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http://purl.uniprot.org/citations/34625544http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34625544http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34625544http://www.w3.org/2000/01/rdf-schema#comment"Despite the involvement of Poly(ADP-ribose) polymerase-1 (PARP1) in many important biological pathways, the target residues of PARP1-mediated ADP-ribosylation remain ambiguous. To explicate the ADP-ribosylation regulome, we analyze human cells depleted for key regulators of PARP1 activity, histone PARylation factor 1 (HPF1) and ADP-ribosylhydrolase 3 (ARH3). Using quantitative proteomics, we characterize 1,596 ADP-ribosylation sites, displaying up to 1000-fold regulation across the investigated knockout cells. We find that HPF1 and ARH3 inversely and homogenously regulate the serine ADP-ribosylome on a proteome-wide scale with consistent adherence to lysine-serine-motifs, suggesting that targeting is independent of HPF1 and ARH3. Notably, we do not detect an HPF1-dependent target residue switch from serine to glutamate/aspartate under the investigated conditions. Our data support the notion that serine ADP-ribosylation mainly exists as mono-ADP-ribosylation in cells, and reveal a remarkable degree of histone co-modification with serine ADP-ribosylation and other post-translational modifications."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.org/dc/terms/identifier"doi:10.1038/s41467-021-26172-4"xsd:string
http://purl.uniprot.org/citations/34625544http://purl.org/dc/terms/identifier"doi:10.1038/s41467-021-26172-4"xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Ahel I."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Ahel I."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Hendriks I.A."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Hendriks I.A."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Nielsen M.L."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Nielsen M.L."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Zhu K."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Zhu K."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Ahel D."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Ahel D."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Buch-Larsen S.C."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Buch-Larsen S.C."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Elsborg J.D."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Elsborg J.D."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Lukas C."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Lukas C."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Prokhorova E."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Prokhorova E."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Rebak A.K.L.F.S."xsd:string
http://purl.uniprot.org/citations/34625544http://purl.uniprot.org/core/author"Rebak A.K.L.F.S."xsd:string