Difference between revisions of "Phosphoproteins"
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* [[DhbF]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | * [[DhbF]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
* [[Eno]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | * [[Eno]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| − | * [[ | + | * [[FusA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] |
| − | + | * [[LicB]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | |
* [[Mdh]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | * [[Mdh]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[MtlA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[Ndk]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[PdhB]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[Pgk]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[Pgm]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[PnbA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[Pnp]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[PtsI|Enzyme I]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[Pyk]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[PyrB]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| Line 144: | Line 154: | ||
* [[Eno]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | * [[Eno]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
* [[FbaA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | * [[FbaA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| − | * [[ | + | * [[FusA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] |
* [[Hbs]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | * [[Hbs]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
* [[IspU]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | * [[IspU]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[Ndk]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[OppA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[Pgi]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| + | * [[Pgk]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
===Phosphorylation on a Tyr residue=== | ===Phosphorylation on a Tyr residue=== | ||
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* [[Eno]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | * [[Eno]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
* [[InfA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | * [[InfA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| − | * [[ | + | * [[Ldh]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] |
| + | * [[OppA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| Line 159: | Line 174: | ||
* [[GapA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | * [[GapA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
* [[GlgP]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | * [[GlgP]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
| − | + | * [[Pta]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | |
| + | * [[RocA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] | ||
==Related Lists== | ==Related Lists== | ||
Revision as of 20:12, 21 January 2010
These proteins are subject to a phosphorylation event. Most often, protein phosphorylation affects the conformation of the protein resulting in changes in biological activity and/ or localization.
Contents
- 1 Phosphoproteins in B. subtilis
- 1.1 Phosphorylation on an Arg residue
- 1.2 Phosphorylation on an Asp residue: Response regulators of two-component systems
- 1.3 Phosphorylation on a Cys residue: Enzyme IIB components of the PTS
- 1.4 Phosphorylation on a His residue
- 1.5 Phosphorylation on a Ser residue
- 1.6 Phosphorylation on a Thr residue
- 1.7 Phosphorylation on a Tyr residue
- 1.8 Phosphorylation on either a Ser, Thr or Tyr residue
- 2 Related Lists
- 3 Original papers on the B. subtilis phosphoproteome
- 4 Reviews
Phosphoproteins in B. subtilis
Phosphorylation on an Arg residue
Phosphorylation on an Asp residue: Response regulators of two-component systems
- ComA: phosphorylated by ComP
- DegU: phosphorylated by DegS
- DesR: phosphorylated by DesK
- LiaR: phosphorylated by LiaS
- YdfI: phosphorylated by YdfH
- YfiK: phosphorylated by YfiJ
- YhcZ: phosphorylated by YhcY
- YvfU: phosphorylated by YvfT
- YxjL: phosphorylated by YxjM
- BceR: phosphorylated by BceS
- CssR: phosphorylated by CssS
- NatR: phosphorylated by NatK
- PhoP: phosphorylated by PhoR
- ResD: phosphorylated by ResE
- WalR: phosphorylated by WalK
- YbdJ: phosphorylated by YbdK
- YcbL: phosphorylated by YcbM
- YclJ: phosphorylated by YclK
- YkoG: phosphorylated by YkoH
- YrkP: phosphorylated by YrkO
- YvcP: phosphorylated by YvcQ
- YvrHb: phosphorylated by YvrG
- YxdJ: phosphorylated by YxdK
- CheY: phosphorylated by CheA
- CitT: phosphorylated by CitS
- DctR: phosphorylated by DctS
- GlnL: phosphorylated by GlnK
- MalR: phosphorylated by MalK
- LytT: phosphorylated by LytS
- YesN: phosphorylated by YesM
- Spo0F: part of the phosphorelay, phosphorylated by KinA, KinB, KinC, KinD, or KinE
- Spo0A: part of the phosphorelay, phosphorylated by Spo0B
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
- SacY: 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
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
- Non-PTS proteins controlled by PTS-dependent phosphorylation
- GlpK: phosphorylated by HPr
- GlcT: phosphorylated by HPr and by PtsG
- LicT: phosphorylated by HPr and likely by BglP
- SacT: phosphorylated by HPr and likely by SacP
- SacY: phosphorylated by HPr and likely by SacY
- LevR: phosphorylated by HPr and by LevE
- LicR: phosphorylated by HPr and likely by LicB
- ManR: phosphorylated by HPr and likely by ManP
- MtlR: phosphorylated by HPr and likely by MtlA
- Protein kinases of two-component systems (These kinases are dimeric proteins. Phosphorylation occurs from one subunit to the other (not quite an autophosphorylation).)
Phosphorylation on a Ser residue
- Crh: phosphorylated by HPrK
- Hpr: phosphorylated by HPrK
- AhpF Macek et al., 2007
- AroA Macek et al., 2007
- Asd Macek et al., 2007
- CitZ Macek et al., 2007
- CodY Macek et al., 2007
- DegS Macek et al., 2007
- DhbC Macek et al., 2007
- DhbF Macek et al., 2007
- Eno Macek et al., 2007
- FusA Macek et al., 2007
- LicB Macek et al., 2007
- Mdh Macek et al., 2007
- MtlA Macek et al., 2007
- Ndk Macek et al., 2007
- PdhB Macek et al., 2007
- Pgk Macek et al., 2007
- Pgm Macek et al., 2007
- PnbA Macek et al., 2007
- Pnp Macek et al., 2007
- Enzyme I Macek et al., 2007
- Pyk Macek et al., 2007
- PyrB Macek et al., 2007
Phosphorylation on a Thr residue
- LtaS
- Drm Macek et al., 2007
- Eno Macek et al., 2007
- FbaA Macek et al., 2007
- FusA Macek et al., 2007
- Hbs Macek et al., 2007
- IspU Macek et al., 2007
- Ndk Macek et al., 2007
- OppA Macek et al., 2007
- Pgi Macek et al., 2007
- Pgk Macek et al., 2007
Phosphorylation on a Tyr residue
- AhpF Macek et al., 2007
- Asd Macek et al., 2007
- Eno Macek et al., 2007
- InfA Macek et al., 2007
- Ldh Macek et al., 2007
- OppA Macek et al., 2007
Phosphorylation on either a Ser, Thr or Tyr residue
Related Lists
- two-component systems
- PTS
- PRD-containing transcription factors
- phosphorelay
- response regulator aspartate phosphatases
Original papers on the B. subtilis phosphoproteome
Reviews
Daniel C Lee, Zongchao Jia
Emerging structural insights into bacterial tyrosine kinases.
