Difference between revisions of "Phosphoproteins"
(→Phosphorylation on an Arg residue) |
(→Phosphorylation on an Arg residue) |
||
| (5 intermediate revisions by the same user not shown) | |||
| Line 72: | Line 72: | ||
* [[IolE]] (R216) | * [[IolE]] (R216) | ||
* [[KatA]] | * [[KatA]] | ||
| + | * [[Kre]] (R26) | ||
* [[LeuB]] | * [[LeuB]] | ||
* [[LeuC]] | * [[LeuC]] | ||
| Line 80: | Line 81: | ||
* [[MelA]] (R56) | * [[MelA]] (R56) | ||
* [[MenB]] | * [[MenB]] | ||
| + | * [[MntB]] (R132) | ||
* [[MtnA]] | * [[MtnA]] | ||
| Line 86: | Line 88: | ||
* [[Nin]] | * [[Nin]] | ||
* [[OdhA]] | * [[OdhA]] | ||
| − | * [[OdhB]] | + | * [[OdhB]] (R300) |
* [[OxdC]] | * [[OxdC]] | ||
* [[PdxS]] | * [[PdxS]] | ||
| Line 94: | Line 96: | ||
* [[RecA]] | * [[RecA]] | ||
* [[RplK]] | * [[RplK]] | ||
| − | * [[RplN]] | + | * [[RplN]] (R17) |
| + | * [[RplV]] (R11) | ||
* [[RplW]] | * [[RplW]] | ||
* [[RpmEB]] | * [[RpmEB]] | ||
| Line 101: | Line 104: | ||
* [[RpoC]] | * [[RpoC]] | ||
* [[RpsG]] | * [[RpsG]] | ||
| − | * [[RpsH]] | + | * [[RpsH]] (R47, R72) |
* [[RpsI]] | * [[RpsI]] | ||
* [[RpsL]] | * [[RpsL]] | ||
| Line 107: | Line 110: | ||
* [[RpsN]] | * [[RpsN]] | ||
* [[ScoC]] | * [[ScoC]] | ||
| + | * [[SrfAA]] (R226) | ||
* [[SrfAB]] | * [[SrfAB]] | ||
* [[SsbA]] | * [[SsbA]] | ||
| Line 113: | Line 117: | ||
* [[ThyB]] | * [[ThyB]] | ||
* [[Tig]] | * [[Tig]] | ||
| − | * [[TufA]] | + | * [[TufA]] (R384) |
* [[YceE]] | * [[YceE]] | ||
* [[YciC]] | * [[YciC]] | ||
* [[YdcI]] | * [[YdcI]] | ||
* [[YdjO]] | * [[YdjO]] | ||
| + | * [[YerA]] (R14) | ||
* [[YfmG]] | * [[YfmG]] | ||
* [[YheA]] | * [[YheA]] | ||
| + | * [[YkoM]] (R89) | ||
| + | |||
* [[YlbN]] | * [[YlbN]] | ||
* [[YloV]] | * [[YloV]] | ||
| + | * [[YpiF]] (R4) | ||
* [[YrvO]] | * [[YrvO]] | ||
* [[YtxH]] | * [[YtxH]] | ||
| + | * [[YvfU]] (R116, R143) | ||
* [[YvrO]] | * [[YvrO]] | ||
Latest revision as of 11:12, 24 October 2016
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 | |
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
- 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 Original papers on the B. subtilis phosphoproteome
- 3 Reviews
- 4 Back to categories
Phosphoproteins in B. subtilis
Phosphorylation on an Arg residue
- CtsR (R55), phosphorylated by McsB
- AccD
- AhpF
- AlaR
- AlbF (R17)
- Apt
- ArgG
- AroA
- AroF
- AtpH
- BdhA
- BfmBAB (R23)
- ClpC
- ClpP
- ComFA
- ComFC
- ComGA
- ComK
- CsoR (R24)
- DivIVA
- FadB
- FliY
- FlgN
- FrlB
- GanA
- GapA
- GatC
- GgaA
- GltA
- Gmk
- GroEL
- GtaB
- GudB
- Hbs
- HemB
- Hpf
- HrcA
- Icd
- IlvB
- IlvC
- IolE (R216)
- KatA
- Kre (R26)
- LeuB
- LeuC
- LutB
- LutC
- McsA
- Mdh
- MelA (R56)
- MenB
- MntB (R132)
- MtnA
- MtnK
- NadB
- Nin
- OdhA
- OdhB (R300)
- OxdC
- PdxS
- PfkA
- PurA
- RadC
- RecA
- RplK
- RplN (R17)
- RplV (R11)
- RplW
- RpmEB
- RpmGA
- RpoB
- RpoC
- RpsG
- RpsH (R47, R72)
- RpsI
- RpsL
- RpsM
- RpsN
- ScoC
- SrfAA (R226)
- SrfAB
- SsbA
- SsbB
- ThiC
- ThyB
- Tig
- TufA (R384)
- YceE
- YciC
- YdcI
- YdjO
- YerA (R14)
- YfmG
- YheA
- YkoM (R89)
