MT-ND1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0003954 NADH dehydrogenase activity	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation, with contributes_to, to the parent term NADH dehydrogenase activity. Reason: Correct. The contributes_to qualifier is right for a membrane-arm core subunit, and the inherited parent term is consistent with the more specific complex-level activity, NADH dehydrogenase (ubiquinone) activity, that ND1 contributes to (recorded in core_functions). Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Essential for the catalytic activity and assembly of complex I PMID:1959619 The ND1/3460 mutation exhibits 80% reduction in rotenone-sensitive and ubiquinone-dependent electron transfer activity
GO:0005515 protein binding	IPI PMID:12762840 Novel complex integrating mitochondria and the microtubular ...	REMOVE	Summary: IPI protein binding annotation (PMID:12762840). Reason: Protein binding carries no functional information, and no more informative MF follows from this report: the partner (MAP1S/C19ORF5) is not a Complex I subunit or assembly factor, and the interaction says nothing about ND1's role in the membrane arm. Removal does not mean the reported interaction is false. Supporting Evidence: PMID:12762840 C19ORF5 complexed with mitochondria-associated NADH dehydrogenase I and cytochrome c oxidase I
GO:0005515 protein binding	IPI PMID:18486613 Interactions between PBEF and oxidative stress proteins--a p...	REMOVE	Summary: IPI protein binding annotation (PMID:18486613). Reason: Protein binding carries no functional information, and no more informative MF follows from this report: the partner (NAMPT/PBEF) is not a Complex I subunit or assembly factor, and the interaction says nothing about ND1's role in the membrane arm. Removal does not mean the reported interaction is false. Supporting Evidence: PMID:18486613 The interactions between PBEF and NADH dehydrogenase subunit 1(ND1), ferritin light chain and interferon induced transmembrane 3 (IFITM3) in human pulmonary vascular endothelial cells were identified and validated.
GO:0005515 protein binding	IPI PMID:19822128 DJ-1 binds to mitochondrial complex I and maintains its acti...	REMOVE	Summary: IPI protein binding annotation (PMID:19822128). Reason: Protein binding carries no functional information, and no more informative MF follows from this report: the partner (PARK7/DJ-1) is not a Complex I subunit or assembly factor, and the interaction says nothing about ND1's role in the membrane arm. Removal does not mean the reported interaction is false. Supporting Evidence: PMID:19822128 DJ-1 directly bound to NDUFA4 and ND1, nuclear and mitochondrial DNA-encoding subunits of mitochondrial complex I
GO:0005739 mitochondrion	HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an...	ACCEPT	Summary: HTP annotation to mitochondrion. Reason: Correct; ND1 is encoded and translated inside mitochondria and resides in the inner membrane. The term is less specific than mitochondrial inner membrane, which is also annotated, but it is not wrong. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane PMID:34800366 defined a mitochondrial high-confidence proteome of >1,100 proteins (MitoCoP)
GO:0005743 mitochondrial inner membrane	IDA PMID:28844695 Architecture of Human Mitochondrial Respiratory Megacomplex ...	ACCEPT	Summary: IDA annotation to mitochondrial inner membrane (PMID:28844695). Reason: ND1 is a multi-pass integral membrane subunit of the Complex I membrane arm, which is embedded in the inner mitochondrial membrane. Correct and appropriately specific location. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane file:human/MT-ND1/MT-ND1-uniprot.txt Multi-pass membrane protein PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII
GO:0005743 mitochondrial inner membrane	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation to mitochondrial inner membrane (GO_REF:0000120). Reason: ND1 is a multi-pass integral membrane subunit of the Complex I membrane arm, which is embedded in the inner mitochondrial membrane. Correct and appropriately specific location. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane file:human/MT-ND1/MT-ND1-uniprot.txt Multi-pass membrane protein PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII
GO:0005743 mitochondrial inner membrane	ISS GO_REF:0000024	ACCEPT	Summary: ISS annotation to mitochondrial inner membrane (GO_REF:0000024). Reason: ND1 is a multi-pass integral membrane subunit of the Complex I membrane arm, which is embedded in the inner mitochondrial membrane. Correct and appropriately specific location. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane file:human/MT-ND1/MT-ND1-uniprot.txt Multi-pass membrane protein PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-163217	ACCEPT	Summary: TAS annotation to mitochondrial inner membrane (Reactome:R-HSA-163217). Reason: ND1 is a multi-pass integral membrane subunit of the Complex I membrane arm, which is embedded in the inner mitochondrial membrane. Correct and appropriately specific location. The Reactome reference is a mitochondrial translation or Complex I assembly/catalysis event, and the stated compartment is correct for it. