What is Phosphosite?

A site on a protein, fat or other biomolecule which can be phosphorylated.

What is Phosphosite plus?

How do you cite PhosphoSitePlus?

Information derived from PhosphoSitePlus® (PSP) used in publications and presentations, should cite PSP as follows: Printed presentations (journals, books, etc.), should cite this reference: “Hornbeck PV, Zhang B, Murray B, Kornhauser JM, Latham V, Skrzypek E PhosphoSitePlus, 2014: mutations, PTMs and recalibrations.

Why is Phosphoproteomics important?

Phosphoproteomic analyses are ideal for the study of the dynamics of signalling networks. The ability to measure the global phosphorylation state of many proteins at various time points makes this approach much more powerful than traditional biochemical methods for analyzing signalling network behavior.

How do you find a phosphorylation site in a protein?

Methods for Detecting Protein Phosphorylation

Introduction.
Kinase Activity Assays.
Phospho-Specific Antibody Development.
Western Blot.
Enzyme-Linked Immunosorbent Assay (ELISA)
Cell-Based ELISA.
Intracellular Flow Cytometry and ICC/IHC.
Mass Spectrometry.

What residues can be phosphorylated?

Phosphorylation can occur on serine, threonine and tyrosine side chains (often called ‘residues’) through phosphoester bond formation, on histidine, lysine and arginine through phosphoramidate bonds, and on aspartic acid and glutamic acid through mixed anhydride linkages.

How much of the proteome is phosphorylated?

performed a deep phosphoproteome analysis on HeLa cells and estimated that at least 75 % of the proteome expressed in those cells can be phosphorylated, and this number may well rise to 90 % if phosphoproteomic experiments are performed at higher coverage [13].

Which is bigger genome or proteome?

The proteome is larger than the genome, especially in eukaryotes, in the sense that there are more proteins than genes. This is due to alternative splicing of genes and post-translational modifications like glycosylation or phosphorylation.

How many phosphorylation sites are there?

More than 100,000 different phosphorylation sites have been reported in literature-curated databases (PhosphoSitePlus [www.phosphosite.org], Phospho. ELM [phospho.elm.eu.org], and PHOSIDA [www.phosida.com]). It is unclear, however, how many of these sites are physiologically relevant.

How do you check for phosphorylation?

Researchers use several techniques for detecting and quantifying protein phosphorylation, including kinase activity assays, phospho-specific antibodies, Western blot, enzyme-linked immunosorbent assays (ELISA), cell-based ELISA, intracellular flow cytometry, mass spectrometry, and multi-analyte profiling.

Which is the best site to study phosphosite?

PhosphoSitePlus (http://www.phosphosite.org) is an open, comprehensive, manually curated and interactive resource for studying experimentally observed post-translational modifications, primarily of human and mouse proteins. It encompasses 1,30,000 non-redundant modification sites, primarily phosphorylation, ubiquitinylation and acetylation.

Which is the best description of PhosphoSitePlus ( PSP )?

PhosphoSitePlus ® ( PSP ), reengineered from PhosphoSite ® [4], is an open, dynamic, continuously curated, and highly interactive systems biology resource for studying experimentally observed PTMs in the regulation of biological processes. PhosphoSite ® was limited to phosphorylation.

How does PhosphoSitePlus help in the study of PTMs?

PhosphoSitePlus ® provides comprehensive information and tools for the study of protein post-translational modifications (PTMs) including phosphorylation, acetylation, and more. The web use is free for everyone including commercial. Protein, Sequence, or Reference Search: Protein Searches retrieve lists of proteins and their modification types

What is the purpose of the phosphorylation site page?

The Phosphorylation Site page serves information specific to the selected phosphosite. It contains three sections.