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Information on EC 2.3.1.48 - histone acetyltransferase and Organism(s) Drosophila melanogaster
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2.3.1.48 histone acetyltransferaseIUBMB Comments
A group of enzymes acetylating histones. Several of the enzymes can also acetylate lysines in other proteins [3,4].
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Word Map
- 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
-
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
The taxonomic range for the selected organisms is: Drosophila melanogaster
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
clock, histone acetyltransferase, n-acetyltransferase, tip60, histone acetyltransferases, cbp/p300, creb-binding protein, ep300, crebbp, creb binding protein, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyltransferase, histone
-
-
-
-
elongator protein 3
catalytic subunit of the elongator complex
factor acetyltransferase
-
enzyme form A is also able to acetylate nonhistone proteins, mostly transcription factors, overview
FAT
-
when acetylating nonhistone transcription factor proteins, factor specific, overview
histone acetokinase
-
-
-
-
histone acetylase
-
-
-
-
histone transacetylase
-
-
-
-
Mof
MYST1
nucleosome-histone acetyltransferase
-
-
-
-
Tip60
additional information
additional information
-
the enzyme belongs to the MYST family histone acetyltransferases which is divided in three sub-families, overview
additional information
-
type A enzymes are localized in the nuclei and acetylate nucleosomal histones as well as nonhistone proteins, type B enzymes can be found in the cytoplasmic fraction and are responsible for acetylation of newly synthesized histones before their translocation into the nucleus for chromatin assembly during DNA replication
additional information
-
type A enzymes can be grouped into different families based on amino acid sequence comparison and binding motifs, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:[protein]-L-lysine acetyltransferase
A group of enzymes acetylating histones. Several of the enzymes can also acetylate lysines in other proteins [3,4].
CAS REGISTRY NUMBER
COMMENTARY
9054-51-7
-
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
acetyl-CoA + [ATM]-L-lysine
CoA + [ATM]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [c-myc]-L-lysine
CoA + [c-myc]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [DNMT1]-L-lysine
CoA + [DNMT1]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [E2F1]-L-lysine
CoA + [E2F1]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-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-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
?
acetyl-CoA + [p53]-L-lysine
CoA + [p53]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [p53]-L-lysine120
CoA + [p53]-N6-acetyl-L-lysine120
-
-
-
?
acetyl-CoA + [TIP5]-L-lysine
CoA + [TIP5]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [TRRAP]-L-lysine
CoA + [TRRAP]-N6-acetyl-L-lysine
-
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation of Lys9, and Lys14
-
-
?
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 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 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]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
main substrate
-
-
?
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
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys9, Lys14, Lys18, Lys23, Lys27, Lys36, and Lys37
-
-
?
acetyl-CoA + [ATM]-L-lysine
CoA + [ATM]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [c-myc]-L-lysine
CoA + [c-myc]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [DNMT1]-L-lysine
CoA + [DNMT1]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [E2F1]-L-lysine
CoA + [E2F1]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-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-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
?
acetyl-CoA + [p53]-L-lysine
CoA + [p53]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [p53]-L-lysine120
CoA + [p53]-N6-acetyl-L-lysine120
-
-
-
?
acetyl-CoA + [TIP5]-L-lysine
CoA + [TIP5]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [TRRAP]-L-lysine
CoA + [TRRAP]-N6-acetyl-L-lysine
-
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation of Lys9, and Lys14
-
-
?
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
-
-
?
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 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 of Lys5, Lys8, Lys12, and Lys16
-
-
?
