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Information on EC 2.3.1.48 - histone acetyltransferase

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EC Tree
     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:
UNIPROT: Q9BQG0
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Word Map
The enzyme appears in 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
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Myb-binding protein 1A
UniProt
acetyltransferase, histone
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histone acetokinase
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histone acetylase
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histone transacetylase
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nucleosome-histone acetyltransferase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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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
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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 H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
show the reaction diagram
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-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
show the reaction diagram
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-
-
?
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 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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the nuclear receptors coactivators
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
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MBB1A_HUMAN
1328
0
148855
Swiss-Prot
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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