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N-lysine methyltransferase SETD8; H4-K20-HMTase SETD8; histone-lysine N-methyltransferase SETD8; lysine N-methyltransferase 5A; PR/SET domain-containing protein 07; PR-Set7; PR/SET07; SET domain-containing protein 8 (SETD8, KMT5A, PRSET7, SET07, SET8)

Function: - protein-lysine N-methyltransferase - monomethylates both histones & non-histone proteins - specifically monomethylates Lys-20 of histone H4 (H4K20me1) - H4K20me1 is enriched during mitosis & represents a specific tag for epigenetic transcriptional repression - mainly functions in euchromatin regions, thus playing a role in silencing of euchromatic genes - required for cell proliferation, probably by contributing to maintenance of proper higher order structure of DNA during mitosis - involved in chromosome condensation & proper cytokinesis - nucleosomes are preferred as substrate compared to free histones - mediates monomethylation of p53/TP53 at Lys-382, leading to repress p53/TP53-target genes - interacts with L3MBTL1 - inhibition of SETD8 alone is sufficient to trigger replicative senescence in fibroblasts [2] S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone] Structure: - although the SET domain contains the active site, both sequences upstream & downstream of the SET domain are required for methyltransferase activity - belongs to the histone-lysine methyltransferase family, PR/SET subfamily - contains 1 SET domain Compartment: - nucleus, chromosome - specifically localizes to mitotic chromosomes - associates with silent chromatin on euchromatic arms - not associated with constitutive heterochromatin Alternative splicing: named isoforms=2 Expression: - not detected during G1 phase - first detected during S through G2 phases, & peaks during mitosis (at protein level) - induced by HCFC1 C-terminal chain, independently of HCFC1 N- terminal chain - SETD8 decreases markedly in senescent fibroblasts [2] Note: - uncertain whether Met-1 or Met-72 is the initiator

General

nuclear protein N-methyltransferase phosphoprotein SET domain-containing protein

Properties

SIZE: entity length = 393 aa MW = 43 kD COMPARTMENT: cell nucleus MOTIF: alanine-rich region {6-67} MOTIF: alanine residue (SEVERAL) arginine-rich region {29-32} MOTIF: arginine residue (SEVERAL) Ser phosphorylation site {S100} coiled coil {134-163} SET domain {256-382} MOTIF: S-adenosyl-L-methionine binding {267-269} binding site SITE: 312-312 FOR-BINDING-OF: S-adenosylmethionine S-adenosyl-L-methionine binding {339-340}

Database Correlations

OMIM 607240 UniProt Q9NQR1 Pfam PF00856 Entrez Gene 387893 Kegg hsa:387893 ENZYME correlations

References

  1. UniProt :accession Q9NQR1
  2. Kumamoto University Cellular senescence prevented by the SETD8 enzyme Science Daily. March 8, 2017 https://www.sciencedaily.com/releases/2017/03/170308092443.htm - Tanaka H, Takebayashi S, Sakamoto A et al The SETD8/PR-Set7 Methyltransferase Functions as a Barrier to Prevent Senescence-Associated Metabolic Remodeling. Cell Reports, 2017; 18 (9): 2148 PMID: 28249161 Free Article