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RPM2 protein (Saccharomyces cerevisiae) - STRING interaction network
"RPM2" - Protein subunit of mitochondrial RNase P, has roles in nuclear transcription, cytoplasmic and mitochondrial RNA processing, and mitochondrial translation in Saccharomyces cerevisiae
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Predicted Interactions
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textmining
co-expression
protein homology
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RPM2Protein subunit of mitochondrial RNase P, has roles in nuclear transcription, cytoplasmic and mitochondrial RNA processing, and mitochondrial translation; distributed to mitochondria, cytoplasmic processing bodies, and the nucleus; Ribonuclease P generates mature tRNA molecules by cleaving their 5’-ends (1202 aa)    
Predicted Functional Partners:
POP1
Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5’ ends and facilitates turnover of nuclear RNAs; binds to the RPR1 RNA subunit in RNase P; Required for processing of 5.8S rRNA (short form) at site A3 and for 5’ and 3’ processing of pre-tRNA (875 aa)
         
  0.873
RPR2
Subunit of nuclear RNase P; nuclear RNase P cleaves tRNA precursors to generate mature 5’ ends and facilitates turnover of nuclear RNAs; not shared between RNase MRP and RNase P, in contrast to all other RNase P protein subunits; Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5’-ends (144 aa)
         
  0.873
POP6
Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5’ ends and facilitates turnover of nuclear RNAs; Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5’-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences (158 aa)
         
  0.853
POP5
Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5’ ends and facilitates turnover of nuclear RNAs; Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5’-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences (173 aa)
         
  0.852
POP8
Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5’ ends and facilitates turnover of nuclear RNAs; Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5’-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences (133 aa)
         
  0.838
POP7
Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5’ ends and facilitates turnover of nuclear RNAs; Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5’-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences (140 aa)
         
  0.817
RPP1
Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5’ ends and facilitates turnover of nuclear RNAs; Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5’-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences (293 aa)
         
  0.814
POP4
Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5’ ends and facilitates turnover of nuclear RNAs; binds to the RPR1 RNA subunit in RNase P; Required for 5.8S rRNA and tRNA processing; associated with RNase MRP and RNase P (279 aa)
         
  0.813
POP3
Subunit of both RNase MRP and nuclear RNase P; RNase MRP cleaves pre-rRNA, while nuclear RNase P cleaves tRNA precursors to generate mature 5’ ends and facilitates turnover of nuclear RNAs; Required for processing of 5.8S rRNA (short form) at site A3 and for 5’- and 3’-processing of pre-tRNA (195 aa)
         
    0.800
DCP1
Subunit of the Dcp1p-Dcp2p decapping enzyme complex, which removes the 5’ cap structure from mRNAs prior to their degradation; enhances the activity of catalytic subunit Dcp2p; regulated by DEAD box protein Dhh1p; Component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5’-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent [...] (231 aa)
       
      0.735
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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