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Details on Person Trimethylation of lysine-5 of histone H3 (H3K4) has been lin...

Class:Id	Summation:5244702
_displayName	Trimethylation of lysine-5 of histone H3 (H3K4) has been lin...
_timestamp	2015-04-16 12:18:58
created	[InstanceEdit:5244704] Jupe, S, 2014-01-20
literatureReference	[LiteratureReference:5244767] Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark [LiteratureReference:5669136] MLL targets SET domain methyltransferase activity to Hox gene promoters [LiteratureReference:5244699] Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus [LiteratureReference:4687068] PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex [LiteratureReference:5244703] Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1 [LiteratureReference:5244709] ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation [LiteratureReference:5244701] Regulation of MLL1 H3K4 methyltransferase activity by its core components [LiteratureReference:5244731] Molecular recognition of histone H3 by the WD40 protein WDR5 [LiteratureReference:5669145] Molecular basis for DPY-30 association to COMPASS-like and NURF complexes [LiteratureReference:5244737] Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex [LiteratureReference:5244747] Myc-binding-site recognition in the human genome is determined by chromatin context [LiteratureReference:5637676] Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity [LiteratureReference:5637680] SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells [LiteratureReference:5688407] Histone methyltransferase SETD3 regulates muscle differentiation
modified	[InstanceEdit:5173311] Jupe, S, 2013-11-26 [InstanceEdit:5637682] Jupe, Steve, 2014-11-12 [InstanceEdit:5651814] Jupe, Steve, 2014-11-25 [InstanceEdit:5669142] Jupe, Steve, 2015-01-30 [InstanceEdit:5674398] Jupe, Steve, 2015-02-12 [InstanceEdit:5688409] Jupe, Steve, 2015-04-16
text	Trimethylation of lysine-5 of histone H3 (H3K4) has been linked to transcriptional activation in a variety of eukaryotic species (Ruthenberg et al. 2007). Several H3K4 methyltransferases have been identified in mammals, predominantly members of the Mixed Lineage Leukemia (MLL) protein family. Five of these, KMT2A (MML1), KMT2D (MLL2), KMT2C (MLL3), KMT2B (MLL4) and SETD1A (KMT2F) have been shown to display H3K4 mono-, di- and tri-methyltransferase activity (Milne et al. 2002, Hughes et al. 2004, Cho et al. 2007, Wysocka et al. 2003). KMT2G (SETD1B) is believed to have similar activity on the basis of sequence homology (Ruthenberg et al. 2007). MLLs are a component of large multiprotein complexes that also include WDR5, RBBP5, ASH2 and DPY30, assembled to form the core MLL complex (Nakamura et al. 2002, Hughes et al. 2004, Dou et al. 2006, Tremblay et al. 2014). The WD40 domain of WDR5 recognizes and binds the histone H3 N-terminus, presenting the lysine-4 side chain for methylation by one of the catalytically active MLL family (Couture et al. 2006, Ruthenburg et al. 2006). Histone H3 recognition by WDR5 is regulated by the methylation state of the adjacent arginine (H3R2) residue. H3R2 methylation abolishes WDR5 interaction with the H3 histone tail (Couture et al. 2006); H3K4 di-/trimethylation and H3R2 methylation have an inverse relationship (Guccione et al. 2006). WHSC1L1 (KMT3F, WHISTLE), SMYD3 (KMT3E) and SETD3 are able to di-methylate H3K4 (Kim et al. 2006, Hamamoto et al. 2004, Eom et al. 2011).
(summation)	[Reaction:5637686] WHSC1L1 (KMT3F), Core MLL complex, SMYD3 (KMT3E) methylate methyl-lysine-5 of histone H3 (H3K4) [Homo sapiens]
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