2.3.1.48: histone acetyltransferase
This is an abbreviated version!
For detailed information about histone acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.48
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2.3.1.48
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rhythm
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oscillation
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suprachiasmatic
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chromatin
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entrain
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night
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scn
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sleep
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melatonin
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drosophila
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diurnal
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pacemaker
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locomotor
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light-dark
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nuclei
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deacetylases
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pineal
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morning
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photoperiodic
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retinal
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draw
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hypothalamus
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hdacs
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light-induced
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melanogaster
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photoreceptors
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noise
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bayesian
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nocturnal
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evening
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daytime
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deacetylation
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coherent
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co-activator
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oscillatory
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dementia
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transactivation
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flies
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neuropeptide
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wake
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schedule
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24-hour
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pulses
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circuit
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medicine
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lengthen
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molecular biology
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trichostatin
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mood
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verbal
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neuropsychological
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drug development
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tick
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analysis
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pharmacology
- 2.3.1.48
- rhythm
-
oscillation
-
suprachiasmatic
- chromatin
-
entrain
-
night
- scn
- sleep
- melatonin
- drosophila
-
diurnal
-
pacemaker
-
locomotor
-
light-dark
- nuclei
- deacetylases
-
pineal
-
morning
-
photoperiodic
- retinal
-
draw
- hypothalamus
- hdacs
-
light-induced
- melanogaster
- photoreceptors
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noise
-
bayesian
-
nocturnal
-
evening
-
daytime
-
deacetylation
-
coherent
-
co-activator
-
oscillatory
- dementia
-
transactivation
- flies
-
neuropeptide
-
wake
-
schedule
-
24-hour
-
pulses
-
circuit
- medicine
-
lengthen
- molecular biology
-
trichostatin
-
mood
-
verbal
-
neuropsychological
- drug development
- tick
- analysis
- pharmacology
Reaction
Synonyms
AAPatA, acetyltransferase, histone, Ada2/Ada3/Gcn5 complex, AIB1, amino acid sensing acetyltransferase, AmiPatA, Amir 5672, ARD1, ARD1 acetyltransferase, arginine methyltransferase A, arginine methyltransferase B, arrest defective 1, arrest defective protein 1 acetyltransferase, At3g14980, ATAC2, ATase1, ATase2, cAMP-regulated protein lysine acetyltransferase, Cbp, CBP histone acetyltransferase, CBP/p300, chameau, circadian locomoter output cycles protein kaput, CLOCK, CREB binding protein, CREB-binding protein, CREBBP, east1, ELO3, ELONGATA3, elongator protein 3, ELP3, enhancer-of-asymmetric leaves-two1, Enok, EP300, Esa1, factor acetyltransferase, FAT, Gcn5, GCN5 family KAT, Gcn5 HAT, GCN5 lysine acetyltransferase, GCN5 N acetyltransferase 5, Gcn5 related N-acetyltransferase, GCN5-like acetyltransferase, GCN5-like enzyme, GCN5-related N-acetyltransferase, Gcn5/PCAF histone acetyltransferase, GCN5b, GCN5L2, general control non-derepressible 5, general control non-repressed protein5, general control nonderepressible 5, general control nonrepressed-protein 5, general control of amino acid synthesis 5, GNAT, GNAT-related histone acetyltransferase complex, GTF3C4, H4 lysine acetyltransferase, HAC1, HAG1, HAG3, HAG4, HAG5, HAM1, HAM2, hARD1, HAT, HAT-B, HAT-B complex, Hat1, Hat1p, Hat2, HatB3.I, HBO1, histone (H4 K16) acetyltransferase, histone acetokinase, histone acetyl transferase, histone acetylase, histone acetyltransferase, histone acetyltransferase 1, histone acetyltransferase AtGCN5, histone acetyltransferase B, histone acetyltransferase Tip60, histone acetyltransferase-1, histone acetyltransferases, histone H3 acetyltransferase, histone H4 acetyltransferase, histone H4 lysine 16 acetyltransferase, histone transacetylase, histone/protein lysine acetyltransferase, HIV-1 Tat-interactive protein, hMOF, Hpa2, Hpa3, human acetylase binding to ORC1, Idm1, K (lysine) acetyltransferase 8, K(lysine) acetyltransferase 8, KAT, KAT10, KAT11, KAT12, KAT13A, KAT13B, KAT13C, KAT13D, KAT2, Kat2A, KAT2A/GCN5, Kat2b, KAT3A, KAT3B, KAT4, KAT5, KAT6, KAT6A, KAT6B, KAT7, KAT8, KAT9, Lsy-12, lysine acetyltransferase, lysine acetyltransferase 2, lysine acetyltransferase 2A, lysine acetyltransferase 2B, lysine acetyltransferase 5, lysine acetyltransferase 8, lysine acetyltransferase complex, lysine acetyltransferase p300, lysine acetyltransferases, lysine-acetyltransferase, Mof, monocytic leukemia zinc finger, monocytic leukemia zinc finger protein, More, Morf, MORF histone acetyltransferase, MOZ, MOZ histone acetyltransferase, Moz related factor, Mst1, MtPat, Myb-binding protein 1A, MYBBP1A, MYST, MYST protein lysine acetyltransferase, MYST-related histone acetyltransferase complex, MYST1, MYST2, MYST3, MYST4, N(alpha)-acetyltransferase 10, N-acetyltransferase, N-terminal acetyltransferase, NAA10, NAT, NAT4, NCoA-1, NCoA-3, NCOAT, Nepsilon-lysine acetyltransferase, NuA4, NuA4 histone acetyltransferase, nuclear cytoplasmicO-GlcNAcase and acetyltransferase, nuclear receptor coactivator 1, nuclear receptor coactivator 3, nucleosome-histone acetyltransferase, Nut1, p/CAF, P/CAF histone acetyltransferase, p160, p300, p300 HAT, p300 histone acetyltransferase, p300/CBP, p300/CBP associated factor, p300/CBP histone acetyltransferase, P300/CBP-associated factor, p300/CBP-associated factor (pCAF), p300HAT, PA4534, Pat, PCAF, PCAF histone acetyltransferase, PF11_0192, PfGCN5, PfGCN5 HAT, Piccolo NuA4 complex, protein acetyl-transferase, protein acetyltransferase, Qkf, regulator of Ty1 transposition protein 109, RmtA, RmtB, RPD3, Rtt109, Rv0998, SAS complex, Sas2, Sas3, SRC1, SRC3, Sven 0867, SvePatA, TAF, TAF1, Tat interacting protein of 60 kDa, Tat-interactive protein, 60 kDa, TBP1, TFIIIC90, tGCN5, TgGCN5b, TgMYST-B, Tip60, tumor suppressor histone H3 lysine 23 acetyltransferase, type B histone acetyltransferase, YfmK, zMoz
ECTree
2.3.1.48 histone acetyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.3.1.48 - histone acetyltransferase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3 acetyl-CoA + histone H4
3 CoA + triacetylhistone H4
-
enzyme form B
mono-, di- and triacetylated products
?
3-azidopropionyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-3-azidopropionyl-L-lysine
3-azidopropionyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-3-azidopropionyl-L-lysine
4 acetyl-CoA + histone H4
4 CoA + tetraacetylhistone H4
-
-
NuA4 randomly acetylates free and nucleosomal H4, with a small preference for lysines 5, 8, and 12 over 16
-
?
4-pentynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-4-pentynoyl-L-lysine
4-pentynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-4-pentynoyl-L-lysine
5-hexynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-5-hexynoyl-L-lysine
5-hexynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-5-hexynoyl-L-lysine
6-heptynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-6-heptynoyl-L-lysine
6-heptynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-6-heptynoyl-L-lysine
acetyl-CoA + 1,6-hexanediamine
?
