Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.11.B19 - [histone H3]-trimethyl-L-lysine56 demethylase and Organism(s) Mus musculus and UniProt Accession Q3U2K5

for references in articles please use BRENDA:EC1.14.11.B19
preliminary BRENDA-supplied EC number
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
UNIPROT: Q3U2K5 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
a [histone H3]-N6,N6,N6-trimethyl-L-lysine56
+
3
+
3
=
a [histone H3]-L-lysine56
+
3
+
3
+
3
Synonyms
kdm4dl, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
[histone H3]-N6,N6,N6-trimethyl-L-lysine56,2-oxoglutarate:oxygen oxidoreductase
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[histone H3]-N6,N6,N6-trimethyl-L-lysine56 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine56 + 2 succinate + 2 formaldehyde + 2 CO2
show the reaction diagram
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine56 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine56 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine56 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine56 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
additional information
?
-
trimethylation of H3K56 is removed by members of the JMJD2 family of demethylases that also target H3K9me3, reaction of EC 1.14.11.65
-
-
?
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
[histone H3]-N6,N6,N6-trimethyl-L-lysine56 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine56 + 2 succinate + 2 formaldehyde + 2 CO2
show the reaction diagram
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine56 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine56 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine56 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine56 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
additional information
?
-
trimethylation of H3K56 is removed by members of the JMJD2 family of demethylases that also target H3K9me3, reaction of EC 1.14.11.65
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform JMJD2d
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
embryonic fibroblast cell
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
overexpression of mouse Jmjd2D strongly diminishes [histone H3]-N6,N6,N6-trimethyl-L-lysine9, as well as [histone H3]-N6,N6,N6-trimethyl-L-lysine56 signals, in HeLa Kyoto cells. The loss of the respective trimethyl signal is accompanied with an increase in the monomethyl, but not dimethyl state. the activity is dependent on the enzymatic active jmjC domain
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KDM4D_MOUSE
510
0
57212
Swiss-Prot
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jack, A.P.M.; Bussemer, S.; Hahn, M.; Pnzeler, S.; Snyder, M.; Wells, M.; Csankovszki, G.; Solovei, I.; Schotta, G.; Hake, S.B.
H3K56me3 is a novel, conserved heterochromatic mark that largely but not completely overlaps with H3K9me3 in both regulation and localization
PLoS ONE
8
e51765
2013
Homo sapiens (B2RXH2), Mus musculus (Q3U2K5)
Manually annotated by BRENDA team