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Information on EC 2.1.1.362 - [histone H4]-N-methyl-L-lysine20 N-methyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9NQR1

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IUBMB Comments
This entry describes a group of enzymes that catalyse a single methylation of monomethylated lysine20 of histone H4 (H4K20m1, generated by EC 2.1.1.361, [histone H4]-lysine20 N-methyltransferase), forming the dimethylated form. This modification is broadly distributed across the genome and is likely important for general chromatin-mediated processes. The double-methylated form of lysine20 in histone H4 is the most abundant methylation state of this residue and is found on ~80% of all histone H4 molecules. Full activity of the enzyme requires that the lysine at position 9 of histone H3 is trimethylated.
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Homo sapiens
UNIPROT: Q9NQR1
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
suv420h2, papa2, kmt5c, histone h4 lysine20 di- and trimethyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
histone methyltransferase
-
-
KMT5C
-
-
-
-
papA2
-
-
-
-
SUV39H1
-
-
-
-
SUV420H2
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
show the reaction diagram
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[histone H4]-N6-methyl-L-lysine20 N6-methyltransferase
This entry describes a group of enzymes that catalyse a single methylation of monomethylated lysine20 of histone H4 (H4K20m1, generated by EC 2.1.1.361, [histone H4]-lysine20 N-methyltransferase), forming the dimethylated form. This modification is broadly distributed across the genome and is likely important for general chromatin-mediated processes. The double-methylated form of lysine20 in histone H4 is the most abundant methylation state of this residue and is found on ~80% of all histone H4 molecules. Full activity of the enzyme requires that the lysine at position 9 of histone H3 is trimethylated.
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 L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
show the reaction diagram
S-adenosyl-L-methionine + histone H4(K20)
?
show the reaction diagram
-
trimethylation at lysine 20 of histone H4
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-
?
additional information
?
-
histone methylation has significant effects on heterochromatin formation and transcriptional regulation
-
-
?
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 L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
show the reaction diagram
Lys20 of histone 4, SET8
-
?
additional information
?
-
histone methylation has significant effects on heterochromatin formation and transcriptional regulation
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
SUV420H2 is strongly associated to pericentric heterochromatin, the N-terminus of SUV420H2 comprising then catalytically active SET domain is dispersed within the nucleus, whereas the C-terminal part of the protein is associated with heterochromatin
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KMT5A_HUMAN
393
1
42890
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
SDS-PAGE
52000
-
about 52000 Da, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 45000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the SET domain is composed of three groups of canonical beta-sheets arranged in a triangular fashion with a group of two beta-sheets closely neighboring a conserved alpha-helix defining a cleft for the binding to the histone-tail ligand. The cofactor AdoMet and substrate bind at two adjacent sites to the SET domain. The histone-tail ligand binds into a groove formed by both the SET and postSET domains. The cofactor AdoMet binds into a distinct pocket located on the other side of the SET domain and acts as a methyl group donor. Both AdoMet and the L-lysine-histone are connected through a narrow tunnel where the methyl group is channeled. In the structure of the peptide-less NSDx02SET domain, the postSET domain loop is extended on top of the histone binding site, which sterically prevents the binding of either H3K36 or H4K20 substrates. In the presence of ligand, a network of residues stabilizes the H4-peptide tail on the binding site
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
tandem affinity purification
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-S-transferase-fusion protein, SET gene
TAP-tagged protein is expressed in L929 cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fang, J.; Feng, Q.; Ketel, C.S.; Wang, H.; Cao, R.; Xia, L.; Erdjument-Bromage, H.; Tempst, P.; Simon, J.A.; Zhang, Y.
Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase
Curr. Biol.
12
1086-1099
2002
Drosophila elegans, Drosophila melanogaster, Homo sapiens (Q9NQR1)
Manually annotated by BRENDA team
Souza, P.; Voelkel, P.; Trinel, D.; Vandamme, J.; Rosnoblet, C.; Heliot, L.; Angrand, P.
The histone methyltransferase SUV420H2 and heterochromatin proteins HP1 interact but show different dynamic behaviours
BMC Cell Biol.
10
41
2009
Homo sapiens
Manually annotated by BRENDA team
Morishita, M.; Di Luccio, E.
Structural insights into the regulation and the recognition of histone marks by the SET domain of NSD1
Biochem. Biophys. Res. Commun.
412
214-219
2011
Homo sapiens (Q96L73)
Manually annotated by BRENDA team