NDUFV2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0003954 NADH dehydrogenase activity	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) annotation with the contributes_to qualifier capturing that NDUFV2 is a subunit of the NADH dehydrogenase enzyme (Complex I). This is the general NADH dehydrogenase activity term; the ubiquinone-specific child term GO:0008137 is also annotated and is the more precise molecular function for this enzyme. Reason: NDUFV2 is a bona fide core subunit of the flavoprotein module of Complex I and contributes to its NADH-oxidising activity; contributes_to is the correct qualifier for a multi-subunit enzyme subunit. Supporting Evidence: file:human/NDUFV2/NDUFV2-uniprot.txt Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor
GO:0006120 mitochondrial electron transport, NADH to ubiquinone	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) annotation to the core biological process of Complex I. This is the central, defining biological role of NDUFV2 as part of the electron-transfer chain from NADH to ubiquinone. Reason: This is the core BP of NDUFV2; strongly supported by the IBA plus experimental (IDA/IMP) and UniProt evidence that NDUFV2 is a core subunit of the NADH-oxidising module of Complex I. Supporting Evidence: file:human/NDUFV2/NDUFV2-uniprot.txt catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor
GO:0045271 respiratory chain complex I	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) annotation placing NDUFV2 as part of respiratory chain complex I. This is the correct complex/location for this core subunit and is corroborated by multiple experimental (IDA/IMP/IPI) annotations. Reason: NDUFV2 is an established structural component of Complex I (flavoprotein/FP subcomplex of the peripheral arm); the complex membership is well supported. Supporting Evidence: file:human/NDUFV2/NDUFV2-uniprot.txt Core subunit of respiratory chain NADH dehydrogenase (Complex I) which is composed of 45 different subunits. This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme.
GO:0005743 mitochondrial inner membrane	IEA GO_REF:0000120	ACCEPT	Summary: Electronic (IEA) subcellular-location annotation to the mitochondrial inner membrane, the correct anatomical location for Complex I. NDUFV2 is a peripheral inner-membrane protein on the matrix side. Corroborated by IDA (PMID:28844695), ISS and TAS annotations to the same term. Reason: Consistent with UniProt subcellular location and the well-established topology of Complex I; NDUFV2 sits in the matrix-side peripheral arm anchored at the inner membrane. Supporting Evidence: file:human/NDUFV2/NDUFV2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane
GO:0008137 NADH dehydrogenase (ubiquinone) activity	IEA GO_REF:0000120	MODIFY	Summary: Electronic (IEA) annotation to the enzyme's specific catalytic molecular function, NADH:ubiquinone oxidoreductase activity (EC 7.1.1.2, RHEA:29091). This is the defining catalytic activity of Complex I; NDUFV2 is a core subunit contributing to it. Reason: The NADH:ubiquinone oxidoreductase reaction is a property of the assembled holoenzyme, not of NDUFV2 in isolation. A single subunit does not independently enable the full reaction, so the enables qualifier over-states NDUFV2's role; contributes_to is the appropriate qualifier (as for the curated IBA/IMP annotations to the same term). Retain the term but with contributes_to. Proposed replacements: NADH dehydrogenase (ubiquinone) activity Supporting Evidence: file:human/NDUFV2/NDUFV2-uniprot.txt Reaction=a ubiquinone + NADH + 5 H(+)(in) = a ubiquinol + NAD(+) + 4 H(+)(out)
GO:0016491 oxidoreductase activity	IEA GO_REF:0000002	MARK AS OVER ANNOTATED	Summary: InterPro-based (IEA) annotation to the very general parent term oxidoreductase activity. NDUFV2's redox function is captured far more precisely by the child terms NADH dehydrogenase (ubiquinone) activity (GO:0008137) and electron transfer activity (GO:0009055), which are also annotated. Reason: The term is not wrong (Complex I is an oxidoreductase) but is uninformatively general given that more specific and better-supported MF terms are already present.
