| + |
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I | up-regulates 
|
Respiratory electron transport chain |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262141 |
|
|
|
|
| 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 |
| + |
NDUFA9 | form complex 
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.822 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262160 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5) |
|
| Publications: |
1 |
| + |
NDUFC2 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.802 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262174 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND2-module is formed by an initial intermediate that contains MT-ND2, NDUFC1 and NDUFC2 bound to NDUFAF1/CIA30 [49,50], ECSIT [51] and ACAD9 [52,53]. Then, MT-ND3 is added together with TMEM126B [54], forming a larger intermediate to which subunits MT-ND6 and MT-ND4L bind. The latest assembly stages involve the incorporation of subunits NDUFA1, NDUFA10 and NDUFS5 [24,34]. |
|
| Publications: |
1 |
| + |
NDUFA11 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.801 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262142 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5) |
|
| Publications: |
1 |
| + |
NDUFB7 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.814 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262170 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND5-module corresponds to the distal part of the membrane arm and it is composed of MT-ND5, NDUFB2, NDUFB3, NDUFB7, NDUFB8, NDUFB9 and NDUFAB1 |
|
| Publications: |
1 |
| + |
NDUFA8 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.815 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262159 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND1-module builds around the Q-module with the help of TIMMDC1/C3ORF1 [47,48], which remains bound to the Q/ND1 subassembly until the last maturation steps. MT-ND1 joins first and then NDUFA3, NDUFA8 and NDUFA13 are added |
|
| Publications: |
1 |
| + |
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I | up-regulates quantity 
chemical modification
|
NAD(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280284 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12231006 |
The energy-transducing NADH: quinone (Q) oxidoreductase (complex I) is the largest and most complicated enzyme complex in the oxidative phosphorylation system. Complex I is a redox pump that uses the redox energy to translocate H(+) (or Na(+)) ions across the membrane, resulting in a significant contribution to energy production. Complex I is located at an entry point of the electron transport chain and initiates electron transfer by oxidizing NADH and the electrons are transferred to a lipid-soluble electron carrier quinone (coenzyme Q) as an electron acceptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NDUFA3 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.784 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262155 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND1-module builds around the Q-module with the help of TIMMDC1/C3ORF1 [47,48], which remains bound to the Q/ND1 subassembly until the last maturation steps. MT-ND1 joins first and then NDUFA3, NDUFA8 and NDUFA13 are added |
|
| Publications: |
1 |
| + |
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I | down-regulates quantity 
chemical modification
|
NADH(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280279 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12231006 |
The energy-transducing NADH: quinone (Q) oxidoreductase (complex I) is the largest and most complicated enzyme complex in the oxidative phosphorylation system. Complex I is a redox pump that uses the redox energy to translocate H(+) (or Na(+)) ions across the membrane, resulting in a significant contribution to energy production. Complex I is located at an entry point of the electron transport chain and initiates electron transfer by oxidizing NADH and the electrons are transferred to a lipid-soluble electron carrier quinone (coenzyme Q) as an electron acceptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I | up-regulates quantity
relocalization
|
hydron |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280280 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12231006 |