-
enzyme form A shows low activity , B not
-
-
?
acetyl-CoA + beta-site amyloid precursor protein-cleaving enzyme 1
CoA + acetylated beta-site amyloid precursor protein-cleaving enzyme 1
acetyl-CoA + biotinylated histone H3 (1-21) peptide
CoA + acetylated biotinylated histone H3 (1-21) peptide
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-
-
?
acetyl-CoA + histone H
CoA + acetylhistone H
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histone acetyltransferase AtGCN5 is required to regulate the floral meristem activity through the WUS/AG pathway
-
-
?
acetyl-CoA + histone H2A
Nalpha-acetylated-histone H2A + CoA
-
-
-
?
acetyl-CoA + histone H3
peptide CoA + acetylhistone H3 peptide
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preferred substrate, the N-terminal substrate region plays an importsant role in enhanced affinity of the Gcn5/PCAF proteins for histone H3
-
-
?
acetyl-CoA + histone H3 N-terminal tail
CoA + acetylated histone H3 N-terminal tail
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50 mM Tris-HCl, pH 8.0, 30°C
-
-
?
acetyl-CoA + histone H3 peptide
CoA + actylhistone H3
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residues 1-21 of human histone H3
-
-
?
acetyl-CoA + histone H3 tail peptide
CoA + acetylhistone H3 peptide
H3 peptide substrate, amino acid sequence ARTKQTARKSTGGKAPRKQL
-
-
?
acetyl-CoA + histone H3-peptide p19
CoA + acetylhistone H3 -peptide p19
-
-
-
-
?
acetyl-CoA + histone H3-peptide p19
CoA + acetylhistone H3-peptide p19
-
-
-
-
?
acetyl-CoA + histone H3-peptide p27
CoA + acetylhistone H3 -peptide p27
-
-
-
-
?
acetyl-CoA + histone H4
Nalpha-acetylated-histone H4 + CoA
acetylation of N-terminal Ser
-
-
?
acetyl-CoA + histone H4 peptide
CoA + acetylhistone H4 peptide
a synthetic peptide corresponding to the first 20 amino acids of the histone H4 N-terminus
-
-
?
acetyl-CoA + histone H4 peptide
CoA + acetylpeptide of histone H4
residues 1-20 of histone H4
-
-
?
acetyl-CoA + histone H4 peptide
CoA + actylhistone H4
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residues 2-24 of human histone H4
-
-
?
acetyl-CoA + N-terminal L-lysyl-[beta-catenin]
CoA + H+ + N-terminal Nalpha-acetyl-lysyl-[beta-catenin]
-
-
-
ir
acetyl-CoA + N-terminal L-lysyl-[Hsp70]
CoA + H+ + N-terminal Nalpha-acetyl-L-lysyl-[Hsp70]
acetyl-CoA + NF-kB p65
CoA + acetyl-NF-kB p65
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acetylation of the subunit at Lys310 by p300 or PCAF
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-
?
acetyl-CoA + non-histone chromatin high-mobility group protein
CoA + acetylated non-histone chromatin high-mobility group protein
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or chymotryptic peptides of
-
-
?
acetyl-CoA + peptide H4-20
CoA + acetylpeptide H4-20
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histone H4-derived peptide substrate
-
-
?
acetyl-CoA + poly-L-lysine
CoA + N6-acetyllysine
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enzyme form A, not enzyme form B1 and B2
-
?
acetyl-CoA + transcription factor TFIIE
CoA + acetylated transcription factor TFIIE
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substrate is a basal transcription factor
-
-
?
acetyl-CoA + transcription factor TFIIF
CoA + acetylated transcription factor TFIIF
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substrate is a basal transcription factor
-
-
?
acetyl-CoA + VPAFKPGK
CoA + VPAFKPGKac
histone-like protein HBsu peptide
-
-
?
acetyl-CoA + [AuA]-L-lysine125
CoA + [AuA]-N6-acetyl-L-lysine125
lysine residues at positions 75 and 125 of aurora kinase A (AuA) are acetylated by ARD1, mutational analysis with AUA mutant substrates, overview
-
-
?
acetyl-CoA + [AuA]-L-lysine75
CoA + [AuA]-N6-acetyl-L-lysine75
lysine residues at positions 75 and 125 of aurora kinase A (AuA) are acetylated by ARD1, mutational analysis with AUA mutant substrates, overview
-
-
?
acetyl-CoA + [beta-catenin]-L-lysine
CoA + [beta-catenin]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [CDC6]-L-lysine
CoA + [CDC6]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [connexin 43]-L-lysine
CoA + [connexin 43]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [Foxo1]-L-lysine
CoA + [Foxo1]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H2B]-L-lysine
CoA + [histone H2B]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H2B]-L-lysine12
CoA + [histone H2B]-N6-acetyl-L-lysine12
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H2B]-L-lysine15
CoA + [histone H2B]-N6-acetyl-L-lysine15
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine13
CoA + [histone H3]-N6-acetyl-L-lysine13
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine20
CoA + [histone H3]-N6-acetyl-L-lysine20
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine79
CoA + [histone H3]-N6-acetyl-L-lysine79
-
-
-
-
ir
acetyl-CoA + [histone H4]-L-lysin16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-acetyl-L-lysine
acetyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-acetyl-L-lysine
acetyl-CoA + [Hsp70]-L-lysine
CoA + [Hsp70]-N6-acetyl-L-lysine
difference in the acetylation of Hsp70 with or without rhARD1 can be observed at low ratio of enzyme: substrate up to 1:25 but not at that of higher ratio over 1:25. The enzyme targets Lys77 of Hsp70, the hARD1/NAA10-mediated catalysis of Hsp70 is abolished with K77R mutation in Hsp70
-
-
?
acetyl-CoA + [NFkappaB]-L-lysine
CoA + [NFkappaB]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [p27]-L-lysine
CoA + [p27]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [PGC-1alpha]-L-lysine
CoA + [PGC-1alpha]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [PGC-1]-L-lysine
CoA + [PGC-1]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [PTEN]-L-lysine
CoA + [PTEN]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
acetylation of the oncosuppressor protein PTEN on two lysine residues (Lys125 and Lys128)
-
-
?
acetyl-CoA + [STAT3]-L-lysine
CoA + [STAT3]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
activated RNA polymerase II transcriptional coactivator p15 + 4-pentynoyl-CoA
?
-
-
-
-
?
histone H2A + acetyl-CoA
acetyl-histone H2A + CoA
-
acetylation of the tail of the histone, the enzyme is organized in the NuA4 subcomplex acting on the nucleosome, overview
-
-
?
histone H2B + acetyl-CoA
acetyl-histone H2B + CoA
-
acetylation of the tail of the histone, the enzyme is organized in the catalytic Ada2/Ada3/Gcn5 subcomplex of SAGA acting on the nucleosome, overview
-
-
?
histone H3 tail peptide + acetyl-CoA
acetyl-histone H3 tail peptide + CoA
-
-
-
-
?
histone H4 N-terminal peptide + acetyl-CoA
acetyl-histone H4 N-terminal peptide + CoA
N-terminal peptide of histone H4 of different length and sequence, prepared in HeLa cell extract, overview, acetylation by Hat1 requires positively charged amino acids at positions 8 and 16 of the H4 tail, substituting glutamine for lysine at Lys8 and Lys16 dramatically reduces the ability of yHat1p to acetylate the H4 tail peptide, phosphorylation of Ser1 also reduces the acetylation of H4 peptides
-
-
?
isoform 1 of DNA polymerase zeta catalytic subunit + 4-pentynoyl-CoA
?
-
-
-
-
?
isoform 1 of transcription factor BTF3 + 4-pentynoyl-CoA
?
-
-
-
-
?
piccoloNuA4 peptide + acetyl-CoA
acetyl-piccoloNuA4 peptide + CoA
the peptide is part of the physiologic enzme complex, overview
-
-
?
piccoloNuA4 peptide + propionyl-CoA
propionyl-piccoloNuA4 peptide + CoA
-
-
-
?
promyelotic leukemia zinc finger gene + acetyl-CoA
acetylated promyelotic leukemia zinc finger gene + CoA
2 acetyl-CoA + histone H4
2 CoA + diacetylhistone H4
-
-
mono-, di- and triacetylated products
?
2 acetyl-CoA + histone H4
2 CoA + diacetylhistone H4
-
enzyme form B
mono- and diacetylated products
?
2 acetyl-CoA + histone H4
2 CoA + diacetylhistone H4
-
enzyme form B
mono- and diacetylated products
?
3-azidopropionyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-3-azidopropionyl-L-lysine
-
-
-
?
3-azidopropionyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-3-azidopropionyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
3-azidopropionyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-3-azidopropionyl-L-lysine
-
-
-
?
3-azidopropionyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-3-azidopropionyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
4-pentynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-4-pentynoyl-L-lysine
-
-
-
?
4-pentynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-4-pentynoyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
4-pentynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-4-pentynoyl-L-lysine
-
-
-
?
