Lysine Methyltransferase

SET domain-containing proteins are potential histone methyltransferases (HMTases), which are classified into subgroups by their putative substrate specificities. Histone H3 Lys9 (H3-K9) methyltransferase group genes include Suv39h1, Suv39h2, G9a, G9a related protein (GLP) and SETDB1/ESET. The H3-K9 methylation mark plays an important role as a binding site for the chromo-containing protein, resulting in chromatin compaction and heterochromatin generation. Histone H3-K4 methylation is exclusively associated with actively transcribed genes. The first H3-K4 methylase complex, COMPASS, was identified in the yeast S. cerevisiae and consists of Set1/KMT2 and seven other polypeptides, Cps60-Cps15. Set1/KMT2 functions within COMPASS and is capable of mono-, di-, and trimethylating H3-K4. There are several Set1 related proteins in mammals including WDR5, RBBP5, ASH2L, CXXC1, and DPY30. SET7/SET9 is a member of the SET domain-containing family that can specifically methylate H3-K4, Lys189 of the TAF10, a member of the TFIID transcription factor complex, and Lys372 of the p53 tumor suppressor protein. SET domain-containing lysine methyltransferase 8 (SET8), also known as PR/SET domain-containing protein 7 (PR/SET7), is a single-subunit enzyme that mono-methylates histone H4-K20, preferably on nucleosomal substrates. SET and MYND domain-containing protein 2 (SMYD2), also known as lysine methyltransferase protein 3C (KMT3C), functions to repress transcription by interacting with the Sin3A repressor complex and methylating H3-K36. SMYD2 also methylates H3-K4 through interaction with HSP90α, and methylates p53 at Lys370 to repress p53-mediated transcriptional activation and apoptosis.

Product List

TargetCatalog#Product NameReactivityApplication
EHMT2/G9AMRe03938EHMT2/G9A Rabbit Monoclonal AntibodyHuman, Mouse, RatWB,IHC-F,IHC-P,ICC/IF,FC,IP
SETDB1AMM80918SETDB1 Mouse Monoclonal AntibodyHuman,Mouse,MonkeyWB,ICC,ELISA
ASH2LAMRe01469ASH2L Rabbit Monoclonal AntibodyHuman,RatWB,ICC/IF,IP
ASH2LAMRe01682ASH2L Rabbit Monoclonal AntibodyHuman,Mouse,RatWB,IHC-F,IHC-P,ICC/IF
ASH2LAMM81819ASH2L Mouse Monoclonal AntibodyHuman,MouseWB,IHC,FC,ELISA
RBBP5 (1C9)AMM03540RBBP5 (1C9) Mouse Monoclonal AntibodyHuman,Mouse,RatWB,ICC/IF
SETD7AMM82270SETD7 Mouse Monoclonal AntibodyHuman,Rat,MonkeyWB,FC,ELISA
SETD7AMM82271SETD7 Mouse Monoclonal AntibodyHuman,Rat,MonkeyWB,IHC,ELISA
SET7AMRe86923SET7 Rabbit Monoclonal AntibodyHuman,Mouse,RatWB, IP
SMYD2APRab18039SMYD2 Rabbit Polyclonal AntibodyHuman,Mouse,RatWB,ELISA,IHC-P
KMT5AAMM82217KMT5A Mouse Monoclonal AntibodyHumanICC,FC,ELISA
KMT5AAMM82291KMT5A Mouse Monoclonal AntibodyHumanIHC,FC,ELISA
SET07AMM86128SET07 Mouse Monoclonal AntibodyHumanWB,IHC,ICC

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References

  • Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9. Tachibana M, et al. Genes Dev. 2005. [PMID: 15774718]
  • Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation. Shilatifard A. Curr Opin Cell Biol. 2008. [PMID: 18508253]
  • Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex. Lee JH, et al. J Biol Chem. 2007. [PMID: 17355966]
  • Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Nishioka K, et al. Genes Dev. 2002. [PMID: 11850410]
  • Gene-specific modulation of TAF10 function by SET9-mediated methylation. Kouskouti A, et al. Mol Cell. 2004. [PMID: 15099517]
  • Regulation of p53 activity through lysine methylation. Chuikov S, et al. Nature. 2004. [PMID: 15525938]
  • Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase. Fang J, et al. Curr Biol. 2002. [PMID: 12121615]
  • Specificity and mechanism of the histone methyltransferase Pr-Set7. Xiao B, et al. Genes Dev. 2005. [PMID: 15933069]
  • Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase. Couture JF, et al. Genes Dev. 2005. [PMID: 15933070]
  • Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex. Brown MA, et al. Mol Cancer. 2006. [PMID: 16805913]
  • The tale of two domains: proteomics and genomics analysis of SMYD2, a new histone methyltransferase. Abu-Farha M, et al. Mol Cell Proteomics. 2008. [PMID: 18065756]
  • Repression of p53 activity by Smyd2-mediated methylation. Huang J, et al. Nature. 2006. [PMID: 17108971]
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