STRINGSTRING
A0A1B6QHS2 A0A1B6QHS2 A0A1B6QKM3 A0A1B6QKM3 A0A1B6QR86 A0A1B6QR86 A0A1W0VRZ3 A0A1W0VRZ3 A0A1W0VU17 A0A1W0VU17 A0A1W0VUZ4 A0A1W0VUZ4 A0A1W0VXQ9 A0A1W0VXQ9 A0A1W0W0U6 A0A1W0W0U6 A0A1B6P999 A0A1B6P999 C5YD00_SORBI C5YD00_SORBI C5Y0A7_SORBI C5Y0A7_SORBI C5XNZ0_SORBI C5XNZ0_SORBI C5XLQ3_SORBI C5XLQ3_SORBI C5XLB7_SORBI C5XLB7_SORBI C5XIL2_SORBI C5XIL2_SORBI C5XIG7_SORBI C5XIG7_SORBI C5XIG6_SORBI C5XIG6_SORBI C5XIC9_SORBI C5XIC9_SORBI C5XD18_SORBI C5XD18_SORBI C5XC83_SORBI C5XC83_SORBI C5XBL6_SORBI C5XBL6_SORBI C5X760_SORBI C5X760_SORBI C5WZX4_SORBI C5WZX4_SORBI C5WQR1_SORBI C5WQR1_SORBI C5WN22_SORBI C5WN22_SORBI ndhH ndhH ndhA ndhA ndhI ndhI ndhG ndhG ndhE ndhE ndhD ndhD ndhC ndhC ndhK ndhK ndhJ ndhJ A0A1Z5SBI4 A0A1Z5SBI4 Nad7 Nad7 A0A1Z5RP74 A0A1Z5RP74 A0A1Z5RN43 A0A1Z5RN43 A0A1Z5R1U0 A0A1Z5R1U0 Nad2 Nad2 A0A1B6P9F4 A0A1B6P9F4 A0A1B6PF58 A0A1B6PF58 A0A1B6PFE9 A0A1B6PFE9 A0A1B6PFP2 A0A1B6PFP2 A0A1B6PHU5 A0A1B6PHU5 A0A1B6PR27 A0A1B6PR27 A0A1B6Q6E1 A0A1B6Q6E1 A0A1B6Q6I7 A0A1B6Q6I7 A0A1B6Q885 A0A1B6Q885 A0A1B6Q9S9 A0A1B6Q9S9 A0A1B6QB11 A0A1B6QB11 A0A1B6QFX4 A0A1B6QFX4 C5YN29_SORBI C5YN29_SORBI ndhF ndhF ndhB2 ndhB2 ndhB1 ndhB1 C5Z889_SORBI C5Z889_SORBI C5Z408_SORBI C5Z408_SORBI C5Z141_SORBI C5Z141_SORBI C5YUG3_SORBI C5YUG3_SORBI C5YN91_SORBI C5YN91_SORBI Nad6 Nad6 A0A194YI93 A0A194YI93 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:
A0A1B6QHS24Fe-4S ferredoxin-type domain-containing protein. (251 aa)
A0A1B6QKM3Flavodoxin-like domain-containing protein. (255 aa)
A0A1B6QR86PKS_ER domain-containing protein. (384 aa)
A0A1W0VRZ3Uncharacterized protein. (854 aa)
A0A1W0VU17Proton_antipo_M domain-containing protein. (185 aa)
A0A1W0VUZ4Uncharacterized protein; Belongs to the complex I LYR family. (114 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)
A0A1W0W0U6Uncharacterized protein. (260 aa)
A0A1B6P999Uncharacterized protein. (281 aa)
C5YD00_SORBIUncharacterized protein. (218 aa)
C5Y0A7_SORBIPyr_redox_2 domain-containing protein. (476 aa)
C5XNZ0_SORBIPyr_redox_2 domain-containing protein. (503 aa)
C5XLQ3_SORBIEF-hand domain-containing protein. (578 aa)
C5XLB7_SORBIUncharacterized protein. (132 aa)
C5XIL2_SORBIUncharacterized protein. (157 aa)
C5XIG7_SORBIFMN_red domain-containing protein. (213 aa)
C5XIG6_SORBIFMN_red domain-containing protein. (206 aa)
C5XIC9_SORBIOxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. (200 aa)
C5XD18_SORBIUncharacterized protein. (157 aa)
C5XC83_SORBIUncharacterized protein. (201 aa)
C5XBL6_SORBIPyr_redox_2 domain-containing protein. (566 aa)
C5X760_SORBIFlavodoxin-like domain-containing protein. (216 aa)
C5WZX4_SORBIUncharacterized protein. (108 aa)
C5WQR1_SORBIUncharacterized protein. (104 aa)
C5WN22_SORBIUncharacterized protein; Belongs to the complex I 75 kDa subunit family. (744 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)
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)
ndhENAD(P)H-quinone oxidoreductase subunit 4L, 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. (101 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)
A0A1Z5SBI4VKc domain-containing protein. (374 aa)
Nad7Complex1_49kDa domain-containing protein. (68 aa)
A0A1Z5RP74Pyr_redox_2 domain-containing protein. (491 aa)
A0A1Z5RN43Flavodoxin-like domain-containing protein. (218 aa)
A0A1Z5R1U0Uncharacterized protein; Belongs to the complex I subunit 6 family. (304 aa)
Nad2Proton_antipo_M domain-containing protein. (225 aa)
A0A1B6P9F4Flavodoxin-like domain-containing protein. (204 aa)
A0A1B6PF58Uncharacterized protein. (431 aa)
A0A1B6PFE9Pyr_redox_2 domain-containing protein. (504 aa)
A0A1B6PFP2zf-CHCC domain-containing protein. (110 aa)
A0A1B6PHU5Uncharacterized protein. (67 aa)
A0A1B6PR27Uncharacterized protein. (130 aa)
A0A1B6Q6E1Plus3 domain-containing protein. (873 aa)
A0A1B6Q6I7Flavodoxin-like domain-containing protein. (203 aa)
A0A1B6Q885FMN_red domain-containing protein. (198 aa)
A0A1B6Q9S9Flavodoxin-like domain-containing protein. (276 aa)
A0A1B6QB11Pyr_redox_2 domain-containing protein. (435 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)
C5YN29_SORBIEF-hand domain-containing protein. (581 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)
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)
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)
C5Z889_SORBIUncharacterized protein. (584 aa)
C5Z408_SORBIUncharacterized protein. (411 aa)
C5Z141_SORBIL51_S25_CI-B8 domain-containing protein. (99 aa)
C5YUG3_SORBIOxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. (202 aa)
C5YN91_SORBIPyr_redox_2 domain-containing protein. (433 aa)
Nad6Uncharacterized protein; Belongs to the complex I subunit 6 family. (224 aa)
A0A194YI93Uncharacterized protein; Belongs to the complex I subunit 6 family. (139 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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