4-pentynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-4-pentynoyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
5-hexynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-5-hexynoyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
5-hexynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-5-hexynoyl-L-lysine
very low activity with 5-hexynoyl-CoA
-
-
?
5-hexynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-5-hexynoyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
5-hexynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-5-hexynoyl-L-lysine
very low activity with 5-hexynoyl-CoA
-
-
?
6-heptynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-6-heptynoyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
6-heptynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-6-heptynoyl-L-lysine
very low activity with 6-heptynoyl-CoA
-
-
?
6-heptynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-6-heptynoyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
6-heptynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-6-heptynoyl-L-lysine
very low activity with 6-heptynoyl-CoA
-
-
?
acetyl-CoA + 1,5-pentanediamine
?
-
enzyme form A and B, low activity
-
-
?
acetyl-CoA + AVDSVFDTILDALK
CoA + AVDSVFDTILDALKac
histone-like protein HBsu peptide
-
-
?
acetyl-CoA + AVDSVFDTILDALK
CoA + AVDSVFDTILDALKac
histone-like protein HBsu peptide
-
-
?
acetyl-CoA + beta-site amyloid precursor protein-cleaving enzyme 1
CoA + acetylated beta-site amyloid precursor protein-cleaving enzyme 1
-
-
-
-
?
acetyl-CoA + beta-site amyloid precursor protein-cleaving enzyme 1
CoA + acetylated beta-site amyloid precursor protein-cleaving enzyme 1
-
50 mM Tris-HCl, pH 8.0, 30°C
-
-
?
acetyl-CoA + c-Myc
CoA + acetylated c-Myc
-
acetylation by Tip60 increases c-Myc protein stability in transfected H-1299 human lung carcinoma cells
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
Artemia nauplii
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H1 is a better substrate than H3 or H4
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
important role of the enzyme for chromatin modulating activity
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
enzyme form B nearly exclusively acetylates histones H4 and H2a
formation of N6-acetyllysine as the only acetylation product
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
or chymotryptic peptides of histone
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
most likely involved in acetylation of newly synthesized histones in cytoplasm prior to chromatin assembly
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
in the assay the CoA thiolate is detected by the thiol sensitive fluorescent dye 7-diethylamino-3-(4'-maleimidylphenyl)-4-methylcoumarin
-
?
acetyl-CoA + histone
CoA + acetylhistone
calf thymus and HeLa cell histones
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H1 is not acetylated in vivo
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
involved in chromatin remodeling and DNA repair
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
neutralization of positively charged lysine residues by acetylation lowering the affinity of histone octamers for the negatively charged DNA
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H1 is not acetylated in vivo
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
neutralization of positively charged lysine residues by acetylation lowering the affinity of histone octamers for the negatively charged DNA
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
involved in chromatin remodeling and DNA repair
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
acetylates histones H2A, H3, and H4, but not histone 2B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
the bifunctional enzyme NCOAT, nuclear cytoplasmic O-GlcNacase and acetyltransferase, may be regulated to reduce the state of glycosylation of transcriptional activators while increasing the acetylation of histones to allow for concerted activation of eukaryotic gene transcription
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H2A is a substrate for enzyme form A1
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H2B: poor substrate for enzyme form A2
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
involved in dynamic equilibrium of core histone acetylation
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
pea histones, enzyme form A and B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
chicken erythrocyte histones, enzyme form A and B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
free pea and chicken histones H4, enzyme form B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
acetylation of lysine 5, 8, 12, and 16 of free histone H4 with increasing preference
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
nucleosome-histones, enzyme form A, not enzyme form B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone f1, enzyme form A
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone f2a1, enzyme form B1 and B2
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
nucleosome-histones, enzyme form A and B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H1 poor substrate
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
chicken erythrocyte histones, enzyme form A and B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
Esa1 protein is involved in cell cycle regulation
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
involved in chromatin remodeling and DNA repair
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
neutralization of positively charged lysine residues by acetylation lowering the affinity of histone octamers for the negatively charged DNA
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone acetylation on Lys16 by Sas2
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
chymostatic peptides of histones
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
neutralization of positively charged lysine residues by acetylation lowering the affinity of histone octamers for the negatively charged DNA
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
histone H1 is a better substrate than H3 or H4
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
histone H1 poor substrate
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
acetylation of histone H1 only in vitro
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
histone H1 poor substrate
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
acetylation of histone H1 only in vitro
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
histone H1 poor substrate
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
enzyme form B nearly exclusively acetylates histones H4 and H2a
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
MYST-related histone acetyltransferase complex Tip60
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
acetylation at Lys5 by Tip60
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
histone H2A is a substrate for enzyme form A1
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
NuA4-like protein acetylates histone H4 and H2A
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
NuA4-like protein acetylates histone H4 and H2A
-
?
acetyl-CoA + histone H2B
CoA + acetylhistone H2B
-
GNAT-related histone acetyltransferase complexes STAGA or TFTC
-
-
?
acetyl-CoA + histone H2B
CoA + acetylhistone H2B
-
histone H2B: poor substrate for enzyme form A2
-
?
acetyl-CoA + histone H2B
CoA + acetylhistone H2B
-
histone H2B: preferred substrate of enzyme form A
-
?
acetyl-CoA + histone H2B
CoA + acetylhistone H2B
-
GNAT-related histone acetyltransferase complexes SAGA, ADA or H2B
-
-
?
acetyl-CoA + histone H3
CoA + acetyl-histone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
residues K14, K18, and K23 of H3 are acetylated by domain C1 of isoform Idm1 in vitro
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Gcn5 protein: preferred substrate, acetylation at Lys14
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys9
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys14 of histone H3
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H1 is a better substrate than H3 or H4
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Gcn5 protein: preferred substrate, acetylation at Lys14
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys9, Lys14, Lys18, Lys23, Lys27, Lys36, and Lys37
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Gcn5 protein: preferred substrate, acetylation at Lys14
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Lys14 of histone H3 and a peptide containing Lys14 thereof are the preferred substrates for Gnc5 and PCAF protein, as well as Gnc5 and PCAF catalytic domain
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Lys14 of histone H3 and a peptide containing Lys14 thereof are the preferred substrates for Gnc5 and PCAF protein, as well as Gnc5 and PCAF catalytic domain
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
GNAT-related histone acetyltransferase complexes PCAF, STAGA or TFTC
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
substrate is a H3 peptide
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
the sequence G-K-X-P within histone H3 makes several key contacts within the active site that are conserved in GNAT members including p/CAF
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
acetylation of Lys23
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys4 and Lys9
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
regulation, detailed overview. Acetylation and deacetylation events, in combination with other post-translational protein modifications, generate an NF-kappaB-signaling code and regulate NF-kappaB-dependent gene transcription in an inducer- and promoter-dependent manner, overview
-
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Gcn5 protein: preferred substrate, acetylation at Lys14
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
CBP binds and acetylates histones at neural promoters, and regulates Corpus Callosum development. CBP binds to neuronal and glial promoters and globally promotes histone acetylation in the embryonic cortex, e.g. the beta-actin promoter, overview
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
H4R3 methylation, catalyzed by PRMT1, facilitates beta-globin transcription by regulating histone acetyltransferase binding, and histone H3 and H4 acetylation, overview
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys9 and Lys14
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys9 and Lys14 by PCAF. PCAF binds to dimethyl-Arg3 at histone H4 tails, dimethyl H4R3 provides a binding surface for PCAF and directly enhances histone H3 and H4 acetylation in vitro
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H3 is the preferred substrate of enzyme form A1 and A2
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H3: preferred substrate
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Gcn5 protein: specific for Lys14 of histone H3
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Gcn5 protein: preferred substrate, acetylation at Lys14
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H3: preferred substrate
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H3 preferred substrate of enzyme form A
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
recombinant and native SAS complex acetylates Lys14
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
GNAT-related histone acetyltransferase complexes SAGA, ADA or HAT-A2, MYST-related histone acetyltransferase complex NuA3
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
strong preference for free histones relative to chromatin substrate
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Rtt109 association with distinct histone chaperones directs substrate selection between N-terminal lysines, H3K9, H3K23, and those within the histone fold domain, H3K56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Rtt109 is specific for histone H3, acetylation at Lys9 and Lys56. RTT109 has functions in addition to maintaining genome stability
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Rtt109 association with distinct histone chaperones directs substrate selection between N-terminal lysines, H3K9, H3K23, and those within the histone fold domain, H3K56. The sequence G-K-X-P within histone H3, which includes the primary Gcn5 substrate K14, makes several key contacts within the active site that are conserved with other GNAT members
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Rtt109 is specific for histone H3, acetylation at Lys9 and Lys56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys18
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H3: preferred substrate
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
the sequence G-K-X-P within histone H3, which includes the primary Gcn5 substrate K14, makes several key contacts within the active site that are conserved in GNAT members
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
the sequence G-K-X-P within histone H3, which includes the primary Gcn5 substrate K14, makes several key contacts within the active site that are conserved in GNAT members
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys14 by tGCN5 in the consensus sequence QTARKSTGGK14APRKLASK
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys14 by tGCN5 in the consensus sequence QTARKSTGGK14APRKLASK. Phe125 and Phe164 interact with the substrate, but are not directly involved in the acetylation reaction, while residues Glu122, Val123 and Tyr160 are critical for catalysis
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
preferred substrate
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
preferred substrate
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
enzyme form B, very low activity
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
enzyme form B, very low activity
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
Lys14 of histone H3 and a peptide containing Lys14 thereof are the preferred substrates for Gnc5 and PCAF protein, as well as Gnc5 and PCAF catalytic domain
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
Lys14 of histone H3 and a peptide containing Lys14 thereof are the preferred substrates for Gnc5 and PCAF protein, as well as Gnc5 and PCAF catalytic domain
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptides H3p19, H3p27, H3p11 are substrates for the catalytic domain of Gcn5 and PCAF
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptides H3p19, H3p27, H3p11 are substrates for the catalytic domain of Gcn5 and PCAF
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
Lys14 of histone H3 and a peptide containing Lys14 thereof are the preferred substrates for Gnc5 and PCAF protein, as well as Gnc5 and PCAF catalytic domain
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptides H3p19, H3p27, H3p11 are substrates for the catalytic domain of Gcn5 and PCAF
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptides H3p19, H3p27, H3p11 are substrates for the catalytic domain of Gcn5 and PCAF
-
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptides H3p19, H3p27, H3p11 are substrates for the catalytic domain of Gcn5 and PCAF
-
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
-
?
