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Information on EC 2.1.1.359 - [histone H3]-lysine36 N-trimethyltransferase
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2.1.1.359 [histone H3]-lysine36 N-trimethyltransferaseIUBMB Comments
The enzyme, characterized from yeast and mammals, catalyses the successive methylation of lysine36 of histone H3 (H3K36), forming the trimethylated form. These modifications influence the binding of chromatin-associated proteins. The enzyme couples the methylation reactions with transcriptional elongation through an interaction with the large subunit of RNA polymerase II. cf. EC 2.1.1.357, [histone H3]-lysine36 N-dimethyltransferase.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
met-1, histone lysine methyltransferases, set domain containing 2, wolf-hirschhorn syndrome candidate 1, sdg725, histone h3k36 methyltransferase, h3k36 trimethyltransferase, set domain containing protein 2, kmt3a, pr domain-containing protein 9, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ASHH2
EC 2.1.1.358
-
-
formerly
-
EC 2.1.1.43
-
-
formerly, part transferred
-
H3 K36 methyltransferase
H3K36 trimethyltransferase
H3K36-specific methyltransferase
H3K36me3 methyltransferase
histone H3 lysine 36 methyltransferase
histone methyltransferase
HMTase
HSPC069
HYPB
KMT3A
NSD2
SET2
SETD2
Whsc1
Wolf-Hirschhorn Syndrome candidate 1
SET2
-
-
-
-
SETD2
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
-
S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
(1a)
-
-
-
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
(1c)
-
-
-
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
(1b)
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[histone H3]-L-lysine36 N6-trimethyltransferase
The enzyme, characterized from yeast and mammals, catalyses the successive methylation of lysine36 of histone H3 (H3K36), forming the trimethylated form. These modifications influence the binding of chromatin-associated proteins. The enzyme couples the methylation reactions with transcriptional elongation through an interaction with the large subunit of RNA polymerase II. cf. EC 2.1.1.357, [histone H3]-lysine36 N-dimethyltransferase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + [histone H4]-L-lysine44
2 S-adenosyl-L-homocysteine + [histone H4]-N6,N6-dimethyl-L-lysine44
histone H4 lysine-44 is the primary target of NSD2 in the case of octamer substrates, irrespective of the histones being native or recombinant
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
3 S-adenosyl-L-methionine + [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine36
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-methionine + chicken nucleosome
S-adenosyl-L-homocysteine + chicken nucleosome N6-methyl-L-lysine
-
-
-
?
S-adenosyl-L-methionine + histone H3(K36)
S-adenosyl-L-homocysteine + histone H3(K36) N6-methyl-L-lysine
S-adenosyl-L-methionine + histone H3(peptide 21-44)
S-adenosyl-L-homocysteine + histone H3(peptide21-44) N6-methyl-L-lysine
-
-
-
?
S-adenosyl-L-methionine + recombinant nucleosome
S-adenosyl-L-homocysteine + recombinant nucleosome N6-methyl-L-lysine
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine36
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine36
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction. Trimethylation of [histone H3]-L-lysine36 by the enzyme is directed through its association with the phosphorylated repeats of the RNA polymerase C-terminal domain
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + histone H3(K36)
?
-
histone H3(K36) di- and trimethylation
-
-
?
S-adenosyl-L-methionine + histone H3(K36)
?
the enzyme has histone methyltransferase activity specifically towards mono-, di- and trimethylation of histone H3(K36) residues both in vitro and in vivo
-
-
?
S-adenosyl-L-methionine + histone H3(K36)
?
NSD2 shows specific targeting of histone H3 lysine-36, DNA acts as an allosteric effector of NSD2 such that H3K36 becomes the preferred target
-
-
?
S-adenosyl-L-methionine + histone H3(K36)
?
-
SDG724 mediates histone H3(K36)me2/3 deposition at MADS50 and RFT1
-
-
?
