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PRB1 protein (Saccharomyces cerevisiae) - STRING interaction network
"PRB1" - Vacuolar proteinase B in Saccharomyces cerevisiae
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second shell of interactors
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proteins of unknown 3D structure
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Known Interactions
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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PRB1Vacuolar proteinase B (yscB), a serine protease of the subtilisin family; involved in protein degradation in the vacuole and required for full protein degradation during sporulation; activity inhibited by Pbi2p; Vacuolar proteinase B involved in protein degradation in the vacuole. Among other substrates, acts on carboxypeptidase Y (cpY/PRC1) to activate it by processing its Pro-peptide. Required for meiosis and spore formation, and for optimal survival in stationary phase (635 aa)    
Predicted Functional Partners:
PEP4
Vacuolar aspartyl protease (proteinase A), required for the posttranslational precursor maturation of vacuolar proteinases; important for protein turnover after oxidative damage; synthesized as a zymogen, self-activates; Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself (405 aa)
     
 
  0.987
TFS1
Protein that interacts with and inhibits carboxypeptidase Y and Ira2p; phosphatidylethanolamine-binding protein (PEBP) family member; targets to vacuolar membranes during stationary phase; acetylated by NatB N-terminal acetyltransferase; Specific and potent inhibitor of carboxypeptidase Y (219 aa)
     
   
  0.970
PRC1
Vacuolar carboxypeptidase Y (proteinase C, CPY); broad-specificity C-terminal exopeptidase involved in non-specific protein degradation in the vacuole; member of the serine carboxypeptidase family; Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1’ position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (532 aa)
     
 
  0.954
CHC1
Clathrin heavy chain, subunit of the major coat protein involved in intracellular protein transport and endocytosis; two heavy chains form the clathrin triskelion structural component; the light chain (CLC1) is thought to regulate function; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi (1653 aa)
     
 
  0.935
RRT12
Probable subtilisin-family protease; role in formation of the dityrosine layer of spore walls; localizes to the spore wall and also the nuclear envelope and ER region in mature spores; Subtilisin-related protease involved in the formation of a protective dityrosine layer required for spore wall assembly. Identified in a screen for mutants with increased levels of rDNA transcription (491 aa)
   
   
0.918
CPS1
Vacuolar carboxypeptidase S; expression is induced under low-nitrogen conditions; Necessary for use of certain peptides as sole nitrogen source. May also cleave intracellularly generated peptides to recycle amino acids for protein synthesis (576 aa)
     
 
  0.917
PBI2
Cytosolic inhibitor of vacuolar proteinase B (PRB1), required for efficient vacuole inheritance; with thioredoxin forms protein complex LMA1, which assists in priming SNARE molecules and promotes vacuole fusion; Cytosolic inhibitor of vacuolar proteinase B (yscB), probably regulating protease B activity during limited proteolysis. PBI2 is a component of the LMA1 complex, which is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi (75 aa)
     
 
  0.917
APM1
Mu1-like medium subunit of the clathrin-associated protein complex (AP-1); binds clathrin; involved in clathrin-dependent Golgi protein sorting; Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin. AP57 is probably a subunit of the Golgi membrane adaptor (475 aa)
       
  0.913
APL3
Alpha-adaptin, large subunit of the clathrin associated protein complex (AP-2); involved in vesicle mediated transport; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Alpha adaptin is a subunit of the plasma membrane adaptor. Facilitates interaction between APL1 and APS2 (1025 aa)
     
 
  0.908
YSP3
Putative precursor to the subtilisin-like protease III; Serine protease with unknown substrate (478 aa)
   
   
0.902
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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