acetyl-CoA + histone H3-peptide
CoA + acetylhistone H3 -peptide
-
-
-
-
?
acetyl-CoA + histone H3-peptide
CoA + acetylhistone H3 -peptide
-
-
-
-
?
acetyl-CoA + histone H3-peptide
CoA + acetylhistone H3-peptide
-
-
-
-
?
acetyl-CoA + histone H3-peptide p20
CoA + acetylhistone H3 -peptide p20
-
-
-
-
?
acetyl-CoA + histone H3-peptide p20
CoA + acetylhistone H3 -peptide p20
-
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Gcn5 protein acetylates H4 when purified and presented separately to the enzyme at Lys8 and Lys16
-
r
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys14
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
RmtA is specific for histone H4 with Arg3 as the methylation site. Methylation of histone H4 by recombinant RmtA affects the acetylation by p300/CBP, supporting aninterrelation of histone methylation and acetylation in transcriptional regulation. Important role of the enzyme for chromatin modulating activity
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
RmtA is specific for histone H4 with Arg3 as the methylation site
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B nearly exclusively acetylates histones H4 and H2a
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
highly specific for
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Gcn5 protein acetylates H4 when purified and presented separately to the enzyme at Lys8 and Lys16
-
r
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4: all of the acetate groups are introduced within the NH2-terminal amino acids 4 to 17
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys16 by MYST1 is essential for chromatin remodeling and is used for regulation of gene expression in eukaryotes. The nucleosome is a disc-shaped octamer consisting of two heterotetramers formed by histones H3/H4 and histones H2A and H2B
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Mof is required for sex chromosome dosage compensation acting in the MSL complex, which also contains Msl1-3, Mle, and RNA, to acetylate H4K16 and to increase gene transcription from the single male X chromosome
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys16
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys16 by MYST1
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation of Lys5, Lys8, Lys12, and Lys16
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Hat1 is a primary enzyme for di-acetylating cytosolic histone H4 at Lys5 and Lys12 in the cytosol
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Gcn5 protein acetylates H4 when purified and presented separately to the enzyme at Lys8 and Lys16
-
r
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is the preferred substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
histone H4 is the preferred substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
specific acetylation of Lys16, reversible acetylation of histones play an important role in regulation of chromatin structure and function. HMOF has a role in DNA damage responseduring cell cycle progression
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
MYST-related histone acetyltransferase complex Tip60, GNAT-related histone acetyltransferase complex PCAF
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
HBO1 is an H4-specific histone acetylase, and is a coactivator of the DNA replication licensing factor Cdt1. HBO1 acetylase activity is essential for DNA licensing of replication origins, where it controls H4 acetylation at the origins. H4 acetylation at origins is cell-cycle regulated, with maximal activity at the G1/S transition
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
HBO1 regulates global histone H4 acetylation
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
MSL-associated MOF acetylates nucleosomal histone H4 almost exclusively on Lys16, while NSL-associated MOF exhibits a relaxed specificity and also acetylates nucleosomal histone H4 on Lys5 and Lys8
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
MYST1 specificity to Lys16 of histone H4 is not absolute, because in experiments in vitro the protein is also able to acetylate histones H3 and H2A, whereas in vivo only modification of histone H4 is specific. Acetylation at Lys16 by MYST1 is essential for chromatin remodeling and is used for regulation of gene expression in eukaryotes. The nucleosome is a disc-shaped octamer consisting of two heterotetramers formed by histones H3/H4 and histones H2A and H2B. All human autosomes are susceptible to histone H4 acetylation by Lys16 residue and acetyltransferase MYST1
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation at Lys16 by MYST1
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
activity with synthetic histone H4 tail peptide substrate of p300 that shows different degrees of autoacetylation, overview. Tyr1467 appears to serve as a general acid protonating the departing coenzyme A sulfur
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
recombinant ATAC2 has a weak HAT activity directed to histone H4
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
recombinant Hbo1 can acetylate nucleosomal histone H4 in vitro, with a preference for Lys5 and Lys12, mapping of acetylation sites, overview
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
substrate is a H4 peptide
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation of Lys16
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation of Lys16
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation of Lys16
in the assay the CoA thiolate is detected by the thiol sensitive fluorescent dye 7-diethylamino-3-(4'-maleimidylphenyl)-4-methylcoumarin
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
the enzyme PCAF acetylates histone H4 at lysine 8
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is the preferred substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
H4R3 methylation, catalyzed by PRMT1, facilitates beta-globin transcription by regulating histone acetyltransferase binding, and histone H3 and H4 acetylation, overview
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Mof is solely responsible for H4K16 acetylation in mouse blastocysts. Tip60 plays essential roles in cell cycle progression in vitro
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
PCAF binds to dimethyl-Arg3 at histone H4 tails, dimethyl H4R3 provides a binding surface for PCAF and directly enhances histone H3 and H4 acetylation in vitro
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
recombinant ATAC2 has a weak HAT activity directed to histone H4
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B is specific for histone H4
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
highly specific for
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B
mono-, di- and triacetylated products
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylates histone H4 in vitro at K5, K8, K12 and K16
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B is specific for histone H4
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is a poor substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Gcn5 protein acetylates H4 when purified and presented separately to the enzyme at Lys8 and Lys16
-
r
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
NuA4-like protein acetylates histone H4 and H2A
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
SAS complex, native and recombinant, acetylates Lys16
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B has a marked specificity for histone H4
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is the preferred substrate
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is the preferred substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is the preferred substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation of histone H4 by NuA4 is required for the cellular resistance to spindle stress. The NuA4 histone acetyltransferase subunit Yaf9, is required for the cellular response to spindle stress in yeast
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
exclusively acetylates of Lys16 of histone H4, the enzyme is required for bulk of H4 lysine 16 acetylation in vivo, role of SAS complex in antagonizing the speading of Sir proteins at silent loci in Saccharomyces cerevisiae
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
the level of HAT-B-dependent acK12H4 may be very low under normal growth condition
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetyltion of Lys16, acetylates free histones and weakly acetylates nucleosomes
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
MYST-related histone acetyltransferase complex NuA4 or SAS(SAS-I)
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
specifically acetylates Lys12, and to a lesser extent Lys5 of free, non-chromatin-bound histone H4
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
both Lys12 and Lys5 of soluble, non-chromatin-bound histone H4 are in vivo targets of acetylation for the yeast HAT-B enzyme. Lys12/Lys5-acetylated histone H4 is bound to the HAT-B complex in the soluble cell fraction. Exchange of Lys for Arg at position 12 of histone H4 do not interfere with histone H4 association with the complex, but prevented acetylation on Lys5 by the HAT-B enzyme, in vivo as well as in vitro
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
full-length histone H4 is acetylated 2000fold faster than histone tail peptides
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
substrates are synthetic N-terminal H4 peptides. The HAT-B complex acetylates only Lys12, recombinant Hat1 is able to modify Lys12 and Lys5. Exchange of Lys for Arg at position 12 of histone H4 does not interfere with histone H4 association with the complex, but prevents acetylation on Lys5 by the HAT-B enzyme, in vivo as well as in vitro
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
NuA4-like protein acetylates histone H4 and H2A
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B
mono- and diacetylated products
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B
mono- and diacetylated products
?
