2.1.1.367: [histone H3]-lysine9 N-methyltransferase
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For detailed information about [histone H3]-lysine9 N-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.367
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2.1.1.367
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adipose
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adipocytes
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obesity
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thermogenesis
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thermogenic
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beige
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adipogenesis
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myeloid
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cidea
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depot
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high-fat
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diet-induced
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adipogenic
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preadipocytes
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brown-like
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adiposity
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tmem26
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inguinal
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hfd-induced
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ppargc1a
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anti-obesity
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fat-specific
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tfam
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fat-like
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cited1
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adipocyte-specific
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non-shivering
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multilocular
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interscapular
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irisin
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adipose-specific
- 2.1.1.367
- adipose
- adipocytes
- obesity
-
thermogenesis
-
thermogenic
-
beige
-
adipogenesis
- myeloid
-
cidea
-
depot
-
high-fat
-
diet-induced
-
adipogenic
- preadipocytes
-
brown-like
-
adiposity
-
tmem26
-
inguinal
-
hfd-induced
-
ppargc1a
-
anti-obesity
-
fat-specific
- tfam
-
fat-like
-
cited1
-
adipocyte-specific
-
non-shivering
-
multilocular
-
interscapular
-
irisin
-
adipose-specific
Reaction
Synonyms
At1g73100, EHMT1, EHMT2, G9a, GLP, H3 lysine-9 specific histone-lysine N-methyltransferase, KMT1C, KMT1D, Mecom, MEL, PFM13, positive regulatory domain containing 16, PRDM16, PRDM3, SUVH3
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General Information
General Information on EC 2.1.1.367 - [histone H3]-lysine9 N-methyltransferase
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physiological function
Prdm3 and Prdm16 are redundant histone H3K9me1-specific methyltransferases that direct cytoplasmic H3K9me1 methylation. The H3K9me1 is converted in the nucleus to H3K9me3 by the Suv39h enzymes to reinforce heterochromatin. Simultaneous depletion of Prdm3 and Prdm16 abrogates H3K9me1 methylation, prevents Suv39h-dependent H3K9me3 trimethylation, and derepresses major satellite transcription. Combined impairment of Prdm3 and Prdm16 results in disintegration of heterochromatic foci and disruption of the nuclear lamina
physiological function
histone H3K9 methyltransferases G9a/KMT1C, GLP/KMT1D, SETDB1/KMT1E, and Suv39h1/KMT1A, coexist in the same megacomplex. In Suv39h or G9a null cells, the remaining histone H3K9 methyltransferases are destabilized at the protein level, indicating. The four enzymes are recruited to major satellite repeats, a known Suv39h1 genomic target, but also to multiple G9a target genes. The four H3K9 histone H3K9 methyltransferases display a functional cooperation in the regulation of known G9a target genes
physiological function
loss of Prdm16 causes craniofacial defects including anterior mandibular hypoplasia, clefting in the secondary palate and severe middle ear defects. Loss of Prdm16 significantly decreases histone 3 lysine 9 methylation in the palatal shelves but does not change histone 3 lysine 4 methylation
physiological function
loss of Prdm3 or Prdm16 in zebrafish causes craniofacial defects including hypoplasia of the craniofacial cartilage elements, undefined posterior ceratobranchials, and decreased mineralization of the parasphenoid. Prdm3 and Prdm16 compensate for each other as well as a Prdm1a. Combinatorial loss of Prdm1a, Prdm3, and Prdm16 alleles results in severe hypoplasia of the anterior cartilage elements, abnormal formation of the jaw joint, complete loss of the posterior ceratobranchials, and clefting of the ethmoid plate. Loss of Prdm3 and Prdm16 reduces methylation of histone 3 lysine 9 (repression) and histone 3 lysine 4 (activation) in zebrafish
physiological function
overexpression of the PR domain of PRDM16 represses the differentiation of porcine preadipocytes. Overexpression of the PR domain significantly increases the level of lipolysis and mitochondrial oxidative capacity during differentiation. The protein coded by the PR domain has H3K9me1 methyltransferase activity
physiological function
PRDM16 is a histone H3 K9 methyltransferase on chromatin. Mutation in the N-terminal PR-domain of PRDM16 completely abolishes the intrinsic enzymatic activity of PRDM16. The methyltransferase activity of PRDM16 is required for specific suppression of mixed lineage leukemia leukemogenesis both in vitro and in vivo. PRDM16 directly activates the SNAG family transcription factor GFI1b, which in turn down regulates the HOXA gene cluster. Knockdown GFI1b represses PRDM16-mediated tumor suppression while GFI1b overexpression mimics PRDM16 overexpression. Silencing PRDM16 by DNA methylation is concomitant with mixed lineage leukemia MLL-AF9 induced leukemic transformation
physiological function
simultaneous depletion of Prdm3 and Prdm16 abrogates H3K9me1 methylation, prevents Suv39h-dependent H3K9me3 trimethylation, and derepresses major satellite transcription. Combined impairment of Prdm3 and Prdm16 results in disintegration of heterochromatic foci and disruption of the nuclear lamina
physiological function
SUVH3 binds methylated DNA in vitro, is associated with euchromatic methylation in vivo, and forms a complex with two DNAJ domain-containing homologs, DNAJ1 and DNAJ2. Ectopic recruitment of DNAJ1 enhances gene transcription