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
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
the enzyme belongs to the MYST family. The MYST family takes its name from the first identified members: (MOZ, KAT6A), Ybf2 (Sas3, KAT6), something about silencing (Sas2, KAT8) and Tat-interacting protein (Tip60, KAT5). To date, five human KATs have been identified in this family: MOZ, MOZ related factor (MORF, KAT6B), Tip60, HAT bound to ORC1 (HBO1, KAT7) and males absent on the first (MOF, KAT8 or MYST 1), the functional orthologue of yeast's Sas2. The defining feature of MYST family is the presence of the highly conserved MYST domain. MYST enzymes possess a highly-conserved acetyl-CoA-binding motif A within the catalytic domain. Additionally, some family members have also structural features in common with one another, such as chromodomains or plant homeodomain-linked zinc fingers. The members of this family utilize a double displacement (or ping-pong) catalytic mechanism. Autoacetylation is an important process in modulating the activity of MYST family members
evolution
the enzyme TAF1/TBP belongs to the components of transcription factor complexes
physiological function
-
genome-wide increase in histone acetylation stimulates replication independently of transcription in follicle cells. Enok is essential for mushroom body development, the mushroom bodies are the sites of olfactory learning and memory and in this function equivalent to the mammalian brain. Mof is required for sex chromosome dosage compensation acting in the MSL complex
physiological function
-
MYST1 plays a role in tumor suppression mechanisms, functional composition and mechanisms of MYST1-containing complexes, overviewS
physiological function
targeted reduction of ELP3 specifically in the developing Drosophila nervous system leads to a hyperactive phenotype with increase in climbing and locomotor activities and sleep loss in the adult flies, a significant expansion in synaptic bouton number and axonal length and branching in the larval neuromuscular junction as well as the misregulation of genes involved in sleep, vesicle transport and fusion, and protein chaperone activity. Ubiquitous reduction of ELP3 results in lethality
physiological function
-
regulation of histone acetylation is fundamental to the utilization of eukaryotic genomes in chromatin. H4K16 acetylation is thought to affect the basic properties of the chromatin fiber. Male cells display twice the amount of H4K16 acetylation but reduced levels of several other acetylation motifs including H4K5, H4K12, and H3K14 acetylation as compared to female cells due to acetyltransferase MOF. Drosophila's histone acetylation system includes (1) the extensively studied model KATs (GCN5/PCAF, CBP/P300, MOF, HAT1, and TIP60), (2) less well characterized KATs (KAT6 [MOZ/MORF], HBO1, ELP3, TAF1, and ATAC2), (3) a mostly uncharacterized class of GCN5-related KATs (NAT6, NAT9, and NAT10), (4) N-terminal acetyltransferases suggested to also acetylate internal lysines (NAA10, NAA20, NAA30, NAA40, NAA50, and NAA60), (5) putative acetyltransferases with no recognizable direct homologue in non-Drosophilid species (CG5783 and CG12560), (6) the acetyltransferase ECO, and (7) a bifunctional enzyme containing a O-GlcNAcase activity and potentially a KAT activity (MGEA5, also known as NCOAT or OGA)
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. MYST enzymes have their acetylase activity regulated by autoacetylation. Tip60 activates the machinery for DNA repair
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. TAF1 is a regulatory element in hormone-related transcriptional processes
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MOF catalyzes the acetylation of p53 at lysine120, which helps to discriminate cell-cycle arrest and apoptotic functions. MYST enzymes have their acetylase activity regulated by autoacetylation
additional information
-
development of a quantitative proteomic strategy to generate a comprehensive catalog of combinatorial histone acetylation and methylation motifs in Drosophila cells, acetylation patterns and their genesis by integrated enzyme activities, e.g. via enzymes MOF, RPD3, KAT6, NAA10, and GCN5, overview
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NAA60_DROME
276
1
31869
Swiss-Prot
other Location (Reliability: 2)
TIP60_DROME
541
0
61234
Swiss-Prot
other Location (Reliability: 1)
MOF_DROME
827
0
92657
Swiss-Prot
other Location (Reliability: 1)
Q7K3G5_DROME
497
0
55234
TrEMBL
other Location (Reliability: 2)
B1A1N4_DROME
122
0
14104
TrEMBL
other Location (Reliability: 2)
I1V4X5_DROME
827
0
92932
TrEMBL
other Location (Reliability: 1)
B1A1M9_DROME
122
0
14063
TrEMBL
other Location (Reliability: 2)
A0A0B4KEC3_DROME
496
0
55177
TrEMBL
other Location (Reliability: 2)