acetyl-CoA + histone H4
peptide CoA + acetylhistone H4 peptide
-
specific acetylation of Lys16
-
-
?
acetyl-CoA + histone H4
peptide CoA + acetylhistone H4 peptide
-
-
-
?
acetyl-CoA + N-terminal L-lysyl-[Hsp70]
CoA + H+ + N-terminal Nalpha-acetyl-L-lysyl-[Hsp70]
-
-
-
ir
acetyl-CoA + N-terminal L-lysyl-[Hsp70]
CoA + H+ + N-terminal Nalpha-acetyl-L-lysyl-[Hsp70]
acetylation of residue K77
-
-
ir
acetyl-CoA + p50 protein
CoA + acetyl-p50 protein
-
acetylation of p50 by p300 independent of shear stress
-
-
?
acetyl-CoA + p50 protein
CoA + acetyl-p50 protein
-
acetylation of histones H4 at the site of SSRE within the eNOS promoter
-
-
?
acetyl-CoA + p53
CoA + acetyl-p53
p53 protein-acetylation of the Lys120 residue
-
-
?
acetyl-CoA + p53
CoA + acetyl-p53
p53 protein-acetylation of the Lys120 residue is carried out by acetyltransferases MYST1 and TIP60 to approximately equal extent
-
-
?
acetyl-CoA + p65 protein
CoA + acetyl-p65 protein
-
acetylation of p65 by p300 during translocation into the nuclei in response to shear stress
-
-
?
acetyl-CoA + p65 protein
CoA + acetyl-p65 protein
-
acetylation of histones H3 at the site of SSRE within the eNOS promoter
-
-
?
acetyl-CoA + protamine sulfate
?
-
enzyme form A, not enzyme form B
-
-
?
acetyl-CoA + protein p53
CoA + acetylprotein p53
-
substrate is a DNA-binding transcription activator and a tumor suppressor
-
-
?
acetyl-CoA + protein p53
CoA + acetylprotein p53
-
peptide of p53 is a substrate for PCAF catalytic domain
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine40
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine40
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
KAT2A acetylates Lys40 of TUBA
-
-
?
acetyl-CoA + [ATM]-L-lysine
CoA + [ATM]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [ATM]-L-lysine
CoA + [ATM]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [c-myc]-L-lysine
CoA + [c-myc]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [c-myc]-L-lysine
CoA + [c-myc]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [DNMT1]-L-lysine
CoA + [DNMT1]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [DNMT1]-L-lysine
CoA + [DNMT1]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [E2F1]-L-lysine
CoA + [E2F1]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [E2F1]-L-lysine
CoA + [E2F1]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [EGR2]-L-lysine
CoA + [EGR2]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [Geminin]-L-lysine14
CoA + [Geminin]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [Geminin]-L-lysine14
CoA + [Geminin]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [HBsu]-L-lysine
CoA + [HBsu]-N6-acetyl-L-lysine
essential histone-like protein HBsu contains seven acetylation sites in vivo, mutational analysis using mutants hbsK86Q, hbsK41Q, hbsK3Q, hbsK41R, and hbsK37R
-
-
?
acetyl-CoA + [HBsu]-L-lysine
CoA + [HBsu]-N6-acetyl-L-lysine
histone-like protein HBsu
-
-
?
acetyl-CoA + [HBsu]-L-lysine
CoA + [HBsu]-N6-acetyl-L-lysine
essential histone-like protein HBsu contains seven acetylation sites in vivo, mutational analysis using mutants hbsK86Q, hbsK41Q, hbsK3Q, hbsK41R, and hbsK37R
-
-
?
acetyl-CoA + [HBsu]-L-lysine
CoA + [HBsu]-N6-acetyl-L-lysine
histone-like protein HBsu
-
-
?
acetyl-CoA + [histone H2A]-L-lysine5
CoA + [histone H2A]-N6-acetyl-L-lysine5
-
-
-
-
ir
acetyl-CoA + [histone H2A]-L-lysine5
CoA + [histone H2A]-N6-acetyl-L-lysine5
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine18
CoA + [histone H3]-N6-acetyl-L-lysine18
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine18
CoA + [histone H3]-N6-acetyl-L-lysine18
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine23
CoA + [histone H3]-N6-acetyl-L-lysine23
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine23
CoA + [histone H3]-N6-acetyl-L-lysine23
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine27
CoA + [histone H3]-N6-acetyl-L-lysine27
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine27
CoA + [histone H3]-N6-acetyl-L-lysine27
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine56
CoA + [histone H3]-N6-acetyl-L-lysine56
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine56
CoA + [histone H3]-N6-acetyl-L-lysine56
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine56
CoA + [histone H3]-N6-acetyl-L-lysine56
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
-
ir
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
main substrate
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
-
ir
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
main substrate
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
-
ir
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
-
ir
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
?
acetyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-acetyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
acetyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-acetyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
acetyl-CoA + [p53]-L-lysine
CoA + [p53]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [p53]-L-lysine
CoA + [p53]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [p53]-L-lysine120
CoA + [p53]-N6-acetyl-L-lysine120
-
-
-
?
acetyl-CoA + [p53]-L-lysine120
CoA + [p53]-N6-acetyl-L-lysine120
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
endogenous GCN5 and EGR2 in iNKT cells
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
endogenous GCN5 and EGR2 in iNKT cells
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [TIP5]-L-lysine
CoA + [TIP5]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [TIP5]-L-lysine
CoA + [TIP5]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
acetyl-CoA + [TRRAP]-L-lysine
CoA + [TRRAP]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [TRRAP]-L-lysine
CoA + [TRRAP]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9
-
-
-
?
androgen receptor + acetyl-CoA
acetylated androgen receptor + CoA
-
receptor signaling in prostate cancer cells is augmented by the androgen receptor coactivator p300, which transactivates and acetylates the androgen receptor in the presence of 100 nM dihydrotestosterone, involvement of p300 in neuropeptide activation of androgen receptor signaling, overview
-
-
?
androgen receptor + acetyl-CoA
acetylated androgen receptor + CoA
-
the KLKK motif of androgen receptor protein is both necessary and sufficient for acetylation by p300 in the presence of 100 nM dihydrotestosterone
-
-
?
ATM kinase + acetyl-CoA
acetylated ATM kinase + CoA
-
ATM protein kinase regulates the cells response to DNA damage through the phosphorylation of proteins involved in cell-cycle checkpoints and DNA repair, suppression of Tip60 blocks the activation of ATMs kinase activity, ATM autophosphorylation e.g. at Ser1981, and prevents the ATM-dependent phosphorylation of p53 and chk2, inactivation of Tip60 sensitizes cells to ionizing radiation, overview
-
-
?
