STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
JEM1DnaJ-like chaperone required for nuclear membrane fusion during mating; localizes to the ER membrane; exhibits genetic interactions with KAR2. (645 aa)    
Predicted Functional Partners:
LCL2
Long chronological lifespan protein 2; Putative protein of unknown function; mutant is deficient in cell wall mannosylphosphate and has long chronological lifespan; genetic interactions suggest a role in ER-associated protein degradation (ERAD); SWAT-GFP fusion protein localizes to the endoplasmic reticulum and vacuole, while mCherry fusion localizes to just the vacuole.
   
   0.994
SCJ1
DnaJ-related protein SCJ1; One of several homologs of bacterial chaperone DnaJ; located in the ER lumen where it cooperates with Kar2p to mediate maturation of proteins.
   
0.985
KAR2
Endoplasmic reticulum chaperone BiP; 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.
  
 0.974
LHS1
Heat shock protein 70 homolog LHS1; 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.
  
 0.941
ERJ5
ER-localized J domain-containing protein 5; 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; Belongs to the DnaJ family.
   
 
 0.916
JJJ3
Diphthamide biosynthesis protein 4; Protein of unknown function; contains a CSL Zn finger and a DnaJ-domain; involved in diphthamide biosynthesis; ortholog human Dph4; Belongs to the DPH4 family.
   
  
 0.845
SWA2
Auxilin-like clathrin uncoating factor SWA2; Auxilin-like protein involved in vesicular transport; clathrin-binding protein required for uncoating of clathrin-coated vesicles.
   
 
 0.833
JAC1
J-type co-chaperone JAC1, mitochondrial; Specialized J-protein that functions in Fe-S cluster biogenesis; functions with Hsp70 in Fe-S cluster biogenesis in mitochondria; involved in iron metabolism; contains a J domain typical to J-type chaperones; localizes to the mitochondrial matrix.
   
  
 0.832
JJJ2
J protein JJJ2; Protein of unknown function; contains a J-domain, which is a region with homology to the E. coli DnaJ protein.
   
  
 0.823
MDJ2
Mitochondrial DnaJ homolog 2; Constituent of the mitochondrial import motor; associated with the presequence translocase; function overlaps with that of Pam18p; stimulates the ATPase activity of Ssc1p to drive mitochondrial import; contains a J domain.
   
  
 0.821
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.