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. Author manuscript; available in PMC: 2014 May 1.
Published in final edited form as: Trends Biochem Sci. 2013 Mar 13;38(5):243–252. doi: 10.1016/j.tibs.2013.02.004

Table 1.

SET-domain protein lysine methyltransferases in the yeast Saccharomyces cerevisiae

Protein Substrate(s)
(position given from
the mature N-
terminal residue
unless otherwise
indicated)
Product(s) Methylated
residue
surface
exposed or
buried
References
Subfamily one
Set1 (as the catalytic component of the COMPASS complex) histone H3 Lys-4
Dam1 Lys-233 (from initiator methionine)
trimethyl
dimethyl (possible trimethyl)
surface
unknown
[30]
Set2 histone H3 Lys-36 trimethyl surface [31]
Set3 no known methyltransferase activity
Set4 no known methyltransferase activity
Set5 histone H4 Lys-5, Lys-8, Lys12
histone H2A Lys-4, Lys-7
monomethyl at all three sites
unknown
surface [32]
Set6 no known methyltransferase activity
Subfamily two
Rkm1 ribosomal protein Rpl23ab Lys-105, Lys-109 dimethyl at both sites surface (interface between small and large subunits) [33]
Rkm2 ribosomal protein Rpl12ab Lys-3 trimethyl surface [25]
Rkm3 ribosomal protein Rpl42ab Lys-39 monomethyl buried [25]
Rkm4 ribosomal protein Rpl42ab Lys-54 monomethyl buried (close contacts to 25S rRNA O2 of cytosine 2764 and OP2 of
cytosine-93)
[25]
Efm1 elongation factor eEF1A Lys-30 monomethyl surface [34,35]
Ctm1 iso-1-cytochrome c Lys-72 trimethyl surface [36]