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Phosphorylation

Phosphorylation

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.
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Phosphorylation

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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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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.
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Related Experiment Video

Updated: Apr 4, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Mining Conditional Phosphorylation Motifs.

Xiaoqing Liu, Jun Wu, Haipeng Gong

IEEE/ACM Transactions on Computational Biology and Bioinformatics

|September 11, 2015

Summary

This study introduces conditional phosphorylation motifs and the C-Motif algorithm for efficient and non-redundant discovery of significant phosphorylation patterns. C-Motif improves upon existing methods in coverage, redundancy, and execution speed.

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Last Updated: Apr 4, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination

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Published on: May 18, 2017

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

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Identification of Kinase-substrate Pairs Using High Throughput Screening

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Published on: August 29, 2015

Area of Science:

Bioinformatics
Computational Biology
Proteomics

Background:

Phosphorylation motifs are critical for understanding kinase specificity and cellular signaling.
Existing algorithms struggle to efficiently identify significant, non-redundant phosphorylation motifs with high coverage.

Purpose of the Study:

To introduce the novel concept of conditional phosphorylation motifs.
To develop an efficient algorithm (C-Motif) for discovering significant and non-redundant phosphorylation motifs.

Main Methods:

Proposed the concept of conditional phosphorylation motifs to filter redundant patterns.
Developed the C-Motif algorithm based on the Apriori framework.
Integrated statistical significance testing and motif frequency analysis in a single stage.

Main Results:

C-Motif effectively filters motifs whose significance is derived from constituent parts.
Experimental results show C-Motif outperforms MMFPh and Motif-All in coverage and non-redundancy.
C-Motif demonstrates superior execution efficiency compared to existing methods.

Conclusions:

Conditional phosphorylation motifs offer a refined approach to motif discovery.
C-Motif provides an efficient and effective solution for identifying significant, non-redundant phosphorylation motifs.
The C-Motif algorithm advances the field of phosphoproteomics data analysis.