JEM1 protein (Saccharomyces cerevisiae) - STRING interaction network
"JEM1" - DnaJ-like chaperone required for nuclear membrane fusion during mating, localizes to the ER membrane in Saccharomyces cerevisiae
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
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Gene Fusion
JEM1DnaJ-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)    
Predicted Functional Partners:
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)
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)
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)
Type I membrane protein with a J domain; required to preserve the folding capacity of the endoplasmic reticulum; loss of the non-essential ERJ5 gene leads to a constitutively induced unfolded protein response; DnaJ-like chaperone required for the folding capacity of the endoplasmic reticulum (295 aa)
Putative protein of unknown function; mutant is deficient in amounts of cell wall mannosylphosphate and has long chronological lifespan; genetic interactions suggest a role in ER-associated protein degradation (ERAD); Probable component of the endoplasmic reticulum- associated degradation (ERAD) pathway that acts upstream of HRD3 and USA1 (131 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)
ATPase that is a component of the heat shock protein Hsp90 chaperone complex; binds unfolded proteins; member of the heat shock protein 70 (HSP70) family; localized to the cytoplasm; Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures (693 aa)
Heat shock protein of the Hsp70 family, localized in mitochondrial nucleoids, plays a role in protein translocation, interacts with Mge1p in an ATP-dependent manner; overexpression induces extensive mitochondrial DNA aggregations; Plays a role in facilitating the assembly of some protein complexes inside the mitochondria. It may initiate the events that lead to refolding of imported precursors in the matrix space (644 aa)
Mitochondrial hsp70-type molecular chaperone, required for assembly of iron/sulfur clusters into proteins at a step after cluster synthesis, and for maturation of Yfh1p, which is a homolog of human frataxin implicated in Friedreich’s ataxia; Has a role in mitochondrial iron homeostasis. Appears to be involved in the processing of the intermediate form of the frataxin homolog YFH1. Required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria (657 aa)
Putative chaperone of the HSP40 (DNAJ) family; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; Putative chaperone involved in protein folding. Interferes with propagation of [PSI+] prion when overproduced (528 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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