Reviewed, UniProtKB/Swiss-Prot Q02248 (CTNB1_MOUSE)

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

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.
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. 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) By similarity.
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Nucleus. 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. 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 By similarity. EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding By similarity. 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 By similarity.
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	Cytoplasm Cytoskeleton Nucleus
Domain	Repeat
Molecular function	Activator
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	T cell differentiation in the thymus Inferred from mutant phenotype. Source: MGI Wnt receptor signaling pathway through beta-catenin Inferred from direct assay. Source: MGI anterior/posterior axis specification Inferred from mutant phenotype. Source: MGI apoptosis Inferred from mutant phenotype. Source: MGI bone resorption Inferred from genetic interaction. Source: MGI camera-type eye morphogenesis Inferred from mutant phenotype. Source: MGI cell fate specification Inferred from mutant phenotype. Source: MGI cell maturation Inferred from direct assay. Source: MGI cell morphogenesis involved in differentiation Inferred from mutant phenotype. Source: MGI cell proliferation Inferred from mutant phenotype. Source: MGI cell-cell adhesion Inferred from mutant phenotype. Source: MGI cell-matrix adhesion Inferred from mutant phenotype. Source: MGI cellular protein localization Inferred from mutant phenotype. Source: MGI 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 digit morphogenesis Inferred from mutant phenotype. Source: MGI embryonic hindlimb morphogenesis Inferred from mutant phenotype. Source: MGI endoderm formation Inferred from mutant phenotype. Source: MGI endodermal cell fate commitment Inferred from mutant phenotype. Source: MGI forebrain development Inferred from mutant phenotype. Source: MGI gastrulation with mouth forming second Inferred from mutant phenotype. Source: MGI glial cell fate determination Inferred from direct assay. Source: MGI heart development Inferred from mutant phenotype. Source: MGI lung development Inferred from mutant phenotype. Source: MGI morphogenesis of embryonic epithelium Inferred from mutant phenotype. Source: MGI negative regulation of chondrocyte differentiation Inferred from genetic interaction. 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 odontogenesis of dentine-containing tooth Inferred from mutant phenotype. Source: MGI osteoclast differentiation 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 MAPKKK cascade Inferred from genetic interaction. Source: MGI positive regulation of epithelial cell differentiation 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 direct assay. Source: MGI proximal/distal pattern formation Inferred from mutant phenotype. Source: MGI regulation of cell proliferation Inferred from direct assay. Source: MGI skeletal system development Inferred from mutant phenotype. Source: MGI synapse organization Inferred from mutant phenotype. Source: MGI synaptic transmission Inferred from mutant phenotype. Source: MGI synaptic vesicle transport Inferred from mutant phenotype. Source: MGI thymus development Inferred from mutant phenotype. Source: MGI transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Z disc Inferred from direct assay. Source: MGI apical junction complex Inferred from direct assay. Source: MGI apical part of cell Inferred from direct assay. Source: MGI basolateral plasma membrane Inferred from direct assay. Source: MGI cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell fascia adherens Inferred from direct assay. Source: MGI 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 transcription factor complex Inferred from direct assay. Source: MGI
Molecular function	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 phosphatase binding Inferred from physical interaction. Source: UniProtKB transcription coactivator activity Inferred from direct assay. Source: MGI transcription factor activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APC	P25054	3	EBI-397872,EBI-727707	From a different organism.
AXIN1	O15169	2	EBI-397872,EBI-710484	From a different organism.
Cdh1	P09803	4	EBI-397872,EBI-984420
Ctnna1	P26231	1	EBI-397872,EBI-647895
CTNNBIP1	Q9NSA3	3	EBI-397872,EBI-747082	From a different organism.
Lef1	P27782	2	EBI-397872,EBI-984464
MAPK9	P45984-1	1	EBI-397872,EBI-713586	From a different organism.
Pik3r1	P26450	2	EBI-397872,EBI-641764
Prop1	P97458	2	EBI-397872,EBI-937831
PSEN1	P49768	1	EBI-397872,EBI-297277	From a different organism.
Psen1	P49769	1	EBI-397872,EBI-990067
Tax1bp3	Q9DBG9	4	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

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 By similarity

Modified residue

37

1

Phosphoserine; by GSK3-beta By similarity

Modified residue

41

1

Phosphothreonine; by GSK3-beta By similarity

Modified residue

45

1

Phosphoserine By similarity

Modified residue

86

1

Phosphotyrosine; by CSK By similarity

Modified residue

191

1

Phosphoserine By similarity

Modified residue

551

1

Phosphothreonine Ref.13 Ref.14

Modified residue

552

1

Phosphoserine Ref.14

Modified residue

556

1

Phosphothreonine Ref.13 Ref.14

Modified residue

654

1

Phosphotyrosine Ref.6

Modified residue

675

1

Phosphoserine

Experimental info

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)
	Q02248-1 [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]	"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.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[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]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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 AND UNPHOSPHORYLATED CDH1.
[19]	"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.
[20]	"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

EMBLGenBankDDBJ

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_031640.1.

UniGene

Mm.291928

3D structure databases

PDBPDBe

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	[»]

DisProt

DP00341.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q02248. 27 interactions.

PTM databases

PhosphoSite

Q02248.

Proteomic databases

PRIDE

Q02248.

Genome annotation databases

Ensembl

ENSMUSG00000006932. Mus musculus. [Contig view]

GeneID

12387.

KEGG

mmu:12387.

Organism-specific databases

MGI

MGI:88276. Ctnnb1.

Phylogenomic databases

HOGENOM

Q02248.

HOVERGEN

Q02248.

OMA

Q02248. NNVKFLA.

Gene expression databases

ArrayExpress

Q02248.

Bgee

Q02248.

CleanEx

MM_CTNNB1.

GermOnline

ENSMUSG00000006932. Mus musculus.

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

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Other Resources

NextBio

281106.

PMAP-CutDB

Q02248.

SOURCE

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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:	June 16, 2009
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)