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POC4 protein (Saccharomyces cerevisiae) - STRING interaction network
"POC4" - Component of a heterodimeric Poc4p-Irc25p chaperone involved in assembly of alpha subunits into the 20S proteasome in Saccharomyces cerevisiae
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POC4Component of a heterodimeric Poc4p-Irc25p chaperone involved in assembly of alpha subunits into the 20S proteasome; may regulate formation of proteasome isoforms with alternative subunits under different conditions; Involved in 20S proteasome assembly, facilitating the alpha-ring formation. Involved in maintenance of telomere length (148 aa)    
Predicted Functional Partners:
IRC25
Component of a heterodimeric Poc4p-Irc25p chaperone involved in assembly of alpha subunits into the 20S proteasome; may regulate formation of proteasome isoforms with alternative subunits under different conditions; Involved in 20S proteasome assembly, facilitating the alpha-ring formation (179 aa)
       
 
  0.994
PRE1
Beta 4 subunit of the 20S proteasome; localizes to the nucleus throughout the cell cycle; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. This subunit has a chymotrypsin-like activity (198 aa)
       
 
  0.920
PBA1
Protein involved in 20S proteasome assembly; forms a heterodimer with Add66p that binds to proteasome precursors; similar to human PAC1 constituent of the PAC1-PAC2 complex involved in proteasome assembly; Involved in 20S proteasome assembly (276 aa)
           
  0.893
ADD66
Protein involved in 20S proteasome assembly; forms a heterodimer with Pba1p that binds to proteasome precursors; similar to human PAC2 constituent of the PAC1-PAC2 complex involved in proteasome assembly; Involved in 20S proteasome assembly. Required for maximal proteasome activity. Affects the chymotrypsin-like activity of the proteasome. Can be degraded by the proteasome. Involved in the endoplasmic reticulum-associated degradation (ERAD) (267 aa)
           
  0.892
PUP2
Alpha 5 subunit of the 20S proteasome involved in ubiquitin-dependent catabolism; human homolog is subunit zeta; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity (260 aa)
       
 
  0.873
UMP1
Short-lived chaperone required for correct maturation of the 20S proteasome; may inhibit premature dimerization of proteasome half-mers; degraded by proteasome upon completion of its assembly; Short-lived chaperone present in the precursor form of the 20S proteasome and absent in the mature complex. Required for the correct assembly and enzymatic activation of the proteasome. Also prevents premature processing of the PRE2 propeptide (148 aa)
       
 
  0.780
PRE8
Alpha 2 subunit of the 20S proteasome; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity (250 aa)
       
 
  0.709
CYC7
Cytochrome c isoform 2, expressed under hypoxic conditions; electron carrier of the mitochondrial intermembrane space that transfers electrons from ubiquinone-cytochrome c oxidoreductase to cytochrome c oxidase during cellular respiration; Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain (113 aa)
       
      0.699
PRE6
Alpha 4 subunit of the 20S proteasome; may replace alpha 3 subunit (Pre9p) under stress conditions to create a more active proteasomal isoform; GFP-fusion protein relocates from cytosol to the mitochondrial surface upon oxidative stress; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving [...] (254 aa)
       
      0.647
NAS6
Proteasome-interacting protein involved in the assembly of the base subcomplex of the 19S proteasomal regulatory particle (RP); ortholog of human oncoprotein gankyrin, which interacts with the Rb tumor suppressor and CDK4/6; Acts as a chaperone during the assembly of the 26S proteasome, specifically of the 19S regulatory complex (RC) and appears to have an overlapping role with RPN14 (228 aa)
           
  0.641
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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