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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...
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...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Protein Families02:47

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key locations, protein...

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Related Experiment Video

Updated: Jul 9, 2026

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
09:17

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay

Published on: January 11, 2017

The histidine phosphatase superfamily: structure and function.

Daniel J Rigden1

  • 1School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, UK. drigden@liv.ac.uk

The Biochemical Journal
|December 21, 2007
PubMed
Summary

The histidine phosphatase superfamily, including cofactor-dependent phosphoglycerate mutase (dPGM), comprises diverse proteins. Structural analysis reveals conserved elements and surprising variations, aiding accurate functional annotation.

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Last Updated: Jul 9, 2026

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
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Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay

Published on: January 11, 2017

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • The histidine phosphatase superfamily is a large, functionally diverse protein group.
  • Members share a conserved catalytic core with a phosphorylated histidine residue.
  • Includes enzymes like cofactor-dependent phosphoglycerate mutase (dPGM), fructose-2,6-bisphosphatase, and phytases.

Purpose of the Study:

  • To review and synthesize current knowledge on histidine phosphatase superfamily structure and function.
  • To clarify conserved elements and variations within the superfamily.
  • To aid in correcting over- and mis-annotation of superfamily members.

Main Methods:

  • Analysis of an expanding set of histidine phosphatase superfamily structures.
  • Comparison of conserved elements and substrate-binding/proton donor residues.
  • Integration of structural knowledge with experimental assays.

Main Results:

  • A clearer picture of conserved structural elements has emerged.
  • Significant variation exists in substrate-binding and proton donor residues across the superfamily.
  • Structural insights help differentiate between functionally similar but distinct enzymes.

Conclusions:

  • Structural knowledge is crucial for accurate functional description within the histidine phosphatase superfamily.
  • This analysis aids in correcting historical annotation errors.
  • Future research should combine structural data with experimental assays for precise functional characterization.