B1A1N0_DROME
122
0
13957
TrEMBL
other Location (Reliability: 2)
B1A1N2_DROME
122
0
14031
TrEMBL
other Location (Reliability: 2)
D0IQI5_DROME
1092
0
123446
TrEMBL
other Location (Reliability: 2)
B1A1T0_DROME
122
0
14137
TrEMBL
other Location (Reliability: 2)
M9PHL0_DROME
2006
0
212726
TrEMBL
other Location (Reliability: 2)
B1A1M6_DROME
122
0
14121
TrEMBL
other Location (Reliability: 2)
M9PH08_DROME
473
0
53049
TrEMBL
other Location (Reliability: 1)
B1A1P4_DROME
122
0
14131
TrEMBL
other Location (Reliability: 2)
B1A1N8_DROME
122
0
14010
TrEMBL
other Location (Reliability: 2)
M9NEW2_DROME
703
0
77145
TrEMBL
other Location (Reliability: 2)
Q9VTZ1_DROME
813
0
92169
TrEMBL
other Location (Reliability: 1)
Q9W1A9_DROME
2291
0
254682
TrEMBL
other Location (Reliability: 2)
M9MS40_DROME
3282
0
341431
TrEMBL
other Location (Reliability: 1)
B1A1T8_DROME
122
0
14174
TrEMBL
other Location (Reliability: 2)
Q9VAV6_DROME
421
0
48425
TrEMBL
other Location (Reliability: 1)
Q4QQC4_DROME
405
0
47977
TrEMBL
other Location (Reliability: 2)
M9PH39_DROME
3266
0
339679
TrEMBL
other Location (Reliability: 1)
Q9W321_DROME
3276
0
340728
TrEMBL
other Location (Reliability: 1)
B1A1N5_DROME
122
0
14104
TrEMBL
other Location (Reliability: 1)
Q9VJ73_DROME
774
0
89175
TrEMBL
other Location (Reliability: 2)
B1A1Q0_DROME
122
0
14123
TrEMBL
other Location (Reliability: 2)
Q9VID9_DROME
2663
0
292562
TrEMBL
other Location (Reliability: 2)
A0A0B4K602_DROME
2172
0
244125
TrEMBL
other Location (Reliability: 2)
A1Z6E6_DROME
495
0
55120
TrEMBL
other Location (Reliability: 2)
M9PGN1_DROME
541
0
61234
TrEMBL
other Location (Reliability: 1)
M9PI16_DROME
2012
0
213288
TrEMBL
other Location (Reliability: 2)
Q7YTZ9_DROME
538
0
62229
TrEMBL
other Location (Reliability: 4)
B1A1Q9_DROME
122
0
14105
TrEMBL
other Location (Reliability: 2)
O76216_DROME
813
0
92096
TrEMBL
other Location (Reliability: 1)
O01368_DROME
3190
0
331878
TrEMBL
other Location (Reliability: 1)
Q0E9P4_DROME
339
0
36764
TrEMBL
other Location (Reliability: 1)
B1A1S4_DROME
122
0
14131
TrEMBL
other Location (Reliability: 2)
Q9VM15_DROME
811
0
89625
TrEMBL
other Location (Reliability: 2)
B1A1M5_DROME
122
0
14061
TrEMBL
other Location (Reliability: 2)
B1A1R1_DROME
122
0
14122
TrEMBL
other Location (Reliability: 2)
B1A1R2_DROME
122
0
14118
TrEMBL
other Location (Reliability: 2)
B1A1T3_DROME
122
0
14131
TrEMBL
other Location (Reliability: 2)
Q0KIB3_DROME
405
0
47947
TrEMBL
other Location (Reliability: 2)
B1A1Q6_DROME
122
0
14107
TrEMBL
other Location (Reliability: 2)
M9PHZ0_DROME
2011
0
213383
TrEMBL
other Location (Reliability: 2)
Q9NHW0_DROME
811
0
89656
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylation
MYST enzymes have their acetylase activity regulated by autoacetylation. Autoacetylation is an important process in modulating the activity of MYST family members
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E355stop
-
site-directed mutagenesis of the Gn5 gene, inactive mutant, the loss of either dGcn5 or dAda2a function results in similar chromosome structural and developmental defects, in dAda2a mutants, the nucleosomal H4 acetylation at lysines 12 and 5 is significantly reduced, while the acetylation established by dAda2b-containing Gcn5 complexes at H3 lysines 9 and 14 is unaffected, overview
additional information
additional information
-
Both an enok null allele and a point mutation in the zinc finger of the MYST histone acetyltransferase domain cause an arrest in neuroblast proliferation. Enok mutation also results in a slow, but steady decline of egg production over time. However, no difference occurs in the proliferation of wing disk cells. Effects of mutating mof in flies are certainly most pronounced at and most relevant to the male X chromosome. Null mutation of the Hbo1 homologue in Drosophila melanogaster, chameau, leads to lethality at the pupal stage. Haploinsufficiency for chameau leads to defects in position effect variegation, in polycomb group protein mediated repression of homeotic genes and consequent homeotic transformation in thoracic and abdominal segments. Compound heterozygous flies for chameau and the PcG genes polycomb, polyhomeotic, or a mutation in a polycomb response element, Mcp, show more pronounced homeotic transformation than heterozygotes of the PcG genes alone. Depletion of Tip60 by RNAi leads to developmental lethality before or at the early pupal stage
additional information
-
MOF levels are strongly diminished after incubating cells for 4 days with interfering RNAs directed against MOF transcript, and are undetectable after 5.5 days
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dGN5, genetic crosses and phenotype analysis, overview, determination of genetic interaction of dGcn5 and dAda2a
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wiegand, R.C.; Brutlag, D.L.
