Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

N-Lysine Methyltransferase SMYD

  • Andria Zaidan
  • Nicholas Spellmon
  • Vishakha Choudhary
  • Chunying Li
  • Zhe YangEmail author
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_101729


Historical Background

SMYD proteins are a family of histone and protein lysine methyltransferases containing a SET domain interrupted by a MYND zinc finger motif (Spellmon et al. 2015) (Fig. 1). The SET domain is evolutionally conserved in N-lysine methyltransferases and responsible for the methyltransferase activity (Sirinupong et al. 2010). The MNYD domain is a protein–protein interaction module involved in transcriptional cofactor recruitment (Spellmon et al. 2015). The SMYD family achieves the methyltransferase activity by adding methyl groups to target lysine residues using S-adenosylmethionine (AdoMet) as a donor substrate (Fig. 1). Recent studies show the SMYD protein family to be involved in cancer proliferation, epigenetic transcription regulation, the immune system,...
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Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  • Andria Zaidan
    • 1
  • Nicholas Spellmon
    • 1
  • Vishakha Choudhary
    • 1
  • Chunying Li
    • 2
  • Zhe Yang
    • 3
    Email author
  1. 1.DetroitUSA
  2. 2.AtlantaUSA
  3. 3.Department of Biochemistry and Molecular BiologyWayne State University School of MedicineDetroitUSA