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
A0A0E0MQ08Uncharacterized protein. (298 aa)    
Predicted Functional Partners:
A0A0E0JE27
S5A_REDUCTASE domain-containing protein.
    
 0.934
A0A0E0JJX9
Cytochrome b5 heme-binding domain-containing protein.
     
 0.882
A0A0E0M029
Cytochrome b5 heme-binding domain-containing protein.
     
 0.882
A0A0E0LVB2
FA_desaturase domain-containing protein.
     
 0.788
A0A0E0JE31
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase; Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors [...]
    
 0.711
A0A0E0JE36
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase; Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors [...]
    
 0.711
A0A0E0JE37
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase; Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors [...]
    
 0.711
A0A0E0L3F7
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase; Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors [...]
    
 0.711
A0A0E0K869
2-Hacid_dh_C domain-containing protein.
     
 0.639
A0A0E0MA34
2-Hacid_dh_C domain-containing protein.
     
 0.639
Your Current Organism:
Oryza punctata
NCBI taxonomy Id: 4537
Other names: O. punctata, Oryza punctata Kotschy ex Steud.
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