2.1.1.361: [histone H4]-lysine20 N-methyltransferase
This is an abbreviated version!
For detailed information about [histone H4]-lysine20 N-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.361
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2.1.1.361
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monomethylation
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methyltransferases
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trimethylation
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h4k20me
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crl4cdt2
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histone-modifying
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medicine
- 2.1.1.361
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monomethylation
- methyltransferases
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trimethylation
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h4k20me
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crl4cdt2
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histone-modifying
- medicine
Reaction
Synonyms
CG3307, EC 2.1.1.43, H4-K20-specific HMT, H4-K20-specific HMTase, H4-K20-specific methyltransferase, H4K20 di- and trimethyltransferase, H4K20 methyltransferase, H4K20 protein lysine methyltransferase, histone 4 K20 methyltransferase, histone H4 Lys 20 methyltransferase, histone H4 Lys 20 monomethyltransferase, histone H4 lysine 20 methyltransferase, histone H4 lysine 20 monomethyltransferase, histone H4 lysine20 trimethyltransferase, histone H4-K20 methyltransferase, histone H4-K20 trimethyltransferase, histone H4-lysine 20-specific methyltransferase, histone lysine methyltransferase, Hmt4-20, KMT5a, PKMT, Pr-Set7, PR-Set7/9, protein lysine methyltransferase, SET-4, SET8, SETD8, Suv4-20, Suv4-20h2
ECTree
2.1.1.361 [histone H4]-lysine20 N-methyltransferaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.1.1.361 - [histone H4]-lysine20 N-methyltransferase
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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
3 S-adenosyl-L-methionine + a [histone H4]-L-lysine20
3 S-adenosyl-L-homocysteine + a [histone H4]-N6,N6,N6-trimethyl-L-lysine20
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-
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?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
S-adenosyl-L-methionine + a [histone H4]-N6,N6-dimethyl-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6,N6,N6-trimethyl-L-lysine20
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-
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?
S-adenosyl-L-methionine + a [histone H4]-N6-methyl-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6,N6-dimethyl-L-lysine20
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?
S-adenosyl-L-methionine + p53 (K382)
?
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SET8 activity is strongly reduced by the arginine methylation at position R379
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?
S-adenosyl-L-methionine + [p53]-L-lysine382
S-adenosyl-L-homocysteine + [p53]-N6-methyl-L-lysine382
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?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
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-
-
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
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-
-
-
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
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-
-
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
highly specific substrate
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-
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
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-
-
-
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
-
-
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
-
-
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
-
-
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
highly specific substrate
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-
?
S-adenosyl-L-methionine + histone H4(K20)
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histone H4 is specifically methylated at lysine-20
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?
S-adenosyl-L-methionine + histone H4(K20)
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SET8 specifically methylates K20 on the histone H4. Enzyme activity is strongly reduced by the arginine methylation at position R17
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?
additional information
?
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the enzyme is completely inactive toward histone H4 with a K20L mutation
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?
additional information
?
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the proteolytic degradation of the enzyme is controlled by the SCFSlimb ligase complex
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?
additional information
?
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In addition to K20 (the target methylation site), R17 and H18 are very important specificity determinants for SET8 for substrate recognition. Any other amino acid introduced at these positions completely abolishes the activity of SET8. SET8 equally accepts K and R at position 19, followed by Y and other hydrophobic amino acids like L, H and I. Residues on the C-terminal side of K20 also play important roles in the specificity of SET8. The enzyme accepts majorly I at the -1 position followed by V. Other hydrophobic amino acids like F, Y and L give weaker methylation signals. SET8 also exhibits strong specificity on L22 and R23. At L22 some other hydrophobic amino acids are tolerated. At the +3 position, SET8 majorly prefers R, however it exhibits weak methylation when itis exchanged with other amino acids. SET8 activity is strongly reduced by the arginine methylation at positions R17 in case of H4 and R379 in case of p53
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?
additional information
?
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enzyme binding to the nucleosome protects it from degradation during the cell cycle. Full length enzyme has 3.8% of its histone methyltransferase activity on nucleosomes containing the H2A/E61A/ E64A/D90A/E92A mutations compared to wild type nucleosomes
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?
additional information
?
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the enzyme is completely inactive toward histone H4 with a K20L mutation
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?
additional information
?
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the enzyme is completely inactive toward histone H4 with a K20L mutation
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?
additional information
?
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no methylation of Numb protein by the enzyme is detectable
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?
additional information
?
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the enzyme interacts with the UBC9 E2 SUMO conjugating enzyme and is preferentially modified with SUMO1 in vivo
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?
additional information
?
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the enzyme interacts with the UBC9 E2 SUMO conjugating enzyme and is preferentially modified with SUMO1 in vivo
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?