S-adenosyl-L-methionine + histone H3(K36)
S-adenosyl-L-homocysteine + histone H3(K36) N6-methyl-L-lysine
-
di- and trimethylation of resdídue K36
-
?
S-adenosyl-L-methionine + histone H3(K36)
S-adenosyl-L-homocysteine + histone H3(K36) N6-methyl-L-lysine
-
-
-
?
S-adenosyl-L-methionine + histone H3(K36)
S-adenosyl-L-homocysteine + histone H3(K36) N6-methyl-L-lysine
-
-
transfer of three methyl groups
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine36
highest activity
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
additional information
?
-
-
SETD2 downregulates human ortholog of murine double min 2 protein expression by targeting its P2 promoter and then enhances p53 protein stability, enhances the transcriptional activity of p53, and regulates expression of select p53 target genes
-
-
?
additional information
?
-
enzyme mono- and dimethylates H3K36 and is inactive with H3K4 as substrate. Nucleosome containing histone H3 mutant K36A is not a substrate. Isoform SETD2 is able to trimethylate H3K36 in vitro
-
-
?
additional information
?
-
no activity with unmethylated/methylated [histone H3]-L-lysine27 and [histone H3]-L-lysine20 as well as trimethylated [histone H3]-L-lysine4 and [histone H3]-L-lysine36 peptides
-
-
?
additional information
?
-
the enzyme also efficiently trimethylates [histone H3]-L-lysine4
-
-
?
additional information
?
-
no activity with [histone H3]-L-lysine9 and [histone H3]-L-lysine4
-
-
?
additional information
?
-
-
SDG724 prefers oligonucleosomes rather than core histones as a substrate
-
-
?
additional information
?
-
-
Asf1 stimulates the enzyme occupancy of the coding region of a highly transcribed gene by a mechanism that depends on Asf1 binding to histone H3/H4. This function of Asf1 promotes the switch from di- to trimethylation of histone H3 lysine 36 at that gene
-
-
?
additional information
?
-
the enzyme associates with the phosphorylated C-terminal domain of RNA polymerase II
-
-
?
additional information
?
-
-
Asf1 stimulates the enzyme occupancy of the coding region of a highly transcribed gene by a mechanism that depends on Asf1 binding to histone H3/H4. This function of Asf1 promotes the switch from di- to trimethylation of histone H3 lysine 36 at that gene
-
-
?
additional information
?
-
the enzyme associates with the phosphorylated C-terminal domain of RNA polymerase II
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
3 S-adenosyl-L-methionine + [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine36
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-methionine + histone H3(K36)
?
-
SDG724 mediates histone H3(K36)me2/3 deposition at MADS50 and RFT1
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine36
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine36
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction. Trimethylation of [histone H3]-L-lysine36 by the enzyme is directed through its association with the phosphorylated repeats of the RNA polymerase C-terminal domain
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
3 S-adenosyl-L-methionine + [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine36
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine36
highest activity
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
-
?
additional information
?
-
no activity with unmethylated/methylated [histone H3]-L-lysine27 and [histone H3]-L-lysine20 as well as trimethylated [histone H3]-L-lysine4 and [histone H3]-L-lysine36 peptides
-
-
?
additional information
?
-
the enzyme also efficiently trimethylates [histone H3]-L-lysine4
-
-
?
additional information
?
-
no activity with [histone H3]-L-lysine9 and [histone H3]-L-lysine4
-
-
?
additional information
?
-
-
SDG724 prefers oligonucleosomes rather than core histones as a substrate
-
-
?
additional information
?
-
-
Asf1 stimulates the enzyme occupancy of the coding region of a highly transcribed gene by a mechanism that depends on Asf1 binding to histone H3/H4. This function of Asf1 promotes the switch from di- to trimethylation of histone H3 lysine 36 at that gene
-
-
?
additional information
?
