2023 Fiscal Year Final Research Report
Elucidation of the specific substrate recognition mechanism of protein kinases
| Project/Area Number |
19K12220
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Review Section |
Basic Section 62010:Life, health and medical informatics-related
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| Research Institution | Maebashi Institute of Technology |
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Principal Investigator |
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| Project Period (FY) |
2019-04-01 – 2024-03-31
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| Keywords | タンパク質リン酸化 / 生命情報学 / 配列解析 |
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| Outline of Final Research Achievements |
Data of phosphorylation sites were obtained from the protein phosphorylation database, PhosphoSitePlus. We developed a pipeline to generate a phylogenetic tree by calculating the distances between substrates based on the input feature vectors. The phylogenetic trees were drawn without considering specific amino acid residues or only in specific regions, suggesting that the substrates phosphorylated by MAPK family kinases are characterized by the distribution of charged residues near the phosphorylation sites and proline distributions on distant regions from the phosphorylation sites. This suggests that there are sequence features in other parts of the substrates in addition to the motifs near phosphorylation sites.
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| Free Research Field |
生命情報学
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| Academic Significance and Societal Importance of the Research Achievements |
よく似た配列を異なるキナーゼがリン酸化する際，どのように基質を見分けているのかという機構については不明な点が多い．本研究は，基質配列のリン酸化サイトから離れた位置の配列的特徴を示唆するものである．これまで，MAPキナーゼ基質にはDモチーフと呼ばれる配列があることが知られていたが，本研究で示唆された領域はDモチーフとは異なっている．本研究はアミノ酸残基の配置のみの解析であり，また，全ての基質に共通に見られる特徴であるか，といった点には踏み込めていない．しかしながら，今後さらなる検討により，キナーゼの認識部位のヒントとなる可能性がある．
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