STRINGSTRING
MPD1 protein (Saccharomyces cerevisiae) - STRING interaction network
"MPD1" - Member of the protein disulfide isomerase 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
MPD1Member 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)    
Predicted Functional Partners:
GLT1
NAD(+)-dependent glutamate synthase (GOGAT), synthesizes glutamate from glutamine and alpha-ketoglutarate; with Gln1p, forms the secondary pathway for glutamate biosynthesis from ammonia; expression regulated by nitrogen source; Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate (2145 aa)
   
 
  0.957
MPD2
Member of the protein disulfide isomerase (PDI) family, exhibits chaperone activity; overexpression suppresses the lethality of a pdi1 deletion but does not complement all Pdi1p functions; undergoes oxidation by Ero1p; Non essential disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. Able to fold proteins by being directly oxidized by ERO1 (277 aa)
           
  0.937
TSA1
Thioredoxin peroxidase, acts as both a ribosome-associated and free cytoplasmic antioxidant; self-associates to form a high-molecular weight chaperone complex under oxidative stress; deletion results in mutator phenotype; Physiologically important antioxidant which constitutes an enzymatic defense against sulfur-containing radicals. Can provide protection against a thiol-containing oxidation system but not against an oxidation system without thiol (196 aa)
   
 
  0.878
TSA2
Stress inducible cytoplasmic thioredoxin peroxidase; cooperates with Tsa1p in the removal of reactive oxygen, nitrogen and sulfur species using thioredoxin as hydrogen donor; deletion enhances the mutator phenotype of tsa1 mutants; Reduces peroxides. May play an important role in eliminating peroxides generated during metabolism (By similarity) (196 aa)
   
 
  0.878
PRX1
Mitochondrial peroxiredoxin (1-Cys Prx) with thioredoxin peroxidase activity, has a role in reduction of hydroperoxides; reactivation requires Trr2p and glutathione; induced during respiratory growth and oxidative stress; phosphorylated; Has a thioredoxin peroxidase activity with a role in reduction of hydroperoxides (261 aa)
   
 
  0.878
TRR2
Mitochondrial thioredoxin reductase involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p; contains active-site motif (CAVC) present in prokaryotic orthologs; binds NADPH and FAD; Acts on mitochondrial thioredoxin 3. Implicated in the defense against oxidative stress (342 aa)
   
 
  0.877
TRR1
Cytoplasmic thioredoxin reductase, key regulatory enzyme that determines the redox state of the thioredoxin system, which acts as a disulfide reductase system and protects cells against both oxidative and reductive stress; Acts on thioredoxins 1 and 2 (319 aa)
   
 
  0.877
EPS1
ER protein with chaperone and co-chaperone activity, involved in retention of resident ER proteins; has a role in recognizing proteins targeted for ER-associated degradation (ERAD), member of the protein disulfide isomerase family; Acts as a membrane-bound chaperone in endoplasmic reticulum quality control. Probably facilitates presentation of substrate to membrane-bound components of the degradation machinery (701 aa)
           
  0.846
KAR2
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)
   
 
  0.834
GLR1
Cytosolic and mitochondrial glutathione oxidoreductase, converts oxidized glutathione to reduced glutathione; mitochondrial but not cytosolic form has a role in resistance to hyperoxia; Maintains high levels of reduced glutathione in the cytosol (483 aa)
   
 
  0.828
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 (9%) [HD]