In animals, histone-lysine N-methyltransferase SETD1A () is a histone methyltransferase that produces mono-, di-, and trimethylated histone H3 at 'Lys-4. However, if 'Lys-9' residue is already methylated, 'Lys-4' will not be. The 'Lys-4' methylation is a tag for epigenetic transcriptional activation [, ]. The SET1 complex contains either SETD1A or SETD1B.The SET1 complex is a methyltransferase that that produces trimethylated histone H3 at Lys(4). It is composed of at least the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 []. In yeast there is only one SET1 complex, but in mammals there are additional H3K4 methylases [].
Histone-lysine N-methyltransferase SETD1B () is a histone methyltransferase that produces trimethylated histone H3 at 'Lys-4'. However, if 'Lys-9' residue is already methylated, 'Lys-4' will not be. The 'Lys-4' methylation is a tag for epigenetic transcriptional activation []. The SET1 complex contains either SETD1A or SETD1B.The SET1 complex is a methyltransferase that that produces trimethylated histone H3 at Lys(4). It is composed of at least the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 []. In yeast there is only one SET1 complex, but in mammals there are additional H3K4 methylases [].
This entry represents the RNA recognition motif (RRM) of Setd1A (also known as Set1A), a ubiquitously expressed vertebrates histone methyltransferase that exhibits high homology to yeast Set1. Set1A is localized to euchromatic nuclear speckles and associates with a complex containing six human homologs of the yeast Set1/COMPASS complex, including CXXC finger protein 1 (CFP1; homologous to yeast Spp1), Rbbp5 (homologous to yeast Swd1), Ash2 (homologous to yeast Bre2), Wdr5 (homologous to yeast Swd3), and Wdr82 (homologous to yeast Swd2) []. Set1A contains an N-terminal RNA recognition motif (RRM), an N-SET domain, and a C-terminal catalytic SET domain followed by a post-SET domain. In contrast to Set1B, Set1A additionally contains an HCF-1 binding motif that interacts with HCF-1 in vivo.
The UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase (OGT; ) is a heterotrimer of one 78kDa subunit and two 110kDa subunits. OGT catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in a protein. Substrate proteins include histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. The consequences of this form of glycosylation are diverse, including insulin resistance in muscle and adipocyte cells (brought about by inhibiting the 'Thr-308' phosphorylation of AKT1) []; regulation of glycolysis by inhibiting PFKL activity []; in the cell cycle O-glycosylation stabilizes ARNTL/BMAL1 and CLOCK, preventing their ubiquitination and subsequent degradation []; glycosylation of HCFC1 and interaction with TET proteins promotes binding of the SET1/COMPASS methyltransferase SETD1A to chromatin []; and H2B GlcNAcylation is a histone modification that facilitates H2BK120 monoubiquitination []. It is a component of several complexes, including MLL5-L, NSL []and THAP1/THAP3-HCFC1-OGT [].This entry represents the 110kDa subunit which has thirteen tetratricopeptide (TPR) repeats that are required for substrate binding and oligomerization [].The NSL complex is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. The complex is composed of at least MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 [].
