Difference between revisions of "Phosphoproteins"

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===Phosphorylation on an Arg residue===
 
===Phosphorylation on an Arg residue===
 
* [[CtsR]], phosphorylated by [[McsB]]
 
* [[CtsR]], phosphorylated by [[McsB]]
 +
* [[AccD]]
 +
* [[AlaR]]
 +
* [[Apt]]
 +
* [[ArgG]]
 +
* [[AroA]]
 +
* [[AroF]]
 +
* [[AtpH]]
 +
* [[BdhA]]
 +
* [[ClpC]]
 +
* [[ClpP]]
 +
* [[ComFA]]
 +
* [[ComFC]]
 +
* [[ComGA]]
 +
* [[ComK]]
 +
 +
 +
* [[DivIVA]]
 +
* [[FadB]]
 +
* [[FliY]]
 +
* [[FrlB]]
 +
* [[GapA]]
 +
* [[GatC]]
 +
* [[GgaA]]
 +
* [[GltA]]
 +
* [[Gmk]]
 +
* [[GroEL]]
 +
* [[GtaB]]
 +
* [[GudB]]
 +
* [[HemB]]
 +
* [[HupA]]
 +
 +
* [[Icd]]
 +
* [[IlvB]]
 +
* [[IlvC]]
 +
* [[IscC]]
 +
* [[KatA]]
 +
* [[LacA]]
 +
* [[LeuB]]
 +
* [[LeuC]]
 +
* [[LutB]]
 +
* [[LutC]]
 +
* [[McsA]]
 +
* [[Mdh]]
 +
* [[MenB]]
 +
* [[MtnA]]
 +
 +
* [[MtnK]]
 +
* [[NadB]]
 +
* [[Nin]]
 +
* [[OdhA]]
 +
* [[OxdC]]
 +
* [[PdxS]]
 +
* [[PfkA]]
 +
* [[PurA]]
 +
* [[RadC]]
 +
* [[RecA]]
 +
* [[RplK]]
 +
* [[RplN]]
 +
* [[RplW]]
 +
* [[RpmE2]]
 +
 +
* [[RpmGA]]
 +
* [[RpoB]]
 +
* [[RpoC]]
 +
* [[RpsG]]
 +
 +
* [[GapA]]
 +
* [[GatC]]
 +
* [[GgaA]]
 +
* [[GltA]]
 +
* [[Gmk]]
 +
* [[GroEL]]
 +
* [[GtaB]]
 +
* [[GudB]]
 +
* [[HemB]]
 +
* [[HupA]]
  
 
===Phosphorylation on an Asp residue: Response regulators of [[two-component systems]]===
 
===Phosphorylation on an Asp residue: Response regulators of [[two-component systems]]===

Revision as of 14:01, 20 April 2012

These proteins are subject to a phosphorylation event. Most often, protein phosphorylation affects the conformation of the protein resulting in changes in biological activity, interaction properties and/ or localization.

Parent category
Neighbouring categories
Related categories

none






Phosphoproteins in B. subtilis

Phosphorylation on an Arg residue


Phosphorylation on an Asp residue: Response regulators of two-component systems

Phosphorylation on a Cys residue

  • Enzyme IIB components of the PTS
    • PtsG: glucose permease, EIICBA: phosphorylated by PtsG-IIA domain
    • GamP: glucosamine permease, EIICBA: phosphorylated by GamP-IIA domain
    • MurP: N-acetyl muramic acid-specific phosphotransferase system, EIIBC: likely phosphorylated by PtsG-IIA domain
    • SacP: sucrose permease (high affinity): phosphorylated by PtsG-IIA domain
    • SacX: sucrose permease (low affinity): phosphorylated by PtsG-IIA domain
    • MtlA: mannitol permease: phosphorylated by MtlF
    • GmuB: galactomannan permease: phosphorylated by GmuA
    • TreP: trehalose permease: phosphorylated by PtsG-IIA domain
    • MalP: maltose permease: likely phosphorylated by PtsG-IIA domain
    • FruA: fructose permease: phosphorylated by FruA-IIA domain
    • ManP: mannose permease: phosphorylated by ManP-IIA domain
    • LicB: lichenan permease: phosphorylated by LicA
    • BglP: ß-glucoside permease: phosphorylated by BglP-IIA domain
    • NagP: N-acetylglucosamine permease: phosphorylated by PtsG-IIA domain

Phosphorylation on a His residue

  • PTS proteins
    • Enzyme I: autophosphorylated using phosphoenolpyruvate as phosphate donor
    • HPr: phosphorylated by Enzyme I
    • PtsG: glucose permease, EIICBA: phosphorylated by HPr
    • GamP: glucosamine permease, EIICBA: phosphorylated by HPr
    • MtlF: mannitol permease: phosphorylated by HPr
    • GmuA: galactomannan permease: phosphorylated by HPr
    • MalP: maltose permease: phosphorylated by HPr
    • FruA: fructose permease: phosphorylated by HPr
    • ManP: mannose permease: phosphorylated by HPr
    • LevD: fructose permease: phosphorylated by HPr
    • LevE: fructose permease: phosphorylated by LevD
    • LicA: lichenan permease: phosphorylated by HPr
    • BglP: ß-glucoside permease
    • YpqE: unknown EIIA component: phosphorylated by HPr
    • YyzE: truncated PTS IIA protein: might perhaps be phosphorylated by HPr

Phosphorylation on a Ser residue

Phosphorylation on a Thr residue

Phosphorylation on a Tyr residue

Phosphorylation on either a Ser, Thr or Tyr residue

Related Lists

Original papers on the B. subtilis phosphoproteome

Boumediene Soufi, Chanchal Kumar, Florian Gnad, Matthias Mann, Ivan Mijakovic, Boris Macek
Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis.
J Proteome Res: 2010, 9(7);3638-46
[PubMed:20509597] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)


Reviews


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