GO:1902600 proton transmembrane transport	IEA GO_REF:0000108	MARK AS OVER ANNOTATED	Summary: Automatic inference (from the GO:0008137 catalytic activity mapping) that the gene product is involved in proton transmembrane transport. This is a complex-level property arising from the proton-pumping membrane (ND) arm of Complex I, not from NDUFV2, which sits in the soluble N-module of the peripheral arm and coordinates the N1a [2Fe-2S] cluster of the electron-input pathway. Reason: Proton translocation is performed by the antiporter-like subunits of the membrane arm; attributing it to the N-module electron-input subunit NDUFV2 over-annotates a whole-complex activity onto an individual peripheral-arm subunit.
GO:0005515 protein binding	IPI PMID:28380382 A Single Adaptable Cochaperone-Scaffold Complex Delivers Nas...	MARK AS OVER ANNOTATED	Summary: IPI evidence (with HSCB/HSC20 co-chaperone, UniProtKB:Q8IWL3) that NDUFV2 binds the HSC20-based Fe-S transfer complex. This is a real and biologically meaningful interaction (Fe-S cluster delivery to Complex I), but the GO term itself is the uninformative bare 'protein binding'. Reason: Bare protein binding conveys no specific molecular function. The underlying biology (NDUFV2 acquires its [2Fe-2S] cluster via the HSC20 co-chaperone system) is better represented by the Fe-S cluster binding MF (proposed as a NEW annotation) rather than by generic protein binding. Supporting Evidence: PMID:28380382 The five Fe-S cluster subunits of Complex I also interact with HSC20 to acquire their clusters, highlighting the crucial role of HSC20 in the assembly of the mitochondrial respiratory chain.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	MARK AS OVER ANNOTATED	Summary: IPI from a genome-scale binary interactome (yeast two-hybrid reference map). Contributes a bare 'protein binding' annotation with no functional specificity. Reason: Bare protein binding from a high-throughput interactome screen is uninformative as a molecular function and does not reflect NDUFV2's characterized role in Complex I.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	MARK AS OVER ANNOTATED	Summary: IPI from a large-scale neurodegenerative-disease interactome mapping study; the many partner proteins captured under this single 'protein binding' term are mostly high-throughput screen hits without a defined functional relationship to NDUFV2. Reason: Bare protein binding from a high-throughput screen is uninformative and does not add specific molecular-function knowledge beyond NDUFV2's role in Complex I.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	MARK AS OVER ANNOTATED	Summary: IPI from a proteome-scale affinity-purification interactome (BioPlex). Bare 'protein binding' with no functional specificity. Reason: Bare protein binding from a high-throughput interactome dataset is uninformative as a molecular function.
GO:0006120 mitochondrial electron transport, NADH to ubiquinone	IEA GO_REF:0000120	ACCEPT	Summary: Electronic (IEA) annotation to the core biological process. Duplicates the IBA and experimental annotations to the same term and is fully consistent with NDUFV2's characterized role. Reason: Core BP of NDUFV2; independently supported by IBA and experimental (IDA/IMP) evidence to the same term. Supporting Evidence: file:human/NDUFV2/NDUFV2-uniprot.txt catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor
GO:0045271 respiratory chain complex I	IEA GO_REF:0000120	ACCEPT	Summary: Electronic (IEA) annotation placing NDUFV2 as part of respiratory chain complex I. Duplicates the IBA and multiple experimental (IDA/IMP/IPI) annotations to the same term. Reason: Well-established complex membership; corroborated by phylogenetic and experimental evidence. Supporting Evidence: file:human/NDUFV2/NDUFV2-uniprot.txt This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme.
GO:0005743 mitochondrial inner membrane	IDA PMID:28844695 Architecture of Human Mitochondrial Respiratory Megacomplex ...	ACCEPT	Summary: Direct assay (IDA, ComplexPortal) localising NDUFV2 to the mitochondrial inner membrane, based on the cryo-EM structure of the human respiratory megacomplex in which the position of each Complex I subunit including NDUFV2 was assigned. Reason: Correct anatomical location for this Complex I subunit; supported by the structural study and consistent with UniProt subcellular location. Supporting Evidence: PMID:28844695 The structure not only reveals the precise assignment of individual subunits of human CI and CIII
GO:0009060 aerobic respiration	NAS PMID:30030361 Assembly of mammalian oxidative phosphorylation complexes I-...	KEEP AS NON CORE	Summary: Author-statement (NAS, ComplexPortal) annotation of the Complex I holoenzyme to aerobic respiration. As a core Complex I subunit, NDUFV2 participates in the OXPHOS system that underpins aerobic respiration, though this is a broad complex-level process rather than NDUFV2's specific molecular role. Reason: Valid at the pathway level (Complex I is central to aerobic respiration/OXPHOS) but broader than the core electron-transport function; retained as non-core context. Supporting Evidence: PMID:30030361 The assembly of the five oxidative phosphorylation system (OXPHOS) complexes in the inner mitochondrial membrane is an intricate process.
