SIL1 protein (Saccharomyces cerevisiae) - STRING interaction network
"SIL1" - Nucleotide exchange factor for the ER lumenal Hsp70 chaperone Kar2p in Saccharomyces cerevisiae
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Known Interactions
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Predicted Interactions
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Gene Fusion
SIL1Nucleotide exchange factor for the ER lumenal Hsp70 chaperone Kar2p; required for protein translocation into the endoplasmic reticulum (ER); homolog of Yarrowia lipolytica SLS1; GrpE-like protein; Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone KAR2 (421 aa)    
Predicted Functional Partners:
Molecular chaperone of the endoplasmic reticulum lumen, involved in polypeptide translocation and folding; nucleotide exchange factor for the ER lumenal Hsp70 chaperone Kar2p; regulated by the unfolded protein response pathway; Chaperone required for protein translocation and folding in the endoplasmic reticulum (881 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)
Serine-threonine kinase and endoribonuclease; transmembrane protein that mediates the unfolded protein response (UPR) by regulating Hac1p synthesis through HAC1 mRNA splicing; Kar2p binds inactive Ire1p and releases from it upon ER stress; Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices HAC1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes (1115 aa)
Dubious open reading frame unlikely to encode a functional protein, based on available experimental and comparative sequence data (123 aa)
Essential subunit of Sec63 complex (Sec63p, Sec62p, Sec66p and Sec72p); with Sec61 complex, Kar2p/BiP and Lhs1p forms a channel competent for SRP-dependent and post-translational SRP-independent protein targeting and import into the ER; Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. [...] (663 aa)
ATPase involved in protein folding and nuclear localization signal (NLS)-directed nuclear transport; member of heat shock protein 70 (HSP70) family; forms a chaperone complex with Ydj1p; localized to the nucleus, cytoplasm, and cell wall; 98% identi /.../th Ssa2p, but subtle differences between the two proteins provide functional specificity with respect to propagation of yeast [URE3] prions and vacuolar-mediated degradations of gluconeogenesis enzymes; May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functio [...] (642 aa)
Member of the protein disulfide isomerase (PDI) family; interacts with and inhibits the chaperone activity of Cne1p; MPD1 overexpression in a pdi1 null mutant suppresses defects in Pdi1p functions such as carboxypeptidase Y maturation; Participates in the folding of proteins containing disulfide bonds (318 aa)
One of several homologs of bacterial chaperone DnaJ, located in the ER lumen where it cooperates with Kar2p to mediate maturation of proteins; Regulates protein folding in the endoplasmic reticulum lumen. Probably acts as a J-protein for the Hsp70-type chaperone KAR2 by stimulating its ATP-dependent reaction cycle and initiating folding reactions. Also involved in the endoplasmic reticulum-associated degradation (ERAD) process. Cooperates with KAR2 and another J-protein JEM1 to facilitate the export of ERAD substrates to the cytoplasm by maintaining them in a translocation-competent st [...] (377 aa)
DnaJ-like chaperone required for nuclear membrane fusion during mating, localizes to the ER membrane; exhibits genetic interactions with KAR2; Acts as a DnaJ-like chaperone required for nuclear membrane fusion during mating (645 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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