Enzymes
| UniProtKB help_outline | 1,096 proteins |
| GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
L-tyrosyl-[protein]
Identifier
RHEA-COMP:10136
Reactive part
help_outline
- Name help_outline L-tyrosine residue Identifier CHEBI:46858 Charge 0 Formula C9H9NO2 SMILEShelp_outline O=C(*)[C@@H](N*)CC=1C=CC(=CC1)O 2D coordinates Mol file for the small molecule Search links Involved in 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,142 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline nicotinamide Identifier CHEBI:17154 (Beilstein: 383619; CAS: 98-92-0) help_outline Charge 0 Formula C6H6N2O InChIKeyhelp_outline DFPAKSUCGFBDDF-UHFFFAOYSA-N SMILEShelp_outline NC(=O)c1cccnc1 2D coordinates Mol file for the small molecule Search links Involved in 60 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
O-(ADP-D-ribosyl)-L-tyrosyl-[protein]
Identifier
RHEA-COMP:15092
Reactive part
help_outline
- Name help_outline O-(ADP-D-ribosyl)-L-tyrosine residue Identifier CHEBI:142557 Charge -2 Formula C24H28N6O15P2 SMILEShelp_outline N1(C2=C(C(=NC=N2)N)N=C1)[C@@H]3O[C@H](COP(OP(OC[C@H]4OC(OC=5C=CC(=CC5)C[C@@H](C(*)=O)N*)[C@@H]([C@@H]4O)O)(=O)[O-])(=O)[O-])[C@H]([C@H]3O)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
Cross-references
| RHEA:58236 | RHEA:58237 | RHEA:58238 | RHEA:58239 | |
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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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Interplay of histone marks with serine ADP-ribosylation.
Bartlett E., Bonfiglio J.J., Prokhorova E., Colby T., Zobel F., Ahel I., Matic I.
Serine ADP-ribosylation (Ser-ADPr) is a recently discovered protein modification that is catalyzed by PARP1 and PARP2 when in complex with the eponymous histone PARylation factor 1 (HPF1). In addition to numerous other targets, core histone tails are primary acceptors of Ser-ADPr in the DNA damage ... >> More
Serine ADP-ribosylation (Ser-ADPr) is a recently discovered protein modification that is catalyzed by PARP1 and PARP2 when in complex with the eponymous histone PARylation factor 1 (HPF1). In addition to numerous other targets, core histone tails are primary acceptors of Ser-ADPr in the DNA damage response. Here, we show that specific canonical histone marks interfere with Ser-ADPr of neighboring residues and vice versa. Most notably, acetylation, but not methylation of H3K9, is mutually exclusive with ADPr of H3S10 in vitro and in vivo. We also broaden the O-linked ADPr spectrum by providing evidence for tyrosine ADPr on HPF1 and other proteins. Finally, we facilitate wider investigations into the interplay of histone marks with Ser-ADPr by introducing a simple approach for profiling posttranslationally modified peptides. Our findings implicate Ser-ADPr as a dynamic addition to the complex interplay of modifications that shape the histone code. << Less
Cell Rep. 24:3488-3502(2018) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.