Matches in DBpedia 2014 for { <http://dbpedia.org/resource/Ankyrin_repeat> ?p ?o. }
Showing items 1 to 36 of
36
with 100 items per page.
- Ankyrin_repeat abstract "The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops, first discovered in signaling proteins in yeast Cdc10 and Drosophila Notch. Domains consisting of ankyrin repeats mediate protein-protein interactions and are among the most common structural motifs in known proteins. They appear in bacterial, archaeal, and eukaryotic proteins, but are far more common in eukaryotes. Ankyrin repeat proteins, though absent in most viruses, are common among poxviruses. Most proteins that contain the motif have four to six repeats, although its namesake ankyrin contains 24, and the largest known number of repeats is 34, predicted in a protein expressed by Giardia lamblia.Ankyrin repeats typically fold together to form a single, linear solenoid structure called ankyrin repeat domains. These domains are one of the most common protein–protein interaction platforms in nature. They occur in a large number of functionally diverse proteins, mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers. The repeat has been found in proteins of diverse function such as transcriptional initiators, cell cycle regulators, cytoskeletal, ion transporters, and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function, since there is no specific sequence or structure that is universally recognised by it.".
- Ankyrin_repeat symbol "Ank".
- Ankyrin_repeat thumbnail Ankyrin_R_membrane-binding_domain_1N11.png?width=300.
- Ankyrin_repeat wikiPageID "5822839".
- Ankyrin_repeat wikiPageRevisionID "590591883".
- Ankyrin_repeat caption "Ribbon diagram of a fragment of the membrane-binding domain of ankyrin R.".
- Ankyrin_repeat hasPhotoCollection Ankyrin_repeat.
- Ankyrin_repeat interpro "IPR002110".
- Ankyrin_repeat name "Ankyrin repeat domain".
- Ankyrin_repeat pdb ", , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , ,".
- Ankyrin_repeat pfam "PF00023".
- Ankyrin_repeat prosite "PDOC50088".
- Ankyrin_repeat scop "1".
- Ankyrin_repeat smart "SM00248".
- Ankyrin_repeat symbol "Ank".
- Ankyrin_repeat subject Category:Protein_structural_motifs.
- Ankyrin_repeat type Artifact100021939.
- Ankyrin_repeat type Decoration103169390.
- Ankyrin_repeat type Design103178782.
- Ankyrin_repeat type Motif103789014.
- Ankyrin_repeat type Object100002684.
- Ankyrin_repeat type PhysicalEntity100001930.
- Ankyrin_repeat type ProteinStructuralMotifs.
- Ankyrin_repeat type Whole100003553.
- Ankyrin_repeat type Biomolecule.
- Ankyrin_repeat type Protein.
- Ankyrin_repeat type BiologicalObject.
- Ankyrin_repeat comment "The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops, first discovered in signaling proteins in yeast Cdc10 and Drosophila Notch. Domains consisting of ankyrin repeats mediate protein-protein interactions and are among the most common structural motifs in known proteins. They appear in bacterial, archaeal, and eukaryotic proteins, but are far more common in eukaryotes.".
- Ankyrin_repeat label "Ankyrin repeat".
- Ankyrin_repeat sameAs m.02p9t25.
- Ankyrin_repeat sameAs Q4766126.
- Ankyrin_repeat sameAs Q4766126.
- Ankyrin_repeat sameAs Ankyrin_repeat.
- Ankyrin_repeat wasDerivedFrom Ankyrin_repeat?oldid=590591883.
- Ankyrin_repeat depiction Ankyrin_R_membrane-binding_domain_1N11.png.
- Ankyrin_repeat isPrimaryTopicOf Ankyrin_repeat.