Reaction participants Show >> << Hide
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N6-(2-hydroxyisobutanoyl)-L-lysyl-[protein]
Identifier
RHEA-COMP:15921
Reactive part
help_outline
- Name help_outline N6-(2-hydroxyisobutanoyl)-L-lysine residue Identifier CHEBI:144968 Charge 0 Formula C10H18N2O3 SMILEShelp_outline C(*)([C@@H](N*)CCCCNC(C(O)(C)C)=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2-hydroxy-2-methylpropanoate Identifier CHEBI:19641 Charge -1 Formula C4H7O3 InChIKeyhelp_outline BWLBGMIXKSTLSX-UHFFFAOYSA-M SMILEShelp_outline CC(C)(O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-lysyl-[protein]
Identifier
RHEA-COMP:9752
Reactive part
help_outline
- Name help_outline L-lysine residue Identifier CHEBI:29969 Charge 1 Formula C6H13N2O SMILEShelp_outline C([C@@H](C(*)=O)N*)CCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 134 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:69176 | RHEA:69177 | RHEA:69178 | RHEA:69179 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| Gene Ontology help_outline |
Publications
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Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway.
Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J., Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.
Short-chain fatty acids and their corresponding acyl-CoAs sit at the crossroads of metabolic pathways and play important roles in diverse cellular processes. They are also precursors for protein post-translational lysine acylation modifications. A noteworthy example is the newly identified lysine ... >> More
Short-chain fatty acids and their corresponding acyl-CoAs sit at the crossroads of metabolic pathways and play important roles in diverse cellular processes. They are also precursors for protein post-translational lysine acylation modifications. A noteworthy example is the newly identified lysine 2-hydroxyisobutyrylation (K<sub>hib</sub>) that is derived from 2-hydroxyisobutyrate and 2-hydroxyisobutyryl-CoA. Histone K<sub>hib</sub> has been shown to be associated with active gene expression in spermatogenic cells. However, the key elements that regulate this post-translational lysine acylation pathway remain unknown. This has hindered characterization of the mechanisms by which this modification exerts its biological functions. Here we show that Esa1p in budding yeast and its homologue Tip60 in human could add K<sub>hib</sub> to substrate proteins both in vitro and in vivo. In addition, we have identified HDAC2 and HDAC3 as the major enzymes to remove K<sub>hib</sub>. Moreover, we report the first global profiling of K<sub>hib</sub> proteome in mammalian cells, identifying 6 548 K<sub>hib</sub> sites on 1 725 substrate proteins. Our study has thus discovered both the "writers" and "erasers" for histone K<sub>hib</sub> marks, and major K<sub>hib</sub> protein substrates. These results not only illustrate the landscape of this new lysine acylation pathway, but also open new avenues for studying diverse functions of cellular metabolites associated with this pathway. << Less
Cell Res. 28:111-125(2018) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.