The energy-transducing NADH: quinone (Q) oxidoreductase (complex I) is the largest and most complicated enzyme complex in the oxidative phosphorylation system. Complex I is a redox pump that uses the redox energy to translocate H(+) (or Na(+)) ions across the membrane, resulting in a significant contribution to energy production. Complex I is located at an entry point of the electron transport chain and initiates electron transfer by oxidizing NADH and the electrons are transferred to a lipid-soluble electron carrier quinone (coenzyme Q) as an electron acceptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I | down-regulates quantity
chemical modification
|
coenzyme Q10 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280281 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12231006 |
The energy-transducing NADH: quinone (Q) oxidoreductase (complex I) is the largest and most complicated enzyme complex in the oxidative phosphorylation system. Complex I is a redox pump that uses the redox energy to translocate H(+) (or Na(+)) ions across the membrane, resulting in a significant contribution to energy production. Complex I is located at an entry point of the electron transport chain and initiates electron transfer by oxidizing NADH and the electrons are transferred to a lipid-soluble electron carrier quinone (coenzyme Q) as an electron acceptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I | up-regulates quantity
chemical modification
|
ubiquinol-10 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280285 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12231006 |
The energy-transducing NADH: quinone (Q) oxidoreductase (complex I) is the largest and most complicated enzyme complex in the oxidative phosphorylation system. Complex I is a redox pump that uses the redox energy to translocate H(+) (or Na(+)) ions across the membrane, resulting in a significant contribution to energy production. Complex I is located at an entry point of the electron transport chain and initiates electron transfer by oxidizing NADH and the electrons are transferred to a lipid-soluble electron carrier quinone (coenzyme Q) as an electron acceptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MT-ND4 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.778 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262146 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and |The main ND4-module intermediate binds NDUFB1, NDUFB4, NDUFB5, NDUFB6, NDUFB10, NDUFB11 and MT-ND4 |
|
| Publications: |
1 |
| + |
NDUFS6 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.836 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262180 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)The N-module, which is the tip of the hydrophilic arm and the last one to be incorporated [30,35], results from the assembly of NDUFV1, NDUFV2, NDUFS1 and NDUFA2 [34], to which NDUFA6, NDUFA7, NDUFA12, NDUFS4, NDUFS6 and NDUFV3 must be further associated with to complete the module [24]. |
|
| Publications: |
1 |
| + |
MT-ND3 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.769 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262145 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND2-module is formed by an initial intermediate that contains MT-ND2, NDUFC1 and NDUFC2 bound to NDUFAF1/CIA30 [49,50], ECSIT [51] and ACAD9 [52,53]. Then, MT-ND3 is added together with TMEM126B [54], forming a larger intermediate to which subunits MT-ND6 and MT-ND4L bind. The latest assembly stages involve the incorporation of subunits NDUFA1, NDUFA10 and NDUFS5 [24,34]. |
|
| Publications: |
1 |
| + |
NDUFA12 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.822 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262152 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)The N-module, which is the tip of the hydrophilic arm and the last one to be incorporated [30,35], results from the assembly of NDUFV1, NDUFV2, NDUFS1 and NDUFA2 [34], to which NDUFA6, NDUFA7, NDUFA12, NDUFS4, NDUFS6 and NDUFV3 must be further associated with to complete the module [24]. |
|
| Publications: |
1 |
| + |
NDUFB6 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262169 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and |The main ND4-module intermediate binds NDUFB1, NDUFB4, NDUFB5, NDUFB6, NDUFB10, NDUFB11 and MT-ND4 |
|
| Publications: |
1 |
| + |
NDUFS7 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.856 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262181 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The Q-module is built through the association of NDUFA5, NDUFS2 and NDUFS3 plus NDUFS7 and NDUFS8. The chaperones NDUFAF3/C3ORF60 and NDUFAF4/C6ORF66 [36,37] remain bound to this module until the final assembly steps [34]. NDUFAF6/C8ORF38 [38] also seems to participate in the assembly of the Q-module [24,39]. NDUFAF3, 4 and 6, are necessary to maintain normal MT-ND1 synthesis [40,41]. NDUFAF5 adds a hydroxyl group to Arg73 of NDUFS7 [42] and NDUFAF7 dimethylates NDUFS2 in Arg85 [43], an essential modification for cI assembly [44]. NUBPL/IND1 delivers [4Fe–4S] clusters specifically to the N- and Q-module subunits [45,46]. |
