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rpl16 rpl16 rpl2-A rpl2-A ndhD ndhD ndhG ndhG ndhH ndhH ndhB1 ndhB1 ndhJ ndhJ ndhK ndhK ndhC ndhC clpP clpP
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.
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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:
rpl1650S ribosomal protein L16, chloroplastic; Belongs to the universal ribosomal protein uL16 family. (136 aa)
rpl2-A50S ribosomal protein L2, chloroplastic; Belongs to the universal ribosomal protein uL2 family. (271 aa)
ndhDNAD(P)H-quinone oxidoreductase chain 4, chloroplastic. (500 aa)
ndhGNAD(P)H-quinone oxidoreductase subunit 6, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity). (176 aa)
ndhHNAD(P)H-quinone oxidoreductase subunit H, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. (393 aa)
ndhB1NAD(P)H-quinone oxidoreductase subunit 2 A, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. (510 aa)
ndhJNAD(P)H-quinone oxidoreductase subunit J, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. (159 aa)
ndhKNAD(P)H-quinone oxidoreductase subunit K, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Belongs to the complex I 20 kDa subunit family. (227 aa)
ndhCNAD(P)H-quinone oxidoreductase subunit 3, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. (120 aa)
clpPATP-dependent Clp protease proteolytic subunit; 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. Belongs to the peptidase S14 family. (216 aa)
Your Current Organism:
Sorghum bicolor
NCBI taxonomy Id: 4558
Other names: Andropogon sorghum, Andropogon sorghum (L.) Brot., S. bicolor, Sorghum bicolor (L.) Moench, Sorghum bicolor subsp. bicolor, Sorghum nervosum, Sorghum nervosum Besser ex Schult., Sorghum saccharatum, Sorghum saccharatum (L.) Moench, Sorghum vulgare, Sorghum vulgare Pers., broomcorn, milo, sorghum
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