Reaction participants Show >> << Hide
- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,280 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-seryl-[protein]
Identifier
RHEA-COMP:9863
Reactive part
help_outline
- Name help_outline L-serine residue Identifier CHEBI:29999 Charge 0 Formula C3H5NO2 SMILEShelp_outline C([C@H](CO)N*)(=O)* 2D coordinates Mol file for the small molecule Search links Involved in 72 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
3-O-(5'-adenylyl)-L-seryl-[protein]
Identifier
RHEA-COMP:15073
Reactive part
help_outline
- Name help_outline 3-O-adenylyl-L-serine residue Identifier CHEBI:142516 Charge -1 Formula C13H16N6O8P SMILEShelp_outline NC1=NC=NC2=C1N=CN2[C@@H]3O[C@H](COP(=O)(OC[C@H](N*)C(*)=O)[O-])[C@@H](O)[C@H]3O 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 diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,129 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:58120 | RHEA:58121 | RHEA:58122 | RHEA:58123 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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| EC numbers help_outline |
Publications
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Protein AMPylation by an Evolutionarily Conserved Pseudokinase.
Sreelatha A., Yee S.S., Lopez V.A., Park B.C., Kinch L.N., Pilch S., Servage K.A., Zhang J., Jiou J., Karasiewicz-Urbanska M., Lobocka M., Grishin N.V., Orth K., Kucharczyk R., Pawlowski K., Tomchick D.R., Tagliabracci V.S.
Approximately 10% of human protein kinases are believed to be inactive and named pseudokinases because they lack residues required for catalysis. Here, we show that the highly conserved pseudokinase selenoprotein-O (SelO) transfers AMP from ATP to Ser, Thr, and Tyr residues on protein substrates ( ... >> More
Approximately 10% of human protein kinases are believed to be inactive and named pseudokinases because they lack residues required for catalysis. Here, we show that the highly conserved pseudokinase selenoprotein-O (SelO) transfers AMP from ATP to Ser, Thr, and Tyr residues on protein substrates (AMPylation), uncovering a previously unrecognized activity for a member of the protein kinase superfamily. The crystal structure of a SelO homolog reveals a protein kinase-like fold with ATP flipped in the active site, thus providing a structural basis for catalysis. SelO pseudokinases localize to the mitochondria and AMPylate proteins involved in redox homeostasis. Consequently, SelO activity is necessary for the proper cellular response to oxidative stress. Our results suggest that AMPylation may be a more widespread post-translational modification than previously appreciated and that pseudokinases should be analyzed for alternative transferase activities. << Less
Cell 175:809-821(2018) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.