| + |
iron-sulfur cluster | up-regulates activity 
chemical activation
|
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 |
| + |
Inner_mitochondrial_membrane | up-regulates
relocalization
|
Mitochondrial respiratory chain complex III |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267007 |
|
|
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 |
| + |
UQCR10 | form complex 
binding
|
Mitochondrial respiratory chain complex III |
0.927 |
| 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 |
| + |
UQCRH | form complex
binding
|
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 |
| + |
UQCRQ | form complex
binding
|
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 
|
Mitochondrial respiratory chain complex III |
0.288 |
| 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 |
| + |
CYC1 | form complex
binding
|
Mitochondrial respiratory chain complex III |
0.929 |
| 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 |
| + |
UQCRC2 | form complex
binding
|
Mitochondrial respiratory chain complex III |
0.9 |
| 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 |
| + |
UQCRC1 | form complex
binding
|
Mitochondrial respiratory chain complex III |
0.892 |
| 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 |
| + |
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 |
| + |
UQCRB | form complex
binding
|
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 |
| + |
UQCR11 | form complex
binding
|
Mitochondrial respiratory chain complex III |
0.842 |
| 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 |
| + |
UQCRFS1 | form complex
binding
|
Mitochondrial respiratory chain complex III |
0.935 |
| 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 |
| + |
MT-CYB | form complex
binding
|
Mitochondrial respiratory chain complex III |
0.883 |
| 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 |
Mitochondrial respiratory chain complex III
CPX-560
3.0