|
| Publications: |
1 |
| + |
NDUFA1 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.844 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262150 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND2-module is formed by an initial intermediate that contains MT-ND2, NDUFC1 and NDUFC2 bound to NDUFAF1/CIA30 [49,50], ECSIT [51] and ACAD9 [52,53]. Then, MT-ND3 is added together with TMEM126B [54], forming a larger intermediate to which subunits MT-ND6 and MT-ND4L bind. The latest assembly stages involve the incorporation of subunits NDUFA1, NDUFA10 and NDUFS5 [24,34]. |
|
| Publications: |
1 |
| + |
NDUFC1 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.781 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262173 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND2-module is formed by an initial intermediate that contains MT-ND2, NDUFC1 and NDUFC2 bound to NDUFAF1/CIA30 [49,50], ECSIT [51] and ACAD9 [52,53]. Then, MT-ND3 is added together with TMEM126B [54], forming a larger intermediate to which subunits MT-ND6 and MT-ND4L bind. The latest assembly stages involve the incorporation of subunits NDUFA1, NDUFA10 and NDUFS5 [24,34]. |
|
| Publications: |
1 |
| + |
NDUFB8 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.814 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262171 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND5-module corresponds to the distal part of the membrane arm and it is composed of MT-ND5, NDUFB2, NDUFB3, NDUFB7, NDUFB8, NDUFB9 and NDUFAB1 |
|
| Publications: |
1 |
| + |
MITRAC complex | up-regulates quantity
relocalization
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272486 |
|
|
|
|
| pmid |
sentence |
| 23260140 |
Each association relies on the supply of subunits from either the cytosol or the mitochondrial matrix, suggesting that human TIM21 ushers nuclear-encoded proteins to assembly intermediates. In agreement with this, assembly of the early cytochrome c oxidase subunit COX4-1 requires TIM21, whereas it is dispensable for late-assembling subunits. The finding that TIM21 also interacts with complex I intermediates points to a more general role of TIM21 in respiratory-chain assembly. Furthermore, TIM21 appears to be tightly connected to MITRAC15, which, in contrast to TIM23 and MITRAC12, coimmunoprecipitates with TIM21 under all tested conditions. MITRAC15 associates with MITRAC and is required for complex IV but also complex I assembly. |
|
| Publications: |
1 |
| + |
NDUFS2 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.86 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262176 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The Q-module is built through the association of NDUFA5, NDUFS2 and NDUFS3 plus NDUFS7 and NDUFS8. The chaperones NDUFAF3/C3ORF60 and NDUFAF4/C6ORF66 [36,37] remain bound to this module until the final assembly steps [34]. NDUFAF6/C8ORF38 [38] also seems to participate in the assembly of the Q-module [24,39]. NDUFAF3, 4 and 6, are necessary to maintain normal MT-ND1 synthesis [40,41]. NDUFAF5 adds a hydroxyl group to Arg73 of NDUFS7 [42] and NDUFAF7 dimethylates NDUFS2 in Arg85 [43], an essential modification for cI assembly [44]. NUBPL/IND1 delivers [4Fe–4S] clusters specifically to the N- and Q-module subunits [45,46]. |
|
| Publications: |
1 |
| + |
NDUFV1 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.856 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262183 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)The N-module, which is the tip of the hydrophilic arm and the last one to be incorporated [30,35], results from the assembly of NDUFV1, NDUFV2, NDUFS1 and NDUFA2 [34], to which NDUFA6, NDUFA7, NDUFA12, NDUFS4, NDUFS6 and NDUFV3 must be further associated with to complete the module [24]. |
|
| Publications: |
1 |
| + |
NDUFS8 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.846 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262182 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The Q-module is built through the association of NDUFA5, NDUFS2 and NDUFS3 plus NDUFS7 and NDUFS8. The chaperones NDUFAF3/C3ORF60 and NDUFAF4/C6ORF66 [36,37] remain bound to this module until the final assembly steps [34]. NDUFAF6/C8ORF38 [38] also seems to participate in the assembly of the Q-module [24,39]. NDUFAF3, 4 and 6, are necessary to maintain normal MT-ND1 synthesis [40,41]. NDUFAF5 adds a hydroxyl group to Arg73 of NDUFS7 [42] and NDUFAF7 dimethylates NDUFS2 in Arg85 [43], an essential modification for cI assembly [44]. NUBPL/IND1 delivers [4Fe–4S] clusters specifically to the N- and Q-module subunits [45,46]. |
