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CYS4 protein (Saccharomyces cerevisiae) - STRING interaction network
"CYS4" - Cystathionine beta-synthase, catalyzes synthesis of cystathionine from serine and homocysteine, the first committed step in cysteine biosynthesis in Saccharomyces cerevisiae
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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CYS4Cystathionine beta-synthase, catalyzes synthesis of cystathionine from serine and homocysteine, the first committed step in cysteine biosynthesis; responsible for hydrogen sulfide generation; mutations in human ortholog cause homocystinuria (507 aa)    
Predicted Functional Partners:
GUA1
GMP synthase; highly conserved enzyme that catalyzes the second step in the biosynthesis of GMP from inosine 5’-phosphate (IMP); transcription is not subject to regulation by guanine but is negatively regulated by nutrient starvation; reduction-of-f /.../n mutation gua1-G388D causes changes in cellular guanine nucleotide pools, defects in general protein synthesis, and impaired translation of GCN4 mRNA (525 aa)
   
  0.999
CYS3
Cystathionine gamma-lyase, catalyzes one of the two reactions involved in the transsulfuration pathway that yields cysteine from homocysteine with the intermediary formation of cystathionine (394 aa)
 
  0.999
YLR126C
Putative protein of unknown function with similarity to glutamine amidotransferase proteins; has Aft1p-binding motif in the promoter; may be involved in copper and iron homeostasis; YLR126C is not an essential protein; May have a role in copper and iron homeostasis (251 aa)
   
  0.998
STR2
Cystathionine gamma-synthase, converts cysteine into cystathionine; Catalyzes the formation of L-cystathionine from O- succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma- replacement reaction. In the absence of thiol, catalyzes gamma- elimination to form 2-oxobutanoate, succinate and ammonia (By similarity) (639 aa)
   
  0.997
STR3
Peroxisomal cystathionine beta-lyase, converts cystathionine into homocysteine; may be redox regulated by Gto1p (465 aa)
 
  0.997
YLL058W
Putative protein of unknown function with similarity to Str2p, which is a cystathionine gamma-synthase important in sulfur metabolism; YLL058W is not an essential gene; Catalyzes the formation of L-cystathionine from O- succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma- replacement reaction. In the absence of thiol, catalyzes gamma- elimination to form 2-oxobutanoate, succinate and ammonia (By similarity) (575 aa)
   
  0.994
YML082W
Putative protein predicted to have carbon-sulfur lyase activity; transcriptionally regulated by Upc2p via an upstream sterol response element; green fluorescent protein (GFP)-fusion protein localizes to the nucleus and the cytoplasm; YML082W is not /.../ential gene; Catalyzes the formation of L-cystathionine from O- succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma- replacement reaction. In the absence of thiol, catalyzes gamma- elimination to form 2-oxobutanoate, succinate and ammonia (By similarity) (649 aa)
   
  0.994
MET17
O-acetyl homoserine-O-acetyl serine sulfhydrylase; required for Methionine and cysteine biosynthesis; Transforms O-acetylhomoserine into homocysteine and O- acetylserine into cysteine (444 aa)
     
  0.994
IRC7
Beta-lyase involved in the production of thiols; null mutant displays increased levels of spontaneous Rad52p foci; expression induced by nitrogen limitation in a GLN3, GAT1-dependent manner and by copper levels in a Mac1-dependent manner (340 aa)
 
  0.993
SAH1
S-adenosyl-L-homocysteine hydrolase, catabolizes S-adenosyl-L-homocysteine which is formed after donation of the activated methyl group of S-adenosyl-L-methionine (AdoMet) to an acceptor; Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine (449 aa)
   
 
  0.990
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
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