NDUFAF7

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0032981 mitochondrial respiratory chain complex I assembly	IBA GO_REF:0000033	ACCEPT	Summary: Core biological process. NDUFAF7 is required for assembly of mitochondrial respiratory chain Complex I; its methylation of NDUFS2 stabilizes an early assembly intermediate. Directly supported by experimental knockdown/knockout studies in human, zebrafish, and mouse, so the phylogenetic (IBA) inference is well founded. Supporting Evidence: PMID:24838397 produced a specific complex I assembly defect
GO:0035243 protein-arginine omega-N symmetric methyltransferase activity	IBA GO_REF:0000033	ACCEPT	Summary: Core molecular function. NDUFAF7 is a genuine SAM-dependent protein arginine methyltransferase that produces a symmetrically dimethylated arginine (Arg-85 of NDUFS2), consistent with a type II (symmetric) arginine methyltransferase. This IBA is corroborated by direct biochemical evidence (IMP, EC 2.1.1.320) and is the correct specific MF term. Supporting Evidence: PMID:24089531 responsible for the symmetrical dimethylation of Arg-85 of the NDUFS2 subunit of complex I
GO:0005739 mitochondrion	IBA GO_REF:0000033	ACCEPT	Summary: Correct compartment. NDUFAF7 is a mitochondrial matrix protein (cleaved N-terminal transit peptide) where it acts on NDUFS2. Consistent with all experimental localization data. The more specific matrix term (GO:0005759) is captured by other annotations. Supporting Evidence: PMID:24089531 the presence of NDUFAF7 in the mitochondrial matrix has been confirmed
GO:0005739 mitochondrion	IEA GO_REF:0000044	ACCEPT	Summary: Electronic annotation from the UniProt subcellular-location keyword (Mitochondrion), consistent with the experimentally confirmed matrix localization. Supporting Evidence: PMID:24089531 the presence of NDUFAF7 in the mitochondrial matrix has been confirmed
GO:0032981 mitochondrial respiratory chain complex I assembly	IEA GO_REF:0000117	ACCEPT	Summary: ARBA electronic annotation to the core assembly process; redundant with, and confirmed by, the experimental IMP annotations for this term. Supporting Evidence: PMID:24838397 produced a specific complex I assembly defect
GO:0035243 protein-arginine omega-N symmetric methyltransferase activity	IEA GO_REF:0000120	ACCEPT	Summary: Electronic annotation derived from the RHEA/EC mapping (RHEA:48108, EC 2.1.1.320) for the symmetric dimethylarginine-producing reaction. Consistent with the experimentally established catalytic activity. Supporting Evidence: PMID:24089531 responsible for the symmetrical dimethylation of Arg-85 of the NDUFS2 subunit of complex I
GO:0005515 protein binding	IPI PMID:24510904 Unbiased screen for interactors of leucine-rich repeat kinas...	MARK AS OVER ANNOTATED	Summary: Bare "protein binding" IPI from an unbiased LRRK2 (Q5S007) interactome screen; NDUFAF7 was recovered as an LRRK2 interactor. Uninformative about NDUFAF7's molecular function and of unclear physiological significance; over-annotation rather than a core function.
GO:0005515 protein binding	IPI PMID:29513927 Comparative Protein Interaction Network Analysis Identifies ...	MARK AS OVER ANNOTATED	Summary: Bare "protein binding" IPI, again capturing the NDUFAF7-LRRK2 (Q5S007) interaction from a ROCO protein interaction network analysis. Uninformative term; not a core function.
GO:0005739 mitochondrion	EXP PMID:28837730 A Novel Potentially Causative Variant of NDUFAF7 Revealed by...	ACCEPT	Summary: Experimental mitochondrial localization reported in the pathologic-myopia study (immunofluorescence of the protein and its variant). Consistent with the matrix localization. Supporting Evidence: PMID:28837730 The subcellular localization
GO:0005739 mitochondrion	HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an...	ACCEPT	Summary: High-throughput mitochondrial proteome placement of NDUFAF7 in the mitochondrion; concordant with the experimental (IDA/EXP) localization data. Supporting Evidence: PMID:24089531 the presence of NDUFAF7 in the mitochondrial matrix has been confirmed
