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Table 1 Histone post-translational modification and variant-specific turnover.1

From: Global turnover of histone post-translational modifications and variants in human cells

Peptide2-4,6 Turnover, per day5 Peptide2-4,6 Turnover, per day5
H3K65un 0.6230 ± 0.0001 H3K27unK36un 1.9213 ± 0.0001
H3K122un 0.6400 ± 0.0001 H3K27me1 1.1391 ± 0.0000
H3K4un 0.6638 ± 0.0001 H3K36me1 1.6913 ± 0.0000
H3K4me1 0.4863 ± 0.0000 H3K27me2 0.8207 ± 0.0000
H3K56un 0.6378 ± 0.0000 H3K36me2 1.0892 ± 0.0000
H3K56ac1 2.4335 ± 0.0014 H3K27me3 0.5148 ± 0.0000
H3K18K23un 0.6806 ± 0.0001 H3K27me1K36me2 0.7540 ± 0.0000
H3K18/K23ac14 0.8793 ± 0.0000 H3K27me2K36me1 0.6210 ± 0.0001
H3K18ac1K23ac1 1.1446 ± 0.0001 H3K27me2K36me2 0.4537 ± 0.0000
H3K79un 0.6785 ± 0.0001 H3K27me3K36me1 0.3681 ± 0.0000
H3K79me1 0.4526 ± 0.0000 H3K27me1K36me3 0.4547 ± 0.0000
H3K79me2 0.3841 ± 0.0000 H4K5K8K12K16un 0.6495 ± 0.0000
H3K9unK14un 1.1335 ± 0.0001 H4K5/K8/K12/K16ac14 0.7773 ± 0.0000
H3K9me1 0.7967 ± 0.0001 H4K5/K8/K12/K16ac24 0.9819 ± 0.0000
H3K9me2 0.6620 ± 0.0000 H4K5/K8/K12/K16ac34 1.0423 ± 0.0000
H3K9me3 0.4652 ± 0.0000 H4K5K8K12K16ac4 1.0056 ± 0.0000
H3K9/K14ac14 1.3393 ± 0.0001 H4K20un 2.2672 ± 0.0005
H3K9me1K14ac1 0.9205 ± 0.0000 H4K20me1 1.3340 ± 0.0002
H3K9me2K14ac1 0.6454 ± 0.0000 H4K20me2 0.5177 ± 0.0000
H1.4K26un 0.7721 ± 0.0000 H4K20me3 0.3307 ± 0.0000
H4K31un 0.6182 ± 0.0001 H2A: ATIAGGGVIPHIHK 0.8016 ± 0.0001
H2A: GKQGGKAR 0.7222 ± 0.0000 H2A: NDEELNKLLGR 0.7135 ± 0.0000
H2A: KGNYAER 0.6311 ± 0.0000 H2B: LAHYNKR 0.6448 ± 0.0000
H2A: KGNYSER 0.7215 ± 0.0001 H2B: PEPAK 0.6293 ± 0.0000
  1. 1Absolute turnover values (mean ± standard deviation per day) extrapolated from the relative distribution of the isotopically labeled bulk H3, H4 and H1.4 peptides with a particular post-translational modification.
  2. 2me = methyl
  3. 3ac = acetyl
  4. 4The H2A and H2B turnover values are averages of all histone variants containing the specific peptide sequence.
  5. 5The model was iterated 200 times for each individual peptide, where the average and standard deviation were taken for parameters within 105% of the determined optimum parameter.
  6. 6For H3K18/K23ac1, H3K9/K14ac1, and H4K5/K8/K12/K16ac1, ac2 and ac3, the localization of the acetyl(s) on the multiple lysines was not determined.
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