STRINGSTRING
CTM1 protein (Saccharomyces cerevisiae) - STRING interaction network
"CTM1" - Cytochrome c lysine methyltransferase, trimethylates residue 72 of apo-cytochrome c in Saccharomyces cerevisiae
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
CTM1Cytochrome c lysine methyltransferase, trimethylates residue 72 of apo-cytochrome c (Cyc1p) in the cytosol; not required for normal respiratory growth; Methyltransferase which mediates trimethylation of ’Lys- 78’ of cytochrome c (CYC1) (585 aa)    
Predicted Functional Partners:
SET2
Histone methyltransferase with a role in transcriptional elongation, methylates a lysine residue of histone H3; associates with the C-terminal domain of Rpo21p; histone methylation activity is regulated by phosphorylation status of Rpo21p; Histone methyltransferase that methylates histone H3 to form H3K36me. Involved in transcription elongation as well as in transcription repression. The methyltransferase activity requires the recruitment to the RNA polymerase II, which is CTK1 dependent (733 aa)
         
  0.928
DOT1
Nucleosomal histone H3-Lys79 methylase; methylation is required for telomeric silencing, meiotic checkpoint control, and DNA damage response; Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. Can bind to DNA (in vitro) (582 aa)
         
  0.928
SET1
Histone methyltransferase, subunit of the COMPASS (Set1C) complex; COMPASS methylates histone H3K4; Set1p-dependent H3K4 trimethylation recruits Nrd1p, allowing efficient termination of snoRNAs and cryptic unstable transcripts (CUTs) by Nrd1p-Nab3p- /.../pathway; modulates histone acetylation levels in promoter proximal regions to ensure efficient Nrd1p-dependent termination; required in transcriptional silencing near telomeres and at silent mating type loci; has a SET domain; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 t [...] (1080 aa)
         
  0.925
RKM2
Ribosomal protein lysine methyltransferase, responsible for trimethylation of the lysine residue at position 3 of Rpl12Ap and Rpl12Bp; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that trimethylates 60S ribosomal protein L12 (RPL12A and RPL12B) at ’Lys-4’ and ’Lys-11’ (479 aa)
           
  0.894
RKM3
Ribosomal lysine methyltransferase specific for monomethylation of Rpl42ap and Rpl42bp (lysine 40); nuclear SET domain containing protein; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that monomethylates 60S ribosomal protein L42 (RPL42A and RPL42B) at ’Lys-40’ (552 aa)
           
  0.848
HOM6
Homoserine dehydrogenase (L-homoserine-NADP oxidoreductase), dimeric enzyme that catalyzes the third step in the common pathway for methionine and threonine biosynthesis; enzyme has nucleotide-binding, dimerization and catalytic regions (359 aa)
       
      0.800
RKM1
SET-domain lysine-N-methyltransferase, catalyzes the formation of dimethyllysine residues on the large ribsomal subunit protein L23a (RPL23A and RPL23B); S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that monomethylates ribosomal protein S18 (RPS18A and RPS18B) at ’Lys-48’ and dimethylates ribosomal protein L23 (RPL23A and RPL23B) at ’Lys-106’ and ’Lys-110’ (583 aa)
           
  0.795
RMT2
Arginine N5 methyltransferase; methylates ribosomal protein Rpl12 (L12) on Arg67; S-adenosyl-L-methionine-dependent protein-arginine N- methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins (PubMed-9873020). Monomethylates ribosomal protein L12 (RPL12A/RPL12B) at ’Arg-67’ (PubMed-11856739) (412 aa)
           
  0.795
EFM1
Lysine methyltransferase; involved in the monomethylation of eEF1A (Tef1p/Tef2p); SET-domain family member; predicted involvement in ribosome biogenesis; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that monomethylates elongation factor 1-alpha (TEF1/TEF2) at ’Lys-30’ (585 aa)
           
  0.760
RKM4
Ribosomal lysine methyltransferase specific for monomethylation of Rpl42ap and Rpl42bp (lysine 55); nuclear SET-domain containing protein; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that monomethylates 60S ribosomal protein L42 (RPL42A and RPL42B) at ’Lys-55’ (494 aa)
           
  0.642
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
Server load: low (4%) [HD]