GO:0005515 protein binding	IPI PMID:24089531 NDUFAF7 methylates arginine 85 in the NDUFS2 subunit of huma...	MARK AS OVER ANNOTATED	Summary: Bare "protein binding" IPI recording the interaction with the substrate subunit NDUFS2 (UniProtKB:O75306). The interaction itself is biologically important (NDUFS2 is the methylation substrate), but the generic GO:0005515 term is uninformative; the informative version of this interaction is captured by the GO:0019899 enzyme-binding annotation (same reference set).
GO:0005739 mitochondrion	IDA PMID:24089531 NDUFAF7 methylates arginine 85 in the NDUFS2 subunit of huma...	ACCEPT	Summary: Direct experimental evidence (confocal microscopy of FLAG-tagged NDUFAF7 co-localizing with MitoTracker) placing NDUFAF7 in the mitochondrion; the same study confirms matrix localization. Supporting Evidence: PMID:24089531 the presence of NDUFAF7 in the mitochondrial matrix has been confirmed
GO:0005739 mitochondrion	IDA PMID:24838397 The arginine methyltransferase NDUFAF7 is essential for comp...	ACCEPT	Summary: Direct experimental mitochondrial localization; NDUFAF7 is described as a soluble matrix protein in this study. Supporting Evidence: PMID:24838397 soluble matrix protein comprised of a DUF185 domain that harbors a
GO:0019918 peptidyl-arginine methylation, to symmetrical-dimethyl arginine	IMP PMID:24089531 NDUFAF7 methylates arginine 85 in the NDUFS2 subunit of huma...	ACCEPT	Summary: Core process describing the specific protein modification NDUFAF7 carries out: symmetric dimethylation of a peptidyl-arginine (Arg-85 of NDUFS2). Directly supported by mass-spectrometric demonstration that suppression of NDUFAF7 abolishes Arg-85 dimethylation. Supporting Evidence: PMID:24089531 This methylation step occurs early in the assembly of complex I
GO:0032981 mitochondrial respiratory chain complex I assembly	IMP PMID:24089531 NDUFAF7 methylates arginine 85 in the NDUFS2 subunit of huma...	ACCEPT	Summary: Core biological process. siRNA suppression of NDUFAF7 impairs Complex I assembly; the Arg-85 methylation is required for formation of the early 400-kDa peripheral-arm intermediate. Supporting Evidence: PMID:24089531 the methylation of Arg-85 in NDUFS2 is required for the formation of the 400-kDa
GO:0032981 mitochondrial respiratory chain complex I assembly	IMP PMID:24838397 The arginine methyltransferase NDUFAF7 is essential for comp...	ACCEPT	Summary: Core biological process, independently supported. siRNA (human), morpholino (zebrafish), and germline knockout (mouse, embryonic-lethal) all give a specific Complex I assembly defect. Supporting Evidence: PMID:24838397 produced a specific complex I assembly defect
GO:0035243 protein-arginine omega-N symmetric methyltransferase activity	IMP PMID:24089531 NDUFAF7 methylates arginine 85 in the NDUFS2 subunit of huma...	ACCEPT	Summary: Core molecular function with direct biochemical support. Suppression of NDUFAF7 causes loss of symmetric dimethylation of Arg-85 of NDUFS2, establishing NDUFAF7 as the responsible symmetric protein-arginine methyltransferase (EC 2.1.1.320). This is the primary catalytic function of the gene. Supporting Evidence: PMID:24089531 NDUFAF7 is a protein methylase that modifies residue Arg-85 of subunit NDUFS2 of complex I
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-6799178	ACCEPT	Summary: Reactome (Complex I biogenesis pathway) localizes NDUFAF7 to the mitochondrial matrix, consistent with the experimentally confirmed matrix localization. This is the most precise correct compartment term. Supporting Evidence: PMID:24089531 the presence of NDUFAF7 in the mitochondrial matrix has been confirmed
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-6799179	ACCEPT	Summary: Reactome matrix localization from a Complex I biogenesis reaction; concordant with experimental data. Supporting Evidence: PMID:24089531 the presence of NDUFAF7 in the mitochondrial matrix has been confirmed
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-6799191	ACCEPT	Summary: Reactome matrix localization from a Complex I biogenesis reaction; concordant with experimental data. Supporting Evidence: PMID:24089531 the presence of NDUFAF7 in the mitochondrial matrix has been confirmed
