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CLPB3 CLPB3 CLPC1 CLPC1 ERD1 ERD1 CLPX CLPX CLPP3 CLPP3 AT4G12060 AT4G12060 AT5G49840 AT5G49840 AT1G33360 AT1G33360 CLPP6 CLPP6 AT4G25370 AT4G25370 HSP93-III HSP93-III
"CLPP6" - CLP protease proteolytic subunit 6 in Arabidopsis thaliana
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
CLPP6CLP protease proteolytic subunit 6 (289 aa)    
Predicted Functional Partners:
CLPX
CLP protease regulatory subunit X; ATP-dependent specificity component of the mitochondrial Clp protease (PubMed-11352464). It directs the protease to specific substrates (By similarity). Can perform chaperone functions in the absence of ClpP (By similarity) (579 aa)
 
 
  0.983
AT4G25370
Double Clp-N motif protein; Accessory protein regulating the assembly of the plastidial Clp protease system (PubMed-21266658, PubMed-25921872). CLPT1 first binds to the heptameric P-ring containing the CLP3-6 subunits followed by CLPT2, and only then does the P-ring combine with the R-ring composed of the clpP1 and CLPR1-4 subunits (PubMed-21266658). Once the core complex is fully assembled, it then associates to the CLPC chaperone partner to form the functional protease (PubMed-21266658). CLPT1 and CLPT2 are partially redundant (PubMed-25921872) (238 aa)
   
 
  0.968
AT5G49840
ATP-dependent Clp protease; ATP-dependent specificity component of the mitochondrial Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (608 aa)
 
 
  0.967
AT1G33360
ATP-dependent Clp protease; ATP-dependent specificity component of the mitochondrial Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (656 aa)
 
 
  0.946
AT4G12060
Double Clp-N motif protein; Accessory protein regulating the assembly of the plastidial Clp protease system (PubMed-21266658, PubMed-25921872). CLPT1 first binds to the heptameric P-ring containing the CLP3-6 subunits followed by CLPT2, and only then does the P-ring combine with the R-ring composed of the clpP1 and CLPR1-4 subunits (PubMed-21266658). Once the core complex is fully assembled, it then associates to the CLPC chaperone partner to form the functional protease (PubMed-21266658). CLPT2 and CLPT1 are partially redundant (PubMed-25921872) (241 aa)
     
 
  0.920
CLPC1
CLPC homologue 1; Molecular chaperone that hydrolyzes ATP and is associated with the chloroplast protein import apparatus. May function as the motor for chloroplast protein translocation, as translocation requires ATP hydrolysis in the stroma. May interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast. Involved in the regulation of chlorophyll b biosynthesis through the destabilization of chlorophyllide a oxygenase (CAO) protein in response to the accumulation of chlorophyll b. Involved in leaf iron homeostasis (929 aa)
   
 
  0.902
CLPB3
Casein lytic proteinase B3; Molecular chaperone essential for chloroplast development and seedling viability. Mediates internal thylakoid membrane formation and confers thermotolerance to chloroplasts during heat stress (968 aa)
   
 
  0.843
ERD1
ERD1 protein; Molecular chaperone that interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast (PubMed-21737456). The ATPase activity of CLPD is stimulated by CLPT1 (PubMed-25149061). Has no ADPase activity (PubMed-21737456). Interacts with transit peptides with a positional preference (PubMed-21737456, PubMed-22545953). Localization of the signal sequence at the N-terminal end of a protein seems mandatory for interaction to take place (PubMed-22545953) (945 aa)
   
 
  0.835
HSP93-III
Clp ATPase; Molecular chaperone (PubMed-15304652, PubMed-21737456, PubMed-24599948). May act as a suppressor of FtsH-mediated thylakoid membrane biogenesis and may enhance photoinhibition (PubMed-15304652). Seems not involved in chloroplastic protein import (PubMed-15304652). Probable component of the TIC-associated stromal import motor involved in inner membrane translocation (PubMed-17376159). Has an ATPase activity, but no ADPase activity (PubMed-21737456). Interacts with transit peptides with a positional preference (PubMed-21737456, PubMed-22545953). Localization of the signal seq [...] (952 aa)
   
 
  0.828
CLPP3
CLP protease proteolytic subunit 3; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). In the absence of CLPP3, modified ClpPR core(s) could be formed, albeit at strongly reduced levels (PubMed-23548781) (309 aa)
   
 
0.794
Your Current Organism:
Arabidopsis thaliana
NCBI taxonomy Id: 3702
Other names: A. thaliana, Arabidopsis thaliana, Arabidopsis thaliana (L.) Heynh., mouse-ear cress, thale cress, thale-cress
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