PRC1 protein (Saccharomyces cerevisiae) - STRING interaction network
"PRC1" - Vacuolar carboxypeptidase Y (proteinase C, CPY) in Saccharomyces cerevisiae
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Known Interactions
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Predicted Interactions
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Gene Fusion
PRC1Vacuolar 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)    
Predicted Functional Partners:
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)
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)
Type I transmembrane sorting receptor for multiple vacuolar hydrolases; cycles between the late-Golgi and prevacuolar endosome-like compartments; Functions as a sorting receptor in the Golgi compartment required for the intracellular sorting and delivery of soluble vacuolar proteins, like carboxypeptidase Y (CPY) and proteinase A. May execute multiple rounds of sorting by cycling between the late Golgi and a prevacuolar endosome-like compartment. Binds the Golgi-modified P2 form of CPY, and this interaction is dependent on the presence of an intact CPY vacuolar protein sorting signal (1579 aa)
Essential subunit of Sec61 complex (Sec61p, Sbh1p, and Sss1p); forms a channel for SRP-dependent protein import and retrograde transport of misfolded proteins out of the ER; with Sec63 complex allows SRP-independent protein import into ER; Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post- translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded pro [...] (480 aa)
Adenylate cyclase, required for cAMP production and cAMP-dependent protein kinase signaling; the cAMP pathway controls a variety of cellular processes, including metabolism, cell cycle, stress response, stationary phase, and sporulation; Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP (2026 aa)
Vacuolar 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)
ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis (682 aa)
Subtilisin-like protease (proprotein convertase), a calcium-dependent serine protease involved in the activation of proproteins of the secretory pathway; Processing of precursors of alpha-factors and killer toxin (814 aa)
Ubiquitin, becomes conjugated to proteins, marking them for selective degradation via the ubiquitin-26S proteasome system; essential for the cellular stress response; encoded as a polyubiquitin precursor comprised of 5 head-to-tail repeats; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiqui [...] (381 aa)
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)
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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