STRINGSTRING
C5WQR1_SORBI C5WQR1_SORBI C5WRD5_SORBI C5WRD5_SORBI C5WUR7_SORBI C5WUR7_SORBI C5WZX4_SORBI C5WZX4_SORBI C5XD18_SORBI C5XD18_SORBI C5XEC4_SORBI C5XEC4_SORBI C5XGM4_SORBI C5XGM4_SORBI C5XIC9_SORBI C5XIC9_SORBI C5XIZ5_SORBI C5XIZ5_SORBI C5XLB7_SORBI C5XLB7_SORBI C5XNF5_SORBI C5XNF5_SORBI C5XPH5_SORBI C5XPH5_SORBI C5XVW3_SORBI C5XVW3_SORBI C5XZJ0_SORBI C5XZJ0_SORBI C5YTK7_SORBI C5YTK7_SORBI C5YUG3_SORBI C5YUG3_SORBI C5Z141_SORBI C5Z141_SORBI C5Z238_SORBI C5Z238_SORBI C5Z3H5_SORBI C5Z3H5_SORBI ndhB1 ndhB1 ndhB2 ndhB2 ndhF ndhF C5WN22_SORBI C5WN22_SORBI C5WME2_SORBI C5WME2_SORBI ndhH ndhH ndhA ndhA ndhI ndhI psaC psaC ndhD ndhD ndhC ndhC ndhK ndhK ndhJ ndhJ A0A1Z5SA07 A0A1Z5SA07 Nad7 Nad7 A0A1Z5R346 A0A1Z5R346 Nad2 Nad2 Nad4 Nad4 A0A1W0VXQ9 A0A1W0VXQ9 A0A1W0VUZ4 A0A1W0VUZ4 A0A1W0VU17 A0A1W0VU17 A0A1W0VT45 A0A1W0VT45 A0A1B6QLK3 A0A1B6QLK3 A0A1B6QHS2 A0A1B6QHS2 A0A1B6QFX4 A0A1B6QFX4 A0A1B6QDG1 A0A1B6QDG1 A0A1B6Q6E1 A0A1B6Q6E1 A0A1B6PFP2 A0A1B6PFP2 A0A1B6PAC4 A0A1B6PAC4 A0A1B6P999 A0A1B6P999 A0A194YRJ8 A0A194YRJ8
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:
C5WQR1_SORBIUncharacterized protein. (104 aa)
C5WRD5_SORBIUncharacterized protein. (200 aa)
C5WUR7_SORBIUncharacterized protein. (143 aa)
C5WZX4_SORBIUncharacterized protein. (108 aa)
C5XD18_SORBIUncharacterized protein. (157 aa)
C5XEC4_SORBIWRKY domain-containing protein. (413 aa)
C5XGM4_SORBIUncharacterized protein. (229 aa)
C5XIC9_SORBIOxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. (200 aa)
C5XIZ5_SORBICIA30 domain-containing protein. (109 aa)
C5XLB7_SORBIUncharacterized protein. (132 aa)
C5XNF5_SORBICIA30 domain-containing protein. (229 aa)
C5XPH5_SORBIProtein arginine methyltransferase NDUFAF7; Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). (499 aa)
C5XVW3_SORBIEpimerase domain-containing protein. (408 aa)
C5XZJ0_SORBIWRKY domain-containing protein. (375 aa)
C5YTK7_SORBIMethyltransf_11 domain-containing protein. (343 aa)
C5YUG3_SORBIOxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. (202 aa)
C5Z141_SORBIL51_S25_CI-B8 domain-containing protein. (99 aa)
C5Z238_SORBIUncharacterized protein. (302 aa)
C5Z3H5_SORBIWRKY domain-containing protein. (350 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)
ndhB2NAD(P)H-quinone oxidoreductase subunit 2 B, 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)
ndhFNAD(P)H-quinone oxidoreductase subunit 5, 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). (738 aa)
C5WN22_SORBIUncharacterized protein; Belongs to the complex I 75 kDa subunit family. (744 aa)
C5WME2_SORBIUncharacterized protein. (173 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)
ndhANAD(P)H-quinone oxidoreductase subunit 1, 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. (362 aa)
ndhINAD(P)H-quinone oxidoreductase subunit I, 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 23 kDa subunit family. (180 aa)
psaCPhotosystem I iron-sulfur center; Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, [...] (81 aa)
ndhDNAD(P)H-quinone oxidoreductase chain 4, chloroplastic. (500 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)
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)
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)
A0A1Z5SA07CHCH domain-containing protein. (110 aa)
Nad7Complex1_49kDa domain-containing protein. (68 aa)
A0A1Z5R3464Fe-4S ferredoxin-type domain-containing protein. (49 aa)
Nad2Proton_antipo_M domain-containing protein. (225 aa)
Nad4Uncharacterized protein. (92 aa)
A0A1W0VXQ9NADH-ubiquinone oxidoreductase chain 3; Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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. (70 aa)
A0A1W0VUZ4Uncharacterized protein; Belongs to the complex I LYR family. (114 aa)
A0A1W0VU17Proton_antipo_M domain-containing protein. (185 aa)
A0A1W0VT45WRKY domain-containing protein. (385 aa)
A0A1B6QLK3NADH 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. (171 aa)
A0A1B6QHS24Fe-4S ferredoxin-type domain-containing protein. (251 aa)
A0A1B6QFX4NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial; Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. (499 aa)
A0A1B6QDG1NADH 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. (181 aa)
A0A1B6Q6E1Plus3 domain-containing protein. (873 aa)
A0A1B6PFP2zf-CHCC domain-containing protein. (110 aa)
A0A1B6PAC4WRKY domain-containing protein. (364 aa)
A0A1B6P999Uncharacterized protein. (281 aa)
A0A194YRJ8Proton_antipo_M domain-containing protein. (95 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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