GO:0042776 proton motive force-driven mitochondrial ATP synthesis	NAS PMID:30030361 Assembly of mammalian oxidative phosphorylation complexes I-...	MARK AS OVER ANNOTATED	Summary: Author-statement (NAS, ComplexPortal) annotation to proton motive force-driven ATP synthesis. ATP synthesis is the function of Complex V (ATP synthase); Complex I contributes only indirectly by helping establish the proton-motive force via its membrane arm, and NDUFV2 (an N-module electron-input subunit) is doubly removed from ATP synthesis. Reason: ATP synthesis is performed by Complex V, not Complex I; attributing it to the peripheral-arm subunit NDUFV2 over-annotates a downstream, whole-OXPHOS-system outcome onto an individual electron-transport subunit.
GO:0045271 respiratory chain complex I	IPI PMID:28844695 Architecture of Human Mitochondrial Respiratory Megacomplex ...	ACCEPT	Summary: IPI evidence (ComplexPortal) that NDUFV2 is a component of respiratory chain complex I, based on the cryo-EM megacomplex structure with defined subunit composition. Reason: Direct structural/physical evidence for Complex I membership; a core, well-supported annotation. Supporting Evidence: 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: Sequence-similarity (ISS) annotation to the mitochondrial inner membrane, transferred from the bovine ortholog (UniProtKB:P04394). Consistent with the IDA and IEA annotations to the same location. Reason: Correct location; the bovine ortholog basis is sound and matches UniProt subcellular location and the topology of Complex I. Supporting Evidence: file:human/NDUFV2/NDUFV2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane
GO:0005739 mitochondrion	HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an...	ACCEPT	Summary: High-throughput (HTP) proteomics annotation to mitochondrion from a quantitative high-confidence human mitochondrial proteome. Correct but less specific than the mitochondrial inner membrane annotations. Reason: Correct localisation; a broader parent of the inner-membrane location and consistent with the well-established mitochondrial residence of NDUFV2. Supporting Evidence: PMID:34800366 Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
GO:0045271 respiratory chain complex I	IDA PMID:12611891 The subunit composition of the human NADH dehydrogenase obta...	ACCEPT	Summary: Direct assay (IDA) demonstrating NDUFV2 as a component of human NADH dehydrogenase (Complex I) by one-step immunopurification followed by mass-spectrometric identification of the subunit composition. Reason: Direct biochemical evidence for Complex I membership from purified human enzyme; a core, well-supported annotation. Supporting Evidence: 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
GO:0045271 respiratory chain complex I	IMP PMID:12754703 Mutant NDUFV2 subunit of mitochondrial complex I causes earl...	ACCEPT	Summary: Mutant-phenotype (IMP) evidence for Complex I membership. A homozygous splice-site mutation reducing NDUFV2 protein by 70% causes isolated Complex I deficiency, demonstrating that NDUFV2 is required for a functional Complex I. Reason: Human loss-of-function evidence directly links NDUFV2 to Complex I integrity/function; strongly supports complex membership. Supporting Evidence: PMID:12754703 resulted in 70% decreased NDUFV2 protein and complex I deficiency
GO:0045271 respiratory chain complex I	IDA PMID:28844695 Architecture of Human Mitochondrial Respiratory Megacomplex ...	ACCEPT	Summary: Direct assay (IDA) for Complex I membership from the cryo-EM structure of the human respiratory megacomplex, which assigns NDUFV2 to a defined position within Complex I. Reason: Structural evidence directly places NDUFV2 within Complex I; core, well-supported annotation. Supporting Evidence: 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:9878551 cDNA of eight nuclear encoded subunits of NADH:ubiquinone ox...	ACCEPT	Summary: Author-statement (NAS) annotation of NDUFV2 as one of the nuclear-encoded subunits of human NADH:ubiquinone oxidoreductase (Complex I). Reason: Consistent with the many stronger (IDA/IMP/IPI) annotations to the same term; NDUFV2 is an established Complex I subunit. Supporting Evidence: PMID:9878551 NADH:ubiquinone oxidoreductase (complex I) is an extremely complicated multiprotein complex located in the inner mitochondrial membrane.
