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SHR5 protein (Saccharomyces cerevisiae) - STRING interaction network
"SHR5" - Subunit of a palmitoyltransferase, composed of Shr5p and Erf2p, that adds a palmitoyl lipid moiety to heterolipidated substrates such as Ras1p and Ras2p through a thioester linkage in Saccharomyces cerevisiae
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SHR5Subunit of a palmitoyltransferase, composed of Shr5p and Erf2p, that adds a palmitoyl lipid moiety to heterolipidated substrates such as Ras1p and Ras2p through a thioester linkage; palmitoylation is required for Ras2p membrane localization; The ERF2-SHR5 complex is a palmitoyltransferase specific for Ras proteins. Palmitoylates RAS2, which is required for its proper plasma membrane localization (237 aa)    
Predicted Functional Partners:
ERF2
Subunit of a palmitoyltransferase, composed of Erf2p and Shr5p, that adds a palmitoyl lipid moiety to heterolipidated substrates such as Ras1p and Ras2p through a thioester linkage; mutants partially mislocalize Ras2p to the vacuole; The ERF2-SHR5 complex is a palmitoyltransferase specific for Ras proteins. Palmitoylates RAS2, which is required for its proper plasma membrane localization (359 aa)
     
  0.989
PFA5
Palmitoyltransferase with autoacylation activity; likely functions in pathway(s) outside Ras; member of a family of putative palmitoyltransferases containing an Asp-His-His-Cys-cysteine rich (DHHC-CRD) domain (374 aa)
     
 
  0.855
RAS2
GTP-binding protein that regulates the nitrogen starvation response, sporulation, and filamentous growth; farnesylation and palmitoylation required for activity and localization to plasma membrane; homolog of mammalian Ras proto-oncogenes; The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP (322 aa)
       
 
  0.818
AKR1
Palmitoyl transferase involved in protein palmitoylation; acts as a negative regulator of pheromone response pathway; required for endocytosis of pheromone receptors; involved in cell shape control; contains ankyrin repeats; Palmitoyltransferase specific for casein kinase 1. Palmitoylates isoforms YCK1 and YCK2 at both C-terminal cysteine residues, which is required for their proper plasma membrane localization. Required for constitutive endocytosis of a-factor receptor STE3 and both constitutive and pheromone-induced endocytosis of alpha-factor receptor STE2 (764 aa)
     
 
  0.800
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)
       
 
  0.793
PFA4
Palmitoyltransferase with autoacylation activity, required for palmitoylation of amino acid permeases containing a C-terminal Phe-Trp-Cys site; required for modification of Chs3p; member of the DHHC family of putative palmitoyltransferases; Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function. Palmitoylates several amino acid permeases (PubMed-16751107). Palmitoylates chitin synthase CHS3, which is required for its proper export from the ER (PubMed-16818716). Can palmitoylate RAS2 in vitro (PubMed-12379641) (378 aa)
     
 
  0.762
PFA3
Palmitoyltransferase for Vac8p, required for vacuolar membrane fusion; contains an Asp-His-His-Cys-cysteine rich (DHHC-CRD) domain; autoacylates; required for vacuolar integrity under stress conditions; Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at one or more of its N-terminal cysteine residues, which is required for its proper membrane localization (336 aa)
     
 
  0.762
SWF1
Palmitoyltransferase that acts on transmembrane proteins, including the SNAREs Snc1p, Syn8p, Tlg1p and likely all SNAREs; contains an Asp-His-His-Cys-cysteine rich (DHHC-CRD) domain; may have a role in vacuole fusion; Palmitoyltransferase that targets several endosomal SNAREs. Palmitoylates the SNAREs SNC1, SNC2, SYN8 and TLG1, at cysteine residues close to the cytoplasmic end of their transmembrane domain. May have a role in the cellular quality control of transmembrane domain-containing proteins (336 aa)
     
 
  0.748
TSC3
Protein that stimulates the activity of serine palmitoyltransferase (Lcb1p, Lcb2p) several-fold; involved in sphingolipid biosynthesis; Stimulates the activity of serine palmitoyltransferase (SPT) (80 aa)
         
  0.727
LCB1
Component of serine palmitoyltransferase, responsible along with Lcb2p for the first committed step in sphingolipid synthesis, which is the condensation of serine with palmitoyl-CoA to form 3-ketosphinganine; Component of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine (558 aa)
         
    0.720
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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