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane file:human/MT-ND1/MT-ND1-uniprot.txt Multi-pass membrane protein PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII Reactome:R-HSA-163217 This electron transfer is coupled with the translocation of protons from the mitochondrial matrix to the intermembrane space.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-5419271	ACCEPT	Summary: TAS annotation to mitochondrial inner membrane (Reactome:R-HSA-5419271). Reason: ND1 is a multi-pass integral membrane subunit of the Complex I membrane arm, which is embedded in the inner mitochondrial membrane. Correct and appropriately specific location. The Reactome reference is a mitochondrial translation or Complex I assembly/catalysis event, and the stated compartment is correct for it. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane file:human/MT-ND1/MT-ND1-uniprot.txt Multi-pass membrane protein PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII Reactome:R-HSA-163217 This electron transfer is coupled with the translocation of protons from the mitochondrial matrix to the intermembrane space.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799179	ACCEPT	Summary: TAS annotation to mitochondrial inner membrane (Reactome:R-HSA-6799179). Reason: ND1 is a multi-pass integral membrane subunit of the Complex I membrane arm, which is embedded in the inner mitochondrial membrane. Correct and appropriately specific location. The Reactome reference is a mitochondrial translation or Complex I assembly/catalysis event, and the stated compartment is correct for it. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane file:human/MT-ND1/MT-ND1-uniprot.txt Multi-pass membrane protein PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII Reactome:R-HSA-163217 This electron transfer is coupled with the translocation of protons from the mitochondrial matrix to the intermembrane space.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799191	ACCEPT	Summary: TAS annotation to mitochondrial inner membrane (Reactome:R-HSA-6799191). Reason: ND1 is a multi-pass integral membrane subunit of the Complex I membrane arm, which is embedded in the inner mitochondrial membrane. Correct and appropriately specific location. The Reactome reference is a mitochondrial translation or Complex I assembly/catalysis event, and the stated compartment is correct for it. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane file:human/MT-ND1/MT-ND1-uniprot.txt Multi-pass membrane protein PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII Reactome:R-HSA-163217 This electron transfer is coupled with the translocation of protons from the mitochondrial matrix to the intermembrane space.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799196	ACCEPT	Summary: TAS annotation to mitochondrial inner membrane (Reactome:R-HSA-6799196). Reason: ND1 is a multi-pass integral membrane subunit of the Complex I membrane arm, which is embedded in the inner mitochondrial membrane. Correct and appropriately specific location. The Reactome reference is a mitochondrial translation or Complex I assembly/catalysis event, and the stated compartment is correct for it. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane file:human/MT-ND1/MT-ND1-uniprot.txt Multi-pass membrane protein PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII Reactome:R-HSA-163217 This electron transfer is coupled with the translocation of protons from the mitochondrial matrix to the intermembrane space.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799197	ACCEPT	Summary: TAS annotation to mitochondrial inner membrane (Reactome:R-HSA-6799197). Reason: ND1 is a multi-pass integral membrane subunit of the Complex I membrane arm, which is embedded in the inner mitochondrial membrane. Correct and appropriately specific location. The Reactome reference is a mitochondrial translation or Complex I assembly/catalysis event, and the stated compartment is correct for it. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane file:human/MT-ND1/MT-ND1-uniprot.txt Multi-pass membrane protein PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII Reactome:R-HSA-163217 This electron transfer is coupled with the translocation of protons from the mitochondrial matrix to the intermembrane space.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799202	ACCEPT	Summary: TAS annotation to mitochondrial inner membrane (Reactome:R-HSA-6799202). Reason: ND1 is a multi-pass integral membrane subunit of the Complex I membrane arm, which is embedded in the inner mitochondrial membrane. Correct and appropriately specific location. The Reactome reference is a mitochondrial translation or Complex I assembly/catalysis event, and the stated compartment is correct for it. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane file:human/MT-ND1/MT-ND1-uniprot.txt Multi-pass membrane protein PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII Reactome:R-HSA-163217 This electron transfer is coupled with the translocation of protons from the mitochondrial matrix to the intermembrane space.