GO:0006120 mitochondrial electron transport, NADH to ubiquinone	IDA PMID:28844695 Architecture of Human Mitochondrial Respiratory Megacomplex ...	ACCEPT	Summary: Direct assay (IDA) supporting NDUFV2's involvement in NADH-to-ubiquinone electron transport, from the structural and functional characterisation of the human respiratory megacomplex including determination of catalytic activity and cofactor content. Reason: Core BP of NDUFV2, directly supported by the structural and functional study of the human enzyme. Supporting Evidence: file:human/NDUFV2/NDUFV2-uniprot.txt the electrons from NADH are accepted by flavin mononucleotide (FMN) and then passed along a chain of iron-sulfur clusters by electron tunnelling to the final acceptor ubiquinone
GO:0008137 NADH dehydrogenase (ubiquinone) activity	IDA PMID:28844695 Architecture of Human Mitochondrial Respiratory Megacomplex ...	MODIFY	Summary: Direct assay (IDA) annotation of the specific NADH:ubiquinone oxidoreductase catalytic activity, based on the cryo-EM structure that established the function, catalytic activity and cofactor of the human enzyme. As a subunit, NDUFV2 contributes to rather than solely enables the holoenzyme activity, but the catalytic molecular function is the defining function of the assembly it belongs to. Reason: The catalytic activity is a property of the assembled complex, not of NDUFV2 alone; a single subunit does not independently enable the full NADH:ubiquinone reaction. The complex-level MF is best expressed with the contributes_to qualifier (as in the curated IMP annotation from PMID:12754703), rather than enables. Retain the term but with contributes_to. Proposed replacements: NADH dehydrogenase (ubiquinone) activity Supporting Evidence: file:human/NDUFV2/NDUFV2-uniprot.txt Reaction=a ubiquinone + NADH + 5 H(+)(in) = a ubiquinol + NAD(+) + 4 H(+)(out)
GO:0008137 NADH dehydrogenase (ubiquinone) activity	IMP PMID:12754703 Mutant NDUFV2 subunit of mitochondrial complex I causes earl...	ACCEPT	Summary: Mutant-phenotype (IMP) evidence with the contributes_to qualifier. Reducing NDUFV2 protein by ~70% causes Complex I deficiency, showing NDUFV2 contributes to the NADH:ubiquinone oxidoreductase activity of the holoenzyme. Reason: Human loss-of-function evidence that NDUFV2 is required for full Complex I catalytic activity; contributes_to is the appropriate qualifier for a subunit. Supporting Evidence: PMID:12754703 resulted in 70% decreased NDUFV2 protein and complex I deficiency
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-163217	ACCEPT	Summary: Reactome-derived (TAS) annotation to the mitochondrial inner membrane, from the pathway event in which Complex I oxidises NADH and reduces ubiquinone. Correct location for this Complex I subunit. Reason: Correct location, redundant with the IDA/ISS/IEA inner-membrane annotations; consistent with the topology of Complex I.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6788556	ACCEPT	Summary: Reactome-derived (TAS) annotation to the mitochondrial inner membrane, from a Complex I biogenesis event (Fe-S transfer to NDUFV1/V2). Correct location. Reason: Correct location; redundant with other inner-membrane annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799179	ACCEPT	Summary: Reactome-derived (TAS) annotation to the mitochondrial inner membrane, from a Complex I assembly event. Correct location. Reason: Correct location; redundant with other inner-membrane annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799196	ACCEPT	Summary: Reactome-derived (TAS) annotation to the mitochondrial inner membrane, from a Complex I assembly event. Correct location. Reason: Correct location; redundant with other inner-membrane annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6800870	ACCEPT	Summary: Reactome-derived (TAS) annotation to the mitochondrial inner membrane, from the event in which NDUF subunits bind to form the FP subcomplex. Correct location for NDUFV2, which is part of the FP subcomplex. Reason: Correct location; consistent with NDUFV2 being a component of the flavoprotein (FP) subcomplex of the peripheral arm.