-
-
Asf1 stimulates the enzyme occupancy of the coding region of a highly transcribed gene by a mechanism that depends on Asf1 binding to histone H3/H4. This function of Asf1 promotes the switch from di- to trimethylation of histone H3 lysine 36 at that gene
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
histone H4
in the presence of histone H4, there is a 5-7fold increase in enzyme activity on histone H3
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0033
S-adenosyl-L-methionine
cosubstrate recombinant nucleosome, pH 9.0, 23°C
0.004
S-adenosyl-L-methionine
cosubstrate chicken nucleosome, pH 9.0, 23°C
0.0055
S-adenosyl-L-methionine
cosubstrate histone H3(peptide 21-44), pH 9.0, 23°C
0.062
S-adenosyl-L-methionine
with [histone H3]-N6,N6-dimethyl-L-lysine36 as cosubstrate, at pH 8.5 and 23°C
0.087
S-adenosyl-L-methionine
with [histone H3]-L-lysine36 as cosubstrate, at pH 8.5 and 23°C
0.13
S-adenosyl-L-methionine
with [histone H3]-N6-methyl-L-lysine36 as cosubstrate, at pH 8.5 and 23°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
ashh2 mutants are defective in ovule and embryo sac development, mutation in ASHH2 leads to substantial changes in inflorescence gene expression
malfunction
-
ASH1 knockdown causes reduced expression of Hox genes. Knockdown of ASH1 in K-562 cells in vitro causes increased expression of epsilon-globin gene and reduced expression of myelomonocytic markers GPIIb and GPIIIa, whereas knockdown of ASH1 in haematopoietic stem cells in vivo results in decreased number of macrophages and granulocytes
malfunction
-
mutations in enzyme SDG724 are responsible for the late-flowering phenotype of late-flowering long vegetative phase 1 plants
malfunction
cells lacking the enzyme display microsatellite instability and an elevated spontaneous mutation frequency, characteristic of DNA mismatch repair-deficient cells. Enzyme-deficient cells fail to recruit MutSalpha to chromatin
malfunction
enzyme downregulation leads to higher RNA polymerase II turnover at the transcription site and leads to intragenic transcription initiation in human cells
malfunction
-
enzyme knockdown affects processing of late viral RNAs
malfunction
enzyme knockdown in human endothelial cells impairs migration and tubule formation activities
malfunction
enzyme knockdown leads to defective repair of DNA double-strand breaks via the homologous recombination pathway
malfunction
enzyme knockdown significantly reduces survival after treatment with mitomycin C, camptothecin, or ionizing radiation in U2OS cells and HeLa cells
malfunction
enzyme loss is associated with alterations in mRNA splicing in human clear cell renal cell carcinoma
malfunction
-
enzyme mutants display pleiotropic defects, including typical brassinosteroid-deficient morphologies and late flowering associated with the down-regulation of the brassinosteroid pathway and flowering regulatory genes
malfunction
enzyme mutations are associated with Wolf-Hirschhorn syndrome, which is characterized by skeletal abnormalities. Enzyme-deficient embryos exhibit defects in ossification in the occipital bone and sternum. Enzyme knockdown in pre-osteoblast cells perturbs histone modification patterns in bone-related genes and leads to defects in bone differentiation
malfunction
enzyme silencing impairs the interaction between N6-methyladenosine methyltransferase complex proteins and their target mRNAs
malfunction
enzyme-deficient mice show growth retardation and various Wolf-Hirschhorn syndrome-like midline defects, including congenital cardiovascular anomalies
malfunction
homozygous disruption of the enzyme gene impairs [histone H3]-L-lysine36 trimethylation but not mono- or dimethylation, and results in embryonic lethality at E10.5-E11.5. Severe vascular defects are observed in the enzyme-deficient embryo, yolk sac, and placenta
malfunction
-
inactivation of the enzyme results in a decrease in global [histone H3]-N6,N6,N6-trimethyl-L-lysine36 marks, an increase in mRNA expression change with age, and a shortened life span
malfunction
