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Literature summary for 2.1.1.354 extracted from

  • Schibler, A.; Koutelou, E.; Tomida, J.; Wilson-Pham, M.; Wang, L.; Lu, Y.; Cabrera, A.P.; Chosed, R.J.; Li, W.; Li, B.; Shi, X.; Wood, R.D.; Dent, S.Y.
    Histone H3K4 methylation regulates deactivation of the spindle assembly checkpoint through direct binding of Mad2 (2016), Genes Dev., 30, 1187-1197 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.354

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta 2 cells Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
G951S the mutation displays benomyl resistance equivalent to that caused by enzyme deletion. The mutation affects Mad2 localization in dividing cells Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine4 Saccharomyces cerevisiae overall reaction 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine4
-
 ?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine4 Saccharomyces cerevisiae BY4741 overall reaction 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine4
-
 ?
S-adenosyl-L-methionine + a [histone H3]-L-lysine4 Saccharomyces cerevisiae
-
 S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine4
-
 ?
S-adenosyl-L-methionine + a [histone H3]-L-lysine4 Saccharomyces cerevisiae BY4741
-
 S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine4
-
 ?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine4 Saccharomyces cerevisiae
-
 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine4
-
 ?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine4 Saccharomyces cerevisiae BY4741
-
 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine4
-
 ?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine4 Saccharomyces cerevisiae
-
 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine4
-
 ?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine4 Saccharomyces cerevisiae BY4741
-
 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine4
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae BY4741
-
-
-

Purification (Commentary)

Purification (Comment) Organism
glutathione Sepharose 4B column chromatography and Superdex S200 gel filtration Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine4 overall reaction Saccharomyces cerevisiae 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine4
-
 ?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine4 overall reaction Saccharomyces cerevisiae BY4741 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine4
-
 ?
S-adenosyl-L-methionine + a [histone H3]-L-lysine4
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine4
-
 ?
S-adenosyl-L-methionine + a [histone H3]-L-lysine4
-
 Saccharomyces cerevisiae BY4741 S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine4
-
 ?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine4
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine4
-
 ?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine4
-
 Saccharomyces cerevisiae BY4741 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine4
-
 ?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine4
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine4
-
 ?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine4
-
 Saccharomyces cerevisiae BY4741 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine4
-
 ?

Synonyms

Synonyms Comment Organism
SET1
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction enzyme loss induces benomyl resistance. Enzyme mutants display a thick mitotic spindle and a defect in the release of the spindle assembly checkpoint Saccharomyces cerevisiae
physiological function the enzyme's catalytic activity is required for a normal response to microtubule depolymerization Saccharomyces cerevisiae