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Hop1 protein (Arabidopsis thaliana) - STRING interaction network
Hop1 in Arabidopsis thaliana
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
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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[Homology]
Score
Hop1Hop1; Mediates the association of the molecular chaperones HSP70 and HSP90. Mediates nuclear encoded chloroplast preproteins binding to HSP90 prior to chloroplastic sorting (By similarity) (572 aa)    
Predicted Functional Partners:
SHD
SHEPHERD; May have a molecular chaperone role in the processing of secreted materials. Required for shoot apical meristem (SAM), root apical meristem (RAM) and floral meristem (FM) formation, probably by regulating the folding of CLAVATA proteins (CLVs). Also involved in pollen tube elongation (PubMed-11867518). Involved in resistance to tunicamycin- or high calcium-induced ER stresses. Possesses ATPase activity (PubMed-25297550) (823 aa)
     
 
  0.998
Hsp89.1
HEAT SHOCK PROTEIN 89.1; Molecular chaperone which stabilizes unfolding protein intermediates and functions as a folding molecular chaperone that assists the non-covalent folding of proteins in an ATP-dependent manner (799 aa)
     
 
  0.996
Hsp81.4
HEAT SHOCK PROTEIN 81.4; Molecular chaperone which stabilizes unfolding protein intermediates and functions as a folding molecular chaperone that assists the non-covalent folding of proteins in an ATP-dependent manner (699 aa)
     
 
  0.995
CR88
Chaperone protein htpG family protein; Molecular chaperone required for chloroplast biogenesis (PubMed-12943545, PubMed-25216779). Essential for chloroplast biogenesis and maintenance, and thus for embryogenesis (PubMed-23875936, PubMed-23382192). May be involved in the disassembly of VIPP1 for thylakoid membrane formation and/or maintenance (PubMed-23875936). Cooperates with TIC components and other molecular chaperones to drive transport of preproteins into chloroplasts and functions in the chloroplast stroma to facilitate membrane translocation during protein import into the organel [...] (780 aa)
     
 
  0.995
HSP81-3
Heat shock protein 81-3; Functions as a holding molecular chaperone (holdase) which stabilizes unfolding protein intermediates and rapidly releases them in an active form once stress has abated. Functions as a folding molecular chaperone (foldase) that assists the non- covalent folding of proteins in an ATP-dependent manner (PubMed-23827697). Regulates RPP4-mediated temperature-dependent cell death and defense responses (PubMed-24611624). May assist SGT1B in the formation of SCF E3 ubiquitin ligase complexes that target the immune receptors SNC1, RPS2 and RPS4 for degradation, to regul [...] (699 aa)
     
 
  0.994
HSP81-2
Heat shock protein 81-2 (728 aa)
     
 
  0.994
HSP90.1
Heat shock protein 81-1; Functions as a holding molecular chaperone (holdase) which stabilizes unfolding protein intermediates and rapidly releases them in an active form once stress has abated. Functions as a folding molecular chaperone (foldase) that assists the non- covalent folding of proteins in an ATP-dependent manner (PubMed-23827697). Molecular chaperone involved in R gene-mediated disease resistance. Required for full RPS2-mediated resistance through interaction with RAR1. Possesses probably ATPase activity (PubMed-14504384) (705 aa)
     
 
  0.994
AT5G58110
Chaperone binding;ATPase activators (196 aa)
     
 
  0.992
AT3G12050
Aha1 domain-containing protein (360 aa)
     
 
  0.992
ASY1
ASYNAPTIC 1 (596 aa)
     
   
  0.960
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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