Enzymes
| UniProtKB help_outline | 844 proteins |
| GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
- Name help_outline 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate Identifier CHEBI:58628 (Beilstein: 7970764) help_outline Charge -13 Formula C6H6O27P7 InChIKeyhelp_outline UPHPWXPNZIOZJL-KXXVROSKSA-A SMILEShelp_outline [O-]P([O-])(=O)O[C@@H]1[C@H](OP([O-])([O-])=O)[C@@H](OP([O-])([O-])=O)[C@H](OP([O-])(=O)OP([O-])([O-])=O)[C@@H](OP([O-])([O-])=O)[C@@H]1OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
O-phospho-L-seryl-[protein]
Identifier
RHEA-COMP:11604
Reactive part
help_outline
- Name help_outline O-phospho-L-serine residue Identifier CHEBI:83421 Charge -2 Formula C3H4NO5P SMILEShelp_outline [O-]P([O-])(=O)OC[C@H](N-*)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
O-diphospho-L-seryl-[protein]
Identifier
RHEA-COMP:16509
Reactive part
help_outline
- Name help_outline O-diphospho-L-serine residue Identifier CHEBI:149682 Charge -3 Formula C3H4NO8P2 SMILEShelp_outline C(*)(=O)[C@H](COP(OP([O-])(=O)[O-])(=O)[O-])N* 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1D-myo-inositol hexakisphosphate Identifier CHEBI:58130 (Beilstein: 3886124) help_outline Charge -12 Formula C6H6O24P6 InChIKeyhelp_outline IMQLKJBTEOYOSI-GPIVLXJGSA-B SMILEShelp_outline [O-]P([O-])(=O)O[C@@H]1[C@H](OP([O-])([O-])=O)[C@H](OP([O-])([O-])=O)[C@@H](OP([O-])([O-])=O)[C@H](OP([O-])([O-])=O)[C@H]1OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:64104 | RHEA:64105 | RHEA:64106 | RHEA:64107 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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| Gene Ontology help_outline |
Publications
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Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event.
Bhandari R., Saiardi A., Ahmadibeni Y., Snowman A.M., Resnick A.C., Kristiansen T.Z., Molina H., Pandey A., Werner J.K. Jr., Juluri K.R., Xu Y., Prestwich G.D., Parang K., Snyder S.H.
In a previous study, we showed that the inositol pyrophosphate diphosphoinositol pentakisphosphate (IP(7)) physiologically phosphorylates mammalian and yeast proteins. We now report that this phosphate transfer reflects pyrophosphorylation. Thus, proteins must be prephosphorylated by ATP to prime ... >> More
In a previous study, we showed that the inositol pyrophosphate diphosphoinositol pentakisphosphate (IP(7)) physiologically phosphorylates mammalian and yeast proteins. We now report that this phosphate transfer reflects pyrophosphorylation. Thus, proteins must be prephosphorylated by ATP to prime them for IP(7) phosphorylation. IP(7) phosphorylates synthetic phosphopeptides but not if their phosphates have been masked by methylation or pyrophosphorylation. Moreover, IP(7) phosphorylated peptides are more acid-labile and more resistant to phosphatases than ATP phosphorylated peptides, indicating a different type of phosphate bond. Pyrophosphorylation may represent a novel mode of signaling to proteins. << Less
Proc. Natl. Acad. Sci. U.S.A. 104:15305-15310(2007) [PubMed] [EuropePMC]
Comments
This reaction can occur spontaneously.