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MCX1 protein (Saccharomyces cerevisiae) - STRING interaction network
"MCX1" - Mitochondrial matrix protein in Saccharomyces cerevisiae
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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MCX1Mitochondrial matrix protein; putative ATP-binding chaperone with non-proteolytic function; similar to bacterial ClpX proteins; ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5- aminolevulinate synthase (HEM1), thereby activating 5- aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Upregulates heme biosynthesis (520 aa)    
Predicted Functional Partners:
PIM1
ATP-dependent Lon protease, involved in degradation of misfolded proteins in mitochondria; required for biogenesis and maintenance of mitochondria; ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mi [...] (1133 aa)
   
 
  0.911
CCT3
Subunit of the cytosolic chaperonin Cct ring complex, related to Tcp1p, required for the assembly of actin and tubulins in vivo; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (534 aa)
     
 
  0.748
CCT4
Subunit of the cytosolic chaperonin Cct ring complex, related to Tcp1p, required for the assembly of actin and tubulins in vivo; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (528 aa)
     
 
  0.748
URA2
Bifunctional carbamoylphosphate synthetase/aspartate transcarbamylase; catalyzes the first two enzymatic steps in the de novo biosynthesis of pyrimidines; both activities are subject to feedback inhibition by UTP; This protein is a "fusion" protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase) (2214 aa)
         
  0.715
CCT2
Subunit beta of the cytosolic chaperonin Cct ring complex, related to Tcp1p, required for the assembly of actin and tubulins in vivo; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (527 aa)
     
 
  0.714
HSP78
Oligomeric mitochondrial matrix chaperone; cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; able to prevent the aggregation of misfolded proteins as well as resolubilize protein aggregates; Required, in concert with mitochondrial Hsp70 (SSC1), for the dissociation, resolubilization and refolding of aggregates of damaged proteins in the mitochondrial matrix after heat stress. May extract proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by the Hsp [...] (811 aa)
   
 
  0.701
JAC1
Specialized J-protein that 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; Co-chaperone required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria. Stimulates the ATPase activity of its specialized Hsp70 chaperone partner SSQ1. Binds to the substrate protein ISU1 and targets it to SSQ1. May function together with SSQ1 in the dislocation of the Fe/S cluster from ISU1 and its insertion into apoproteins (184 aa)
       
 
  0.691
CCT7
Subunit of the cytosolic chaperonin Cct ring complex, related to Tcp1p, required for the assembly of actin and tubulins in vivo; mutant has increased aneuploidy tolerance; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity) (550 aa)
     
 
  0.691
TCP1
Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (559 aa)
     
 
  0.691
ECM10
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)
   
 
  0.667
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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