Histone acetylase from Drosophila melanogaster specific for H4
J. Biol. Chem.
256
4578-4583
1981
Drosophila melanogaster
Hasan, S.; Hottiger, M.O.
Histone acetyl transferases: a role in DNA repair and DNA replication
J. Mol. Med.
80
463-474
2002
Arabidopsis thaliana, Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Mus musculus, Tetrahymena thermophila, Homo sapiens GCN5
Ciurciu, A.; Komonyi, O.; Pankotai, T.; Boros, I.M.
The Drosophila histone acetyltransferase Gcn5 and transcriptional adaptor Ada2a are involved in nucleosomal histone H4 acetylation
Mol. Cell. Biol.
26
9413-9423
2006
Drosophila melanogaster
Dmitriev, R.I.; Shakhparonov, M.I.; Pestov, N.B.
Structure and function of MYST1 histone acetyltransferase in the interactome of animal cells
Biochemistry (Moscow)
73
839-852
2008
Drosophila melanogaster, Homo sapiens (Q9H7Z6)
Voss, A.K.; Thomas, T.
MYST family histone acetyltransferases take center stage in stem cells and development
Bioessays
31
1050-1061
2009
Arabidopsis thaliana, Danio rerio, Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Danio rerio zMoz
Singh, N.; Lorbeck, M.T.; Zervos, A.; Zimmerman, J.; Elefant, F.
The histone acetyltransferase Elp3 plays in active role in the control of synaptic bouton expansion and sleep in Drosophila
J. Neurochem.
115
493-504
2010
Drosophila melanogaster (Q9VQZ6)
Feller, C.; Forne, I.; Imhof, A.; Becker, P.B.
Global and specific responses of the histone acetylome to systematic perturbation
Mol. Cell
57
559-571
2015
Drosophila melanogaster
Fiorentino, F.; Mai, A.; Rotili, D.
Lysine acetyltransferase inhibitors structure-activity relationships and potential therapeutic implications
Future Med. Chem.
10
1067-1091
2018
Drosophila melanogaster (O02193), Drosophila melanogaster (P51123), Drosophila melanogaster (Q960X4), Homo sapiens (O15516), Homo sapiens (O95251), Homo sapiens (P21675), Homo sapiens (Q15788), Homo sapiens (Q8WYB5), Homo sapiens (Q92793), Homo sapiens (Q92794), Homo sapiens (Q92830), Homo sapiens (Q92831), Homo sapiens (Q92993), Homo sapiens (Q9BQG0), Homo sapiens (Q9H7Z6), Homo sapiens (Q9H9T3), Homo sapiens (Q9UKN8), Homo sapiens (Q9Y6Q9), Homo sapiens, Saccharomyces cerevisiae (P39979), Saccharomyces cerevisiae (P46677), Saccharomyces cerevisiae (P53114), Saccharomyces cerevisiae (Q06592), Saccharomyces cerevisiae (Q07794), Saccharomyces cerevisiae ATCC 204508 (P39979), Saccharomyces cerevisiae ATCC 204508 (P46677), Saccharomyces cerevisiae ATCC 204508 (P53114), Saccharomyces cerevisiae ATCC 204508 (Q06592), Saccharomyces cerevisiae ATCC 204508 (Q07794)
EXTERNAL LINKS (specific for EC-Number 2.3.1.48)
Transporter Classification Database (TCDB): 1.I.1.1.3
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