ATM kinase + acetyl-CoA
acetylated ATM kinase + CoA
-
the ataxia telangiectasia mutant, i.e. ATM, protein kinase, ATM forms a stable complex with Tip60 through the conserved, highly required FATC domain of ATM, the interaction between ATM and Tip60 is not regulated in response to DNA damage, but is specifically induced by DNA damage, overview, mutations in the FATC domain that abolish the interaction between ATM and Tip60
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
histone acetylation is an important posttranslational modification correlated with gene activation, the HAC1 is involved in the regulation of flowering time via repression of flowering locus C, the enzyme participates in many physiological processes, including proliferation, differentiation, and apoptosis
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
phosphorylation of p300 at Ser1834 by the kinase Akt is essential for its histone acetyltransferase and transcriptional activity
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
histones from the Hela cell core
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
key enzyme in post-translational modification of histones associated with transcriptionally active genes
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation of Lys9, and Lys14
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation of Lys9, and Lys14
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
the enzyme is involved in ethanol-induced acetylation of histone H3 in hepatocytes, potential mechanism for gene expression activation by the enzyme, overview
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation at Lys9
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation at Lys9 and Lys14
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation of the tail of the histone, the enzyme is organized in the catalytic Ada2/Ada3/Gcn5 subcomplex of SAGA acting on the nucleosome, overview
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
acetylation of Lys5, Lys8, and Lys12, Gcn5 and transcriptional adaptor Ada2a are involved in nucleosomal histone H4 acetylation
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
acetylation of Lys5, Lys8, and Lys12
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
acetylation of Lys5, Lys8, and Lys12
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
acetylation at Lys8, NCOAT has the ability to directly associate with both an acetylated and unacetylated histone H4 tail in vitro without tequiring acetyl-lysine contacts, binding and interaction mechanism, overview
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
acetylation of the tail of the histone, the enzyme is organized in the NuA4 subcomplex acting on the nucleosome, overview
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
acetylation at Lys5 and Lys12, acetylation by Hat1 requires positively charged amino acids at positions 8 and 16 of the H4 tail
-
-
?
promyelotic leukemia zinc finger gene + acetyl-CoA
acetylated promyelotic leukemia zinc finger gene + CoA
-
-
-
-
?
promyelotic leukemia zinc finger gene + acetyl-CoA
acetylated promyelotic leukemia zinc finger gene + CoA
-
i.e. PLZF, a direct and specific substrate of the p300 HAT, no activity with the substrate deletion mutant lacking zinc fingers 6 to 9
-
-
?
additional information
?
-
-
Gcn5 is a coactivator of transcription
-
-
?
additional information
?
-
-
Gcn5 and PCAF protein are transcription cofactors
-
-
?
additional information
?
-
-
affects the inflorescence meristem and stamen development in Arabidopsis thaliana
-
-
?
additional information
?
-
-
histone acetylation and deacetylation is an epigenetic mechanism in volved in regulation of mIRNA production. GCN5 has a general repressive effect on microRNAs, miRNAs, and it targets a subset of MIRNA genes, GCN5 is required for acetylation of histone H3 lysine 14 at these loci, overview
-
-
?
additional information
?
-
isoform GCN5 is not the enzyme responsible for histone acetylation at cold-regulated genes COR promoters during cold acclimation
-
-
?
additional information
?
-
-
GCN5 directly targets HSFA3 and UVH6 and affects their H3K9 and H3K14 acetylation levels
-
-
?
additional information
?
-
quantification of HBsu acetylation by parallel reaction monitoring-tandem mass spectrometry
-
-
-
additional information
?
-
quantification of HBsu acetylation by parallel reaction monitoring-tandem mass spectrometry
-
-
-
additional information
?
-
-
protamine, bovine serum albumin, and ubiquitin are no substrates
-
-
?
additional information
?
-
-
Tip60, in complex with homologues of the mammalian Tip60 complex, exhibits functional redundancy with two other groups of genes, known as synthetic multivulva A and B genes, synMUV. Therefore, the genes encoding proteins of the Tip60 complex are termed class C synMUV genes. SynMUV A and B counteract EGF to Ras to MAPK signaling and the Tip60 complex is a chromatin-modifying complex
-
-
?
additional information
?
-
-
a homologue of Moz, zMoz, occurs in zebrafish to perform a potential Moz function in the trunk region
-
-
?
additional information
?
-
-
a homologue of Moz, zMoz, occurs in zebrafish to perform a potential Moz function in the trunk region
-
-
?
additional information
?
-
-
Gcn5 is a coactivator of transcription
-
-
?
additional information
?
-
-
Gcn5 and PCAF protein are transcription cofactors
-
-
?
additional information
?
-
-
the enzyme plays a role in chromatin structure and gene expression regulation as a catalytic component of multiprotein complexes, some of which also contain Ada2-type transcriptional coactivators
-
-
?
additional information
?
-
-
MYST1 is a part of multiprotein complexes that accomplish functions of male X chromosome activation and thereby functions of dosage compensation in Drosophila and, in mammals, global acetylation of histone H4 K16. Functional links between MYST1 and proteins ATM and p53. Interactions between MSL1 and MYST1 within the MSL complex in Drosophila melanogaster, the compensasome includes proteins MSL1, MSL2, MSL3, MLE, MOF, a histone acetyltransferase homologous to MYST1, JIL1, and two non-coding RNA: roX1 and roX2, structure and function of the compensasome, detailed overview. Cell interactome fragments including protein homologs of hampin and MYST1, overview
-
-
?
additional information
?
-
-
histones H3 and H4 and their chaperone Asf1, including RbAp48, a regulatory subunit of Hat1 enzyme, are associated with Hat1 in the cytosol of chicken cells. Hat1 regulates integrity of cytosolic histone H3-H4 containing complex, effect of Hat1 on status for the cytosolic histones H3/H4 pre-deposition complexes with respective chaperone proteins, overview
-
-
?
additional information
?
-
-
Gcn5 and PCAF protein are transcription cofactors
-
-
?
additional information
?
-
-
Gcn5 and PCAF protein are transcription cofactors
-
-
?
additional information
?
-
-
Gcn5 and PCAF protein are transcription cofactors
-
-
?
additional information
?
-
-
Gcn5 and PCAF protein are transcription cofactors
-
-
?
additional information
?
-
-
enzyme activity is regulated by phosphorylation and interaction with other regulating protein factors
-
-
?
additional information
?
-
-
MOZ and MORF genes are rearranged by chromosome abnormalities associated with several types of leukemia
-
-
?
additional information
?
-
-
MYST-related histone acetyltransferase complex Tip60 also acts as a transcriptional coactivator in several systems including class I nuclear hormone receptors, NF-kappaB and at the superoxide dismutase gene. Tip 60 has been implicated in Alzheimer disease because it stimulates transcription when asociated with the cleaved cytoplasmic tail fragment of the amyloid-beta precursor protein
-
-
?
additional information
?
-
-
Tip60 plays a role in the control of cell-related events
-
-
?
additional information
?
-
-
acetylation of proteins by the enzyme plays a critical role in the regulation of gene expression
-
-
?
additional information
?
-
-
androgen Src kinase and PKCd kinase are involved in the regulation of p300 HAT activity via bombesin, overview
-
-
?
additional information
?
-
-
deregulated HAT activity plays a role in the development of a range of cancers
-
-
?
additional information
?
-
-
the enzyme is involved in Sp1 activation of the cyclin D1 promoter, TAF1-dependent histone acetylation facilitates transcription factor binding to the Sp1 sites, thereby activating cyclin D1 transcription and ultimately G1-to-S-phase progression, regulation, overview
-
-
?
additional information
?
-
-
the histone acetyltransferase activity of p300 is required for transcriptional repression by the promyelocytic leukemia zinc finger protein
-
-
?
additional information
?
-
-
in absence of acceptor substrate the enzyme performs autoacetylation, identification of 13 autoacetylation sites and mechanism, autoacetylation catalyzed by p300 HAT is about 1000-fold more efficient than p300/CREB-binding protein-associated factor-mediated acetylation of catalytically defective p300 HAT, overview
-
-
?
additional information
?
-
ATAC2 associates with GCN5 and other proteins linked to chromatin metabolism
-
-
?
additional information
?
-
-
besides the male-specific lethal, MSL, HAT complex, MOF is also a component of the second HAT complex, designated the non-specific lethal, NSL complex, substrate specificity of the NSL complex, overview. Assembly of the MOF HAT into MSL or NSL complexes controls its substrate specificity
-
-
?
additional information
?
-
besides the male-specific lethal, MSL, HAT complex, MOF is also a component of the second HAT complex, designated the non-specific lethal, NSL complex, substrate specificity of the NSL complex, overview. Assembly of the MOF HAT into MSL or NSL complexes controls its substrate specificity
-
-
?
additional information
?