|
| Publications: |
1 |
| + |
NDUFS3 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.862 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262177 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The Q-module is built through the association of NDUFA5, NDUFS2 and NDUFS3 plus NDUFS7 and NDUFS8. The chaperones NDUFAF3/C3ORF60 and NDUFAF4/C6ORF66 [36,37] remain bound to this module until the final assembly steps [34]. NDUFAF6/C8ORF38 [38] also seems to participate in the assembly of the Q-module [24,39]. NDUFAF3, 4 and 6, are necessary to maintain normal MT-ND1 synthesis [40,41]. NDUFAF5 adds a hydroxyl group to Arg73 of NDUFS7 [42] and NDUFAF7 dimethylates NDUFS2 in Arg85 [43], an essential modification for cI assembly [44]. NUBPL/IND1 delivers [4Fe–4S] clusters specifically to the N- and Q-module subunits [45,46]. |
|
| Publications: |
1 |
| + |
iron-sulfur cluster | up-regulates activity
chemical activation
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262135 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Respiratory chain complexes I–III depend on Fe-S clusters for function |
|
| Publications: |
1 |
| + |
NDUFB9 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.802 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262172 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND5-module corresponds to the distal part of the membrane arm and it is composed of MT-ND5, NDUFB2, NDUFB3, NDUFB7, NDUFB8, NDUFB9 and NDUFAB1 |
|
| Publications: |
1 |
| + |
NDUFA5 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.823 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262156 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The Q-module is built through the association of NDUFA5, NDUFS2 and NDUFS3 plus NDUFS7 and NDUFS8. The chaperones NDUFAF3/C3ORF60 and NDUFAF4/C6ORF66 [36,37] remain bound to this module until the final assembly steps [34]. NDUFAF6/C8ORF38 [38] also seems to participate in the assembly of the Q-module [24,39]. NDUFAF3, 4 and 6, are necessary to maintain normal MT-ND1 synthesis [40,41]. NDUFAF5 adds a hydroxyl group to Arg73 of NDUFS7 [42] and NDUFAF7 dimethylates NDUFS2 in Arg85 [43], an essential modification for cI assembly [44]. NUBPL/IND1 delivers [4Fe–4S] clusters specifically to the N- and Q-module subunits [45,46]. |
|
| Publications: |
1 |
| + |
NDUFB1 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.766 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262162 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and |The main ND4-module intermediate binds NDUFB1, NDUFB4, NDUFB5, NDUFB6, NDUFB10, NDUFB11 and MT-ND4 |
|
| Publications: |
1 |
| + |
NDUFB3 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.799 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262166 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND5-module corresponds to the distal part of the membrane arm and it is composed of MT-ND5, NDUFB2, NDUFB3, NDUFB7, NDUFB8, NDUFB9 and NDUFAB1 |
|
| Publications: |
1 |
| + |
NDUFB4 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.787 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262167 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and |The main ND4-module intermediate binds NDUFB1, NDUFB4, NDUFB5, NDUFB6, NDUFB10, NDUFB11 and MT-ND4 |
|
| Publications: |
1 |
| + |
MT-ND1 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.804 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262143 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The Q-module is built through the association of NDUFA5, NDUFS2 and NDUFS3 plus NDUFS7 and NDUFS8. The chaperones NDUFAF3/C3ORF60 and NDUFAF4/C6ORF66 [36,37] remain bound to this module until the final assembly steps [34]. NDUFAF6/C8ORF38 [38] also seems to participate in the assembly of the Q-module [24,39]. NDUFAF3, 4 and 6, are necessary to maintain normal MT-ND1 synthesis [40,41]. NDUFAF5 adds a hydroxyl group to Arg73 of NDUFS7 [42] and NDUFAF7 dimethylates NDUFS2 in Arg85 [43], an essential modification for cI assembly [44]. NUBPL/IND1 delivers [4Fe–4S] clusters specifically to the N- and Q-module subunits [45,46]. |
|
| Publications: |
1 |
| + |
