STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
jmjd-3.3JmjC domain-containing protein. (753 aa)    
Predicted Functional Partners:
atp-3
ATP synthase subunit.
  
 0.953
F58F12.1
ATP synthase subunit delta, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the c [...]
  
 0.953
atp-6
ATP synthase subunit a; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subuni [...]
  
 0.953
Y69A2AR.18
Uncharacterized protein.
  
 0.953
pis-1
PIS (Pax-2, IA-1/6, Smad-2 interacting protein) homolog.
    
 0.897
atp-5
ATP synthase subunit.
   
 0.884
atp-1
ATP synthase subunit alpha, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the [...]
  
 0.877
T26E3.7
ATP-synt_ab domain-containing protein.
  
 0.877
jmjd-1.2
Lysine-specific demethylase 7 homolog; Histone demethylase required for nervous system development. Specifically demethylates dimethylated 'Lys-9' and 'Lys-27' (H3K9me2 and H3K27me2, respectively) of histone H3, thereby playing a central role in histone code. Promotes mitochondrial stress- induced longevity ; Belongs to the JHDM1 histone demethylase family. JHDM1D subfamily.
    
 0.873
vha-2
V-type proton ATPase 16 kDa proteolipid subunit 2; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase (By similarity). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity). Involved in necrotic cell death. Required along with other vacuolar ATPase components for the removal of protein aggregates which form in immature oocytes in the distal gonad. This removal occurs as the oocytes mature and move to the proximal gonad, is triggered by the introduction of sperm through mating and occ [...]
  
 0.822
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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