Trends Biochem Sci: 2009, 34(7);351-7
[PubMed:19525115]
[WorldCat.org]
[DOI]
(I p)
Mary Katherine Tarrant, Philip A Cole
The chemical biology of protein phosphorylation.
Annu Rev Biochem: 2009, 78;797-825
[PubMed:19489734]
[WorldCat.org]
[DOI]
(I p)
Paul G Besant, Paul V Attwood
Detection and analysis of protein histidine phosphorylation.
Mol Cell Biochem: 2009, 329(1-2);93-106
[PubMed:19387796]
[WorldCat.org]
[DOI]
(I p)
Emmanuelle Bechet, Sébastien Guiral, Sophie Torres, Ivan Mijakovic, Alain-Jean Cozzone, Christophe Grangeasse
Tyrosine-kinases in bacteria: from a matter of controversy to the status of key regulatory enzymes.
Amino Acids: 2009, 37(3);499-507
[PubMed:19189200]
[WorldCat.org]
[DOI]
(I p)
Boris Macek, Matthias Mann, Jesper V Olsen
Global and site-specific quantitative phosphoproteomics: principles and applications.
Annu Rev Pharmacol Toxicol: 2009, 49;199-221
[PubMed:18834307]
[WorldCat.org]
[DOI]
(P p)
Carsten Jers, Boumediene Soufi, Christophe Grangeasse, Josef Deutscher, Ivan Mijakovic
Phosphoproteomics in bacteria: towards a systemic understanding of bacterial phosphorylation networks.
Expert Rev Proteomics: 2008, 5(4);619-27
[PubMed:18761471]
[WorldCat.org]
[DOI]
(I p)
Boumediene Soufi, Carsten Jers, Mette Erichsen Hansen, Dina Petranovic, Ivan Mijakovic
Insights from site-specific phosphoproteomics in bacteria.
Biochim Biophys Acta: 2008, 1784(1);186-92
[PubMed:17881301]
[WorldCat.org]
[DOI]
(P p)
Christophe Grangeasse, Alain J Cozzone, Josef Deutscher, Ivan Mijakovic
Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology.
Trends Biochem Sci: 2007, 32(2);86-94
[PubMed:17208443]
[WorldCat.org]
[DOI]
(P p)
Ivan Mijakovic, Dina Petranovic, Nunzio Bottini, Josef Deutscher, Peter Ruhdal Jensen
Protein-tyrosine phosphorylation in Bacillus subtilis.
J Mol Microbiol Biotechnol: 2005, 9(3-4);189-97
[PubMed:16415592]
[WorldCat.org]
[DOI]
(P p)
Josef Deutscher, Milton H Saier
Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established.
J Mol Microbiol Biotechnol: 2005, 9(3-4);125-31
[PubMed:16415586]
[WorldCat.org]
[DOI]
(P p)
Liang Shi
Manganese-dependent protein O-phosphatases in prokaryotes and their biological functions.
Front Biosci: 2004, 9;1382-97
[PubMed:14977554]
[WorldCat.org]
[DOI]
(I e)
Alain J Cozzone, Christophe Grangeasse, Patricia Doublet, Bertrand Duclos
Protein phosphorylation on tyrosine in bacteria.
Arch Microbiol: 2004, 181(3);171-81
[PubMed:14745484]
[WorldCat.org]
[DOI]
(P p)
Susanne Klumpp, Josef Krieglstein
Phosphorylation and dephosphorylation of histidine residues in proteins.
Eur J Biochem: 2002, 269(4);1067-71
[PubMed:11856347]
[WorldCat.org]
[DOI]
(P p)
H S Cho, J G Pelton, D Yan, S Kustu, D E Wemmer
Phosphoaspartates in bacterial signal transduction.
Curr Opin Struct Biol: 2001, 11(6);679-84
[PubMed:11751048]
[WorldCat.org]
[DOI]
(P p)
C J Bakal, J E Davies
No longer an exclusive club: eukaryotic signalling domains in bacteria.
Trends Cell Biol: 2000, 10(1);32-8
[PubMed:10603474]
[WorldCat.org]
[DOI]
(P p)
P J Kennelly, M Potts
Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation.
J Bacteriol: 1996, 178(16);4759-64
[PubMed:8759835]
[WorldCat.org]
[DOI]
(P p)
L N Johnson, D Barford
The effects of phosphorylation on the structure and function of proteins.
Annu Rev Biophys Biomol Struct: 1993, 22;199-232
[PubMed:8347989]
[WorldCat.org]
[DOI]
(P p)
R B Bourret, K A Borkovich, M I Simon
Signal transduction pathways involving protein phosphorylation in prokaryotes.
Annu Rev Biochem: 1991, 60;401-41
[PubMed:1883200]
[WorldCat.org]
[DOI]
(P p)
