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Updated: Jun 4, 2026

12:26
Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Motif-All: discovering all phosphorylation motifs
Zengyou He1, Can Yang, Guangyu Guo
1School of Software, Dalian University of Technology, Dalian, China. zyhe@dlut.edu.cn
BMC Bioinformatics
|February 24, 2011
Summary
Motif-All efficiently identifies statistically significant phosphorylation motifs. This data mining tool aids in understanding biological regulation and predicting phosphorylation events.
Area of Science:
- Bioinformatics
- Computational Biology
- Systems Biology
Background:
- Phosphorylation motifs are key patterns surrounding phosphorylation sites, crucial for understanding cellular regulation.
- Discovering these motifs aids in predicting phosphorylation events and elucidating biological mechanisms.
- Large-scale phosphorylation data enables substrate-driven motif discovery via data mining.
Purpose of the Study:
- To develop an efficient algorithm for identifying statistically significant phosphorylation motifs.
- To improve the accuracy and speed of motif discovery in large biological datasets.
Main Methods:
- Introduced Motif-All, an algorithm utilizing a support constraint to reduce search space and prevent artifacts.
- Employed a two-stage mining process: candidate generation from phosphorylated sequences, followed by statistical significance testing using odds ratio.
- Applied data mining techniques to large phosphorylation datasets.
Main Results:
- Motif-All efficiently identifies all statistically significant motifs.
- The algorithm outperforms existing methods in both effectiveness and efficiency on real-world data.
- Experimental results validate the algorithm's superior performance.
Conclusions:
- Motif-All serves as a valuable tool for discovering significant phosphorylation motifs.
- The developed algorithm enhances the prediction of phosphorylation events and regulatory mechanisms.
- Source code and datasets are publicly available for further research.
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