Phosphorylation on an Asp residue: Response regulators of two-component systems
- BceR: phosphorylated by BceS
- CheB: phosphorylated by CheA
- CheV: phosphorylated by CheA
- CheY: phosphorylated by CheA
- CitT: phosphorylated by CitS
- ComA: phosphorylated by ComP
- CssR: phosphorylated by CssS
- DctR: phosphorylated by DctS
- DegU: phosphorylated by DegS
- DesR: phosphorylated by DesK
- GlnL: phosphorylated by GlnK
- LiaR: phosphorylated by LiaS
- LytT: phosphorylated by LytS
- MalR: phosphorylated by MalK
- NatR: phosphorylated by NatK
- PhoP: phosphorylated by PhoR
- ResD: phosphorylated by ResE
- Spo0A: part of the phosphorelay, phosphorylated by Spo0B
- Spo0F: part of the phosphorelay, phosphorylated by KinA, KinB, KinC, KinD, or KinE
- WalR: phosphorylated by WalK
- YbdJ: phosphorylated by YbdK
- YcbL: phosphorylated by YcbM
- YclJ: phosphorylated by YclK
- YdfI: phosphorylated by YdfH
- YesN: phosphorylated by YesM
- YfiK: phosphorylated by YfiJ
- YhcZ: phosphorylated by YhcY
- YkoG: phosphorylated by YkoH
- YrkP: phosphorylated by YrkO
- YvcP: phosphorylated by YvcQ
- YvfU: phosphorylated by YvfT
- YvrHb: phosphorylated by YvrG
- YxdJ: phosphorylated by YxdK
- YxjL: phosphorylated by YxjM
Phosphorylation on a Cys residue
- PRD-type regulator containing a IIB-like domain
- 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
- 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
- AbrB Soufi et al., 2010
- 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
- CotB Nguyen et al., 2016
- CotG Saggese et al., 2014
- 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
- GerR Soufi et al., 2010
- GlmM Macek et al., 2007, Eymannet al., 2007
- GroES Soufi et al., 2010
- GyrB Soufi et al., 2010
- IlvC Soufi et al., 2010
- LicB Macek et al., 2007
- ManP Macek et al., 2007
- Mdh Macek et al., 2007
- MetS Soufi et al., 2010
- 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
- PupG Macek et al., 2007
- Enzyme I Macek et al., 2007
- Pyk Macek et al., 2007 Eymannet al., 2007
- PyrB Macek et al., 2007
- RecA Soufi et al., 2010
- RocF Soufi et al., 2010
- RpsJ Rosenberg et al., 2015
- RsbRC Macek et al., 2007
- RsbS Macek et al., 2007
- RsbV Macek et al., 2007 Eymannet al., 2007
- SpoIIAA Macek et al., 2007
- SpoVG Macek et al., 2007
- SrfAA Macek et al., 2007
- SrfAB Macek et al., 2007
- SrfAC Macek et al., 2007
- SspA Rosenberg et al., 2015
- SspB Rosenberg et al., 2015
- SucC Macek et al., 2007
- TagE Macek et al., 2007
- ThiC Soufi et al., 2010
- Tpi Macek et al., 2007
- TrmK Macek et al., 2007
- Tsf Macek et al., 2007
- MurQ Macek et al., 2007
- YcnE Macek et al., 2007
- YerA Macek et al., 2007
- YfjC Soufi et al., 2010
- YfkK Macek et al., 2007
- YjbK Soufi et al., 2010
- YpfD Macek et al., 2007
- YpoC Macek et al., 2007
- YqbO Macek et al., 2007
- YtnP Macek et al., 2007
- YukF Soufi et al., 2010
- YurJ Soufi et al., 2010
Phosphorylation on a Thr residue
- LtaS
- AroA Eymannet al., 2007
- CotG Saggese et al., 2014
- CpgA Pompeo et al., 2012
- Drm Macek et al., 2007
- Eno Macek et al., 2007
- FbaA Macek et al., 2007