GO:0005739 mitochondrion	IDA PMID:12754703 Mutant NDUFV2 subunit of mitochondrial complex I causes earl...	ACCEPT	Summary: Direct assay (IDA) annotation to mitochondrion. Correct but less specific than the mitochondrial inner membrane annotations; consistent with NDUFV2's characterized mitochondrial residence. Reason: Correct localisation; a broad parent of the inner-membrane location. Supporting Evidence: file:human/NDUFV2/NDUFV2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane
GO:0006120 mitochondrial electron transport, NADH to ubiquinone	IMP PMID:12754703 Mutant NDUFV2 subunit of mitochondrial complex I causes earl...	ACCEPT	Summary: Mutant-phenotype (IMP) evidence for involvement in NADH-to-ubiquinone electron transport. Reduced NDUFV2 causes Complex I deficiency, i.e. impaired electron transport through Complex I. Reason: Core BP; human loss-of-function evidence directly links NDUFV2 to Complex I electron-transport function. Supporting Evidence: PMID:12754703 resulted in 70% decreased NDUFV2 protein and complex I deficiency
GO:0006120 mitochondrial electron transport, NADH to ubiquinone	NAS PMID:9570948 Genotype in the 24-kDa subunit gene (NDUFV2) of mitochondria...	ACCEPT	Summary: Author-statement (NAS) annotation to the core electron-transport BP, from a study of NDUFV2 as the 24-kDa subunit of mitochondrial Complex I in the context of Parkinson disease susceptibility. Reason: Core BP; consistent with the many stronger annotations to the same term. Supporting Evidence: PMID:9570948 the gene encoding the 24-kDa subunit of mitochondrial complex I
GO:0007399 nervous system development	IMP PMID:9570948 Genotype in the 24-kDa subunit gene (NDUFV2) of mitochondria...	MARK AS OVER ANNOTATED	Summary: IMP annotation to nervous system development, derived from a genetic-association study reporting an NDUFV2 targeting-sequence polymorphism (Ala29Val) as a Parkinson disease susceptibility factor. This is a disease-susceptibility association in a neurodegenerative disorder, not evidence that NDUFV2 has a developmental role in building the nervous system. Reason: The supporting study is a PD case-control association, not a developmental phenotype; annotating NDUFV2 to nervous system development over-interprets a susceptibility polymorphism. The gene's role in neural tissue is better understood as bioenergetic support via Complex I rather than a developmental function. Supporting Evidence: PMID:9570948 A novel polymorphism (Ala29Val) in the mitochondrial targeting sequence of NDUFV2 was found in patients with PD
GO:0008137 NADH dehydrogenase (ubiquinone) activity	NAS PMID:9570948 Genotype in the 24-kDa subunit gene (NDUFV2) of mitochondria...	MODIFY	Summary: Author-statement (NAS) annotation to the specific NADH:ubiquinone oxidoreductase catalytic activity of Complex I, of which NDUFV2 is the 24-kDa subunit. Reason: The NADH:ubiquinone oxidoreductase reaction is a property of the assembled holoenzyme; NDUFV2 as a single subunit contributes to but does not independently enable it. The contributes_to qualifier is appropriate (matching the curated IBA/IMP annotations to the same term). Retain the term but with contributes_to. Proposed replacements: NADH dehydrogenase (ubiquinone) activity Supporting Evidence: PMID:9570948 the gene encoding the 24-kDa subunit of mitochondrial complex I
GO:0009055 electron transfer activity	NAS PMID:7488192 Structural organization and chromosomal localization of the ...	ACCEPT	Summary: Author-statement (NAS) annotation to electron transfer activity. NDUFV2 is the 24-kDa iron-sulfur subunit of Complex I and coordinates the N1a [2Fe-2S] cluster in the electron-input pathway, giving it a genuine electron-transfer role within the enzyme. Reason: Well-founded MF; NDUFV2 carries a [2Fe-2S] redox cofactor and participates in the electron-relay chain from NADH toward ubiquinone. Supporting Evidence: PMID:7488192 the 24-kDa iron-sulfur subunit of mitochondrial NADH-ubiquinone oxidoreductase (Complex I)
