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SRP21 protein (Saccharomyces cerevisiae) - STRING interaction network
"SRP21" - Subunit of the signal recognition particle in Saccharomyces cerevisiae
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Predicted Interactions
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textmining
co-expression
protein homology
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SRP21Subunit of the signal recognition particle (SRP); SRP functions in protein targeting to the endoplasmic reticulum membrane; not found in mammalian SRP; forms a pre-SRP structure in the nucleolus that is translocated to the cytoplasm; Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex [...] (167 aa)    
Predicted Functional Partners:
SRP72
Core component of the signal recognition particle (SRP) ribonucleoprotein (RNP) complex that functions in targeting nascent secretory proteins to the endoplasmic reticulum (ER) membrane; Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the [...] (640 aa)
     
 
  0.987
SRP14
Signal recognition particle (SRP) subunit, interacts with the RNA component of SRP to form the Alu domain, which is the region of SRP responsible for arrest of nascent chain elongation during membrane targeting; homolog of mammalian SRP14; Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) co [...] (146 aa)
     
 
  0.987
SRP68
Core component of the signal recognition particle (SRP) ribonucleoprotein (RNP) complex that functions in targeting nascent secretory proteins to the endoplasmic reticulum (ER) membrane; Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the [...] (599 aa)
     
 
  0.986
SEC65
Subunit of the signal recognition particle (SRP), involved in protein targeting to the ER; interacts with Srp54p; homolog of mammalian SRP19; Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during me [...] (273 aa)
     
 
  0.969
SRP54
Signal recognition particle (SRP) subunit (homolog of mammalian SRP54); contains the signal sequence-binding activity of SRP, interacts with the SRP RNA, and mediates binding of SRP to signal receptor; contains GTPase domain; Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the E [...] (541 aa)
       
 
  0.962
LHP1
RNA binding protein required for maturation of tRNA and U6 snRNA; acts as a molecular chaperone for RNAs transcribed by polymerase III; homologous to human La (SS-B) autoantigen; Molecular chaperone that binds nascent RNA polymerase III transcripts, stabilizing these RNAs against exonucleases. Required for the 3’ endonucleolytic cleavage that matures tRNA precursors and for efficient folding of certain pre-tRNAs. Cooperaes with GCD14 in the maturation of a subset of RNA polymerase III transcripts. Functions also in the assembly of certain RNA polymerase II-transcribed RNAs into RNPs. B [...] (275 aa)
     
 
  0.880
HYP2
Translation elongation factor eIF-5A that may function in translation initiation; similar to and functionally redundant with Anb1p; structural homolog of bacterial EF-P; undergoes an essential hypusination modification; mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Essential for polarized growth, a process necessary for G [...] (157 aa)
       
      0.654
SRP102
Signal recognition particle (SRP) receptor beta subunit; involved in SRP-dependent protein targeting; anchors the alpha subunit, Srp101p to the ER membrane; Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. Has GTPase activity. May mediate the membrane association of SRPR (244 aa)
     
   
  0.447
NTG1
DNA N-glycosylase and apurinic/apyrimidinic (AP) lyase involved in base excision repair; acts in both nucleus and mitochondrion; creates a double-strand break at mtDNA origins that stimulates replication in response to oxidative stress; Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N- glycosidic bond, leaving an AP site. The AP-lyase [...] (399 aa)
           
  0.447
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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