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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.1.1.370 - [histone H3]-lysine4 N-dimethyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9BZ95

for references in articles please use BRENDA:EC2.1.1.370
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This entry describes enzymes that successively methylate the L-lysine4 residue of histone H3 (H3K4) twice, ultimately generating a dimethylated form. These modifications influence the binding of chromatin-associated proteins. The human NSD3 protein also catalyses the activity of EC 2.1.1.hq, [histone H3]-lysine27 N-dimethyltransferase. cf. EC 2.1.1.364, [histone H3]-lysine4 N-methyltransferase, and EC 2.1.1.354, [histone H3]-lysine4 N-trimethyltransferase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q9BZ95
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: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
MEL, NSD3, PFM13, PRDM16, WHISTLE, WHSC1L1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NSD3
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[histone H3]-L-lysine4 N6-dimethyltransferase
This entry describes enzymes that successively methylate the L-lysine4 residue of histone H3 (H3K4) twice, ultimately generating a dimethylated form. These modifications influence the binding of chromatin-associated proteins. The human NSD3 protein also catalyses the activity of EC 2.1.1.hq, [histone H3]-lysine27 N-dimethyltransferase. cf. EC 2.1.1.364, [histone H3]-lysine4 N-methyltransferase, and EC 2.1.1.354, [histone H3]-lysine4 N-trimethyltransferase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + [histone H3]-L-lysine4
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine4
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine4
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine4
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine4
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine4
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine4
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine4
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
S-adenosyl-L-methionine + [histone H3]-L-lysine4
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine4
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine4
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine4
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
physiological function
Nsd3 dimethylates H3K4 and additionally di-, and tri-methylates histones H3K27. Overexpression of Nsd3 represses transcription of the SV40 promoter
physiological function
PRDM16 is a histone H3 K9 methyltransferase on chromatin. Mutation in the N-terminal PR-domain of PRDM16 completely abolishes the intrinsic enzymatic activity of PRDM16. The methyltransferase activity of PRDM16 is required for specific suppression of mixed lineage leukemia leukemogenesis both in vitro and in vivo. PRDM16 directly activates the SNAG family transcription factor GFI1b, which in turn down regulates the HOXA gene cluster. Knockdown GFI1b represses PRDM16-mediated tumor suppression while GFI1b overexpression mimics PRDM16 overexpression. Silencing PRDM16 by DNA methylation is concomitant with mixed lineage leukemia MLL-AF9 induced leukemic transformation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NSD3_HUMAN
1437
0
161613
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C113F/V115G
loss of histone methyltransferase activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
Nsd3 expression is increased in both acute myelogenous leukemia (AML) and acute lymphocytic leukemia (ALL) patients
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, S.M.; Kee, H.J.; Eom, G.H.; Choe, N.W.; Kim, J.Y.; Kim, Y.S.; Kim, S.K.; Kook, H.; Kook, H.; Seo, S.B.
Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity
Biochem. Biophys. Res. Commun.
345
318-323
2006
Homo sapiens (Q9BZ95)
Manually annotated by BRENDA team
Zhou, B.; Wang, J.; Lee, S.Y.; Xiong, J.; Bhanu, N.; Guo, Q.; Ma, P.; Sun, Y.; Rao, R.C.; Garcia, B.A.; Hess, J.L.; Dou, Y.
PRDM16 suppresses MLL1r leukemia via intrinsic histone methyltransferase activity
Mol. Cell
62
222-236
2016
Homo sapiens (Q9HAZ2)
Manually annotated by BRENDA team