2.1.1.356: [histone H3]-lysine27 N-trimethyltransferase
This is an abbreviated version!
For detailed information about [histone H3]-lysine27 N-trimethyltransferase, go to the full flat file.
Word Map on EC 2.1.1.356
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2.1.1.356
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chromatin
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trimethylation
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zeste
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tumorigenesis
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pluripotency
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repressor
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lncrnas
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prc2-mediated
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leukemia
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heterochromatin
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epigenome
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ectoderm
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methyltransferases
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self-renewal
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jarid2
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bivalent
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prc1
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h3k4me3
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nucleosome
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imprint
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cdkn2a
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demethylase
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dznep
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vernalization
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h3k27ac
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ezh2-mediated
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hotair
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de-repression
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3-deazaneplanocin
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lysine-27
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ctcf
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jumonji
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mescs
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analysis
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polycomb-group
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curly
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trithorax
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homeotic
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synthesis
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mpnsts
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polycomb-mediated
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chromatin-modifying
- 2.1.1.356
- chromatin
-
trimethylation
-
zeste
- tumorigenesis
-
pluripotency
- repressor
- lncrnas
-
prc2-mediated
- leukemia
-
heterochromatin
-
epigenome
- ectoderm
- methyltransferases
-
self-renewal
- jarid2
-
bivalent
- prc1
-
h3k4me3
- nucleosome
-
imprint
-
cdkn2a
- demethylase
-
dznep
-
vernalization
-
h3k27ac
-
ezh2-mediated
-
hotair
-
de-repression
-
3-deazaneplanocin
-
lysine-27
- ctcf
-
jumonji
-
mescs
- analysis
-
polycomb-group
-
curly
-
trithorax
-
homeotic
- synthesis
- mpnsts
-
polycomb-mediated
-
chromatin-modifying
Reaction
3 S-adenosyl-L-methionine + = 3 S-adenosyl-L-homocysteine +
Synonyms
CLF, EC 2.1.1.43, EZH1, EZH2, G9a, histone H3 K27 methyltransferase, histone H3 lysine 27 methyltransferase, histone lysine methyltransferase, HMTase, interleukin-5 response element II binding protein, KMT6, KMT6A, KMT6B, lysine-preferring HMTase, NSD2, NSD3, Polycomb repressive complex 2, PRC2, RE-IIBP, SET, SET domain histone lysine methyltransferase, SETDB1, TXR1, vSET, WHSC1/MMSET isoform RE-IIBP
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General Information
General Information on EC 2.1.1.356 - [histone H3]-lysine27 N-trimethyltransferase
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malfunction
physiological function
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mutations in the catalytic subunit E(Z) that abolish methyltransferase activity disrupt Polycomb silencing, causing derepression of Polycomb target genes in cells where they are normally silenced. Increased histone H3(K27) trimethylation activity of mutant E(Z)Trm causes the premature accumulation of trimethylated histone H3(K27) in early embryogenesis, predestining initially active Polycomb target genes to silencing once Polycomb silencing is initiated
malfunction
enzyme depletion leads to heterochromatin protein 1alpha loss from chromatin and degradation
malfunction
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enzyme knockdown sensitizes latent proviruses to external stimuli, such as T-cell receptor stimulation, and slows the reversion of reactivated proviruses to latency
malfunction
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enzyme mutants are sterile, have morphological defects, and are altered in pigment production
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RE-IIBP represses basal transcription via histone deacetylase recruitment, which may be mediated by histone H3(K27) methylation, knockdown of RE-IIBP reduces histone H3-K27 methylation and histone deacetylase occupancy around the interleukin-5 promoter
physiological function
a PRC2 (for Polycomb repressive complex 2) histone H3 lysine-27 (H3K27) methyltransferase complex functions to inhibit founder cell establishment during lateral root initiation. Functional loss of the PRC2 subunits EMF2 (for EMBRYONIC FLOWER 2) or CLF (for CURLY LEAF) leads to a great increase in the number of LRs formed in the primary root. The CLF H3K27 methyltransferase binds to chromatin of the auxin efflux carrier gene PIN FORMED 1 (PIN1), deposits the repressive mark H3K27me3 to repress its expression, and functions to down-regulate auxin maxima in root tissues and inhibit founder cell establishment
physiological function
the enzyme affects DNA replication elongation in Tetrahymena thermophila
physiological function
the enzyme and H3K27me3 cooperate with [histone H3]-L-lysine27 methylation to maintain heterochromatin protein 1alpha at chromatin
physiological function
the enzyme contributes to the regulation of chromatin structure
physiological function
knockdown of SETDB1 gene expression leads to gonocyte apoptosis and a decrease in H3K27me3, but no significant change in H3K9me3
physiological function
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the enzyme affects DNA replication elongation in Tetrahymena thermophila
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