Pub. Date : 2019 Dec 25
PMID : 31881804
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | O-GlcNAc-Modification of NSL3 at Thr755 Site Maintains the Holoenzyme Activity of MOF/NSL Histone Acetyltransfease Complex. | peptide T amide | KAT8 regulatory NSL complex subunit 3 | Homo sapiens |
| 2 | Here, we present evidence from biochemical experiments arguing that O-GlcNAcylation of NSL3 at Thr755 is tightly associated with holoenzyme activity of the MOF/NSL complex. | peptide T amide | KAT8 regulatory NSL complex subunit 3 | Homo sapiens |
| 3 | Using in vitro O-GlcNAc-transferase assays combined with mass spectrometry, we suppose that the residue Thr755 on NSL3 C-terminus is the major site O-GlcNAc-modified by OGT1. | peptide T amide | KAT8 regulatory NSL complex subunit 3 | Homo sapiens |
| 4 | Furthermore, O-GlcNAcylation of NSL3 Thr755 site regulates the histone H4 acetylation levels at lysine 5, 8, and 16, suggesting that the O-GlcNAcylation of NSL3 at Thr755 is required for maintaining the integrity and holoenzyme activity of the MOF/NSL complex. | peptide T amide | KAT8 regulatory NSL complex subunit 3 | Homo sapiens |
| 5 | Furthermore, O-GlcNAcylation of NSL3 Thr755 site regulates the histone H4 acetylation levels at lysine 5, 8, and 16, suggesting that the O-GlcNAcylation of NSL3 at Thr755 is required for maintaining the integrity and holoenzyme activity of the MOF/NSL complex. | peptide T amide | KAT8 regulatory NSL complex subunit 3 | Homo sapiens |