GO:0006120 mitochondrial electron transport, NADH to ubiquinone	IMP PMID:1959619 Electron transfer properties of NADH:ubiquinone reductase in...	ACCEPT	Summary: IMP annotation to mitochondrial electron transport, NADH to ubiquinone. Reason: This is the process carried out by Complex I, and ND1 is a core subunit required for it; loss or pathogenic variants of ND1 reduce NADH:ubiquinone oxidoreductase activity. Core process. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Core subunit of the mitochondrial membrane respiratory chain PMID:1959619 The ND1/3460 mutation exhibits 80% reduction in rotenone-sensitive and ubiquinone-dependent electron transfer activity PMID:1959619 This is in accordance with the proposal that the ND1 subunit interacts with rotenone and ubiquinone.
GO:0006120 mitochondrial electron transport, NADH to ubiquinone	NAS PMID:3921850 Six unidentified reading frames of human mitochondrial DNA e...	ACCEPT	Summary: NAS annotation to mitochondrial electron transport, NADH to ubiquinone. Reason: This is the process carried out by Complex I, and ND1 is a core subunit required for it; loss or pathogenic variants of ND1 reduce NADH:ubiquinone oxidoreductase activity. Core process. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Core subunit of the mitochondrial membrane respiratory chain PMID:3921850 We conclude that the six reading frames encode components of the respiratory-chain NADH dehydrogenase.
GO:0008137 NADH dehydrogenase (ubiquinone) activity	IEA GO_REF:0000120	MODIFY	Summary: IEA annotation with the enables qualifier to NADH dehydrogenase (ubiquinone) activity, the EC 7.1.1.2 activity of the whole complex (NADH + Q + 5H+ in = NAD+ + QH2 + 4H+ out). Reason: The activity belongs to the assembled holoenzyme: NADH oxidation, the flavin and Fe-S cofactors and the terminal electron donor N2 are all in nuclear-encoded peripheral-arm subunits. ND1 lines the ubiquinone-binding channel at the junction with the peripheral arm and contributes the first part of the E-channel, so it is required for, and contributes to, the complex activity but does not carry it alone. The term is right; the qualifier should be contributes_to. Its own subunit-level activity is captured in core_functions. Proposed replacements: NADH dehydrogenase (ubiquinone) activity Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Essential for the catalytic activity and assembly of complex I PMID:15250827 Mitochondria-encoded ND (NADH dehydrogenase) subunits, as components of the hydrophobic part of complex I, are essential for NADH:ubiquinone oxidoreductase activity.
GO:0008137 NADH dehydrogenase (ubiquinone) activity	IMP PMID:1959619 Electron transfer properties of NADH:ubiquinone reductase in...	MODIFY	Summary: IMP annotation with the enables qualifier to NADH dehydrogenase (ubiquinone) activity, the EC 7.1.1.2 activity of the whole complex (NADH + Q + 5H+ in = NAD+ + QH2 + 4H+ out). Reason: The activity belongs to the assembled holoenzyme: NADH oxidation, the flavin and Fe-S cofactors and the terminal electron donor N2 are all in nuclear-encoded peripheral-arm subunits. ND1 lines the ubiquinone-binding channel at the junction with the peripheral arm and contributes the first part of the E-channel, so it is required for, and contributes to, the complex activity but does not carry it alone. The term is right; the qualifier should be contributes_to. Its own subunit-level activity is captured in core_functions. Proposed replacements: NADH dehydrogenase (ubiquinone) activity Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Essential for the catalytic activity and assembly of complex I PMID:1959619 The ND1/3460 mutation exhibits 80% reduction in rotenone-sensitive and ubiquinone-dependent electron transfer activity PMID:1959619 This is in accordance with the proposal that the ND1 subunit interacts with rotenone and ubiquinone.
