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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Phosphorylation01:02

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.
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...
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...

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Related Experiment Video

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Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Using multitask classification methods to investigate the kinase-specific phosphorylation sites.

Shan Gao1, Shuo Xu, Yaping Fang

  • 1Applied Bioinformatics Laboratory, Kansas University, 2034 Becker Dr,, Lawrence, KS 66047, USA. jwfang@ku.edu.

Proteome Science
|July 5, 2012
PubMed
Summary
This summary is machine-generated.

Computational methods for identifying protein phosphorylation sites are crucial. This study presents a multitask learning framework that identifies 18 common features across four kinase families, improving understanding of phosphorylation mechanisms.

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Last Updated: May 20, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

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Published on: August 29, 2015

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

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

Published on: May 3, 2018

Area of Science:

  • Biochemistry
  • Computational Biology
  • Bioinformatics

Background:

  • Computational methods for identifying protein phosphorylation sites are increasingly vital.
  • These methods reduce experimental costs and enhance understanding of phosphorylation mechanisms.
  • Protein phosphorylation plays a critical role in cellular signaling pathways.

Purpose of the Study:

  • To develop a multitask learning framework for simultaneous analysis of four kinase families.
  • To identify common features predictive of phosphorylation sites across these families.
  • To improve the efficiency and accuracy of phosphorylation site prediction.

Main Methods:

  • Implemented a multitask learning framework for analyzing four kinase families concurrently.
  • Utilized two multitask classification methods: Multi-Task Least Squares Support Vector Machines (MTLS-SVMs) and Multi-Task Feature Selection (MT-Feat3).
  • Focused on identifying shared features predictive of phosphorylation sites.

Main Results:

  • Successfully identified 18 common features shared by the four kinase families.
  • Demonstrated the reliability and consistency of the selected features across both multitask learning methods.
  • The identified features are significant predictors of phosphorylation sites.

Conclusions:

  • The identified features enable the development of efficient multitask classifiers for protein phosphorylation.
  • These features are important for understanding protein phosphorylation across multiple kinase families.
  • The findings contribute to advancing computational approaches in phosphoproteomics.