MT-ND2 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.771 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262144 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND2-module is formed by an initial intermediate that contains MT-ND2, NDUFC1 and NDUFC2 bound to NDUFAF1/CIA30 [49,50], ECSIT [51] and ACAD9 [52,53]. Then, MT-ND3 is added together with TMEM126B [54], forming a larger intermediate to which subunits MT-ND6 and MT-ND4L bind. The latest assembly stages involve the incorporation of subunits NDUFA1, NDUFA10 and NDUFS5 [24,34]. |
|
| Publications: |
1 |
| + |
NDUFB5 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.821 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262168 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and |The main ND4-module intermediate binds NDUFB1, NDUFB4, NDUFB5, NDUFB6, NDUFB10, NDUFB11 and MT-ND4 |
|
| Publications: |
1 |
| + |
NDUFB11 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.738 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262164 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and |The main ND4-module intermediate binds NDUFB1, NDUFB4, NDUFB5, NDUFB6, NDUFB10, NDUFB11 and MT-ND4 |
|
| Publications: |
1 |
| + |
NDUFV2 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.852 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262184 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)The N-module, which is the tip of the hydrophilic arm and the last one to be incorporated [30,35], results from the assembly of NDUFV1, NDUFV2, NDUFS1 and NDUFA2 [34], to which NDUFA6, NDUFA7, NDUFA12, NDUFS4, NDUFS6 and NDUFV3 must be further associated with to complete the module [24]. |
|
| Publications: |
1 |
| + |
MT-ND6 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.756 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262149 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND2-module is formed by an initial intermediate that contains MT-ND2, NDUFC1 and NDUFC2 bound to NDUFAF1/CIA30 [49,50], ECSIT [51] and ACAD9 [52,53]. Then, MT-ND3 is added together with TMEM126B [54], forming a larger intermediate to which subunits MT-ND6 and MT-ND4L bind. The latest assembly stages involve the incorporation of subunits NDUFA1, NDUFA10 and NDUFS5 [24,34]. |
|
| Publications: |
1 |
| + |
NDUFA6 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.826 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262157 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)The N-module, which is the tip of the hydrophilic arm and the last one to be incorporated [30,35], results from the assembly of NDUFV1, NDUFV2, NDUFS1 and NDUFA2 [34], to which NDUFA6, NDUFA7, NDUFA12, NDUFS4, NDUFS6 and NDUFV3 must be further associated with to complete the module [24]. |
|
| Publications: |
1 |
| + |
NDUFS5 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.813 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262179 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND2-module is formed by an initial intermediate that contains MT-ND2, NDUFC1 and NDUFC2 bound to NDUFAF1/CIA30 [49,50], ECSIT [51] and ACAD9 [52,53]. Then, MT-ND3 is added together with TMEM126B [54], forming a larger intermediate to which subunits MT-ND6 and MT-ND4L bind. The latest assembly stages involve the incorporation of subunits NDUFA1, NDUFA10 and NDUFS5 [24,34]. |
|
| Publications: |
1 |
| + |
LETM1 | up-regulates
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262547 |
|
|
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 |
| + |
NDUFS4 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.839 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262178 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)The N-module, which is the tip of the hydrophilic arm and the last one to be incorporated [30,35], results from the assembly of NDUFV1, NDUFV2, NDUFS1 and NDUFA2 [34], to which NDUFA6, NDUFA7, NDUFA12, NDUFS4, NDUFS6 and NDUFV3 must be further associated with to complete the module [24]. |
|
| Publications: |
1 |
| + |
NDUFAB1 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.814 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262161 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND5-module corresponds to the distal part of the membrane arm and it is composed of MT-ND5, NDUFB2, NDUFB3, NDUFB7, NDUFB8, NDUFB9 and NDUFAB1 |
|
| Publications: |
1 |
| + |
NDUFA10 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.818 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262151 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND2-module is formed by an initial intermediate that contains MT-ND2, NDUFC1 and NDUFC2 bound to NDUFAF1/CIA30 [49,50], ECSIT [51] and ACAD9 [52,53]. Then, MT-ND3 is added together with TMEM126B [54], forming a larger intermediate to which subunits MT-ND6 and MT-ND4L bind. The latest assembly stages involve the incorporation of subunits NDUFA1, NDUFA10 and NDUFS5 [24,34]. |
