Literature summary for 2.1.1.369 extracted from

Jacob, Y.; Bergamin, E.; Donoghue, M.T.; Mongeon, V.; LeBlanc, C.; Voigt, P.; Underwood, C.J.; Brunzelle, J.S.; Michaels, S.D.; Reinberg, D.; Couture, J.F.; Martienssen, R.A.
Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication (2014), Science, 343, 1249-1253 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
ATXR5 contains a bipartite catalytic domain composed of nSET and SET. The selectivity pocket and safety belt of ATXR5/6-type H3K27 methyltransferases are responsible for H3.1 preference over H3.3	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q8VZJ1	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + [histone H3.1]-L-lysine27	-	Arabidopsis thaliana	S-adenosyl-L-homocysteine + [histone H3.1]-N6-methyl-L-lysine27	-	?

Synonyms

Synonyms	Comment	Organism
Arabidopsis trithorax-related protein 5	-	Arabidopsis thaliana
ATXR5	-	Arabidopsis thaliana

General Information

General Information	Comment	Organism
physiological function	ATXR5 selectively methylates the replication-dependent histone H3 variant H3.1. ATXR5 contains a bipartite catalytic domain that specifically reads alanine-31 of H3.1. Variation at position 31 between H3.1 and replication-independent H3.3 is conserved in plants and animals, and threonine-31 in H3.3 is responsible for inhibiting the activity of ATXR5 and its paralog, ATXR6	Arabidopsis thaliana

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Release 2023.1 (January 2023)