loss-of function mutants show a dramatically reduced level of histone H3 lysine 36 dimethylation and have an early-flowering phenotype
malfunction
reduction of histone H3 lysine 36 trimethylation is lethal in Drosophila larvae and leads to elevated levels of acetylation, specifically at lysine 16 of histone H4
physiological function
-
the main requirement of ASHH2 is in the sporophyte for proper development or function of ovules and anthers, ASHH2 is required for normal embryo-sac development, anther differentiation, tapetum development and pollen maturation
physiological function
-
ASH1 regulates endogenous Hox gene expression positively and negatively and is required for myelomonocytic differentiation. ASH1 and MLL1 co-operate in Hox promoter activation
physiological function
-
SDG724 promotes flowering in rice. The enzyme Is required in the MADS50-Ehd1-RFT1 flowering pathway under long-day conditions and promotes the MADS51-Ehd1-Hd3a flowering pathway under short-day conditions
physiological function
the enzyme plays roles as an activator of general transcription and inhibits cell viability by inducing caspase-3 activation overexpression
physiological function
histone lysine methyltransferase SDG8 is involved in brassinosteroid-regulated gene expression. Transcription factor BES1 interacts with SDG8, directly or indirectly through IWS1, a transcription elongation factor involved in brassinosteroid-regulated gene expression. The knockout mutant sdg8 displays a reduced growth phenotype with compromised brassinosteroid responses. While brassinosteroids regulate about 5000 genes in wild-type plants, the hormone regulates fewer than 700 genes in SDG8 mutant. More than half of brassinosteroid-regulated genes are differentially affected in SDG8 mutant
physiological function
-
Whsc1-/- embryos exhibit defects in ossification in the occipital bone and sternum. Whsc1 knockdown in pre-osteoblast cells perturbs histone modification patterns in bone-related genes and leads to defects in bone differentiation. Whsc1 increases the association of p300 with Runx2, activating the bone-related genes osteopontin and collagen type Ia, and Whsc1 suppresses the overactivation of these genes via H3K36 trimethylation
physiological function
histone H3 trimethylation at lysine 36 by the enzyme guides m6A RNA modification co-transcriptionally
physiological function
enzyme-dependent histone H3 lysine 36 trimethylation is required for homologous recombination repair and genome stability. The enzyme plays a presynaptic role for in homologous recombination, where it facilitates the recruitment of C-terminal binding protein interacting protein and promotes DNA double-strand break resection, allowing replication protein A and RAD51 binding to DNA damage sites
physiological function
enzyme-mediated histone H3 lysine 36 trimethylation is implicated in the regulation of alternative splicing and DNA mismatch repair
physiological function
the enzyme coordinates FACT complex-mediated exchange of histone H2B during transcription-coupled nucleosome displacement. The enzyme activity modulates FACT recruitment and nucleosome dynamics, thereby repressing cryptic transcription initiation
physiological function
the enzyme is essential for Drosophila melanogaster development
physiological function
-
the enzyme is involved in controlling flowering time in rice
physiological function
the enzyme is required for embryonic vascular remodeling
physiological function
the enzyme is required for the appropriate transcription of Nkx2-5-dependent genes
physiological function
the enzyme is required for viability and methylation of [histone H3]-L-lysine36 in Drosophila melanogaster
physiological function
the enzyme plays an important role in stimulating [histone H3]-N6,N6,N6-trimethyl-L-lysine36 at a specifically generated DNA double-strand breaks site
physiological function
