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IID50072
 UniprotP26231
ProteinCatenin alpha-1
GeneCtnna1
OrganismMus musculus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
906
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-906 Homo dimer :
 Evidence X-RAY 4k1n B Reference
       Region 4k1n B 1-84 disorder
       Region 4k1n B 85-262 order
       Region 4k1n B 263-289 disorder
       Region 4k1n B 290-631 order
       Region 4k1n B 632-906 disorder
 Evidence X-RAY 4k1n A Reference
       Region 4k1n A 1-84 disorder
       Region 4k1n A 85-262 order
       Region 4k1n A 263-289 disorder
       Region 4k1n A 290-631 order
       Region 4k1n A 632-906 disorder
Seq 57-261 Hetero dimer : IID50011Complex
 Evidence X-RAY 1dow A Reference
       Region 1dow A 57-261 order
Seq 82-262 Homo dimer :
 Evidence X-RAY 1dov A Reference
       Region 1dov A 82-262 order
Seq 302-356 Hetero dimer : P12003
 Evidence X-RAY 4e18 B Reference
       Region 4e18 B 302-317 order
       Region 4e18 B 318-327 disorder
       Region 4e18 B 328-354 order
       Region 4e18 B 355-356 disorder
Seq 321-356 Hetero dimer : P12003
 Evidence X-RAY 4e17 B Reference
       Region 4e17 B 321-325 disorder
       Region 4e17 B 326-353 order
       Region 4e17 B 354-356 disorder
Seq 385-651 Monomer :
 Evidence X-RAY 1l7c C Reference
       Region 1l7c C 385-392 disorder
       Region 1l7c C 393-600 order
       Region 1l7c C 601-606 disorder
       Region 1l7c C 607-631 order
       Region 1l7c C 632-651 disorder
 Evidence X-RAY 1l7c B Reference
       Region 1l7c B 385-390 disorder
       Region 1l7c B 391-562 order
       Region 1l7c B 563-565 disorder
       Region 1l7c B 566-597 order
       Region 1l7c B 598-606 disorder
       Region 1l7c B 607-631 order
       Region 1l7c B 632-651 disorder
 Evidence X-RAY 1l7c A Reference
       Region 1l7c A 385-387 disorder
       Region 1l7c A 388-601 order
       Region 1l7c A 602-605 disorder
       Region 1l7c A 606-631 order
       Region 1l7c A 632-651 disorder
Seqphosphorylation
    297-297 Phosphoserine
    264-264 Phosphoserine
    295-295 Phosphoserine
    634-634 Phosphothreonine
    641-641 Phosphoserine
    645-645 Phosphothreonine
    655-655 Phosphoserine
    652-652 Phosphoserine
    658-658 Phosphothreonine
    851-851 Phosphoserine
Seqacetylation
    2-2 N-acetylthreonine
 
Prediction
NeProc
Disorder 1-7,636-710,719-723,730-734,849-906
Order 8-635,711-718,724-729,735-848
ProS 636-693,699-710,730-734,853-860,867-885,891-906
AlphaFold
Disorder 1-9,13-13,15-17,39-56,262-275,632-667,798-809,843-856,862-906
Order 10-12,14-14,18-38,57-261,276-631,668-797,810-842,857-861
SEG 32-43 ,258-269 ,540-551
Function
Function in SwissProt
Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (PubMed:21145499). May play a crucial role in cell differentiation.
Biological Process
See also
Diagram with PDB data
Cdh1/Ctnnb1BETA-CATENIN/E-CADHERIN COMPLEX