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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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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.
Protein kinases
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.
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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PhosphoNetworks: a database for human phosphorylation networks.

Jianfei Hu1, Hee-Sool Rho, Robert H Newman

  • 1Department of Ophthalmology, Johns Hopkins School of Medicine, Department of Pharmacology and Molecular Sciences, Center for High-Throughput Biology, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA, Department of Biology, North Carolina Agricultural and Technical State University, Greensboro, NC 27411, USA and The Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA.

Bioinformatics (Oxford, England)
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Summary

PhosphoNetworks offers a detailed map of cellular phosphorylation networks, identifying kinase-substrate relationships and specific phosphorylation sites. This comprehensive database aids proteomics and disease research.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Systems Biology

Background:

  • Phosphorylation is crucial for cellular signal transduction.
  • Existing databases often lack detailed kinase-substrate relationships (KSRs) and specific phosphorylation sites.
  • Mass spectrometry is a common method for identifying phosphorylation sites.

Purpose of the Study:

  • To present PhosphoNetworks, a novel database for phosphorylation research.
  • To provide a high-resolution map of phosphorylation networks, including KSRs and specific sites.
  • To offer analytical tools for dissecting these networks.

Main Methods:

  • Development of PhosphoNetworks database.
  • Integration of high-throughput protein microarray data for KSR identification.
  • Curation of known KSRs from scientific literature.
  • Inclusion of analytical tools for network analysis.

Main Results:

  • PhosphoNetworks provides a comprehensive dataset of KSRs.
  • The database maps specific phosphorylation sites acted upon by kinases.
  • It includes data from both high-throughput experiments and literature curation.

Conclusions:

  • PhosphoNetworks offers a valuable resource for proteomics and phosphorylation-related disease research.
  • The database's detailed network information is expected to advance the field.
  • It facilitates a deeper understanding of cellular signal transduction pathways.