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-6799196	ACCEPT	Summary: Reactome matrix localization from the Complex I biogenesis reaction in which the MCIA complex and NDUFAF2-7 dissociate from the 980kDa complex; concordant with the experimentally confirmed matrix localization and with NDUFAF7 acting as a transient (non-structural) assembly factor. Supporting Evidence: PMID:24089531 the presence of NDUFAF7 in the mitochondrial matrix has been confirmed
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-6799197	ACCEPT	Summary: Reactome matrix localization from a Complex I biogenesis reaction; concordant with experimental data. Supporting Evidence: PMID:24089531 the presence of NDUFAF7 in the mitochondrial matrix has been confirmed
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-6799202	ACCEPT	Summary: Reactome matrix localization from a Complex I biogenesis reaction; concordant with experimental data. Supporting Evidence: PMID:24089531 the presence of NDUFAF7 in the mitochondrial matrix has been confirmed
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-6799203	ACCEPT	Summary: Reactome matrix localization from a Complex I biogenesis reaction; concordant with experimental data. Supporting Evidence: PMID:24089531 the presence of NDUFAF7 in the mitochondrial matrix has been confirmed
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-6800868	ACCEPT	Summary: Reactome matrix localization from a Complex I biogenesis reaction; concordant with experimental data. Supporting Evidence: PMID:24089531 the presence of NDUFAF7 in the mitochondrial matrix has been confirmed
GO:0005576 extracellular region	HDA PMID:22664934 Comparison of tear protein levels in breast cancer patients ...	MARK AS OVER ANNOTATED	Summary: Isolated high-throughput mass-spectrometry detection of the protein in tear fluid (a breast-cancer vs control tear proteomics survey; NDUFAF7 is not discussed by name in the paper). Biologically implausible as a functional location for a mitochondrial matrix enzyme bearing a cleaved mitochondrial transit peptide; a contaminant/secretion artifact of body-fluid proteomics rather than a functional localization.
GO:0005739 mitochondrion	IDA PMID:20406883 MidA is a putative methyltransferase that is required for mi...	ACCEPT	Summary: Direct experimental mitochondrial localization of MidA/NDUFAF7 (the founding functional study). Consistent with all later data. Supporting Evidence: PMID:20406883 These results indicate a role for MidA in complex I assembly or stability
GO:0008168 methyltransferase activity	NAS PMID:20406883 MidA is a putative methyltransferase that is required for mi...	MODIFY	Summary: This 2010 non-traceable statement correctly identified a (then putative) methyltransferase domain, but the term is too general. Subsequent biochemistry (PMID:24089531) established the specific activity as symmetric protein-arginine methyltransferase. MODIFY to the specific term. Proposed replacements: protein-arginine omega-N symmetric methyltransferase activity Supporting Evidence: PMID:20406883 site-directed mutagenesis of specific
GO:0019899 enzyme binding	IPI PMID:20406883 MidA is a putative methyltransferase that is required for mi...	KEEP AS NON CORE	Summary: Records the interaction with NDUFS2 (UniProtKB:O75306), the enzymatic substrate subunit, identified by yeast two-hybrid and pull-down. More informative than bare protein binding (it is substrate/enzyme binding), but it is a supporting activity rather than the core catalytic function; keep as non-core. Supporting Evidence: PMID:20406883 both proteins interact with the
GO:0032981 mitochondrial respiratory chain complex I assembly	IMP PMID:20406883 MidA is a putative methyltransferase that is required for mi...	ACCEPT	Summary: Core biological process. Knockdown of human MidA/NDUFAF7 reduced levels of assembled Complex I, and Dictyostelium midA(-) cells show a specific Complex I defect, establishing the assembly role. Supporting Evidence: PMID:20406883 reduced levels of assembled complex

Gene Description

Existing Annotations Review

Core Functions

SAM-dependent protein arginine methyltransferase that symmetrically dimethylates Arg-85 of the Complex I core subunit NDUFS2, an early step in mitochondrial respiratory chain Complex I biogenesis.

References

📚 Additional Documentation

Notes

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