GO:0008137 NADH dehydrogenase (ubiquinone) activity	NAS PMID:3921850 Six unidentified reading frames of human mitochondrial DNA e...	MODIFY	Summary: NAS annotation with the enables qualifier to NADH dehydrogenase (ubiquinone) activity, the EC 7.1.1.2 activity of the whole complex (NADH + Q + 5H+ in = NAD+ + QH2 + 4H+ out). Reason: The activity belongs to the assembled holoenzyme: NADH oxidation, the flavin and Fe-S cofactors and the terminal electron donor N2 are all in nuclear-encoded peripheral-arm subunits. ND1 lines the ubiquinone-binding channel at the junction with the peripheral arm and contributes the first part of the E-channel, so it is required for, and contributes to, the complex activity but does not carry it alone. The term is right; the qualifier should be contributes_to. Its own subunit-level activity is captured in core_functions. Proposed replacements: NADH dehydrogenase (ubiquinone) activity Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Essential for the catalytic activity and assembly of complex I PMID:15250827 Mitochondria-encoded ND (NADH dehydrogenase) subunits, as components of the hydrophobic part of complex I, are essential for NADH:ubiquinone oxidoreductase activity. PMID:3921850 We conclude that the six reading frames encode components of the respiratory-chain NADH dehydrogenase.
GO:0009060 aerobic respiration	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: IBA annotation to aerobic respiration. Reason: Correct but very general; Complex I is the entry point of the respiratory chain. The specific process mitochondrial electron transport, NADH to ubiquinone is the core process. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Core subunit of the mitochondrial membrane respiratory chain Reactome:R-HSA-163217 This electron transfer is coupled with the translocation of protons from the mitochondrial matrix to the intermembrane space.
GO:0009060 aerobic respiration	NAS PMID:30030361 Assembly of mammalian oxidative phosphorylation complexes I-...	KEEP AS NON CORE	Summary: NAS annotation to aerobic respiration. Reason: Correct but very general; Complex I is the entry point of the respiratory chain. The specific process mitochondrial electron transport, NADH to ubiquinone is the core process. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Core subunit of the mitochondrial membrane respiratory chain PMID:30030361 it is now well established that complexes I, III and IV interact with each other, forming the so-called respiratory supercomplexes
GO:0016020 membrane	IEA GO_REF:0000002	MODIFY	Summary: IEA (InterPro) annotation to the generic term membrane. Reason: ND1 is an integral subunit of the inner mitochondrial membrane; the generic term should be replaced by mitochondrial inner membrane. Proposed replacements: mitochondrial inner membrane Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane file:human/MT-ND1/MT-ND1-uniprot.txt Multi-pass membrane protein
GO:0031966 mitochondrial membrane	IDA PMID:17209039 Identification of mitochondrial complex I assembly intermedi...	MODIFY	Summary: IDA annotation to mitochondrial membrane from an NDUFS3-GFP assembly-intermediate study. Reason: Correct but less specific than the established location; ND1 is an integral inner-membrane subunit, so mitochondrial inner membrane is the better term. Proposed replacements: mitochondrial inner membrane Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Mitochondrion inner membrane PMID:17209039 Composition analysis showed that this event was accompanied by the incorporation of at least one mitochondrial DNA-encoded subunit, thereby revealing the first entry point of these subunits.
