| http://purl.uniprot.org/citations/11956323 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11956323 | http://www.w3.org/2000/01/rdf-schema#comment | "Dictyostelium Nek2 (DdNek2) is the first structural and functional non-vertebrate homologue of human Nek2, a NIMA-related serine/threonine kinase required for centrosome splitting in early mitosis. DdNek2 shares 43% overall amino-acid identity with its human counterpart and 54% identity within the catalytic domain. Both proteins can be subdivided in an N-terminal catalytic domain, a leucine zipper and a C-terminal domain. Kinase assays with bacterially expressed DdNek2 and C-terminal deletion mutants revealed that catalytic activity requires the presence of the leucine zipper and that autophosphorylation occurs at the C-terminus. Microscopic analyses with DdNek2 antibodies and expression of a GFP-DdNek2 fusion protein in Dictyostelium showed that DdNek2 is a permanent centrosomal resident and suggested that it is a component of the centrosomal core. The GFP-DdNek2-overexpressing mutants frequently exhibit supernumerary microtubule-organizing centers (MTOCs). This phenotype did not require catalytic activity because it was also observed in cells expressing inactive GFP-K33R. However, it was shown to be caused by overexpression of the C-terminal domain since it also occurred in GFP-mutants expressing only the C-terminus or a leucine zipper/C-terminus construct but not in those mutants expressing only the catalytic domain or a catalytic domain/leucine zipper construct. These results suggest that DdNek2 is involved in the formation of MTOCs. Furthermore, the localization of the GFP-fusion proteins revealed two independent centrosomal targeting domains of DdNek2, one within the catalytic or leucine zipper domain and one in the C-terminal domain."xsd:string |
| http://purl.uniprot.org/citations/11956323 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.115.9.1919"xsd:string |
| http://purl.uniprot.org/citations/11956323 | http://purl.uniprot.org/core/author | "Graf R."xsd:string |
| http://purl.uniprot.org/citations/11956323 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11956323 | http://purl.uniprot.org/core/name | "J Cell Sci"xsd:string |
| http://purl.uniprot.org/citations/11956323 | http://purl.uniprot.org/core/pages | "1919-1929"xsd:string |
| http://purl.uniprot.org/citations/11956323 | http://purl.uniprot.org/core/title | "DdNek2, the first non-vertebrate homologue of human Nek2, is involved in the formation of microtubule-organizing centers."xsd:string |
| http://purl.uniprot.org/citations/11956323 | http://purl.uniprot.org/core/volume | "115"xsd:string |
| http://purl.uniprot.org/citations/11956323 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11956323 |
| http://purl.uniprot.org/citations/11956323 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11956323 |
| http://purl.uniprot.org/uniprot/Q55BN8#attribution-9463E81F2871B9EB0FD8778CCE9D2328 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/11956323 |
| http://purl.uniprot.org/uniprot/Q55BN8#attribution-CF9A9C9468E8C4C8948C3C9687D73282 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/11956323 |
| http://purl.uniprot.org/uniprot/#_Q55BN8-mappedCitation-11956323 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11956323 |
| http://purl.uniprot.org/uniprot/Q55BN8 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11956323 |