Difference between revisions of "Phosphoproteins"
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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. | 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. | ||
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| + | {{CategoryTree2 | ||
| + | |Parents= | ||
| + | * 6. [[Groups of genes]] | ||
| + | |Neighbours= | ||
| + | * 6.1. [[Ribosomal RNA]] | ||
| + | * 6.2. [[tRNA]] | ||
| + | * 6.3. [[ncRNA]] | ||
| + | * 6.4. [[Short peptides]] | ||
| + | * 6.5. [[GTP-binding proteins]] | ||
| + | * 6.6. [[Phosphoproteins]] | ||
| + | * 6.7. [[Universally conserved proteins]] | ||
| + | * 6.8. [[Membrane proteins]] | ||
| + | * 6.9. [[Essential genes]] | ||
| + | * 6.10. [[Pseudogenes]] | ||
| + | * 6.11. [[Poorly characterized/ putative enzymes]] | ||
| + | * 6.12. [[Proteins of unknown function]] | ||
| + | |Related= | ||
| + | none | ||
| + | |}} | ||
| + | |||
| + | <br/><br/><br/><br/><br/> | ||
| + | |||
| + | __TOC__ | ||
==Phosphoproteins in ''B. subtilis''== | ==Phosphoproteins in ''B. subtilis''== | ||
Revision as of 12:20, 15 November 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.
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| Neighbouring categories |
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| Related categories |
none |
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 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
- 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
- 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
- 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
- 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
- YwfI Macek et al., 2007
- YwjH Macek et al., 2007
- YwrJ Soufi et al., 2010
Phosphorylation on a Thr residue
- LtaS
- AroA Eymannet al., 2007
- 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
- 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
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
- 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
- YvyG 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
- GpsB Macek et 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
- YxxG Macek et al., 2007
- Zur Levine et al., 2007
Related Lists
- two-component systems
- PTS
- PRD-containing transcription factors
- phosphorelay
- response regulator aspartate phosphatases
- protein kinases and phosphatases
Original papers on the B. subtilis phosphoproteome
Reviews