-
-
HBO1 histone acetylase is involved in DNA replication licensing and associates with replication origins, located within the HPRT1 coding sequence, specifically during the G1 phase of the cell cycle in a manner that depends on the replication licensing factor Cdt1, but is independent of the Cdt1 repressor geminin
-
-
?
additional information
?
-
-
HBO1 occurs as a component of a multiprotein complex with histone H3 and H4 acetyltransferase activity in 293 cells. The mammalian complex corresponding to the yeast NuA4 complex contains the MYST HAT Tip60
-
-
?
additional information
?
-
-
in response to DNA damage, Tip60 acetylates ATM, a DNA damage related kinase, allowing for phosphorylation of Chk2 and p53 by ATM. HATs perform a conserved mechanism of acetyl-transfer, where the lysine-containing substrate directly attacks enzyme-bound acetyl-CoA. The ability of HATs to form distinct multi-subunit complexes provide a means to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex
-
-
?
additional information
?
-
-
increase in eNOS mRNA, caused by shear stress, is completely blocked by pharmacological inhibition of p300/HAT activity with curcumin or by p300 small interfering RNA
-
-
?
additional information
?
-
mechanistically, p300 acts as a transcriptional coactivator through the direct interaction with a diverse set of transcription factors and RNA polymerase II transcription machinery
-
-
?
additional information
?
-
MYST1 is a part of multiprotein complexes that accomplish functions of male X chromosome activation and thereby functions of dosage compensation in Drosophila and, in mammals, global acetylation of histone H4 K16. Functional links between MYST1 and proteins ATM and p53. MYST1 interacts with WDR5. Cell interactome fragments including protein homologs of hampin and MYST1, overview
-
-
?
additional information
?
-
-
Tip60 is part of the evolutionarily conserved NuA4 complex
-
-
?
additional information
?
-
-
HBO1 interacts both with transcriptional activator proteins and with MCM2 and ORC1
-
-
?
additional information
?
-
MYST1 specificity to Lys16 of histone H4 is not absolute, because in experiments in vitro the protein is also able to acetylate histones H3 and H2A, whereas in vivo only modification of histone H4 is specific
-
-
?
additional information
?
-
-
no activity with histones H3, H2A and H2B by recombinant MOF in HeLa nucleosomes
-
-
?
additional information
?
-
no activity with histones H3, H2A and H2B by recombinant MOF in HeLa nucleosomes
-
-
?
additional information
?
-
-
p/CAF and p300 appear to be constitutive HATs that do not require helper proteins to exhibit full catalytic activity
-
-
?
additional information
?
-
-
assembly of the enzyme into male-specific lethal, MSL, or non-specific lethal, NSL, complexes controls its substrate specificity. Although MSL-associated enzyme acetylates nucleosomal histone H4 almost exclusively on lysine 16, NSL-associated enzyme exhibits a relaxed specificity and also acetylates nucleosomal histone H4 on lysines 5 and 8
-
-
?
additional information
?
-
assembly of the enzyme into male-specific lethal, MSL, or non-specific lethal, NSL, complexes controls its substrate specificity. Although MSL-associated enzyme acetylates nucleosomal histone H4 almost exclusively on lysine 16, NSL-associated enzyme exhibits a relaxed specificity and also acetylates nucleosomal histone H4 on lysines 5 and 8
-
-
?
additional information
?
-
Glu187 and Glu276 could act as the general catalytic base and together with Asp277 have a cumulative effect on deprotonation of the ?-amino group of substrate Lys12 of the histone H4 peptide, which could be mediated by water molecules
-
-
?
additional information
?
-
-
Glu187 and Glu276 could act as the general catalytic base and together with Asp277 have a cumulative effect on deprotonation of the ?-amino group of substrate Lys12 of the histone H4 peptide, which could be mediated by water molecules
-
-
?
additional information
?
-
-
enzyme p300 can directly interact with myocardin, and consequently induce the acetylation of myocardin and nucleosomal histones surrounding SRF-binding sites. Acetylation of both histone and myocardin by p300
-
-
?
additional information
?
-
GCN5 directly binds to and increases the histone H3 and H4 acetylation of the cyclin E1, cyclin D1, and E2F1 promoters
-
-
?
additional information
?
-
HBO1 exerts significant acetyltransferase activity on proteins such as ORC2, MCM2, CDC6, and Geminin in in vitro assays
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
lysine acetyltransferase (KAT) activity of recombinant human ARD1/NAA10, overview. Arrest defective 1 (ARD1) is the only enzyme known so far to exhibit both N-terminal acetyltransferase (NAT) and N-terminal lysine acetyltransferase (KAT) activities. Only the monomeric rhARD1/NAA10 form, but not the oligomeric form, can acetylate lysine residues of substrate proteins. rhARD1/NAA10-mediated Hsp70 acetylation increased in a time-dependent manner
-
-
-
additional information
?
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lysine acetyltransferase (KAT) activity of recombinant human ARD1/NAA10, overview. Arrest defective 1 (ARD1) is the only enzyme known so far to exhibit both N-terminal acetyltransferase (NAT) and N-terminal lysine acetyltransferase (KAT) activities. Only the monomeric rhARD1/NAA10 form, but not the oligomeric form, can acetylate lysine residues of substrate proteins. rhARD1/NAA10-mediated Hsp70 acetylation increased in a time-dependent manner
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additional information
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recombinant hARD1/NAA10 exhibits KAT activity, which disappears soon in vitro due to enzyme oligomerization, which results in the loss of KAT activity. While oligomeric recombinant hARD1/NAA10 loses its ability for lysine acetylation, its monomeric form clearly exhibits lysine acetylation activity in vitro. Assay optimization, under optimal conditions, hARD1/NAA10 retains its KAT activity, overview
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additional information
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recombinant hARD1/NAA10 exhibits KAT activity, which disappears soon in vitro due to enzyme oligomerization, which results in the loss of KAT activity. While oligomeric recombinant hARD1/NAA10 loses its ability for lysine acetylation, its monomeric form clearly exhibits lysine acetylation activity in vitro. Assay optimization, under optimal conditions, hARD1/NAA10 retains its KAT activity, overview
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screening of interacting proteins for substrate identification, testing of more than four hundred proteins, KAT substrate enrichment with biotin-streptavidin pulldown and semiquantitative LC-MS/MS studies, overview. The proteins are either p300- or GCN5-unique or shared by the two KATs. 3-Azidopropionyl CoA (3AZ-CoA) is applied as a bioorthogonal surrogate of acetyl-, propionyl- and butyryl-CoA for KAT substrate identification, method overview. Comparison of the substrate profiles of p300 and GCN5, different acetyl-CoA surrogates and histone peptide H3-20 or H4-20 (the first 20 amino acids from the N-terminus of histone H3 or H4) are used as substrates. 3AZ-CoA is a sensitive and specific probe for both p300 and GCN5-T612G with comparable or even stronger activity than Ac-CoA. Substrate validations
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additional information
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screening of interacting proteins for substrate identification, testing of more than four hundred proteins, KAT substrate enrichment with biotin-streptavidin pulldown and semiquantitative LC-MS/MS studies, overview. The proteins are either p300- or GCN5-unique or shared by the two KATs. 3-Azidopropionyl CoA (3AZ-CoA) is applied as a bioorthogonal surrogate of acetyl-, propionyl- and butyryl-CoA for KAT substrate identification, method overview. Comparison of the substrate profiles of p300 and GCN5, different acetyl-CoA surrogates and histone peptide H3-20 or H4-20 (the first 20 amino acids from the N-terminus of histone H3 or H4) are used as substrates. 3AZ-CoA is a sensitive and specific probe for both p300 and GCN5-T612G with comparable or even stronger activity than Ac-CoA. Substrate validations
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
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Gcn5 and PCAF protein are transcription cofactors
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additional information
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enzyme activity is regulated by phosphorylation and interaction with other regulating protein factors
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additional information
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Gcn5 and PCAF protein are transcription cofactors
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additional information
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Gcn5 and PCAF protein are transcription cofactors
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additional information
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the nuclear cytoplasmic O-GlcNAcase and acetyltransferase, NCOAT, is a bifunctional enzyme with both glycoside hydrolase and alkyltransferase activity and contains a zinc finger-like motif responsible for substrate recognition, via making contacts with the histone tails within nucleosomes, essential for activity, overview
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MOZ specifically interacts and associates with transcription factors such as AML1, PU.1, p53, Runx2 and NF-kappaB, functioning as their transcriptional coactivator and cooperatively activating target gene transcription
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ATAC2 associates with GCN5 and other proteins linked to chromatin metabolism
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specific role of MOZ-driven acetylation in controlling a desirable balance between proliferation and differentiation during hematopoiesis. MOZ also shows activity either as Runx1 coactivator or in the induction of leukemic transformation via transcriptional intermediary factor 2, TIF2, but is not essentially required
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the mammalian complex corresponding to the yeast NuA4 complex contains the MYST HAT Tip60. Myc recruits the Tip60 complex to the chromatin in Rat1 wild-type cells, but not in Rat1 Myc mutant cells. Hbo1 appears to function predominantly in transcriptional repression
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HBO1 exerts significant acetyltransferase activity on proteins such as ORC2, MCM2, CDC6, and Geminin in in vitro assays
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additional information
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specific role of MOZ-driven acetylation in controlling a desirable balance between proliferation and differentiation during hematopoiesis. MOZ also shows activity either as Runx1 coactivator or in the induction of leukemic transformation via transcriptional intermediary factor 2, TIF2, but is not essentially required
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protein participates in var gene activation
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protein participates in var gene activation
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diaminodipropylamine and 1,3-propanediamine are no substrates
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the enzyme modulates gene expression in liver nuclei in an epigenetic manner at high blood alcohol levels, no alteratins of MAP kinase levels, overview
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HeLa nucleosome or core histones are no substrate for recombinant SAS complex
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for acetylation activity of Sas2, Sas4 is absolutely required, while Sas5 stimulate
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additional information
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Gcn5 is a coactivator of transcription
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additional information
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Gcn5 and PCAF protein are transcription cofactors
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additional information
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Gcn5 and PCAF protein are transcription cofactors
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additional information
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Gcn5 and PCAF protein are transcription cofactors
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additional information
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Gcn5 and PCAF protein are transcription cofactors