GO:0048738 cardiac muscle tissue development	IMP PMID:12754703 Mutant NDUFV2 subunit of mitochondrial complex I causes earl...	KEEP AS NON CORE	Summary: IMP annotation to cardiac muscle tissue development, from the observation that a homozygous NDUFV2 splice mutation causes early-onset hypertrophic cardiomyopathy. This reflects a bioenergetic disease phenotype of Complex I deficiency in cardiac tissue rather than a direct role of NDUFV2 in the developmental program of the heart. Reason: The cardiomyopathy phenotype is real and clinically important, but it arises from loss of Complex I energy production rather than a developmental function of NDUFV2; retained as a non-core, tissue-context annotation rather than a core molecular role. Supporting Evidence: PMID:12754703 causes complex I deficiency and early onset hypertrophic cardiomyopathy with trunk hypotonia in three affected sibs
GO:0006120 mitochondrial electron transport, NADH to ubiquinone	NAS PMID:9878551 cDNA of eight nuclear encoded subunits of NADH:ubiquinone ox...	ACCEPT	Summary: Author-statement (NAS) annotation to the core electron-transport BP, from the characterisation of the nuclear-encoded subunits of human NADH:ubiquinone oxidoreductase (Complex I). Reason: Core BP; consistent with the many stronger annotations to the same term. Supporting Evidence: PMID:9878551 Its main function is the transport of electrons from NADH to ubiquinone
GO:0008137 NADH dehydrogenase (ubiquinone) activity	NAS PMID:9878551 cDNA of eight nuclear encoded subunits of NADH:ubiquinone ox...	MODIFY	Summary: Author-statement (NAS) annotation to the specific NADH:ubiquinone oxidoreductase catalytic activity, from the characterisation of the human Complex I subunits. Reason: The NADH:ubiquinone oxidoreductase reaction is a property of the assembled holoenzyme; NDUFV2 as a single subunit contributes to but does not independently enable it. The contributes_to qualifier is appropriate (matching the curated IBA/IMP annotations to the same term). Retain the term but with contributes_to. Proposed replacements: NADH dehydrogenase (ubiquinone) activity Supporting Evidence: PMID:9878551 Its main function is the transport of electrons from NADH to ubiquinone
GO:0051537 2 iron, 2 sulfur cluster binding	IEA file:human/NDUFV2/NDUFV2-uniprot.txt	NEW	Summary: NDUFV2 binds one [2Fe-2S] iron-sulfur cluster (the N1a cluster) via conserved cysteine ligands, a cofactor central to its role in the electron-input pathway of Complex I. UniProt annotates the [2Fe-2S] cofactor with experimental (PubMed:28844695) evidence and four ligand residues from the cryo-EM structures, and the corresponding GO term (GO:0051537) is present in the UniProt GO cross-references (UniProtKB-KW). This specific metal-cofactor MF is not represented in the current GOA TSV and is proposed here as a NEW annotation to capture NDUFV2's redox chemistry more precisely than the generic electron transfer activity term. Reason: The [2Fe-2S] cluster binding is a well-supported, defining molecular feature of NDUFV2 (2Fe-2S keyword, experimental cofactor annotation, and four structural ligand-binding residues in UniProt) that is missing from the curated GO annotation set and directly underlies its electron-transfer function in the N-module of Complex I. Supporting Evidence: file:human/NDUFV2/NDUFV2-uniprot.txt Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135 file:human/NDUFV2/NDUFV2-uniprot.txt Contains one iron-sulfur cluster

Gene Description

Existing Annotations Review

Core Functions

As a core subunit of the flavoprotein (FP) module of mitochondrial Complex I, NDUFV2 coordinates a [2Fe-2S] iron-sulfur cluster (N1a) and contributes to the NADH:ubiquinone oxidoreductase activity of the holoenzyme, participating in electron transfer from NADH toward ubiquinone.

NDUFV2 binds one [2Fe-2S] iron-sulfur cluster (the N1a cluster) near the FMN/NADH site, providing a redox center in the electron-input pathway of Complex I.

References

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