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Information on EC 2.1.1.359 - [histone H3]-lysine36 N-trimethyltransferase and Organism(s) Danio rerio and UniProt Accession Q7SXS7

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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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Danio rerio
UNIPROT: Q7SXS7
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The taxonomic range for the selected organisms is: Danio rerio
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
histone H3K36 methyltransferase
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SET2
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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
S-adenosyl-L-methionine + histone H3(K36)
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show the reaction diagram
the enzyme has histone methyltransferase activity specifically towards mono-, di- and trimethylation of histone H3(K36) residues both in vitro and in vivo
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme plays roles as an activator of general transcription and inhibits cell viability by inducing caspase-3 activation overexpression
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SETD3_DANRE
596
0
67251
Swiss-Prot
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team