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Information on EC 2.1.1.359 - [histone H3]-lysine36 N-trimethyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P46995

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IUBMB 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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Saccharomyces cerevisiae
UNIPROT: P46995
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H3 K36 methyltransferase
-
-
H3K36-specific methyltransferase
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-
PATHWAY SOURCE
PATHWAYS
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.
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-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
show the reaction diagram
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
show the reaction diagram
-
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
show the reaction diagram
-
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
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
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
show the reaction diagram
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
show the reaction diagram
-
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
show the reaction diagram
-
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
show the reaction diagram
-
-
-
-
?
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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-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
histone H4
in the presence of histone H4, there is a 5-7fold increase in enzyme activity on histone H3
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R195C
the mutation results in a complete loss of histone H3 lysine 36 trimethylation activity but does not affect dimethylated histone H3 lysine 36
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team