GO:0032981 mitochondrial respiratory chain complex I assembly	IMP PMID:26929434 Loss of mitochondrial DNA-encoded protein ND1 results in dis...	KEEP AS NON CORE	Summary: IMP annotation to mitochondrial respiratory chain complex I assembly. Reason: Loss or pathogenic variants of ND1 block or destabilise Complex I assembly, and ND1 enters at a defined assembly step. This shows ND1 is a required building block of the complex rather than an assembly factor; the annotation is kept, but the core role is catalytic (contribution to proton-pumping NADH:ubiquinone oxidoreduction). Supporting Evidence: PMID:26929434 We conclude that the loss of ND1 stalls complex I assembly during the early stages of its biogenesis PMID:17209039 Composition analysis showed that this event was accompanied by the incorporation of at least one mitochondrial DNA-encoded subunit, thereby revealing the first entry point of these subunits. Reactome:R-HSA-6799191 The IP subcomplex is anchored to the inner mitochondrial membrane by NADH-ubiquinone oxidoreductase chain 1 (MT-ND1)
GO:0042776 proton motive force-driven mitochondrial ATP synthesis	NAS PMID:30030361 Assembly of mammalian oxidative phosphorylation complexes I-...	MARK AS OVER ANNOTATED	Summary: NAS annotation (ComplexPortal) to proton motive force-driven mitochondrial ATP synthesis. Reason: Complex I generates the proton motive force but does not synthesise ATP; that process is carried out by ATP synthase. The annotation reflects a whole-OXPHOS view of the complex and over-states this subunit's role. Supporting Evidence: Reactome:R-HSA-163217 This electron transfer is coupled with the translocation of protons from the mitochondrial matrix to the intermembrane space.
GO:0045271 respiratory chain complex I	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation placing MT-ND1 in respiratory chain complex I. Reason: ND1 is one of the seven mtDNA-encoded core subunits of the membrane arm of Complex I; membership is supported by immunopurification of human Complex I, the human megacomplex structure, and the original identification of the ND reading frames as Complex I components. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Core subunit of the mitochondrial membrane respiratory chain PMID:3921850 We conclude that the six reading frames encode components of the respiratory-chain NADH dehydrogenase. PMID:12611891 we can resolve and identify the human homologues of 42 polypeptides detected so far in the more extensively studied beef heart complex I PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII
GO:0045271 respiratory chain complex I	IDA PMID:12611891 The subunit composition of the human NADH dehydrogenase obta...	ACCEPT	Summary: IDA annotation placing MT-ND1 in respiratory chain complex I. Reason: ND1 is one of the seven mtDNA-encoded core subunits of the membrane arm of Complex I; membership is supported by immunopurification of human Complex I, the human megacomplex structure, and the original identification of the ND reading frames as Complex I components. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Core subunit of the mitochondrial membrane respiratory chain PMID:3921850 We conclude that the six reading frames encode components of the respiratory-chain NADH dehydrogenase. PMID:12611891 we can resolve and identify the human homologues of 42 polypeptides detected so far in the more extensively studied beef heart complex I PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII
GO:0045271 respiratory chain complex I	IDA PMID:17209039 Identification of mitochondrial complex I assembly intermedi...	ACCEPT	Summary: IDA annotation placing MT-ND1 in respiratory chain complex I. Reason: ND1 is one of the seven mtDNA-encoded core subunits of the membrane arm of Complex I; membership is supported by immunopurification of human Complex I, the human megacomplex structure, and the original identification of the ND reading frames as Complex I components. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Core subunit of the mitochondrial membrane respiratory chain PMID:3921850 We conclude that the six reading frames encode components of the respiratory-chain NADH dehydrogenase. PMID:12611891 we can resolve and identify the human homologues of 42 polypeptides detected so far in the more extensively studied beef heart complex I PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII
GO:0045271 respiratory chain complex I	IEA GO_REF:0000107	ACCEPT	Summary: IEA annotation placing MT-ND1 in respiratory chain complex I. Reason: ND1 is one of the seven mtDNA-encoded core subunits of the membrane arm of Complex I; membership is supported by immunopurification of human Complex I, the human megacomplex structure, and the original identification of the ND reading frames as Complex I components. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Core subunit of the mitochondrial membrane respiratory chain PMID:3921850 We conclude that the six reading frames encode components of the respiratory-chain NADH dehydrogenase. PMID:12611891 we can resolve and identify the human homologues of 42 polypeptides detected so far in the more extensively studied beef heart complex I PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII
GO:0045271 respiratory chain complex I	IPI PMID:28844695 Architecture of Human Mitochondrial Respiratory Megacomplex ...	ACCEPT	Summary: IPI annotation placing MT-ND1 in respiratory chain complex I. Reason: ND1 is one of the seven mtDNA-encoded core subunits of the membrane arm of Complex I; membership is supported by immunopurification of human Complex I, the human megacomplex structure, and the original identification of the ND reading frames as Complex I components. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Core subunit of the mitochondrial membrane respiratory chain PMID:3921850 We conclude that the six reading frames encode components of the respiratory-chain NADH dehydrogenase. PMID:12611891 we can resolve and identify the human homologues of 42 polypeptides detected so far in the more extensively studied beef heart complex I PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII
GO:0045271 respiratory chain complex I	NAS PMID:3921850 Six unidentified reading frames of human mitochondrial DNA e...	ACCEPT	Summary: NAS annotation placing MT-ND1 in respiratory chain complex I. Reason: ND1 is one of the seven mtDNA-encoded core subunits of the membrane arm of Complex I; membership is supported by immunopurification of human Complex I, the human megacomplex structure, and the original identification of the ND reading frames as Complex I components. Supporting Evidence: file:human/MT-ND1/MT-ND1-uniprot.txt Core subunit of the mitochondrial membrane respiratory chain PMID:3921850 We conclude that the six reading frames encode components of the respiratory-chain NADH dehydrogenase. PMID:12611891 we can resolve and identify the human homologues of 42 polypeptides detected so far in the more extensively studied beef heart complex I PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII
GO:1902600 proton transmembrane transport	IEA GO_REF:0000108	ACCEPT	Summary: IEA annotation to proton transmembrane transport. Reason: The membrane arm of Complex I is the proton pump, and ND1 forms part of one of its four proton-translocation units. Proton transport coupled to electron transfer is core work done by this subunit, not a downstream consequence. Supporting Evidence: PMID:36920092 which form, together with part of ND1, the E-channel containing key glutamates PMID:32747785 The four units each comprise a proton-uptake and a proton-exit half-channel Reactome:R-HSA-163217 This electron transfer is coupled with the translocation of protons from the mitochondrial matrix to the intermembrane space.
GO:0048039 ubiquinone binding	ISS PMID:35589726 Cryo-EM structures define ubiquinone-10 binding to mitochond...	NEW	Summary: Proposed new annotation: ND1 enables ubiquinone binding, as part of the Complex I quinone-binding channel. Reason: Mammalian Complex I structures show the ubiquinone-10 isoprenoid chain running along the ND1-NDUFS7 interface and leaving the complex through ND1, with ND1 loops forming part of the Q-binding site. Patient-cell biochemistry is consistent: the ND1 m.3460G>A variant selectively lowers rotenone-sensitive, ubiquinone-dependent electron transfer. Evidence is from the conserved mammalian enzyme (sheep/mouse/bovine structures), so ISS. This is ND1's subunit-level contribution to the complex activity. Supporting Evidence: PMID:35589726 then extending, as the isoprenoid chain, along the NDUFS2-NDUFS7 then ND1-NDUFS7 interfaces to exit from ND1 PMID:32747785 ubiquinone is thought to worm its way up a channel at the hydrophilic/hydrophobic domain interface of the NDUFS2, NDUFS7, ND1 and ND3 subunits PMID:1959619 This is in accordance with the proposal that the ND1 subunit interacts with rotenone and ubiquinone.

Gene Description

Existing Annotations Review

Core Functions

References

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Notes

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