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RAM1 protein (Saccharomyces cerevisiae) - STRING interaction network
"RAM1" - Beta subunit of the CAAX farnesyltransferase in Saccharomyces cerevisiae
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Predicted Interactions
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RAM1Beta subunit of the CAAX farnesyltransferase (FTase) that prenylates the a-factor mating pheromone and Ras proteins; required for the membrane localization of Ras proteins and a-factor; homolog of the mammalian FTase beta subunit; Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins such as a-factor and RAS. The beta subunit is responsible for peptide-binding (431 aa)    
Predicted Functional Partners:
RAM2
Alpha subunit of both the farnesyltransferase and type I geranylgeranyltransferase that catalyze prenylation of proteins containing a CAAX consensus motif; essential protein required for membrane localization of Ras proteins and a-factor; Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the [...] (316 aa)
     
  0.999
BET4
Alpha subunit of Type II geranylgeranyltransferase required for vesicular transport between the endoplasmic reticulum and the Golgi; provides a membrane attachment moiety to Rab-like proteins Ypt1p and Sec4p; Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or -XCXC, where both cysteines may become modified. Acts on YPT1 and SEC4 (327 aa)
     
  0.996
RCE1
Type II CAAX prenyl protease involved in the proteolysis and maturation of Ras and the a-factor mating pheromone; Proteolytically removes the C-terminal three residues of farnesylated proteins, including the a-factor mating pheromone and RAS (315 aa)
       
  0.991
BTS1
Geranylgeranyl diphosphate synthase, increases the intracellular pool of geranylgeranyl diphosphate, suppressor of bet2 mutation that causes defective geranylgeranylation of small GTP-binding proteins that mediate vesicular traffic; Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane attachment of YPT1 and SEC4. May be involved in vesicle trafficking and protein sorting (335 aa)
     
  0.990
ERG20
Farnesyl pyrophosphate synthetase, has both dimethylallyltranstransferase and geranyltranstransferase activities; catalyzes the formation of C15 farnesyl pyrophosphate units for isoprenoid and sterol biosynthesis; Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (352 aa)
       
  0.988
STE24
Highly conserved zinc metalloprotease that functions in two steps of a-factor maturation, C-terminal CAAX proteolysis and the first step of N-terminal proteolytic processing; contains multiple transmembrane spans; Proteolytically removes the C-terminal three residues of farnesylated A-factor mating pheromone. Also acts to cleave the N- terminal extension of the pheromone. Does not act on Ras (453 aa)
         
  0.984
COQ1
Hexaprenyl pyrophosphate synthetase, catalyzes the first step in ubiquinone (coenzyme Q) biosynthesis; Assembly of polyisoprenoid side chains. The polyprenyl synthase of coenzyme Q biosynthesis catalyzes the formation from isopentenyl diphosphate of all trans-polyprenyl pyrophosphates generally ranging in length of between 6 and 10 isoprene units depending on the species (473 aa)
       
  0.971
RER2
Cis-prenyltransferase involved in dolichol synthesis; participates in endoplasmic reticulum (ER) protein sorting; With NUS1, forms the dehydrodolichyl diphosphate syntase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precusrosor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER) (286 aa)
     
 
  0.949
SRT1
Cis-prenyltransferase involved in synthesis of long-chain dolichols (19-22 isoprene units; as opposed to Rer2p which synthesizes shorter-chain dolichols); localizes to lipid bodies; transcription is induced during stationary phase; With NUS1, forms the dehydrodolichyl diphosphate syntase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precusrosor of dolichol which is utilized as a sugar carrier i [...] (343 aa)
     
 
  0.942
STE14
Farnesyl cysteine-carboxyl methyltransferase, mediates the carboxyl methylation step during C-terminal CAAX motif processing of a-factor and RAS proteins in the endoplasmic reticulum, localizes to the ER membrane; Mediates C-terminal methylation of the isoprenylated C- terminal cysteine in A-factor mating pheromone and Ras proteins (239 aa)
           
  0.933
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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