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Information on EC 2.3.1.48 - histone acetyltransferase and Organism(s) Drosophila melanogaster and UniProt Accession O02193

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     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.48 histone acetyltransferase
IUBMB Comments
A group of enzymes acetylating histones. Several of the enzymes can also acetylate lysines in other proteins [3,4].
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This record set is specific for:
Drosophila melanogaster
UNIPROT: O02193
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lysine acetyltransferase
-
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 (H4 K16) acetyltransferase
-
-
histone acetokinase
-
-
-
-
histone acetylase
-
-
-
-
histone transacetylase
-
-
-
-
lysine acetyltransferase
-
nucleosome-histone acetyltransferase
-
-
-
-
Tip60
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
9054-51-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
show the reaction diagram
main substrate
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
show the reaction diagram
-
-
-
?
acetyl-CoA + [p53]-L-lysine120
CoA + [p53]-N6-acetyl-L-lysine120
show the reaction diagram
-
-
-
?
acetyl-CoA + [TIP5]-L-lysine
CoA + [TIP5]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
show the reaction diagram
acetyl-CoA + histone H3
CoA + acetylhistone H3
show the reaction diagram
acetyl-CoA + histone H4
CoA + acetylhistone H4
show the reaction diagram
acetyl-CoA + [ATM]-L-lysine
CoA + [ATM]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [c-myc]-L-lysine
CoA + [c-myc]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [DNMT1]-L-lysine
CoA + [DNMT1]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [E2F1]-L-lysine
CoA + [E2F1]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
show the reaction diagram
-
-
-
?
acetyl-CoA + [p53]-L-lysine
CoA + [p53]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [TRRAP]-L-lysine
CoA + [TRRAP]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
show the reaction diagram
-
acetylation of Lys9, and Lys14
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
show the reaction diagram
main substrate
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
show the reaction diagram
-
-
-
?
acetyl-CoA + [p53]-L-lysine120
CoA + [p53]-N6-acetyl-L-lysine120
show the reaction diagram
-
-
-
?
acetyl-CoA + [TIP5]-L-lysine
CoA + [TIP5]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
show the reaction diagram
acetyl-CoA + histone H3
CoA + acetylhistone H3
show the reaction diagram
-
acetylation of Lys9, Lys14, Lys18, Lys23, Lys27, Lys36, and Lys37
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
show the reaction diagram
acetyl-CoA + [ATM]-L-lysine
CoA + [ATM]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [c-myc]-L-lysine
CoA + [c-myc]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [DNMT1]-L-lysine
CoA + [DNMT1]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [E2F1]-L-lysine
CoA + [E2F1]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
show the reaction diagram
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
show the reaction diagram
-
-
-
?
acetyl-CoA + [p53]-L-lysine
CoA + [p53]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [TRRAP]-L-lysine
CoA + [TRRAP]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
show the reaction diagram
-
acetylation of Lys9, and Lys14
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
show the reaction diagram
-
acetylation of Lys5, Lys8, and Lys12, Gcn5 and transcriptional adaptor Ada2a are involved in nucleosomal histone H4 acetylation
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
histone
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histones H2A, H2B, and H3
Polyarginine
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Polyglutamic acid
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potassium phosphate
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90 mM
Triton X-100
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043 - 0.064
anacardic acid
Drosophila melanogaster
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
mushroom bodies, expression of Enok
Manually annotated by BRENDA team
-
tissue culture cell, HTC cells
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
evolution
malfunction
-
aberrant histone acetylation contributes to disease
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MOF_DROME
827
0
92657
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
-
nondenaturing PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
MYST enzymes have their acetylase activity regulated by autoacetylation. Autoacetylation is an important process in modulating the activity of MYST family members
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 hide
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
rapid loss of activity below
487078
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
1 min, irreversible denaturation
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
Tip60 is downregulated in breast cancer
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team