q02248.

CleanEx

MM_CTNNB1.

Genevestigator

Q02248.

GermOnline

ENSMUSG00000006932. Mus musculus.

Family and domain databases

InterPro

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

Gene3D

G3DSA:1.25.10.10. ARM-like. 1 hit.

KO

K02105.

Pfam

PF00514. Arm. 5 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

NextBio

281106.

PMAP-CutDB

Q02248.

SOURCE

Search...

Entry information

Entry name

CTNB1_MOUSE

Accession

Primary (citable) accession number: Q02248
Secondary accession number(s): Q922W1, Q9D335

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	January 25, 2012
This is version 142 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program