|
| Publications: |
1 |
| + |
Inner_mitochondrial_membrane | up-regulates
relocalization
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
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 |
| + |
NDUFA13 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.783 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262153 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND1-module builds around the Q-module with the help of TIMMDC1/C3ORF1 [47,48], which remains bound to the Q/ND1 subassembly until the last maturation steps. MT-ND1 joins first and then NDUFA3, NDUFA8 and NDUFA13 are added |
|
| Publications: |
1 |
| + |
NDUFA2 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.854 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262154 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)The N-module, which is the tip of the hydrophilic arm and the last one to be incorporated [30,35], results from the assembly of NDUFV1, NDUFV2, NDUFS1 and NDUFA2 [34], to which NDUFA6, NDUFA7, NDUFA12, NDUFS4, NDUFS6 and NDUFV3 must be further associated with to complete the module [24]. |
|
| Publications: |
1 |
| + |
NDUFA7 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.816 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262158 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)The N-module, which is the tip of the hydrophilic arm and the last one to be incorporated [30,35], results from the assembly of NDUFV1, NDUFV2, NDUFS1 and NDUFA2 [34], to which NDUFA6, NDUFA7, NDUFA12, NDUFS4, NDUFS6 and NDUFV3 must be further associated with to complete the module [24]. |
|
| Publications: |
1 |
| + |
NDUFB2 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.774 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262165 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND5-module corresponds to the distal part of the membrane arm and it is composed of MT-ND5, NDUFB2, NDUFB3, NDUFB7, NDUFB8, NDUFB9 and NDUFAB1 |
|
| Publications: |
1 |
| + |
MT-ND5 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.759 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262148 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND5-module corresponds to the distal part of the membrane arm and it is composed of MT-ND5, NDUFB2, NDUFB3, NDUFB7, NDUFB8, NDUFB9 and NDUFAB1 |
|
| Publications: |
1 |
| + |
NDUFS1 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.851 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262175 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)The N-module, which is the tip of the hydrophilic arm and the last one to be incorporated [30,35], results from the assembly of NDUFV1, NDUFV2, NDUFS1 and NDUFA2 [34], to which NDUFA6, NDUFA7, NDUFA12, NDUFS4, NDUFS6 and NDUFV3 must be further associated with to complete the module [24]. |
|
| Publications: |
1 |
| + |
MT-ND4L | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.685 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262147 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)|The ND2-module is formed by an initial intermediate that contains MT-ND2, NDUFC1 and NDUFC2 bound to NDUFAF1/CIA30 [49,50], ECSIT [51] and ACAD9 [52,53]. Then, MT-ND3 is added together with TMEM126B [54], forming a larger intermediate to which subunits MT-ND6 and MT-ND4L bind. The latest assembly stages involve the incorporation of subunits NDUFA1, NDUFA10 and NDUFS5 [24,34]. |
|
| Publications: |
1 |
| + |
NDUFB10 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.815 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262163 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and |The main ND4-module intermediate binds NDUFB1, NDUFB4, NDUFB5, NDUFB6, NDUFB10, NDUFB11 and MT-ND4 |
|
| Publications: |
1 |
| + |
NDUFV3 | form complex
binding
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.774 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262185 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Thus, we now know the complete mammalian cI structure [22,23] and how the subunits are organized in six modules (N, Q, ND1, ND2, ND4 and ND5)The N-module, which is the tip of the hydrophilic arm and the last one to be incorporated [30,35], results from the assembly of NDUFV1, NDUFV2, NDUFS1 and NDUFA2 [34], to which NDUFA6, NDUFA7, NDUFA12, NDUFS4, NDUFS6 and NDUFV3 must be further associated with to complete the module [24]. |
|
| Publications: |
1 |
4.0
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I
CPX-577