STRINGSTRING
NDUS8 NDUS8 FRO1 FRO1 A4A49_19357 A4A49_19357 A4A49_18137 A4A49_18137 A4A49_16147 A4A49_16147 A4A49_10813 A4A49_10813 A4A49_05168 A4A49_05168
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:
NDUS8Nadh dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial. (252 aa)
FRO1Nadh dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial. (156 aa)
A4A49_19357Nadh dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial. (116 aa)
A4A49_18137Nadh dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8-b. (105 aa)
A4A49_16147Nadh dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial. (397 aa)
A4A49_10813Nadh dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2. (98 aa)
A4A49_05168NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12; Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. (158 aa)
Your Current Organism:
Nicotiana attenuata
NCBI taxonomy Id: 49451
Other names: N. attenuata, Nicotiana attenuata Torr. ex S.Watson
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