Bioinformatic search of plant microtubule-and cell cycle related serine-threonine protein kinases
Autor: | Pavel Karpov, Nadezhda Yu Shashina, Yaroslav B. Blume, Alla I. Yemets, Alexey Nyporko, Elena S. Nadezhdina, Vadym G Matusov |
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Jazyk: | angličtina |
Rok vydání: | 2010 |
Předmět: |
0106 biological sciences
PLK4 Models Molecular lcsh:QH426-470 lcsh:Biotechnology Molecular Sequence Data Serine threonine protein kinase Biology Protein Serine-Threonine Kinases 01 natural sciences PLK1 Microtubules 03 medical and health sciences lcsh:TP248.13-248.65 Genetics Humans Protein phosphorylation Amino Acid Sequence Phosphorylation Protein kinase A Conserved Sequence Phylogeny 030304 developmental biology 0303 health sciences Protein-Serine-Threonine Kinases Binding Sites Kinase Research Cell Cycle Computational Biology Plants Cell biology Protein Structure Tertiary lcsh:Genetics Structural Homology Protein Biocatalysis Sequence Alignment 010606 plant biology & botany Biotechnology |
Zdroj: | BMC Genomics BMC Genomics, Vol 11, Iss Suppl 1, p S14 (2010) |
ISSN: | 1471-2164 |
Popis: | A bioinformatic search was carried for plant homologues of human serine-threonine protein kinases involved in regulation of cell division and microtubule protein phosphorylation (SLK, PAK6, PAK7, MARK1, MAST2, TTBK1, TTBK2, AURKA, PLK1, PLK4 and PASK). A number of SLK, MAST2 and AURKA plant homologues were identified. The closest identified homologue of human AURKA kinase was a protein of unknown function, A7PY12/GSVIVT00026259001 from Vitis vinifera (herein named as "STALK", Serine-Threonine Aurora-Like Kinase). Analysis of STALK's three-dimensional structure confirmed its relationship to the subgroup of AURKA-like protein kinases. |
Databáze: | OpenAIRE |
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