| General information | | DisProt: | DP00341 | | Name: | Catenin beta-1 | | Synonym(s): | CTNB1_MOUSE
Beta-catenin
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | Q02248 | | UniGene: | Mm.291928 | | SwissProt: | CTNB1_MOUSE | | TrEMBL: | | | NCBI (GI): | 399310 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 781 | | Percent disordered: | 9% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTS - 60
QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDAAHPT - 120
NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK - 180
KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL - 240
VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC - 300
LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC SSNKPAIVEA - 360
GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA - 420
AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM - 480
AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL - 540
VRAHQDTQRR TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV - 600
QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF - 660
RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI GAQGEALGYR QDDPSYRSFH - 720
SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD - 780
L
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| Functional narrative |
Involved in the regulation of cell adhesion and in signal transduction through the Wnt pathway.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 134 - 149 | | Length: | 16 | | Region sequence: |
HAVVNLINYQDDAELA | | Modification type: | | | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (PEG; NaCl; Tris)
- Sensitivity to proteolysis (297 K; CaCl2 2 mM; DTT 4 mM; Tris-HCl (pH 8.5) 90 mM)
- X-ray crystallography (PEG; Tris; Urea)
| References:
- Huber AH, Nelson WJ, Weis WI. "Three-dimensional structure of the armadillo repeat region of beta-catenin." Cell. 1997; 90(5): 871-82. PubMed: 9298899
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 550 - 562 | | Length: | 13 | | Region sequence: |
RTSMGGTQQQFVE | | Modification type: | | | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (NaCl; PEG; Tris)
- Sensitivity to proteolysis (297 K; CaCl2 2 mM; DTT 4 mM; Tris-HCl (pH 8.5) 90 mM)
- X-ray crystallography (PEG; Tris; Urea)
| References:
- Huber AH, Nelson WJ, Weis WI. "Three-dimensional structure of the armadillo repeat region of beta-catenin." Cell. 1997; 90(5): 871-82. PubMed: 9298899
| Comments:
|
| Region 3 | | Type: | Disordered | | Name: | | | Location: | 666 - 671 | | Length: | 6 | | Region sequence: |
KPQDYK | | Modification type: | | | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (NaCl; PEG; Tris)
- Sensitivity to proteolysis (297 K; CaCl2 2 mM; DTT 4 mM; Tris-HCl (pH 8.5) 90 mM)
- X-ray crystallography (PEG; Tris; Urea)
| References:
- Huber AH, Nelson WJ, Weis WI. "Three-dimensional structure of the armadillo repeat region of beta-catenin." Cell. 1997; 90(5): 871-82. PubMed: 9298899
| Comments:
|
| Region 4 | | Type: | Disordered | | Name: | | | Location: | 17 - 48 | | Length: | 32 | | Region sequence: |
DRKAAVSHWQQQSYLDSGIHSGATTTAPSLSG | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Modification site
| | Functional subclasses: | Phosphorylation
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; )
- Nuclear magnetic resonance (NMR) (278 K; pH: 7.2; H2O/D2O (90/10) 500 ul; NaN3 (0.02%); Sodium Phosphate Buffer 20 mM)
| References:
- Megy S, Bertho G, Gharbi-Benarous J, Baleux F, Benarous R, Girault JP. "Solution structure of a peptide derived from the oncogenic protein beta-Catenin in its phosphorylated and nonphosphorylated states." Peptides. 2005; 26(2): 227-41. PubMed: 15629534
| Comments:
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| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
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