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Information on EC 2.1.1.356 - [histone H3]-lysine27 N-trimethyltransferase and Organism(s) Mus musculus and UniProt Accession Q61188

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IUBMB Comments
This entry describes enzymes that successively methylate the L-lysine27 residue of histone H3 (H3K27), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. The methylation of lysine27 leads to transcriptional repression of the affected target genes. The enzyme associates with other proteins to form a complex that is essential for activity. The enzyme can also methylate some non-histone proteins. cf. EC 2.1.1.369, [histone H3]-lysine27 N-methyltransferase and EC 2.1.1.371, [histone H3]-lysine27 N-dimethyltransferase.
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This record set is specific for:
Mus musculus
UNIPROT: Q61188
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
polycomb repressive complex 2, re-iibp, histone h3 lysine 27 methyltransferase, set domain histone lysine methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EZH2
catalytic subunit
Polycomb repressive complex 2
-
EZH1
-
-
-
-
EZH2
-
-
-
-
KMT6A
-
-
-
-
KMT6B
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[histone H3]-L-lysine27 N6-methyltransferase
This entry describes enzymes that successively methylate the L-lysine27 residue of histone H3 (H3K27), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. The methylation of lysine27 leads to transcriptional repression of the affected target genes. The enzyme associates with other proteins to form a complex that is essential for activity. The enzyme can also methylate some non-histone proteins. cf. EC 2.1.1.369, [histone H3]-lysine27 N-methyltransferase and EC 2.1.1.371, [histone H3]-lysine27 N-dimethyltransferase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
show the reaction diagram
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
show the reaction diagram
-
-
-
?
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
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
show the reaction diagram
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
enzyme depletion leads to heterochromatin protein 1alpha loss from chromatin and degradation
physiological function
the enzyme and H3K27me3 cooperate with [histone H3]-L-lysine27 methylation to maintain heterochromatin protein 1alpha at chromatin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
EZH2_MOUSE
746
0
85292
Swiss-Prot
other Location (Reliability: 2)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boros, J.; Arnoult, N.; Stroobant, V.; Collet, J.F.; Decottignies, A.
Polycomb repressive complex 2 and H3K27me3 cooperate with H3K9 methylation to maintain heterochromatin protein 1alpha at chromatin
Mol. Cell. Biol.
34
3662-3674
2014
Mus musculus (Q61188), Mus musculus
Manually annotated by BRENDA team