the enzyme regulates gene expression through Runt-related transcription factor 2, a transcription factor central to bone development, and p300, a histone acetyltransferase, to promote bone differentiation. The enzyme fine-tunes the expression of bone-related genes by acting as a modulator in balancing histone H3 lysine 36 trimethylation and histone acetylation. The enzyme is involved in osteoblast differentiation but not proliferation
physiological function
-
the enzyme regulates the viral life cycle through the recruitment of [histone H3]-N6,N6,N6-trimethyl-L-lysine36 readers to viral DNA and contributes to a productive viral replication
physiological function
-
the enzyme regulates the viral life cycle through the recruitment of [histone H3]-N6,N6,N6-trimethyl-L-lysine36 readers to viral DNA and contributes to a productive viral replication
physiological function
the interaction between Set2 and histone H4 mediates trans-histone regulation of histone H3 lysine 36 methylation, which is needed for the preventative maintenance and integrity of the genome
physiological function
-
the interaction between Set2 and histone H4 mediates trans-histone regulation of histone H3 lysine 36 methylation, which is needed for the preventative maintenance and integrity of the genome
-
Show AA Sequence and Transmembrane Helices (1465 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ubiquitination
the speckle-type POZ protein/cullin 3 complex polyubiquitinates and regulates the stability of the enzyme in vivo and in vitro
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R1625C
the mutation results in a complete loss of histone H3 lysine 36 trimethylation activity. The mutant shows unchanged thermal stability as compared with the wild type protein but diminished binding to the histone H3 tail
R2510H
the mutation does not result in an observable defect in enzymatic function
R195C
the mutation results in a complete loss of histone H3 lysine 36 trimethylation activity but does not affect dimethylated histone H3 lysine 36
D329A
-
the mutant shows strongly decreased activity compared to the wild type enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
yeast mutants defective in RNA polymerase C-terminal domain phosphorylation at serine 2 show a destabilization of enzyme protein levels and histone H3 lysine 36 methylation
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Hi-Trap column chromatography, Source30Q column chromatography, and Superdex S200 gel filtration
Ni-NTA bead chromatography, glutathione bead chromatography, and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
GST-SET domain fusion proteins are expressed in Escherichia coli, SET2-C is expressed in baculovirus insect cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme levels are increased in human papillomavirus-positive foreskin keratinocytes
enzyme levels are increased in human papillomavirus-positive foreskin keratinocytes
-
enzyme levels are increased in human papillomavirus-positive foreskin keratinocytes
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xie, P.; Tian, C.; An, L.; Nie, J.; Lu, K.; Xing, G.; Zhang, L.; He, F.
Histone methyltransferase protein SETD2 interacts with p53 and selectively regulates its downstream genes
Cell. Signal.
20
1671-1678
2008
Homo sapiens
brenda
Li, Y.; Trojer, P.; Xu, C.F.; Cheung, P.; Kuo, A.; Drury, W.J.; Qiao, Q.; Neubert, T.A.; Xu, R.M.; Gozani, O.; Reinberg, D.
The target of the NSD family of histone lysine methyltransferases depends on the nature of the substrate
J. Biol. Chem.
284
34283-34295
2009
Homo sapiens (O96028), Homo sapiens (Q9BYW2), Homo sapiens
brenda
Grini, P.; Thorstensen, T.; Alm, V.; Vizcay-Barrena, G.; Windju, S.; Jorstad, T.; Wilson, Z.; Aalen, R.
The ASH1 HOMOLOG 2 (ASHH2) histone H3 methyltransferase is required for ovule and anther development in Arabidopsis
PLoS ONE
4
e7817
2009
Arabidopsis thaliana
brenda
Kim, D.W.; Kim, K.B.; Kim, J.Y.; Seo, S.B.
Characterization of a novel histone H3K36 methyltransferase setd3 in zebrafish
Biosci. Biotechnol. Biochem.
75
289-294
2011
Danio rerio (Q7SXS7), Danio rerio
brenda
Sun, C.; Fang, J.; Zhao, T.; Xu, B.; Zhang, F.; Liu, L.; Tang, J.; Zhang, G.; Deng, X.; Chen, F.; Qian, Q.; Cao, X.; Chu, C.