- FusA Macek et al., 2007
- GndA Macek et al., 2007
- GpsB Pompeo et al., 2015
- Hbs Macek et al., 2007
- Ndk Macek et al., 2007
- OppA Macek et al., 2007
- Pgi Macek et al., 2007
- Pgk Macek et al., 2007
- PrkC Macek et al., 2007
- PrkD Pietacket al., 2010
- RsbR Macek et al., 2007 Eymannet al., 2007
- RsbRB Eymannet al., 2007 Macek et al., 2007
- RsbRC Macek et al., 2007
- RsbRD Macek et al., 2007 Eymannet al., 2007
- SodA Macek et al., 2007
- TyrZ Soufi et al., 2010
- YdcC Soufi et al., 2010
- YvcK Foulquier et al., 2014
Phosphorylation on a Tyr residue
- AhpF Macek et al., 2007
- Asd Macek et al., 2007
- EF-G Rosenberg et al., 2015
- EF-Tu Rosenberg et al., 2015
- Eno Macek et al., 2007
- EpsB Elsholz et al., 2007
- EpsE Elsholz et al., 2007
- FlgN Macek et al., 2007
- InfA Macek et al., 2007
- Ldh Macek et al., 2007
- OppA Macek et al., 2007
- PtkA Soufi et al., 2010
- SsbA Mijakovic et al., 2006
- SsbB Mijakovic et al., 2006
- ThiC Soufi et al., 2010
- TuaD Mijakovic et al., 2003
- Ugd Mijakovic et al., 2003, Macek et al., 2007
- YjoA Macek et al., 2007
- YnfE Macek et al., 2007
- YorK Macek et al., 2007
Phosphorylation on either a Ser, Thr or Tyr residue
- AhpC Levine et al., 2007
- AlsD Levine et al., 2007
- AspS Levine et al., 2007
- AtpA Levine et al., 2007
- AtpD Levine et al., 2007
- DnaK Eymannet al., 2007
- DppA Levine et al., 2007
- GapA Macek et al., 2007 Eymannet al., 2007
- GlgP Macek et al., 2007
- GlnA Levine et al., 2007
- GlyA Levine et al., 2007 Eymannet al., 2007
- GroEL Levine et al., 2007 Eymannet al., 2007
- GtaB Levine et al., 2007
- GuaB Eymannet al., 2007
- Icd Levine et al., 2007 Eymannet al., 2007
- MetE Eymannet al., 2007
- PdhD Eymannet al., 2007
- PdxS Levine et al., 2007 Eymannet al., 2007
- PgcA Levine et al., 2007 Eymannet al., 2007
- PstS Levine et al., 2007
- Pta Macek et al., 2007
- RocA Macek et al., 2007
- SdhA Levine et al., 2007 Eymannet al., 2007
- SucD Macek et al., 2007
- ThiG Eymannet al., 2007
- Tig Levine et al., 2007
- Tkt Levine et al., 2007
- TufA Levine et al., 2007 Eymannet al., 2007
- YerB Macek et al., 2007
- YfiY Macek et al., 2007
- YfjR Levine et al., 2007
- YfnI Macek et al., 2007
- YhfK Levine et al., 2007
- YoxD Levine et al., 2007
- YsnF Levine et al., 2007
- YtaG Levine et al., 2007
- YtxJ Macek et al., 2007
- SufC Levine et al., 2007
- WapI Macek et al., 2007
Original papers on the B. subtilis phosphoproteome
Vaishnavi Ravikumar, Lei Shi, Karsten Krug, Abderahmane Derouiche, Carsten Jers, Charlotte Cousin, Ahasanul Kobir, Ivan Mijakovic, Boris Macek
Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC.
Mol Cell Proteomics: 2014, 13(8);1965-78
[PubMed:24390483]
[WorldCat.org]
[DOI]
(I p)
Andreas Schmidt, Débora Broch Trentini, Silvia Spiess, Jakob Fuhrmann, Gustav Ammerer, Karl Mechtler, Tim Clausen
Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response.
Mol Cell Proteomics: 2014, 13(2);537-50
[PubMed:24263382]
[WorldCat.org]
[DOI]
(I p)
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
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
