STRINGSTRING
JID1 protein (Saccharomyces cerevisiae) - STRING interaction network
"JID1" - Probable Hsp40p co-chaperone, has a DnaJ-like domain and appears to be involved in ER-associated degradation of misfolded proteins containing a tightly folded cytoplasmic domain in Saccharomyces cerevisiae
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
JID1Probable Hsp40p co-chaperone, has a DnaJ-like domain and appears to be involved in ER-associated degradation of misfolded proteins containing a tightly folded cytoplasmic domain; inhibits replication of Brome mosaic virus in S. cerevisiae; Probable chaperone (301 aa)    
Predicted Functional Partners:
APJ1
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)
     
   
  0.741
MDJ1
Co-chaperone that stimulates HSP70 protein Ssc1p ATPase activity; involved in protein folding/refolding in the mitochodrial matrix; required for proteolysis of misfolded proteins; member of the HSP40 (DnaJ) family of chaperones; Plays a role in mitochondrial biogenesis and protein folding (511 aa)
     
   
  0.734
SEC63
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)
           
  0.730
MDJ2
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; Plays a role in mitochondrial biogenesis and protein folding. Participates in the translocation of transit peptide- containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner, probably by stimulating activity of mtHSP70 (SSC1) (146 aa)
           
  0.730
JJJ1
Co-chaperone that stimulates the ATPase activity of Ssa1p, required for a late step of ribosome biogenesis; associated with the cytosolic large ribosomal subunit; contains a J-domain; mutation causes defects in fluid-phase endocytosis (590 aa)
           
  0.730
SIS1
Type II HSP40 co-chaperone that interacts with the HSP70 protein Ssa1p; not functionally redundant with Ydj1p due to due to substrate specificity; shares similarity with bacterial DnaJ proteins; Required for nuclear migration during mitosis. It is required for the normal initiation of translation. Might mediate the dissociation of a specific protein complex of the translation machinery. Essential for viability (352 aa)
           
  0.730
SCJ1
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)
           
  0.730
HLJ1
Co-chaperone for Hsp40p, anchored in the ER membrane; with its homolog Ydj1p promotes ER-associated protein degradation (ERAD) of integral membrane substrates; similar to E. coli DnaJ (224 aa)
           
  0.730
XDJ1
Putative chaperone, homolog of E. coli DnaJ, closely related to Ydj1p; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies (459 aa)
           
  0.730
PAM18
Constituent of the import motor (PAM complex) component of the Translocase of the Inner Mitochondrial membrane (TIM23 complex); essential J-protein cochaperone that stimulates Ssc1p ATPase activity to drive import; inhibited by Pam16p; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1) (168 aa)
           
  0.730
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
Server load: low (11%) [HD]