The histone methyltransferase SDG724 mediates H3K36me2/3 deposition at MADS50 and RFT1 and promotes flowering in rice
Plant Cell
24
3235-3247
2012
Oryza sativa Indica Group
brenda
Tanaka, Y.; Kawahashi, K.; Katagiri, Z.; Nakayama, Y.; Mahajan, M.; Kioussis, D.
Dual function of histone H3 lysine 36 methyltransferase ASH1 in regulation of Hox gene expression
PLoS ONE
6
e28171
2011
Homo sapiens
brenda
Eram, M.S.; Kuznetsova, E.; Li, F.; Lima-Fernandes, E.; Kennedy, S.; Chau, I.; Arrowsmith, C.H.; Schapira, M.; Vedadi, M.
Kinetic characterization of human histone H3 lysine 36 methyltransferases, ASH1L and SETD2
Biochim. Biophys. Acta
1850
1842-1848
2015
Homo sapiens (Q9BYW2)
brenda
Wang, X.; Chen, J.; Xie, Z.; Liu, S.; Nolan, T.; Ye, H.; Zhang, M.; Guo, H.; Schnable, P.S.; Li, Z.; Yin, Y.
Histone lysine methyltransferase SDG8 is involved in brassinosteroid-regulated gene expression in Arabidopsis thaliana
Mol. Plant
7
1303-1315
2014
Arabidopsis thaliana (Q2LAE1)
brenda
Lee, Y.F.; Nimura, K.; Lo, W.N.; Saga, K.; Kaneda, Y.
Histone H3 lysine 36 methyltransferase Whsc1 promotes the association of Runx2 and p300 in the activation of bone-related genes
PLoS ONE
9
e106661
2014
Mus musculus
brenda
Li, F.; Mao, G.; Tong, D.; Huang, J.; Gu, L.; Yang, W.; Li, G.M.
The histone mark H3K36me3 regulates human DNA mismatch repair through its interaction with MutSalpha
Cell
153
590-600
2013
Homo sapiens (Q9BYW2), Homo sapiens
brenda
Pfister, S.X.; Ahrabi, S.; Zalmas, L.P.; Sarkar, S.; Aymard, F.; Bachrati, C.Z.; Helleday, T.; Legube, G.; La Thangue, N.B.; Porter, A.C.; Humphrey, T.C.
SETD2-dependent histone H3K36 trimethylation is required for homologous recombination repair and genome stability
Cell Rep.
7
2006-2018
2014
Homo sapiens (Q9BYW2)
brenda
Zhang, K.; Haversat, J.M.; Mager, J.
CTR9/PAF1c regulates molecular lineage identity, histone H3K36 trimethylation and genomic imprinting during preimplantation development
Dev. Biol.
383
15-27
2013
Mus musculus (E9Q5F9)
brenda
Bell, O.; Wirbelauer, C.; Hild, M.; Scharf, A.N.; Schwaiger, M.; MacAlpine, D.M.; Zilbermann, F.; van Leeuwen, F.; Bell, S.P.; Imhof, A.; Garza, D.; Peters, A.H.; Schuebeler, D.
Localized H3K36 methylation states define histone H4K16 acetylation during transcriptional elongation in Drosophila
EMBO J.
26
4974-4984
2007
Drosophila melanogaster (Q9VYD1)
brenda
Du, H.N.; Fingerman, I.M.; Briggs, S.D.
Histone H3 K36 methylation is mediated by a trans-histone methylation pathway involving an interaction between Set2 and histone H4
Genes Dev.
22
2786-2798
2008
Saccharomyces cerevisiae (P46995), Saccharomyces cerevisiae BY4741 (P46995)
brenda
Pu, M.; Ni, Z.; Wang, M.; Wang, X.; Wood, J.G.; Helfand, S.L.; Yu, H.; Lee, S.S.
Trimethylation of Lys36 on H3 restricts gene expression change during aging and impacts life span
Genes Dev.
