| + |
MT-CYB | form complex 
binding
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.884 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262193 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Complex III (EC 1.10.2.2) or quinol-cytochrome c reductase performs electron transfer coupled to proton pumping using the ‘Q-cycle’ mechanism [79,80]. Structurally, it is a tightly bound symmetrical dimer (cIII2), being each ‘monomer’ composed of three catalytic core (MT-CYB, CYC1 and UQCRFS1) and seven supernumerary subunits |
|
| Publications: |
1 |
| + |
UQCRQ | form complex
binding
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.926 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262197 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Complex III (EC 1.10.2.2) or quinol-cytochrome c reductase performs electron transfer coupled to proton pumping using the ‘Q-cycle’ mechanism [79,80]. Structurally, it is a tightly bound symmetrical dimer (cIII2), being each ‘monomer’ composed of three catalytic core (MT-CYB, CYC1 and UQCRFS1) and seven supernumerary subunits |
|
| Publications: |
1 |
| + |
LETM1 | up-regulates 
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262546 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18628306 |
LETM1 knockdown obviously reduced the formation of the supercomplexes (Fig. 5C, arrowhead). Complexes I and IV failed to form, and the assembly of complex III was significantly decreased. By contrast, the assembly of complex II (succinate dehydrogenase) and complex V (ATP synthase) – which are not proton pumps – was unaffected. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UQCRB | form complex
binding
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.927 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262194 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Complex III (EC 1.10.2.2) or quinol-cytochrome c reductase performs electron transfer coupled to proton pumping using the ‘Q-cycle’ mechanism [79,80]. Structurally, it is a tightly bound symmetrical dimer (cIII2), being each ‘monomer’ composed of three catalytic core (MT-CYB, CYC1 and UQCRFS1) and seven supernumerary subunits |
|
| Publications: |
1 |
| + |
UQCRFS1 | form complex
binding
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.936 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262190 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Complex III (EC 1.10.2.2) or quinol-cytochrome c reductase performs electron transfer coupled to proton pumping using the ‘Q-cycle’ mechanism [79,80]. Structurally, it is a tightly bound symmetrical dimer (cIII2), being each ‘monomer’ composed of three catalytic core (MT-CYB, CYC1 and UQCRFS1) and seven supernumerary subunits |
|
| Publications: |
1 |
| + |
iron-sulfur cluster | up-regulates activity 
chemical activation
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262137 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Respiratory chain complexes I–III depend on Fe-S clusters for function |
|
| Publications: |
1 |
| + |
UQCR10 | form complex
binding
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.928 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262199 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Complex III (EC 1.10.2.2) or quinol-cytochrome c reductase performs electron transfer coupled to proton pumping using the ‘Q-cycle’ mechanism [79,80]. Structurally, it is a tightly bound symmetrical dimer (cIII2), being each ‘monomer’ composed of three catalytic core (MT-CYB, CYC1 and UQCRFS1) and seven supernumerary subunits |
|
| Publications: |
1 |
| + |
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III | down-regulates quantity 
chemical modification
|
ubiquinol-10 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280288 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14977419 |
The bc1 complexes are intrinsic membrane proteins that catalyze the oxidation of ubihydroquinone and the reduction of cytochrome c in mitochondrial respiratory chains and bacterial photosynthetic and respiratory chains. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III | up-regulates quantity
relocalization
|
hydron |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280289 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14977419 |
The bc1 complexes are intrinsic membrane proteins that catalyze the oxidation of ubihydroquinone and the reduction of cytochrome c in mitochondrial respiratory chains and bacterial photosynthetic and respiratory chains. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III | up-regulates activity
chemical modification
|
CYCS |
0.849 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280290 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14977419 |
The bc1 complexes are intrinsic membrane proteins that catalyze the oxidation of ubihydroquinone and the reduction of cytochrome c in mitochondrial respiratory chains and bacterial photosynthetic and respiratory chains. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III | up-regulates quantity
chemical modification
|
coenzyme Q10 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280291 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14977419 |
The bc1 complexes are intrinsic membrane proteins that catalyze the oxidation of ubihydroquinone and the reduction of cytochrome c in mitochondrial respiratory chains and bacterial photosynthetic and respiratory chains. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Inner_mitochondrial_membrane | up-regulates
relocalization
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280302 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25627476 |
One of the main functions of the IMM is the housing of proteins that make up the electron transport chain (ETC) which ultimately produces ATP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CYC1 | form complex
binding
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.93 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262192 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Complex III (EC 1.10.2.2) or quinol-cytochrome c reductase performs electron transfer coupled to proton pumping using the ‘Q-cycle’ mechanism [79,80]. Structurally, it is a tightly bound symmetrical dimer (cIII2), being each ‘monomer’ composed of three catalytic core (MT-CYB, CYC1 and UQCRFS1) and seven supernumerary subunits |
|
| Publications: |
1 |
| + |
UQCRC1 | form complex
binding
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.893 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262198 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Complex III (EC 1.10.2.2) or quinol-cytochrome c reductase performs electron transfer coupled to proton pumping using the ‘Q-cycle’ mechanism [79,80]. Structurally, it is a tightly bound symmetrical dimer (cIII2), being each ‘monomer’ composed of three catalytic core (MT-CYB, CYC1 and UQCRFS1) and seven supernumerary subunits |
|
| Publications: |
1 |
| + |
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III | up-regulates
|
Respiratory electron transport chain |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262139 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
The oxidative phosphorylation system (OXPHOS) of the mitochondrial inner membrane is composed of five enzymes (complexes I–V; cI–V). In mammals, they are all multimeric and, except for cII, have subunits encoded both in the mitochondrial genome (mtDNA) and the nuclear genome (nDNA). |
|
| Publications: |
1 |
| + |
UQCRH | form complex
binding
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.91 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262195 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Complex III (EC 1.10.2.2) or quinol-cytochrome c reductase performs electron transfer coupled to proton pumping using the ‘Q-cycle’ mechanism [79,80]. Structurally, it is a tightly bound symmetrical dimer (cIII2), being each ‘monomer’ composed of three catalytic core (MT-CYB, CYC1 and UQCRFS1) and seven supernumerary subunits |
|
| Publications: |
1 |
| + |
UQCR11 | form complex
binding
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.844 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262196 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Complex III (EC 1.10.2.2) or quinol-cytochrome c reductase performs electron transfer coupled to proton pumping using the ‘Q-cycle’ mechanism [79,80]. Structurally, it is a tightly bound symmetrical dimer (cIII2), being each ‘monomer’ composed of three catalytic core (MT-CYB, CYC1 and UQCRFS1) and seven supernumerary subunits |
|
| Publications: |
1 |
| + |
UQCRC2 | form complex
binding
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.901 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262191 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Complex III (EC 1.10.2.2) or quinol-cytochrome c reductase performs electron transfer coupled to proton pumping using the ‘Q-cycle’ mechanism [79,80]. Structurally, it is a tightly bound symmetrical dimer (cIII2), being each ‘monomer’ composed of three catalytic core (MT-CYB, CYC1 and UQCRFS1) and seven supernumerary subunits |
|
| Publications: |
1 |
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III
CPX-560
4.0