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additional information
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enzyme activity is regulated by phosphorylation and interaction with other regulating protein factors
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additional information
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MYST-related histone acetyltransferase complex NuA4: required for cell growth, required for p53-dependent transcription activation in yeast, presumably through its Yng2 subunit, homolog of the tumor suppressor ING1. GNAT-related histone acetyltransferase complex SAGA can stimulate Gal4-VP16 activation in a manner dependent on HAT activity. D´SAGA can be recruited by several yeast activators. SAGA is targeted to promoter regions proximal to the activator binding site. Once targeted, SAGA acetylates histone h3 in the vicinity of the promoter. Targeted acetylation by SAGA stabilizes its binding and that of a targeted SWI/SNF chromatin-remodeling complex. SAGA is required for both activation of the yeast ARG1 promoter by Gcn4 activator and repression by the ArgR/Mcm1 repressor complex
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additional information
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no acetylation of adrenocorticotropin or a H3 peptide
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additional information
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in the absence of histone acceptor, slow rates of enzyme autoacetylation and of CoA formation occur
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Esa1 is the catalytic subunit of at least two multiprotein complexes, NuA4 and Piccolo NuA4, picNuA4
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additional information
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HATs perform a conserved mechanism of acetyl-transfer, where the lysine-containing substrate directly attacks enzyme-bound acetyl-CoA. The ability of HATs to form distinct multi-subunit complexes provide a means to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex
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additional information
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HBO1, Sas2 and Sas3 are involved in transcriptional repression enhancing Sir1-mediated epigenetic gene silencing. NuA3 and NuA4 complexes contain the MYST HATs Sas3 and Esa1, respectively. Sas2 histone acetylation of H4K16 opposed by Sir2 deacetylation of H4K16 at the euchromatin/heterochromatin interface maintains the boundary between regions of transcriptionally active and silent telomeric chromatin. Esa1 plays a role in maintaining the integrity of the DNA, rather than open chromatin structure and high-level transcriptional activity
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additional information
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in addition to Asf1, Rtt109 is also functionally linked to Rtt101, Mms1, and Mms22
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additional information
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Rtt109 facilitates error-free replication to prevent CAG/CTG repeat contractions. The Rtt107/Rtt101 complex is recruited to stalled replication forks in an Rtt109-dependent manner
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additional information
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soluble histone H4 Hat1-dependently acetylated on Lys12 is present in cells arrested at all cell cycle stages, G1, S, G2/M and also G0. Histone H3 seems to be no substrate for the HAT-B complex
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additional information
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Gcn5 and p300 appear to be constituitive HATs that do not require helper proteins to exhibit full catalytic activity. Esa1 and Rtt109 represent low-activity HATs that are stimulated by regulatory helper proteins, Yng2-Epl1 and Vps75/Asf1, respectively. p300/CBP exhibits the broadest protein specificity, p300 prefers histone acetylation sites with a positive charge in the -3 or +4 position. Ability of some HATs to utilize longer chain acyl-CoA, i.e. propionyl-CoA
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additional information
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histone chaperone Vps75 acts as activiating subunit. The rate-determining step of the activated complex is the transfer of the acetyl group from acetyl-CoA to the acceptor lysine residue. Vps75 stimulates catalysis more than 250fold, not by contributing a catalytic base, but by stabilizing the catalytically active conformation of enzyme Rtt109
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additional information
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removal of lysine residues does not substantially affect the ability of NuA4 histone actyltransferase complex to acetylate remaining sites, and insertion of an additional lysine into the substrate histone H4 tail leads to rapid quintuple-acetylation. Conversion of the native histone H2A tail to an H4-like sequence results in enhanced multi-site acetylation. NuA4's site selectivity is dictated by accessibility on the nucleosome surface, the relative proximity from the histone fold domain, and a preference for intervening glycine residues with a minimal (n + 2) spacing between lysines
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additional information
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NuA4 targets histone and nonhistone proteins
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additional information
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NuA4 targets histone and nonhistone proteins
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
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additional information
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Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
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additional information
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Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
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additional information
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Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
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additional information
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Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
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additional information
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Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
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additional information
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Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
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additional information
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Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
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additional information
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Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
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additional information
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Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
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additional information
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Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
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additional information
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Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
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additional information
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Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
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additional information
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Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
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additional information
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Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
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additional information
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Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
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additional information
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
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additional information
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Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
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additional information
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Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
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additional information
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Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
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additional information
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Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
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additional information
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Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
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additional information
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Rtt109 facilitates error-free replication to prevent CAG/CTG repeat contractions. The Rtt107/Rtt101 complex is recruited to stalled replication forks in an Rtt109-dependent manner
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additional information
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NuA4 targets histone and nonhistone proteins
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additional information
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substrate specificity and order of acetylation of histone H4 by Hat1, overview
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additional information
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substrate specificity and order of acetylation of histone H4 by Hat1, overview
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additional information
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Mst1 interacts with a number of proteins involved in chromosome integrity and centromere function, including the methyltransferase Skb1, the recombination mediator Rad22, Sc Rad52, the chromatin assembly factor Hip1, Sc Hir1, and the Msc1 protein related to a family of histone demethylases, detailed interaction analysis, overview
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additional information
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Gcn5 appears to be constituitive HAT that does not require helper proteins to exhibit full catalytic activity
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additional information
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Gcn5 appears to be constituitive HAT that does not require helper proteins to exhibit full catalytic activity
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additional information
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enzyme GCN5b interacts with AP2-domain proteins, apicomplexan plant-like transcription factors, as well as a core complex that includes the co-activator ADA2-A, TFIID subunits, LEO1 polymerase-associated factor (Paf1) subunit, and RRM proteins
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additional information
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enzyme GCN5b interacts with AP2-domain proteins, apicomplexan plant-like transcription factors, as well as a core complex that includes the co-activator ADA2-A, TFIID subunits, LEO1 polymerase-associated factor (Paf1) subunit, and RRM proteins
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additional information
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TgGCN5b performs autoacetylation. Proteome-wide acetylome analyses of Toxoplasma tachyzoites identifies seven acetylated lysines on TgGCN5b, i.e. K811, K857, K941, K989, K997, K1002, and K1027
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additional information
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TgGCN5b performs autoacetylation. Proteome-wide acetylome analyses of Toxoplasma tachyzoites identifies seven acetylated lysines on TgGCN5b, i.e. K811, K857, K941, K989, K997, K1002, and K1027
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