29
718-731
2015
Caenorhabditis elegans
brenda
Dhayalan, A.; Rajavelu, A.; Rathert, P.; Tamas, R.; Jurkowska, R.Z.; Ragozin, S.; Jeltsch, A.
The Dnmt3a PWWP domain reads histone 3 lysine 36 trimethylation and guides DNA methylation
J. Biol. Chem.
285
26114-26120
2010
Schizosaccharomyces pombe
brenda
Fuchs, S.M.; Kizer, K.O.; Braberg, H.; Krogan, N.J.; Strahl, B.D.
RNA polymerase II carboxyl-terminal domain phosphorylation regulates protein stability of the Set2 methyltransferase and histone H3 di- and trimethylation at lysine 36
J. Biol. Chem.
287
3249-3256
2012
Saccharomyces cerevisiae (P46995)
brenda
Eram, M.S.; Bustos, S.P.; Lima-Fernandes, E.; Siarheyeva, A.; Senisterra, G.; Hajian, T.; Chau, I.; Duan, S.; Wu, H.; Dombrovski, L.; Schapira, M.; Arrowsmith, C.H.; Vedadi, M.
Trimethylation of histone H3 lysine 36 by human methyltransferase PRDM9 protein
J. Biol. Chem.
289
12177-12188
2014
Homo sapiens (Q9NQV7)
brenda
Hacker, K.E.; Fahey, C.C.; Shinsky, S.A.; Chiang, Y.J.; DiFiore, J.V.; Jha, D.K.; Vo, A.H.; Shavit, J.A.; Davis, I.J.; Strahl, B.D.; Rathmell, W.K.
Structure/function analysis of recurrent mutations in SETD2 protein reveals a critical and conserved role for a SET domain residue in maintaining protein stability and histone H3 Lys-36 trimethylation
J. Biol. Chem.
291
21283-21295
2016
Saccharomyces cerevisiae (P46995), Homo sapiens (Q9BYW2)
brenda
Li, L.; Wang, Y.
Cross-talk between the H3K36me3 and H4K16ac histone epigenetic marks in DNA double-strand break repair
J. Biol. Chem.
292
11951-11959
2017
Homo sapiens (Q9BYW2)
brenda
Larschan, E.; Alekseyenko, A.A.; Gortchakov, A.A.; Peng, S.; Li, B.; Yang, P.; Workman, J.L.; Park, P.J.; Kuroda, M.I.
MSL complex is attracted to genes marked by H3K36 trimethylation using a sequence-independent mechanism
Mol. Cell
28
121-133
2007
Drosophila melanogaster (Q9VYD1)
brenda
Xu, L.; Zhao, Z.; Dong, A.; Soubigou-Taconnat, L.; Renou, J.P.; Steinmetz, A.; Shen, W.H.
Di- and tri- but not monomethylation on histone H3 lysine 36 marks active transcription of genes involved in flowering time regulation and other processes in Arabidopsis thaliana
Mol. Cell. Biol.
28
1348-1360
2008
Arabidopsis thaliana (Q2LAE1)
brenda
Lin, L.J.; Minard, L.V.; Johnston, G.C.; Singer, R.A.; Schultz, M.C.
Asf1 can promote trimethylation of H3 K36 by Set2
Mol. Cell. Biol.
30
1116-1129
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Nimura, K.; Ura, K.; Shiratori, H.; Ikawa, M.; Okabe, M.; Schwartz, R.J.; Kaneda, Y.
A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf-Hirschhorn syndrome
Nature
460
287-291
2009
Mus musculus (Q8BVE8), Mus musculus
brenda
Huang, H.; Weng, H.; Zhou, K.; Wu, T.; Zhao, B.S.; Sun, M.; Chen, Z.; Deng, X.; Xiao, G.; Auer, F.; Klemm, L.; Wu, H.; Zuo, Z.; Qin, X.; Dong, Y.; Zhou, Y.; Qin, H.; Tao, S.; Du, J.; Liu, J.; Lu, Z.; Yin, H.; Mesquita, A.; Yuan, C.L.; Hu, Y.C.; Sun, W.; Su, R.; Dong, L.; Shen, C.; Li, C.; Qing, Y.; Jiang, X.; Wu, X.; Sun, M.
Histone H3 trimethylation at lysine 36 guides m6A RNA modification co-transcriptionally
Nature
567
414-419
2019
Homo sapiens (Q9BYW2)
brenda
Carvalho, S.; Raposo, A.C.; Martins, F.B.; Grosso, A.R.; Sridhara, S.C.; Rino, J.; Carmo-Fonseca, M.; de Almeida, S.F.
Histone methyltransferase SETD2 coordinates FACT recruitment with nucleosome dynamics during transcription
Nucleic Acids Res.
41
2881-2893
2013
Homo sapiens (Q9BYW2)
brenda
Zhu, K.; Lei, P.J.; Ju, L.G.; Wang, X.; Huang, K.; Yang, B.; Shao, C.; Zhu, Y.; Wei, G.; Fu, X.D.; Li, L.; Wu, M.
SPOP-containing complex regulates SETD2 stability and H3K36me3-coupled alternative splicing
Nucleic Acids Res.
45
92-105
2017
Homo sapiens (Q9BYW2)
brenda
Ho, T.H.; Park, I.Y.; Zhao, H.; Tong, P.; Champion, M.D.; Yan, H.; Monzon, F.A.; Hoang, A.; Tamboli, P.; Parker, A.S.; Joseph, R.W.; Qiao, W.; Dykema, K.; Tannir, N.M.; Castle, E.P.; Nunez-Nateras, R.; Teh, B.T.; Wang, J.; Walker, C.L.; Hung, M.C.; Jonasch, E.
High-resolution profiling of histone h3 lysine 36 trimethylation in metastatic renal cell carcinoma
Oncogene
35
1565-1574
2016
Homo sapiens (Q9BYW2)
brenda
Jin, J.; Shi, J.; Liu, B.; Liu, Y.; Huang, Y.; Yu, Y.; Dong, A.
MORF-RELATED GENE702, a reader protein of trimethylated histone H3 lysine 4 and histone H3 lysine 36, is involved in brassinosteroid-regulated growth and flowering time control in rice
Plant Physiol.
168
1275-1285
2015
Oryza sativa
brenda
Sein, H.; Vrv, S.; Kristjuhan, A.
Distribution and maintenance of histone H3 lysine 36 trimethylation in transcribed locus lysine 36 trimethylation in transcribed locus
PLoS ONE
10
e0120200
2015
Saccharomyces cerevisiae
brenda
Lee, Y.F.; Nimura, K.; Lo, W.N.; Saga, K.; Kaneda, Y.
Histone H3 lysine 36 methyltransferase Whsc1 promotes the association of Runx2 and p300 in the activation of bone-related genes
PLoS ONE
9
e106661
2014
Mus musculus (Q8BVE8)
brenda
Gautam, D.; Johnson, B.A.; Mac, M.; Moody, C.A.
SETD2-dependent H3K36me3 plays a critical role in epigenetic regulation of the HPV31 life cycle
PLoS Pathog.
14
e1007367
2018
Human papillomavirus type 16, human papillomavirus 31
brenda
Hu, M.; Sun, X.J.; Zhang, Y.L.; Kuang, Y.; Hu, C.Q.; Wu, W.L.; Shen, S.H.; Du, T.T.; Li, H.; He, F.; Xiao, H.S.; Wang, Z.G.; Liu, T.X.; Lu, H.; Huang, Q.H.; Chen, S.J.; Chen, Z.
Histone H3 lysine 36 methyltransferase Hypb/Setd2 is required for embryonic vascular remodeling
Proc. Natl. Acad. Sci. USA
107
2956-2961
2010
Mus musculus (E9Q5F9), Homo sapiens (Q9BYW2)
brenda
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